CA2447357A1 - Molecular toxicology modeling - Google Patents

Abstract

The present invention is based on the elucidation of the global changes in gene expression and the identification of toxicity markers in tissues or cel ls exposed to a known renal toxin. The genes may be used as toxicity markers in drug screening and toxicity assays. The invention includes a database of gen es characterized by toxin-induced differential expression that is designed for use with microarrays and other solid-phase probes.

Description

DEMANDE OU BREVET VOLUMINEUX
LA PRESENTE PARTIE DE CETTE DEMANDE OU CE BREVET COMPREND
PLUS D'UN TOME.

NOTE : Pour les tomes additionels, veuillez contacter 1e Bureau canadien des brevets JUMBO APPLICATIONS/PATENTS
THIS SECTION OF THE APPLICATION/PATENT CONTAINS MORE THAN ONE
VOLUME

NOTE: For additional volumes, please contact the Canadian Patent Office NOM DU FICHIER / FILE NAME
NOTE POUR LE TOME / VOLUME NOTE:

MOLECULAR TOXICOLOGY MODELING
INVENTORS: Donna MENDRICK, Mark PORTER, Kory JOHNSON, Brandon HIGGS, Arthur CASTLE, and Michael ELASHOFF
RELATED APPLICATIONS
This application claims priority to U.S. Provisional Applications 60/292,335;
60/297,523; 60/298,925; 60/303,810; 60/303,807; 60/303,808; 60/315,047;
60/324,928;
60/330,867; 60/330,462; 60/331,805; 60/336,144; 60/340,873; 60/357,843;
60/357,842;
60/357,844; 60/364,134; 60/370,206; 60/370,247; 60/370,144; 60/371,679; and 60/372,794, all of which are herein incorporated by reference in their entirety. This application is also related to U.S. Application Nos. 09/917,800 and 10/060,087, both of which are also herein incorporated by reference in their entirety.
SEQUENCE LISTING SUBMISSION ON COMPACT DISC
The Sequence Listing submitted concurrently herewith on compact disc is herein incorporated by reference in its entirety. Four copies of the Sequence Listing, one on each of four compact discs are provided. Copy 1, Copy 2 and Copy 3 are identical.
Copies l, 2, and 3 are also identical to the CRF. Each electronic copy of the Sequence Listing was created on May 22, 2002 with a file size of 3088 KB. The file names are as follows: Copy 1- g15089wo.txt; Copy 2- g15089wo.txt; CRF- g15089wo.txt.
BACKGROUND OF THE INVENTION
The need for methods of assessing the toxic impact of a compound, pharmaceutical agent or environmental pollutant on a cell or living organism has led to the development of procedures which utilize living organisms as biological monitors.
The simplest and most convenient of these systems utilize unicellular microorganisms such as yeast and bacteria, since they are the most easily maintained and manipulated. In addition, unicellular screening systems often use easily detectable changes in phenotype to monitor the effect of test compounds on the cell. Unicellular organisms, however, are inadequate models for estimating the potential effects of many compounds on complex multicellular animals, as they do not have the ability to carry out biotransformations.
The biotransformation of chemical compounds by multicellular organisms is a significant factor in determining the overall toxicity of agents to which they are exposed.
Accordingly, multicellular screening systems may be preferred or required to detect the toxic effects of compounds. The use of multicellular organisms as toxicology screening tools has been significantly hampered,. however, by the lack of convenient screening mechanisms or endpoints, such as those available in yeast or bacterial systems.
Additionally, previous attempts to produce toxicology prediction systems have failed to provide the necessary modeling data and statistical information to accurately predict toxic responses (e.g., WO 00/12760, WO 00/47761, WO 00/63435, WO 01/32928, and WO 01/38579).
SUMMARY OF THE INVENTION
The present invention is based on the elucidation of the global changes in gene expression in tissues or cells exposed to known toxins, in particular renal toxins, as compared to unexposed tissues or cells as well as the identification of individual genes that are differentially expressed upon toxin exposure.
In various aspects, the invention includes methods of predicting at least one toxic effect of a compound, predicting the progression of a toxic effect of a compound, and predicting the renal toxicity of a compound. The invention also includes methods of identifying agents that modulate the onset or progression of a toxic response.
Also provided are methods of predicting the cellular pathways that a compound modulates in a cell. The invention also includes methods of identifying agents that modulate protein activities.
In a further aspect, the invention includes probes comprising sequences that specifically hybridize to genes in Tables 1-5. Also included are solid supports comprising at least two of the previously mentioned probes. The invention also includes a computer system that has a database containing information identifying the expression level in a tissue or cell sample exposed to a renal toxin of a set of genes comprising at least two genes in Tables 1-5.
DETAILED DESCRIPTION
Many biological functions are accomplished by altering the expression of various genes through transcriptional (e.g. through control of initiation, provision of RNA
precursors, RNA processing, etc.) and/or translational control. For example, fundamental biological processes such as cell cycle, cell differentiation and cell death, are often characterized by the variations in the expression levels of groups of genes.

Changes in gene expression are also associated with the effects of various chemicals, drugs, toxins, pharmaceutical agents and pollutants on an organism or cell.
For example, the lack of sufficient expression of functional tumor suppresser genes and/or the over expression of oncogene/protooncogenes after exposure to an agent could lead to tumorgenesis or hyperplastic growth of cells (Marshall (1991), Cell 64: 313-326;
Weinberg (1991), Science 254: 1138-1146). Thus, changes in the expression levels of particular genes (e.g. oncogenes or tumor suppressers) may serve as signposts for the presence and progression of toxicity or other cellular responses to exposure to a particular compound.
Monitoring changes in gene expression may also provide certain advantages during drug screening and development. Often drugs are screened for the ability to interact with a major target without regard to other effects the drugs have on cells. These cellular effects may cause toxicity in the whole animal, which prevents the development and clinical use of the potential drug.
The present inventors have examined tissue from animals exposed to known renal toxins which induce detrimental kidney effects, to identify global changes in gene expression induced by these compounds. These global changes in gene expression, which can be detected by the production of expression profiles (an expression level of one or more genes), provide useful toxicity markers that can be used to monitor toxicity and/or toxicity progression by a test compound. Some of these markers may also be used to monitor or detect various disease or physiological states, disease progression, drug efficacy, and drug metabolism.
Identification of Toxicity Markers To evaluate and identify gene expression changes that are predictive of toxicity, studies using selected compounds with well characterized toxicity have been conducted by the present inventors to catalogue altered gene expression during exposure in vivo and in vitro. In the present study, cephaloridine, cisplatin, puromycin aminonucleoside (PAN), bromoethylamine hydrobromide (BEA), gentamicin, ifosfamide, cyclophosphamide, carboplatin, AY-25329, indomethacin, acyclovir, citrinin, mercuric chloride, diflunisal, cidofovir, pamidronate, lithium, hydralazine, colchicine, sulfadiazine, and adriamycin were selected as known renal toxins.

Cephaloridine is an amphoteric, semi-synthetic, broad-spectrum cephalosporin derived from cephalosporin C. Cephalosporins are (3-lactam-containing antibiotics which prevent bacterial growth by inhibiting polymerization of the peptidoglycan bacterial cell wall. The linear glycan chains (composed of N-acetylglucosime and N-acetylmuramic acid) are cross-linked to each other by the coupling of short chains of several amino acids, the coupling resulting from the action of a transpeptidase. It is believed that cephalosporins act by blocking the activity of the transpeptidase (Goodman & Gilman's The Pharmalo~ical Basis of Therapeutics 9'~ ed., J.G. Hardman et al. Eds., McGraw Hill, New York, 1996, pp. 1074-1075, 1089-1095).
Cephaloridine is administered intramuscularly and is used to treat infections of the respiratory tract, gastrointestinal tract and urinary tract, as well as infections of soft tissue, bones and joints. Noted adverse effects include hypersensitivity reactions (such as anaphylactic shock, urticaria and bronchospasm), gastrointestinal disturbances, candidiasis, and cardiovascular and blood toxicity, in particular, toxicity to the hematopoietic system (cells responsible for the formation of red and white blood cells and platelets).
Although cephaloridine may be nephrotoxic at high dosages, it is not as harmful to the kidneys as are the aminoglycosides and polymixins. High dosages of cephaloridine may cause acute renal tubular necrosis (Cecil Textbook of Medicine, 20"' ed., part XII, p. 586, J. C. Bennett and F. Plum Eds., W. B. Saunders Co., Philadelphia, 1996) or drug-induced interstitial nephritis, which is accompanied by elevated IgE levels, fever, arthralgia and maculopapular rash. Renal biopsopy demonstrates edema and interstitial inflammatory lesions, mainly with lymphocytes, monocytes, eosinophils and plasma cells. Vasculitis of small vessels may develop, leading to necrotising glomerulonephritis (G. Koren, "The nephrotoxic potential of drugs and chemicals.
Pharmacological basis and clinical relevance.," Med Toxicol Adverse Drug Exp 4(1):59-72, 1989).
Cephaloridine has also been shown to reduce mitochondria) respiration and uptake of anionic succinate and carrier-mediated anionic substrate transport (Tune et al.
(1990), JPharmacol Exp Ther 252: 65-69). In a study of oxidative stress and damage to kidney tissue, cephaloridine depleted reduced glutathione (GSH) and produced oxidized glutathione (GSSG) in the renal cortex. This drug also inhibited glutathione reductase and produced malondialdehyde and conjugated dimes (Tune et al. (1989), Biochem Pharmacol 38: 795-802). Because cephaloridine is actively transported into the proximal renal tubule, but slowly transported across the lumenal membrane into the tubular fluid, high concentrations can accumulate and cause necrosis. Necrosis can be prevented by administering inhibitors of organic anion transport, although such treatment may be counterproductive, as cephaloridine is passed in and out of the kidney by the renal organic anion transport system (Tune et al. (1980), JPharmacol Exp Ther 215:
186-190).
Cisplatin (Pt (NH3)2(C1)2), a broad-spectrum anti-tumor agent, is commonly used to treat tumors of the testicles, ovaries, bladder, skin, head and neck, and lungs (PDR 47'"
ed., pp. 754-757, Medical Economics Co., Inc., Montvale, NJ, 1993; Goodman &
Gilman's The Pharmaloglcal Basis of Therapeutics 9"' ed., pp. 1269-1271, J.G.
Hardman et al. Eds., McGraw Hill, New York, 1996). Cisplatin diffuses into cells and functions mainly by alkylating the N' of guanine, a highly reactive site, causing interstrand and 1 S intrastrand crosslinks in the DNA that are lethal to cells. The drug is not sensitive to the cell cycle, although its effects are most pronounced in S phase.
Because the drug is cleared from the body mainly by the kidneys, the most frequent adverse effect of cisplatin usage is nephrotoxicity, the severity of which increases with increasing dosage and treatment terms. Other adverse effects include renal tubule damage, myelosuppression (reduced numbers of circulating platelets, leukocytes and erythrocytes), nausea and vomiting, ototoxicity, serum electrolyte disturbances (decreased concentrations of magnesium, calcium, sodium, potassium and phosphate, probably resulting from renal tubule damage), increased serum concentrations of urea and creatinine, and peripheral neuropathies.
' In one study on rats (Nonclercq et al. (1989), Exp Mol Pathol 51: 123-140) administration of cisplatin or carboplatin induced renal injury, carboplatin causing less damage than cisplatin. The most prominent injury was to the straight portion of proximal renal tubule.
In another rat study (Goldstein et al. (1981), Toxicol Appl Pharmacol 60: 163-175) animals injected with cisplatin displayed decreased food intake as drug dosage increased. On day 2, the high-dose groups (10-15 mglkg) exhibited a six or seven-fold elevation in BIJN. On day 4, BUN elevation was noted in the Smg/kg group. An increase in urine volume was observed beginning on days 3-4, along with decreased urine osmolality in the low-dose groups (2.5 or S mg/kg). Another experiment on rats (Agarwal et al. (1995), Kidney Int 48: 1298-1307) showed that cisplatin treatment produced elevations in serum creatinine levels, which began on day 3 and progressed for the duration of the study.
PAN (CZZH29N,05), an antibiotic produced by Streptomyces alboniger, inhibits protein synthesis and is commonly used experimentally on rats to mimic human minimal change disease. One study showed that PAN-injected rats demonstrated an increase in levels of serum non-esterified fatty acids, while the serum albumin concentration was negatively affected (Sasaki et al. (1999), Adv Exp Med Biol 467: 341-346).
In another rat study, an adenosine deaminase inhibitor prevented PAN
nephrotoxicity, indicating that PAN toxicity is linked to adenosine metabolism (Nosaka et al. (1997), Free Radic Biol Med 22: 597-605). Another group showed that PAN, when administered to rats, led to proteinuria, a condition associated with abnormal amounts of 1 S protein in the urine, and renal damage, e.g. blebbing of glomerular epithelial cells, focal separation of cells from the glomerular basement membrane, and fusion of podocytes (Olson et al. (1981), Lab Invest 44: 271-279). In another study on rats, administration of PAN induced glomerular epithelial cell apoptosis in a dose- and time-dependent manner (Sanwal et al. (2001), Exp Mol Pathol 70: 54-64).
One study with PAN-injected rats (Koukouritaki et al. (1998), Jlnvestig Med 46:
284-289) examined the changes in the expression of the proteins paxillin, focal adhesion kinase, and Rho, all of which regulate cell adhesion to the extracellular matrix. Paxillin levels increased steadily, peaked at day 9 after PAN injection, and then remained elevated even after proteinuria resolved. There was no observed change in expression of either focal adhesion kinase or Rho.
BEA, (CZH6BrN.HBr), is commonly used experimentally on rats to induce papillary necrosis and renal cortex damage, which is similar to human analgesic nephropathy. BEA-induced papillary necrosis in rats eventually leads to the onset of focal glomerular sclerosis and nephrotic proteinuria (Garber et al. (1999), Am JKidney Dis 33: 1033-1039). Even at low doses (50 mglkg), BEA can induce an apex limited renal papillary necrosis (Bach et al. (1983), Toxicol Appl Pharmacol 69: 333-344). In male Wistar rats, BEA administered at 100 mg/kg was shown to cause renal papillary _7_ necrosis within 24 hours (Back et al. (1991), Food Chem Toxicol 29: 211-219).
Additionally, Bach et al. showed that there was an increase in urinary triglycerides, and lipid deposits were seen by Oil Red O lipid staining in the cells of the collecting ducts and hyperplastic urothelia adjacent to the necrosed region.
It has also been shown that succinate and citrate concentrations are significantly lower in the urine of BEA-treated rats (Holmes et al. (1995), Arch Toxicol 70:
89-95).
Moreover, BEA treatment induced glutaric and adipic aciduria, which is symptomatic of an enzyme deficiency in the acyl CoA dehydrogenases. The same study examined urinary taurine levels in desert mice, and in BEA-treated desert mice there was an increase in the urinary taurine level which is indicative of liver toxicity.
Another study on BEA-treated rats showed that there was an increase in the concentrations of creatine in the renal papilla and glutaric acid in the liver, renal cortex, and renal medulla as soon as 6 hours post-treatment (Garrod et al. (2001), Magn Reson Med 45: 781-790).
Discovered and purified in the early 1960's, gentamicin is a broad-spectrum aminoglycoside antibiotic that is cidal to aerobic gram-negative bacteria and commonly used to treat infections, e.g., those of the urinary tract, lungs and meninges. As is typical for an aminoglycoside, the compound is made of two amino sugar rings linked to a central aminocyclitol ring by glycosidic bonds. Aminoglycosides are absorbed poorly with oral administration, but are excreted rapidly by the kidneys. As a result, kidney toxicity is the main adverse effect, although ototoxicity and neuromuscular blockade can also occur. Gentamicin acts by interfering with bacterial protein synthesis.
This compound is more potent than most other antibacterial inhibitors of protein synthesis, which are merely bacteriostatic, and its effects on the body are, likewise, more severe (Goodman & Gilman's The Pharmalogical Basis of Therapeutics 9'~ ed., pp. 1103-1115, J.G. Hardman et al. Eds., McGraw Hill, New York, 1996).
Aminoglycosides work rapidly, and the rate of bacterial killing is concentration-dependent. Residual bactericidal activity remains after serum concentration has fallen below the minimum inhibitory concentration (MIC), with a duration that is also dosage/concentration-dependent. The residual activity allows for once-a-day administration in some patients. These drugs diffuse into bacterial cells through porin channels in the outer membrane and are then transported across the cytoplasmic _g_ membrane via a membrane potential that is negative on the inside (Goodman &
Gilman, supra).
Kidney damage, which can develop into renal failure, is due to the attack of gentamicin on the proximal convoluted tubule, particularly in the S 1 and S2 segments.
The necrosis, however, is often patchy and focal (Shanley et al. (1990), Ren Fail 12: 83-87). A rat study by Shanley et al. showed that superficial nephrons are more susceptible to necrosis than juxtamedullary nephrons, although the initial segment of the superficial nephrons is remarkably resistant to necrosis.
Reported enzymatic changes upon gentamicin treatment are increased activities of N-acetyl-beta-D-glucosaminidase and alkaline phosphatase and decreased activities of sphingomyelinase, cathepsin B, Na+!K+-ATPase, lactate dehydrogenase and NADPH
cytochrome C reductase, along with decreased protein synthesis and alpha-methylglucose transport (Monteil et al. (1993), Ren Fail 15: 475-483). An increase in gamma-glutamyl transpeptidase activity in urine has also been reported (Kocaoglu et al.
(1994), Arch Immunol Ther Exp (Warsz) 42: 125-127), and the quantification of this enzyme in urine is a useful marker for monitoring gentamicin toxicity.
One source of renal pathology resulting from gentamicin treatment is the generation of reactive oxygen metabolites. Gentamicin has been shown, both in vitro and in vivo, to be capable of enhancing the production of reactive oxygen species. Iron, a necessary co-factor that catalyzes free-radical formation, is supplied by cytochrome P450 (Baliga et al. (1999), Drug Metab Rev 31: 971-997).
A gene delivery experiment in rats, in which the human kallikrein gene was cloned into an adenovirus vector and the construct then co-administered with a gentamicin preparation, showed that kallikrein can protect against gentamicin-induced nephrotoxicity. Significantly increased renal blood flow, glomerular filtration rates and urine flow were observed, along with decreased renal tubular damage, cellular necrosis and lumenal protein casts. Kallikrein gene delivery also caused a decrease in blood urea nitrogen levels and increases in urinary kinin and nitrite/nitrate levels.
This study provides evidence that the tissue kallikrein-kinin system may be a key pathway that is perturbed during the induction of nephrotoxicity by gentamicin (Murakami et al. (1998), Kidney Int 53: 1305-1313).

Ifosfamide, an alkylating agent, is commonly used in chemotherapy to treat testicular, cervical, and lung cancer. Ifosfamide is slowly activated in the liver by hydroxylation, forming the triazene derivative 5-(3,3-dimethyl-1-triazeno)-imidazole-4-carboxamide (DTIC) (Goodman & Gilman's The Pharmacological Basis of Therapeutics S 9"' ed., p.1235, J.G. Hardman et al., Eds., McGraw Hill, New York, 1996).
Cytochrome P450 activates DTIC via an N-demethylation reaction yielding an alkylating moiety, diazomethane. The active metabolites are then able to cross-link DNA causing growth arrest and cell death. Though ifosfamide is therapeutically useful, it is also associated with nephrotoxicity, urotoxicity, and central neurotoxicity.
Mesna, another therapeutic, is often administered concomitantly to prevent kidney and bladder problems from arising (Brock and Pohl (1986), IARC Sci Publ 78:
269-279). However, there are documented cases in which tubular toxicity occurred and elevated urinary levels of alanine aminopeptidase and N-acetyl-beta-D-glucosaminidase were found in patients even though mesna was administered alongside ifosfamide (Goren et al. (1987), Cancer Treat Rep 71: 127-130).
One study examined 42 patients that had been administered ifosfamide to treat advanced soft-tissue sarcoma (Stuart-Harris et al. (1983), Cancer Chemother Pharmacol 11: 69-72). The ifosfamide dosage varied from S.0 g/m2 to 8.0 g/mz, and all of the .
patients were given mesna to counteract the negative effects of ifosfamide.
Even so, nausea and vomiting were common to all of the patients. Out of the 42 patients, seven developed nephrotoxicity, and two of the cases progressed to fatal renal failure.
In another clinical study, renal tubular function was monitored in 18 neuroblastoma patients (Caron et al. (1992), Med Pediatr Oncol 20: 42-47).
Tubular toxicity occurred in at least 12 of the patients, and seven of those patients eventually developed Debre-de Toni-Fanconi syndrome, although in 3 cases the syndrome was reversible.
Fanconi syndrome is a disorder marked by dysfunction of the proximal tubules of the kidney. It is associated with aminoaciduria, renal glycosuria, and hyperphosphaturia.
Ifosfamide is often used experimentally on rats to induce Fanconi syndrome. In one study, rats that were administered 80 mg/kg of ifosfamide had significantly lower body weight and hematocrit than control rats (Springate and Van Liew (1995), .I
Appl Toxicol 15: 399-402). Additionally, the rats had low-grade glucosuria, proteinuria, and phosphaturia. In a mouse study, ifosfamide induced elevated serum creatinine and urea levels and decreased the clearance rate of creatinine (Badary (1999), JEthnopharmacol 67: 135-142).
Cyclophosphamide, a nitrogen mustard and alkylating agent, is highly toxic to dividing cells and is commonly used in chemotherapy to treat malignant lymphomas, such as non-Hodgkin's lymphomas and Burkitt's lymphoma, multiple myeloma, leukemias, neuroblastomas, ovarian adenocarcinomas and retinoblastomas, as well as breast and lung cancer (Goodman & Gilman's The Pharmacological Basis of Therapeutics 9'~ ed., pp.1234, 1237-1239, J.G. Hardman et al., eds., McGraw Hill, New York, 1996; Physicians Desk Reference, 47'~ ed., pp. 744-745, Medical Economics Co., Inc., Montvale, NJ, 1993). Additionally, cyclophosphamide is used as an immunosuppressive agent in bone marrow transplantation and following organ transplantation. Although cyclophosphamide is therapeutically useful against certain types of cancer, it is also associated with cardiotoxicity, nephrotoxicity (including renal tubular necrosis), hemorrhagic cystitis, myelosuppression, hepatotoxicity, impairment of male and female reproductive systems, interstitial pneumonitis and central nervous system toxicity.
Once in the liver, cyclophosphamide is hydroxylated by the cytochrome P450 mixed function oxidase system, producing the active metabolites phosphoramide mustard and acrolein, which cross-link DNA and cause growth arrest and cell death.
These metabolites, however, are highly toxic and cause adverse effects in the other organs into which they are transported, such as the kidneys. Acrolein is removed from the kidneys by secretion into the urine, resulting in cystitis (inflammation of the bladder), often hemorrhagic cystitis.
In the kidney, cyclophosphamide induces necrosis of the renal distal tubule.
Cyclophosphamide, which is structurally similar to the anti-cancer drug ifosfamide, does not induce damage to the renal proximal tubule nor does it induce Debre-de Toni-Fanconi syndrome (Rossi et al. (1997), Nephrol Dial Transplant 12: 1091-1092).
One clinical trial of patients being treated with cyclophosphamide showed that renal damage from the drug leads to a reduced biotransformation rate and low renal clearance of the drug, resulting in a build-up of toxic alkylating metabolic products (Wagner et al. (1980), Arzneimittelforschung 30: 1588-1592).

In a study of patients suffering from malignant lymphomas and mammary carcinomas, a direct relationship was found between the dose of cyclophosphamide used in treatment and the concentration of allcylating metabolites in the patients' urine. The upper limit of the dose was determined by the nature and degree of the toxic side effects, rather than by the rate at which the drug could be metabolized (Said et al.
(1979), J
Cancer Res Clin Oncol 94: 277-286). It is the acrolein itself that is toxic, not the alkylating activity of cyclophosphamide (Brock et al. (1979), Arzneimittelforschung 29:
659-661). A study on rats also showed that acrolein from the kidneys can produce hemorrhagic cystitis and that the acrolein concentration is directly related to the frequency and severity of the cystitis (Chijiwa et al. (1983), Cancer Res 43:
5205-5209).
Carboplatin, a platinum coordination complex, is commonly used in chemotherapy as an anti-tumor agent. As a chemotherapeutic agent, carboplatin acts similarly to cisplatin. Carboplatin enters the cell by diffusion where it is activated by hydrolysis (Goodman & Gilman's The Pharmacological Basis of Therapeutics 9th ed., p.
1270-1271, J.G. Hardman et al. Eds., McGraw Hill, New York 1996). Once activated, the platinum complexes are able to react with DNA causing cross-linking to occur. One of the differences between carboplatin and cisplatin is that carboplatin is better tolerated clinically. Some of the side-effects associated with cisplatin, such as nausea, neurotoxicity, and nephrotoxicity, are seen at a lesser degree in patients administered carboplatin. Some other side-effects are hypomagnesaemia and hypokalaemia (Kintzel (2001), Drug Saf 24: 19-38).
In one study on male Wistar rats, carboplatin was administered at a dosage of 65mg/kg (Wolfgang et al. (1994), Fundam Appl Toxicol 22: 73-79). After treatment with carboplatin, CGT excretion was increased approximately two-fold.
Another study compared cisplatin and carboplatin when given in combination with vindesine and mitomycin C (Jelic et al. (2001) Lung Cancer 34: 1-13). The study showed that carboplatin administered with vindesine and mitomycin C was advantageous in terms of overall survival, although the regimen was more hematologically toxic than when cisplatin was given.
AY-25329, is a phenothiazine that has been shown to be mildly hepatotoxic and to induce nephrosis. Its structure is shown below.

i i CI N
O' v 'N
~NJ
Phenothiazines are a class of psychoactive drugs. They have been used to treat schizophrenia, paranoia, mania, hyperactivity in children, some forms of senility, and anxiety (http://www.encyclopedia.com/articlesnew/ 36591.htm1). Some side effects associated with prolonged use of the drugs are reduced blood pressure, Parkinsonism, reduction of motor activity, and visual impairment.
Chlorpromazine (Thorazine or Largactil) is an aliphatic phenothiazine and is widely used for treating schizophrenia and manic depression. Prolactin secretion is increased while taking chlorpromazine, and galactorrhea and gynecomastia have both been associated with the drug (http://www.mentalhealth.com/drug/p30-cOl.html).
Trifluoperazine is another prescribed phenothiazine. It is used to treat anxiety, to prevent nausea and vomiting, and to manage psychotic disorders (http://www.mentalhealth.com/
drug/p30-s04.html). Negative side-effects that have been associated with the drug are liver damage, bone marrow depression, and Parkinsonism.
Acyclovir (9-[(2-hydroxyethyl) methyl] guanine, Zovirax~), an anti-viral guanosine analogue, is used to treat herpes simplex virus (HSV), varicella zoster virus (VZV) and Epstein-Barr virus (EBV) infections. It is transported into cells by the nucleoside transporter that imports guanine, and acyclovir is phosphorylated by virally encoded thymidine kinase (TK). Other kinases convert acyclovir to its activated di- and triphosphate forms, which prevent the polymerization of viral DNA. Acyclovir triphosphate competes with dGTP for the viral polymerase, and acyclovir is preferentially incorporated, but as a monophosphate. As a result, chain elongation ceases (Fields Virology 3d ed., Fields et al., eds., pp. 436-440, Lippincott-Raven Publishers, Philadelphia, 1996; Cecil Textbook of Medicine. 20"' ed., part XII, p. 1742, J. C. Bennett and F. Plum Eds., W. B. Saunders Co., Philadelphia, 1996).
The pharmacokinetics of acyclovir show that it has a useful half life of about three hours and that most of it is excreted in the urine largely unchanged (Brigden et al.
(1985), Scand Jlnfect Dis Suppl 47: 33-39). Not surprisingly, the most frequent adverse effect of acyclovir treatment is damage to various parts of the kidney, particularly the renal tubules. Crystalluria, or the precipitation of crystals (in this case, crystals of acyclovir), in the lumina of the renal tubules can occur (Fogazzi (1996), Nephrol Dial Transplant 11: 379-387). If the drug crystallizes in the renal collecting tubules, obstructive nephropathy and tubular necrosis can result (Richardson (2000), Vet Hum Toxicol 42: 370-371). Tissues from biopsies of affected patients showed dilation of the proximal and distal renal tubules, with loss of the brush border, flattening of the lining cells and focal nuclear loss (Becker et al. (1993), Am JKidney Dis 22: 611-615).
Citrinin, a mycotoxin produced by the fungus Penicillium citrinum, is a natural contaminant of foods and feeds (Bondy and Armstrong (1998) Cell Biol. Toxicol.
14:
323-332). It is known that mycotoxins can have negative effects on the immune system, however citrinin-treated animals have been shown to stimulate responses against antigens (Sharma (1993) J. Dairy Sci. 76: 892-897). Citrinin is a known nephrotoxin, and in birds such as chickens, ducklings, and turkeys, it causes diarrhea, increased food consumption and reduced weight gain due to kidney degeneration (Mehdi et al. ( 1981 ) Food Cosmet. Toxicol. 19: 723-733; Mehdi et al. (1984) Vet. Pathol. 21: 216-223). In the turkey and duckling study, both species exhibited nephrosis with the occurrence of hepatic and lymphoid lesions (Mehdi et al., 1984).
In one study, citrinin was administered to rabbits as a single oral dose of either 120 or 67 mg/kg (Hanika et al. (1986) Vet. Pathol. 23: 245-253). Rabbits treated with citrinin exhibited renal alterations such as condensed and distorted mitochondria, distended intercellular spaces of the medullary and straight cortical distal tubules, and disorganization of interdigitating processes. In another rabbit study, citrinin-administered rabbits displayed azotaemia and metabolic acidosis (Hanika et al.
(1984) Food Chem. Toxicol. 22: 999-1008). Renal failure was indicated by decreased creatinine clearance and increased blood urea nitrogen and serum-creatinine levels.
In the past, mercury was an important component of pharmaceuticals, particularly of antiseptics, antibacterials, skin ointments, diuretics and laxatives.
Although, mercury has been largely replaced by more effective, more specific and safer compounds, making drug-induced mercury poisoning rare, it is still widely used in industry.
Poisoning from occupational exposure and environmental pollution, such as mercury release into public water supplies, remains a concern as wildlife, domestic animals and humans are affected.

Because of their lipid solubility and ability to cross the blood-brain barrier, the most dangerous form of mercury is the organomercurials, the most common of which is methylmercury, a fungicide used for disinfecting crop seeds. In a number of countries, incidents involving large-scale illness and death from mercury poisoning have been reported when mercury-contaminated seeds were planted and the crops harvested and consumed. A second source of organic mercury poisoning results from industrial chemicals containing inorganic mercury, such as mercury catalysts, which form methylmercury as a reaction product. If this waste product is released into reservoirs, lakes, rivers or bays, the surrounding population can become sick or die, particularly those who eat local fish.
The inorganic salt mercuric chloride, HgCl2, as well as other mercuric salts, are more irritating and more toxic than the mercurous forms. Mercuric chloride is used today in industry, for the manufacture of bleach, electronics, plastics, fungicides and dental amalgams. The main source of human exposure is industrial dumping into rivers (Goodman & Gilinan's: The Pharmacological Basis of Therapeutics (9th ed.), pp.

1659, McGraw-Hill, New York, 1996).
When inorganic mercury salts are ingested, about 10% of the mercuric ions are absorbed by the gastrointenstinal tract, and a considerable portion of the Hg2+can remain bound to the mucosal surfaces. The highest concentration of Hg2+ is found in the kidneys, as it is retained there longer than in other tissues. Consequently, the kidneys are the organ most adversely affected by inorganic mercury poisoning. The proximal tubules are the major site of damage, where tubular necrosis results. The mercury affects primarily the S2 and S3 portions of the proximal tubules, but, at high levels of mercury exposure, the S 1 and distal portions of the tubules are also damaged. These regions of the nephrons are affected because they contain enzymes (such as gamma-glutamyltranspeptidase) and transport proteins (such as the basolateral organic anion transport system) involved in mercury uptake (Diamond et al. ~ (1998), Toxicol Pathol 26:
92-103).
Urinary markers of mercury toxicity which can be detected in NMR spectra include elevated levels of lactate, acetate and taurine and decreased levels of hippurate (Holmes et al. (2000), Chem Res Toxicol 13: 471-478). Known changes in gene expression in kidneys exposed to Hg2+ include up-regulation of the heat-shock protein hsp72 and of the glucose-regulated protein grp94. The degree of tissue necrosis and level of expression of these proteins is proportional to both the dose of mercury (Hgz+) and the length of the exposure time to mercury (Hgz+), with hsp72 accumulating in the renal cortex and grp94 accumulating in the renal medulla (Goering et al.
(2000), Toxicol Sci 53: 447-457).
Diflunisal, a non-steroidal anti-inflammatory drug (NSAID), is a difluorophenyl derivative of salicylic acid (Goodman & Gilman's The Pharmacological Basis of Therapeutics 9'~ ed., p. 631, J.G. Hardman et al., Eds., McGraw Hill, New York, 1996).
It is most frequently used in the treatment of osteoarthritis and musculoskeletal strains.
NSAIDs have analgesic, antipyretic and anti-inflammatory actions, however hepatotoxicity is known to be an adverse side effect of NSAID treatment (Masubuchi et al. (1998) J. Pharmacol. Exp. Ther. 287: 208-213). Diflunisal has been shown to be less toxic than other NSAIDs, nevertheless over long periods of dosage it can lead to deleterious effects on platelet or kidney function (Bergamo et al. (1989) Am.
J. Nephrol.
1 S 9: 460-463). Other side effects that have been associated with diflunisal treatment are diarrhea, dizziness, drowsiness, gas or heartburn, headache, nausea, vomiting, and insomnia (http://arthritisinsight.com/medical/ meds/dolobid.html).
Masubuchi et al. compared the hepatotoxicity of 18 acidic NSAIDs. In the study, diflunisal (administered at a concentration of S00 pM) was shown to increase LDH
leakage in rat hepatocytes, a marker for cell injury, when compared to the control sample. In addition, treatment with diflunisal led to decreased intracellular ATP
concentrations.
One study compared the effects of diflunisal and ibuprofen when given to patients over a two week period (Muncie and Nasrallah (1989) Clin. Ther. 11:
539-544).
In both the ibuprofen and the diflunisal group, two patients complained of abdominal cramping. The study indicated that even during short-term usage some gastrointestinal effects may occur. The toxic dose used in this study was chosen as one that did not induce significant gastric ulceration in rats. The group of rats given the high dosage of diflunisal had increased concentrations of creatinine which is consistent with renal injury, although dehydration may also cause increases in creatinine concentration.
Cidofovir (Vistide~) is an antiviral cytosine analog used in the treatment of viral infections such as herpesvirus, adenovirus, papillomavirus, poxvirus and hepadnavirus (Goodman & Gilman's The Pharmacological Basis of Therapeutics 9"' ed., p.
1216, J.G.
Hardman et al., Eds., McGraw Hill, New York, 1996). It is also useful for the treatment of cytomegalovirus (CMV) infection, which is a type of herpesvirus.
Some mild side effects seen in patients receiving cidofovir are nausea, vomiting, S and fever. The most serious reported side effect of the drug is kidney toxicity (http://tthivclinic. com/cido.html). In response to the threat of nephrotoxicity, it is necessary for patients receiving cidofovir to have their kidneys checked before treatment, and the patients must be monitored during treatment for early symptoms of kidney problems. In addition, cidofovir is given with fluids to help reduce the risk of kidney toxicity (http://www.aidsinfonyc.org/ network/simple/cido.html). Probenecid, a drug that helps protect the kidneys, is normally administered concomitantly (Lalezari and Kuppermann (1997) J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 14: S27-31).
One study compared the safety and efficacy of cidofovir in the treatment of CMV
(Lalezari et al. (1998) J. Acquir. Immune Defic. Syndr. Hum. Retrovirol. 17:
339-344).
Approximately 40% of the patients exhibited dose-dependent asymptomatic proteinuria and 25% of the patients had elevated serum creatinine levels.
Pamidronate (Aredia~) is a bisphosphonate drug that is clinically used to inhibit bone resorption and make bones more stable. It is used to treat hypercalcemia (too much calcium in the blood) that occurs with some types of cancer. Typically administered by intravenous injection, pamidronate is frequently used in patients with breast cancer or multiple myeloma whose disease has spread to the bones. Some side effects related to pamidronate treatment are abdominal cramps, chills, confusion, fever, muscle spasms, nausea, muscle stiffness, and swelling at the injection site (http://www.nursing.
uiowa.edu/sites/PedsPain/Adjuvants/PAMIDRnt.html). Patients with kidney problems may be prohibited from using pamidronate as it is excreted through the kidneys.
In one study, rats and mice were given varying doses of labeled pamidronate (Cal and Daley-Yates (1990) Toxicology 65: 179-197). Pamidronate treatment led to significant weight loss and a decrease in creatinine clearance. Morphological studies showed a loss of brush border membranes and the presence of focal proximal tubular necrosis.
Another study compared the tolerability of different treatments for hypercalcemia of malignancy by reviewing articles published between 1979 and 1998 (Zojer et al.

(1999) Drug Saf. 21: 389-406). The authors found that elevated serum creatinine level, nausea, and fever were reported following treatment with bisphosphonates such as pamidronate.
Markowitz et al. (2001, J. Am. Soc. Nephrol. 12: 1164-1172) tried to determine S whether there was a correlation between pamidronate treatment and collapsing focal segmental glomerulosclerosis (FSGS). The authors examined the histories of seven patients who had developed collapsing FSGS, and they found that the only drug treatment in common was the administration of pamidronate. When given at the recommended dose of 90 mg per month, renal toxicity was rare. However, when pamidronate was given at higher doses nephrotoxicity occurred.
Lithium, an alkali metal, is the main pharmacological treatment for bipolar disorders. It is typically given as a salt, such as lithium carbonate or lithium citrate.
Some common side effects of lithium treatment are an increase in urination, increase in drinking, dry mouth, weight gain, fine tremor, and fatigue. Some more serious side effects related to lithium treatment are blurred vision, mental confusion, seizures, vomiting, diarrhea, muscle weakness, drowsiness, and coarse tremor (Goodman &
Gilman's The Pharmacological Basis of Therapeutics 9'~ ed., p. 448, J.G.
Hardman et al., Eds., McGraw Hill, New York, 1996).
Since lithium is often used on a maintenance basis for a lifelong period, numerous studies have been performed to try and elucidate the effects of lithium on the kidney. One group administered lithium in daily doses within the human therapeutic range to male Wistar rats (Kung et al. (1984) Lab Invest 50: 526-535). Rats that were given lithium developed marked polyuric within three weeks of the initial dosing. The rats displayed elevated free water clearance and vasopressin-resistant diabetes insipidus.
The cortical collecting tubules displayed morphological changes, e.g. dilation of the tubules, bulging cells lining the tubules, enlarged nuclei, following lithium treatment.
Another study examined a human population that had been given lithium for the treatment of bipolar disorder (Markowitz et al. (2000) .l. Am. Soc. Nephrol.
11: 1439-1448). The patients had a mean age of 42.5 years and had been undergoing lithium treatment from 2 to 25 years (mean of 13.6 years). Approximately one fourth of the patients had nephrotic proteinuria, almost 90% of them had nephrogenic diabetes insipidus (NDI), and renal biopsies revealed a chronic tubulointerstitial nephropathy in all of the patients. Following cessation of lithium treatment, seven of the patients proceeded to end-stage renal disease.
Even though nephrotoxicity is a known side effect of lithium treatment, some studies have indicated that in actuality it is not all that common (Johnson (1998) Neuropsychopharmacology 19: 200-205). One study showed that the NDI-like effect in lithium treatment was easily overcome by increasing the levels of arginine vasopressin (AVP) (Carney et al. (1996) Kidney Int 50: 377-383). Other studies have suggested that patients with psychiatric disorders display certain defects in renal function without undergoing lithium treatment (Gitlin (1999) Drug Saf 20: 231-243).
Hydralazine, an antihypertensive drug, causes relaxation of arteriolar smooth muscle. Such vasodilation is linked to vigorous stimulation of the sympathetic nervous system, which in turn leads to increased heart rate and contractility, increased plasma renin activity, and fluid retention (Goodman & Gilman's The Pharmacological Basis of Therapeutics 9"' ed., p. 794, J.G. Hardman et al., Eds., McGraw Hill, New York, 1996).
The increased renin activity leads to an increase in angiotensin II, which in turn causes stimulation of aldosterone and sodium reabsorption.
Hydralazine is used for the treatment of high blood pressure (hypertension) and for the treatment of pregnant women suffering from high blood pressure (pre-eclampsia or eclampsia). Some common side effects associated with hydralazine use are diarrhea, rapid heartbeat, headache, decreased appetite, and nausea. Hydralazine is often used concomitantly with drugs that inhibit sympathetic activity to combat the mild pulmonary hypertension that can be associated with hydralazine usage.
In one hydralazine study, rats were fed hydralazine and mineral metabolism was monitored (Peters et al. (1988) Toxicol Lett 41: 193-202). Manganese and zinc concentrations were not effected by hydralazine treatment, however tissue iron concentrations were decreased and kidney copper concentrations were increased compared to control groups.
Another study compared the effects of hydrazine, phenelzine, and hydralazine treatment on rats (Runge-Morris et al. (1996) Drug Metab Dispos 24: 734-737).
Hydralazine caused an increase in renal GST-alpha subunit expression, although unlike hydrazine and phenelzine it did not alter renal cytochrome P4502E1 expression.

Colchicine, an alkoloid of Colchicum autumale, is an antiinflammatory agent used in the treatment of gouty arthritis (Goodman & Gilman's The Pharmacological Basis of Therapeutics 9'" ed., p. 647, J.G. Hardman et al., Eds., McGraw Hill, New York, 1996).
An antimitotic agent, colchicine binds to tubulin which leads to depolymerization and disappearance of the fibrillar microtubules in granulocytes and other motile cells. In doing so, the migration of granulocytes into the inflamed area is inhibited.
Through a series of events, the inflammatory response is blocked.
Some common, mild side effects associated with colchicine treatment are loss of appetite and hair loss. More severe side effects that warrant cessation of treatment are nausea, vomiting, diarrhea, and abdominal pain. Colchicine overdose can induce multiorgan failure with a high incidence of mortality. In this setting, renal failure is multifactorial and related to prolonged hypotension, hypoxemia, sepsis, and rhabdomyolysis. In rats, less dramatic doses have been shown to inhibit the secretion of many endogenous proteins such as insulin and parathyroid hormone.
One study investigated the effects of colchicine on microtubule polymerization status and post-translational modifications of tubulin in rat seminiferous tubules (Correa and Miller (2001) Biol Reprod 64: 1644-1652). Colchicine caused extensive microtubule depolymerization, and total tubulin levels decreased twofold after colchicine treatment. The authors also found that colchicine treatment led to a decrease in tyrosination of the microtubule pool of tubulin which was associated with depolymerization of microtubules.
Sulfadiazine, a sulfonamide, is an antimicrobial agent. It is commonly used concomitantly with pyrimethamine to treat toxoplasmosis, an infection of the brain, in patient suffering from AIDS. These drugs are able to cross the blood-brain barner and are used at relatively high doses. In addition, sulfadiazine has been shown to be effective at preventing certain types of meningococcal diseases and in treating urinary tract infections.
Sulfonamides in general are structural analogs of para-aminobenzoic acid (PABA). Because they are competitive antagonists of PABA, sulfonamides are effective against bacteria that are required to utilize PABA for the synthesis of folic acid (Goodman & Gilman's The Pharmacological Basis of Therapeutics 9"' ed., p. 1058-1060, J.G. Hardman et al., Eds., McGraw Hill, New York, 1996).
The main side effects associated with sulfadiazine treatment are fever and skin rashes. Decreases in white blood cells, red blood cells, and platelets, nausea, vomiting, and diarrhea are some other side effects that may result from sulfadiazine treatment. The most troublesome problem with this drug for HIV/AIDS patients is kidney toxicity.
These patients tend to use these drugs for extended periods of time, which puts a constant strain on the kidneys. In addition, kidney stones tend to form in the bladder and ureter thereby blocking the flow of urine. Kidney damage may result, and if left untreated kidney failure may occur. Therefore, patients being treated with sulfadiazine are instructed to increase their fluid intake in order to prevent crystal formation in the kidneys.
One case study examined four HIV-positive patients who had been given sulfadiazine to treat toxoplasmosis (Crespo et al. (2000) Clin Nephrol 54: 68-72). All four of the patients, one of whom was a previously healthy person, developed oliguria, abdominal pain, renal failure, and displayed multiple radiolucent renal calculi in echography. Following extensive hydration and alcalinization, the renal function of the patients returned to normal.
Adriamycin, known generically as doxorubicin, is an anthracycline antibiotic produced by the fungus Streptomyces peucetius. It is an anti-tumor drug used in the treatment of breast, ovarian, bladder, and lung cancers as well as non-Hodgkin's lymphoma, Hodgkin's disease and sarcoma (Goodman & Gilman's The Pharmacological Basis of Therapeutics 9"' ed., p. 1264-1265, J.G. Hardman et al., Eds., McGraw Hill, New York, 1996).
Adriamycin has tetracycline ring structures with the sugar daunosamine attached by glycosidic linkage. It is able to intercalate with DNA, it affects DNA and RNA
synthesis, and it can interact with cell membranes and alter their functions.
Typically the drug is cell-cycle specific for the S phase of cell division. By binding to the cancer cells' DNA and blocking topoisomerase II, cancer cells are unable to divide and grow.
Some common side effects associated with adriamycin treatment are fatigue, a drop in white blood cell, red blood cell, or platelet count, hair loss, skin discoloration, and watery eyes (www.cancerhelp.org.uk/help/default.asp?page=4025). More serious side effects include myocardial toxicity, ulceration and necrosis of the colon, and development of a second cancer.
Because of its utility in fighting cancer, numerous studies have been performed in attempts to further understand the mechanisms and effects of adriamycin. In one study, investigators injected mice with a single dose of adriamycin (Chen et al.
(1998) Nephron 78: 440-452). The mice exhibited signs of combined glomerular albuminuria and immunoglublinuria, progressively elevated levels of nitrite/nitrate in the urine, abnormal renal function, and other symptoms indicative of focal segmental glomerulosclerosis.
In another study, rats were given adriamycin and the effects on angiotensin converting enzyme (ACE) were monitored (Venkatesan et al. (1993) Toxicology 85: 137-148). The rats developed glomerular and tubular injury, and serum ACE levels were significantly elevated 20, 25, and 30 days post-treatment. A different study followed rabbits for up to one year that were treated with either adriamycin, nephrectomy, or combinations thereof (Gadeholt-Gothlin et al. (1995) Urol Res 23: 169-173).
The rabbits that were treated with adriamycin exhibited signs of nephrotoxicity at relatively low doses.
Toxicity Prediction and Modeling The genes and gene expression information, gene expression profiles, as well as the portfolios and subsets of the genes provided in Tables 1-5, may be used to predict at least one toxic effect, including the nephrotoxicity of a test or unknown compound. As used, herein, at least one toxic effect includes, but is not limited to, a detrimental change in the physiological status of a cell or organism. The response may be, but is not required to be, associated with a particular pathology, such as tissue necrosis.
Accordingly, the toxic effect includes effects at the molecular and cellular level.
Nephrotoxicity is an effect as used herein and includes but is not limited to the pathologies of nephritis, kidney necrosis, glomerular and tubular injury, and focal segmental glomerulosclerosis. As used herein, a gene expression profile comprises any quantitative representation of the expression of at least one mRNA species in a cell sample or population and includes profiles made by various methods such as differential display, PCR, hybridization analysis, etc.
In general, assays to predict the toxicity or nephrotoxicity of a test agent (or compound or multi-component composition) comprise the steps of exposing a cell population to the test compound, assaying or measuring the level of relative or absolute gene expression of one or more of the genes in Tables 1-5 and comparing the identified expression levels) to the expression levels disclosed in the Tables and databases) disclosed herein. Assays may include the measurement of the expression levels of about 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 50, 75, 100 or more genes from Tables 1-5.
In the methods of the invention, the gene expression level for a gene or genes induced by the test agent, compound or compositions may be comparable to the levels found in the Tables or databases disclosed herein if the expression level varies within a factor of about 2, about 1.5 or about 1.0 fold. In some cases, the expression levels are comparable if the agent induces a change in the expression of a gene in the same direction (e.g., up or down) as a reference toxin.
The cell population that is exposed to the test agent, compound or composition may be exposed in vitro or in vivo. For instance, cultured or freshly isolated renal cells, in particular rat renal cells, may be exposed to the agent under standard laboratory and cell culture conditions. In another assay format, in vivo exposure may be accomplished by administration of the agent to a living animal, for instance a laboratory rat.
Procedures for designing and conducting toxicity tests in in vitro and in vivo systems are well known, and are described in many texts on the subject, such as Loomis et al., Loomis's Esstentials of Toxicology, 4th Ed., Academic Press, New York, 1996;
Echobichon, The Basics of Toxicity Testing,,CRC Press, Boca Raton, 1992;
Frazier, editor, In Vitro Toxicity Testing, Marcel Dekker, New York, 1992; and the like.
In in vitro toxicity testing, two groups of test organisms are usually employed:
One group serves as a control and the other group receives the test compound in a single dose (for acute toxicity tests) or a regimen of doses (for prolonged or chronic toxicity tests). Because, in some cases, the extraction of tissue as called for in the methods of the invention requires sacrificing the test animal, both the control group and the group receiving compound must be large enough to permit removal of animals for sampling tissues, if it is desired to observe the dynamics of gene expression through the duration of an experiment.
In setting up a toxicity study, extensive guidance is provided in the literature for selecting the appropriate test organism for the compound being tested, route of administration. dose ranges, and the like. Water or physiological saline (0.9%
NaCI in water) is the solute of choice for the test compound since these solvents permit administration by a variety of routes. When this is not possible because of solubility limitations, vegetable oils such as corn oil or organic solvents such as propylene glycol may be used.
Regardless of the route of administration, the volume required to administer a given dose is limited by the size of the animal that is used. It is desirable to keep the volume of each dose uniform within and between groups of animals. When rats or mice are used, the volume administered by the oral route generally should not exceed about 0.005 ml per gram of animal. Even when aqueous or physiological saline solutions are used for parenteral injection the volumes that are tolerated are limited, although such solutions are ordinarily thought of as being innocuous. The intravenous LDso of distilled water in the mouse is approximately 0.044 ml per gram and that of isotonic saline is 0.068 ml per gram of mouse. In some instances, the route of administration to the test animal should be the same as, or as similar as possible to, the route of administration of 1 S the compound to man for therapeutic purposes.
When a compound is to be administered by inhalation, special techniques for generating test atmospheres are necessary. The methods usually involve aerosolization or nebulization of fluids containing the compound. If the agent to be tested is a fluid that has an appreciable vapor pressure, it may be administered by passing air through the solution under controlled temperature conditions. Under these conditions, dose is estimated from the volume of air inhaled per unit time, the temperature of the solution, and the vapor pressure of the agent involved. Gases are metered from reservoirs. When particles of a solution are to be administered, unless the particle size is less than about 2 pm the particles will not reach the terminal alveolar sacs in the lungs. A
variety of apparatuses and chambers are available to perform studies for detecting effects of irritant or other toxic endpoints when they are administered by inhalation. The preferred method of administering an agent to animals is via the oral route, either by intubation or by incorporating the agent in the feed.
When the agent is exposed to cells in vitro or in cell culture, the cell population to be exposed to the agent may be divided into two or more subpopulations, for instance, by dividing the population into two or more identical aliquots. In some preferred embodiments of the methods of the invention, the cells to be exposed to the agent are derived from kidney tissue. For instance, cultured or freshly isolated rat renal cells may be used.
The methods of the invention may be used generally to predict at least one toxic response, and, as described in the Examples, may be used to predict the likelihood that a compound or test agent will induce various specific kidney pathologies, such as nephritis, kidney necrosis, glomerular and tubular injury, focal segmental glomerulosclerosis, or other pathologies associated with at least one of the toxins herein described. The methods of the invention may also be used to determine the similarity of a toxic response to one or more individual compounds. In addition, the methods of the invention may be used to predict or elucidate the potential cellular pathways influenced, induced or modulated by the compound or test agent due to the similarity of the expression profile compared to the profile induced by a known toxin (see Tables 5-SCC).
Diagnostic Uses for the Toxicity Markers As described above, the genes and gene expression information or portfolios of 1 S the genes with their expression information as provided in Tables 1-5 may be used as diagnostic markers for the prediction or identification of the physiological state of tissue or cell sample that has been exposed to a compound or to identify or predict the toxic effects of a compound or agent. For instance, a tissue sample such as a sample of peripheral blood cells or some other easily obtainable tissue sample may be assayed by any of the methods described above, and the expression levels from a gene or genes from Tables 1-S may be compared to the expression levels found in tissues or cells exposed to the toxins described herein. These methods may result in the diagnosis of a physiological state in the cell or may be used to identify the potential toxicity of a compound, for instance a new or unknown compound or agent. The comparison of expression data, as well as available sequence or other information may be done by researcher or diagnostician or may be done with the aid of a computer and databases as described below.
In another format, the levels of a genes) of Tables 1-5, its encoded protein(s), or any metabolite produced by the encoded protein may be monitored or detected in a sample, such as a bodily tissue or fluid sample to identify or diagnose a physiological state of an organism. Such samples may include any tissue or fluid sample, including urine, blood and easily obtainable cells such as peripheral lymphocytes.

Use of the Markers for Monitoring Toxicity Progression As described above, the genes and gene expression information provided in Tables 1-5 may also be used as markers for the monitoring of toxicity progression, such as that found after initial exposure to a drug, drug candidate, toxin, pollutant, etc. For instance, a tissue or cell sample may be assayed by any of the methods described above, and the expression levels from a gene or genes from Tables 1-5 may be compared to the expression levels found in tissue or cells exposed to the renal toxins described herein.
The comparison of the expression data, as well as available sequence or other information may be done by a researcher or diagnostician or may be done with the aid of a computer and databases.
Use of the Toxicity Markers for Drug Screening According to the present invention, the genes identified in Tables 1-5 may be used as markers or drug targets to evaluate the effects of a candidate drug, chemical compound or other agent on a cell or tissue sample. The genes may also be used as drug targets to screen for agents that modulate their expression and/or activity.
In various formats, a candidate drug or agent can be screened for the ability to stimulate the transcription or expression of a given marker or markers or to down-regulate or counteract the transcription or expression of a marker or markers. According to the present invention, one can also compare the specificity of a drug's effects by looking at the number of markers which the drug induces and comparing them. More specific drugs will have less transcriptional targets. Similar sets of markers identified for two drugs may indicate a similarity of effects.
Assays to monitor the expression of a marker or markers as defined in Tables 1-may utilize any available means of monitoring for changes in the expression level of the nucleic acids of the invention. As used herein, an agent is said to modulate the expression of a nucleic acid of the invention if it is capable of up- or down-regulating expression of the nucleic acid in a cell.
In one assay format, gene chips containing probes to one, two or more genes from Tables 1-5 may be used to directly monitor or detect changes in gene expression in the treated or exposed cell. Cell lines, tissues or other samples are first exposed to a test agent and in some instances, a known toxin, and the detected expression levels of one or more, or preferably 2 or more of the genes of Tables 1-S are compared to the expression levels of those same genes exposed to a known toxin alone. Compounds that modulate the expression patterns of the known toxins) would be expected to modulate potential toxic physiological effects in vivo. The genes in Tables 1-5 are particularly appropriate markers in these assays as they are differentially expressed in cells upon exposure to a known renal toxin. Tables 1 and 2 disclose those genes that are differentially expressed upon exposure to the named toxins and their corresponding GenBank Accession numbers. Table 3 discloses the human homologues and the corresponding GenBank Accession numbers of the differentially expressed genes of Tables 1 and 2.
In another format, cell lines that contain reporter gene fusions between the open reading frame and/or the transcriptional regulatory regions of a gene in Tables 1-5 and any assayable fusion partner may be prepared. Numerous assayable fusion partners are known and readily available including the firefly luciferase gene and the gene encoding chloramphenicol acetyltransferase (Alum et al. (1990), Anal Biochem 188: 245-254).
Cell lines containing the reporter gene fusions are then exposed to the agent to be tested under appropriate conditions and time. Differential expression of the reporter gene between samples exposed to the agent and control samples identifies agents which modulate the expression of the nucleic acid.
Additional assay formats may be used to monitor the ability of the agent to modulate the expression of a gene identified in Tables 1-5. For instance, as described above, mRNA expression may be monitored directly by hybridization of probes to the nucleic acids of the invention. Cell lines are exposed to the agent to be tested under appropriate conditions and time, and total RNA or mRNA is isolated by standard procedures such those disclosed in Sambrook et al. (Molecular Cloning: A
Laboratory Manual, 2nd Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1989).
In another assay format, cells or cell lines are first identified which express the gene products of the invention physiologically. Cells and/or cell lines so identified would be expected to comprise the necessary cellular machinery such that the fidelity of modulation of the transcriptional apparatus is maintained with regard to exogenous contact of agent with appropriate surface transduction mechanisms and/or the cytosolic cascades. Further, such cells or cell lines may be transduced or transfected with an expression vehicle (e.g., a plasmid or viral vector) construct comprising an operable non-translated 5'-promoter containing end of the structural gene encoding the gene products of Tables 1-5 fused to one or more antigenic fragments or other detectable markers, which are peculiar to the instant gene products, wherein said fragments are under the transcriptional control of said promoter and are expressed as polypeptides whose molecular weight can be distinguished from the naturally occurring polypeptides or may further comprise an immunologically distinct or other detectable tag. Such a process is well known in the art (see Sambrook et al., supra).
Cells or cell lines transduced or transfected as outlined above are then contacted with agents under appropriate conditions; for example, the agent comprises a pharmaceutically acceptable excipient and is contacted with cells comprised in an aqueous physiological buffer such as phosphate buffered saline (PBS) at physiological pH, Eagles balanced salt solution (BSS) at physiological pH, PBS or BSS
comprising serum or conditioned media comprising PBS or BSS and/or serum incubated at 37°C.
Said conditions may be modulated as deemed necessary by one of skill in the art.
Subsequent to contacting the cells with the agent, said cells are disrupted and the polypeptides of the lysate are fractionated such that a polypeptide fraction is pooled and contacted with an antibody to be further processed by immunological assay (e.g., ELISA, immunoprecipitation or Western blot). The pool of proteins isolated from the agent-contacted sample is then compared with the control samples (no exposure and exposure to a known toxin) where only the excipient is contacted with the cells and an increase or decrease in the immunologically generated signal from the agent-contacted sample compared to the control is used to distinguish the effectiveness and/or toxic effects of the agent.
Another embodiment of the present invention provides methods for identifying agents that modulate at least one activity of a proteins) encoded by the genes in Tables 1-5. Such methods or assays may utilize any means of monitoring or detecting the desired activity.
In one format, the relative amounts of a protein (Tables 1-5) between a cell population that has been exposed to the agent to be tested compared to an un-exposed control cell population and a cell population exposed to a known toxin may be assayed.
In this format, probes such as specific antibodies are used to monitor the differential expression of the protein in the different cell populations. Cell lines or populations are exposed to the agent to be tested under appropriate conditions and time.
Cellular lysates may be prepared from the exposed cell line or population and a control, unexposed cell line or population. The cellular lysates are then analyzed with the probe, such as a specific antibody.
Agents that are assayed in the above methods can be randomly selected or rationally selected or designed. As used herein, an agent is said to be randomly selected when the agent is chosen randomly without considering the specific sequences involved in the association of a protein of the invention alone or with its associated substrates, binding partners, etc. An example of randomly selected agents is the use a chemical library or a peptide combinatorial library, or a growth broth of an organism.
As used herein, an agent is said to be rationally selected or designed when the agent is chosen on a nonrandom basis which takes into account the sequence of the target site and/or its conformation in connection with the agent's action. Agents can be rationally selected or rationally designed by utilizing the peptide sequences that make up these sites. For example, a rationally selected peptide agent can be a peptide whose amino acid sequence is identical to or a derivative of any functional consensus site.
The agents of the present invention can be, as examples, peptides, small molecules, vitamin derivatives, as well as carbohydrates. Dominant negative proteins, DNAs encoding these proteins, antibodies to these proteins, peptide fragments of these proteins or mimics of these proteins may be introduced into cells to affect function.
"Mimic" used herein refers to the modification of a region or several regions of a peptide molecule to provide a structure chemically different from the parent peptide but topographically and functionally similar to the parent peptide (see G.A. Grant in:
Molecular Biology and Biotechnology, Meyers, ed., pp. 659-664, VCH Publishers, New York, 1995). A skilled artisan can readily recognize that there is no limit as to the structural nature of the agents of the present invention.
Nucleic Acid Assay Formats The genes identified as being differentially expressed upon exposure to a known renal toxin (Tables 1-S) may be used in a variety of nucleic acid detection assays to detect or quantify the expression level of a gene or multiple genes in a given sample.
The genes described in Tables 1-5 may also be used in combination with one or more additional genes whose differential expression is associate with toxicity in a cell or tissue. In preferred embodiments, the genes in Tables 1-5 may be combined with one or more of the genes described in prior and related applications 60/292,335;
60/297,523;
60/298,925; 60/303,810; 60/303,807; 60/303,808; 60/315,047; 60/324,928;
60/330,867;
60/330,462; 60/331,805; 60/336,144; 60/340,873; 60/357,843; 60/357,842;
60/357,844;
60/364,134; 60/370,206; 60/370,247; 60/370,144; 60/371,679; 60/372,794, 09/917,800 and 10/060,087 all of which are incorporated by reference on page 1 of this application.
Any assay format to detect gene expression may be used. For example, traditional Northern blotting, dot or slot blot, nuclease protection, primer directed amplification, RT- PCR, semi- or quantitative PCR, branched-chain DNA and differential display methods may be used for detecting gene expression levels.
Those methods are useful for some embodiments of the invention. In cases where smaller numbers of genes are detected, amplification based assays may be most efficient.
Methods and assays of the invention, however, may be most efficiently designed with hybridization-based methods for detecting the expression of a large number of genes.
Any hybridization assay format may be used, including solution-based and solid support-based assay formats. Solid supports containing oligonucleotide probes for differentially expressed genes of the invention can be filters, polyvinyl chloride dishes, particles, beads, microparticles or silicon or glass based chips, etc. Such chips, wafers and hybridization methods are widely available, for example, those disclosed by Beattie (WO 95/11755).
Any solid surface to which oligonucleotides can be bound, either directly or indirectly, either covalently or non-covalently, can be used. A preferred solid support is a high density array or DNA chip. These contain a particular oligonucleotide probe in a predetermined location on the array. Each predetermined location may contain more than one molecule of the probe, but each molecule within the predetermined location has an identical sequence. Such predetermined locations are termed features. There may be, for example, from 2, 10, 100, 1000 to 10,000, 100,000 or 400,000 or more of such features on a single solid support. The solid support, or the area within which the probes are attached may be on the order of about a square centimeter. Probes corresponding to the genes of Tables 1-5 or from the related applications described above may be attached to single or multiple solid support structures, e.g., the probes may be attached to a single chip or to multiple chips to comprise a chip set.
Oligonucleotide probe arrays for expression monitoring can be made and used according to any techniques known in the art (see for example, Lockhart et al.
(1996), Nat Biotechnol 14: 1675-1680; McGall et al. (1996), Proc Nat Acad Sci USA 93:

13460). Such probe arrays may contain at least two or more oligonucleotides that are complementary to or hybridize to two or more of the genes described in Tables 1-5. For instance, such arrays may contain oligonucleotides that are complementary to or hybridize to at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 20, 30, 50, 70, 100 or more of the genes described herein. Preferred arrays contain all or nearly all of the genes listed in Tables 1-5, or individually, the gene sets of Tables 5-SCC. In a preferred embodiment, arrays are constructed that contain oligonucleotides to detect all or nearly all of the genes in any one of or all of Tables 1-5 on a single solid support substrate, such as a chip.
The sequences of the expression marker genes of Tables 1-5 are in the public databases. Table 1 provides the GenBank Accession Number or NCBI RefSeq ID for each of the sequences (see www.ncbi.nlm.nih.gov~. Table 3 provides the LocusLink and Unigene names and descriptions for the human homologues of the genes described in Tables 1 and 2. The sequences of the genes in GenBank and/or RefSeq are expressly herein incorporated by reference in their entirety as of the filing date of this application, as are related sequences, for instance, sequences from the same gene of different lengths, variant sequences, polymorphic sequences, genomic sequences of the genes and related sequences from different species, including the human counterparts, where appropriate.
These sequences may be used in the methods of the invention or may be used to produce the probes and arrays of the invention. In some embodiments, the genes in Tables 1-5 that correspond to the genes or fragments previously associated with a toxic response may be excluded from the Tables.
As described above, in addition to the sequences of the GenBank Accession Numbers or NCBI RefSeq ID's disclosed in the Tables 1-5, sequences such as naturally occurring variants or polymorphic sequences may be used in the methods and compositions of the invention. For instance, expression levels of various allelic or homologous forms of a gene disclosed in Tables 1-5 may be assayed. Any and all nucleotide variations that do not alter the functional activity of a gene listed in the Tables 1-5, including all naturally occurnng allelic variants of the genes herein disclosed, may be used in the methods and to make the compositions (e.g., arrays) of the invention.
Probes based on the sequences of the genes described above may be prepared by any commonly available method. Oligonucleotide probes for screening or assaying a tissue or cell sample are preferably of sufficient length to specifically hybridize only to appropriate, complementary genes or transcripts. Typically the oligonucleotide probes will be at least about 10, 12, 14, 16, 18, 20 or 25 nucleotides in length. In some cases, longer probes of at least 30, 40, or 50 nucleotides will be desirable.
As used herein, oligonucleotide sequences that are complementary to one or more of the genes described in Tables 1-5 refer to oligonucleotides that are capable of hybridizing under stringent conditions to at least part of the nucleotide sequences of said genes. Such hybridizable oligonucleotides will typically exhibit at least about 75%
sequence identity at the nucleotide level to said genes, preferably about 80%
or 85%
sequence identity or more preferably about 90% or 95% or more sequence identity to said genes.
"Bind(s) substantially" refers to complementary hybridization between a probe nucleic acid and a target nucleic acid and embraces minor mismatches that can be accommodated by reducing the stringency of the hybridization media to achieve the desired detection of the target polynucleotide sequence.
The terms "background" or "background signal intensity" refer to hybridization signals resulting from non-specific binding, or other interactions, between the labeled target nucleic acids and components of the oligonucleotide array (e.g., the oligonucleotide probes, control probes, the array substrate, etc.). Background signals may also be produced by intrinsic fluorescence of the array components themselves. A
single background signal can be calculated for the entire array, or a different background signal may be calculated for each target nucleic acid. In a preferred embodiment, background is calculated as the average hybridization signal intensity for the lowest 5%
to 10% of the probes in the array, or, where a different background signal is calculated for each target gene, for the lowest 5% to 10% of the probes for each gene. Of course, one of skill in the art will appreciate that where the probes to a particular gene hybridize well and thus appear to be specifically binding to a target sequence, they should not be used in a background signal calculation. Alternatively, background may be calculated as the average hybridization signal intensity produced by hybridization to probes that are not complementary to any sequence found in the sample (e.g. probes directed to nucleic acids of the opposite sense or to genes not found in the sample such as bacterial genes where the sample is mammalian nucleic acids). Background can also be calculated as the average signal intensity produced by regions of the array that lack any probes at all.
The phrase "hybridizing specifically to" or "specifically hybridizes" refers to the binding, duplexing, or hybridizing of a molecule substantially to or only to a particular nucleotide sequence or sequences under stringent conditions when that sequence is present in a complex mixture (e.g., total cellular) DNA or RNA.
Assays and methods of the invention may utilize available formats to simultaneously screen at least about 100, preferably about 1000, more preferably about 10,000 and most preferably about 1,000,000 different nucleic acid hybridizations.
As used herein a "probe" is defined as a nucleic acid, capable of binding to a target nucleic acid of complementary sequence through one or more types of chemical bonds, usually through complementary base pairing, usually through hydrogen bond formation. As used herein, a probe may include natural (i.e., A, G, U, C, or T) or modified bases (7-deazaguanosine, inosine, etc.). In addition, the bases in probes may be joined by a linkage other than a phosphodiester bond, so long as it does not interfere with hybridization. Thus, probes may be peptide nucleic acids in which the constituent bases are joined by peptide bonds rather than phosphodiester linkages.
The term "perfect match probe" refers to a probe that has a sequence that is perfectly complementary to a particular target sequence. The test probe is typically perfectly complementary to a portion (subsequence) of the target sequence. The perfect match (PM) probe can be a "test probe", a "normalization control" probe, an expression level control probe and the like. A perfect match control or perfect match probe is, however, distinguished from a "mismatch control" or "mismatch probe."
The terms "mismatch control" or "mismatch probe" refer to a probe whose sequence is deliberately selected not to be perfectly complementary to a particular target sequence. For each mismatch (MM) control in a high-density array there typically exists a corresponding perfect match (PM) probe that is perfectly complementary to the same particular target sequence. The mismatch may comprise one or more bases.
While the mismatches) may be located anywhere in the mismatch probe, terminal mismatches are less desirable as a terminal mismatch is less likely to prevent hybridization of the target sequence. In a particularly preferred embodiment, the mismatch is located at or near the center of the probe such that the mismatch is most likely to destabilize the duplex with the target sequence under the test hybridization conditions.
The term "stringent conditions" refers to conditions under which a probe will hybridize to its target subsequence, but with only insubstantial hybridization to other sequences or to other sequences such that the difference may be identified.
Stringent conditions are sequence-dependent and will be different in different circumstances.
Longer sequences hybridize specifically at higher temperatures. Generally, stringent conditions are selected to be about S°C lower than the thermal melting point (Tm) for the specific sequence at a defined ionic strength and pH.
Typically, stringent conditions will be those in which the salt concentration is at least about 0.01 to 1.0 M Na+ ion concentration (or other salts) at pH 7.0 to 8.3 and the temperature is at least about 30°C for short probes (e.g., 10 to 50 nucleotides). Stringent conditions may also be achieved with the addition of destabilizing agents such as formamide.
The "percentage of sequence identity" or "sequence identity" is determined by comparing two optimally aligned sequences or subsequences over a comparison window or span, wherein the portion of the polynucleotide sequence in the comparison window may optionally comprise additions or deletions (i.e., gaps) as compared to the reference sequence (which does not comprise additions or deletions) for optimal alignment of the two sequences. The percentage is calculated by determining the number of positions at which the identical submit (e.g. nucleic acid base or amino acid residue) occurs in both sequences to yield the number of matched positions, dividing the number of matched positions by the total number of positions in the window of comparison and multiplying the result by 100 to yield the percentage of sequence identity. Percentage sequence identity when calculated using the programs GAP or BESTFIT (see below) is calculated using default gap weights.
Probe design One of skill in the art will appreciate that an enormous number of array designs are suitable for the practice of this invention. The high density array will typically include a number of test probes that specifically hybridize to the sequences of interest.
Probes may be produced from any region of the genes identified in the Tables and the attached representative sequence listing. In instances where the gene reference in the Tables is an EST, probes may be designed from that sequence or from other regions of the corresponding full-length transcript that may be available in any of the sequence databases, such as those herein described. See WO 99/32660 for methods of producing probes for a given gene or genes. In addition, any available software may be used to produce specific probe sequences, including, for instance, software available from Molecular Biology Insights, Olympus Optical Co. and Biosoft International. In a preferred embodiment, the array will also include one or more control probes.
High density array chips of the invention include "test probes." Test probes may be oligonucleotides that range from about 5 to about 500, or about 7 to about SO
nucleotides, more preferably from about 10 to about 40 nucleotides and most preferably from about 15 to about 35 nucleotides in length. In other particularly preferred embodiments, the probes are 20 or 25 nucleotides in length. In another preferred embodiment, test probes are double or single strand DNA sequences such as cDNA
fragments. DNA sequences are isolated or cloned from natural sources or amplified from natural sources using native nucleic acid as templates. These probes have sequences complementary to particular subsequences of the genes whose expression they are designed to detect. Thus, the test probes are capable of specifically hybridizing to the target nucleic acid they are to detect.
In addition to test probes that bind the target nucleic acids) of interest, the high density array can contain a number of control probes. The control probes may fall into three categories referred to herein as 1) normalization controls; 2) expression level controls; and 3) mismatch controls.
Normalization controls are oligonucleotide or other nucleic acid probes that are complementary to labeled reference oligonucleotides or other nucleic acid sequences that are added to the nucleic acid sample to be screened. The signals obtained from the normalization controls after hybridization provide a control for variations in hybridization conditions, label intensity, "reading" efficiency and other factors that may cause the signal of a perfect hybridization to vary between arrays. In a preferred embodiment, signals (e.g., fluorescence intensity) read from all other probes in the array are divided by the signal (e.g., fluorescence intensity) from the control probes thereby normalizing the measurements.
Virtually any probe may serve as a normalization control. However, it is recognized that hybridization efficiency varies with base composition and probe length.
Preferred normalization probes are selected to reflect the average length of the other probes present in the array, however, they can be selected to cover a range of lengths.
The normalization controls) can also be selected to reflect the (average) base composition of the other probes in the array, however in a preferred embodiment, only one or a few probes are used and they are selected such that they hybridize well (i.e., no secondary structure) and do not match any target-specific probes.
Expression level controls are probes that hybridize specifically with constitutively expressed genes in the biological sample. Virtually any constitutively expressed gene provides a suitable target for expression level controls. Typically expression level control probes have sequences complementary to subsequences of constitutively expressed "housekeeping genes" including, but not limited to the actin gene, the transferrin receptor gene, the GAPDH gene, and the like.
Mismatch controls may also be provided for the probes to the target genes, for expression level controls or for normalization controls. Mismatch controls are oligonucleotide probes or other nucleic acid probes identical to their corresponding test or control probes except for the presence of one or more mismatched bases. A
mismatched base is a base selected so that it is not complementary to the corresponding base in the target sequence to which the probe would otherwise specifically hybridize.
One or more mismatches are selected such that under appropriate hybridization conditions (e.g., stringent conditions) the test or control probe would be expected to hybridize with its target sequence, but the mismatch probe would not hybridize (or would hybridize to a significantly lesser extent). Preferred mismatch probes contain a central mismatch. Thus, for example, where a probe is a 20 mer, a corresponding mismatch probe will have the identical sequence except for a single base mismatch (e.g., substituting a G, a C or a T for an A) at any of positions 6 through 14 (the central mi smatch).
Mismatch probes thus provide a control for non-specific binding or cross hybridization to a nucleic acid in the sample other than the target to which the probe is directed. For example, if the target is present the perfect match probes should be consistently brighter than the mismatch probes. In addition, if all central mismatches are present, the mismatch probes can be used to detect a mutation, for instance, a mutation of a gene in the accompanying Tables 1-5. The difference in intensity between the perfect match and the mismatch probe provides a good measure of the concentration of the hybridized material.
Nucleic Acid Samples Cell or tissue samples may be exposed to the test agent in vitro or in vivo.
When cultured cells or tissues are used, appropriate mammalian cell extracts, such as liver extracts, may also be added with the test agent to evaluate agents that may require biotransformation to exhibit toxicity. In a preferred format, primary isolates of animal or human renal cells which already express the appropriate complement of drug-metabolizing enzymes may be exposed to the test agent without the addition of mammalian kidney extracts.
The genes which are assayed according to the present invention are typically in the form of mRNA or reverse transcribed mRNA. The genes may or may not be cloned.
The genes may or may not be amplified. The cloning and/or amplification do not appear to bias the representation of genes within a population. In some assays, it may be preferable, however, to use polyA+ RNA as a source, as it can be used with less processing steps. -As is apparent to one of ordinary skill in the art, nucleic acid samples used in the methods and assays of the invention may be prepared by any available method or process. Methods of isolating total mRNA are well known to those of skill in the art.
For example, methods of isolation and purification of nucleic acids are described in detail in Chapter 3 of Laboratory Techniques in Biochemistry and Molecular Biology Vol. 24, Hybridization With Nucleic Acid Probes: Theory and Nucleic Acid Probes, P.
Tijssen, Ed., Elsevier Press, New York, 1993. Such samples include RNA
samples, but also include cDNA synthesized from a mRNA sample isolated from a cell or tissue of interest. Such samples also include DNA amplified from the cDNA, and RNA
transcribed from the amplified DNA. One of skill in the art would appreciate that it is desirable to inhibit or destroy RNase present in homogenates before homogenates are used.
Biological samples may be of any biological tissue or fluid or cells from any organism as well as cells raised in vitro, such as cell lines and tissue culture cells.
Frequently the sample will be a tissue or cell sample that has been exposed to a compound, agent, drug, pharmaceutical composition, potential environmental pollutant or other composition. In some formats, the sample will be a "clinical sample"
which is a sample derived from a patient. Typical clinical samples include, but are not limited to, sputum, blood, blood-cells (e.g., white cells), tissue or fine needle biopsy samples, urine, S peritoneal fluid, and pleural fluid, or cells therefrom. Biological samples may also include sections of tissues, such as frozen sections or formalin fixed sections taken for histological purposes.
Forming High Density Arrays Methods of forming high density arrays of oligonucleotides with a minimal number of synthetic steps are known. The oligonucleotide analogue array can be synthesized on a single or on multiple solid substrates by a variety of methods, including, but not limited to, light-directed chemical coupling, and mechanically directed coupling (see Pirrung, U.S. Patent No. 5,143,854).
In brief, the light-directed combinatorial synthesis of oligonucleotide arrays on a glass surface proceeds using automated phosphoramidite chemistry and chip masking techniques. In one specific implementation, a glass surface is derivatized with a silane reagent containing a functional group, e.g., a hydroxyl or amine group blocked by a photolabile protecting group. Photolysis through a photolithographic mask is used selectively to expose functional groups which are then ready to react with incoming 5' photoprotected nucleoside phosphoramidites. The phosphoramidites react only with those sites which are illuminated (and thus exposed by removal of the photolabile blocking group). Thus, the phosphoramidites only add to those areas selectively exposed from the preceding step. These steps are repeated until the desired array of sequences have been synthesized on the solid surface. Combinatorial synthesis of different oligonucleotide analogues at different locations on the array is determined by the pattern of illumination during synthesis and the order of addition of coupling reagents.
In addition to the foregoing, additional methods which can be used to generate an array of oligonucleotides on a single substrate are described in PCT
Publication Nos.
WO 93/09668 and WO 01/23614. High density nucleic acid arrays can also be fabricated by depositing pre-made or natural nucleic acids in predetermined positions.
Synthesized or natural nucleic acids are deposited on specific locations of a substrate by light directed targeting and oligonucleotide directed targeting. Another embodiment uses a dispenser that moves from region to region to deposit nucleic acids in specific spots.
Hybridization Nucleic acid hybridization simply involves contacting a probe and target nucleic acid under conditions where the probe and its complementary target can form stable hybrid duplexes through complementary base pairing. See WO 99/32660. The nucleic acids that do not form hybrid duplexes are then washed away leaving the hybridized nucleic acids to be detected, typically through detection of an attached detectable label.
It is generally recognized that nucleic acids are denatured by increasing the temperature or decreasing the salt concentration of the buffer containing the nucleic acids. Under low stringency conditions (e.g., low temperature and/or high salt) hybrid duplexes (e.g., DNA:DNA, RNA:RNA, or RNA:DNA) will form even where the annealed sequences are not perfectly complementary. Thus, specificity of hybridization is reduced at lower stringency. Conversely, at higher stringency (e.g., higher temperature or lower salt) successful hybridization tolerates fewer mismatches. One of skill in the art will 1 S appreciate that hybridization conditions may be selected to provide any degree of stringency.
In a preferred embodiment, hybridization is performed at low stringency, in this case in 6x SSPET at 37°C (0.005% Triton X-100), to ensure hybridization and then subsequent washes are performed at higher stringency (e.g., lx SSPET at 37°C) to eliminate mismatched hybrid duplexes. Successive washes may be performed at increasingly higher stringency (e.g., down to as low as 0.25x SSPET at 37°C to SO°C) until a desired level of hybridization specificity is obtained. Stringency can also be increased by addition of agents such as formamide. Hybridization specificity may be evaluated by comparison of hybridization to the test probes with hybridization to the various controls that can be present (e.g., expression level control, normalization control, mismatch controls, etc.).
In general, there is a tradeoff between hybridization specificity (stringency) and signal intensity. Thus, in a preferred embodiment, the wash is performed at the highest stringency that produces consistent results and that provides a signal intensity greater than approximately 10% of the background intensity. Thus, in a preferred embodiment, the hybridized array may be washed at successively higher stringency solutions and read between each wash. Analysis of the data sets thus produced will reveal a wash stringency above which the hybridization pattern is not appreciably altered and which provides adequate signal for the particular oligonucleotide probes of interest.
Signal Detection The hybridized nucleic acids are typically detected by detecting one or more labels attached to the sample nucleic acids. The labels may be incorporated by any of a number of means well known to those of skill in the art. See WO 99/32660.
Databases The present invention includes relational databases containing sequence information, for instance, for the genes of Tables 1-5, as well as gene expression information from tissue or cells exposed to various standard toxins, such as those herein described (see Tables 5-5CC). Databases may also contain information associated with a given sequence or tissue sample such as descriptive information about the gene associated with the sequence information (see Tables 1 and 2), or descriptive information concerning the clinical status of the tissue sample, or the animal from which the sample was derived. The database may be designed to include different parts, for instance a sequence database and a gene expression database. Methods for the configuration and construction of such,databases and computer-readable media to which such databases are saved are widely available, for instance, see U.S. Patent No. 5,953,727, which is herein incorporated by reference in its entirety.
The databases of the invention may be linked to an outside or external database such as GenBank (www.ncbi.nlm.nih.govlentrez.index.html); KEGG
(www.genome.ad jplkegg); SPAR (www.grt.kyushu-u.ac jplspadlindex.html); HLTGO
(www.gene.ucl.ac.uklhugo); Swiss-Prot (www.expasy.ch.sprot); Prosite (www.expasy.chltoolslscnpsitl.html); OMIM (www.ncbi.nlm.nih.govlomim); and GDB
(www.gdb.org). In a preferred embodiment, as described in Tables 1-5, the external database is GenBank and the associated databases maintained by the National Center for Biotechnology Information (NCBI) (www.ncbi.nlm.nih.gov).
Any appropriate computer platform, user interface, etc. may be used to perform the necessary comparisons between sequence information, gene expression information and any other information in the database or information provided as an input.
For example, a large number of computer workstations are available from a variety of manufacturers, such has those available from Silicon Graphics. Client/server environments, database servers and networks are also widely available and appropriate platforms for the databases of the invention.
The databases of the invention may be used to produce, among other things, electronic Northerns that allow the user to determine the cell type or tissue in which a S given gene is expressed and to allow determination of the abundance or expression level of a given gene in a particular tissue or cell.
The databases of the invention may also be used to present information identifying the expression level in a tissue or cell of a set of genes comprising one or more of the genes in Tables 1-5, comprising the step of comparing the expression level of at least one gene in Tables 1-5 in a cell or tissue exposed to a test agent to the level of expression of the gene in the database. Such methods may be used to predict the toxic potential of a given compound by comparing the level of expression of a gene or genes in Tables 1-5 from a tissue or cell sample exposed to the test agent to the expression levels found in a control tissue or cell samples exposed to a standard toxin or renal toxin such as those herein described. Such methods may also be used in the drug or agent screening assays as described herein.
Kits The invention further includes kits combining, in different combinations, high-density oligonucleotide arrays, reagents for use with the arrays, protein reagents encoded by the genes of the Tables, signal detection and array-processing instruments, gene expression databases and analysis and database management software described above.
The kits may be used, for example, to predict or model the toxic response of a test compound, to monitor the progression of renal disease states, to identify genes that show promise as new drug targets and to screen known and newly designed drugs as discussed above.
The databases packaged with the kits are a compilation of expression patterns from human or laboratory animal genes and gene fragments (corresponding to .the genes of Tables 1-5). In particular, the database software and packaged information that may contain the databases saved to a computer-readable medium include the expression results of Tables 1-5 that can be used to predict toxicity of a test agent by comparing the expression levels of the genes of Tables 1-5 induced by the test agent to the expression levels presented in Tables 5-SCC. In another format, database and software information may be provided in a remote electronic format, such as a website, the address of which may be packaged in the kit.
The kits may used in the pharmaceutical industry, where the need for early drug testing is strong due to the high costs associated with drug development, but where bioinformatics, in particular gene expression informatics, is still lacking.
These kits will reduce the costs, time and risks associated with traditional new drug screening using cell cultures and laboratory animals. The results of large-scale drug screening of pre-grouped patient populations, pharmacogenomics testing, can also be applied to select drugs with greater efficacy and fewer side-effects. The kits may also be used by smaller biotechnology companies and research institutes who do not have the facilities for performing such large-scale testing themselves.
Databases and software designed for use with microarrays is discussed-in Balaban et al., U.S. Patent Nos. 6,229,911, a computer-implemented method for managing information, stored as indexed Tables 1-5, collected from small or large numbers of microarrays, and 6,185,561, a computer-based method with data mining capability for collecting gene expression level data, adding additional attributes and reformatting the data to produce answers to various queries. Chee et al., U.S. Patent No.
5,974,164, disclose a software-based method for identifying mutations in a nucleic acid sequence based on differences in probe fluorescence intensities between wild type and mutant sequences that hybridize to reference sequences.
Without further description, it is believed that one of ordinary skill in the art can, using the preceding description and the following illustrative examples, make and utilize the compounds of the present invention and practice the claimed methods. The following working examples therefore, specifically point out the preferred embodiments of the present invention, and are not to be construed as limiting in any way the remainder of the disclosure.

EXAMPLES
Example 1: Identification of Toxicity Markers The renal toxins cephaloridine, cisplatin, puromycin aminonucleoside (PAN), bromoethylamine hydrobromide (BEA), gentamicin, ifosfamide, cyclophosphamide, carboplatin, AY-25329, indomethacin, acyclovir, citrinin, mercuric chloride, diflunisal, cidofovir, pamidronate, lithium, hydralazine, colchicine, sulfadiazine, and adriamycin and control compositions were administered to male Sprague-Dawley rats at various timepoints using administration diluents, protocols and dosing regimes as previously described in the art and previously described in the priority applications discussed above.
The low and high dose level for each compound are provided in the chart below.
Renal Toxin Low Dose (mg/kg)High Dose (mglkg)Method of Administration ce haloridine _100 800 intravenous cis latin 1 5 intravenous PAN _ 10 150 intravenous BEA 10 200 intra eritoneal entamicin 2 80 intramuscular ifosfamide 5 100 intraeritoneal c clo hos hamide20 2000 intra eritoneal carbo latin 5 50 intravenous AY-25329 25 250 oral ava a indomethacin 1 10 oral ava a ac clovir 10 100 intra eritoneal citrinin 1 35 intra eritoneal mercuric chloride0.1 1 intravenous diflunisal 2 400 oral ava a cidofovir 10 100 intra eritoneal amidronate 1 60 intra eritoneal lithium 0.3 nmol/k 3 nmol/k intra eritoneal h dralazine 2.5 25 intra eritoneal colchicine 0.15 1.5 intra eritoneal sulfadiazine 100 1000 intravenous adriam cin 1.3 12.8 intravenous After administration, the dosed animals were observed and tissues were collected as described below:
OBSERVATION OF ANIMALS
1. Clinical Observations- Twice daily: mortality and moribundity check.
Cage Side Observations - skin and fur, eyes and mucous membrane, respiratory system, circulatory system, autonomic and central nervous system, somatomotor pattern, and behavior pattern.

Potential signs of toxicity, including tremors, convulsions, salivation, diarrhea, lethargy, coma or other atypical behavior or appearance, were recorded as they occurred and included a time of onset, degree, and duration.
2. Physical Examinations- Prior to randomization, prior to initial treatment, and prior to sacrifice.
3. Body Weights- Prior to randomization, prior to initial treatment, and prior to sacrifice.
CLINICAL PATHOLOGY
1. Frequency Prior to necropsy.
2. Number of animals All surviving animals.
3. Bleeding Procedure Blood was obtained by puncture of the orbital sinus while under 70% COZ/ 30% Oz anesthesia.
4. Collection of Approximately 0.5 mL of blood was Blood Samples collected into EDTA tubes for evaluation of hematology parameters. Approximately 1 mL of blood was collected into serum separator tubes for clinical chemistry analysis. Approximately 200 uL
of plasma was obtained and frozen at ~-80°C for test compound/metabolite estimation. An additional ~2 mL of blood was collected into a 15 mL conical polypropylene vial to which ~3 mL of Trizol was immediately added. The contents were immediately mixed with a vortex and by repeated inversion. The tubes were frozen in liquid nitrogen and stored at -r-80°C.
TERMINATION PROCEDURES
Terminal Sacrifice Approximately 3, 6, 24, 48, 72, 120, 144, 168, 336, and/or 360 hours after the initial dose, rats were weighed, physically examined, sacrificed by decapitation, and exsanguinated. The animals were necropsied within approximately five minutes of sacrifice. Separate sterile, disposable instruments were used for each animal, with the exception of bone cutters, which were used to open the skull cap. The bone cutters were dipped in disinfectant solution between animals.
Necropsies were conducted on each animal following procedures approved by board-certified pathologists.
Animals not surviving until terminal sacrifice were discarded without necropsy (following euthanasia by carbon dioxide asphyxiation, if moribund). The approximate time of death for moribund or found dead animals was recorded.
Postmortem Procedures Fresh and sterile disposable instruments were used to collect tissues.
Gloves were worn at all times when handling tissues or vials. All tissues were collected and frozen within approximately 5 minutes of the animal's death. The liver sections and kidneys were frozen within approximately 3-5 minutes of the animal's death. The time of euthanasia, an interim time point at freezing of liver sections and kidneys, and time at completion of necropsy were recorded. Tissues were stored at approximately -80°C or preserved in 10% neutral buffered formalin.
Tissue Collection and Processing Liver 1. Right medial lobe - snap frozen in liquid nitrogen and stored at ~-80°C.
2. Left medial lobe - Preserved in 10% neutral-buffered formalin (NBF) and evaluated for gross and microscopic pathology.
3. Left lateral lobe - snap frozen in liquid nitrogen and stored at ~-80°C.

Heart A sagittal cross-section containing portions of the two atria and of the two ventricles was preserved in 10% NBF. The remaining heart was frozen in liquid nitrogen and stored at ~ -80°C.
S Kidneys (both) 1. Left - Hemi-dissected; half was preserved in 10% NBF and the remaining half was frozen in liquid nitrogen and stored at ~ -80°C.
2. Right - Hemi-dissected; half was preserved in 10% NBF and the remaining half was frozen in liquid nitrogen and stored at ~ -80°C.
Testes (both) A sagittal cross-section of each testis was preserved in 10% NBF. The remaining testes were frozen together in liquid nitrogen and stored at ~-80°C.
Brain (whole) A cross-section of the cerebral hemispheres and of the diencephalon was preserved in 10% NBF, and the rest of the brain was frozen in liquid nitrogen and stored at ~ -80°C.
Microarray sample preparation was conducted with minor modifications, following the protocols set forth in the Affymetrix GeneChip Expression Analysis Manual. Frozen tissue was ground to a powder using a Spex Certiprep 6800 Freezer Mill. Total RNA was extracted with Trizol (GibcoBRL) utilizing the manufacturer's protocol. The total RNA yield for each sample was 200-500 ~,g per 300 mg tissue weight. mRNA was isolated using the Oligotex mRNA Midi kit (Qiagen) followed by ethanol precipitation. Double stranded cDNA was generated from mRNA using the Superscript Choice system (GibcoBRL). First strand cDNA synthesis was primed with a T7-(dT24) oligonucleotide. The cDNA was phenol-chloroform extracted and ethanol precipitated to a final concentration of 1 ~g/ml. From 2 ~g of cDNA, cRNA was synthesized using Ambion's T7 MegaScript in vitro Transcription Kit.
To biotin label the cRNA, nucleotides Bio-11-CTP and Bio-16-UTP (Enzo Diagnostics) were added to the reaction. Following a 37°C incubation for six hours, impurities were removed from the labeled cRNA following the RNeasy Mini kit protocol (Qiagen). cRNA was fragmented (fragmentation buffer consisting of 200 mM Tris-acetate, pH 8.1, 500 mM KOAc, 150 mM MgOAc) for thirty-five minutes at 94°C.
Following the Affymetrix protocol, 55 ~.g of fragmented cRNA was hybridized on the Affymetrix rat array set for twenty-four hours at 60 rpm in a 45°C
hybridization oven.
The chips were washed and stained with Streptavidin Phycoerythrin (SAPE) (Molecular Probes) in Affymetrix fluidics stations. To amplify staining, SAPE solution was added twice with an anti-streptavidin biotinylated antibody (Vector Laboratories) staining step in between. Hybridization to the probe arrays was detected by fluorometric scanning (Hewlett Packard Gene Array Scanner). Data was analyzed using Affymetrix GeneChip~ version 2.0 and Expression Data Mining (EDMT) software (version 1.0), GeneExpress2000, and S-Plus.
Tables 1 and 2 disclose those genes that are differentially expressed upon exposure to the named toxins and their corresponding GenBank Accession and Sequence Identification numbers, the identities of the metabolic pathways in which the genes function, the gene names if known, and the unigene cluster titles. The model code represents the various toxicity state that each gene is able to discriminate as well as the individual toxin type associated with each gene. The codes are defined in Table 4. The GLGC ID is the internal Gene Logic identification number.
Table 3 discloses those genes that are the human homologues of those genes in Tables l and 2 that are differentially expressed upon exposure to the named toxins. The corresponding GenBank Accession and Sequence Identification numbers, the gene names if known, and the unigene cluster titles of the human homologues are listed.
Table 4 defines the comparison codes used in Tables 1, 2, 3, and 5.
Tables 5-5CC disclose the summary statistics for each of the comparisons performed. Each of these tables contains a set of predictive genes and creates a model for predicting the renal toxicity of an unlrnown, i.e., untested compound.
Each gene is identified by its Gene Logic identification number and can be cross-referenced to a gene name and representative SEQ ID NO. in Tables 1 and 2. For each comparison of gene expression levels between samples in the toxicity group (samples affected by exposure to a specific toxin) and samples in the non-toxicity group (samples not affected by exposure to that same specific toxin), the tox mean (for toxicity group samples) is the mean signal intensity, as normalized for the various chip parameters that are being assayed. The non-tox mean represents the mean signal intensity, as normalized for the various chip parameters that are being assayed, in samples from animals other than those treated with the high dose of the specific toxin. These animals were treated with a low dose of the specific toxin, or with vehicle alone, or with a different toxin. Samples in the toxicity groups were obtained from animals sacrificed at the timepoint(s) indicated in the Table S
headings, while samples in the non-toxicity groups were obtained from animals sacrificed at all time points in the experiments. For individual genes, an increase in the tox mean compared to the non-tox mean indicates up-regulation upon exposure to a toxin. Conversely, a decrease in the tox mean compared to the non-tox mean indicates down-regulation.
The mean values are derived from Average Difference (AveDiff) values for a particular gene, averaged across the corresponding samples. Each individual Average Difference value is calculated by integrating the intensity information from multiple probe pairs that are tiled for a particular fragment. The normalization multiplies each expression intensity for a given experiment (chip) by a global scaling factor.
The intent of this normalization is to make comparisons of individual genes between chips possible.
The scaling factor is calculated as follows:
1. From all the unnormalized expression values in the experiment, delete the largest 2% and smallest 2% of the values. That is, if the experiment yields 10,000 expression values, order the values and delete the smallest 200 and largest 200.
2. Compute the trimmed mean, which is equal to the mean of the remaining values.
3. Compute the scale factor SF = 100/(trimmed mean) The value of 100 used here is the standard target valued used. Some AveDiff values may be negative due to the general noise involved in nucleic acid hybridization experiments. Although many conclusions can be made corresponding to a negative value on the GeneChip platform, it is difficult to assess the meaning behind the negative value for individual fragments. Our observations show that, although negative values are observed at times within the predictive gene set, these values reflect a real biological phenomenon that is highly reproducible across all the samples from which the measurement was taken. For this reason, those genes that exhibit a negative value are included in the predictive set. It should be noted that other platforms of gene expression measurement may be able to resolve the negative numbers for the corresponding genes.
The predictive ability of each of those genes should extend across platforms, however.
Each mean value is accompanied by the standard deviation for the mean. The linear discriminant analysis score (discriminant score), as disclosed in the tables, measures the ability of each gene to predict whether or not a sample is toxic. The discriminant score is calculated by the following steps:
Calculation of a discriminant score Let X; represent the AveDiff values for a given gene across the non-tox samples, i=1 ...n.
Let Y; represent the AveDiff values for a given gene across the tox samples, i=1 ...t.
The calculations proceed as follows:
1. Calculate mean and standard deviation for X;'s and Y;'s, and denote these by mX, my, sx,sY.
2. For all X;'s and Y;'s, evaluate the function f(z) _ ((1/sy)*exp( -.5*((z-mY)/sY)2)) /
(((1/sY)*exp( -.S*((z-mY)/sY)z)) +((1/s~*exp( -.5*((z-m,~/s~2))).
3. The number of correct predictions, say P, is then the number of Y;'s such that f(Y;)>.S
plus the number of X;'s such that f(X;)<.5.
4. The discriminant score is then P/(n+t).
Linear discriminant analysis uses both the individual measurements of each gene and the calculated measurements of all combinations of genes to classify samples. For each gene a weight is derived from the mean and standard deviation of the toxic and nontox groups. Every gene is multiplied by a weight and the sum of these values results in a collective discriminate score. This discriminant score is then compared against collective centroids of the tox and nontox groups. These centroids are the average of all tox and nontox samples respectively. Therefore, each gene contributes to the overall prediction. This contribution is dependent on weights that are large positive or negative numbers if the relative distances between the tox and nontox samples for that gene are large and small numbers if the relative distances are small. The discriminant score for each unknown sample and centroid values can be used to calculate a probability between zero and one as to the group in which the unknown sample belongs.

Example 2: General Toxicity Modeling Samples were selected for grouping into tox-responding and non-tox-responding groups by examining each study individually with Principal Components Analysis (PCA) to determine which treatments had an observable response. Only groups where confidence of their tox-responding and non-tox-responding status was established were included in building a general tox model (Table 5).
Linear discriminant models were generated to describe toxic and non-toxic samples. The top discriminant genes and/or EST's were used to determine toxicity by calculating each gene's contribution with homo and heteroscedastic treatment of variance and inclusion or exclusion of mutual information between genes. Prediction of samples within the database exceeded 80% true positives with a false positive rate of less than 5%. It was determined that combinations of genes and/or EST's generally provided a better predictive ability than individual genes and that the more genes and/or EST used the better predictive ability. Although the preferred embodiment includes fifty or more genes, many pairings or greater combinations of genes and/or EST can work better than individual genes. All combinations of two or more genes from the selected list (Table 5) could be used to predict toxicity. These combinations could be selected by pairing in an agglomerate, divisive, or random approach. Further, as yet undetermined genes and/or EST's could be combined with individual or combination of genes and/or EST's described here to increase predictive ability. However, the genes and/or EST's described here would contribute most of the predictive ability of any such undetermined combinations.
Other variations on the above method can provide adequate predictive ability.
These include selective inclusion of components via agglomerate, divisive, or random approaches or extraction of loading and combining them in agglomerate, divisive, or random approaches. Also the use of composite variables in logistic regression to determine classification of samples can also be accomplished with linear discriminate analysis, neural or Bayesian networks, or other forms of regression and classification based on categorical or continual dependent and independent variables.
Example 3: Modeling Methods The above modeling methods provide broad approaches of combining the expression of genes to predict sample toxicity. One could also provide no weight in a simple voting method or determine weights in a supervised or unsupervised method using agglomerate, divisive, or random approaches. All or selected combinations of genes may be combined in ordered, agglomerate, or divisive, supervised or unsupervised clustering algorithms with unknown samples for classification. Any form of correlation S matrix may also be used to classify unknown samples. The spread of the group distribution and discriminate score alone provide enough information to enable a skilled person to generate all of the above types of models with accuracy that can exceed discriminate ability of individual genes. Some examples of methods that could be used individually or in combination after transformation of data types include but are not limited to: Discriminant Analysis, Multiple Discriminant Analysis, logistic regression, multiple regression analysis, linear regression analysis, conjoint analysis, canonical correlation, hierarchical cluster analysis, k-means cluster analysis, self organizing maps, multidimensional scaling, structural equation modeling, support vector machine determined boundaries, factor analysis, neural networks, bayesian classifications, and resampling methods.
Example 4: Grounin~ of Individual compound and Patholo~v Classes Samples were grouped into individual pathology classes based on known toxicological responses and observed clinical chemical and pathology measurements or into early and late phases of observable toxicity within a compound (Tables SA-SCC).
The top 10, 25, 50, 100 genes based on individual discriminate scores were used in a model to ensure that combination of genes provided a better prediction than individual genes. As described above, all combinations of two or more genes from this list could pote~.tially provide better prediction than individual genes when selected in any order or by ordered, agglomerate, divisive, or random approaches. In addition, combining these genes with other genes could provide better predictive ability, but most of this predictive ability would come from the genes listed herein.
Samples may be considered toxic if they score positive in any pathological or individual compound class represented here or in any modeling method mentioned under general toxicology models based on combination of individual time and dose grouping of individual toxic compounds obtainable from the data. The pathological groupings and early and late phase models are preferred examples of all obtainable combinations of sample time and dose points. Most logical groupings with one or more genes and one or more sample dose and time points should produce better predictions of general toxicity, pathological specific toxicity, or similarity to known toxicant than individual genes.
Although the present invention has been described in detail with reference to S examples above, it is understood that various modifications can be made without departing from the spirit of the invention. Accordingly, the invention is limited only by the following claims. All cited patents, patent applications and publications referred to in this application are herein incorporated by reference in their entirety.

TABLE UMMARY -~ ~' ~, ~ptty. Dockets 1: Nod. ~44 S ~9-2~~~9W0 n ~
~, Doe. No. 179897.1 ~ ~ ~ r, ii .
Sequence GenBank Model Accl ~

IU No. IdentifierRef. Seq Code Gene Name 1~~~U,~n,~,igene G~luster IU ~ Title ~

1 6949 AA012785 q ESTs ~

2 25098 AA108277 h,v ESTs, Highly similar to includes exons 3 17312 AA108308 3 through 12 M.musculus r ESTs, Moderately similar to NADH-ubiquinone oxidoreductase subunit CI-4 16882 AA684537 o SGDH H.sapiens ESTs, Highly similar to alpha 6049 AA685178 y NAC/1.9.2. protein [M.musculus]

6 4426 AA685974 ,m ESTs I

ESTs, Weakly similar to T23657 hypothetical protein M01 F1.6 -7 21815 AA686423 g Caenorhabditis elegans [C.elegans]

DNA-damage inducible 8 1600 AA686470 t ranscri t 3 DNA-damage inducible i transcript 3 DNA-damage inducible 8 1599 AA686470 t ranscript 3 DNA-damage inducible i transcript 3 9 21997 AA799325 a ESTs ESTs, Highly similar to AF132951 1 18396 AA799330 v CGI-17 protein [H.sapiens ESTs, Weakly similar to ESR1 RAT

ESTROGEN RECEPTOR

11 6581 AA799412 ,l [R.norvegicus]
f ESTs, Weakly similar to nucleosome 12 16538 AA799449 k assembl protein R.norvegicus]

ESTs, Moderately similar to CGI-116 13 23294 AA799472 a protein [H.sapiens 14 18290 AA799497 ESTs r ESTs, Moderately similar to hnRNP

18981 AA799523 a protein [R.norvegicus]

ESTs, Weakly similar to TCPA RAT T-COMPLEX PROTEIN
1, ALPHA

16 20843 AA799545 h SUBUNIT R.norvegicus 17 16993 AA799560 b ESTs 18 16576 AA799570 d ESTs ESTs, Highly similar to TBB1 RAT

TUBULIN BETA CHAIN

19 18361 AA799591 [R.norvegicus i 17712 AA799598 z ESTs 22 18346 AA799718 ESTs f 23 8768 AA799726 ESTs I

ESTs, Highly similar to Dgcr6 protein 24 11687 AA799732 w [M.musculus]

18349 AA799744 a ESTs 26 17494 AA799751 n ESTs ' 27 18360 AA799771 General ESTs 28 18880 AA799801 w ESTs ESTs, Weakly similar to serine 29 20998 AA799803 z rotease R.norvegicus ESTs, Highly similar to IRF7 MOUSE

INTERFERON REGULATORY

21006 AA799861 c FACTOR 7 [M.musculus]

ESTs, Highly similar to DDRT helix-destabilizing protein - rat 31 15011 AA799893 General [R.norvegicus ESTs, Highly similar to 60S

RIBOSOMAL PROTEIN

32 20811 AA799899 a R.norvegicus]

ESTs, Weakly similar to S52675 probable membrane protein YDR109c yeast (Saccharomyces cerevisiae) 33 23202 AA799971 General S.cerevisiae ESTs, Highly similar to glycogen 34 4832 AA800190 b phos ho lase R.norvegicus 21656 AA800202 d ~ ESTs [

TABLE MMARY Atty. Docket No.
1: 44921-5U89W0 -SU

Doe. No. 1798397.1 Sequence GenBank Model iAccl '1U dentifierRef. Seq Code Gene Name Unigene Cluster No. ID Title I

ESTs, Weakly similar to T15476 hypothetical protein C09F5.2 -36 18433 AA800218 ,y,z Caenorhabditis j elegans C.elegans 37 6386 AA800235 a ESTs 38 18442 AA800258 h,k ESTs ESTs, Weakly similar to CORTICOSTEROID

DEHYDROGENASE, 39 21092 AA800380 R.norvegicus]

ESTs, Weakly similar to glutathione 40 17325 AA800587 General peroxidase [R.norvegicus]

cc, Rattus norvegicus gene for TIS11, 41 13930 AA800613 General complete cds 42 21372 AA800693 v ESTs 42 21373 AA800693 s ESTs 43 18161 AA800701 k ESTs 44 6595 AA800753 w ESTs 45 13348 AA800928 General ESTs ESTs, Highly similar to H2A1 RAT

46 23115 AA801165 0, HISTONE H2A.1 R.norvegicus]

47 12399 AA801307 General ESTs 48 7543 AA801395 General ESTs 49 24237 AA817726 ,General ESTs t ESTs, Moderately similar to T25763 hypothetical protein F46F11.4 -50 11215 AA817921 o Caenorhabditis elegans [C.elegans]

51 5985 AA818005 g ESTs ESTs, Highly similar to rabkinesin-6 52 11338 AA818016 [ M.musculus]
x ESTs, Weakly similar to PRSC

REGULATORY SUBUNIT

53 2845 AA818026 k,General M.musculus]

i ,k, ESTs, Highly similar to glycyl-tRNA

54 16756 AA818089 General synthetase [H.sa iens]

ESTs, Highly similar to TBBi RAT

e,g,p, TUBULIN BETA CHAIN

55 17771 AA818224 General[ R.norvegicus ESTs, Moderately similar to 56 6522 AA818261 g,m autoantigen 542 H.sapiens 57 5924 AA818359 ESTs 58 7806 AA818421 b,aa ESTs 59 8237 AA818512 v ESTs 60 17434 AA818574 h ESTs 61 8728 AA818615 General ESTs Diphtheria toxin receptor ( heparin bindingDiphtheria toxin epidermal receptor (heparin b,v,cc,rowth factor binding epidermal g - like growth growth factor - like 62 6054 AA818658 Generalactor) growth factor) f ESTs, Moderately similar to S65785 63 11590 AA818721 mel-13a rotein d - mouse [M.musculus]

64 4291 AA818741 ,General ESTs q 65 4330 AA818747 o,General ESTs 66 19723 AA818761 ,General ESTs v Rattus norvegicus serine protease 67 13684 AA818770 h,j,l,m gene, complete cds 68 6322 AA818801 k ESTs 69 7690 AA818875 Generalroguan lin uroguan lin u 70 4952 AA818907 ,General ESTs q 71 6094 AA818911 ESTs t ESTs, Weakly similar to HP33 72 10985 AA818998 o,General[ R.norvegicus]

73 6120 AA819008 ESTs t TABLE MMARY ~tty. Docket No.
1: 44931-5U89W0 SU

Uoc. No. 1798897.1 _-~

Sequence GenBank Model Acc/

IU No. dentifierRef. Seq Code Gene Narne Unig~"ene Cluster I ID Title ESTs, Weakly similar to testis specific 74 2586 AA819081 c rotein [R.norvegicus 76 6438 AA819269 o ESTs 77 24721 AA819306 d,w ESTs Rattus norvegicus mRNA for inositol hexakisphosphate kinase, complete 78 6250 AA819376 0, cds ESTs, Weakly similar to JC5707 80 6281 AA819517 HYA22 protein [H.sapiens j 81 10141 AA819526 ESTs j 82 6551 AA819558 ESTs t ESTs, Moderately similar to dJ30M3.1 83 6723 AA819653 [H.sa lens]
r 84 14958 AA819744 as ESTs ESTs, Weakly similar to HS98 RAT

HEAT SHOCK PROTEIN

85 19433 AA819776 v BETA [R.norvegicus 86 6204 AA819889 as ESTs ESTs, Weakly similar to guanosine HMm:inosine monophosphate reductase 5'-phosphate 87 22820 AA848315 Generaldeh drogenase [R.norvegicus ESTs, Weakly similar to T26686 hypothetical protein Y38F1A.6 -88 6614 AA848389 bb Caenorhabditis elegans C.elegans]

89 21125 AA848437 General ESTs ESTs, Moderately similar to IF4B_HUMAN EUKARYOTIC

TRANSLATION INITIATION
FACTOR

90 23504 AA848496 4B H.sapiens]

ESTs, Weakly similar to FM01 RAT

DIMETHYLANILINE

91 18532 AA848675 g MONOOXYGENASE [R.norvegicus 92 21140 AA848738 c ESTs ESTs, Moderately similar to AF132946 93 16128 AA848807 0 1 CGI-12 protein H.sapiens 94 22923 AA848929 g ESTs 95 17339 AA849497 General ESTs 96 11727 AA849518 ESTs I

i ,1,m, 97 21275 AA849796 General ESTs 98 16678 AA849827 as ESTs 99 8515 AA849917 a ESTs 100 18447 AA849939 General ESTs 101 12130 AA850037 ESTs cyclase-associated protein 102 23981 AA850040 ,aa homologue c clase-associated x protein homologue ESTs, Moderately similar to RB17 MOUSE RAS-RELATED
PROTEIN

103 13615 AA850364 RAB-17 M.musculus t ESTs, Highly similar to hypothetical 105 2637 AA850893 rotein H.sa iens]
x 106 22093 AA850909 ESTs d 107 21766 AA850916 ESTs c ESTs, Weakly similar to dithiolethione-108 2847 AA850919 w i nducible gene-1 R.norvegicus]

Rattus norvegicus mRNA for ras-GTPase-activating protein SH3-109 2162 AA850975 h domain binding 1 rotein, partial cds 110 9514 AA850978 General ESTs ESTs, Highly similar to molybdopterin-111 3924 AA851017 ,q s nthase large e subunit M.musculus ESTs, Highly similar to molybdopterin-111 3925 AA851017 ,General s nthase lar a o subunit [M.musculus Rattus norvegicus 0 ~ mRNA for 112 49 851184 ,k cathepsin Y, partial 4 a cds TABLE MMARY ~~ ~' I ' ~tty': Docket : SU I a'i~' '' No. 44921-5U89W0 , D oe. No. 1798397.1 ~I I
Sequence GenBank~i4~~1~Model ~~, ID No. IdentifierRef. Seq CoeJeGene Name Unigene Cluster ID Tittle ESTs, Weakly similar to T28050 hypothetical protein ZK856.11 -113 19187 AA851230 General Caenorhabditis elegans C.elegans]

ESTs, Highly similar to ubiquitin specific protease 114 19189 AA851237 c M.musculus ESTs, Highly similar to hypothetical 115 15386 AA851241 m protein H.sa iens]

ESTs, Weakly similar to A61382 g,1, phosphorylation regulatory protein HP-116 21462 AA851261 General 10 H.sapiens 117 21471 AA851343 General ESTs HHs:NADH dehydrogenaseESTs, Moderately similar to (ubiquinone) NUIM_HUMAN NADH-UBIQUINONE
Fe-S protein (23kD) (NADH-coenzymeOXIDOREDUCTASE

118 16902 AA851379 p reductase PRECURSOR [H.sapiens]

ESTs, Moderately similar to kinesin-119 23376 AA851392 i,x like DNA binding rotein H.sapiens ESTs, Moderately similar to kinesin-119 23377 AA851392 x like DNA binding rotein H.sapiens]

120 13349 AA851417 General ESTs 121 21527 AA851733 r,u ESTs i,o,u, Rattus norvegicus osteoactivin mRNA, 122 4048 AA851814 General complete cds ESTs, Highly similar to SSRA HUMAN

TRANSLOCON-ASSOCIATED

PROTEIN, ALPHA
SUBUNIT

123 10561 AA851871 bb PRECURSOR [H.sapiens]

Rattus norvegicus CaM-kinase II

124 17411 AA858621 j, inhibitor al ha mRNA, complete cds ESTs, Weakly similar to MCM6 RAT

DNA REPLICATION
LICENSING

125 1801 AA858636 k,s,x,bb FACTOR MCM6 [R.norvegicus 126 18350 AA858674 p ESTs 127 19484 AA858693 a ESTs 128 6360 AA858696 d ESTs ESTs, Weakly similar to Reg receptor 129 17334 AA858704 p [R.norvegicus ESTs, Weakly similar to dJ413H6.1.1 130 6380 AA858758 q H.sapiens 131 13219 AA858759 a ESTs I,m,Gener 132 6384 AA858788 al ESTs ESTs, Highly similar to p40 seven-transmembrane-domain protein 134 13412 AA858830 [M.musculus]

135 7279 AA858892 f ESTs 136 18217 AA858930 t ESTs ASPARAGINYL-TRNA

HHs:asparaginyl-tRNASYNTHETASE, CYTOPLASMIC

137 5867 AA858953 v,Generals nthetase H.sapiens ESTs, Moderately similar to 156526 interleukin 1 receptor type I - rat 138 14479 AA858969 r [R.norvegicus]

139 6431 AA859085 t ESTs 140 17361 AA859114 o,General ESTs 141 21025 AA859241 Generalouter membraneouter membrane protein protein 142 10076 AA859271 c ESTs ESTs, Weakly similar to CYSR RAT

CYSTEINE-RICH PROTEIN

143 21791 AA859333 k R.norvegicus cc,Gener 144 16314 AA859348 al ESTs 145 18862 AA859520 f ES1's 146 15059 AA859545 r ESTs TABLE MMARY "iii-- Atty. Docket No.
1: 44921-5U89W0 SU

l7oe. No. 1798397.1 Sequence GenBar;k Model Ac'el ' ID No. dentifierRef. SequID~C,odeGene Narne Unige~,ne Cluster I Tittle Rattus norvegicus late gestation lung 147 19894 AA859581 s protein 1 (Lgl1 mRNA, com lets cds 148 14353 AA859585 h ESTs ESTs, Weakly similar to DnaJ

149 16318 AA859648 h homolog 2 R.norvegicus 150 17316 AA859652 General ESTs 151 19067 AA859663 n,q ESTs 152 22406 AA859680 n ESTs 153 20599 AA859690 x ESTs ESTs, Weakly similar to YNH2_CAEEL HYPOTHETICAL
31.0 KD PROTEIN 8107.2 IN

154 14261 AA859693 a CHROMOSOME III
[C.elegans]

ESTs, Highly similar to PPOX MOUSE

HHs:protoporphyrinogenPROTOPORPHYRINOGEN
OXIDASE

155 14138 AA859700 v oxidase [M.musculus ESTs, Highly similar to PPOX MOUSE

HHs:protoporphyrinogenPROTOPORPHYRINOGEN
OXIDASE

155 14139 AA859700 v oxidase M.musculus ESTs, Weakly similar to IF4E MOUSE

EUKARYOTIC TRANSLATION

INITIATION FACTOR

157 22374 AA859804 I [R.norvegicus]

ESTs, Moderately similar to LYOX

RAT PROTEIN-LYSINE

158 22385 AA859805 b,k PRECURSOR [R.norvegicus]

159 22773 AA859885 n ESTs 160 22816 AA859898 k,x,z ESTs 161 11891 AA859926 x ESTs ESTs, Highly similar to N-162 23070 AA859942 k m risto Itransferase 1 [M.musculus]

163 23121 AA859948 k ESTs cc,Gener 164 23166 AA859954 al ESTs ESTs, Weakly similar to Edp1 protein 165 18468 AA859966 as M.musculus]

MYO-INOSITOL-1(OR
4)-HHs:inositol(myo)-1(or4)-MONOPHOSPHATASE

166 23336 AA859981 q monophos hatase[R.norvegicus]

ESTs, Highly similar to EF1G_HUMAN ELONGATION

167 4222 AA860024 a,bb FACTOR 1-GAMMA
[H.sa iens]

u,x,Gener Rattus norvegicus mRNA for class I

168 3974 AA860030 al beta-tubulin, complete 1 cds Hyaluronan EST,Hyaluronan mediated motilitymediated motility 169 7090 AA860039 x ece for (RHAMMreceptor (RHAMM) r ESTs, Moderately similar to T08661 anti-silencing protein ASF1 homolog 170 23769 AA860055 k,x DKFZp547E2110.1 H.sapiens 171 6323 AA866240 w EST

ESTs, Weakly similar to PE2R RAT 20 ALPHA-HYDROXYSTEROID

172 462 AA866264 General DEHYDROGENASE [R.norvegicus ESTs, Weakly similar to A60543 173 5884 AA866276 k rotein kinase [R.norve 1 icus 4 -hydroxyphenylpyruvic4-hydroxyphenylpyruvic acid acid 174 7742 AA866302 c, iox genase diox genase 1 d Solute carrierSolute carrier family 4, family 4, member 1, member 1, anionanion exchange exchange protein 1 (kidney 175 6333 AA866414 a,h rotein 1 (kidneband 3) 1 band 3) ESTs, Moderately similar to AF141884 1 oligophrenin-1 like protein 176 8918 AA866444 ,q [H.sapiens 177 6853 AA866454 j,l,m, ESTs 1 ,z 178 8995 AA866459 h,m ESTs TABLE MMARY ~E1 y. ~oeket No.
1: 44921-5U89W0 SU

Doe. No. 1798397.1 ~

( i.;,i Sequence GenBank Model ' Aecl ID N dentifierRef. Seq Code Gene Name ~Unigene Cluster o. I ID Title ESTs, Highly similar to FGD1 MOUSE

PUTATIVE RHO/RAC
GUANINE

NUCLEOTIDE EXCHANGE
FACTOR

179 16013 AA866482 s [M.musculus]

180 26036 AA874849 r 181 16059 AA874857 h ESTs 182 16069 AA874873 r ESTs ESTs, Weakly similar to RNA binding 183 21633 AA874951 f protein H.sa iens]

184 16192 AA874995 w ESTs ESTs, Highly similar to RET3 BOVIN

RETINOIC ACID-BINDING
PROTEIN

185 16254 AA875025 I, CELLULAR R.norvegicus]

cc,Gener 186 16312 AA875032 al ESTs 187 20701 AA875097 b Rat alpha-fibrinogen mRNA, 3' end ESTs, Highly similar to ARF3_HUMAN

ADP-RIBOSYLATION
FACTOR

188 16416 AA875098 bb [R.norvegicus]

ESTs, Highly similar to RUXE_HUMAN SMALL
NUCLEAR

RIBONUCLEOPROTEIN
E

189 16419 AA875102 bb M.musculus I,m, 190 15313 AA875126 General ESTs ESTs, Weakly similar to AF151834 1 191 10936 AA875146 w CGI-76 rotein H.sa lens]

192 18084 AA875186 h ESTs ESTs, Highly similar to IF39_HUMAN

EUKARYOTIC TRANSLATION

INITIATION FACTOR

193 15371 AA875205 a (H.sa lens]

194 15401 AA875257 x,z ESTs HHs:NADH dehydrogenase ( ubiquinone) Fe-S protein ( 20kD) (NADH-coenzymeESTs, Highly similar O to NUKM

195 15410 AA875268 ,s eductase HUMAN, partial r CDS [H.sapiens]

196 15420 AA875286 f ESTs 197 15446 AA875327 s,w ESTs 198 7936 AA875495 b,General ESTs ESTs, Highly similar to includes exons 199 17314 AA875509 i,l,m 3 through 12 [M.musculus ESTs, Highly similar to MLES RAT

MYOSIN LIGHT CHAIN
ALKALI, SMOOTH-MUSCLE ISOFORM

200 24472 AA875523 k [R.norve icus]

201 15587 AA875577 ESTs 202 5617 AA875620 General E$Ts 202 15618 AA875620 General ESTs f,cc,Gene 203 5384 AA891041 ral un B roto-onco'un B roto-oncogene j ene ESTs, Moderately similar to 833729 204 24814 AA891209 f, 1, partial CDS
H.sa lens ESTs, Weakly similar to AF151373 1 nucleolin-related protein NRP

205 21930 AA891322 d [R.norvegicus ESTs, Highly similar to eIF3 p66 206 17225 AA891553 h M.musculus ESTs, Weakly similar to S67314 regulatory protein RMS1 - yeast (Saccharomyces cerevisiae) 207 7522 AA891571 j,m S.cerevisiae 208 9071 AA891578 b ESTs melanoma antigen, ( ~ ~ family D, ~ ( 209 9321 AA891666 melanoma antigen, family D, 1 TABLE MMARY Atty. Docket No.
1: 44921-5U89W0 SU

Doe. No. 1798397.1 E ~
" y Sequence GenB-ank Model "
Ace/ ' ~

IU No. dentifierRef. Seq Code Gene Name U~,nigestne Cluster I I~ Title 210 7693 AA891737 j,l,m,n, ESTs 1 ,z ESTs, Weakly similar to T22521 hypothetical protein F52H3.5 -211 7256 AA891739 General Caenorhabditis 1 elegans [C.elegans ESTs, Moderately similar to FINC
RAT

FIBRONECTIN PRECURSOR

213 8269 AA891769 General [R.norvegicus s,bb, D239Gen 214 9905 AA891774 eral ESTs ESTs, Highly similar to alpha-adducin, hypertensive phenotype 215 7061 AA891812 d [R.norvegicus]

Rattus norvegicus clone ZG52 mRNA

216 7050 AA891824 h se uence ESTs, Weakly similar to PE2R RAT 20 ALPHA-HYDROXYSTEROID

217 4463 AA891831 General DEHYDROGENASE [R.norvegicus ESTs, Highly similar to muscle protein 218 14289 AA891838 i 684 [M.musculus]

2 20523 AA891842 r,cc ESTs _ ESTs, Moderately similar to ACY1_HUMAN AMINOACYLASE-1 220 17779 AA891914 g,s,z H.sapiens) 221 17438 AA891943 General ESTs 222 22862 AA891944 p ESTs 223 1159 AA8g1949 e,z ESTs ESTs, Weakly similar to T31496 hypothetical protein Y116A8C.25 -224 4473 AA891965 General Caenorhabditis ele ans [C.elegans]

ESTs, Highly similar to chromatin structural protein homolog Supt5hp 225 6362 AA892053 f,j,l,m [M.musculus 226 9037 AA892066 ESTs ESTs, Weakly similar to proline 227 19469 AA892112 General dehydrogenase [M.musculus]

228 14595 AA892128 o,t,v ESTs 229 16527 AA892154 cc ESTs 230 4482 AA892173 bb EST

231 20917 AA892238 h ESTs ESTs, Weakly similar to PC4221 232 2357 AA892268 d rotein-tyrosine kinase R.norvegicus 233 18183 AA892271 h ESTs 234 6523 AA892299 d ESTs ESTs, Highly similar to RL3 RAT 60S

RIBOSOMAL PROTEIN

236 13647 AA892367 a [R.norvegicus]

ESTs, Highly similar to AF151893 1 237 3473 AA892378 v CGI-135 protein H.sapiens ESTs, Moderately similar to AF185570 j,p,s,x, 1 putative N-acetyltransferase 238 17682 AA892382 General Camello 4 R.norvegicus Aldolase B, fructose-239 820 AA892395 ,s bi hosphate Aldolase B, fructose-bi hos hate 240 14754 AA892414 a ESTs 241 17439 AA892446 f ESTs ESTs, Moderately similar to UCRY_HUMAN UBIQUINOL-CYTOCHROME C REDUCTASE

COMPLEX 6.4 KD
PROTEIN

242 16469 AA892462 p H.sapiens]

Rattus norvegicus mRNA for prostasin 243 13609 AA892468 i,General precursor, complete cds n,v,Gener Rattus norvegicus mRNA for prostasi~

243 13610 AA892468 al precursor, complete cds TABLE MMARY Atty. Doek'et No.
1: SU 44921-5U89 O

Uoc. No. 798397.

Sequence GenBank Model Accl IU No. dentifierRef. Seq Code Gene Name Unigene Cluster I . ID Title ESTs, Highly similar to HISTONE

244 9254 AA892470 n,u H2A.Z R.norvegicus 245 11991 AA892483 s ESTs ESTs, Moderately similar to LYAG

MOUSE LYSOSOMAL
ALPHA-GLUCOSIDASE PRECURSOR

246 1522 AA892486 f M.musculus ESTs, Moderately similar to S63540 247 11994 AA892507 as protein DS 1, 24K
H.sapiens]

248 23888 AA892520 w ESTs 248 23889 AA892520 h ESTs 249 8599 AA892522 p ESTs 250 15154 AA892532 p R.norvegicus (Wistar) CaBP1 mRNA

ESTs, Highly similar to multi-membrane spanning polyspecific 251 17468 AA892545 r t ransporter [M.musculus]

ESTs, Highly similar to ras-GTPase-activating protein SH3-domain binding 252 11203 AA892554 f,h rotein [M.musculus]

a,bb, ESTs, Moderately similar to PTD012 253 18906 AA892561 General H.sapiens R.norvegicus mRNA
for nucleolar 254 19327 AA892562 f,j, rotein NAP57 ,z 255 18274 AA892572 p ESTs 256 4512 AA892578 cc ESTs ESTs, Highly similar to RL8_HUMAN

L

257 15876 AA892582 w [ R.norvegicus 258 19085 AA892598 General ESTs 258 19086 AA892598 General ESTs ESTs, Highly similar to H4_HUMAN

259 20065 AA892647 I HISTONE H4 [R.norvegicus]

260 20088 AA892666 a,n ESTs 261 23783 AA892773 n ESTs Rat mitochondria) proton/phosphate 262 1 7549 AA892776 f,z s mporter mRNA, com lete cds 263 1 3542 AA892798 b ESTs HHs:glyoxylateESTs, Weakly similar to SERA RAT D

r eductase/hydroxypyruvate3-PHOSPHOGLYCERATE

264 22537 AA892799 Generaleductase DEHYDROGENASE R.norvegicus]
r HHs:glyoxylateESTs, Weakly similar to SERA RAT D

r eductase/hydroxypyruvate3-PHOSPHOGLYCERATE

264 22539 AA892799 v eductase DEHYDROGENASE [R.norvegicus]
r HHs:glyoxylateESTs, Weakly similar to SERA RAT D

r eductase/hydroxypyruvate3-PHOSPHOGLYCERATE

264 22538 AA892799 Generaleductase DEHYDROGENASE [R.norvegicus r ESTs, Weakly similar to S70642 ubiquitin ligase Nedd4 - rat 265 6951 AA892820 h R.norvegicus]

Rattus norvegicus aiar mRNA for a ndrogen-inducible aldehyde 266 23322 AA892821 ',z r eductase, complete cds ESTs, Weakly similar to T29904 hypothetical protein F59A3.3 -267 1 7923 AA892843 f Caenorhabditis elegans [C.elegans ESTs, Weakly similar to procollagen-268 2 2871 AA892859 m I sine 5-diox genase R.norvegicus p,v.

269 9 053 AA892861 General ESTs ESTs, Weakly similar to EF2 RAT

ELONGATION FACTOR

270 1 6482 AA892940 w R.norvegicus]

Rattus norvegicus HP33 mRNA, 271 1 2020 AA893035 c omplete cds 272 3 863 AA893060 General ESTs 273 1 3332 AA893080 i,GeneralS STs -so-TABLE MMARY Atty. Docket No.
1: 44921-5U89W0 SU

Doc. No. 1798397.1 Sequence GenBank Model Accl ID N~o.IdentifierRef. Seq Code Gene Name Unige~,,n_e Cluster ID Tittle 274 21305 AA893082 General ESTs 275 16591 AA893191 ,z ESTs j 276 17447 AA893192 General ESTs 277 3876 AA893205 n ESTs ESTs, Weakly similar to CALM_HUMAN CALMODULIN

278 3878 AA893230 General [R.norvegicus Acyl CoA synthetase, long 279 20986 AA893242 chain Ac I CoA s nthetase, long chain i ,z, ESTs, Moderately similar to 280 16168 AA893280 General adi ophilin H.sapiens 281 3886 AA893289 ,m,y ESTs j 282 15209 AA893327 ESTs 283 17800 AA893436 cc ESTs ESTs, Weakly similar to LIS1 MOUSE

PLATELET-ACTIVATING
FACTOR

ACETYLHYDROLASE
IB ALPHA

284 17836 AA893626 h SUBUNIT R.norve icusj 285 9084 AA893717 x ESTs 286 22731 AA893743 d ESTs ESTs, Moderately similar to SYTC_HUMAN THREONYL-TRNA

HHsahreonyl-tRNASYNTHETASE, CYTOPLASMIC

287 12031 AA893860 v s nthetase [H.sapiensj 288 17897 AA893905 k ESTs 289 3447 AA893982 d ESTs 290 22583 AA894009 n ESTs, Highly similar to A55748 292 4569 AA894059 protein kinase x M.musculus]

ESTs, Weakly similar to APP2 RAT

AMYLOID-LIKE PROTEIN

293 18419 AA894130 d PRECURSOR [R.norvegicus 294 17336 AA894297 ESTs j 295 19120 AA894318 ,j ESTs f 296 19762 AA899113 ESTs i 297 18286 AA899219 a Rat mRNA for beta-tubulin T betal5 ESTs, Weakly similar to T26581 hypothetical protein Y32B12A.3 -298 22051 AA899498 w Caenorhabditis elegans C.elegans ESTs, Weakly similar to T26581 hypothetical protein Y32B12A.3 -298 22052 AA899498 q Caenorhabditis ele ans C.ele ans]

299 21628 AA899563 as ESTs 300 4262 AA899590 ESTs i receptor activity modifying 301 4661 AA899709 ,Generalrotein 3 receptor activit t modi in protein 302 21354 AA899721 ESTs q Rattus norvegicus epidermal growth factor receptor related protein (Errp) 303 17905 AA899762 General mRNA, com lete cds 304 15231 AA899840 ESTs r topoisomerase (DNA) II

305 23778 AA899854 ,k,x alpha topoisomerase (DNA) c II alpha 306 22060 AA899898 b ESTs 307 9114 AA899951 ,General ESTs v 308 8988 AA900148 ESTs f Rattus norvegicus mRNA for 309 11841 AA900247 Hsp70/Hsp90 or v anizing rotein ESTs, Highly similar to ALPHA-2-MACROGLOBULIN PRECURSOR

310 4725 AA900290 c [R.norve icus]
c 311 4747 AA900465 General ESTs 312 20988 AA900562 ESTs b,g, ESTs, Weakly similar I to nuclear RNA

313 3822 AA900863 General helicase [R.norvegicusj TABLE MMARY Atty. Docket No.
1: 44921-5U89W0 SU

Doe. No. 1798397 Sequence GenBank-AcclModel I~ No. dentifierRef: S~eg,;IDCode Gene Name Unigene" Cluster I Title ESTs, Weakly similar to T20702 hypothetical protein F10C2.6 -315 12420 AA901017 b Caenorhabditis elegans C.elegans]

316 4849 AA901155 s Rattus norvegicus CDK105 mRNA

ESTs, Highly similar to IF2B_HUMAN

EUKARYOTIC TRANSLATION

INITIATION FACTOR

317 3959 AA901338 General SUBUNIT [H.sapiens]

ESTs, Highly similar to ATP-specific succinyl-CoA synthetase beta subunit 318 22846 AA923982 a,d M.musculus 319 4895 AA923999 k ESTs cc, 320 21546 AA924188 General ESTs 321 24192 AA924210 n,General ESTs g,I,Gener 322 4933 AA924301 al EST

ESTs, Moderately similar to N056_HUMAN NUCLEOLAR

323 4944 AA924405 ,General PROTEIN NOP56 [H.sapiens ( 324 4948 AA924428 ESTs r ESTs, Weakly similar to NPT2 RAT

RENAL SODIUM-DEPENDENT

PHOSPHATE TRANSPORT

325 4949 AA924432 General PROTEIN 2 [R.norvegicus 326 18891 AA924598 a ESTs HHs:glyoxylateESTs, Weakly similar to SERA RAT D

r eductasefhydroxypyruvate3-PHOSPHOGLYCERATE

327 22540 AA924630 v,Generaleductase DEHYDROGENASE [R.norvegicus]
r HHs:glyoxylateESTs, Weakly similar fo SERA RAT D

r eductase/hydroxypyruvate3-PHOSPHOGLYCERATE

327 22541 AA924630 Generaleductase DEHYDROGENASE [R.norvegicus r 328 14759 AA924766 k ESTs 329 23123 AA924794 ESTs x 330 4067 AA924813 ,p ESTs 331 2888 AA924902 ,General ESTs r ESTs, Highly similar to sec? domain 332 18130 AA924964 f amily member [H.sapiens]
d 333 23141 AA925019 ESTs r ESTs, Weakly similar to MCT7 RAT

MAST CELL PROTEASE

334 23195 AA925026 General PRECURSOR R.norvegicus f ,aa, 335 21458 AA925049 General ESTs ESTs, Moderately similar to S20710 hypothetical protein, 16K - mouse 336 5073 AA925061 m M.musculus]

337 14790 AA925087 ,General ESTs o EST, Highly similar to T50621 hypothetical protein DKFZp7620076.1 338 5089 AA925126 [ H.sa iens]
g ESTs, Moderately similar to BHMT

RAT BETAINE--HOMOCYSTEINE
S-METHYLTRANSFERASE

339 23261 AA925145 ,General[ R.norve icus]
k ESTs, Moderately similar to neurodegeneration-associated protein 340 7363 AA925150 1 R.norve icus 1 a 341 3448 AA925167 ESTs 342 3159 AA925318 I -ka pa-B-beta -kap a-B-beta 2 a I

343 1500 AA925353 ESTs 2 k 344 2479 AA925418 ESTs 2 t 345 1151 AA925539 ESTs 2 b -s2-TABLE MMAR Att~y. Docket No.
1: 44931-5U89W0 SU

Doe. No. 1798897.1 'Sequence_ GenBank _ Aeel Model IU No. dentifierRef. Seq Code Gene Name Unigene Cluster I ID Title h eterogeneous heterogeneous nuclear nuclear 346 6944 AA925541 r ibonucleoproteinribonucleo rotein 1 f L L

h eterogeneous heterogeneous nuclear nuclear 346 6945 AA925541 r ibonucleoproteinribonucleo rotein 1 t L L

HHsauccinate ESTs, Highly similar to d ehydrogenase DHSA_HUMAN SUCCINATE
complex, 347 7514 AA925554 bb ubunit A, flavoproteinDEHYDROGENASE H.sapiens 1 s Fp) 348 5183 AA925662 ,General ESTs i 349 23189 AA925844 ESTs r ESTs, Highly similar to IMB3_HUMAN

SUBUNIT

350 23190 AA925863 as [H.sapiens]

351 5252 AA926051 General EST

352 22967 AA926080 h,cc ESTs 353 17157 AA926129 b ESTs 354 13411 AA926196 u,General ESTs putative potassium channel 355 5295 AA926247 GeneralTWIK utative potassium channel TWIK

ESTs, Moderately similar to NEURONAL PROTEIN
3.1 356 22928 AA926262 General [M.musculus]

ESTs, Moderately similar to T13963 formin related protein, lymphocyte 357 8948 AA926316 s ecific - mouse r M.musculus]

ESTs, Moderately similar to AF151827 358 21798 AA926365 as 1 CGI-69 rotein [H.sa iens]

359 9942 AA942697 s ESTs ESTs, Highly similar to HN1 360 6039 AA942716 x,General [M.musculus]

361 11174 AA942745 g,o,w ESTs 362 23005 AA942770 g ESTs 363 21318 AA942774 General ESTs ESTs, Weakly similar to T26686 hypothetical protein Y38F1A.6 -364 6615 AA942889 v Caenorhabditis elegans [C.elegans ESTs, Highly similar to KFMS RAT

MACROPHAGE COLONY

STIMULATING FACTOR
I

RECEPTOR PRECURSOR

365 6691 AA943028 c R.norvegicus]

ESTs, Weakly similar to p68 RNA

366 22142 AA943066 helicase [R.norvegicus ESTs, Weakly similar to T00084 hypothetical protein 367 21993 AA943149 v,General H.sapiens ESTs, Weakly similar to T08666 hypothetical protein 368 9061 AA943508 General DKFZ 547N0510.1 [H.sapiens ESTs, Weakly similar to VIL1 MOUSE

369 24390 AA943531 b,',n, VILLIN M.musculus]

Rattus norvegicus mRNA for class I

370 13976 AA943532 ,s,x beta-tubulin, complete f cds cc, Rattus norvegicus zyxin mRNA, partial 371 22248 AA943537 General cds ESTs, Highly similar to T2DA_HUMAN

TRANSCRIPTION INITIATION

KDA

372 22257 AA943558 m SUBUNITS H.sapiens]

u,cc, 373 12673 AA943773 General ESTs 374 13641 AA944154 a ESTs 375 2658 AA944155 ESTs f 376 12770 AA944161 d ESTs TABLE MMA ~ Atty. Docket No.
1: Y 44931-5U89W0 SU enBank odel '' ,' Doe. No. 1798897.
Aeel Code Gene Name ~
SequenceentifierRef. Seq ~ ~ ~U"~nigene Cluster IU No. ID Title I ESTs, Highly similar x to CKS2 MOUSE

77 i REGULATORY SUBUNIT

M.musculus 378 13507 AA944244 v ESTs 379 15596 AA944353 General ESTs i ,v,cc, 380 22681 AA944413 General ESTs ESTs, Highly similar 381 6711 AA944439 General to hypothetical protein M.musculus ESTs, Weakly similar i ,q, to FIBA RAT
82 1 763 AA944481 General FIBRINOGEN ALPHA/ALPHA-E
CHAIN PRECURSOR
R.norvegicus 383 22466 AA944605 h ESTs ESTs, Weakly similar b to A44437 84 1 301 A944727 regenerating liver inhibitory factor RUIF-1 - rat [R.norvegicus HHs:polymeraseESTs, Highly similar ( (RNA) II to RNA
85 023 A944792 d,m,aaDNA directed) polymerase II 23kD
( polypeptide subunit E [H.sapiens 25kD) 386 22536 AA944803 bb ESTs 387 22501 AA944811 g,) ESTs 388 23967 AA944831 s ESTs i 390 11974 AA944958 General ESTs 391 22547 AA944970 as ESTs 392 22554 AA945076 z,General ESTs 393 14352 AA945181 General ESTs R.norvegicus alpha-1-macroglobulin 395 1798 AA945569 General mRNA, complete cds 396 22050 AA945604 ,aa ESTs i 397 19731 AA945615 d,o ESTs ESTs, Weakly similar to DHOU RAT
98 2612 A945624 ,General NAD(P)H DEHYDROGENASE
R.norvegicus]

399 22618 AA945656 as ESTs 400 11871 AA945679 v ESTs 401 22656 AA945818 General ESTs 402 6720 AA945828 p ESTs 403 22351 AA945867 m ESTs 404 22665 AA945877 ESTs f 405 24243 AA945950 b ESTs 406 22689 AA945962 General ESTs 407 22692 AA945986 d ESTs 408 22696 AA945996 c,General ESTs 408 22697 AA945996 c,o ESTs 409 22658 AA945998 w ESTs ESTs, Highly similar s HMm:RIKEN cDNAto COXG

gene C OXIDASE
POLYPEPTIDE VIB
M.musculus 411 18337 AA946046 General ESTs Rattus norvegicus 412 825 AA946108 General laminin-5 alpha chain mRNA, com lets cds e,cc, 413 8639 AA946221 General ESTs 414 23237 AA946224 ESTs f 415 15600 AA946250 o,aa ESTs ESTs, Highly similar to AR21_HUMAN

t 21 KD SUBUNIT
[H.sapiens]

PCTAIRE-1 proteinPCTAIRE-1 protein 417 6351 AA946344 d kinase, kinase, alternative) alternative) spliced spliced ESTs, Highly similar 418 22057 AA946348 a to autoantigen [H.sapiens 419 22069 AA946349 as ESTs TABLE IJMMARY~5_,'~ f ,i ~' At~ty. Docket No.
1: ~ r 44921-5U89W0 S; ~'i4f'"

I _ _ , Doe. No. 1798397.1 ,i~~
Sequence GenBank Model C
A~cch~
' ~ID IdentifierRef. Seq Geode Gene Narne U~ynig~ne No. IDS ~ luster Title 420 13962 AA946351 General ESTs ESTs. Highly similar to Ring3 421 18280 AA946361 g [M.musculus 422 18944 AA946391 ESTs v ESTs, Moderately similar to p18 component of aminoacyl-tRNA

424 21410 AA946408 synthetase complex t [H.sapiens]

425 643 AA946439 0, Rat H4 gene for somatic histone ESTs, Highly similar to NPD1 MOUSE

NEURAL PROLIFERATION

DIFFERENTIATION
AND CONTROL

426 20736 AA946443 [M.musculus]
x 427 21878 AA946448 ESTs r ESTs, Highly similar to AF151863 1 428 21947 AA946451 bb CGI-105 protein [H.sa iens]

429 17499 AA946467 General ESTs Rat mRNA for alpha-2u globulin-430 1809 AA946503 ,General related protein x 431 23360 AA955104 ESTs f 432 23471 AA955162 General ESTs 433 9452 AA955206 b.General ESTs 434 23512 AA955282 General ESTs 435 22596 AA955298 General ESTs 436 23283 AA955391 h ipo rotein-bindinglipoprotein-binding l protein protein 437 23546 AA955393 General ESTs ESTs, Weakly similar to SX10 RAT

TRANSCRIPTION FACTOR

438 12404 AA955408 b [R.norvegicus 439 23626 AA955540 as ESTs EST,EST, Moderately similar to FBRL

MOUSE FIBRILLARIN

[M.musculus],ESTs, Highly similar to FBRL MOUSE FIBRILLARIN

441 17540 AA955914 bb [M.musculus]

442 24277 AA955962 General ESTs ESTs, Moderately similar to pescadillo 443 19939 AA955980 General [H.sa iens) ESTs, Weakly similar to AF139894 1 RNA-binding protein alpha-CP1 444 24000 AA956005 M.musculus i ESTs, Weakly similar to TCPA RAT T-COMPLEX PROTEIN
1, ALPHA

445 11050 AA956164 s,v SUBUNIT R.norvegicus]

446 498 AA956278 a,General ESTs 447 23409 AA956294 ESTs 449 23773 AA956476 ,x ESTs f ESTs, Highly similar to ET putative 450 23799 AA956530 d translation product [M.musculus ESTs, Weakly similar to PROTEIN

451 23800 AA956534 as H.sapiens cc, 452 23834 AA956659 General EST

ESTs, Moderately similar to C8 453 16425 AA956688 ,x M.musculus f s ESTs, Highly similar to Mi-2 protein 455 23852 AA956746 ,l,m,z [H.sapiens j ESTs, Highly similar to p162 protein 456 5989 AA956907 g,s [M.musculus]

ESTs, Highly similar to p162 protein 456 5990 AA956907 General [M.musculus]

TABLE UMMARY A~tty. Docket No.
1: 44921-5U89W0 S

Uoc. N_v;1t7~9839r7~1!

Sequence~ GenB~ank Model ~scl tD No. IdentifierRef. Seq Code Gene Name Unigene Cluster ID Title ESTs, Weakly similar to AF187065 1 p75NTR-associated cell death 457 23957 AA957123 u,General executor (R.norvegicus]

ESTs, Highly similar to hypothetical 458 22357 AA957264 General protein [H.sapiens]

9,I,m,P.v, cc, 459 23314 AA957270 General ESTs 460 23995 AA957292 a,b ESTs ESTs, Moderately similar to SYS_HUMAN SERYL-TRNA

461 2702 AA957307 GeneralHHsaeryl-tRNA SYNTHETASE H.sa synthetase lens]

ESTs, Highly similar to HIGH

AFFINITY IMMUNOGLOBULIN

EPSILON RECEPTOR
GAMMA-SUBUNIT PRECURSOR

462 24040 AA957422 c [R.norvegicus]

ESTs, Highly similar to P3 MOUSE P3 463 12478 AA957554 m PROTEIN [M.musculus]

464 21306 AA957811 v ESTs 465 24183 AA957889 t ESTs 466 24178 AA957905 d ESTs ESTs, Highly similar to epsilon-COP

467 17034 AA963071 a M.musculus]

ESTs, Weakly similar to AF187065 1 p75NTR-associated cell death 468 24053 AA963092 General executor [R.norvegicus]

469 2767 AA963201 o ESTs 470 2022 AA963259 g ESTs 471 2126 AA963488 d ESTs ESTs, Highly similar to cell cycle 472 24246 AA963703 b rotein p38-2G4 homolog [H.sa iens 473 2195 AA963746 General ESTs 474 19370 AA963797 i ESTs 475 2282 AA964147 a ESTs 476 2284 AA964152 x EST

ESTs, Highly similar to TGT HUMAN

QUEUINE TRNA-478 2350 AA964368 g,General RIBOSYLTRANSFERASE
[H.sapiens]

ESTs, Highly similar to ATRTC actin 479 18830 AA964496 as beta - rat R.norvegicus 480 2392 AA964541 b EST

ESTs. Highly similar to U3 snoRNP

481 2395 AA964554 General associated 55 kDa rotein H.sa lens]

482 2410 AA964589 i,aa EST

483 19145 AA964613 t ESTs 484 2424 AA964617 g ESTs 485 3107 AA964687 General ESTs 486 2457 AA964752 ,t EST

ESTs, Highly similar to DRIM protein 487 6778 AA964763 b [H.sapiens ESTs, Weakly similar to T23337 hypothetical protein K05C4.2 -489 2468 AA964807 I Caenorhabditis ele ans C.elegans Glutamate-cysteineGlutamate-cysteine ligase ligase (gamma-( gamma-glutamylcysteineglutamylcysteine synthetase), 490 2469 AA964814 w nthetase), regulato s regulato 491 12561 AA964815 General ESTs ESTs, Highly similar to PROCOLLAGEN ALPHA
1(1V) CHAIN

492 2326 AA964892 as PRECURSOR [M.musculus ESTs, Highly similar to ABC1 MOUSE

ATP-BINDING CASSETTE, SUB-493 21339 AA964962 General FAMILY A, MEMBER
1 M.musculus 494 21390 AA964988 General ESTs 495 12569 AA965023 g ESTs TABLE UMMAR ''~ ty. Docket 1: No. 44921-5U89W0 S

Doe. No. 1798397.1 Er' ~Sequeriee GenBank Model Acel ID No..'1'IdentifierRef. Seq Code Gene Name UnigeY n_e Cluster ID '~ Titte ESTs, Moderately similar to inorganic 496 2583 AA965166 bb p ro hos hatase [H.sapiens]

ESTs, Highly similar to KIAA0958 497 15885 AA965207 r protein H.sapiens]

b,l.m,u, 499 2905 AA996727 General ESTs ESTs, Moderately similar to S27267 500 2915 AA996782 u,bb lamin A - rat R.norvegicus]

501 2920 AA996813 d ESTs aa,Gener 502 19525 AA996856 al EST

503 2984 AA997015 c ESTs 504 2986 AA997028 General ESTs 505 3145 AA997237 General ESTs 506 19249 AA997342 m ESTs ESTs, Weakly similar to nitrilase 507 16883 AA997345 General homolog 1 M.musculus ESTs, Moderately similar to LONN_HUMAN MITOCHONDRIAL

LON PROTEASE HOMOLOG

508 12598 AA997362 s PRECURSOR H.sapiens ESTs, Weakly similar to LIS1 MOUSE

PLATELET-ACTIVATING
FACTOR

ACETYLHYDROLASE
IB ALPHA

509 3470 AA997374 SUBUNIT [R.norvegicus]

510 3180 AA997425 ESTs t ESTs, Weakly similar to PA12 RAT

PLASMINOGEN ACTIVATOR

511 3245 AA997608 General INHIBITOR-2, TYPE
A R.norvegicus ESTs, Moderately similar to T09071 SH3 domains-containing protein 512 3020 AA997656 POSH - mouse [M.musculus]
t ESTs, Moderately similar to T30249 cell proliferation antigen Ki-67 - mouse 513 3269 AA997800 x,aa (M.musculus]

514 3288 AA997877 ESTs f 515 23992 AA998164 k,x Cyclin B1 C clin B1 ESTs, Moderately similar to FLRE_HUMAN FLAVIN
REDUCTASE

516 17470 AA998264 b [H.sapiens ESTs, Weakly similar to BCL3_HUMAN B-CELL
LYMPHOMA

517 3773 AA998356 General 3-ENCODED PROTEIN
[H.sa iens]

518 19623 AA998422 General EST

ESTs, Highly similar to CGA2 MOUSE

519 3572 AA998516 x CYCLIN A2 [M.musculus]

ESTs, Moderately similar to CYCLIN-DEPENDENT KINASE

520 2782 AA998565 c M.musculus i ,r,w.

521 26119 AA998576 General 522 22737 AA998660 as ESTs ESTs, Moderately similar to AF132966 523 3696 AA999030 a 1 CGI-32 protein H.sapiens k,x, 524 3079 AA999169 General ESTs Signal transducerSignal transducer and and activator of 525 3081 AA999171 e, ctivator of transcri tion 1 ,r transcription a 1 ESTs, Highly similar to HHs:guanine GUAA HUMAN GMP
monphosphate SYNTHASE

526 3082 AA999172 Generalnthetase [H.sapiens]
s 527 17337 AB000717 k ESTs 528 1535 AB000778 a Phoshpolipase Phoshpoli ase D
D gene 1 gene 1 529 1382 AB002406 k RuvB-like roteinRuvB-like protein d TABLE MMARY ~tty. Docket No.
1: 44921-5U89W0 SU

Doe. 0. 1798897.1 Sequence GenBank Model Accl ' ~ID dentifierRef. Seq Code Gene Name Unigene Cluster No. ID Tittle I

Rattus norvegicus mRNA for carboxylesterase precursor, complete 531 4312 AB010635 c,i,j,k, cds ,z HMm:DNA methyltransferaseESTs, Highly similar to JE0378 DNA

532 21666 AB012214 k (cytosine-5) R.norvegicus]
1 [

Rattus norvegicus mRNA for G protein 533 5772 AB015645 g coupled receptor, 1 complete cds Rattus norvegicus MAP-kinase phosphatase (cpg21 ) mRNA, 534 1183 AF013144 h complete cds Rattus norvegicus NAC-1 protein 535 1582 AF015911 h,z ( NAC-1) mRNA, complete cds ESTs, Moderately similar to MY16 MOUSE MYELOID

DIFFERENTIATION
PRIMARY

RESPONSE PROTEIN

[ M.musculus],Rattus norvegicus u,cc, progression elevated gene 3 protein 536 11483 AF020618 General mRNA, com lete cds Rattus norvegicus MHC class Ib M4 ( RT1.M4) pseudogene, complete 537 20295 AF024712 as sequence Rattus norvegicus chemokine CX3C

538 19077 AF030358 ,z mRNA, complete cds 539 23044 AF034218 Generalh aluronidase h aluronidase 2 540 25178 AF035955 d Rattus norvegicus kidney injury x,bb, molecule-1 (KIM-1) mRNA, complete 541 1564 AF035963 General cds Rattus norvegicus NonO/p54nrb 542 8426 AF036335 homolog mRNA, partial f cds Rattus norvegicus homocysteine r espondent protein HCYP2 mRNA, 543 21817 AF036537 k complete cds Solute carrierSolute carrier family 1 A1 family 1 A1 (brain 544 21145 AF038571 General(brain glutamateglutamate trans transporter) orter) putative peroxisomalputative peroxisomal 2,4- 2,4-dienoyl-CoA

545 22602 AF044574 Generaldienoyl-CoA eductase reductase r UDP-glucose:ceramideUDP-glucose:ceramide 546 13464 AF047707 h g1 cos Itransferaseg1 cos Itransferase 547 24024 AF052695 x cell cycle cell c cle rotein rotein p55CDC p55CDC

Rattus norvegicus trpl beta variant 548 12259 AF061266 h transient receptormRNA, complete rotein 1 cds Rattus norvegicus kidney-specific 549 4589 AF062389 ,z protein KS) mRNA, complete cds Rattus norvegicus nucleosome nucleosome assembly protein assembly mRNA, complete 550 16007 AF062594 protein 1-likecds t 1 Rattus norvegicus pyruvate dehydrogenase phosphatase 551 15761 AF062741 a i soenz me 2 mRNA, com late cds Rattus norvegicus bithoraxoid-like 552 17426 AF073839 p protein mRNA, complete cds 553 18615 AF074608 s RT1 class Ib RT1 class Ib gene gene Rattus norvegicus serine/threonine protein kinase TA01 mRNA, complete 554 15797 AF084205 cds f Rattus norvegicus 190 kDa ankyrin 555 12932 AF102552 s ank rin 3 (G) soform mRNA, complete i cds ESTs, Highly similar to A49013 tumor cell suppression protein HTS1 556 18603 A1007649 x [ H.sa lens 557 22733 A1007668 ESTs r 558 22746 A1007672 ESTs r 559 24109 A1007725 General ESTs TABLE UMMARY Atty. Docket No.
1: 44931-5U89W0 S

Uoe. No. 1798597.1 Sequence GenBank Model I~eel IU No: IdentifierRet. Seq Code Gene Narne Unigene Cluster ID Title ESTs,ESTs, Highly similar to HS9B

RAT HEAT SHOCK
PROTEIN HSP

560 15848 A1007820 n,v 90-BETA [R.norvegicus 561 10108 A1007857 f Hrs Hrs 562 6804 A1007877 General ESTs 563 20099 A1007893 f,u ESTs ESTs, Weakly similar to T18778 hypothetical protein B0513.2b -564 11368 A1007948 d Caenorhabditis elegans [C.elegans]

ESTs,ESTs, Highly similar to HS98 RAT HEAT SHOCK
PROTEIN HSP

565 15849 A1008074 h 90-BETA [R.norvegicus]

ESTs, Moderately similar to AF151841 566 3121 A1008160 General 1 CGI-83 protein [H.sapiens]

ESTs, Highly similar to Chain G, G

Protein Heterotrimer Gi alpha 1 Beta Gamma 2 With Gdp Bound 567 16646 A1008190 t [R.norvegicus]

ESTs, Weakly similar to G2/MITOTIC-568 12683 A1008203 x SPECIFIC CYCLIN
B1 R.norvegicus ESTs, Moderately similar to PIM1 RA

PROTO-ONCOGENE

SERINE/THREONINE-PROTEIN

569 22018 A1008309 b KINASE PIM-1 [R.norvegicus]

ESTs, Highly similar to PHOSPHOGLUCONATE

DEHYDROGENASE, 570 23917 A1008441 n DECARBOXYLATIN
[H.sa lens]

571 22599 A1008458 General ESTs 572 22698 A1008578 p,General ESTs 573 14405 A1008579 r,x ESTs ESTs, Moderately similar to JH0446 574 4086 A1008629 x 75K autoantigen H.sapiens i,v, ESTs, Weakly similar to heat shock 575 3808 A1008643 General protein hsp40-3 M.musculus ESTs. Weakly similar to T29897 hypothetical protein F38A5.1 -576 3931 A1008697 I Caenorhabditis elegans C.elegans 577 7785 A1008758 as Dipeptid I Di eptidyl a tidase eptidase 4 4 ESTs, Weakly similar to LONN_HUMAN MITOCHONDRIAL

LON PROTEASE HOMOLOG

578 16701 A1008838 PRECURSOR [H.sa lens]

ESTs, Weakly similar to CYSR RAT

CYSTEINE-RICH PROTEIN

579 21789 A1008930 k (R.norvegicus 580 21895 A1008971 General ESTs R.norvegicus mRNA
encoding 45kDa i,aa, protein which binds to heymann 581 410 A1008974 General nephritis antigen g 330 ESTs, Highly similar to BAG-family molecular chaperone regulator-2 582 21632 A1009167 General (H.sapiens]

583 21596 A1009168 General ESTs 584 22801 A1009197 General ESTs ESTs, Highly similar to similar to cc, human DNA-binding protein 5 585 11876 A1009321 General [H.sa lens 586 2506 A1009341 General ESTs 587 6382 A1009362 General ESTs ESTs, Highly similar to LmplO

588 14370 A1009427 k proteasome subunit [M.musculus]

TABLE MMARY ~ Atty. Docket No.
1: 44921-5U89W0 SU

w~" Doe. No. 1798397.1 ~Seyuence GenBank Model Accl .,.,., ~~

ID No. dentifier, Code Gene Name Unigene Cluster I Ref. Seq Tittle ID

ESTs, Highly similar to filamin 589 19275 A1009460 x [H.sa iens]

590 4154 A1009467 g ESTs 591 3464 A1009589 cc ESTs ESTs, Highly similar to molybdopterin-592 3926 A1009592 a s nthase large subunit M.musculus 593 19358 A1009675 c EST

594 22545 A1009747 g ESTs cc, 595 15089 A1009752 General ESTs 596 5458 A1009756 h ALG-2 interactingALG-2 interacting protein 1 rotein 1 597 6844 A1009770 e,r,cc ESTs ESTs, Highly similar to RS16_HUMAN

598 15627 A1009810 as [R.norvegicus]

599 22619 A1009825 d ESTs 600 7857 A1009898 ',I,m,z ESTs 601 13259 A1009946 r ESTs 602 21105 A1010067 General ESTs Testis enhanced gene 603 24627 A1010102 as ranscri t Testis enhanced t gene transcript ESTs, Moderately similar to YA00_HUMAN HYPOTHETICAL

PRECURSOR

604 12716 A1010178 General [H.sa iens]

605 18757 A1010216 as ESTs aa, ESTs, Weakly similar to claudin-7 606 2912 A1010220 General R.norvegicus 607 3316 A1010237 t ESTs 608 15644 A1010256 General R.norvegicus mRNA
for histone H3.3 Rattus norvegicus mRNA for inetrleukin-4 receptor (membrane-609 657 A1010262 b bound form), complete cds 610 3271 A1010303 b ESTs ESTs, Moderately similar to erythroblast macrophage protein EMP

611 11081 A1010407 bb H.sapiens]

c,s,t, 612 16521 A1010470 GeneralCerulo lasmin Ceruloplasmin (ferroxidase) (ferroxidase) 613 6927 A1010542 General ESTs a,l,Y.

614 17524 A1010568 GeneralGrowth hormoneGrowth hormone receptor receptor 615 6946 A1010642 n ESTs ESTs, Highly similar to SDP3 616 23509 A1010962 as [M.musculus 617 6044 A1011285 t ESTs 618 13855 A1011361 o ESTs 619 21779 A1011380 cc ESTs 621 12534 A1011460 cc ESTs ESTs, Moderately similar to HYA22 622 2629 A1011492 e,f [H.sapiens ESTs, Weakly similar to B Chain B, Solution Structure Of The C-Terminal Negative Regulatory Domain Of P53 In A Complex With Ca2+-Bound 623 735 A1011560 f S100b(Bb R.norvegicus ESTs, Moderately similar to LMAS

CHAIN

624 3941 A1011598 General [M.musculus ESTs, Weakly similar to JE0360 gamma-Butyrobetaine hydroxylase 625 7550 A1011607 ',General [H.sa lens ESTs, Weakly similar to I(3)S12 626 0636 A1011634 a protein [D.melano 1 aster]

627 3995 A1011678 General ESTs TABLE MMARY Atty. Docket No.
1: 44921-5U89W0 SU

_ Doe. No. 1798897.1 Sequence GenBank Model Accl tD No. dentifierRef. Sey ' Gene Narne Unigre,~ne Cluster I IU ~ ode Tittle ESTs, Weakly similar to SFRS RAT

SPLICING FACTOR, ARGININE/SERINE-RICH

628 16112 A1011706 h [R.norvegicus ESTs, Weakly similar to A35902 Fc 629 13354 A1011757 c gamma R.norvegicus 630 12745 A1011799 cc ESTs ESTs, Highly similar to AF151842 1 631 18684 A1011812 t CGI-84 protein [H.sapiens 632 4205 A1011982 b ESTs ESTs, Moderately similar to 829425 633 6518 A1012114 General [H.sapiens 634 17407 A1012145 General ESTs ESTs, Weakly similar to PPP5 RAT

SERINE/THREONINE
PROTEIN

635 13093 A1012177 r PHOSPHATASE 5 [R.norvegicus]

ESTs, Moderately similar to Y33K_HUMAN HYPOTHETICAL
33.4 636 15395 A1012216 f KDA PROTEI H.sapiens ESTs, Weakly similar to S70484 RS43 637 21796 A1012221 d,General protein - rat (fragment) [R.norvegicus]

638 3981 A1012235 i,General ESTs 639 6606 A1012308 i,r ESTs ESTs, Highly similar to NHPX RAT

PROTEIN

640 3417 A1012337 w YEL026W HOMOLOG
R.norvegicus b,t, 641 24200 A1012356 General ESTs 642 7471 A1012379 cc ESTs 643 7247 A1012438 g ESTs 644 7127 A1012464 p,General ESTs ESTs, Weakly similar to T26998 hypothetical protein Y48B6A.6 -645 3304 A1012471 b Caenorhabditis elegans C.elegans 646 2311 A1012485 as ESTs glutathione S-transferase, pi 647 20817 A1012589 g,n,q2 glutathione S-transferase, pi 2 648 3493 A1012590 v,General ESTs 649 8975 A1012613 General ESTs ESTs, Highly similar to unknown 650 11335 A1012619 j [H.sa lens]

651 21409 A1012637 General ESTs ESTs, Moderately similar to AF151834 652 8015 A1012638 as 1 CGI-76 rotein [H.sa iens]

ESTs, Highly similar to RS20_HUMAN

653 8476 A1012647 w R.norve icus]

e,p, 654 232 A1012958 General ESTs 655 23128 A1013011 General ESTs 656 20086 A1013260 Generalamin lamin l ESTs, Highly similar to GLIA

DERIVED NEXIN PRECURSOR

657 1969 A1013273 k R.norvegicus]

658 26147 A1013387 as 659 8815 A1013437 p ESTs Rattus norvegicus Hsp70 binding 660 9722 A1013508 k rotein Hs BP mRNA, 1 complete cds 661 674 A1013568 General ESTs 662 3145 A1013647 o,t ESTs 663 5130 A1013876~w ESTs ]1 ~

_71 _ TABLE UMMARY Att~y. Docket No.
1: 44931-5U89W0 S enf3ank odel a floe. No. 1798397.1 dentifier~ccl Code Gene Name ~ ~ ~~ i ~Sequenee ~ , gene Cluster Title IU No: Ref. Seq ' ID ;, ESTs, Moderately similar to BMP6 RAT BONE MORPHOGENETIC
64 274 1013715 s PROTEIN 6 PRECURSOR
[R.norvegicus]

ESTs, Highly similar 665 7276 A1013730 a to KIAA1102 protein H.sapiens]

666 7278 A1013738 ,z,aa ESTs s,x,bb, ESTs, Highly similar 667 22592 A1013740 General to proteolipid protein 2 [M.musculus]

668 16584 A1013765 w Arrestin, betaArrestin, beta ESTs, Highly similar to T27225 ADP-ribosylation factor 69 4143 1013804 ,1 Y57G11C.13 (similarity] -Caenorhabditis elegans (C.elegans]

670 15928 A1013829 a,General ESTs 3-hydroxyisobutyrate 671 21950 A1013861 j dehydrogenase 3-h drox isobut rate deh drogenase 672 3260 A1013875 t ESTs ESTs, Moderately 673 2708 A1013882 d, similar to MSSP
[M.musculus 674 8585 A1013886 i ESTs p,r,t, ESTs, Weakly similar 675 7299 A1013911 General to CIRP
[R.norvegicus]

Rat ankyrin binding 676 15904 A1013971 General glycoprotein-1 related mRNA sequence ESTs, Moderately 677 12781 A1014023 w similar to 832184 H.sapiens Rattus norvegicus mRNA for beta-78 9372 1014135 s carotene 15,15'-dioxygenase, complete cds ESTs, Highly similar 679 4241 A1014140 w to hypothetical protein H.sapiens]

680 15247 A1014169 c,u Rattus norvegicus clone N27 mRNA

ESTs, Moderately n similar to mitogen-81 315 1028831 activated protein kinase kinase kinase 6 H.sapiens]

682 16631 A1028856 General ESTs ESTs, Highly similar 683 23297 A1028953 x to S55054 Sm protein G H.sapiens]

684 11326 A1029015 b ESTs 685 2866 A1029058 n, ESTs 686 12812 A1029126 General ESTs 687 17602 A1029156 p ESTs 688 7392 A1029185 as EST

689 6517 A1029264 d,k,x ESTs 690 7639 A1029292 b ESTs ESTs, Highly similar to CB80_HUMAN
91 874 1029428 ,General 80 KDA NUCLEAR
CAP BINDING
PROTEIN H.sa iens 692 12819 A1029437 f ESTs 693 7452 A1029466 r ESTs 694 7493 A1029608 b ESTs 696 7537 A1029829 o,General ESTs 697 2310 A1029969 v ESTs 698 7585 A1030023 x ESTs 699 7586 A1030024 b,n ESTs 700 14492 A1030091 cc ESTs ESTs, Weakly similar 701 10673 A1030134 f to ankyrin (R.norvegicus]

702 7615 A1030163 o,r ESTs 703 2370 A1030179 General ESTs ESTs, Moderately n similar to 04 681 1030449 methyltransferase related protein M.musculus _72_ T~tBLE UM ARY '~~'~ ' Atty. Docket 1: No. 44921-5U89W0 S

"~ Doe. No. 1798397.1 a Sequence GenB~ank 'Model /',ccl ' IU No. IdentifierRef. Seq 'CodeGene Name :U",n"ige~e Cluster I~ , Tittle ~

705 11559 A1030472 General ESTs - Rattus norvegicus nucleosome assembly protein mRNA, complete 706 7665 A1030668 t,bb cds 707 24222 A1030704 k ESTs 708 10740 A1030743 h EST

709 10742 A1030773 a EST

ESTs, Moderately similar to 711 16169 A1030932 General adipophilin H.sapiens]

712 19527 A1030991 f EST

ESTs, Highly similar to SX17 MOUSE

TRANSCRIPTION FACTOR

713 22614 A1031004 r [M.musculus) ESTs, Highly similar to CLPP MOUSE

PUTATIVE ATP-DEPENDENT
CLP

PROTEASE PROTEOLYTIC

SUBUNIT, MITOCHONDRIAL

714 3167 A1031012 a PRECURSOR [M.musculus 715 5350 A1043611 a ESTs 716 7858 A1043654 t EST

717 10784 A1043678 d EST

ESTs, Weakly similar to T27134 hypothetical protein Y53C12B.2 -718 9180 A1043694 as Caenorhabditis ele ans [C.elegans]

HHs:phosphoribosyl pyrophosphate Rattus norvegicus mRNA for 719 7867 A1043695 as amidotransferaseamido hosphoribos Itransferase 720 7584 A1043724 General ESTs ESTs, Highly similar to AF151810 1 721 7895 A1043768 a CGI-52 protein H.sapiens 722 7903 AIO43805 General ESTs ESTs, Weakly similar to ELL MOUSE

RNA POLYMERASE
II ELONGATION

723 7913 A1043849 cc FACTOR ELL [M.musculus]

724 3899 A1043904 I ESTs 725 6766 A1043914 f ESTs g,l,m, 726 10818 A1043990 General ESTs 727 7956 A1044018 f EST

728 5393 A1044170 p EST

729 5398 A1044177 q EST

ESTs, Weakly similar to AF121893 1 sequence-specific single-stranded-730 5425 A1044237 a,d DNA-binding protein [R.norvegicus]

ESTs, Weakly similar to putative peroxisomal 2,4-dienoyl-CoA

731 8692 A1044247 r reductase R.norvegicus 732 5430 A1044253 i EST

9.p.

733 5461 A1044338 General ESTs 734 5464 A1044345 i ESTs 735 3359 A1044347 as ESTs Rat (clones rLG[08,14,25]) interleukin 737 2695 A1044396 b 6 signal transducer mRNA sequence 738 5494 A1044425 General ESTs 740 9882 A1044588 ',m ESTs 741 5575 A1044688 g ESTs 742 2348 A1044794 General ESTs ESTs, Weakly similar to AF165892 1 RNA-binding protein SiahBP

743 18205 A1044836 n R.norvegicus 744 5626 A1044864 a ESTs 745 5630 A1044869 f ESTs ESTs, Moderately similar to AF151873 746 5634 A1044883 General 1 CGI-115 rotein H.sa lens TABLE MMARY Atty. Doe et No.
1: 44921-5U89W0 SU enBank Model Doe. No. 1798897.1 entifierAcel Code ene Name Sequence Ref. Seq Unigene Cluster 1~ No. 4047 ID I,m Title I ESTs, Moderately A1044947 similar to 747 dJ1183121.1 [H.sa iens]

748 5654 A1044976 w EST

749 5684 A1045056 r ESTs ESTs, Highly similar to BGAL MOUSE
50 9235 1045074 eneral BETA-GALACTOSIDASE
PRECURSOR M.musculus i,aa, ESTs, Moderately 751 5689 A1045075 General similar to HEM45 [H.sapiens ESTs, Moderately 752 5711 A1045151 General similar to AF118838 1 citrin [H.sapiens ESTs, Weakly similar c to TVRTK6 53 1 237 1045153 ribosomal protein S6 kinase R.norvegicus]

754 9964 A1045161 f EST

755 5735 A1045223 f ESTs 756 5474 A1045477 a,General ESTs 757 5811 A1045502 d,e ESTs 758 5819 A1045537 General ESTs 759 5839 A1045594 i ESTs ESTs, Highly similar s to S30034 60 808 1045600 translocating chain-associating membrane protein H.sapiens]

761 7755 A1045608 ESTs 763 10020 A1045632 a ESTs 764 5855 A1045669 General ESTs ESTs, Weakly similar i to T12540 65 881 1045789 hypothetical protein DKFZp434J214.1 H.sapiens]

ESTs, Moderately similar to S64732 66 897 1045862 eneral scaffold attachment factor B
[H.sapiens]

767 5900 A1045866 ,z ESTs ESTs, Weakly similar o,t, to 848013 68 540 1045882 General proline-rich proteoglycan 2 precursor, parotid - rat R.norvegicus 769 5329 A1045970 p ESTs 770 15093 A1058285 d ESTs 771 8002 A1058304 i ESTs 772 8017 A1058341 c EST

ESTs, Weakly similar to T46465 73 828 1058359 eneral hypothetical protein DKFZp434A0530.1 [H.sa lens]

774 8177 A1058603 as ESTs 775 3090 A1058730 as ESTs 776 10093 A1058746 g ESTs 777 8143 A1058759 General ESTs 778 18659 A1058762 f ESTs 779 8163 A1058837 as ESTs 780 4789 A1058889 General ESTs 781 8221 A1059061 General ESTs 782 10159 A1059147 d EST

ESTs, Weakly similar 783 8245 A1059154 b to unnamed protein roduct H.sa iens]

784 8283 A1059290 n ESTs 785 8314 A1059386 g,General ESTs 786 10200 A1059444 i ESTs ESTs, Weakly similar to EGF RAT
s PRO-EPIDERMAL GROWTH

[R.norvegicus Rattus norvegicus n transitional 88 8359 1059675 endoplasmic reticulum ATPase mRNA, com lete cds TABLE MMARY Atty. Docket No.
1: 44921-5U89W~
SU

Doe. No. 179'8397.1 Sequence GenBank Model Accl ID No. dentifierRef. Seq Code Gene Name Un~gene Cluster .I ID Tittle 789 0281 A1059947 b,t EST

790 8494 A1059968 as ESTs ESTs, Weakly similar to TNRC

MOUSE LYMPHOTOXIN-BETA

RECEPTOR PRECURSOR

791 8495 A1059971 General [M.musculus]

ESTs, Moderately similar to KIAA0978 792 8496 A1059974 General protein H.sapiens ESTs, Weakly similar to CGI-142 793 10289 A1060053 hypothetical protein i H.sapiens 794 8548 A1060176 k ESTs t 796 18322 A1060279 , ESTs i ,z 797 8745 A1069939 r ESTs ESTs, Highly similar to rer 798 8785 A1070067 0 [M.musculus]

ESTs, Weakly similar to 2104282A

799 17506 A1070068 cc Gadd45 gene [R.norvegicus ESTs, Weakly similar to NUCL RAT

800 9067 A1070087 General NUCLEOLIN R.norvegicus ESTs, Moderately similar to CGI-97 801 3551 A1070122 a rotein [H.sa lens]

ESTs, Moderately similar to GLMB

RAT GLIA MATURATION
FACTOR

802 4967 A1070179 k BETA [R.norvegicus]

ESTs, Moderately similar to AF132954 803 18 A1070195 General 1 CGI-20 protein H.sapiens]

ESTs, Moderately similar to ARVC_HUMAN ARMADILLO

REPEAT PROTEIN
DELETED IN

VELO-CARDIO-FACIAL
SYNDROME

804 24197 A1070314 General [H.sapiens]

805 8869 A1070330 r ESTs 806 8874 A1070336 b,cc ESTs 807 0417 A1070410 m ESTs ESTs, Moderately similar to T08664 Toll protein-like receptor 808 8901 A1070419 as DKFZp54710610.1 [H.sapiens LP.

809 4424 A1070421 General ESTs 810 0434 A1070497 General ESTs 811 8927 A1070523 v ESTs 812 8946 A1070611 q ESTs 813 8950 A1070621 w ESTs 814 8972 A1070673 General ESTs 815 8981 A1070715 bb EST

816 26184 A1070784 ,l i ESTs, Weakly similar to hypothetical 817 3007 A1070824 w protein H.sapiens 818 8999 A1070839 p ESTs bone morphogeneticbone morphogenetic protein protein 1 819 10477 A1070868 e,f (procollagen (procollagen C-1 C-proetinase) roetinase) 820 24301 A1070911 k ESTs 821 8721 A1071024 General EST

822 9212 A1071098 x ESTs 823 1831 A1071137 c Rat mRNA for cdc25B, complete cds 824 11005 A1071139 r EST

ESTs, Highly similar to HETEROGENEOUS NUCLEAR

RIBONUCLEOPROTEIN
G

825 9104 A1071173 ,m M.musculus j 826 9583 A1071185 General ESTs 827 9644 A1071410 c ESTs TABLE MME1RY ~' Atty. Docket No.44931-5U89W0 : SU

Doe. No. 1798397.1 Sequence GenBanlin4cclModel 1D No. IdentifierRef Seqylp,CodeGene Narne Uni~en~e G~luster Title HHsaerine palmitoyltransferase,ESTs, Highly similar long to JC5180 serine 828 16058 A1071490 Generalchain base C-palmito Itransferase subunit 2 [M.musculus 829 11057 A1071509 f,o ESTs ESTs, Weakly similar to SYBSR

threonine synthase (EC 4.2.99.2) -yeast (Saccharomyces cerevisiae) 831 5695 A1071566 bb (S.cerevisiae]

832 9671 A1071568 w EST

ESTs, Moderately similar to NEURONAL PROTEIN
3.1 833 22929 A1071578 General M.musculus 834 9673 A1071581 General ESTs 835 9699 A1071646 General ESTs 837 9799 A1072008 q,y,z ESTs 838 9808 A1072050 d ESTs 839 22796 A1072213 General ESTs 840 9271 A1072405 v ESTs 841 10869 A1072425 w ESTs ESTs, Weakly similar to S70484 RS43 842 21797 A1072439 General protein - rat (fragment) [R.norvegicus]

843 9306 A1072521 r ESTs 844 9312 A1072550 j ESTs 845 10893 A1072559 x EST

cc,Gener Rattus norvegicus cytokeratin-18 846 1501 A1072634 al mRNA, artial cds 847 6548 A1072658 General ESTs ESTs, Highly similar to JE0170 dnaJ

heat shock protein MCG18 - mouse 848 9363 A1072695 d [M.musculus]

ESTs, Moderately similar to LMG2 CHAIN

850 9409 A1072841 n PRECURSOR M.musculus 851 9410 A1072842 w ESTs 852 9468 A1073021 General ESTs 853 9518 A1073223 f EST

ESTs, Weakly similar to CAH2 RAT

CARBONIC ANHYDRASE
II

854 11183 AI100768 t HHs:carbonic [R.norvegicus anh drase VIII

855 9190 AI100835 a ESTs 856 2029 A1100842 p ESTs 857 5687 A1101006 a ESTs Rat metallothionein-2 and 858 15192 AI101099 g,cc metallothionein-1 enes, com lete cds ESTs, Highly similar to ATPK MOUSE

ATP SYNTHASE F
CHAIN, 859 17399 AI101157 o MITOCHONDRIAL [M.musculus]

ESTs, Weakly similar to S46930 860 9339 AI101160 I,m,o teg292 protein - mouse M.musculus ESTs, Weakly similar to AIF-C1 861 6321 AI101256 General R.norvegicus ESTs, Highly similar to GDIS MOUSE

RHO GDP-DISSOCIATION

862 5421 AI101270 c INHIBITOR 2 [M.musculus]

ESTs, Highly similar to ERM_HUMAN

ETS-RELATED PROTEIN
ERM

863 11910 AI101323 General [H.sapiens]

864 23140 AI101608 a ESTs 865 4119 A1101901 General ESTs ESTs, Weakly similar to TRBP

RNA

866 16324 AI102009 b BINDING PROTEIN
[M.musculus]

ESTs, Moderately similar to unknown 867 18642 AI102023 0 [H.sapiens]

TABLE UMMARY ~tty. Docket No.
1: 44921-5U89W0 S

Doe. No. 1798397.1 i Sequence" GenBank Model , Accl ID No. ~entifierRef. Seq Code Gene Name ~ Unigene C,lus"~ter ~. IU Tittle Rattus norvegicus mRNA for beta-Drosophila carotene 15,15'-dioxygenase, polarity gene 868 19373 AI102044 a frizzled) homologuecomplete cds ( Rattus norvegicus clone ZG52 mRNA

869 7051 AI102055 h sequence ESTs, Weakly similar to AF147718 1 870 6544 AI102064 c g1 tine decarbox lase [R.norvegicus]

871 10227 AI102248 w ESTs 872 23849 A1102318 e, ESTs Rattus norvegicus liver cytochrome c HMm:cytochromeoxidase subunit c oxidase, Vlll (COX-VIII) 873 11954 AI102505 g,j,ssubunit Vllla mRNA, 3' end of cds ESTs, Moderately similar to DAP12 874 2125 AI102519 c,k [M.musculus]

ESTs, Moderately similar to AF161588 1 GABA-A receptor-associated protein 875 5967 AI102520 R.norvegicus]

ESTs, Moderately similar to AF161588 1 GABA-A receptor-associated protein 875 5969 AI102520 ,w [R.norvegicus]

876 11563 AI102560 General ESTs 877 15190 A1102562 b,g,n,p,v Rat metallothionein-i (mt-1) mrna EST, Weakly similar to A60716 somatotropin intron-related protein 878 19769 AI102570 bb RDE.25 - rat R.norvegicus ESTs, Highly similar to 149523 Mouse primary response gene B94 mRNA, 879 22487 AI102578 General 3'end - mouse [M.musculus]

880 19011 AI102618 General ESTs 881 23837 AI102620 q,t ESTs solute carrier family 20 ( phosphate transporter),solute carrier family 20 (phosphate 882 23538 AI102727 g,Generalmember 1 transporter , member Tissue inhibitor of 883 17234 AI102741 c metalloproteinaseTissue inhibitor 3 of metalloproteinase 884 5891 AI102745 k ESTs 885 6796 A1102753 General ESTs 886 8837 AI102849 o,p ESTs ESTs, Weakly similar to phosphoserine aminotransferase 887 15861 AI102868 i H.sapiens]

888 3533 AI102877 g ESTs ESTs, Highly similar to PCAF

889 13222 AI102977 General associated factor 65 beta [H.sapiens]

890 6806 AI103018 o,u ESTs w,cc, 891 10659 AI103059 General ESTs ESTs, Highly similar to ATPK MOUSE

ATP SYNTHASE F
CHAIN, 892 17400 AI103097 a MITOCHONDRIAL [M.musculus 893 3584 AI103106 x,aa ESTs 894 13298 AI103143 r ESTs ESTs, Weakly similar to UBC2_HUMAN UBIQUITIN-CONJUGATING ENZYME

895 15981 AI103150 i,x (R.norvegicus ESTs, Highly similar to AF151893 1 896 3475 AI103245 w CGI-135 rotein [H.sa lens 898 23619 AI103314 ESTs ESTs, Moderately similar to T26785 hypothetical protein Y40B1 B.7 -899 24181 AI103320 a Caenorhabditis elegans C.elegans 901 4355 AI103410 General ESTs 902 7622 A1103472 General ESTs 903 20918 AI103552 n ESTs 904 21579 A1103572 General~ ~ ESTs 'FABLE UMMlkRlf'~ ~ Att'y. Docket No.
1: 44921-5U89W0 S

Doe. No. 1798897.1 ' ~Sequenee GenBank Model Accl 1D No: IdentifierRef. Seq ~Co~deGene Name Unigene Cluster I~ ~ Title ESTs, Highly similar to RIE2 905 2222 AI103631 o M.musculus]

ESTs, Highly similar to sarcosine 906 2752 AI103641 a deh drogenase [R.norvegicus 907 4856 AI103708 i ESTs 908 8990 A1103719 I,m, ,z 909 15942 AI103738 r ESTs 910 22885 A1103828 e,General ESTs 911 15853 A1103841 x Complement Complement com component onent 4 HHs:ubiquinol-cytochrome c r eductase, RieskeRat Rieske iron-sulfur iron-sulfur protein mRNA, 912 15050 AI103911 j, of peptide com lete cds 913 12376 AI103939 a ESTs ESTs, Weakly similar to AF151109 1 putative BRCA1-interacting protein 914 22271 AI103947 o,y [H.sapiens ESTs, Highly similar to COXG

HMm:RIKEN cDNAMOUSE CYTOCHROME
C OXIDASE

915 20833 AI104035 f,q 2010000605 POLYPEPTIDE VIB
gene [M.musculus]

916 7010 AI104099 w ESTs 917 22101 A1104251 General ESTs 918 22833 AI104258 General ESTs ESTs, Highly similar to translation 919 22211 AI104279 g,m initiation factor eIF6 M.musculus 920 10720 AI104296 I ESTs 921 15416 A1104340 i ESTs 922 10991 A1104342 a ESTs ESTs, Highly similar to ATRTC actin 923 18831 AI104357 beta - rat [R.norvegicus]

924 7223 AI104373 a ESTs Cytochrome Cytochrome c oxidase c oxidase subunit Vla 925 23574 A1104520 e,g,subunit Vla (liver) s (liver) ESTs, Weakly similar to NADH:ubiquinone oxidoreductase 926 18509 AI104528 subunit H.sapiens 927 11680 AI104605 v ESTs ESTs, Weakly similar to RENAL

TRANSCRIPTION FACTOR

928 12342 AI104658 w R.norvegicus Rat mitochondrial succinyl-CoA

synthetase alpha subunit (cytoplasmic 929 23689 AI104685 r precursor) mRNA, com lete cds ESTs, Moderately similar to T50611 hypothetical protein 930 15377 AI104821 o,cc DKFZp434H2035.1 H.sapiens ESTs, Moderately similar to meningioma-expressed antigen 11 931 22957 AI104897 General H.sa lens]

HHs:ATP synthase, H+

t ransporting, Rattus norvegicus mitochondrial delta subunit of 932 18451 AI104953 o,s Fi com lex, F1F0 ATPase gene, delta subunit complete cds ESTs, Moderately similar to nucleolar 933 24375 AI104979 n,General rotein p40 H.sapiens ESTs, Moderately similar to SCOT_HUMAN SUCCINYL-COA:3-KETOACID-COENZYME
A

TRANSFERASE PRECURSOR

934 18278 AI105080 bb H.sapiens 935 2196 A1105243 g ESTs ESTs, Weakly similar to T21641 bb, hypothetical protein F32B6.2 -936 5199 AI105272 General Caenorhabditis elegans C.elegans 937 12901 AI105301 o,s ESTs _78_ TABLE MMARY Attjy. Docket No.
1: 44921-5U89W0 SU

Doe. No. 1798397.1 Sequence GenBank Mode Aee/

ID No. dentifierRef. Seq Code Gene Name Unigene Cluster I ID Title ESTs, Weakly similar to T19707 cc, hypothetical protein C34C6.5 -938 7700 AI105383 General Caenorhabditis elegans [C.elegans]

939 3343 AI105398 a ESTs ESTs, Moderately similar to NEURONAL PROTEIN
3.1 940 22931 AI105417 e,General M.musculus ESTs, Highly similar to GCDH

MOUSE GLUTARYL-COA

HMm:glutaryl-CoenzymeDEHYDROGENASE PRECURSOR
A

941 23596 AI105435 bb deh drogenase [M.musculus]

ESTs, Moderately similar to DHSD_HUMAN SUCCINATE

942 15893 AI105465 o DEHYDROGENASE [H.sa iens]

943 12660 AI111492 c ESTs 944 4479 A1111599 General ESTs ESTs, Highly similar to H33_HUMAN

945 24211 AI111853 k HISTONE H3.3 [R.norvegicus ESTs, Weakly similar to FKB5 946 2539 AI111960 PROTEIN [M.musculus]
r EGF-CONTAINING
FIBULIN-LIKE

EXTRACELLULAR MATRIX

(FIBULIN-3) (FIBL-3) (T16 PROTEIN) 947 5729 AI111990 k R.norve icus]

i ,q,u, Rattus norvegicus osteoactivin mRNA, 948 4049 AI112012 General com lete cds 949 12908 AI112043 ESTs i 950 20041 A1112161 ESTs t 951 12937 A1112462 General ESTs 952 3713 A1112571 b ESTs ESTs, Moderately similar to UDP_HUMAN URIDINE

953 12921 AI112636 General PHOSPHORYLASE [H.sapiens 954 12965 AI112926 General ESTs 955 7499 AI112986 General ESTs ESTs, Moderately similar to megakaryocyte stimulating factor 956 4969 AI113008 H.sapiens]
r ESTs, Highly similar to BC-2 protein 957 11817 AI136295 H.sapiens f ESTs, Weakly similar to JC4975 plexin 2 precursor - mouse 959 11165 AI136372 c [M.musculus]

960 4045 A1136460 cc ESTs 961 12782 A1136493 k ESTs 962 6850 A1136665 h ecto-ap race ecto-ap race 963 20920 AI136891 ,v but rate res but rate response once factor factor 1 ESTs, Highly similar to 6.2 kd protein 964 6552 AI137062 o H.sapiens]

965 22722 AI137211 ESTs i ESTs, Highly similar to oxysterol-966 13111 AI137224 o,General binding rotein M.musculus 967 15969 AI137302 a ESTs 968 14349 A1137303 d ESTs 969 9166 A1137406 General ESTs ESTs, Weakly similar to ZF37_RAT

ZINC FINGER PROTEIN
37 (ZFP-37) 970 9525 AI137516 [R.norvegicus r 971 6638 AI137579 General ESTs ESTs, Highly similar to IMB3_HUMAN

SUBUNIT

972 7414 AI137586 General [H.sa lens]

973 11321 AI137752 z ESTs 974 23473 A1137932 ESTs I

_7s_ TABLE UMMAR Atty. Docket No.
1: 44921-5U89W~
S

Doe. No. 1798397.1 Sequence GenBank EModel Acel ID No, IdentifierRef. Seq ~CocJeGene Name Unige"any,,e Cluster , .~ ID Title 975 13158 AI138024 i ESTs UDP-glucose:ceramideUDP-glucose:ceramide 976 13467 AI138034 cc g1 cosyltransferaseg1 cos Itransferase 977 11377 AI138105 y ESTs 978 6790 A1144801 d,h ESTs 979 6506 A1144919 j,1, ESTs 980 8027 AI144958 i ESTS

982 14458 A1145095 General ESTs 983 7476 A1145202 g ESTs ESTs,ESTs, Weakly similar to GTP-984 17545 AI145384 a bindin rotein [H.sapiens]

985 17479 AI145385 r ESTs 986 4194 A1145387 r ESTS

ESTs, Weakly similar to T31511 hypothetical protein Y116A8C.9 -987 8634 AI145722 g Caenorhabditis elegans C.elegans ESTs, Weakly similar to T21659 hypothetical protein F32D8.4 988 8339 AI145761 ,General Caenorhabditis elegans [C.ele ans]

ESTs, Highly similar to pseudouridine 989 2059 AI146005 h,General synthase 1 [M.musculus]

Rattus norvegicus small zinc finger-990 23224 AI146033 0 like protein (TIM9a) mRNA, partial cds branched chain keto acid dehydrogenase branched chain E1, beta keto acid 991 5232 AI168942 bb pol eptide deh drogenase E1, beta polype tide 992 18472 AI168975 a ESTs 992 18473 A1168975 a ESTs 993 13235 A1169020 r ESTs o,y, 994 11618 A1169115 General ESTs ESTs, Weakly similar to T23206 hypothetical protein K01H12.1 -995 17386 AI169144 o Caenorhabditis elegans [C.elegans ESTs, Weakly similar to HP33 996 10984 AI169156 o,u [R.norve icus]

997 8205 AI169176 a ESTs ESTs, Highly similar to RADIATION-INDUCIBLE IMMEDIATE-EARLY

998 12979 AI169177 a GENE IEX-1 M.musculus ESTs, Highly similar to A47318 RNA-binding protein Raly - mouse 999 2607 AI169211 c M.musculus ATPase, H+
transporting, l ysosomal (vacuolarATPase, H+ transporting, proton lysosomal 1000 22661 AI169265 s,z pum ), subun (vacuolar roton pum , subunit 1001 13239 AI169278 ,',I, ESTs ,z 1002 24162 AI169279 m ESTs ESTs, Highly similar to Y069_HUMAN

HYPOTHETICAL PROTEIN

1003 16879 AI169284 o H.sapiens]

ESTs, Highly similar to H33_HUMAN

1004 24213 AI169289 HISTONE H3.3 R.norvegicus]

1005 13240 AI169311 cc ESTs 1006 5931 A1169324 b ESTs ESTs, Highly similar to CGI-117 1007 20891 AI169337 d protein [H.sapiens 1008 11979 AI169365 cc ESTs arachidonic acid 1009 10947 AI169372 s epox genase arachidonic acid epox genase 1010 20697 AI169494 o,u ESTs 1011 8234 A1169517 z ESTs 1012 18343 A1169648 o ESTs 1013 10839 A1169655 I,m ESTs ESTs, Weakly similar to hypothetical 1014 24146 AI169668 j,1 protein (H.sapiens]

-ao-TABLE MMAR '~ Atty. Docket No.
1: 44921-5U89W0 SU

Uoe. No. 17 98397.1 , I _ _ Sequence GenBank Model Accl ~

ID No. dentifierRef. Seq Code Gene Name Unigene Cluster I ID ~ Tit,]"~le ESTs, Moderately similar to T47184 hypothetical protein 1015 22575 AI169728 r DKFZ 434F1526.1 [H.sapiens]

ESTs, Highly similar to GENE 33 1016 804 A1169756 cc POLYPEPTIDE [R.norvegicus]

1017 8213 AI169883 f erritin light ferritin light chain 1 chain 1 1018 3916 AI169947 i,bb ESTs 1019 3733 AI170053 u,General ESTs 1020 14179 AI170224 cc ESTs ESTs, Moderately similar to class II

1021 11406 AI170263 r c tokine receptor 4 [M.musculus]

ESTs, Weakly similar to ZNT1 RAT

ZINC TRANSPORTER

1022 3547 AI170279 General [R.norvegicus]

ESTs, Weakly similar to CL36 RAT

LIM DOMAIN PROTEIN

1023 11524 AI170340 j,y,z [R.norvegicus]

1024 2729 AI170363 e,i ESTs 1025 18811 A1170525 i ESTs 1026 22524 A1170542 h ESTs ESTs, Highly similar to CGI-10 protein 1027 24048 AI170570 a,g [H.sapiens ESTs, Moderately similar to AF161588 1 GABA-A receptor-associated protein 1028 5968 AI170692 ,aa [R.norvegicus 1029 9757 AI170693 b ESTs ESTs, Highly similar to NADH-ubiquinone oxidoreductase 1030 18905 AI170770 e,s subunit H.sapiens ESTs, Moderately similar to 1031 16170 AI170894 i adipo hilin [H.sapiens]

Hyaluronan Hyaluronan mediated mediated motilitymotility receptor 1032 7089 AI171185 c eceptor (RHAMM)(RHAMM) r 1033 17591 AI171354 b ESTs ESTs, Weakly similar to AIF-C1 1034 13285 AI171361 h [R.norvegicus HHs:NADH dehydrogenaseESTs. Moderately similar to ( ubiquinone) NUAM_HUMAN NADH-UBIQUINONE
Fe-S protein ( 75kD) (NADH-coenzymeOXIDOREDUCTASE

1035 4428 AI171362 a eductase) PRECURSOR [H.sa r iens]

ESTs, Highly similar to S16788 probable reverse transcriptase - rat 1036 8126 AI171369 w [R.norvegicus]

ESTs, Moderately similar to 68MP

MOUSE 6.8 KD MITOCHONDRIAL

1037 23253 AI171448 o PROTEOLIPID [M.musculus]

m, 1038 584 A1171492 General ESTs ESTs, Moderately similar to NADH:ubiquinone oxidoreductase 1039 1158 A1171542 r,s subunit H.sapiens) 1040 5345 AI171587 I ESTs 1041 21183 A1171676 k ESTs Rattus norvegicus kynurenine aminotransferase/glutamine transaminase K
(Kat) gene. complete 1042 8215 AI171692 i erritin light cds,ferritin light f chain 1 chain 1 1043 1437 AI171794 i ESTs 1044 625 A1171800 cc ESTs 1045 3579 A1171802 v ESTs 1046 1708 A1171807 I,t ESTs Rattus norvegicus F1-ATPase epsilon HMm:RIKEN cDNAsubunit mRNA, nuclear gene encoding 1047 7204 AI171844 s, 410043619 genemitochondrial rotein, 1 ,z com lete cds _s1_ TABLE MMARY Att~y. Docket No.
1: 44921-5U89W0 SU

Doe. No. 1798397.1 Sequence GenBank Model Accl ID No. IdentifierRef. Seq Code Gene Narne Unigene Cluster IU Ti ~le 1048 4420 AI171916 m ESTs ESTs, Highly similar to T08675 hypothetical protein 1049 3266 AI171948 ,m DKFZp564F0522.1 I [H.sapiens 1050 19012 AI172056 ESTs t 1051 11205 A1172057 a, ESTs ,bb ESTs, Weakly similar to T33238 hypothetical protein T10H9.3 -1052 6057 AI172102 b Caenorhabditis elegans [C.elegans]

1053 19128 AI172103 m ESTs Rat mRNA for 5E5 antigen, complete 1054 15673 AI172107 z cds 1055 6630 A1172184 n ESTs ESTs, Weakly similar to FETA RAT

ALPHA-FETOPROTEIN

1056 11968 AI172208 bb PRECURSOR [R.norvegicus 1057 6974 AI172263 ,m ESTs I

1058 23313 A1172271 d ESTs ESTs, Moderately similar to A53004 t ranscription elongation factor S-II -rat 1059 2140 AI172272 General [R.norvegicus]

ESTs, Weakly similar to S43056 I ,p, hypothetical protein - mouse 1060 15382 AI172302 General[ M.musculus]

1061 18689 A1172329 ESTs I

Rattus norvegicus apoptosis-regulating basic protein mRNA, 1062 17887 AI172414 o complete cds ESTs, Highly similar to A44437 r egenerating liver inhibitory factor 1063 3042 AI172447 General RUIF-1 - rat [R.norve icus]

HMm:isocitrateESTs, Weakly similar to IDHC RAT

dehydrogenase SOCITRATE DEHYDROGENASE
2 (NADP+), I

1064 17291 AI172491 bb mitochondria) R.norvegicus [

1065 26222 A1172506 p 1066 13095 A1172595 ESTs r 1067 8795 A1172618 General ESTs ESTs, Weakly similar to T31067 BIR

r epeat containing ubiquitin-conjugating enzyme BRUCE - mouse 1068 6454 AI175342 ,l,m,y( M.musculus]
j ESTs, Highly similar to RRAS MOUSE

RAS-RELATED PROTEIN
R-RAS

1070 445 AI175466 [ M.musculus 4 x ESTs, Highly similar to NHPX RAT

PROTEIN

1071 3418 AI175475 m YEL026W HOMOLOG
[R.norvegicus]

ESTs, Moderately similar to AF145050 1 translation elongation factor 1-delta 1072 8507 AI175551 bb s ubunit R.norvegicus 1073 0217 AI175628 w ESTs 1074 7262 A1175833 ,m,x ESTs j 1075 9004 AI175875 ESTs 1 r 1076 2352 A1175959 ,General ESTs 2 ( ESTs, Highly similar to pirin 1077 022 AI176041 h,n [ H.sa lens ESTs, Weakly similar to tazarotene-1078 1467 AI176061 i nduced gene 2 H.sapiens 2 t 1079 8581 AI176160 General ESTs 1080 4159 AI176169 ESTs 1 g 1081 1742 A1176172 w ESTs ESTs, Highly similar to P55-C-FOS

PROTO-ONCOGENE
PROTEIN

1082 0182 AI176185 [ R.norve icus 1 v 0083 2765 A1176265 Genera~ ESTs X2 ~ ~

_82_ TABLE MMARY Atty. Docket No.
1: 44931-5U89W0 SU

Doe. No31E7i9899t7~1 1, Sequence GenBank Model Accl ID No. dentifierRef. Seq Code Gene Name Unige~ne Cluster I IU Title ESTs, Weakly similar to GSHH RAT

PHOSPHOLIPID HYDROPEROXIDE

GLUTATHIONE PEROXIDASE

1084 6905 AI176275 a R.norvegicus UAP1_HUMAN UDP-N-ACETYLHEXOSAMINE

1085 12999 A1176276 cc PYROPHOSPHORYLASE
[H.sa iens]

ESTs, Highly similar to SMD2_HUMAN SMALL
NUCLEAR

RIBONUCLEOPROTEIN

1086 6438 AI176294 a H.sapiens) 1087 21130 AI176298 y ESTs 1088 3014 A1176362 a ESTs 1089 15015 A1176363 ESTs r 1090 19006 A1176393 ESTs x ESTs, Moderately similar to OPS1 1091 20001 A1176396 o H.sapiens 1092 12174 AI176435 ,m ESTs j Rat metallothionein-2 and 1093 15191 AI176456 b,o,t,v,cc metallothionein-1 genes, complete cds 109 24236 AI176473 d,General ESTs _ ESTs, Moderately similar to HS9B

RAT HEAT SHOCK
PROTEIN HSP

1095 16518 AI176546 v 90-BETA [R.norvegicus]

1096 2161 AI176592 General ESTs ESTs, Weakly similar to S63220 probable membrane protein YNL247w - yeast (Saccharomyces cerevisiae) 1097 12436 AI176610 General (S.cerevisiae]

I ,v, 1098 2536 AI176616 General ESTs 1099 18525 AI176792 a ESTs 1100 23449 A1176828 g ESTs 1101 23299 A1176839 General ESTs 1102 3580 A1176848 a ESTs 1103 22103 A1176849 d,General ESTs 1104 16036 AI176855 ESTs f ESTs, Highly similar to phosphomannomutase Sec53p 1105 15588 AI176916 General homolog [M.musculus]

1106 16917 AI176951 ESTs t Rattus norvegicus transcription factor 1107 16124 AI176963 cc MRG1 mRNA, complete cds 1108 15146 AI176969 b,General ESTs ESTs, Weakly similar to PSE-binding 1109 5786 AI177058 factor PTF delta f subunit H.sapiens 1110 2852 AI177059 c ESTs ESTs, Highly similar to AF139894 1 RNA-binding protein alpha-CP1 1112 3156 AI177092 g (M.musculus]

Rat adenine HMm:adenine phosphoribosyltransferase (APRT) 1113 14384 AI177096 a phos horibos ene, complete cds I transferase ESTs, Weakly similar to C10B RAT

SUBCOMPONENT, B
CHAIN

1114 13310 AI177119 General PRECURSOR [R.norvegicus]

ESTs, Highly similar to CGI-10 protein 1115 24049 AI177341 g,p,s,u H.sapiens 1116 15964 AI177360 o,General ESTs 1117 14989 AI177366 a Integrin, betaIntegrin, beta 1118 7975 AI177374 as ESTs TABLE MMARY ~~4~~~' ~tty. f7ocket No.
1: 44921-5U89W0 SU

Doe. No. 1798397.1 Sequence GenBank Model Acc/

ID No. dentifierRef. Seq~IDCode Gene Name UniggnVe, Cluste I . Tittle Rattus norvegicus substrate binding subunit of type II 5'-deiodinase D2p29 1119 3006 AI177395 k mRNA, com lete cds Rattus norvegicus mRNA for hnRNP

1120 17570 AI177683 r rotein, artial 1121 9521 AI177706 b ESTs 1122 14425 A1177755 g,General ESTs 1123 10611 A1177790 ,m ESTs j ESTs, Moderately similar to S27962 modulator recognition factor 1 1124 5356 AI177813 cc H.sapiens]

ESTs, Highly similar to SAS_HUMAN

SARCOMA AMPLIFIED
SEQUENC

1125 11791 AI177843 General( H.sapiens]

ESTs, Weakly similar to putative eps 1126 14484 AI177867 General protein [R.norvegicus]

ESTs, Weakly similar to DRAL

1127 5780 AI177869 General R.norvegicus ESTs, Highly similar to TGIF MOUSE

5'-TG-3' INTERACTING
FACTOR

1128 19184 AI178025 General[ M.musculus]

ESTs, Moderately similar to C17orf1 1129 6059 AI178245 c,General protein [H.sapiens]

ESTs, Weakly similar to hypothetical 1130 23248 AI178267 protein (H.sapiens]

ESTs, Weakly similar to YAE6_YEAST HYPOTHETICAL
13.4 1131 4073 A1178272 o I NTERGENIC REGION
S.cerevisiae 1132 7838 AI178291 a ESTs 1133 18996 A1178326 ESTs ESTs, Highly similar to 149523 Mouse primary response gene B94 mRNA, 1134 22488 AI178392 b 3'end - mouse M.musculus 1135 18800 AI178504 n,p,aa ESTs 1136 22197 AI178527 g,General ESTs ESTs, Highly similar to MCM3 MOUSE DNA REPLICATION

LICENSING FACTOR

1137 3401 AI178684 bb [ M.musculus]

1138 17713 AI178700 m ESTs 1139 14874 A1178735 a ESTs 1140 23567 A1178746 v,General ESTs Rattus norvegicus alpha-globin (GIoA) 1141 18907 AI178971 c gene, com lete cds 1142 20991 AI178979 ESTs i ESTs, Moderately similar to Vanin-1 1143 5887 AI179099 q,t M.musculus]

b,e, 1144 8477 A1179167 General ESTs 1145 3348 A1179288 u,v ESTs 1146 3608 AI179314 a ESTs 1147 8849 A1179315 g,p ESTs Rattus norvegicus mRNA for prostasin 1148 3611 AI179378 v,General recursor, complete 1 cds 1149 5438 AI179399 m,x ollagen t pe ollagen t pe V, 1 c V, alpha 2 alpha 2 c ESTs, Moderately similar to RB17 e,t, MOUSE RAS-RELATED
PROTEIN

1150 3614 AI179407 General RAB-17 [M.musculus 1151 5042 AI179422 b,General ESTs 1152 768 AI179481 ,General ESTs 2 i 1153 4041 AI179580 b,i ESTs TABLE MMARY A ~ty. Docke No.
1: 44921-5U89W0 SU

Doe. No. 1798397.1 Sequence GenBank Model Accl ID No. dentifierRef. Seq Code Gene Name Unige~ne, Cluster ,I ID Title R.norvegicus mRNA
for ras-related 1154 19822 AI179599 o,General GTPase Rab29 1155 23270 AI179601 ,General ESTs 1156 5901 A1179605 a ESTs 1157 16081 A1179610 g,i,pHeme ox genaseHeme ox genase 1158 14564 AI179717 k ESTs 1159 7918 A1179750 General ESTs 1160 6647 A1179795 g ESTs hypothetical protein 1161 9097 AI179875 o,GeneralLOC56728 hypothetical protein ESTs, Highly similar to GAP

PROTEIN

1162 23989 AI179953 a R.norvegicus]

1163 12899 AI179967 b ESTs 1164 1687 A1179971 c Hemoglobin, Hemoglobin, alpha alpha 1 1 1165 22569 AI179979 General ESTs ESTs, Highly similar to L-3-HHs:phosphoserinephosphoserine phosphatase 1166 23514 AI179986 o,Generalphosphatase H.sapiens]
[

1167 15892 AI179988 c,General ESTs ESTs, Highly similar to Unknown 1168 12402 AI180004 g H.sapiens ESTs, Moderately similar to testis 1169 5443 AI180165 General specific DNAj-homolog (M.musculus]

ESTs, Highly similar to A Chain A, The Crystal Structure Of Human Eukaryotic Release Factor Ert1-Mechanism Of Stop Codon Recognition And Peptidyl-Trna 1170 5481 AI180170 General H drolysis H.sapiens 1171 24028 AI180239 I ESTs ESTs, Moderately similar to JC4978 oxidative stress protein A170 -mouse 1172 17089 AI180281 [ M.musculus) ESTs, Moderately similar to Y273_HUMAN HYPOTHETICAL

1173 3701 AI180306 as PROTEIN KIAA0273 [H.sa lens) 1174 3352 AI180334 m ESTs ESTs, Highly similar to AF114169 1 nucleotide-binding protein short form 1175 24368 AI180392 I,m [ M.musculus]

ESTs, Moderately similar to SPA1 MOUSE GTPASE-ACTIVATING

1176 14337 AI180414 c PROTEIN SPA-1 M.musculus Rattus norvegicus chemokine CX3C

1177 19080 AI227647 j, mRNA, complete ,z cds 1178 22838 AI227667 as ESTs ESTs, Highly similar to T00367 hypothetical protein 1179 6765 AI227761 i,General H.sapiens ESTs, Weakly similar to AF187065 1 p75NTR-associated cell death 1180 24054 AI227867 General executor R.norve icus) 1181 7324 AI227885 i ESTs 1182 23898 A1227987 d ESTs PeptidylglycinePeptidylglycine alpha- alpha-amidating 1183 1651 AI228068 n,w amidating monooxmonoox genase genase 1184 14237 AI228128 a EST

ESTs, Weakly similar to C211_HUMAN PUTATIVE
PROTEIN

1185 14242 AI228197 General C210RF18 H.sa lens 1186 16913 AI228236 o ESTs ESTs, Highly similar to p97 1187 22915 AI228299 r homologous protein [H.sapiens) TABLE M CRY a'~ ,. ~ Attjy. Docket No.
1: f ,'~ 44911-5U89W0 SU

Doc. No. 1798397.1 Sequence GenBank Mo'del /~ce%

ID No. dentifierRef. Seq Code Gene Name Unige_~.ne Cluster I ID Title 1188 8917 AI228301 General ESTs 1189 15879 AI228313 r,General ESTs ESTs, Weakly similar to AFG1_YEAST AFG1 ' PROTEIN

1190 13727 AI228326 o,General [S.cerevisiae]

1191 6102 AI228335 General ESTs ESTs, Weakly similar to S70642 ubiquitin ligase Nedd4 - rat 1192 13730 AI228356 a R.norvegicus]

1193 13745 AI228494 b,cc EST

ESTs, Weakly similar to M172_HUMAN MEMBRANE

COMPONENT, CHROMOSOME
17, 1194 4217 AI228587 s SURFACE MARKER
2 [H.sa iens]

ESTs, Weakly similar to T16757 hypothetical protein 8144.3 -1195 16053 AI228596 cc Caenorhabditis elegans C.elegans]

1196 3557 AI228672 a ESTs 1197 11605 A1228682 a ESTs 1198 13203 A1228728 r ESTs ESTs, Highly similar to protein inhibitor of activated STAT protein 1199 13771 AI228848 g PIAS1 H.sapiens]

1200 5918 AI229036 r ESTs 1201 8235 A1229154 k ESTs Vesicle-associated membrane proteinVesicle-associated membrane protein 1202 16203 AI229196 r (s naptobrevin(synaptobrevin 2) 2 1203 13826 AI229304 a ESTs 1204 13144 A1229320 g ESTs 1205 4640 A1229404 x,aa ESTs ESTs, Moderately similar to MKK2 MOUSE MAP KINASE-ACTIVATED

2 [M.musculus]

ESTs, Moderately similar to NADH-ubiquinone oxidoreductase PDSW

1207 15426 AI229497 s subunit [H.sa lens]

1208 15193 AI229508 bb ESTs ESTs, Highly similar to KITH RAT

THYMIDINE KINASE, CYTOSOLIC

1209 19243 AI229638 x [R.norvegicus]

1210 23078 AI229647 p ESTs HHs:NADH dehydrogenase (ubiquinone) ESTs, Highly similar Fe-S protein to (30kD) (NADH-coenzymeNADH:ubiquinone Q oxidoreductase 1211 3099 AI229680 o reductase) NDUFS3 subunit [H.sapiens]

Sprague-Dawley D-beta-hydroxybutyrate dehydrogenase 1212 9508 AI229698 bb mRNA, com late 1 cds Rattus norvegicus mRNA for class I

1213 3977 AI229707 x beta-tubulin, complete 1 cds ESTs, Moderately similar to NADC_HUMAN NICOTINATE-NUCLEOTIDE

1214 23983 AI229708 v PYROPHOSPHORYLASE
H.sapiens]

1215 2688 AI229793 a ESTs ESTs, Weakly similar to KIAA0859 1216 3874 AI229832 g rotein [H.sapiens]

ESTs, Weakly similar to MOT2 RAT

MONOCARBOXYLATE

1217 2587 A1229979 General TRANSPORTER 2 R.norvegicus]

1218 20591 AI229993 I,m ESTs a,b,d, 1219 24042 A1230002 General ESTs Rattus norvegicus mRNA for voltage-1220 3880 AI230042 a gated ca channel, 1 complete cds T BLE MMAR ~~' '~, v ~ ' !' Att~y. Docket No.
g1: r' ~ 449 1-5U89W0 SU

Doe. No. 1798397.

~Sequenee GenBankA ,Model ;ID I,dentifierc1 v~ C,o~deGene Name Unig~e~e Cluster No: Ref. Seq~ID~a Title ,' j' ESTs, Highly similar to NIMM MOUSE

HMm:NADH dehydrogenaseNADH-UBIQUINONE

(ubiquinone) OXIDOREDUCTASE MWFE
1 alpha 1221 17672 AI230074 d subcomplex, SUBUNIT (M.musculus Rattus norvegicus hfb2 mRNA, 1222 3652 AI230113 General com lete cds ESTs, Weakly similar to HS9B RAT

HEAT SHOCK PROTEIN

1223 18650 AI230121 as BETA [R.norvegicus ESTs, Moderately similar to CHD3_HUMAN CHROMODOMAIN

HELICASE-DNA-BINDING
PROTEIN

1224 13025 AI230173 c 3 H.sapiens 1225 4280 AI230247 z seleno rotein selenoprotein P, P, lasma, plasma, 1 1226 18528 AI230284 General ESTs ESTs, Moderately similar to T46458 hypothetical protein DKFZp434M102.1 1227 7084 AI230362 p ( H.sa lens]

1228 20895 AI230549 b,n ESTs 1229 12961 AI230554 General ESTs Rattus norvegicus mRNA for galectin-1230 15636 AI230616 r 2 related protein, com lets cds 1231 4121 AI230647 ',m ESTs ESTs, Highly similar to HN1 1232 14388 AI230702 General M.musculus]

1233 18529 AI230716 x,General ESTs Rattus norvegicus phosphoinositide phosphatase SAC1 mRNA, complete 1234 13618 AI230724 General cds 1235 8304 AI230746 cc ESTs 1236 4731 A1230773 a ESTs ESTs, Moderately similar to CDN3_HUMAN CYCLIN-DEPENDENT KINASE

1237 14430 AI230798 c,k,x[ H.sa iens]

ESTs, Highly similar to AF102850 1 HHs:AlgS, S. dolichyl-phosphate cerevisiae, beta-1238 16627 AI230822 bb homolog of glucosyltransferase [H.sapiens Rattus norvegicus mRNA for brain 1239 3125 AI231028 General 4.1(S), complete cds 1240 633 AI231127 k ESTs ESTs, Highly similar to RL2B_HUMAN

1241 20846 AI231140 p [ R.nonregicus]

1242 6743 AI231219 d ESTs 1244 26292 A1231391 k 1245 12343 A1231433 w ESTs 1246 7337 A1231465 as ESTs 1247 16321 A1231506 General ESTs ESTs, Highly similar to Z183_HUMAN

ZINC FINGER PROTEIN

1248 8004 AI231532 ',I [ H.sa lens]

ESTs, Moderately similar to BAG-f amily molecular chaperone regulator-1249 15171 AI231792 3 H.sapiens 1250 6193 AI231797 i ESTs ESTs, Moderately similar to tumor 1252 14227 AI231999 a p rotein D53 [M.musculus Rattus norvegicus translation e longation factor 1-delta subunit 1253 24501 AI232006 w, mRNA, partial cds ,bb g,q,z,cc, 1254 3434 A1232014 General ESTs ESTs, Highly similar to Human T ranslation Initiation Factor Eifl, Nmr, 1255 9094 AI232021 n,General2 9 Structures H.sa 1 lens _87_ TABLE MMARY Atty. Doek'et No.
1: 44921-5U89W0 SU

Doe. No. 1798397.1 '~

5equence GenBank Model ~4cel 1D No. dentifierRef Seq Code Gene Name Unig~ne Cluster I I~ Tittle 1256 14020 AI232076 a ESTs 1257 6726 A1232157 d ESTs 1258 11549 A1232174 I,m ESTs 1259 23125 AI232266 j,s ESTs ESTs, Moderately similar to JC4914 anti-sigma cross-reacting protein 1260 2085 AI232270 bb homolog I beta precursor H.sapiens ESTs, Weakly similar to T25417 hypothetical protein T28D6.9 -1261 2913 AI232272 o Caenorhabditis elegans [C.elegans ESTs, Weakly similar to KIAA0971 1262 14304 AI232281 g protein H.sapiens u,bb, 1263 15955 AI232294 General ESTs ESTs, Weakly similar to Sid1669p 1264 15122 AI232303 y M.musculus purinergic purinergic receptor receptor P2X, P2X, ligand-gated 1265 4716 AI232313 l igand-gated ion channel 4 ion channel 1266 15246 AI232332 t,u ESTs 1267 24321 AI232340 o Stromal cell-derivedStromal cell-derived factor 1 factor 1 ESTs, Weakly similar to YQ42_CAEEL HYPOTHETICAL
40.0 KD PROTEIN C13B9.2 IN

1268 16172 AI232341 d CHROMOSOME III
[C.elegans]

1269 11411 AI232346 h ESTs Platelet-derivedPlatelet-derived growth growth factor receptor 1270 19287 AI232379 f actor receptoralpha f alpha ESTs, Weakly similar to FM01 RAT

DIMETHYLANILINE

1271 5601 AI232461 n,General MONOOXYGENASE [R.norvegicus]

ESTs, Weakly similar to PIR1 1272 14051 AI232489 I,m [H.sapiens]

ESTs, Moderately similar to A27340 1273 5572 AI232490 i,t complement C7 precursor [H.sapiens 1274 11157 AI232494 cc ESTs ESTs, Weakly similar to DnaJ

1275 8709 AI232534 o homolog 2 R.norvegicus]

1276 20350 AI232552 ',v, EST

1277 14069 AI232631 a ESTs 1278 4440 A1232643 w ESTs ESTs, Weakly similar to putative peroxisomal 2,4-dienoyl-CoA

1279 17695 AI232784 a reductase R.norvegicus 1280 15796 AI232874 v ESTs 1281 12467 AI232924 General ESTs 1282 12873 AI232984 i ESTs 1283 5355 A1233031 r ESTs ESTs, Moderately similar to MHC

1284 18794 AI233121 c class I [M.musculus]

b,g, ESTs, Weakly similar to nuclear RNA

1285 3823 AI233147 General helicase R.norvegicus c,k, 1286 11967 A1233155 General ESTs 1287 11561 AI233182 d ESTs ESTs, Highly similar to PM1 HUMAN

1288 3471 AI233183 PROTEIN PM [H.sa iens]

ESTs, Weakly similar to T15919 hypothetical protein EEED8.9 -1289 21948 AI233191 i Caenorhabditis elegans C.elegans 1290 13598 AI233194 ESTs ESTs, Highly similar to Bodenin 1291 15552 AI233195 [M.musculus Rattus norvegicus epidermal growth factor receptor related protein (Errp) 1292 17907 AI233224 bb mRNA, complete cds 1293 14111 AI233269 cc ESTs _8s_ TABLE MMARY f Attsy. Docket No.
1: 44931-5U89W0 SU

Doe. No. 1798397.

Sequence GenB~ank Model <\ccl ID No. dentifierRef. Seq Code Gene Narne Unig~ene Cluster I 7p Titte ESTs, Weakly similar to T24956 hypothetical protein T16G1.10 -1294 2894 AI233365 d Caenorhabditis 1 elegans C.elegans ESTs, Weakly similar to S44853 K12H4.3 protein - Caenorhabditis 1295 7161 AI233407 General elegans C.elegans]

1296 15906 AI233425 q ESTs 1297 4120 A1233433 d ESTs 1298 14095 A1233468 a,d ESTs ESTs, Weakly similar to 138079 OXA1 1299 3075 AI233494 u,aa homolog H.sapiens 1300 6046 AI233530 General ESTs PSD8_HUMAN 26S
PROTEASOME

REGULATORY SUBUNIT

1301 18900 AI233570 General [H.sa lens]

ESTs, Moderately similar to HHs:arginyl-tRNASYR_HUMAN ARGINYL-TRNA

1302 7888 AI233583 Generalsynthetase SYNTHETASE [H.sapiens 1303 16709 AI233602 GeneralAdenosin kinaseAdenosin kinase ESTs, Highly similar to P2CD_MOUSE PROTEIN

ISOFORM (PP2C-DELTA) (P53-INDUCED PROTEIN
PHOSPHATASE

1) (PROTEIN PHOSPHATASE

MAGNESIUM-DEPENDENT

1304 5163 AI233712 DELTA) M.musculus ESTs, Moderately similar to ERHUAH

coatomer complex alpha chain 1305 7243 AI233717 General homolog [H.sapiens]

ESTs, Highly similar to PSD5_HUMAN 26S
PROTEASOME

1306 3816 AI233729 g SUBUNIT S5B H.sapiens]

ESTs, Weakly similar to ALDR RAT

d,h, ALDOSE REDUCTASE

1307 13023 AI233740 General R.norvegicus 1308 14871 AI233743 g ESTs ESTs, Highly similar to Gene product with similarity to KIAA0154 1309 7469 AI233767 cc [H.sa lens]

1310 7804 AI233771 b ESTs ESTs, Weakly similar to T24413 hypothetical protein T04A11.2 -1311 13563 AI233773 a Caenorhabditis elegans C.elegans 1312 2154 AI233818 k,cc ESTs 1313 16616 AI234079 h ESTs a,d, 1314 13393 A1234100 Generalc steins rich c steins rich protein protein 1315 7071 AI234162 r ESTs 1316 14677 A1234620 General EST

ESTs, Weakly similar to transcription 1317 4443 AI234629 m factor C1 (M.musculus]

1318 22453 AI234678 b ESTs 1319 23964 A1234748 t,General ESTs 1320 9581 AI234753 f EST

1321 22152 A1234822 o,GeneralDEXRAS1 (DexraslDEXRAS1 (Dexras1) ESTs, Weakly similar to S12207 1322 8942 AI234865 d hypothetical rotein 1 [M.musculus ATPase, H+
transporting, l ysosomal (vacuolarATPase, H+ transporting, proton lysosomal 1323 22662 AI234939 as ump), subun (vacuolar proton um ), subunit ESTs, Highly similar to CB80_HUMAN

CAP BINDING

1324 3875 AI235047 o,General PROTEIN [H.sapiens]

1325 9479 AI235135 o EST

_89_ ThIB~LEMMARY Atty. Docket No.
1: 44921-5U89W0 SU

Doe. No. 1798397.1 6eyuenee GenBank Model Aeel ID No. dentifierRef. Sey Code Gene Name Unigene Cluster I IL) Title ESTs, Highly similar to ABF2_HUMAN

ATP-BINDING CASSETTE, SUB-FAMILY F, MEMBER
2 (IRON

INHIBITED ABC TRANSPORTER
2) 1326 14906 AI235192 g [H.sa lens]

1327 14718 AI235210 a ESTs Rattus norvegicus tissue inhibitor of metalloproteinase-1 (TIMP1), mRNA, 1328 15004 AI235224 b,General complete cds 1329 6632 AI235277 v ESTs ESTs, Weakly similar to single-pass 1330 14722 AI235284 ,z transmembrane protein x [R.norvegicus]

Rat mRNA for preprocathepsin D (EC

1331 1462 AI235585 u,General 3.4.23.5) 1332 21061 AI235631 ,m ESTs I

1333 14665 A1235646 m MAD homolog MAD homolog 4 (Drosophila) 4 (Drosophila) ESTs, Moderately similar to pescadillo 1334 19940 AI235689 General [H.sapiens]

1335 5698 AI235692 a ESTs ESTs, Highly similar to NID2 MOUSE

1336 23745 AI235732 k [M.musculus ESTs, Moderately similar to A56716 1337 11164 AI235739 General aromatic ester h drolase H.sapiens]

1338 5212 AI235745 d ESTs ESTs, Weakly similar to hypothetical 1339 14768 AI235912 h protein [H.sa ions]

1340 14776 AI235950 m ESTs 1341 3091 A1236027 n,General ESTs 1342 14861 AI236045 ESTs r 1343 14862 A1236048 a EST

ESTs, Highly similar to E25B protein 1344 16943 AI236097 p M.musculus ESTs, Highly similar to JC7107 development related unidentified 27K

1345 8336 AI236101 protein - mouse I M.musculus 1346 23230 AI236146 v ESTs ESTs, Highly similar to JC7301 Down syndrome critical region protein 1347 22855 AI236150 a alpha [H.sapiens 1348 14594 AI236152 ESTs i 1349 18406 A1236168 ESTs r ESTs, Highly similar to ATDA MOUSE

DIAMINE ACETYLTRANSFERASE

1350 15051 AI236332 General [M.musculus]

ESTs, Weakly similar to NHPX RAT

PROTEIN

1351 19298 AI236338 bb YEL026W HOMOLOG
[R.norvegicus siah binding protein 1; FBP interacting s iah binding repressor; pyrimidine protein 1; tract binding FBP

i nteracting splicing factor;
repressor; Ro ribonucleoprotein-1352 10667 AI236366 b p rimidine binding protein tr 1 1353 10774 AI236397 ESTs f 1354 9407 A1236402 as ESTs Rattus norvegicus retinol dehydrogenase type II mRNA, 1355 26335 AI236460 General complete cds 1356 17950 AI236590 ,General ESTs t 1357 18259 AI236601 h,v ESTs 1358 11445 AI236613 ESTs ESTs, Highly similar to SCF complex 1359 17248 AI236635 o,aa protein Sk 1 [M.musculus 1360 16859 AI236753 ,General ESTs t T/>BLE MM~4RY ~ ~ltty. l:)oeket 1: No. 44921-5U89W0 SU

Doe. No. 179-8897.1 6equenee GenBank MoeJel I ~~ ' Aeel 1l7 dentifierRef. Seq Code Gene Narne Unigene, Cluster No. IU Title I

ESTs, Weakly similar to hT41 1361 5208 AI236754 g [H.sapiens 1362 24388 AI236772 e,General ESTs ESTs,ESTs, Highly similar to HS9B

RAT HEAT SHOCK
PROTEIN HSP

1363 15850 AI236795 n,v,w 90-BETA [R.norvegicus]

1364 14800 AI236856 w ESTs 1366 11404 A1237002 m spermidine spermidine synthase s nthase ESTs, Highly similar to hepatitis B

1367 18151 AI237212 o,General virus X interacting protein [H.sapiens]

estrogen-responsive uterine 1368 21653 AI237535 ,Generalranscri t estrogen-responsive t t uterine transcript ESTs. Moderately similar to INIB
RAT

INTERFERON-INDUCIBLE
PROTEIN

1369 11208 AI237586 z [R.norvegicus ESTs, Moderately similar to Y101_HUMAN HYPOTHETICAL

1370 21893 AI237713 ,k,aa PROTEIN KIAA0101 i [H.sapiens]

1371 14842 AI237724 r ESTs ESTs, Moderately similar to MX11 RAT

MAX INTERACTING

1372 3467 AI237835 General [R.norvegicus 1373 25840 AI638972 a ESTs, Highly similar to G9A

1374 17108 AI639017 n M.musculus mini chromosome maintenance mini chromosome deficient maintenance 6 (S.

1375 16676 AI639082 c,k,xcerevisiae) deficient 6 (S.
cerevisiae) 1376 12400 AI639107 k ESTs 1377 19952 A1639108 q,v ESTs 1379 25907 AI639167 o,w ESTs ESTs, Highly similar to T46480 hypothetical protein 1381 18533 AI639231 n DKFZp434L1850.1 H.sa lens]

1382 18353 AI639233 ,aa decorin decorin t 1384 15330 AI639285 General ESTs 1385 20026 A1639354 g EST

r 1388 19152 A1639387 u,General ESTs ESTs, Moderately similar to CAOC

RAT CALSEQUESTRIN, CARDIAC

MUSCLEISOFORM PRECURSOR

1390 18338 A1639422 R.norvegicus]

EST, Highly similar to A42772 mdm2 1392 20082 AI639488 ,m protein - rat [R.norvegicus]
i ESTs, Weakly similar to T13607 a,bb, hypothetical protein EG:87B1.3 - fruit 1394 20056 AI639504 General fl [D.melanogaster ESTs, Highly similar to RPB8_HUMAN DNA-DIRECTED
RNA

POLYMERASES I, II, AND III 17.1 KD

1395 713 AI639518 q POLYPEPTIDE [H.sapiens protein phosphatase 1, r egulatory (inhibitor)protein phosphatase subunit 1, regulatory 1396 4332 AJ001044 bb 5 (inhibitor) subunit 1397 7602 AJ001929 k eticulocalbin reticulocalbin r Rattus norvegicus mRNA for 1398 9867 AJ005424 a BMK1/ERKS rotein, partial 1400 6351 AJ011811 Generallaudin 7 claudin 7 1 c g rowth differentiation factor 1401 20116 AJ011969 ,General5 growth differentiation ( 1 factor 15 Rattus norvegicus mRNA for 1402 7635 AJ223355 ,w mitochondrial dicarbox 1 v late carrier -91 _ TABLE UMMARY ],a ~ ' ~l i~ ~t'ty. Docket No.
1 iI ~ ~ 'l~ 44921-5U8 O
S

Doe. No. 1798397.1 # ~-.
vSequence GenBank Model Accl~~
, ID No. IdentifierRef. Seq~~IDGeodeGene Name ,,ynigene Cluster "~ ~..~ ~ Title U

Rat mRNA for delta3, delta2-enoyl-dodecenoyl-CoenzymeCoA isomerase,dodecenoyl-A

delta isomeraseCoenzyme A delta (3,2 traps- isomerase (3,2 1403 18686 D00729 q enoyl-Coen raps-enoyl-Coen me A t me A isomerase) dihydrolipoamide 1404 5049 D10655 n,w acet Itransferasedih drolipoamide acet Itransferase 1405 15281 D13623 h ESTs 1406 11434 D14014 Cc ESTs Rat mRNA for testicular dynamin, 1407 1613 D14076 x complete cds HHs:hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl Coenzyme A Rat mRNA for mitochondria) thiolase/enoyl-long-Coenzyme A chain 3-ketoacyl-CoA
hydratase thiolase beta-( trifunctional subunit of mitochondria) protein), trifunctional beta 1408 1728 D16479 q subunit protein, complete dds Rat mRNA for polyubiquitin (four repetitive ubiquitins in tandem), 1409 3015 D16554 c,s,v,z com late cds R.norvegicus mRNA
for chloride 1410 472 D26111 d,s,bb channel (putative) 2313b Rattus norvegicus mRNA for alphaB

1412 16233 D29960 j,) crystallin-related protein, complete cds ESTs, Highly similar to PRC6 RAT

PROTEASOME SUBUNIT

1413 9029 D30804 n [ R.norvegicus]

Rattus norvegicus tyrosine phosphatase-like protein IA-2a mRNA, 1414 1485 D38222 ,z partial cds ESTs, Highly similar to PRCE RAT

proteasome PROTEASOME EPSILON
beta type CHAIN

1415 9135 D45247 s subunit 5 PRECURSOR [R.norvegicus]

Rattus norvegicus mRNA for HHs:mercaptopyruvatemercaptopyruvate sulfurtransferase, 1416 16354 D50564 a sulfurtransferasecom lete cds Rattus norvegicus mRNA for proteasomal ATPase (Tat-binding 1417 1884 D50695 I,m,bb protein7), complete cds Solute carrierSolute carrier family 1 A1 family 1 A1 (brain 1418 21147 D63772 Generalbrain glutamateglutamate traps ( traps orter) orter) HHs:CDP-diacylglycerol--i nositol 3-phosphatidyltransferase ( phosphatidylinositolRat mRNA for phosphatidylinositol 1419 826 D82928 f nthase) s ynthase, complete s cds 1420 25306 D84485 a Rattus norvegicus mRNA for serine 1421 18867 D88250 t rotease, com lete cds r,v, 1423 22543 H31117 General 1424 12360 H31456 w ESTs 1425 20514 H31489 h,' ESTs ESTs, Highly similar to mtprd 1426 11358 H31610 h M.musculus ESTs, Moderately similar to T14781 bb, h ypothetical protein 1427 4360 H31813 General DKFZp586B1621.1 H.sa lens]

ESTs, Moderately similar to COF1 RAT COFILIN, NON-MUSCLE

1428 9343 H32169 I I SOFORM [R.norvegicus 1429 4386 H33093 h,w EST

1430 4415 H33636 h ESTs TABLE MMARY Atty. Doe et No.
1: 449 -5U89W0 SU

~oe. No. 1798397.

'Sequence GenBank EModel ~4ce/

ID No. dentifierRef. Seq Code Gene Name Unigene Cluster I I~ Tittle ESTs, Highly similar to IF39_HUMAN

EUKARYOTIC TRANSLATION

I NITIATION FACTOR

1431 15374 H34186 I [ H.sa lens]

1432 17159 00797 u,Generalalpha-tubulin al ha-tubulin J

Rat brain-specific identifier sequence 1433 16260 01878 f RNA, clone p1b224 J

Branched chain alpha-ketoacid dehydrogenaseBranched chain alpha-ketoacid 1434 17284 02827 bb subunit E1 deh drogenase subunit J alpha E1 alpha Rat glutathione S-transferase mRNA, 1435 15017 03752 n complete cds J

Thyroid hormone receptor, beta (avian Thyroid hormone erythroblasticreceptor, beta (avian l eukemia viral erythroblastic (v-erb-a) leukemia viral (v-erb-a) 1436 44 J 03819 ,s oncogene homologoncogene homolog 2) 2) e,r, Glutathione-S-transferase,Glutathione-S-transferase, mu type 2 1437 21014 03914 Generalmu t pe 2 (Yb2)Yb2 J ( Steroid-5-alpha-reductase, alpha polypeptideSteroid-5-alpha-reductase, 1 (3-oxo-5 alpha alpha-steroid polypeptide 1 (3-oxo-5 delta 4- alpha-steroid 1438 20429 05035 f deh drogenase delta 4-deh drogenase J al ha 1) alpha 1) GlutamylcysteineGlutamylcysteine gamma gamma synthetase 1439 1247 05181 j,l,m,s,s nthetase ight chain J ,z light chain l n,u, nositol 1,4,5-triphosphateRat inositol-1,4,5-triphosphate I

1440 10464 05510 Generaleceptor t a ece for mRNA, complete J r 1 r cds 1441 20149 K03243 q Rat peroxisomal enoyl-CoA:

hydrotase-3-hydroxyacyl-CoA

bifunctional enzyme mRNA, complete 1442 17758 K03249 q cds 1443 381 L00124 w Elastase 2, Elastase 2, ancreatic pancreatic 1444 2048 L00382 k,x Rattus norvegicus clone 15 polymeric i mmunoglobulin receptor mRNA, 1447 108 L14002 p 3'UTR microsatellite repeats 1448 25366 L14003 t Rattus norvegicus clone 15 polymeric i mmunoglobulin receptor mRNA, 1449 109 L14004 c, 3'UTR microsatellite repeats 1450 20414 L14323 GeneralPhospholipase Phospholipase C-betal C-beta1 2',3'- Cyclic 2',3'- Cyclic nucleotide nucleotide 3'-3'-1452 16119 L16532 k hosphodiesterasehos hodiesterase 1453 25377 L25387 h ESTs, Highly similar to A53047 6-1453 12058 L25387 h hosphofructokinase R.norvegicus Solute carrierSolute carrier family 1 A1 family 1 A1 (brain 1455 21146 L35558 Generalbrain glutamateglutamate transporter ( transporter) Rattus norvegicus guanylyl cyclase 1456 106 L37203 w ( GC-D) mRNA, com lete cds Rattus norvegicus serine protease 1458 13682 L38482 f,j,k,m,z gene, complete cds 1459 6405 L38615 p Glutathione Glutathione s nthetase s nthetase gene gene 1461 15189 M11794 n,v 1462 17086 M13011 Rat c-ras-H-1 gene, complete cds Rat insulin-like growth factor-I
mRNA, 1464 21053 M15481 0 3'end 1465 25405 M18330 j,1 1466 25415 M19648 a 1468 14967 M22366 w Propionyl Coenzyme A

carboxylase, alpha 1469 20481 M22631 bb of a tide TABLE MMARY Atty. Docket No.
1: 44921-5U89W0 SU

Doc. No. 1798397.1 Sequence GenBank Model Accl ID No. dentifierRef. Seq Code Gene Name Umigene Cluster I IU Title HHs:ubiquinol-cytochrome c reductase, Rat Rieske iron-sulfur Rieske iron-sulfurprotein mRNA, 1471 15048 M24542 pol peptide complete cds Rat cytochrome P-450 isozyme 5 1472 20921 M29853 m (P450 IVB2) mRNA, complete cds Cytochrome P450, an olfactory-specificCytochrome P450, steroid an olfactory-1473 1224 M31931 a h drox lase s ecific steroid hydrox lase Rat mitochondria) 3-hydroxy-3-methylglutaryl-CoA
synthase mRNA, 1474 15579 M33648 q complete cds Rat mitochondria) 3-hydroxy-3-methylglutaryl-CoA
synthase mRNA, 1474 15580 M33648 q complete cds ESTs, Weakly similar to KRAB-zinc 1475 17211 M34331 g,n, finger protein KZF-1 ,v [R.norvegicus]

1476 20699 M35601 b,x,bb Rat alpha-fibrinogen mRNA, 3' end 1476 20700 M35601 b,t,bb Rat al ha-fibrinogen mRNA, 3' end Rat mRNA for MHC
class II antigen RT1.B-1 beta-chain,Rattus norvegicus MHC class II antigen RT1.B beta 1477 9223 M36151 o chain mRNA, artial cds Rat general mitochondria) matrix processing protease (MPP) mRNA, 3' 1479 1585 M57728 ,m, end j 1480 24844 M58040 c ransferrin transferrin receptor t receptor 1481 25057 M58495 h 1482 457 M60666 d,GeneralTropomyosin Tropom osin 1 (al 1 (alpha) ha) Rat cystatin S (CysS) gene, complete 1483 1223 M75281 cds f P-glycoprotein/multidrug 1484 5733 M81855 ,k,aaesistance 1 P-gl coprotein/multidrug i r resistance 1 Rat beta-galactoside-alpha 2,6-1485 4198 M83143 m sial Itransferase mRNA

Rat beta-galactoside-alpha 2,6-1485 4199 M83143 m sialyltransferase mRNA

1486 24651 M83678 k,x,zRAB13 RAB13 Dopa decarboxylase ( aromatic L-aminoDopa decarboxylase acid (aromatic L-1487 1430 M84648 Generaldecarbox lase amino acid decarbox lase) 1488 25467 M93297 c ornithine aminotransferaseornithine aminotransferase Rattus norvegicus GABA transporter 1489 729 M95762 a, GAT-2 mRNA, complete cds Rattus norvegicus Acetyl-CoA acyltransferase, 3-oxo acyl-CoA thiolase A, peroxisomal Acetyl-CoA acyltransferase, (Acaa), mRNA. 3-oxo 1490 23698 NM 012489 length = 1619 ac I-CoA thiolase A, eroxisomal Rattus norvegicus Acetyl-CoA acyltransferase, 3-oxo acyl-CoA thiolase A, peroxisomal Acetyl-CoA acyltransferase, (Acaa), mRNA. 3-oxo 1490 23699 NM 012489q Length = 1619 ac I-CoA thiolase A, peroxisomal Rattus norvegicus Aldolase A, fructose-bisphosphate ( Aldoa), mRNA.
Length =

1491 7062 NM 012495q 442 Aldolase A, fructose-bisphos 1 hate Rattus norvegicus Aldehyde r eductase 1 (low Km aldose r eductase) (5.8 kb Pstl f ragment, probablyAldehyde reductase the 1 (low Km aldose f unctional gene)reductase) (5.8 (Akr1b1), kb Pstl fragment, 1492 5511 NM 012498a mRNA. Length robabl the functional 1 = 1339 gene) TABLE MM~AR
1: f l'~~at~~~ ~~~~ A~wtty.DocketNo~~921-5U89W0 SU ,~!~~~

,, " ,k" Doc__. No. 1798397.1 Sequence GenBank ~ ,H~~ m Acc/
~~, Model ID No. dentifierRef. Seq Gene Narne Unige~ne, Cluster , I IDS Code L Title Rattus norvegicus Benzodiazepin receptor ( peripheral) (Bzrp), mRNA.

1494 7427 NM 012515 Len th = 781 Benzodiazepin receptor General (peripheral) Rattus norvegicus Cholinergic receptor, muscarinic 3 (Chrm3), 1495 24433 NM 012527i mRNA. Length Cholinergic receptor, = 3578 muscarinic 3 Rattus norvegicus Creative kinase, brain (Ckb), mRNA.

1496 4467 NM 012529d Length = 1146 Creative kinase, brain Rattus norvegicus Ceruloplasmin (ferroxidase) 1497 16520 NM 012532GeneralCp), mRNA. Ceruloplasmin (ferroxidase) ( Length = 3700 Rattus norvegicus Angiotensin I-converting enzyme (Dipeptidyl carboxypeptidaseDipeptidyl carboxypeptidase 1) (Ace), 1 1498 225 NM 012544x,z mRNA. Length (Angiotensin I-converting = 4142 enz me) Rattus norvegicus Dopa decarboxylase (aromatic L-amino acid Dopa decarboxylase decarboxylase)(aromatic L-1499 1431 NM 012545GeneralDdc), mRNA. amino acid decarbox ( Length = 1954 lase) Rattus norvegicus Early I,m,v,growth response 1 (Egr1 ), 1500 23868 NM 012551GeneralmRNA. Length Earl growth res = 3112 onse 1 Rattus norvegicus Early I,v,cc,growth response 1 (Egr1 ), 1500 23872 NM 012551GeneralmRNA. Length Earl growth response = 3112 1 Rattus norvegicus Early growth response 1 (Egr1), 1500 23869 NM 012551v,GeneralmRNA. Length Early growth response = 3112 1 Rattus norvegicus Enolase 1 , alpha (Eno1), mRNA.

1501 19407 NM 012554z Length = 1725 Enolase 1, alpha Rattus norvegicus Enolase 1 , alpha (Eno1), mRNA.

1501 19408 NM 012554n,s, Length = 1725 Enolase 1, al ha ,z Rattus norvegicus Ets avian erythroblastosis virus E2 oncogene homologEts avian erythroblastosis 1 (tumor virus E2 p rogression oncogene homolog locus 1) (Ets1),1 (tumor 1502 21836 NM 012555k mRNA. Len th progression locus = 4991 1 ) Rattus norvegicus Fructose-1 ,6- biphosphatase (Fbp1 ), 1503 6895 NM 012558g,s mRNA. Length Fructose-1,6- bi 1 = 1357 hosphatase Rattus norvegicus Fibrinogen, gamma p olypeptide (Fgg), mRNA.

1504 25317 NM 012559bb Length = 1358 Rattus norvegicus Fibrinogen, gamma p olypeptide (Fgg), mRNA.

1504 6477 NM 012559b,bb Length = 1358 Fibrinogen, gamma pol a tide Rattus norvegicus Fibrinogen, gamma p olypeptide (Fgg), mRNA.

1504 478 NM 012559bb Length = 1358 Fibrino en, gamma 6 of peptide Rattus norvegicus Follistatin 1505 1731 NM 012561k Fst), mRNA. Follistatin 1 ( Length = 1035 Rattus norvegicus Group-s pecific component (vitamin D-binding protein)Group-specific component (Cc), (vitamin D-1507 254 NM 012564a mRNA. Len th bindin rotein 4 = 1676 TABLE MMARY Atty. Docket No.
1: 44931-5U89W0 SU

Doe. No. 798397.1 Sequence GenBank Model Accl IU No. dentifierRef. Seq Code Gene Name Unigene Cluster I 1~ Title Rattus norvegicus Histone H1-0 (HlfO), mRNA. Length 1508 16026 NM 012578r = 1779 Histone H1-0 Rattus norvegicus Histone H1-0 (HlfO), mRNA. Length 1508 16024 NM 012578r = 1779 Histone H1-0 Rattus norvegicus Histone H1-0 (HlfO), mRNA. Length 1508 16025 NM 012578r = 1779 Histone H1-0 Rattus norvegicus Heme oxygenase (Hmox1), mRNA.

1509 16080 NM 012580g,m Length = 870 Heme ox genase Rattus norvegicus Insulin-like growth factor-binding protein (IGF-BP3)Insulin-like growth (Igfbp3), factor-binding 1510 15098 NM 012588bb mRNA. Length rotein (IGF-BP3) = 2352 Rattus norvegicus Isovaleryl Coenzyme A Isovaleryl Coenzyme dehydrogenase A

1511 4450 NM 012592bb (Ivd), mRNA. deh drogenase Length = 2104 Rattus norvegicus Isovaleryl Coenzyme A Isovaleryl Coenzyme dehydrogenase A

1511 4451 NM 012592i,bb (Ivd), mRNA. deh drogenase Length = 2104 Rattus norvegicus Isovaleryl Coenzyme A Isovaleryl Coenzyme dehydrogenase A

1511 4452 NM 012592bb (Ivd), mRNA. deh drogenase Length = 2104 Rattus norvegicus Kallikrein 1, renal/pancreas/salivary 1512 17198 NM 012593a,x (KIk1), mRNA. Kallikrein 1, renal/pancreas/saliva Length = 786 Rattus norvegicus Kallikrein 1, renal/pancreaslsalivary 1512 17197 NM 012593x (KIk1), mRNA. Kallikrein 1, renal/pancreas/saliva Length =786 Rattus norvegicus Malic enzyme 1, soluble (Me1), 1513 18749 NM 012600a,h mRNA. Length Malic enz me 1, = 1761 soluble Rattus norvegicus Avian myelocytomatosis viral (v-myc) oncogene Avian myelocytomatosis homolog viral (v-myc) 1514 2628 NM 012603General(M c), mRNA. oncogene homolog Length = 2168 Rattus norvegicus Avian myelocytomatosis viral (v-myc) oncogene Avian myelocytomatosis homolog viral (v-myc) 1514 2629 NM 012603x,General(M c), mRNA. oncogene homolog Length = 2168 Rattus norvegicus Membrane metallo-endopeptidase (neutral endopeptidase/enkephalinasMembrane metallo-endopeptidase e) (Mme), mRNA.(neutral Length =

1515 16849 NM 012608n,o,q3243 endopeptidase/enke halinase) Rattus norvegicus serine (or cysteine) proteinase inhibitor, Glade E (nexin, plasminogen activator inhibitor type 1), member (Serpinel ), mRNA. Length =

1517 5540 NM 012620General3053 Plasminogen activator 1 inhibitor Rattus norvegicus Prolactin receptor (Prlr), mRNA.

1518 24568 NM 012630GeneralLength = 1635 Prolactin receptor Rattus norvegicus Prolactin receptor (Prlr), mRNA.

1518 24566 NM 012630GeneralLength = 1635 Prolactin rece for Ti4BLEa'i:MMAR,iY~ ~~~"'~~';;II~~ Att~y. DO ket NO.44921-5U8 SU ~' O

Doe. No. 1798897.

Wj,t ut Sequence GenBank Model Accl~.

ID No. dentifierRef. Seq Code Gene Name Unigene Cluster I ID Title Rattus norvegicus Prion protein, structural (Prnp), 1519 18553 NM 012631k mRNA. Length Prion protein, = 765 structural Rattus norvegicus protein t yrosine phosphatase, non-receptortype 1 (Ptpn1), 1520 1844 NM 012637GeneralmRNA. Length ESTs,Protein- rosine = 4127 phos hatase Rattus norvegicus Renin 1521 24668 NM 012642f Ren), mRNA. Renin ( Length = 1059 Rattus norvegicus RT1 class I b gene (RT1Aw2), mRNA.

1522 18632 NM 012645a Length = 1540 RT1 class Ib gene Rattus norvegicus Sodium channel, voltage-gated, type I I, alpha polypeptide ( Scn2a1 ), mRNA.
Length =

1523 25435 NM 012647g 8553 Rattus norvegicus Ryudocan/syndecan ( Sdc4), mRNA.
Length =

1524 9423 NM 012649b,cc 2462 R udocan/syndecan Rattus norvegicus Solute carrier family ( sodium/hydrogen exchanger 3), antiporterSolute carrier 3, Na+/H+ family 9 ( amiloride insensitive)(sodium/hydrogen exchanger 3), ( SIc9a3), mRNA.antiporter 3, Na+/H+
Length = (amiloride 1525 24496 NM 012654n 5153 insensitive) x,bb,Rattus norvegicusTestostrone-repressed Clusterin prostate 1526 7101 NM 012679GeneralClu), mRNA. message 2 ( Length = 1638 Rattus norvegicus Cytochrome ( Cyp2a2), mRNA.
Length =

1527 24707 NM 012693i 2259 C tochrome P450 Rattus norvegicus T-kininogen, see also DllEIh1 and DllMit8 (Kng), mRNA.

1528 850 NM 012696t Length = 1417 T-kininogen Rattus norvegicus T-kininogen, see also D11 EIh1 and D11 MitB K-kininogen, differential (Kng), mRNA. splicing leads 1528 854 NM 012696t Length = 1417 to HMW Kngk,T-kininogen Rattus norvegicus Organic c ation transporter (SIc22a1), 1529 603 NM 012697GeneralmRNA. Length Organic cation 1 = 1882 traps orter Rattus norvegicus Hexokinase 1 (Hk1 ), mRNA.

1530 372 NM 012734a Length = 3653 Hexokinase 1 Rattus norvegicus Pyruvate bb, arboxylase c (Pc), mRNA.

1531 478 NM 012744GeneralLength = 3945 P ruvate carbox 1 lase Rattus norvegicus Signal t ransducer and activator of t ranscription Signal transducer 3 (Stat3), and activator of 1532 343 NM 012747h,t mRNA. Length transcri tion 3 = 2924 Rattus norvegicus Nucleolin 1533 8829 NM 012749GeneralNcl), mRNA. Nucleolin ( Length = 2142 Rattus norvegicus a ntigen (Cd24), mRNA.

1534 0828 NM 012752GeneralLen th = 1703 CD24 antigen Rattus norvegicus a ntigen (Cd24), mRNA.

1534 0829 NM 012752i,GeneralLen th = 1703 CD24 anti en _97-TABLE MMARY Atty. Do ket No.
1: 44931-5089W0 SU

Doe. No. 179839 .

Sequence GenBank Model Acc!

ID No. dentifierRef. Seq Code Gene Narne Unige~nte Cluster . I I~ Tittle Rattus norvegicus antigen (Cd24), mRNA.

1534 20830 NM 012752,GeneralLength = 1703 CD24 antigen i Rattus norvegicus Insulin-l ike growth factor 2 receptor ( Igf2r), mRNA.
Length =

1535 5174 NM 012756b 8810 Insulin-like growth 1 factor 2 receptor Rattus norvegicus Lost on t ransformation , 1 (Lot1), 1536 21685 NM 012760,m,n mRNA. Length Lost on transformation j = 5028 1 Rattus norvegicus Interleukin 1beta converting enzyme ( Casp1), mRNA.
Length =

1537 8068 NM 012762 1209 Interleukin lbeta 1 t converting enz me Rattus norvegicus Guanylate cyclase, soluble, beta 2 ( GTP pyrophosphate - lyase) ( Gucylb2), mRNA.Guanylate cyclase, Length = soluble, beta 1538 246 NM 012770a,General2335 (GTP rophosphate 1 - I ase) Rattus norvegicus adrenergic receptor kinase, beta 1 (Adrbkl),G-protein-linked mRNA. receptor kinase (beta 1539 348 NM 012776 Length = 2683 adrenergic receptor 1 f kinase 1 ) Rattus norvegicus dual-specificity tyrosine-(Y)-phosphorylation regulated kinase 1a (Dyrkla),Dual Specificity mRNA. Yaki-related 1540 18135 NM 012791w Length = 2840 kinase,ESTs Rattus norvegicus Guanidinoacetate methyltransferase (Gamt), 1541 16947 NM 012793p,bb mRNA. Length Guanidinoacetate = 924 meth Itransferase Rattus norvegicus glutathione S-transferase, t heta 2 (Gstt2), mRNA.

1542 960 NM 012796a Length = 1258 glutathione S-transferase, theta 2 Rattus norvegicus MAL

protein gene (Mal), mRNA.

1543 260 NM 012798,u Len th = 2268 MAL rotein gene f ~

Rattus norvegicus Protein C

( Proc), mRNA.
Length =

1544 556 NM 012803d 1543 Protein C

Rattus norvegicus ATP-binding cassette, sub-family D (ALD), memberATP-binding cassette, 3 (Abcd3), sub-family D

1545 21729 NM 012804q mRNA. Length (ALD , member 3 = 3324 Rattus norvegicus alpha-methylacyl-CoA
racemase ( Amacr), mRNA.
Length =

1546 15032 NM 012816General1504 Meth lac I-CoA
racemase al ha Rattus norvegicus Insulin-l ike growth factor-binding protein 5 (IgfbpS),Insulin-like growth mRNA. factor-binding 1547 24895 NM 012817GeneralLen th = 1630 protein 5 Rattus norvegicus Annexin A3 (Anx3), ESTs, Weakly similar mRNA. Length to LURT3 =

1548 18109 NM 012823u,General1454 annexin III - rat [R.norvegicus Rattus norvegicus ATP-binding cassette, sub-family C (CFTR/MRP), member 2 h,l,q,Abcc2), mRNA. Canalicular multispecific ( Length = organic anion 1549 373 NM 012833General4918 transporter Rattus norvegicus Cystatin beta (Cstb), mRNA. Length =

1550 2855 NM 012838a 590 C statin beta -9s-TABLE MMARY Atty. Docket No.
1: 44921-5U89W0 SU

Uo ~. No. 1798397.1 Sequence GenBank Model III
Accl ~

ID Nor.dentifierRef. SeqmIDCode Gene Name Unigene Cluste I Title Rattus norvegicus Cytochrome C, expressed in somatic tissuesCytochrome C, expressed (Cycs), in somatic 1551 11136 NM 012839s mRNA. Length tissues = 318 Rattus norvegicus Epidermal growth factor (Egf), mRNA.

1552 20885 NM 012842a Length = 4801 Epidermal growth factor Rattus norvegicus Epidermal growth factor (Egf), mRNA.

1552 20884 NM 012842a,bb Length = 4801 E idermal growth factor Rattus norvegicus Lysosomal associated membrane protein 1 (120 kDa) (Lamp1), Lysosomal associated mRNA. membrane 1553 18770 NM 012857a Length = 2006 protein 1 (120 kDa) Rattus norvegicusESTs, Weakly similar 06- to S21348 methylguanine-DNAprobable pol polyprotein-related methyltranferaseprotein 4 - rat (Mgmt), [R.norvegicus],06-1554 20674 NM 012861 mRNA. Length meth (guanine-DNA
i = 812 methyltranferase Rattus norvegicus Matrix Gla a,r, protein (Mgp), mRNA.

1555 13151 NM 012862GeneralLength = 521 Matrix Gla protein Rattus norvegicus tumor necrosis factor receptor superfamily, member 11b (osteoprotegerin) (Tnfrsfllb), mRNA. Length =

1556 24617 NM 012870General2432 Osteoprotegerin Ribosomal protein (Rp139), mRNA.
Length =

1557 20945 NM 012875a,v 324 Ribosomal protein Rattus norvegicus Solute carrier family 2 A2 (gkucose transporter, Solute carrier type 2) (SIc2a2),family 2 A2 (gkucose 1558 15872 NM 012879o,r mRNA. Length transporter, t = 2573 a 2) Rattus norvegicus Superoxide dismutase (Sod3), mRNA.
Length =

1559 495 NM 012880 1729 Su eroxide dimutase z 3 Rattus norvegicus Superoxide dismutase (Sod3), mRNA.
Length =

1559 494 NM 012880c 1729 Su eroxide dimutase Rattus norvegicus Sialoprotein (osteopontin) d ,u, (Spp1), mRNA.
Length =

1560 23651 NM 012881General1457 Sialoprotein osteo ontin EST, Moderately similar to ACDV
RAT

Rattus norvegicusACYL-COA DEHYDROGENASE, Acyl-Coa dehydrogenase,VERY-LONG-CHAIN
Very long SPECIFIC, chain (Acadvl),MITOCHONDRIAL PRECURSOR
mRNA.

1562 19477 NM 012891 Length = 2117 R.norvegicus]
q Rattus norvegicus aminolevulinate,delta-,dehydratase Delta - aminolevulinic (Alad), mRNA. acid 1563 18564 NM 012899,GeneralLength = 1116 deh dratase v Rattus norvegicus Annexin 1 f ,r,cc,Gen(p35) (Lipocortin 1) (Anxa1), 1564 7197 NM 012904eral mRNA. Len th Annexin 1 (p35 = 1402 (Li ocortin 1 ) Rattus norvegicus Annexin 1 v ,cc, (p35) (Lipocortin 1) (Anxa1), 1564 7196 NM 012904GeneralmRNA. Length Annexin 1 (p35) = 1402 (Li ocortin 1) Rattus norvegicus Aquaporin 2 (Aqp2), mRNA.
Length =

1565 20202 NM 012909b,r 939 A ua orin 2 -ss-TABLE MMAR A ~tty. Docket 1: No. 44921-5U89W0 SU

Uoc. No. 179839 .1 i~~ ~ ~,, -Sequence GenBank Model Acel 'ID dentifierRef. Seq;!ID~Code Gene Name Unigene Cluster No. Title I

Rattus norvegicus Arrestin, beta 2 (Arrb2), mRNA.

1566 16581 NM 012911 c,j Length = 1758 Arrestin, beta Rattus norvegicus Arrestin, beta 2 (Arrb2), mRNA.

1566 16582 NM 012911 c Length = 1758 Arrestin, beta Rattus norvegicus Activating t ranscription factor 3 (Att3), 1567 24431 NM 012912 GeneralmRNA. Length Activating transcription = 1893 factor 3 Rattus norvegicus ATPase, Na+K+ transporting, beta polypeptide ATPase, Na+K+ transporting, 3 (Atp1b3), beta 1568 18118 NM 012913 p mRNA. Length pol eptide 3 = 1818 Rattus norvegicus ATPase i nhibitor (rat mitochondrial I F1 protein) ATPase inhibitor (Atpi), mRNA. (rat mitochondrial 1569 6108 NM 012915 n Length = 833 protein) Rattus norvegicus Cyclin G1 ( Ccng1 ), mRNA.
Length =

1570 20757 NM 012923 c,i,aa3169 Cyclin G1 Rattus norvegicus Cyclin G1 ( Ccng1 ), mRNA.
Length =

1570 20755 NM 012923 3169 C clin G1 i Rattus norvegicus antigen (Cd59), mRNA.

1571 2830 NM 012925 Length = 1523 CD59 antigen f Rattus norvegicus antigen (Cd59), mRNA.

1571 2831 NM 012925 Length = 1523 CD59 antigen f Rattus norvegicus Carnitine palmitoyltransferase ( Cpt2), mRNA.
Length =

1572 1977 NM 012930 q 2296 Carnitine palmito Itransferase 2 Rattus norvegicus v-crk-associated tyrosine kinase s ubstrate (Crkas),v-crk-associated mRNA. tyrosine kinase 1573 18694 NM 012931 ,I,m,zLength = 3335 substrate ' Rattus norvegicus Crystallin, a lpha polypeptide 2 (Cryab), 1574 3723 NM 012935 n mRNA. Length Crystallin, al 1 = 528 ha of eptide 2,ESTs Rattus norvegicus Cathepsin H (Ctsh), mRNA.
Length =

1575 9109 NM 012939 , 362 Cathepsin H
j ,z Rattus norvegicus Cathepsin H (Ctsh), mRNA.
Length =

1575 9398 NM 012939 as 362 EST

Rattus norvegicus Diphtheria t oxin receptor(heparin b inding epidermalDiphtheria toxin growth receptor (heparin f actor- like binding epidermal growth factor)growth factor-like 1576 23 NM 012945 b,cc Dtr), mRNA. growth factor) 2 ( Length = 1550 Rattus norvegicus Thrombin r eceptor (F2r), mRNA.

1577 5058 NM 012950 c Len th = 3418 Thrombin receptor 1 c Rattus norvegicus High mobility group 1 (Hmg1), 1579 9111 NM 012963 g mRNA. Length High mobilit grou 1 = 1225 1 Rattus norvegicus Hyaluronan mediated motility r eceptor (RHAMM)Hyaluronan mediated (Hmmr), motility receptor 1580 9374 NM 012964 mRNA. Length RHAMM) 1 x = 2049 ( Rattus norvegicus I ntercellular adhesion molecule 1 (Icam1), mRNA.

1581 554 NM 012967 Len th = 2602 ntercellular adhesion 2 t I molecule 1 TABLE MMA Atty. Docket No.
: SU 44921-5U89W0 _ Doe. No. 1798397.1 Sequence GenBank Model _ ~lcc/
~

ID No.'dentifierRef. Seq Code Gene Name Unigene Cluster I ID ~~ Title ~

Rattus norvegicus I ntercellular adhesion t,cc,molecule 1 (Icam1), mRNA.

1581 2555 NM 012967GeneralLength = 2602 Intercellular adhesion molecule 1 Rattus norvegicus Potassium ( K+) channel protein, slowly activating Potassium (K+) (Isk) (Kcne1),channel protein, 1582 24528 NM 012973c mRNA. Length slowly activating = 585 (Isk) Rattus norvegicus Lectin, galactose binding, soluble 5 ( Galectin-5) Lectin, galactose (LgalsS), binding, soluble mRNA. 9 1583 956 NM 012976c Length = 872 (Galectin-9) Rattus norvegicus Nucleoprotein 50kD (Nup50), 1584 16417 NM 012991g mRNA. Length Nuclear pore associated = 3027 rotein Rattus norvegicus Nucleoplasmin-related protein (Nuclear protein B23 ( Npm1), mRNA. Nucleoplasmin-related Length = protein 1585 17393 NM 012992d 1232 (Nuclear protein Rattus norvegicus Prosaposin (sulfated glycoprotein, sphingolipid hydrolase activator)Prosaposin (sulfated (Psap), glycoprotein, 1586 23544 NM 013013s mRNA. Length sphingolipid hydrolase = 2175 activator) Rattus norvegicus Syndecan 1 (Sdc1), mRNA.
Length =

1587 1588 NM 013026k 2410 S ndecan 1 Rattus norvegicus Selenoprotein W muscle 1 ( Sepw1 ), mRNA.
Length =

1588 17894 NM 013027m 664 Selenoprotein W
muscle 1 Rattus norvegicus Solute carrier family ( sodium/hydrogen exchanger), member 2 s,v, SIc34a1), mRNA.Rattus norvegicus ( Length = mRNA for NaPi-2 1589 18300 NM 013030General2440 al ha, complete cds Rattus norvegicus Solute carrier family ( sodium/hydrogen exchanger), Solute carrier member 2 family 17 ( SIc34a1 ), (sodium/hydrogen mRNA. Length exchanger), =

1589 18076 NM 013030g,s,z2440 member 2 Rattus norvegicus Solute carrier family ( sodium/hydrogenRattus norvegicus mRNA for NaPi-2 exchanger), alpha, complete member 2 cds,Solute carrier ( SIc34a1 ), family 17 (sodium/hydrogen mRNA. Length =

1589 18078 NM 013030s 2440 exchanger), member Rattus norvegicus Solute carrier family ( sodium/hydrogen exchanger), Solute carrier member 2 family 17 ( SIc34a1 ), (sodium/hydrogen mRNA. Length exchanger), =

1589 18077 NM 013030e,s,z2440 member 2 Rattus norvegicus ATP-binding cassette, sub-family C (CFTR/MRP), member.9 ( Abcc9), mRNA.
Length =

1591 730 NM 013040w 5000 Sulfon lures rece for 2 TABLE MM RY ~,~~fi "jl~~ A y. Do' cket No.44921-5U89W0 1: ,j=~
S~U

Doe. No. 798397.1 ~'1~'I~~~" ~,j ~ ~ 3 f Sequence GenBank~Accl~~Model~ ~ '~'A
~

ID N f Se C Gene Name Unigene Cluster ID de Title ~~~
R

o. I dentifierq. o , e Rattus norvegicus Transforming growth factor beta stimulated clone 22 i,o, Tgfb1i4), mRNA.Transforming growth ( Length = factor beta 1592 7401 NM 013043General1666 stimulated clone Rattus norvegicus Tyrosine 3 monooxygenase/tryptophan 5-monooxygenaseTyrosine 3-activation protein, eta monooxygenase/tryptophan polypeptide 5-( Ywhah), mRNA. monooxygenase activation Length = protein, 1593 6684 NM 013052General1689 eta pol eptide Rattus norvegicus Tyrosine 3 monooxygenase/tryptophan 5-monooxygenaseTyrosine 3-activation protein, thetamonooxygenase/tryptophan polypeptide 5-( Ywhaq), mRNA. monooxygenase activation Length = protein, 1594 4421 NM 013053a 2099 theta olypeptide Rattus norvegicus Inhibitor of DNA binding 3, dominant negative helix-loop-helix protein (1d3),Inhibitor of DNA
mRNA. Length binding 3, dominant 1595 15254 NM 013058k = 568 negative helix-loop-helix rotein Rattus norvegicus Tissue-nonspecific ALP alkaline phosphatase Tissue-nonspecific (Alpl), mRNA. ALP alkaline 1596 14997 NM 013059s,z Length = 2415 phosphatase Rattus norvegicus Tissue-nonspecific ALP alkaline phosphatase Tissue-nonspecific (Alpl), mRNA. ALP alkaline 1596 14996 NM 013059GeneralLength = 2415 phosphatase Rattus norvegicus antigen (invariant polpypeptide of major histocompatibility class II

antigen-associated) (Cd74), 1597 25676 NM 013069as mRNA. Length = 1150 Rattus norvegicus antigen (invariant polpypeptide of major histocompatibilityCD74 antigen (invariant class II polpypeptide antigen-associated)of major histocompatibility (Cd74), class II

1597 16924 NM 013069o mRNA. Length antigen-associated = 1150 Rattus norvegicus Utrophin (Utrn), mRNA.
Length =

1598 24748 NM 013070h,q 10,705 Utro hin Rattus norvegicus Ryudocan/syndecan (Sdc2), mRNA.
Length =

1599 1529 NM 013082d,General2153 R udocan/s ndecan Rattus norvegicus Tumor necrosis factor receptor superfamily, member 1a j,l,z,(Tnfr1 ), mRNA.
Length =

1600 1521 NM 013091General2130 Tumor necrosis factor rece for Rattus norvegicus Hemoglobin, alpha 1 (Hba1), 1601 1685 NM 013096c,aa mRNA. Length Hemoglobin, alpha = 556 1 Rattus norvegicus Hemoglobin, alpha 1 (Hba1), 1601 26150 NM 013096c,i mRNA. Length = 556 Rattus norvegicus Hemoglobin, alpha 1 (Hba1), 1601 1688 NM 013096 mRNA. Len th Hemoglobin, al ha = 556 1 -1 oz-TABLE MMARY ~'' ~ - Atty. Docket No.
1: = 44921-5089W0 SU

i11~

Doe. No. 1798897.1 p Sequence GenBa~nk Moelel Accl ' ID No. dentifierR,~,ef Code Gene Name Unigene Cluster I ~,S q Title ~I~

Rattus norvegicus Hemoglobin, alpha 1 (Hba1), 1601 689 NM 013096 c,p mRNA. Len th Hemoglobin, al 1 = 556 ha 1 Rattus norvegicus Hemoglobin, alpha 1 (Hbai), 1601 684 NM 013096 c,s,aamRNA. Length Hemoglobin, alpha 1 = 556 1 Rattus norvegicus Deoxyribonuclease I

( Dnasel), mRNA.
Length =

1602 20886 NM 013097 u,x,bb143 Deoxyribonuclease Rattus norvegicus Deoxyribonuclease I

( Dnasel), mRNA.
Length =

1602 20887 NM 013097 u,x,bb143 Deox ribonuclease Rattus norvegicus Glucose-6 phosphatase (G6pc), mRNA.

1603 321 NM 013098 c Length = 2237 Glucose-6-phosphatase Rattus norvegicus binding protein 1 (l2kD) ( Fkbpla), mRNA., Length =

1604 5296 NM 013102 I,m 554 FK506-binding protein 1 1 (l2kD) Rattus norvegicus ATPase Na+/K+ transporting beta 1 polypeptide ATPase Na+/K+transporting (Atplb1), beta 1 1606 23709 NM 013113 o,s,z,aamRNA. Length olypeptide = 2528 Rattus norvegicus ATPase Na+/K+ transporting beta 1 polypeptide ATPase Na+/K+transporting (Atp1b1), beta 1 1606 23711 NM 013113 mRNA. Length polype tide = 2528 Rattus norvegicus ATPase Na+/K+ transporting beta 1 polypeptide ATPase Na+/K+transporting (Atplbl), beta 1 1606 23710 NM 013113 s mRNA. Length 0l peptide = 2528 Rattus norvegicus Guanylate cyclase activator 2 (guanylin) ( Guca2a), mRNA.Guanylate cyclase Length = activator 2 1607 1976 NM 013118 a 567 ( guan lin) Rattus norvegicus MAD

( mothers against decapentaplegic,MAD (mothers against Drosophila) homolog 1 (Madh1),decapentaplegic, mRNA. Drosophila) homolog 1609 870 NM 013130 h Length = 2002 1 Rattus norvegicus Annexin V

( AnxS), mRNA.
Length =

1610 16650 NM 013132 u,General1417 Annexin V

Rattus norvegicus 3-hydroxy 3-methylglutaryl-Coenzyme A reductase 3-hydroxy-3-methylglutaryl-Coenzyme (Hmgcr), 1611 650 NM 013134 h mRNA. Length A reductase = 2664 Rattus norvegicus 3-hydroxy 3-methylglutaryl-Coenzyme A reductase 3-hydroxy-3-methylglutaryl-Coenzyme (Hmgcr), 1611 651 NM 013134 h,',1mRNA. Length A reductase = 2664 Rattus norvegicus Inositol 1, 4, 5-triphosphate receptor 3 ( Itpr3), mRNA.
Length =

1612 1712 NM 013138 General8806 I nositol 1, 4, 5-triphosphate receptor 3 Rattus norvegicus Insulin-l ike growth factor binding o,v, protein 1 (Igfbp1),nsulin-like growth mRNA. I factor binding 1613 16982 NM 013144 GeneralLength = 1500 rotein 1 TABLE MMA f>,tty. Docket 1: Y No. 44921-5089W0 SU

Doe. No. 798397.1 Sequence GenBank Model Accl IU No. dentifierRef. Seq Code Gene Name Unige~n~e Cluster I ID Title Rattus norvegicus CCAAT/enhancerbinding, protein (C/EBP) delta t,cc,(Cebpd), mRNA.CCAAT/enhancerbinding, Length = protein 1614 21683 NM 013154General1200 ( C/EBP delta Rattus norvegicus CCAAT/enhancerbinding, protein (C/EBP) delta (Cebpd), mRNA.CCAAT/enhancerbinding, Length = protein 1614 21682 NM 013154cc 1200 ( C/EBP delta Rattus norvegicus Cathepsin L (Ctsl), mRNA.
Length =

1615 3431 NM 013156b,g,n1386 Cathe sin L

Rattus norvegicus Cathepsin L (Ctsl), mRNA.
Length =

1615 25567 NM 013156v,General1386 Rattus norvegicus Cathepsin L (Ctsl), mRNA.
Length =

1615 3430 NM 013156General1386 Cathepsin L

Rattus norvegicus Insulin degrading enzyme (Ide), 1616 1309 NM 013159w mRNA. Length nsulin degrading = 4276 I enz me Rattus norvegicus Insulin degrading enzyme (Ide), 1616 1310 NM 013159w mRNA. Length nsulin degrading = 4276 I enzyme Rattus norvegicus Transforming growth factor, beta 3 (Tgfb3), mRNA.

1617 21723 NM 013174w Length = 2633 Transforming growth factor, beta 3 Rattus norvegicus Protein kinase, cAMP
dependent, regulatory, Protein kinase, type 1 (Prkar1a),cAMP dependent, 1618 1314 NM 013181m mRNA. Length e ulatory, a 1 = 1433 r Rattus norvegicus Meprin 1 p,bb,beta (Meplb), mRNA.

1619 17357 NM 013183GeneralLength = 2290 Meprin 1 beta Rattus norvegicus Phosphofructokinase, liver, B-type (Pfkl), mRNA. Length 1620 1300 NM 013190y = 2740 Phos hofructokinase, liver, B-t a Rattus norvegicus Aminolevulinate synthase 2, delta (Alas2), mRNA. Length 1621 16448 NM 013197c = 1899 Aminolevulinate s nthase 2, delta Rattus norvegicus Carnitine palmitoyltransferase 1 beta, muscle isoformCarnitine palmitoyltransferase (Cptlb), 1 beta, 1622 20856 NM 013200b mRNA. Len th muscle isoform = 2826 Rattus norvegicus brain cytosolic acyl Rattus norvegicusoenzyme A thioester acyl-CoA c hydrolase hydrolase (REACH),mRNA, complete mRNA. cds,acyl-CoA

1623 397 NM 013214f Length = 1523 drolase h Rattus norvegicus aflatoxin B1 aldehyde reductase (AFAR), mRNA.
Length =

1624 20864 NM 013215g,n, 1272 a flatoxin B1 aldeh de reductase Rattus norvegicus afadin (AF

1625 20728 NM 013217v 6), mRNA. Lengthfadin = 5957 a Rattus norvegicus augmenter of liver regeneration (ALR), mRNA.

1626 1396 NM 013222j Len th = 1226 ugmenter of liver a regeneration Rattus norvegicus ribosomal protein S26 (Rps26), mRNA.

1627 815 NM 013224w Length = 435 ibosomal rotein r S26 TI.IB~LEMM<1RY ~' AEty. Docket No.
1: 44921-5U89W0 SU

Doe. No. 1798397.1 Sequence. GenBank Model ~tcc~l~~~

tD No. dentifierRef. Seq ,CodeG~yne Name Unigene Cluster I tD ~ TitJ~,~le ' Rattus norvegicus ribosomal protein L32 (Rp132), mRNA.

1628 8305 NM 013226v Length = 465 Rattus norvegicus Acyl-Coenzyme A

dehydrogenase, C-4 to C-12 straight-chainAcyl-Coenzyme A
(Acadm), dehydrogenase, C-1629 21078 NM 016986d mRNA. Length to C-12 straight-chain = 1866 4 Rattus norvegicus Acid phosphatase 2, lysozymal (Acp2), mRNA.
Length =

1630 24649 NM 016988v 2009 Acid phosphatase 2, lysoz mal Rattus norvegicus adenylate cyclase activating polypeptide R.norvegicus (Sprague 1 (Adcyapl), Dawley) 1631 5239 NM 016989q,w mRNA. Length ibosomal protein 1 = 2681 r L15 mRNA

Rattus norvegicus Calcium-sensing receptor (hypocalciuric hypercalcemia 1, severe neonatalCalcium-sensing receptor hyperparathyroidism)hypocalciuric hypercalcemia (Casr), ( 1, 1632 45 NM 016996GeneralmRNA. Length severe neonatal = 4113 h pe arathyroidism) Rattus norvegicus Cytochrome P450, subfamily IVB, polypeptideCytochrome P450, 1 (Cyp4b1), subfamily IVB, 1633 20714 NM 016999t mRNA. Length pol peptide 1 = 2462 Rattus norvegicus Cytochrome P450, subfamily IVB, polypeptideCytochrome P450, 1 (Cyp4b1), subfamily IVB, 1633 20713 NM 016999t mRNA. Length pol pe tide 1 = 2462 Rattus norvegicus Cytochrome P450, subfamily IVB, polypeptideCytochrome P450, 1 (Cyp4b1), subfamily IVB, 1633 20711 NM 016999,t mRNA. Length 0l peptide 1 = 2462 Rattus norvegicus Cytochrome P450, subfamily IVB, polypeptideCytochrome P450, 1 (Cyp4b1), subfamily IVB, 1633 20715 NM 016999q,t mRNA. Length pol eptide 1 = 2462 Rattus norvegicus Diaphorase (NADH/NADPH) e,n,p,(Dia4), mRNA.
Length =

1634 1698 NM 017000General1396 Diaphorase (NADH/NADPH) Rattus norvegicus Glucose-6 phosphate dehydrogenase h,n, (G6pd), mRNA.
Length =

1635 1399 NM 017006General2324 Glucose-6-phosphate deh dro enase Rattus norvegicus Glutathione-S-transferase, alpha type Glutathione-S-transferase, (Yc?) (Gsta2),alpha type 1637 18989 NM 017013n mRNA. Length Yc?) = 830 Rattus norvegicus Glutathione-S-transferase, mu type 2 (Yb2)Glutathione-S-transferase, (Gstm2), mu type 2 1638 21013 NM 017014e,f mRNA. Length Yb2) = 1055 ( Rattus norvegicus Glutathione-S-transferase, mu type 2 (Yb2)Glutathione-S-transferase, (Gstm2), mu type 2 1638 21015 NM 017014e,GeneralmRNA. Len th Yb2 = 1055 ( TABLE MMARY ~tty. Docket No.
1: 44931-5U89W0 SU

Doe. No. 1798397.1 Sequence GenBank Model Accl ID No. l.dentifierRef. Seq Code Gene Name .nigene, Cl,~uster E I~ Title Rattus norvegicus Potassium inwardly-rectifying channel, subfamily J Potassium inwardly-rectifying (Kcnj1), mRNA.channel, 1639 11836 NM 017023 b Length = 2069 subfamily J

Rattus norvegicus Potassium inwardly-rectifying channel, subfamily J ESTs,Potassium (Kcnj1), mRNA.inwardly-rectifying 1639 5475 NM 017023 b Length = 2069 channel, subfamil J

Rattus norvegicus Potassium inwardly-rectifying channel, subfamily J
(Kcnj1 ), mRNA.

1639 25546 NM 017023 b,bb Length = 2069 Rattus norvegicus Lactate dehydrogenase A (Ldha), 1640 17807 NM 017025 i,GeneralmRNA. Length Lactate deh drogenase = 1609 A

Rattus norvegicus Protein phosphatase 2 (formerly 2A), catalytic subunit, beta isoform (Ppp2cb),Protein phosphatase mRNA. 2 (formerly 2A), 1641 24597 NM 017040 a Length = 1843 catalytic subunit, beta isoform Rattus norvegicus Solute carrier family 4, member 2, anion exchange protein 2 (SIc4a2), mRNA.Solute carrier Length = family 4, member 2, 1642 24696 NM 017048 f,j,z4057 anion exchange rotein 2 Rattus norvegicus Solute carrier family 4, member 3, anion exchange protein 3 (SIc4a3), mRNA.Solute carrier length = family 4, member 3, 1643 24695 NM 017049 a 3877 anion exchange protein 3 Rattus norvegicus Superoxide dismutase 1, soluble (Sod1), mRNA.

1644 20876 NM 017050 j,n,zLength = 650 Superoxide dimutase 1, soluble Rattus norvegicus Bcl2-associated X protein (Bax), 1645 910 NM 017059 f,l,mmRNA. Length Bcl2-associated = 579 X rotein Rattus norvegicus Bcl2-associated X protein (Bax), 1645 912 NM 017059 i mRNA. Length Bcl2-associated = 579 X rotein Rattus norvegicus Lysyl oxidase (Lox), mRNA.

164 1946 NM 017061 h Length = 4557 Lys I oxidase _ Rattus norvegicus Lysyl oxidase (Lox), mRNA.

1646 1942 NM 017061 t,GeneralLength = 4557 L s I oxidase Rattus norvegicus Lysyl oxidase (Lox), mRNA.

1646 1943 NM 017061 t Length = 4557 L s I oxidase Rattus norvegicus Pleiotrophin (Heparine binding factor, Hbnf, in the mouse) (Ptn), Pleiotrophin (Heparine mRNA. Length binding factor, 1647 6062 NM 017066 d = 1246 Hbnf, in the mouse) Rattus norvegicus Lysosomal-associated membrane protein (Lamp2), mRNA.Lysosomal-associated Length = membrane 1648 6654 NM 017068 w 1548 protein 2 Rattus norvegicus Glutamine synthetase (glutamate-ammonia ligase)Glutamine synthetase (Glut), (glutamate-1649 11153 NM 017073 s mRNA. Length ammonia Ii ase) = 2793 TABLE MMARY Atty. Docket No.
1: 44921-5089W0 SU

Doe. No. 1798397.1 ' _ ~u( , Sequence GenBank Model -Accl ;

ID No. dentifierRef. Seq ;Codeem_e Name U~ni'gee Cluster I ID ; ~ G Title Rattus norvegicus Tumor-associated glycoprotein pE4 ( Tage4), mRNA.
Length =

1650 923 NM 017076General2171 Tumor-associated g1 coprotein pE4 Rattus norvegicus antigen (Cd1d), mRNA.

1651 523 NM 017079s Length = 1835 CD1D antigen Rattus norvegicus Hydroxysteroid dehydrogenase, 11 beta type 1 (Hsd11b1), Hydroxysteroid mRNA. Length dehydrogenase, 1652 23660 NM 017080s = 1265 beta type 1 Rattus norvegicus Hydroxysteroid dehydrogenase, 11 beta type b,d, 2 (Hsd11b2), Hydroxysteroid mRNA. Length dehydrogenase, 16 275 NM 017081General= 1864 beta pe 2 _ Rattus norvegicus Urmodulin ( Tamm-Horsfall protein) ( Umod), mRNA.
Length =

1654 16211 NM 017082j,s,z2227 Urmodulin (Tamm-Horsfall protein) Rattus norvegicus Glycine methyltransferase (Gnmt), 1655 1552 NM 017084j mRNA. Length GI tine meth Itransferase = 988 Rattus norvegicus Glycine methyltransferase (Gnmt), 1655 1550 NM 017084y mRNA. Length GI tine methyltransferase = 988 Rattus norvegicus Small proteoglycan I (biglycan), bone (BSPG1) (bone/cartilageSmall proteoglycan proteclycan I (biglycan), 1 bone precursor) (BSPG1) (bone/cartilage (Bgn), mRNA. proteclycan 1656 22552 NM 017087a,k,xLength = 2446 1 precursor Rattus norvegicus guanylate cyclase 1, soluble, alpha (Gucy1a3), Guanylate cyclase, mRNA. Length soluble, alpha = 1 1657 8888 NM 017090m 4775 (GTP rophos hate - lyase) Rattus norvegicus Growth hormone receptor (Ghr), 1658 10887 NM 017094a,GeneralmRNA. Length Growth hormone = 2950 rece for Rattus norvegicus Peptidylprolyl isomerase A

(cyclophilin Peptidylprolyl A) (Ppia), isomerase A (cyclophilin mRNA.

1659 4393 NM 017101a, Length = 743 A) Rattus norvegicus solute carrier family (organic anion transporter) member 1 (SIc21a1), solute carrier mRNA. Length family (organic = anion 1660 24770 NM 017111d 2758 transporter member Rattus norvegicus granulin 1661 20745 NM 017113a (Grn), mRNA. granulin Length = 2113 Rattus norvegicus granulin 1661 20746 NM 017113a (Grn), mRNA. granulin Len th = 2113 Rattus norvegicus hippocalcin (Hpca), mRNA.

1662 1375 NM 017122w Length = 1561 hip ocalcin Rattus norvegicus antigen (Cd37), mRNA.

1663 12903 NM 017124k Length = 1158 CD37 anti en Rattus norvegicus laminin receptor 1 (Lamr1), mRNA.

1664 24885 NM 017138r Length = 1018 laminin receptor Rattus norvegicus laminin receptor 1 (Lamr1), mRNA.

1664 24886 NM 017138d, Len th = 1018 laminin rece for TABLE MMA ~'~r Atty. Docket No.
1: Y 44921-5U89W0 SU

Doe. No. 1798397.1 Sequence GenBank :Model Acc/

ID No. IdentifierRef. Seq Code Gene Name Unige~ne Cluster ID ~ Title Rattus norvegicus cofilin 1, non-muscle (Cfl1), mRNA.

1665 15363 NM 017147n,u Length = 1039 cofilin 1, non-muscle Rattus norvegicus cysteine rich protein 1 (Csrp1), 1666 13392 NM 017148u,GeneralmRNA. Length c steine rich rotein = 1403 Rattus norvegicus ribosomal protein L29 (Rp129), mRNA.

1667 5351 NM 017150q Length = 630 ibosomal protein r L29 Rattus norvegicus ribosomal protein S15 (RpslS), mRNA.

1668 16954 NM 017151a,n Length = 487 ibosomal protein r S15 Rattus norvegicus ribosomal protein 517 (Rpsl7), mRNA.

1669 21643 NM 017152g Length = 466 ibosomal protein r S17 Rattus norvegicus ribosomal protein S3a (Rps3a), mRNA.

1670 1694 NM 017153a,q Length = 880 ibosomal protein r S3a Rattus norvegicus ribosomal bb, protein S6 (Rps6), mRNA.

1671 17104 NM 017160GeneralLength = 801 ibosomal protein r S6 Rattus norvegicus ribosomal protein S6 (Rps6), mRNA.

1671 17106 NM 017160a Length = 801 ibosomal protein r S6 Rattus norvegicus ribosomal protein S6 (Rps6), mRNA.

1671 17107 NM 017160d,e Length = 801 ibosomal protein r S6 Rattus norvegicus glutathione peroxidase 1672 17686 NM 017165n, (Gpx4), mRNA. glutathione peroxidase Length = 872 4 Rattus norvegicus Leukemia-associatedcytosolic phosphoprotein stathmin (Lapl8), mRNA.Leukemia-associated Length = cytosolic 1673 20702 NM 017166c 1054 phos hoprotein stathmin Rattus norvegicus choline/ethanolamine kinase (Chetk), mRNA.
Length =

1674 3513 NM 017177r 1679 c holine/ethanolamine kinase Rattus norvegicus T-cell death associated gene (Tdag), mRNA.
Length =

1675 19031 NM 017180v,General1353 T-cell death associated gene Rattus norvegicus high mobility group box 2 (Hmgb2), mRNA.
Length =

1676 15437 NM 017187x,z 1072 hi h mobili grou protein 2 Rattus norvegicus high mobility group box 2 ( Hmgb2), mRNA.
Length =

1676 15433 NM 017187 1072 high mobili group protein 2 Rattus norvegicus high mobility group box 2 ( Hmgb2), mRNA.
Length =

1676 15434 NM 017187x,z 1072 h igh mobilit grou protein 2 Rattus norvegicus Myelin-associated glycoprotein ( Mag), mRNA.
Length =

1677 24437 NM 017190p 2474 M elfin-associated g1 coprotein Rattus norvegicus kynurenine aminotransferase I I (Kat2), mRNA.
Length =

1678 1542 NM 017193',I,m,z1828 k nurenine aminotransferase II

-(ABLE MMARY Attey. UOGket No.
1: 44931-5U89W~
SU

Doe. No. 1798397.1 Sequence GenBank Model Accl ~' ~i t~ No. dentifierRef. Seq ~ G Unigene Cluster I ID sC~odeene Name Tittle ,'' Rattus norvegicus cytochrome c oxidase, subunit IVa (Cox4a), mRNA.

1679 4695 NM 017202,s Length = 696 c tochrome c oxidase, 1 subunit IV

Rattus norvegicus cytochrome c oxidase, subunit IVa (Cox4a), mRNA.

1679 4694 NM 017202s,z Length = 696 c ochrome c oxidase, 1 subunit IV

Rattus norvegicus outer dense fiber of sperm tails ( Odf2), mRNA.
Length =

1680 428 NM 017213m 2451 outer dense fiber 1 of sperm tails Rattus norvegicus solute carrier family 3, member ( SIc3a1), mRNA.
Length =

1681 1622 NM 017216g,j,s,z2305 solute carrier famil 3, member Rattus norvegicus 6-pyruvoyl t etrahydropterin synthase 1682 13642 NM 017220v Pts), mRNA. ESTs ( Length = 1176 Rattus norvegicus 6-pyruvoyl t etrahydropterin synthase 1682 19976 NM 017220w Pts), mRNA. ESTs ( Length = 1176 Rattus norvegicus organic cationic transporter-like ( Orctl1 ), mRNA.
Length =

1683 1510 NM 017224General2227 organic cationic traps orter-like Rattus norvegicus dentatorubral pallidoluysian atrophy (Drpla), mRNA.

1684 1811 NM 017228j,l,m,zLength = 4387 dentatorubral pallidoluysian atroph Rattus norvegicus eukaryotic t ranslation elongation factor 2 (Eef2), mRNA.eukaryotic translation Length = elongation 1686 17563 NM 017245a,c,e,2626 f actor 2 Rattus norvegicus heterogeneous nuclear r ibonucleoprotein ( Hnrpa1), mRNA.heterogeneous nuclear Length =

1687 17502 NM 017248r 1696 r ibonucleoprotein Ai Rattus norvegicus heterogeneous nuclear r ibonucleoprotein ( Hnrpal), mRNA.heterogeneous nuclear Length =

1687 17501 NM 017248x 1696 r ibonucleoprotein Rattus norvegicus B-cell t ranslocation gene 1, anti-proliferative B-cell translocation (Btg1), mRNA. gene 1, anti-1688 19 NM 017258v,GeneralLength = 1464 proliferative Rattus norvegicus B-cell t ranslocation gene 2, anti-i,v,cc,proliferative B-cell translocation (Btg2), mRNA. gene 2, anti-1689 15300 NM 017259GeneralLength = 2519 roliferative Rattus norvegicus B-cell I,m,v,aa,cranslocation t gene 2, anti-c, proliferative B-cell translocation (Btg2), mRNA. gene 2, anti-1689 15301 NM 017259GeneralLength = 2519 proliferative Rattus norvegicus B-cell t ranslocation gene 2, anti-I,y,cc,proliferative B-cell translocation (Btg2), mRNA. gene 2, anti-1689 15299 NM 017259GeneralLength = 2519 proliferative Rattus norvegicus protease ( prosome, macropain) s ubunit, alpha protease (prosome, (Psme1), macropain) 28 1690 15224 NM 017264d mRNA. Length ubunit, al ha = 921 s TABLE MMARY fty. Docket No.
1: 44921-5U89W0 SU

~oe. No. 1798397.

~ l~
Sequence GenBank Model Reel t~ No elentifierRef. Seq Code Gene Narne ~Unigene Cluster ". IU . Title :I

Rattus norvegicus proteasome (prosome, macropain) subunit, alpha t ype 3 (Psma3),proteasome (prosome, mRNA. macropain) 1691 3987 NM 017280bb Len th = 897 subunit, alpha t pe 3 Rattus norvegicus proteasome (prosome, macropain) subunit, alpha t ype 4 (Psma4),proteasome (prosome, mRNA. macropain) 1692 1447 NM 017281I Length = 1121 subunit, al ha t pe 4 Rattus norvegicus proteasome (prosome, macropain) subunit, alpha t ype 6 (Psma6),proteasome (prosome, mRNA. macropain) 1693 15535 NM 017283s,bb Length = 932 subunit, alpha a 6 Rattus norvegicus ATPase, Ca++ transporting, cardiac muscle, slow twitch 2 ( Atp2a2), mRNA.ATPase, Ca++ transporting, Length = cardiac 1694 12349 NM 017290General5648 muscle, slow twitch Rattus norvegicus calcium channel, voltage-dependent, L type, alpha 1 D subunit ( Cacna1d), mRNA.calcium channel, Length = voltage-dependent, 1695 15819 NM 017298p 7986 L t pe, alpha 1 D subunit Rattus norvegicus solute carrier family ( sodium/hydrogen exchanger), solute carrier member 1 family 19 ( SIc19a1), mRNA.(sodium/hydrogen Length = exchanger), 1696 23825 NM 017299v 2402 member 1 Rattus norvegicus solute carrier family ( sodium/hydrogen exchanger), solute carrier member 1 family 19 ( SIc19a1 ), (sodium/hydrogen mRNA. Length exchanger), =

1696 23826 NM 017299v 2402 member 1 Rattus norvegicus glutamate cysteine ligaseGlutamate-cysteine , modifier ligase (gamma-subunit (Gclm),glutamylcysteine mRNA. synthetase), 1697 14003 NM 017305j,l,m,Length = 1382 re ulatory ,z Rattus norvegicus dodecenoyl-Coenzyme A

delta isomerase (3,2 trans-enoyl-Coenyme A

i somerase) (DCI), mRNA.

1698 26109 NM 017306q,s Length = 972 EST

Rattus norvegicus dodecenoyl-Coenzyme A

delta isomeraseRat mRNA for delta3, (3,2 traps- delta2-enoyl-enoyl-Coenyme CoA isomerase,dodecenoyl-A

i somerase) (DCI),Coenzyme A delta mRNA. isomerase (3,2 1698 18687 NM 017306q,t Length = 972 traps-eno I-Coenyme A isomerase) Rattus norvegicus ubiquitin C (Ubc), mRNA.
Length =

1699 18142 NM 017314g,s,aa2545 ubiquitin C

Rattus norvegicus cathepsin S (Ctss), mRNA.
Length =

1700 1894 NM 017320t 330 cathepsin S

Rattus norvegicus c almodulin (RCM3), mRNA.

1701 20809 NM 017326a Length = 1112 calmodulin Rattus norvegicus t ranscriptional repressor CREM (CREM), mRNA.

1702 355 NM 017334cc Len th = 436 TABLE UMMARY '' Att~y. Docket No.
1: 44921-5U89W0 S

Doe. No. 1798897.1 ~Sequenee GenBank Motiel ID No. Identifier~4ccl Code Gene Name Unfgene Cluster Ref. Seq~lU Title Rattus norvegicus acyl-coA

oxidase (RATACOAi), 1703 16148 NM 017340q,s mRNA. Length ac I-coA oxidase = 3741 Rattus norvegicus acyl-coA

oxidase (RATACOA1 ), 1703 16150 NM 017340a mRNA. Length ac I-coA oxidase = 3741 Rattus norvegicus myosin regulatory light chain r,u, (MRLCB), mRNA.Rat mRNA for myosin Length = regulatory light 1704 20849 NM 017343General1139 chain (RLC

Rattus norvegicus myosin regulatory light chain (MRLCB), mRNA.Rat mRNA for myosin Length = regulatory light 1704 20848 NM 017343b,General1139 chain (RLC) Rattus norvegicus urinary plasminogen activator receptor 2 urinary plasminogen (uPAR-2), activator receptor mRNA.

1705 606 NM 017350b Length = 1272 2 Rattus norvegicus PDZ and LIM domain 1 (elfin) (Pdliml), mRNA.
Length =

1706 1581 NM 017365General1392 LIM protein Rattus norvegicus Tropomyosin 1 (alpha) (Tpm1), mRNA.
Length =

1707 455 NM 019131x 1004 Tropomyosin 1 (alpha) Rattus norvegicus Tropomyosin 1 (alpha) (Tpm1), mRNA.
Length =

1707 456 NM 019131,z 1004 Tropom osin 1 (alpha) Rattus norvegicus Solute carrier family 12, member (bumetanide-sensitive sodium-[potassium]-chlorideSolute carrier family 12, member 1 cotransporter)(bumetanide-sensitive (SIc12a1), sodium-1708 4532 NM 019 b mRNA. Length [potassium -chloride 134 = 4595 cotransporter) _ Rattus norvegicusESTs, Moderately similar to synaptogyrin synaptogyrin 1 (Syngrl), 1709 1608 NM 019166j, mRNA. Length [R.norvegicus],s ,z = 879 na tog rin 1 Rattus norvegicus synuclein, alpha (Snca).
mRNA. Length 1710 7489 NM 019169c,General= 1018 s nuclein, al ha Rattus norvegicus carbonyl reductase (Cbr), mRNA.

1711 17066 NM 019170 Length = 1018 carbon I reductase Rattus norvegicusESTs, Highly similar carbonic to CARBONIC

anhydrase 4 ANHYDRASE IV PRECURSOR
(Ca4), mRNA.

171 23924 NM 019174bb length = 1205 [R.norvegicus]

_ Rattus norvegicus ADP-ribosylation-like 4 (Arl4), 1713 24019 NM 019186t mRNA. Length ADP-ribos lation-like = 1067 4 Rattus norvegicus integrin-associated protein (Cd47), 1714 22063 NM 019195d mRNA. Length integrin-associated = 1053 protein Rattus norvegicus amino-terminal enhancer of split 1715 2079 NM 019220j,k,z(Aes), mRNA. related to Droso Length = 1356 hila groucho ene Rattus norvegicus solute carrier family 12, member (SIc12a4), mRNA. Length =

1716 16284 NM 019229I,m 3726 solute carrier famil 12, member 4 Rattus norvegicus small inducible cytokine subfamily A20 (Scya20), mRNA.

1717 985 NM 019233b,cc Len th = 816 small inducible c tokine subfamil TABLE MMARY ~ltty. Doeke No.
1: 44921-5U89W0 SU

Uoe. No. 1798397.1 I,1'i Sequence GenBank Model ~4ccl I~ No. IdentifierRef. Seq Code Gene Narne U~,nige~ne Cluster - IU Title Rattus norvegicus p rocollagen C-proteinase e nhancer proteinprocollagen C-proteinase (Pcolce), enhancer 1718 15503 NM 019237k,x mRNA. Length protein = 1547 Rattus norvegicus p rocollagen C-proteinase e nhancer proteinprocollagen C-proteinase (Pcolce), enhancer 1718 15504 NM 019237k,x mRNA. Length rotein = 1547 Rattus norvegicus interferon-r elated developmental I ,v,cc,egulator 1 interferon-related r (Ifrd1), mRNA.developmental 1719 17908 NM 019242GeneralLength = 1736 regulator 1 Rattus norvegicus paired-like homeodomain transcription f actor 3 (Pitx3).paired-like homeodomain mRNA. transcription 1720 11218 NM 019247c Length = 1253 factor 3 Rattus norvegicus c omplement component 1, q s ubcomponent binding protein (C1qbp),complement component mRNA. 1, q 1721 15259 NM 019259d,f Length = 1124 subcomponent binding protein Rattus norvegicus c omplement component 1, q subcomponent, beta aa, polypeptide complement component (C1qb), mRNA. 1, q 1722 21443 NM 019262GeneralLength = 1136 subcomponent, beta of peptide Rattus norvegicus complement component 1, q subcomponent, beta polypeptide complement component (Clqb), mRNA. 1, q 1722 21444 NM 019262t,GeneralLength = 1136 subcomponent, beta pol eptide Rattus norvegicus sodium channel, voltage-gated, type VIII, alpha polypeptide ( Scn8a), mRNA. sodium channel, Length = voltage-gated, type 1723 117 NM 019266o,bb 6586 VIII, alpha pol eptide Rattus norvegicus gap j unction membrane channel protein alpha gap junction membrane 5 (GjaS), channel 1724 1145 NM 019280w mRNA. Length rotein alpha 5 = 3115 Rattus norvegicus Alcohol dehydrogenase Alcohol dehydrogenase 3 (Adh3), (class I), 1725 22220 NM 019286c mRNA. Length alpha pol eptide = 1131 Rattus norvegicus Actin-related protein complex 1b I,m,t,x,GeArpcib), mRNA.
( Length =

1726 10015 NM 019289neral1430 Actin-related rotein com lex 1b Rattus norvegicus Actin-related protein complex 1b bb, (Arpc1b), mRNA.
Length =

1726 10016 NM 019289General1430 Actin-related rotein complex 1b Rattus norvegicus Cell division cycle control protein 2 (Cdc2a), mRNA. Length =

1727 21651 NM 019296c,f,x1184 Cell division c cle control rotein Rattus norvegicus Complement receptor related protein (Cr1), mRNA. Length 1728 20751 NM 019301s = 1811 Com lement rece for related rotein Rattus norvegicus solute carrier family 12, member (SIc12a3), mRNA. Length =

1729 645 NM 019345bb 4361 solute carrier famil 12, member 3 TABLE MMARY Atty. Docket No.
1: 44921-5U89W0 SU

_ _ Doe. No. 1798397.1 Sequence _ Model J
~GenBank Reel ID No. IdentifierRef. Seq Code Gene Name Unige"n'e~ Cluster ID _ Title Rattus norvegicus Serine/threonine kinase 2 (Stk2), mRNA. Rat liver stearyl-CoA
Length = desaturase 1730 1301 NM 019349 c 4194 mRNA, com lete cds Rattus norvegicus Uncoupling protein 2, mitochondria) (Ucp2), mRNA.

1731 3776 NM 019354 a,u Length = 1575 Uncoupling protein 2, mitochondria) Rattus norvegicus eukaryotic t ranslation initiation factor 2, subunit 1 (alphaeukaryotic translation ) (Eif2s1), initiation factor 1732 4592 NM 019356 GeneralmRNA. Length 2, subunit 1 (alpha = 1377 ) Rattus norvegicus factor-responsive smooth muscle protein (SM-20),factor-responsive mRNA. smooth muscle 1733 1324 NM 019371 w Length = 2825 rotein Rattus norvegicus protein beta-subtype ( Ywhab), mRNA. ESTs, Moderately Length = similar to S12207 1734 19577 NM 019377 a 2756 hypothetical protein M.musculus]

Rattus norvegicus Testis enhanced gene transcript 1735 24626 NM 019381 s Tegt), mRNA. Testis enhanced Length = 940 gene transcri t Rattus norvegicus espin ( Espn), mRNA.
Length =

1736 744 NM 019622 p 2786 espin Rattus norvegicus cytochrome ( Cyp4f1), mRNA.
Length =

1737 20716 NM 019623 c 1977 c tochrome P450 Rattus norvegicus beta-galactoside-binding lectin ( Lgalsl), mRNA.
Length =

1738 20709 NM 019904 x 519 beta-galactoside-binding lectin Rattus norvegicus clone BB.1.4.1 unknown Glu-Pro dipeptide repeat Rattus norvegicusprotein mRNA, complete calpactin cds,calpactin I

heavy chain I heavy chain,hydroxyacid (Anxa2), mRNA.oxidase 3 1739 574 NM 019905 u,GeneralLength = 1395 medium-chain) Rattus norvegicus hypothetical protein LOC56728 (LOC56728), 1740 9096 NM 019908 j mRNA. Length hypothetical protein = 858 LOC56728 Rattus norvegicus parathyroid hormone r eceptor (LOC56813), 1741 20457 NM 020073 i,GeneralmRNA. Length parath roid hormone = 2065 receptor Rattus norvegicus parathyroid hormone r eceptor (LOC56813), 1741 20458 NM 020073 GeneralmRNA. Length arathyroid hormone = 2065 rece for Rattus norvegicus parathyroid hormone r eceptor (LOC56813), 1741 20460 NM 020073 GeneralmRNA. Length parath roid hormone = 2065 rece for Rattus norvegicus eukaryotic i nitiation factor 5 (eIF-5) 1742 18713 NM 020075 r EifS , mRNA. euka otic initiation ( Length = 3504 factor 5 (eIF-5) Rattus norvegicus eukaryotic i nitiation factor 5 (eIF-5) 1742 18715 NM 020075 r EifS , mRNA. euka otic initiation Length = 3504 factor 5 (eIF-5 T~4BLE MMARY ''~-' Atty. Docket No.
1: 44921-5U891N0 SU

Doc. N_o ~1t7~9839t7~1.

Sequence GenBari'k:Model _ Acel JD No. IdentifierRef. Seq,Code Gene Name Unigeme Cluster ID Title Rattus norvegicus hydroxyanthranilate 3,4-dioxygenase 3-hydroxyanthranilate (Haao), mRNA. 3,4-1743 20493 NM 020076p Length = 1254 diox genase Rattus norvegicus kidney-specific membrane protein (NX-17), mRNA.
Length =

1744 16375 NM 020976g 1181 kidney-specific membrane protein Rattus norvegicus thymosin, beta 10 (Tmsb10), mRNA.

1745 20816 NM 021261k,GeneralLength = 539 th mosin beta-10 Rattus norvegicus ribosomal protein L35a (Rp135), mRNA.

1746 15335 NM 021264a Length = 348 ribosomal rotein L35a Rattus norvegicus transforming growth factor beta-1 gene transforming growth (Tgfb1 ), factor beta-1 mRNA.

1747 18729 NM 021578k,z Length = 1585 gene Rattus norvegicus transforming growth factor-beta (TGF-beta) masking protein large transforming growth subunit (Ltbp1),factor-beta (TGF-1748 19060 NM 021587cc mRNA. Length beta) masking protein = 6244 large subunit Rattus norvegicus kynurenine 3-hydroxylase (Kmo), mRNA.
Length =

1749 17324 NM 021593o,General1733 k nurenine 3-h droxylase Rattus norvegicus Thyroxine deiodinase, type I (Dio1), 1750 19679 NM 021653GeneralmRNA. Length Th roxine deiodinase, = 2106 pe I

Rattus norvegicus Thyroxine a,v, deiodinase, type I (Dio1), 1750 19678 NM 021653GeneralmRNA. Length Thyroxine deiodinase, = 2106 type I

Rattus norvegicus putative potassium channel TWIK

(Kcnk1), mRNA.
Length =

1751 19665 NM 021688u,General1582 putative potassium channel TWIK

Rattus norvegicus cAMP-regulated guanine nucleotide exchange factor I (cAMP-GEFI) (Epac), cAMP-regulated mRNA. guanine nucleotide 1752 19667 NM 021690m Length = 3373 exchange factor I cAMP-GEFI) Rattus norvegicus prothymosin alpha (Ptma), 1754 22916 NM 021740a mRNA. Length roth mosin al ha = 1182 Rattus norvegicus antigen (Cdl4), mRNA.

1755 19710 NM 021744t Length = 1591 CD14 anti en Rattus norvegicus antigen (Cd14), mRNA.

1755 19711 NM 021744t Length = 1591 CD14 anti en Rattus norvegicus farnesoid X activated receptor (LOC60351), mRNA. Length 1756 19712 NM 021745r = 2070 farnesoid X activated rece for Rattus norvegicus cysteine-sulfinate decarboxylase (Csad), mRNA. Rattus norvegicus Length = cca2 mRNA, 1757 1962 NM 021750j,k, 2413 com lete cds ,z Rattus norvegicus cysteine-sulfinate decarboxylase (Csad), mRNA.
Length =

1757 9824 NM 021750a,bb 2413 c steine-sulfinate 1 decarbox lase Rattus norvegicus Nopp140 associated protein (Nap65), 1758 25198 NM 021754h mRNA. Length No 140 associated = 1980 rotein TABLE UMMARY ~~ ~~i''n'' Att~y. Docket No.
1: 44931-SU89W0 S

q, Dec. No. 1798397.1 i I
~

Sequence GenBank Model Accl~

SID IdentifierRef. Seq Code Gene Name U-nige~ne Cluster No. I~ , Title " n Rattus norvegicus Nopp140 b,n,s,v,associated protein (Nap65), 1758 20035 NM 021754GeneralmRNA. Length No 140 associated = 1980 protein Rattus norvegicus pleiotropic regulator 1 (PIrg1), mRNA.

1759 20090 NM 021757m Length = 1545 leiotropic regulator Rattus norvegicus beta prime COP (Copb), mRNA.

1760 17885 NM 021765as Length = 3025 beta rime COP

Rattus norvegicus jun a cc, proto-oncogene (Junb), 1762 20161 NM 021836GeneralmRNA. Length 'un B proto-oncogene = 1035 Rattus norvegicus cytoplasmic linker 2 (Cyln2), 1764 1203 NM 021997k,z mRNA. Length cytoplasmic linker = 4847 2 Rattus norvegicus FXYD

domain-containing ion t ransport regulatorFXYD domain-containing 6 (Fxyd6), ion transport 1765 23151 NM 022005b mRNA. Length regulator 6 = 1711 Rattus norvegicus Hexokinase 3 (Hk3), mRNA.

1767 17101 NM 022179bb Length = 3692 Hexokinase 3 Rattus norvegicus Hexokinase 3 (Hk3), mRNA.

1767 17100 NM 022179bb Length = 3692 Hexokinase 3 Rattus norvegicus Hepatic nuclear factor 4(alpha t ranscription factor 4) w, Hnf4a), mRNA. Hepatic nuclear ( Length = factor 4 (alpha 1768 20257 NM 022180General1446 transcription factor 4) Rattus norvegicus Hepatic nuclear factor 4(alpha t ranscription factor 4) ( Hnf4a), mRNA. Hepatic nuclear Length = factor 4 (alpha 1768 25699 NM 022180i 1446 transcription factor 4) Rattus norvegicus Hepatic nuclear factor 4(alpha t ranscription factor 4) ( Hnf4a), mRNA.
Length =

1768 10860 NM 022180 1446 ESTs Rattus norvegicus t opoisomerase (DNA) II

alpha (Top2a), mRNA.

1769 23780 NM 022183k,x Length = 6052 topoisomerase (DNA) II al ha Rattus norvegicus r esiniferatoxin-binding, phosphotriesterase-related protein (Rpr1),resiniferatoxin-binding, mRNA.

1770 20312 NM 022224o Len th = 1050 phos hotriesterase-related protein Rattus norvegicus c onnective tissue growth f actor (Ctgf), mRNA. Length 1771 6585 NM 022266d,p,cc= 2345 connective tissue growth factor Rattus norvegicus alpha-i,v,cc,ubulin (Tuba1), t mRNA.

1772 17161 NM 022298GeneralLen th = 1617 al ha-tubulin Rattus norvegicus alpha-t ubulin (Tuba1), mRNA.

1772 17162 NM 022298a Length = 1617 alpha-tubulin Rattus norvegicus alpha-t ubulin (Tuba1), mRNA.

1772 17160 NM 022298a Length = 1617 al ha-tubulin Rattus norvegicus alpha-t ubulin (Tuba1), mRNA.

1772 17158 NM 022298 Len th = 1617 al ha-tubulin TA'B'LEMMARY Atty. Docket No.
1: 44921-5089W0 SU

Uoc. No. 1798897.1 _ __ GenBank Model Sequence sec/

ID No. dentifierRef. Seq Code Gene Name Unige"~ne Cluster I ID 'Title Rattus norvegicus Proliferating cell nuclear i,aa,antigen (Pcna), mRNA.

1773 1454 NM 022381GeneralLen th = 1160 Proliferating cell 1 nuclear anti en Rattus norvegicus Proliferating cell nuclear antigen (Pcna), mRNA.

1773 1455 NM 022381(,GeneralLength = 1160 Proliferating cell 1 nuclear antigen Rattus norvegicus quinoid dihydropteridine reductase ( Odpr), mRNA.
Length =

1774 3480 NM 022390s 1307 quinoid dih dropteridine 1 reductase Rattus norvegicus pituitary t umor-transforming 1 (Pttg1), 1775 5184 NM 022391z mRNA. Length ituita tumor transforming 1 = 974 gene Rattus norvegicus growth response protein (CL-6) ( LOC64194), mRNA. Length 1776 22413 NM 022392h = 2410 growth response protein (CL-6) Rattus norvegicus growth response protein (CL-6) ( LOC64194), mRNA. Length 1776 22414 NM 022392n = 2410 growth res onse protein (CL-6) Rattus norvegicus macrophage galactose N-acetyl-galactosamine specific lectin (Mgl), mRNA.

1777 22499 NM 022393t Length = 1358 Gal/GaINAc-specific lectin Rattus norvegicus calreticulin (Calr), mRNA.

1779 24537 NM 022399a Length = 1882 calreticulin Rattus norvegicus calreticulin (Calr), mRNA.

1779 24539 NM 022399y Length = 1882 calreticulin Rattus norvegicus plectin ( PIec1), mRNA.
Length =

1780 141 NM 022401o,General15,231 plectin Rattus norvegicus acidic ribosomal protein PO (Arbp), 1781 069 NM 022402g mRNA. Length acidic ribosomal 1 = 1046 protein PO

Rattus nonregicus ferritin l ight chain 1 (Ftl1), mRNA.

1782 8211 NM 022500j,n,sLength = 552 ferritin light chain 1 Rattus norvegicus ferritin l ight chain 1 (Ftl1), mRNA.

1782 8212 NM 022500n,s Length = 552 ferritin light chain 1 Rattus norvegicus cytochrome c oxidase subunit Vlla 3 (Cox7a3), 1783 6815 NM 022503s mRNA. Length c tochrome c oxidase = 460 subunit Vlla 3 Rattus norvegicus ribosomal protein L36 (Rp136), mRNA.

1784 4259 NM 022504q,w Len th = 364 ribosomal rotein Rattus norvegicus survival motor neuron (Smn), mRNA.

1785 611 NM 022509j Length = 1243 survival motor 1 neuron Rattus norvegicus short chain acyl-coenzyme A

dehydrogenase short chain acyl-coenzyme (Acads), A

1786 2236 NM 022512,z mRNA. Len th deh drogenase = 1749 Rattus norvegicus ribosomal protein L27 (Rp127), mRNA.

1787 3026 NM 022514a Len th = 463 ribosomal rotein TABLE MMARY Atty. Docket No.
1: 44931-5U89W0 SU

Doe. 0. 1798397.1 ~Sequenee GenBank _ Aeel Model ID No. dentifierRef. Seq Code Gene Name Unige~ne Cluster I ID Title Rattus norvegicus ribosomal protein L27 (Rp127), mRNA.

1787 3027 NM 022514a,q,r,aaLength = 463 ribosomal protein Rattus norvegicus ribosomal protein L24 (Rp124), mRNA.

1788 2696 NM 022515a,d Length = 541 ribosomal protein Rattus norvegicus ribosomal protein L24 (Rp124), mRNA.

1788 2697 NM 022515n,w,aaLength = 541 ribosomal protein Rattus norvegicus polypyrimidine tract binding protein (Ptb), mRNA. Length 1789 3900 NM 022516h = 2697 polypyrimidine tract binding protein Rattus norvegicus ADP-r ibosylation factor 1 (Arf1 ), 1790 4151 NM 022518o mRNA. Length ADP-ribosylation = 900 factor 1 Rattus norvegicus ornithine aminotransferase (Oat), 1791 4242 NM 022521c mRNA. Length ornithine aminotransferase = 1938 Rattus norvegicus platelet endothelial tetraspan antigen 3 (Cd151), platelet endothelial mRNA. Length tetraspan antigen-=

Rattus norvegicus plasmolipin (Z49858), 1793 6641 NM 022533GeneralmRNA. Length lasmolipin = 1475 Rattus norvegicus cyclophilin B (Ppib), mRNA.
Length =

1794 8097 NM 022536a 840 c clophilin B

Rattus norvegicus phosphatidate phosphohydrolase type 2 ( Ppap2), mRNA. phosphatidate phosphohydrolase Length = type 1795 8597 NM 022538c,r,u871 2 Rattus norvegicus phosphatidate phosphohydrolase type 2 ( Ppap2), mRNA. phosphatidate phosphohydrolase Length = type 1795 8598 NM 022538a 871 2 Rattus norvegicus small zinc f inger-like protein DDP2 1796 9296 NM 0225410 Dd 2), mRNA. small zinc finger-like ( Length = 494 protein DDP2 Rattus norvegicus ornithine decarboxylase antizyme i nhibitor (Oazi),ornithine decarboxylase mRNA. antizyme 1797 21063 NM 022585h Len th = 4269 inhibitor Rattus norvegicus t elomerase protein component 1 (TIp1), mRNA.

1799 20781 NM 022591z Length = 8216 telomerase rotein component 1 Rattus norvegicus t ransketolase (Tkt), mRNA.

1800 20803 NM 022592n Length = 2098 transketolase Rattus norvegicus enoyl hydratase-like protein, peroxisomal enoyl hydratase-like (Ech1), mRNA. protein, 1801 20925 NM 022594q Length = 1097 peroxisomal Rattus norvegicus cathepsin B (Ctsb), mRNA.
Length =

1802 20944 NM 022597as 1904 cathe sin B

Rattus norvegicus synaptojanin 2 binding protein (Synj2bp), mRNA.

1803 21024 NM 022599o,GeneralLen th = 5215 outer membrane rotein TABLE UMMARY Atty. Docket No.
1: 44921-5U89W0 S

Doe. No. 1798397.1 ~$equenee GenB~ank Model Eleel ID No. [IdentifierRef. Seq Code Gene Name Unigene Cluster :' I~ Title Rattus norvegicus Testis-specific histoneESTs, Highly similar 2b (Th2b), to 0506206A

1804 2250 NM 022643GeneralmRNA. Length histone H2B [R.norvegicus = 470 Rattus norvegicus ribosomal protein S14 (Rps14), mRNA.

1805 17567 NM 022672a, Len th = 492 ibosomal protein r S14 Rattus norvegicus histone family, member Z

( H2afz), mRNA.
Length =

1806 17661 NM 022674bb 811 H2A histone famil , member Z

Rattus norvegicus protein phosphatase 1, regulatory ( inhibitor) subunit 1A

( Ppplria), mRNA.protein phosphatase Length = 1, regulatory 1807 24563 NM 022676b 619 ( inhibitor) subunit Rattus norvegicus protein phosphatase 1, regulatory ( inhibitor) subunit 1A

( Ppp1rla), mRNA.protein phosphatase Length = 1, regulatory 1807 24564 NM 022676b,x 619 inhibitor) subunit Rattus norvegicus germinal histone H4 gene (Hist4), 1808 20506 NM 022686 mRNA. Length germinal histone I = 377 H4 gene Rattus norvegicus preoptic r egulatory factor-1 (Porf1 ), 1809 20508 NM 022688g mRNA. Length preo tic regulato = 689 factor-1 Rattus norvegicus p105 c oactivator (U83883), 1810 17586 NM 022694k mRNA. Length p105 coactivator = 3166 Rattus norvegicus ribosomal protein L28 (Rp128), mRNA.

1811 17730 NM 022697a Length = 466 ibosomal protein r L28 Rattus norvegicus ribosomal protein L28 (Rp128), mRNA.

1811 17729 NM 022697q Length = 466 ibosomal protein r L28 Rattus norvegicus crp-ductin ( Crpd), mRNA.
Length =

1812 154 NM 022849 4344 crp-ductin t Rattus norvegicus casein kinase 1 gamma 3 isoform ( Csnklg3), mRNA.
Length =

1813 127 NM 022855h 2547 casein kinase 1 gamma 3 isoform Rattus norvegicus HNF-3/forkhead homolog-1 ( Hfh1), mRNA.
Length =

1814 152 NM 0228581 760 HNF-3/forkhead j homolog-1 Rattus norvegicus t ricarboxylate carrier-like protein (Loc65042), mRNA.

1816 18101 NM 022948z Length = 2699 ricarbox late carrier-like t rotein Rattus norvegicus t ricarboxylate carrier-like protein (Loc65042), mRNA.

1816 18103 NM 022948a Length = 2699 ricarbox late carrier-like t rotein Rattus norvegicus putative protein phosphatase n uclear targeting subunit ( Ppp1r10), mRNA.putative protein Length = phosphatase 1 1817 21491 NM 022951w 131 nuclear targeting 4 subunit Rattus norvegicus p hosphatidylinositol 3-kinase ( Pik3c3), mRNA.
Length =

1818 15742 NM 0229582 752 hos hatid linositol3-kinase TABLE MMARY ~~ I!~' ~'' ~ ~ ~~I' Atty.'ti'ocl 1: ~~,~~ et No. 44921 5U8 SU O

D oe. No. 1798397.1 ~ ~~~

Sequence GenBank Model Accl ID No. dentifierRef. Seq Code Gene Narne Unigene Cluster I ID ~.~, T~,'~file Rattus norvegicus tRNA

selenocysteine associated protein (Secp43),tRNA selenocysteine mRNA. associated 1819 9286 NM 023027t,w Length = 864 protein Rattus norvegicus casein kinase 1 gamma 2 isoform ( Csnk1g2), mRNA.
Length =

1820 23215 NM 023102z 1572 casein kinase 1 gamma 2 isoform Rattus norvegicus Liver activating protein (LAP,also NF-IL6, nuclear factor-IL6, previously Liver activating designated protein (LAP, TCFS) also NF

cc, Cebpb), mRNA. IL6, nuclear factor-IL6, ( Length = previously 1821 21238 NM 024125General1408 designated TCFS) Rattus norvegicus Liver activating protein (LAP,also NF-IL6, nuclear factor-IL6, previously Liver activating designated protein (LAP, TCFS) also NF

cc, Cebpb), mRNA. IL6, nuclear factor-IL6, ( Length = previously 1821 21239 NM 024125General1408 designated TCF5) Rattus norvegicus DNA-damage-inducible transcript i,n, 1 (Gadd45a), mRNA. Length 1822 353 NM 024127General= 711 DNA-damage-inducible transcript 1 Rattus norvegicus DNA-damage-inducible transcript i,n, 1 (Gadd45a), mRNA. Length 1822 354 NM 024127General= 711 DNA-damage-inducible transcript 1 Rattus norvegicus DNA-damage-inducible transcript 1 (Gadd45a), mRNA. Length 1822 352 NM 024127h,General= 711 DNA-damage-inducible transcript 1 Rattus norvegicus D-dopachrome tautomerase 1823 17227 NM 024131x Ddt), mRNA. D-do achrome tautomerase ( Length = 628 Rattus norvegicus DNA-damage inducible transcript 3 (Ddit3), mRNA. Length =

1824 1598 NM 024134I 806 DNA-damage inducible transcript 3 Rattus norvegicus adrenodoxin reductase ( Fdxr), mRNA.
Length =

1825 1162 NM 024153d 1786 adrenodoxin reductase Rattus norvegicus annexin VI (Anxa6), Rattus norvegicus mRNA. Length mRNA for H(+)-=

1826 7863 NM 024156c 2739 transporting ATPase, complete cds Rattus norvegicus complement factor I (Cfi), 1827 22079 NM 024157x mRNA. Length complement factor = 2021 I

Rattus norvegicus heart fatty acid binding protein (Fabp3), 1828 16476 NM 024162GeneralmRNA. Length heart fatt acid = 666 binding protein Rattus norvegicus heat shock 70kD
protein 8 ( HspaB), mRNA.
Length =

1829 17765 NM 024351b,s.v2073 Heat shock cognate protein 70 Rattus norvegicus hairy and enhancer of split 1, ( Drosophila) hairy and enhancer (Hes1 ), mRNA.of split 1, 1830 8879 NM 024360h Len th = 1453 Droso hila TABLE MMARY Atty. Docket Ne.
1: 44921-SU89W0 SU

Doe. N.'o~1~9839~7~1 5equenee~ _ Model_ 1 GenBank e' Reel IL) dentifierRef. Seq Code Gene Narne Unigealn~e Cluster No. I~ ., Title I

Rattus norvegicus heterogeneous nuclear ribonucleoproteins methyltransferase-likeheterogeneous nuclear 2 (S.

cerevisiae) ribonucleoproteins (Hrmt112), methyltransferase-1831 20772 NM 024363x mRNA. Length ike 2 (S. cerevisiae) = 1201 l Rattus norvegicus 3-hydroxy 3-methylglutaryl CoA lyase ( Hmgcl), mRNA.
Length =

1832 2812 NM 024386c 1390 3-hydrox -3-methylglutaryl CoA I ase Rattus norvegicus heme oxygenase-2 non-reducing i soform (Hmox2),hems oxygenase-2 mRNA. non-reducing 1833 335 NM 024387, Length = 1815 soform j i Rattus norvegicus immediate early gene transcription f actor NGFI-B mmediate early (Nr4a1), i gene transcription 1834 21 NM 024388cc mRNA. Length actor NGFI-B
= 2488 f Rattus norvegicus immediate early gene transcription f actor NGFI-B mmediate early (Nr4a1), i gene transcription 1834 22 NM 024388cc mRNA. Length actor NGFI-B
= 2488 f Rattus norvegicus peroxisomal multifunctional enzyme type peroxisomal multifunctional II (Hsd17b4), enzyme 1836 9929 NM 024392 mRNA. Length a II
f = 2535 t Rattus norvegicus ATP-binding cassette, sub-family A (ABC1 ), member 2 ( Abca2), mRNA. ATP-binding cassette, Length = sub-family A

1837 3582 NM 024396as 8040 ( ABC1), member2 Rattus norvegicus mitochondrial aconitase ( nuclear aco2 mitochondrial aconitase gene) (Aco2), (nuclear aco2 1838 19993 NM 024398e,p,s,aamRNA. Length gene) = 2744 Rattus norvegicus aspartoacylase (Aspa), 1839 10789 NM 024399o mRNA. Length aspartoac lass = 1552 Rattus norvegicus a d isintegrin and metalloproteinase with t hrombospondin a disintegrin and motifs 1 metalloproteinase cc, ADAMTS-1 ) with thrombospondin ( (Adamts1 ), motifs 1 1840 22626 NM 024400GeneralmRNA. Length ADAMTS-1 ) = 4878 Rattus norvegicus activating t ranscription factor ATF-4 1841 13633 NM 024403,GeneralAtt4), mRNA. activating transcription ( Length = 1173 factor ATF-4 Rattus norvegicus activating t ranscription factor ATF-4 1841 13634 NM 024403g,GeneralAtt4), mRNA. activating transcri ( Length = 1173 tion factor ATF-4 Rattus norvegicus RNA

binding protein p45AUF1 ( Hnrpd), mRNA.
Length =

1842 23387 NM 024404b,General240 RNA binding protein Rattus norvegicus a minolevulinic acid synthase 1 (Alas1), mRNA.
Length =

1843 21038 NM 024484h 052 a minolevulinic acid 2 s nthase 1 Rattus norvegicus Glutathione peroxidase ( Gpx1), mRNA.
Length =

1844 853 NM 0308261 539 ESTs.Glutathione 1 s eroxidase 1 TABLE MMA ' Atty. Docket No.
1: Y 44921-5U89W0 SU

Doe. No. 1798397.1 ~

'Se GenBank Model uence Accl ID No. dentifierRef. Seq Code Gene Name ~~Un~igene Cluster I If) v Title ~-~' Rattus norvegicus glycoprotein 330 (Lrp2), 1845 15111 NM 030827e,GeneralmRNA. Length g1 coprotein 330 = 15,438 Rattus norvegicus glycoprotein 330 (Lrp2), 1845 15112 NM 030827,z mRNA. Length g1 coprotein 330 = 15,438 Rattus norvegicus glycoprotein 330 (Lrp2), 1845 15110 NM 030827GeneralmRNA. Length glycoprotein 330 = 15,438 Rattus norvegicus kidney specific organic anion transporter kidney specific (SIc21a4), organic anion 1846 808 NM 030837k,m mRNA. Length traps orter = 2772 Rattus norvegicus islet cell autoantigen 1, 69 kDa (Ica1), 1847 4057 NM 030844k mRNA. Length islet cell autoantigen = 2094 1, 69 kDa Rattus norvegicus gro 1848 1221 NM 030845t (Gro1 ), mRNA.gro Length = 929 Rattus norvegicus epithelial membrane protein 3 (Emp3), 1849 21509 NM 030847x mRNA. Length epithelial membrane = 737 protein 3 Rattus norvegicus pyruvate dehydrogenase kinase 2 subunit p45 pyruvate dehydrogenase (PDK2) (Pdk2),kinase 2 1850 1928 NM 030872v mRNA. Length subunit p45 (PDK2) = 2207 Rattus norvegicus profilin II

(Pfn2), mRNA.
Length =

1851 17342 NM 030873a 1966 profilin II

Rattus norvegicus Angiotensin II receptor, type 1 (AT1A) (Agtrla), mRNA.

1852 24648 NM 030985a Length = 1450 Angiotensin II
receptor, type 1 (AT1A) Rattus norvegicus Angiotensin II receptor, type 1 (AT1A) (Agtr1a), mRNA.

1852 25453 NM 030985GeneralLength = 1450 Rattus norvegicus Guanine nucleotide-binding protein beta 1 (Gnb1),Guanine nucleotide-binding mRNA. protein 1853 21802 NM 030987h Length = 2837 beta 1 Rattus norvegicus aldo-keto reductase family 1, member A1 (aldehyde reductase) (Akrlal), mRNA.aldo-keto reductase Length = family 1, member 1854 23109 NM 031000f,s,z1124 A1 (aldeh de reductase Rattus norvegicus aminobutyrate aminotransferase (Abat), 1855 134 NM 031003a,u mRNA. Length 4-aminobu rate = 1726 aminotransferase Rattus norvegicus angiotensin II type-1 receptor (Agtr1 ), mRNA.

1856 25461 NM 031009o Length = 2156 angiotensin II
t pe-1 rece for Rattus norvegicus arachidonate lipoxygenase (Aloxl2), 1857 1845 NM 031010t mRNA. Length arachidonate 12-lipoxygenase = 2048 Rattus norvegicus arachidonate lipoxygenase (Aloxl2), 1857 25517 NM 031010c,t mRNA. Length arachidonate 12-lipoxygenase = 2048 Rattus norvegicus p38 mitogen activated protein kinase (Mapkl4), mRNA.

1858 16562 NM 031020f Len th = 3132 38 mitogen activated rotein kinase TABLE MM R ~ ' '~,~ " ~'i Atty!~' Docket No.
1 ' '~ ~ 4T4'921-5U89W0 SU I' 4 ~' ~~~~a ~ Doe. No. 1798597.1 ', Sequence GenBank Model Accl~"~

I ID' d N l1 S G i Tittl Cl t D No. dentifier. ;C:o arne gene i Ref. e u ene er eqa n us e Rattus norvegicus casein kinase II beta subunit ( Csnk2b), mRNA.
Length =

1859 1480 NM 031021f 1964 casein kinase II
beta subunit Rattus norvegicus drebrin A

( Dbn1), mRNA.
Length=

1860 1719 NM 031024n 2697 drebrin A

Rattus norvegicus cyclin G-associated kinase (Gak), 1861 1350 NM 031030h mRNA. Length cyclin G-associated = 4454 kinase Rattus norvegicus L-arginine: glycine amidinotransferase (Gatm), 1862 16775 NM 031031GeneralmRNA. Length L-arginine: g1 tine = 2260 amidinotransferase Rattus norvegicus guanine nucleotide binding protein (G

protein) alphaguanine nucleotide 12 (Gnal2), binding protein (G

1863 691 NM 031034w mRNA. Length protein) al ha 12 = 1423 Rattus norvegicus GTP-binding protein (G-alpha-i2) ( Gnai2), mRNA.
Length =

1864 15886 NM 031035z 1748 GTP-binding rotein (G-al ha-i2) Rattus norvegicus histamine N-methyltransferase (Hnmt), 1866 3608 NM 031044k,GeneralmRNA. Length histamine N-meth = 1225 Itransferase Rattus norvegicus histamine N-methyltransferase (Hnmt), 1866 3610 NM 031044d,GeneralmRNA. Length histamine N-meth = 1225 Itransferase Rattus norvegicus macrophage migration i nhibitory factor (Mif), mRNA.

1867 15137 NM 031051s Length = 551 macrophage migration inhibitory factor Rattus norvegicus matrix metalloproteinase 14, membrane-inserted ( Mmpl4), mRNA. matrix metalloproteinase Length = 14, 1868 514 NM 031056General2448 membrane-inserted Rattus norvegicus methylmalonate semialdehyde dehydrogenase gene ( Mmsdh), mRNA. methylmalonate semialdehyde Length =

1869 17269 NM 031057General2059 d eh drogenase gene Rattus norvegicus ribosomal protein LlOa (Rp110a), 1870 11849 NM 031065a mRNA. Len th ibosomal rotein = 710 r L10a Rattus norvegicus nucleoporin 98 (Nup98), 1871 1855 NM 031074h mRNA. Length ucleoporin 98 = 3237 n Rattus norvegicus phosphatidylinositol 4-kinase ( Pik4cb), mRNA.
Length =

1872 683 NM 031083d 3205 p hosphatid linositol4-kinase Rattus norvegicus -ral simian l eukemia viral oncogene homolog A (ras related) 1873 15202 NM 031093a Rata), mRNA. NAME?
' ( Length = 952 #

Rattus norvegicus -ral simian l eukemia viral oncogene homolog A (ras related) 1873 15201 NM 031093a,n Rala), mRNA. NAME7 ( Length = 952 #

Rattus norvegicus ribosomal protein L5 (RplS), mRNA.

1874 12639 NM 031099as Len th = 1069 ibosomal rotein r L5 TABLE MMAR Atty. Docket No.
1: 44921-5089W0 SU

Doe. No. 1798897.1 5eyuenee GenBank Model Accl' ID No. dentifierRef. Seq ;CoeJeGene Narne Unigene Cluster I ID = Tittle Rattus norvegicus ribosomal protein L10 (Rp110), mRNA.

1875 20812 NM 031100a Length = 769 ribosomal protein Rattus norvegicus ribosomal protein L19 (Rp119), mRNA.

1876 16938 NM 031103w Length = 703 ribosomal protein Rattus norvegicus ribosomal protein L22 (Rp122), mRNA.

1877 19268 NM 031104 Length = 465 ribosomal protein Rattus norvegicus mRNA for r ibosomal protein S9 (Rps9), 1878 16929 NM 031108q mRNA. Length mRNA for ribosomal = 688 rotein S9 Rattus norvegicus ribosomal protein S11 (Rps11), mRNA.

1879 10878 NM 031110q,bb Length = 534 ibosomal protein r S11 Rattus norvegicus ribosomal protein S21 (Rps21 ), mRNA.

1880 19162 NM 031111as Length = 359 ribosomal protein Rattus norvegicus ribosomal protein S21 (Rps21), mRNA.

1880 19161 NM 031111a,bb Length = 359 ibosomal protein r S21 Rattus norvegicus ribosomal protein S24 (Rps24), mRNA.

1881 24615 NM 031112a,y Length = 466 ibosomal protein r S24 Rattus norvegicus ribosomal protein S27a (Rps27a), 1882 20839 NM 031113a,q mRNA. Length ibosomal rotein = 552 r S27a Rattus norvegicus r elated protein, clone 42C

I,m, S100A10), mRNA.
( Length =

1883 9040 NM 031114General573 S-100 related rotein, 1 clone 42C

Rattus norvegicus secretin r eceptor (Sctr), mRNA.

1884 6349 NM 031115a Length = 1796 secretin receptor Rattus norvegicus sulfite oxidase (Suox), mRNA.

1885 4970 NM 031127GeneralLength = 1777 sulfite oxidase Rattus norvegicus thyroid hormone receptor alpha ( Thra1), mRNA.
Length =

1886 814 NM 031134n,q 2460 t h roid hormone receptor Rattus norvegicus TGFB

i nducible early growth r esponse (Tieg), mRNA.

1887 3359 NM 031135GeneralLength = 3115 TGFB inducible early 1 rowth response Rattus norvegicus thymosin beta-4 (Tmsb4x), mRNA.

1888 5052 NM 031136a Length = 686 h mosin beta-4 1 t Rattus norvegicus thymosin beta-4 (Tmsb4x), mRNA.

1888 9359 NM 031136a Length = 686 EST

Rattus norvegicus vimentin 1889 5185 NM 031140GeneralVim), mRNA. vimentin 1 ( Length = 1796 Rattus norvegicus c ytoplasmic beta-actin ( Actx), mRNA.
Length =

1890 1625 NM 031144a,e 128 c toplasmic beta-actin Rattus norvegicus RABlIa, member RAS
oncogene f amily (Rablla),RAB1la, member RAS
mRNA. oncogene 1891 38 NM 031152bb Length = 895 amil 2 f Rattus norvegicus RABlIa, member RAS
oncogene f amily (Rablla),RAB11a, member RAS
mRNA. oncogene 1891 40 NM 031152bb en th = 895 amil 2 L f TABLE MMARY ' ~ '~~"" Att~y. Docket No.
1: 44921-5U89W0 SU

Doe. No. 1798397.1 ;. IJ
Sequence GenB~ank Model Accl I~ No. IdentifierRef. Seq Code Gene Name Unigene Cluster ID' ~,. Title , Rattus norvegicus ubiquitin-conjugating enzyme E2D

(homologous to yeast UBC4/5) (Ube2d3),ubiquitin-conjugating mRNA. enzyme E2D 3 1892 15277 NM 031237g Length = 1531 (homologous to east UBC4/5) Rattus norvegicus acyl-CoA

thioesterase 1, cytosolic (Cte1), mRNA. R.norvegicus mRNA
Length = for mitochondria) 1893 18083 NM 031315q 1591 ve -long-chain ac I-CoA thioesterase Rattus norvegicusR.norvegicus mRNA
acyl-CoA for mitochondria) t hioesterase very-long-chain 1, cytosolic acyl-CoA

(Cte1), mRNA. hioesterase,acyl-CoA
Length = t thioesterase 1, 1893 1858 NM 031315 1591 cytosolic Rattus norvegicus t-complex t estis expressed 1 (Tctexl), 1894 15663 NM 031318GeneralmRNA. Length -complex testis = 698 t expressed 1 Rattus norvegicus prolyl bb, endopeptidase (Prep), 1895 1422 NM 031324GeneralmRNA. Length prolyl endo eptidase = 2743 Rattus norvegicus UDP-glucose dehydrogeanse ( Ugdh), mRNA.
Length =

1896 18597 NM 031325g,bb 2318 UDP-glucose deh drogeanse Rattus norvegicus cysteine i,cc,rich protein 61 (Cyr61), 1897 11259 NM 031327GeneralmRNA. Length c steine rich rotein = 1871 61 Rattus norvegicus heterogeneous nuclear ribonucleoprotein A/B

( Hnrpab), mRNA.heterogeneous nuclear Length =

1898 4235 NM 031330General3061 r ibonucleoprotein A/B

Rattus norvegicus proteasome (prosome, macropain) 26S subunit, non ATPase,4 (Psmd4),proteasome (prosome, mRNA. macropain) 1899 18375 NM 031331I,m Length = 1334 26S subunit, non-ATPase,4 Rattus norvegicus E-cadherin (Cdh1), mRNA.

1900 3519 NM 031334cc Len th = 4396 E-cadherin Rattus norvegicus ceroid-l ipofuscinosis, neuronal 2 ( CIn2), mRNA.
Length =

1901 20698 NM 031357b 2485 Rattus norvegicus Glutathione-S-transferase, alpha type Glutathione-S-transferase, (Ya) (Gsta1 alpha type ), 1903 634 NM 031509n mRNA. Length Ya) = 1178 ( Rattus norvegicus Glutathione-S-transferase, alpha type Glutathione-S-transferase, (Ya) (Gsta1), alpha type 1903 25525 NM 031509n mRNA. Length Ya) = 1178 Rattus norvegicus Glutathione-S-transferase, alpha type (Ya) (Gsta1), 1903 25069 NM 031509b,n,wmRNA. Length = 1178 Rattus norvegicus Glutathione-S-transferase, alpha type Glutathione-S-transferase, (Ya) (Gsta1 alpha type ), 1903 35 NM 031509z mRNA. Length Ya) 6 = 1178 ( Rattus norvegicus Met proto-oncogene (Met), mRNA.

1904 48 NM 031517t Length = 4189 Met roto-oncogene Rattus norvegicus Nerve growth factor, gamma polypeptide Nerve growth factor, (Ngfg), mRNA. gamma 1905 872 NM 031523a Len th = 873 0l a tide TI.IBLEMMARY Alty. IJocket No.
1: 44921-5U89W0 SU

Doc. No. 1798397.1 Sequence GenBank Model Accl ID No. IdentifieriRef. Seq Code Gene Name Unigene Cluster '. ID Title Rattus norvegicus Nerve growth factor, gamma polypeptide Rattus (Ngfg), mRNA. norvegicus (clone RSKG50) 1905 16245 NM 031523 a,d,uLength = 873 kallikrein mRNA, 3' end Rattus norvegicus Nerve growth factor, gamma polypeptide Rattus (Ngfg), mRNA. norvegicus (clone RSKG50) 1905 16244 NM 031523 a Length = 873 kallikrein mRNA, 3' end Rattus norvegicus Protein phosphatase type 1 alpha, catalytic subunitProtein (Ppplca), phosphatase type alpha, 1906 9370 NM 031527 w mRNA. Length catal = 1392 tic subunit Rattus norvegicus Small i nducible gene JE (Scya2), 1907 20448 NM 031530 GeneralmRNA. Length Small = 780 inducible gene JE

Rattus norvegicus Small i nducible gene JE (Scya2), 1907 20449 NM 031530 GeneralmRNA. Length Small = 780 inducible gene JE

Rattus norvegicus Androsterone UDP-glucuronosyltransferase ( Ugt2b2), mRNA.Androsterone Length = UDP-1908 14633 NM 031533 a 1593 glucuronos Itransferase Rattus norvegicus antigen (collagen type I

receptor, thrombospondin receptor)-likeCD36 1 (scavanger antigen (collagen type I

receptor classreceptor, B type 1 ) thrombospondin receptor)-( Cd3611 ), mRNA.ike Length = l 1 (scavanger receptor class B

1909 16048 NM 031541 f 2497 t ype Rattus norvegicus Cytochrome P450, subfamily 2e1 (ethanol-inducible) ( Cyp2e1), mRNA.Cytochrome Length = P450, subfamily 2e1 1910 4011 NM 031543 c,q 1624 ( ethanol-inducible) Rattus norvegicus Cytochrome P450, subfamily 2e1 (ethanol-inducible) ( Cyp2e1 ), mRNA.Cytochrome Length = P450, subfamily 2e1 1910 4010 NM 031543 c, 1624 ( ethanol-inducible) Rattus norvegicus Cytochrome P450, subfamily 2e1 (ethanol-inducible) ( Cyp2e1), mRNA.Cytochrome Length = P450, subfamily 2e1 1910 4012 NM 031543 q 1624 ( ethanol-inducible) Rattus norvegicus Regucalcin (Rgn), mRNA.

1911 28 NM 031546 GeneralLength = 1605 Regucalcin Rattus norvegicus Sodium channel, nonvoltage-gated 1, alpha (epithelial)Sodium (Scnnla), channel, nonvoltage-gated 1, 1912 24640 NM 031548 h,cc mRNA. Length al = 3081 ha (epithelial Rattus norvegicus Transgelin ( Smooth muscle 22 protein) ( Tagln), mRNA. Transgelin Length = (Smooth muscle 1913 7149 NM 031549 x 1186 protein Rattus norvegicus Transgelin ( Smooth muscle 22 protein) ( Tagln), mRNA. Transgelin Length = (Smooth muscle 1913 7151 NM 031549 x 1186 protein) Rattus norvegicus Adducin 3, gamma (Add3), mRNA.

1914 3105 NM 031552 w Len th = 2246 Adducin 1 3, amma TABLE MMARY Atty. f)ocket No.
1: 44921-5U89W0 SU

Doe. 0.1798397.

~ 4, , Sequence GenB~ank ~Model ~lccl 117 des Ref. Seq Code Gene Name Unige,~ne Cluster No. iffier ID Title I

Rattus norvegicus Carnitine palmitoyltransferase 1 alpha, l iver isoform Carnitine palmitoyltransferase (Cpt1a), mRNA.1 alpha, 1915 5411 NM 031559d,r Length = 4377 iver isoform 1 l Rattus norvegicus Y box protein 1 (Ybx1), mRNA.

1916 6164 NM 031563a, Length = 1489 Y box rotein 1 Rattus norvegicus ribosomal protein S7 (Rps7), mRNA.

1917 9621 NM 031570bb Length = 650 ribosomal protein Rattus norvegicus ribosomal protein S7 (Rps7), mRNA.

1917 9620 NM 031570w,bb Length = 650 ribosomal protein Rattus norvegicus Phosphorylase kinase, g amma 1 (Phkg1), mRNA.

1918 546 NM 031573f Length = 1388 phos horylase kinase gamma Rattus norvegicus ( cytochrome) oxidoreductase 1919 1921 NM 031576f Por), mRNA. P450 (cytochrome) ( Length = 2441 oxidoreductase Rattus norvegicus ( cytochrome) oxidoreductase 1919 1920 NM 031576r Por), mRNA. P450 (cytochrome) ( Length = 2441 oxidoreductase Rattus norvegicus protein t yrosine phosphatase 4a1 ( Ptp4a1), mRNA.
Length =

1920 24219 NM 031579i,General2638 protein t rosine phosphatase 4a1 Rattus norvegicus solute carrier family 22, member ( SIc22a2), mRNA.
Length =

1921 770 NM 031584k,x 2152 solute carrier famil 22, member Rattus norvegicus neuregulin 1 (Nrg1), mRNA.potassium channel, Length = subfamily K, 1922 18008 NM 031588cc 3272 member 3 Rattus norvegicus neuregulin 1 (Nrg1), mRNA.potassium channel, Length = subfamily K, 1922 18005 NM 031588h 3272 member 3 Rattus norvegicus neuregulin cc, 1 (Nrg1), mRNA.potassium channel, Length = subfamily K, 1922 18011 NM 031588General3272 member 3 Rattus norvegicus proteasome (prosome, macropain) 26S subunit, ATPase 3 (Psmc3),proteasome (prosome, mRNA. macropain) 1923 1584 NM 031595k Length = 1627 26S subunit, ATPase Rattus norvegicus t hioredoxin reductase ( Txnrdl), mRNA.
Length =

1924 24235 NM 031614v 3360 t hioredoxin reductase Rattus norvegicus t hioredoxin reductase ( Txnrdl), mRNA.
Length =

1924 24234 NM 031614General3360 t hioredoxin reductase Rattus norvegicus nuclear r eceptor subfamily 1, group H, member 3 nuclear receptor (Nrlh3), subfamily 1, group H, 1925 1639 NM 031627j,l,vmRNA. Length member 3 = 1723 Rattus norvegicus core promoter element binding m, protein (Copeb), mRNA.

1926 1727 NM 031642GeneralLength = 1356 core romoter element binding rotein -1 2s-'1AB-LEMMARY '~-- Atty. Docket No.
1: 44931-5U89W0 SU

Doe. No. 1798597.1 ~Sequenee GenBank Model Reel 1D No. dentifierRef. Seq Code Gene Name Unigene Cluster I ID *i Title ~'~

Rattus norvegicus mitogen activated protein kinase kinase 2 (Map2k2),mitogen activated mRNA. protein kinase 1927 20766 NM 031643y Length = 1182 kinase 2 k,l,m,Rattus norvegicus latexin 1929 1993 NM 031655GeneralLxn), mRNA. atexin ( Length = 1087 l Rattus norvegicus cyclic AMP phosphoprotein, l9kD

( Arpp19-pending), mRNA.

1930 2057 NM 031660a Length = 339 c clic AMP phos hoprotein, 19kD

Rattus norvegicus solute carrier family 15 (H+/peptide t ransporter), member 2 ( SIc15a2), mRNA.solute carrier Length = family 15 (H+/peptide 1931 15039 NM 031672k,General3923 t rans orter), member Rattus norvegicus hydroxyacyl-Coenzyme A

dehydrogenase, type II

( Hadh2), mRNA. hydroxyacyl-Coenzyme Length = A

1932 15175 NM 031682bb 917 deh dro enase, ty a II

Rattus norvegicus golgi SNAP receptor complex member 2 (Gosr2),golgi SNAP receptor mRNA. complex member 1933 1004 NM 031685v Length = 683 2 Rattus norvegicus ubiquitin A

52 residue ribosomal protein f usion product ubiquitin A-52 1 (Uba52), residue ribosomal 1934 19727 NM 031687a,q,smRNA. Length protein fusion = 467 product 1 Rattus norvegicus claudin 3 ( CIdn3), mRNA.
Length =

1935 20404 NM 031700',r, 1192 claudin 3 Rattus norvegicus claudin 3 ( CIdn3), mRNA.
Length =

1935 20405 NM 031700o,r 1192 claudin 3 Rattus norvegicus dihydropyrimidinase (Dpys), 1936 811 NM 031705GeneralmRNA. Length dihydrop rimidinase = 2091 Rattus norvegicus o,v,bb,dihydropyrimidinase (Dpys), 1936 812 NM 031705GeneralmRNA. Length ih drop rimidinase = 2091 d Rattus norvegicus ribosomal protein S8 (Rps8), mRNA.

1937 16204 NM 031706q,bb Length = 696 ibosomal protein r S8 Rattus norvegicus ribosomal protein S8 (Rps8), mRNA.

1937 16205 NM 031706a, Length = 696 ibosomal rotein r S8 Rattus norvegicus glycoprotein 110 (Gp110-pending), mRNA.
Length =

1938 24081 NM 031708m 444 g l co rotein 110 Rattus norvegicus ribosomal protein S12 (Rpsl2), mRNA.

1939 6918 NM 031709a,q Len th = 499 ibosomal protein 1 r S12 Rattus norvegicus PDZ

d omain containing 1 (Pdzk1), 1940 081 NM 031712GeneralmRNA. Length PDZ domain containing 1 = 2005 1 Rattus norvegicus phosphofructokinase, muscle b,n,u,cc,Pfkm), mRNA.
( Length =

1941 340 NM 031715General2757 p hos hofructokinase, 1 muscle Rattus norvegicus alcohol d ehydrogenase family 3, s ubfamily A2 lcohol dehydrogenase (Aldh3a2), family 3, a 1942 23884 NM 031731',s mRNA. Len th ubfamil A2 = 2977 s TABLE MMA ~tty. Docket No.
1: 44921-5U89W0 SU

___ Uoc. No. 1798397.1 Sequence GenBa Model k Reel ID No. IdentifierRef. Seq Code Gene Name Unigene Cluste ID Tittle Rattus norvegicus UDP-Gal:betaGIcNAc beta 1,4-galactosyltransferase, polypeptide UDP-Gal:betaGIcNAc 6 (B4galt6), beta 1,4-1943 10241 NM 031740d mRNA. Length galactos Itransferase, = 5729 of peptide 6 Rattus norvegicus solute carrier family 2 (facilitated glucose transporter), member 5 (SIc2a5),solute carrier mRNA. family 2 (facilitated 1944 1214 NM 031741r Length = 2169 glucose transporter), member 5 Rattus norvegicus solute carrier family 2 (facilitated glucose transporter), member 5 (SIc2a5),solute carrier mRNA. family 2 (facilitated 1944 1215 NM 031741r Length = 2169 glucose transporter), member 5 Rattus norvegicus activated l eukocyte cell adhesion molecule (Alcam),activated leukocyte mRNA. cell adhesion 1945 20724 NM 031753h Length = 2866 molecule Rattus norvegicus platelet-activating factor acetylhydrolaseplatelet-activating beta subunit factor ( PAF-AH beta) acetylhydrolase (Pafahlbl), beta subunit (PAF-AH

1946 20753 NM 031763h mRNA. Length beta = 1233 Rattus norvegicus platelet-activating factor acetylhydrolaseplatelet-activating beta subunit factor ( PAF-AH beta) acetylhydrolase (Pafahlb1), beta subunit (PAF-AH

1946 20752 NM 031763y mRNA. Length beta) = 1233 Rattus norvegicus rab acceptor 1 (prenylated) ( Rabac1), mRNA.
Length =

1947 14953 NM 031774 861 rab acceptor 1 (pren lated) Rattus norvegicus guanine deaminase (Gda), mRNA.

1948 14184 NM 031776t,GeneralLength = 1568 guanine deaminase Rattus norvegicus guanine d,o,t,deaminase (Gda), mRNA.

1948 14185 NM 031776GeneralLen th = 1568 guanine deaminase Rattus norvegicus r elated factor 2 (Nfe212), 1949 1169 NM 031789c mRNA. Length NF-E2-related factor = 2307 2 Rattus norvegicus defensin beta 1 (Defbi), mRNA.

1950 16155 NM 031810d,z Length = 416 defensin beta 1 Rattus norvegicus defensin beta 1 (Defb1), mRNA.

1950 16156 NM 031810d Length = 416 defensin beta 1 Rattus norvegicus G protein-coupled receptor kinase-associated ADP ribosylation f actor GTPase-activatingG protein-coupled receptor kinase-protein (GIT1 associated ADP
) (Git1 ), ribosylation factor mRNA.

1951 17194 NM 031814z Length = 3236 GTPase-activatin protein (GIT1 Rattus norvegicus r etinoblastoma binding protein 7 (Rbbp7), mRNA.

1952 7535 NM 031816bb Len th = 1947 retinoblastoma 1 binding rotein Rattus norvegicus serum-i nducible kinase (Snk), 1953 2655 NM 031821i,l,m,aamRNA. Len th serum-inducible = 2781 kinase Rattus norvegicus reggie1-1 ( FIot2), mRNA.
Length =

1954 0167 NM 031830i 2629 re ie1-1 TABLE MMARY Atty. Docket No.
1: 44921-5U89W0 SU

Doe. No. 1798397.1 f 'Sequence GenBank Model i4cdl ID No. IdentifierRef. Seq Code Gene Name Unige"ne, Cluster ID Title Rattus norvegicus IgE

o,t,u,binding protein (Lgals3), 1955 22321 NM 031832GeneralmRNA. Length IgE binding protein = 948 Rattus norvegicus sulfotransferase family 1A, phenol-preferring, member 1 ( Sultla1), mRNA.
Length=

1956 4748 NM 031834e,t 1227 minoxidil sulfotransferase Rattus norvegicus sulfotransferase family 1A, phenol-preferring, member 1 ( Sult1al), mRNA.
Length =

1956 4749 NM 031834e,t 1227 minoxidil sulfotransferase Rattus norvegicus beta-alanine-pyruvate aminotransferasebeta-alanine-pyruvate (AGT2), 1957 7914 NM 031835a mRNA. Length aminotransferase = 2151 Rattus norvegicus vascular endothelial growth factor 1958 8385 NM 031836h Vegf), mRNA. vascular endothelial ( Length = 645 growth factor Rattus norvegicus vascular endothelial growth factor 1958 8384 NM 031836h Vegf), mRNA. vascular endothelial ( Length = 645 growth factor Rattus norvegicus ribosomal protein S2 (Rps2), mRNA.

1959 10268 NM 031838a Length = 819 ribosomal protein Rattus norvegicus ribosomal protein S2 (Rps2), mRNA.

1959 10269 NM 031838as Length = 819 ribosomal protein Rattus norvegicus ribosomal protein S2 (Rps2), mRNA.

1959 10267 NM 031838n,aa Length = 819 ribosomal protein Rattus norvegicus stearoyl-CoA desaturase 2 (Scd2), 1960 15077 NM 031841b mRNA. Length stearoyl-CoA desaturase = 5055 2 Rattus norvegicus .

Ketohexokinase (Khk), 1961 16726 NM 031855x mRNA. Length Ketohexokinase = 1342 Rattus norvegicus Calmodulin 1 (phosphorylase kinase, delta)Calmodulin 1 (phosphorylase (Calm1 ), kinase, 1962 25802 NM 031969a mRNA. Length delta) = 3513 Rattus norvegicus Calmodulin 1 (phosphorylase kinase, delta)Calmodulin 1 (phosphorylase (Calm1), kinase, 1962 19191 NM 031969c mRNA. Length delta) = 3513 Rattus norvegicus Calmodulin 1 (phosphorylase kinase, delta)Calmodulin 1 (phosphorylase (Calm1 ), kinase, 1962 19195 NM 031969r mRNA. Length delta) = 3513 Rattus norvegicus Calmodulin 1 (phosphorylase kinase, delta)Calmodulin 1 (phosphorylase (Calm1 ), kinase, 1962 19190 NM 031969 mRNA. Length delta) = 3513 Rattus norvegicus Heat shock 27 kDa protein (Hsp27), mRNA.
Length =

1963 17734 NM 031970v,General787 ESTs,Heat shock 27 kDa protein ESTs, Highly similar to S10A RAT S-Rattus norvegicus100 PROTEIN, ALPHA
Heat CHAIN

shock protein [R.norvegicus],Heat 70-1 (Hspala),shock protein 1964 1475 NM 031971v mRNA. Len th 1 = 2455 TABLE MMARY ~ Atty. Docket No.
1: 44931-5U89W0 SU

Uoc. No. 1798397.

___ Sequence GenBank Model Acef 1D No. dentifierRef. Se,cqCode Gene Name Unigene Cluster ,I ID Title Rattus norvegicus proteasome, subunit p112 ( PSMD1), mRNA.
Length =

1965 15470 NM 031978 3089 26S proteasome, f subunit 112 Rattus norvegicus cerebellar Ca-binding protein, spot protein (Calb1cerebellar Ca-binding ), mRNA. protein, spot 1966 18502 NM 031984c Length = 2280 rotein Rattus norvegicus syntenin v,aa,Sdcbp), mRNA.
( Length =

1967 19768 NM 031986General2077 syntenin Rattus norvegicus chimerin ( chimaerin) 2 (Chn2), mRNA.

1968 723 NM 032084n Length = 1118 chimerin (chimaerin) Rattus norvegicus membrane interacting protein of membrane interacting RGS16 (Mirl6),protein of 1969 17935 NM 032615a mRNA. Length RGS16 = 1203 Rattus norvegicus Crystallin, gamma polypeptide ( Crygd), mRNA.
Length =

1970 16831 NM 033095n 634 Rattus norvegicus Hemoglobin, beta (Hbb), 1971 25468 NM 033234c,z mRNA. Length = 620 Rattus norvegicus Hemoglobin, beta (Hbb), 1971 25469 NM 033234c mRNA. Length = 620 Rattus norvegicus Hemoglobin, Rat major beta-globin beta (Hbb), mRNA, 1971 17832 NM 033234c,p mRNA. Length com lete cds = 620 Rattus norvegicus Hemoglobin, Rat major beta-globin beta (Hbb), mRNA, 1971 17829 NM 033234c,z mRNA. Len th complete cds = 620 Rattus norvegicus Malate dehydrogenase-likeRattus norvegicus enzyme cytosolic malate ( Mdhl), mRNA. dehydrogenase (Mdh) Length = mRNA, 1972 4723 NM 033235z 1266 com lete cds Rattus norvegicus Hydroxyacyl glutathione hydrolase (Hagh),Rattus norvegicus mRNA. round spermatid 1973 1409 NM 033349p,GeneralLength = 783 protein RSP29 gene, complete cds Rattus norvegicus ATP-binding cassette, sub-family D (ALD), member 2 (Abcd2), 1974 19998 NM 033352GeneralmRNA. Length PDZ domain containin = 5531 1 Rattus norvegicus Kidney 1 ( Kid1), mRNA. Rat zinc finger Length = protein (kid-1) mRNA, 1975 1410 NM 052798d 2563 c omplete cds Rattus norvegicus cytosolic cysteine dioxygenase ( Cdo1 ), mRNA. Rat cysteine dioxygenase Length = mRNA, 1976 15028 NM 052809 1458 c omplete cds f Rattus norvegicus Pyruvate kinase 3 (Pkm2),Rat mRNA for pituitary mRNA. pyruvate 1977 5176 NM 053297a Length = 1973 inase k Rattus norvegicus ubiquitin D (Ubd), mRNA.ESTs, Weakly similar Length = to polyubiquitin 1978 7660 NM 053299 684 [ R.norve icus]
i Rattus norvegicus homer, neuronal immediate early gene, 3 (Homer3),Rattus norvegicus mRNA. mRNA for Vesl-3, 1979 5117 NM 053310 Len th = 1207 om lete cds c TABLE MMA Atty. Docket No.
1: Y 44921-5U89W0 SU

Doe. No. 1798397.1 Sequence GenBank Model Accl 1D No. dentifierRef. Seq Code Gene Name Unigene Cluster ' I ID Title Rattus norvegicusRattus norvegicus dynein, protein inhibitor of cytoplasmic, neuronal nitric light chain oxide synthase 1 (PIN) 1981 17473 NM 053319a,v Pin), mRNA. mRNA, complete ( Length = 505 cds Rattus norvegicus insulin-like growth factor binding protein, acid labile subunit (Igfals), 1982 25480 NM 053329g mRNA. Length = 1812 Rattus norvegicus insulin-like growth factor Rattus norvegicus binding protein,insulin-like growth acid labile factor binding subunit (Igfals),protein complex acid-1982 21977 NM 053329 mRNA. Length labile subunit = 1812 ene, complete cds Rattus norvegicus ribosomal protein L21 Rattus norvegicus (Rp121), mRNA.ribosomal protein 1983 14926 NM 053330 Length = 554 L21 mRNA, com lete f cds Rattus norvegicus ribosomal protein L21 Rattus norvegicus (Rp121), mRNA.ribosomal protein 1983 4929 NM 053330e,GeneralLength = 554 L21 mRNA, com lete 1 cds Rattus norvegicus cubilin ( intrinsic factor-cobalaminRattus norvegicus intrinsic factor-B12 r eceptor) (Cubn),receptor precursor mRNA. (CUBILIN) mRNA, 1984 6407 NM 053332c,e Length = 10,872com lete cds Rattus norvegicus regulator of G-protein signaling ( Rgsl9), mRNA.
Length =

1985 5790 NM 053341,x 1607 regulator of G-protein 1 ' signaling 19 Rattus norvegicus procollagen, type I, alpha ( Colla2), mRNA.
Length =

1986 6154 NM 053356p 4474 procollagen, type I, alpha 2 Rattus norvegicus interteron gamma inducing factor binding proteininterteron gamma (Igifbp), inducing factor 1987 9215 NM 053374 mRNA. Length binding protein i = 626 Rattus norvegicus solute carrier family 34 (sodium phosphate), member 2 ( SIc34a2), mRNA.solute carrier Length = family 34 (sodium 1988 6416 NM 053380General3950 phosphate , member Rattus norvegicus small muscle protein, X-linked ( Smpx), mRNA. Rattus norvegicus Length = SMPX protein 1989 19113 NM 053395a 892 (Smpx) mRNA, complete cds Rattus norvegicus flavin-containing monooxygenase 3 (Fmo3), mRNA.
Length =

1990 2242 NM 053433n,General2037 flavin-containing monoox genase Rattus norvegicus zinc finger protein 103 (Zfp103), mRNA.

1991 5561 NM 053438 Length = 3258 zinc finger rotein Rattus norvegicus RAN, member RAS
oncogene f amily (Ran), mRNA. Length 1992 14670 NM 053439n,General= 1084 RAN, member RAS
oncogene famil Rattus norvegicus superiorcervical ganglia, neural specificsuperiorcervical 10 (ScgnlO), ganglia, neural 1993 17102 NM 053440w mRNA. Length s ecific 10 = 1654 Rattus norvegicus solute carrier family 8 (cationic amino acid solute carrier transporter, family 8 (cationic y+ amino system), memberacid transporter, 7 (Lat4), y+ system), member 1994 24762 NM 053442GeneralmRNA. Length 7 = 4117 TABLE MMARY Atty. Docket No.
1: 44931-5U89W0 SU

Uoc. No. 1798397.

Sequence GenBank Model Accl ID No. dentifierRef. Seq Code Gene Name Unigene Cluster , ,I ID Tittle Rattus norvegicus regulator of G-protein signaling protein 2 (Rgs2), mRNA.regulator of G-protein Length = signaling protein 1995 8085 NM 053453General1629 2 Rattus norvegicus nucleobindin (Nucb), mRNA.

1996 4622 NM 053463d Length = 2303 nucleobindin Rattus norvegicus cytochrome c oxidase subunit IV
isoform 2 precursor (CoxIV-2),cytochrome c oxidase mRNA. subunit IV

1997 21866 NM 053472p Length = 704 isoform 2 precursor Rattus norvegicus protein t yrosine phosphatase type I VA, member protein tyrosine 2 (Ptp4a2), phosphatase type 1998 9573 NM 053475h mRNA. Length IVA, member 2 = 1095 Rattus norvegicus DNA

' polymerase alpha subunit II

( Pola2), mRNA.
Length =

1999 16137 NM 053480k 1836 DNA pol merase alpha subunit II

Rattus norvegicus karyopherin (importin) alpha 2 (Kpna2), mRNA. Length =

2000 15556 NM 053483 1886 ka opherin (im ortin) alpha 2 Rattus norvegicus calcium binding protein A6 (calcyclin) ( S100a6), mRNA.
Length =

2001 16394 NM 053485General291 calcium binding protein A6 (calcyclin Rattus norvegicus peroxisomal membrane protein Pmp26p (Peroxin-11 ) ( Pex11a), mRNA.peroxisomal membrane Length = protein 2002 4290 NM 053487 1194 Pmp26p (Peroxin-11) Rattus norvegicus homocysteine-inducible, endoplasmic reticulum stress i nducible, ubiquitin-like domain member ( Herpudl ), Rattus norvegicus mRNA. Length SUP mRNA, =

2004 18826 NM 053523d 1857 com late cds Rattus norvegicus ATP-d ependent, RNA
helicase ( Rok1 ), mRNA. Rattus norvegicus Length = rROK1 L mRNA for 2005 7764 NM 053525as 2175 ROKi-like rotein, complete cds Rattus norvegicus lysosomal associated protein t ransmembrane Rattus norvegicus 5 (LaptmS), gcd-10S mRNA, 2006 14199 NM 053538c mRNA. Length complete cds = 1309 Rattus norvegicus i sopentenyl-diphosphateRattus norvegicus isopentenyl d elta isomerasediphosphate:dimethylallyl (Idi1), diphosphate 2007 1058 NM 053539c,d mRNA. Length isomerase mRNA, = 1182 complete cds Rattus norvegicus nuclear RNA helicase, DECD variant of DEAD box Rattus norvegicus family (Ddxl),nuclear RNA

2008 4327 NM 053563GeneralmRNA. Length helicase mRNA, = 1511 com lets cds Rattus norvegicusRattus norvegicus neuronal olfactomedin olfactomedin-related related ER ER localized l ocalized proteinprotein (D2Sutle) (OIfm1), mRNA, complete 2009 1342 NM 053573h mRNA. Length cds = 2759 Rattus norvegicus thiol-s pecific antioxidantRattus norvegicus protein mRNA for thiol-( PrdxS), mRNA. specific antioxidant Length = protein (1-Cys 2010 19254 NM 053576h,s 414 eroxiredoxin) -fAB~LEMMARY Atty. Docket No.
1: 44921-5089W0 SU

floe. N
o. 1798397.1 Sequence GenBank ~Illlodel _ Acel ID No. dentifierRef. Seq Code Gene Name Unigeyyn"e, Cluster I ID Title Rattus norvegicus thiol-specific antioxidantRattus norvegicus protein mRNA for thiol-( PrdxS), mRNA. specific antioxidant Length = protein (1-Cys 2010 19253 NM 053576h 1414 eroxiredoxin Rattus norvegicus glucocorticoid-inducibleRattus norvegicus gis5 mRNA for p,cc,protein (gis5),glucocorticoid-inducible mRNA. Length protein, 2011 3049 NM 053582General= 1869 complete cds Rattus norvegicus glucocorticoid-inducibleRattus norvegicus gis5 mRNA for protein (gis5),glucocorticoid-inducible mRNA. Length protein, 2011 3050 NM 053582o,General= 1869 complete cds Rattus norvegicus cytochrome c oxidase subunit Vb Rat mRNA for cytochrome (CoxSb), mRNA.c oxidase 2012 21423 NM 053586s, Length = 485 subunit Vla Rattus norvegicus calcium-bindingRattus norvegicus protein A9 intracellular calcium ( calgranulin binding protein B) (S100a9), (MRP14) mRNA, 2013 21445 NM 053587t,v mRNA. Length complete cds = 494 Rattus norvegicus dipeptidase Rat dipeptidase 1 (Dpep1 ), (dpepl ) mRNA, 2014 20871 NM 053591j,1 mRNA. Length complete cds = 2179 Rattus norvegicus dipeptidase Rat dipeptidase 1 (Dpep1), (dpep1) mRNA, 2014 20870 NM 053591I mRNA. Length com lete cds = 2179 Rattus norvegicus protein t yrosine phosphatase, r eceptor type, Rattus norvegicus R (Ptprr), mRNA for tyrosine 2015 21044 NM 053594d mRNA. Length phosphatase CBPTP, = 3565 com lete cds Rattus norvegicus endothelia converting Rat mRNA for endothelia-converting enzyme 1 (Ece1 ), 2016 21709 NM 053596k mRNA. Length enz me, complete = 4469 cds Rattus norvegicus endothelia converting Rat mRNA for endothelia-converting enzyme 1 (Ece1), 2016 21708 NM 053596z mRNA. Length enz me, complete = 4469 cds Rattus norvegicus nuclear proten 1 (Nupr1),Rattus norvegicus mRNA. p8 mRNA, 2017 1597 NM 053611t Length = 602 com lete cds Rattus norvegicus Bardet-Biedl syndrome 2 (human) ( Bbs2), mRNA. Rattus norvegicus Length = BBS2 (Bbs2) 2018 5565 NM 053618General2573 mRNA, com lets cds Rattus norvegicus fatty acid-Coenzyme A
ligase, long c hain 4 (Facl4),Rattus norvegicus mRNA. mRNA for Acyl-2019 13004 NM 053623t Length = 4862 CoA s nthetase, com lets cds Rattus norvegicus D-amino a cid oxidase Rattus norvegicus (Dao1 ), mRNA.mRNA for D-amino-2020 1127 NM 053626 Length = 1646 acid oxidase, com lets cds Rattus norvegicus beta-c arotene 15, Rattus norvegicus 15'- mRNA for beta-d ioxygenase carotene 15,15'-dioxygenase, (Bcdo), mRNA.

2021 18644 NM 053648n Length = 2207 com lete cds Rattus norvegicusESTs, Highly similar vascular to VEGC MOUSE

e ndothelial VASCULAR ENDOTHELIAL
growth factor C

( Vegfc), mRNA. GROWTH FACTOR C
Length = PRECURSOR

2022 21637 NM 0536531 596 M.musculus]

Rattus norvegicus cyclin L

( Ccnl), mRNA. Rattus norvegicus Length = cyclin ania-6a 2023 3454 NM 053662cc 092 mRNA, com lete 2 cds TABLE MMARY '~_ : Atty. Docket 1: No. 44921-5U89W0 SU

Doe. 0. 1798397.1 Sequence GenBank Model Reel ID No. dentifierRef. Seq Code Gene Name p Unigene Cluster I ID Title Rattus norvegicus Cbp/p300-i nteracting transactivator, with Glu/Asp-rich carboxy-t erminal domain,Rattus norvegicus 2 (Cited2), transcription factor 2024 16121 NM 053698h,',zmRNA. Length MRG1 mRNA, complete = 1155 cds Rattus norvegicus Cbp/p300-i nteracting transactivator, with Glu/Asp-rich carboxy-t erminal domain,Rattus norvegicus 2 (Cited2), transcription factor 2024 16122 NM 053698h,j,zmRNA. Length MRG1 mRNA, complete = 1155 cds Rattus norvegicus Kruppel-l ike factor 4 (gut) (KIf4), 2025 25379 NM 053713GeneralmRNA. Length = 2393 Rattus norvegicus Kruppel-l ike factor ESTs, Moderately 4 (gut) (KIf4),similar to zinc Tinge 2025 13622 NM 053713GeneralmRNA. Length protein [R.norvegicus = 2393 Rattus norvegicus ubiquilin ( Ubqln1), mRNA.Rattus norvegicus Length = mRNA for DA41, 2026 15376 NM 053747h 2131 complete cds Rattus norvegicus dipeptidylpeptidase III

( Dpp3), mRNA. Rattus norvegicus Length = mRNA for 2027 1218 NM 053748b 2632 dipe tid I peptidase III, complete cds Rattus norvegicus cytochrome P450, 40 (25-hydroxyvitaminRattus norvegicus D3 1 alpha- 25-hydroxyvitamin hydroxylase) D 1-hydroxylase (Cyp40), (CYP1) mRNA, 2028 1137 NM 053763 mRNA. Length complete cds = 2426 Rattus norvegicus protein t yrosine phosphatase, non-r eceptor type Rattus norvegicus 16 (Ptpnl6), protein tyrosine 2029 15996 NM 053769cc mRNA. Length phosphatase mRNA, = 1104 complete cds Rattus norvegicusRattus norvegicus ubiquitin deubiquitinating specific proteaseenzyme Ubp69 (ubp69) 2 (Usp2), mRNA, 2030 8652 NM 053774g mRNA. Length complete cds = 1857 Rattus norvegicus potassium channel, subfamily K, member 6 (TWIK-2) (Kcnk6), 2031 14664 NM 053806GeneralmRNA. Length ESTs = 2243 Rattus norvegicus antagonisUkillerRattus nonregicus 1 (Bak1), BAK protein (Bak) 2032 4361 NM 053812k mRNA. Length mRNA, complete = 1923 cds Rattus norvegicus tissue i nhibitor of Rattus norvegicus metalloproteinasetissue inhibitor of b,x,bb,(Timp1), mRNA.metalloproteinase-1 1 Length = (TIMP1), mRNA, 2034 15002 NM 053819General740 complete cds Rattus norvegicus tissue i nhibitor of Rattus norvegicus metalloproteinasetissue inhibitor of b,l,x,bb,(Timp1), mRNA.metalloproteinase-1 1 Length = (TIMP1), mRNA, 2034 5003 NM 053819General740 com lete cds Rattus norvegicus c alcium-bindingRattus norvegicus protein AS intercellular calcium ( calgranulin binding protein A) (S100a8), (MRPB) mRNA, 2035 6173 NM 053822t mRNA. Length complete cds 1 = 361 Rattus norvegicusRat clathrin light clathrin, chain (LCB2) mRNA, l ight polypeptidecomplete cds,Rat (Lcb) (Cltb), clathrin light chain 2036 7154 NM 053835j,z mRNA. Length (LCB3) mRNA, complete 1 = 982 cds Rattus norvegicus Fc r eceptor, IgG, low affinity III

( Fcgr3), mRNA. Rat Fc-gamma receptor Length = mRNA, 2037 20868 NM 053843t 318 complete cds Rattus norvegicus Fc r eceptor, IgG, low affinity III

( Fcgr3), mRNA. Rat Fc-gamma receptor Length = mRNA, 2037 0869 NM 053843t 318 com lete cds TABLE MMA Atty. Docket No.
1: Y 449 1-5U89W~
SU

~oe. No. 1798397.1 Sequence GenBank Model Aeel ID No: IdentifierRef. Code Gene Name Unigene Cluster Seq Title IU

Rattus norvegicus solute carrier family 28 (sodium-coupled nucleosideRattus norvegicus Sprague-Dawley t ransporter), sodium-dependent member 1 nucleoside (SIc28a1 ), transporter (rCNT1 mRNA. Length ) mRNA, complete =

2040 714 NM 053863 y 2401 cds Rattus norvegicus dual specificity Rattus norvegicus phosphatase dual-specificity (Dusp6), mRNA.protein tyrosine Length = phosphatase (rVH6) 2041 19781 NM 053883 b 2104 mRNA, complete cds Rattus norvegicus dual specificity Rattus norvegicus phosphatase dual-specificity (Dusp6), mRNA.protein tyrosine Length = phosphatase (rVH6) 2041 19780 NM 053883 b 2104 mRNA, complete cds Rattus norvegicus mitogen activated proteinRattus norvegicus kinase MAP kinase kinase kinase kinase kinase 1 (MEKK1) 1 (Map3k1), mRNA, complete 2042 1454 NM 053887 GeneralmRNA. Length cds = 5180 Rattus norvegicus cyclin-dependent kinase 5, r egulatory subunit 1 (p35) ( CdkSr), mRNA. Rattus norvegicus Length = P35 mRNA, 2043 1660 NM 053891 g 1208 com lets cds Rattus norvegicus aldehyde dehydrogenase family 1, subfamily A2 Rattus norvegicus (Aldhla2), aldehyde 2044 712 NM 053896 k mRNA. Length deh dro enase mRNA, = 2240 complete cds Rattus norvegicus coagulation factor II

( thrombin) receptor-likeRattus norvegicus 1 proteinase-( F2r11), mRNA. activated receptor-2 Length = mRNA, complete 2045 753 NM 053897 k 1428 cds Rattus norvegicus kynureninase (L-kynurenine hydrolase) Rattus norvegicus (Kynu), mRNA. L-kynurenine 2046 794 NM 053902 GeneralLength = 1765 hydrolase mRNA, com lete cds Rattus norvegicus pleckstrin homology, Sec7 and coiled/coil domains 2 ( Pscd2), mRNA. Rattus norvegicus length = sec7B mRNA, 2047 17937 NM 053911 f 561 complete cds Rattus norvegicus erythrocyte membrane protein band 4.1-like 3 ( Epb4113), mRNA.Rattus norvegicus Length = mRNA for type II

2048 8188 NM 053927 General543 brain 4.1, complete 4 cds Rattus norvegicus e ndothelial differentiation, l ysophosphatidic acid G-p rotein-coupledRattus norvegicus receptor, putative G-protein ( Edg2), mRNA. oupled receptor Length = c GPCR91 (Gpcr91 ) 2050 628 NM 053936 h 543 mRNA, com lets 1 1 cds Rattus norvegicus crystallin, mu (Crym), mRNA. Length =

2051 3954 NM 053955 General227 Rattus norvegicus 1 1 CDK108 mRNA

Rattus norvegicus e ndoplasmic R.norvegicus mRNA
retuclum encoding 45kDa p rotein 29 (Erp29),rotein which binds mRNA. p to heymann 2052 08 NM 053961 Generalength = 4529 ephritis antigen 4 L n gp330 Rattus norvegicus e ndoplasmic retuclum p rotein 29 (Erp29),mitochondrial aconitase mRNA. (nuclear aco2 2052 9991 NM 053961 a ength = 4529 ene) TABLE MMARY ~ltty. Docket No.
1: 44921-5U89W0 SU

~oe. No. 798397.1 Sequence GenBank Model Reel 1D No. IdentifierRef. Seq Code Gene Name Unigene Cluster ID ~ Title Rattus norvegicusESTs, Weakly similar to ECHM RAT

e ndoplasmic ENOYL-COA HYDRATASE, retuclum protein 29 MITOCHONDRIAL PRECURSOR
(Erp29), mRNA.

2052 16190 NM 053961q Length = 4529 R.norvegicus]
[

Rattus norvegicus endoplasmic retuclum protein 29 (Erp29), mRNA.

2052 21355 NM 053961,l,y,zLength = 4529 ESTs j Rattus norvegicus ribosomal protein L6 R.norvegicus mRNA
(Rpl6), mRNA. for ribosomal 2055 15136 NM 053971as Length = 963 protein L6 Rattus norvegicus ribosomal protein L6 R.norvegicus mRNA
(Rpl6), mRNA. for ribosomal 2055 15135 NM 053971d Length = 963 protein L6 Rattus norvegicus eukaryotic t ranslation initiation factor 4E

( Eif4e), mRNA.
Length =

2056 1764 NM 053974h 1647 R.norvegicus mRNA
eIF-4E

Rattus norvegicus ADP-r ibosylation factor related protein 1 (Arfrpl),R.norvegicus (Sprague mRNA. Dawley) ARP1 2057 1292 NM 053980 Length = 943 mRNA for ARF-related I rotein Rattus norvegicus ribosomal protein Sl5a R.norvegicus mRNA
(RpslSa), for ribosomal 2058 15468 NM 053982q mRNA. Length protein S15a = 449 Rattus norvegicus histone, family 3B (H3f3b), 2059 15642 NM 053985GeneralmRNA. Length R.norvegicus mRNA
= 1107 for histone H3.3 Rattus norvegicus antigen (collagen type I

r eceptor, thrombospondin r eceptor)-like Rat lysosomal membrane 2 (Cd3612), protein 2060 21066 NM 054001 mRNA. Length LIMPII) mRNA, com t = 1938 ( lete cds Rattus norvegicus Rgc32 protein (Rgc32),Rattus norvegicus mRNA. RGC-32 (RGC-32) 2061 17326 NM 054008o Length = 889 mRNA, complete cds Rattus norvegicus Rgc32 protein (Rgc32),Rattus norvegicus mRNA. RGC-32 (RGC-32) 2061 17327 NM 054008cc Len th = 889 mRNA, com lets cds Rattus norvegicus Rgc32 protein (Rgc32),Rattus norvegicus mRNA. RGC-32 (RGC-32) 2061 17329 NM 054008g,o,ccLength = 889 mRNA, com lets cds Rattus norvegicus proteasome (prosome, macropain) subunit, beta t ype 6 (Psmb6), mRNA.

2062 25253 NM 057099,I,m,p,zLength = 760 ~

Rattus norvegicus proteasome (prosome, macropain) ESTs, Highly similar subunit, beta to t ype 6 (Psmb6),PROTEASOME DELTA
mRNA. CHAIN

2062 22849 NM 057099,l Length = 760 PRECURSOR R.norvegicus j Rattus norvegicus A kinase ( PRKA) anchor Rattus norvegicus protein PKC binding ( gravin) 12 protein and substrate (Akapl2), mRNA, mRNA.

2063 19657 NM 057103b,cc Len th = 5236 complete cds Rattus norvegicus UDP

glycosyltransferase 1 family, polypeptide ESTs,UDP-glucuronosyltransferase A6 (Ugtia6), 1 2064 5492 NM 057105w mRNA. Length amil , member 1 = 1593 f Rattus norvegicus UDP-Rattus norvegicusglucuronosyltransferase glycosyltransferasemRNA, complete cds,UDP-1 family, polypeptide glucuronosyltransferase A6 (Ugt1a6), 1 family, 2064 15126 NM 057105r mRNA. Len th member 1 = 1593 TABLE MMARY Atty. Docket No.
1: 44931-5U89W0 SU

__ -__ Doe. No. 1798397.

f~, Sequence GenBank Model Ace ID No: dentifierRef. Seq Code Gene Name Unige,"~ne Cluster I IU '~~'~~.,, Tittle Rattus norvegicus UDP-Rattus norvegicusglucuronosyltransferase glycosyltransferasemRNA, complete 1 family, cds,UDP-polypeptide glucuronosyltransferase A6 (Ugtla6), 1 family, 2064 5125 NM 057105s mRNA. Length member 1 1 = 1593 Rattus norvegicus peroxiredoxin Rat mRNA for HBP23 1 (Prdx1), (heme-binding 2066 15391 NM 057114n mRNA. Len th protein 23 kDa), = 882 complete cds Rattus norvegicus protease ( prosome, macropain)Rattus norvegicus 26S mRNA for subunit, ATPaseproteasomal ATPase 1 (Psmc1), (S4), complete 2067 727 NM 057123m mRNA. Length ds = 1556 c Rattus norvegicus pyrimidinergic receptor P2Y, G-protein coupled,Rat mRNA for novel 6 (P2ry6), G protein-coupled 2068 915 NM 057124s mRNA. Length P2 receptor, complete = 1922 cds Rattus norvegicus phosphoribosyl pyrophosphate Rattus norvegicus synthetase- mRNA for 41-kDa associated phosphoribosylpyrophosphate protein 2 ( Prpsap2), mRNA.synthetase-associated Length = protein, 2069 15151 NM 057131k 1612 c om lete cds Rattus norvegicus cysteine-r ich protein R.norvegicus mRNA
3 (Csrp3), for muscle LIM

2070 1892 NM 057144b mRNA. Length rotein = 853 Rattus norvegicus X-prolyl aminopeptidase ( aminopeptidase P) 2, membrane-boundRattus norvegicus membrane-bound ( Xpnpep2), mRNA.aminopeptidase Length = P mRNA, complete 2071 12333 NM 057155f 2828 c ds Rattus norvegicus X-prolyl aminopeptidase ( aminopeptidase P) 2, membrane-boundRattus norvegicus membrane-bound ( Xpnpep2), mRNA.minopeptidase P
Length = a mRNA, complete 2071 12331 NM 057155v,General2828 c ds Rattus norvegicus X-prolyl aminopeptidase ( aminopeptidase P) 2, membrane-boundRattus norvegicus membrane-bound ( Xpnpep2), mRNA.minopeptidase P
Length = a mRNA, complete 2071 12332 NM 057155f,General2828 c ds Rattus norvegicus phospholipid Rattus norvegicus scramblase phospholipid ( Plscrl ), mRNA.cramblase PLSCR
Length = s mRNA, complete 2072 17477 NM 057194a,General1569 c ds Rattus norvegicus 2,4-dienoyl CoA Rattus norvegicus reductase mRNA for 2,4-1, mitochondrial ienoyl-CoA reductase (Decr1), d precursor, 2073 15408 NM 057197,t mRNA. Length om lets cds = 1109 c Rattus norvegicus 2,4-dienoyl CoA Rattus norvegicus reductase mRNA for 2,4-1, mitochondrial ienoyl-CoA reductase (Decr1), d precursor, 2073 15409 NM 057197t mRNA. Length omplete cds = 1109 c Rattus norvegicus phosphoribosyl pyrophosphate amidotransferaseRattus norvegicus (Ppat), mRNA for 2074 7866 NM 057198h mRNA. Len th mido hos horibos = 2934 a Itransferase TABLE MMARY Atty. Docket No.
1: 44921-5U89W0 SU

Doe. No. 1798397.1 Sequence GenBank Model ~cel '1U dentifierRef S,eqi~lUCode Gene Narne ~Uenigene Cluster No: ~ Tittle I

Rattus norvegicus tropomyosin non-muscle isoform NM1 (TPM-gamma) Rattus norvegicusmRNA, complete cds,Rattus t ropomyosin norvegicus tropomyosin 3, gamma non-muscle ( Tpm3), mRNA. isoform NM3 (TPM-gamma) Length = mRNA, 2075 4125 NM 057208h,j, 101 com lete cds 1 ,z Rattus norvegicus synaptic vesicle glycoprotein 2 a ( Sv2a), mRNA. Rattus norvegicus Length = synaptic vesicle 2076 743 NM 057210k,s 3844 protein (SV2) mRNA, 1 complete cds Rattus norvegicus ribosomal protein S23 R.norvegicus (Sprague-Dawley) (Rps23), mRNA.

2077 0498 NM 078617a Length = 432 ribosomal protein 1 S23 mRNA

Rattus norvegicus Smhs1 protein (Smhs1), mRNA.

2078 8820 NM 080399n Length = 1107 ESTs Rattus norvegicus ATP-binding cassette, sub-family C (CFTR/MRP), Rattus norvegicus member 3 mRNA for multidrug ( Abcc3), mRNA. resistance-associated Length = protein (MRP)-2079 5701 NM 080581',m, 5174 like protein-2 MLP-2), 1 ,z complete cds Rattus norvegicus ATP-binding cassette, sub-family C (CFTR/MRP), member 3 ( Abcc3), mRNA.
Length =

2079 20105 NM 080581as 5174 ESTs Rattus norvegicus N-ethylmaleimide sensitive f usion protein attachment protein alpha Rattus norvegicus (Napa), mRNA. mRNA for alpha-2080 6109 NM 080585c Length = 1505 soluble NSF attachment 1 rotein Rattus norvegicus Neuroblastoma RAS viral (e-r as) oncogene homolog ( Nras), mRNA. R.norvegicus N-ras Length = gene for p21 2081 1757 NM 080766d 3350 protein Rattus norvegicusRattus norvegicus nuclear ovalbumin r eceptor subfamilyupstream promoter 2, group beta nuclear F, member 2 receptor rCOUPb (Nr2f2), mRNA.mRNA, complete 2082 7108 NM 080778y Length = 1572 cds Rattus norvegicus cyclin-dependent kinase inhibitor 1A (P21) (Cdknla),Rattus norvegicus mRNA. p21 (WAF1) 2083 32 NM 080782k Length = 495 mRNA, complete cds Rattus norvegicus cyclin-dependent kinase inhibitor 1A (P21) (Cdknla),Rattus norvegicus mRNA. p21 (WAF1) 2083 33 NM 080782I Length = 495 mRNA, com late cds Rattus norvegicus t hioredoxin-like (32kD) ( Txnl), mRNA. ESTs, Highly similar Length = to thioredoxin-2084 20122 NM 080887General1061 related protein (M.musculus Rattus norvegicus selenium binding proteinESTs, Moderately 2 (Selenbp2), similar to selenium-2085 6143 NM 080892a mRNA. Length binding protein = 1685 H.sapiens Rattus norvegicus hypoxia i nduced gene ESTs, Moderately 1 (Hig1 ), similar to AF077034 2086 9952 NM 080902h mRNA. Length 1 HSPC010 [H.sa = 355 lens]

Rattus norvegicus membrane-associated protein 17 ESTs, Moderately (Mapl7), mRNA.similar to DD96 2087 17546 NM 130401b Len th = 816 homolog R.norve icus TABLE MMARY Atty. Docket No.
1: 44931-5U89W~
SU

Doe. No. 1798397.1 Sequence GenBank ModelI ' Accl ID No. dentifierRef. $eq Code,.,,Gene Name Un,ige~,ne Cluster I IU Tittle Rattus norvegicus coronin, actin binding protein 1A

(Corola), mRNA.ESTs, Weakly similar Length = to coronin-like 2088 21695 NM 130411c,x 1386 protein [R.norvegicus]

Rattus norvegicus annexin A7 (Anxa7), ESTs, Weakly similar mRNA. Length to ANX4 RAT
=

2089 21391 NM 130416x,General2912 ANNEXIN IV R.norvegicus Rattus norvegicus proteasome (prosome, macropain) 26S subunit, non ATPase, 9 (Psmd9), mRNA.

2090 20694 NM 130430GeneralLength = 1448 EST

Rattus norvegicus proteasome (prosome, macropain) 26S subunit, non ATPase, 9 (Psmd9), mRNA.

2090 19818 NM 130430cc Length = 1448 EST

Rattus norvegicus proteasome (prosome, macropain) 26S subunit, non ATPase, 9 (Psmd9),mitochondrial H+-ATP
mRNA. synthase alpha 2090 18810 NM 130430e,s Length = 1448 subunit Rattus norvegicus acetyl-Coenzyme A
acyltransferase 2 (mitochondrial 3-oxoacyl-Coenzyme A
thiolase) (Acaa2), mRNA.
Length =

2091 18293 NM 130433q 1619 Rat mRNA for 3-oxoac I-CoA thiolase 2092 25064 S45392 a,n 2093 3244 S63519 a ESTs 2094 25501 S63521 q Rat brain glucose-transporter protein 2095 16248 S68135 h mRNA, complete cds ESTs, Weakly similar to HS9B RAT

HEAT SHOCK PROTEIN

2096 18647 S69316 BETA [R.norvegicus]

ESTs, Weakly similar to ABD4 MOUSE ATP-BINDING
CASSETTE, SUB-FAMILY D, MEMBER

2097 24351 S74257 v [M.musculus]

2098 25066 S75280 d ESTs, Highly similar to K2C8 RAT

j,I,m,x,y,G KERATIN, TYPE II
CYTOSKELETAL

2099 1460 S76054 eneral 8 R.norvegicus]

2100 25539 S76742 v 21 16400 S76779 c Rat apolipo rotein 1 a myna _ ESTs, Highly similar _ to MLES RAT

MYOSIN LIGHT CHAIN
ALKALI, SMOOTH-MUSCLE ISOFORM

2102 24469 S77858 n [R.norvegicus]

2103 25545 S77900 k,s 2103 21583 S77900 k ESTs 2104 10260 S81497 s ESTs histamine N-2105 3609 S82579 k meth Itransferasehistamine N-meth Itransferase Rattus norvegicus clone 15 polymeric immunoglobulin receptor mRNA, 2106 111 002506 a 3'UTR microsatellite repeats Rattus norvegicus Sprague Dawley a,q, protein kinase C receptor mRNA, 2107 14959 003390 General complete cds Rattus norvegicus Sprague-Dawley fibrinogen B beta chain mRNA, 2109 2010 005675 b,x,bb complete cds 2110 15462 006230 d rotein S rotein S

Y F?.v TABLE MMARY F~~,j' Atty. Docket No.
1: 44931-5U89W0 SU

tJoc. No. 1798397.1 I
Sequence GenBank Model Acc/
' tD No. IdentifierRef. Seq Code Gene Name Unigene Cluster IDr ~ Title 2112 1583 007201 s,GeneralAsparagine Asparagine s nthetase s nthetase Rattus norvegicus New England Deaconess transcription factor mRNA, 2113 627 009229 h artial cds Rattus norvegicus interferon inducible protein 10 (1P-10) mRNA, complete 2114 809 017035 General cds mini chromosome maintenance mini chromosome deficient maintenance 6 (S.

2115 16675 017565 k,x,bbcerevisiae) deficient 6 (S.
cerevisiae) 2116 25587 020110 r Rattus norvegicus nuclear receptor 2117 90 020796 r Rev-ErbA-beta mRNA, partial cds 2118 25589 021718 h,aa 2119 22196 021719 h ESTs Rattus norvegicus RNA helicase with arginine-serine-rich domain mRNA, 2120 17118 025746 s complete cds Rattus norvegicus UDP-glucuronosyltransferase mRNA, 2121 1537 027518 g,h,n complete cds Rattus norvegicus Na+/Pi 2122 1558 028504 bb cotrans orter-1 mRNA, complete cds Rattus norvegicus B/K protein mRNA, 2123 16193 030831 n com lete cds 2124 17480 031598 z R.norvegicus mRNA
for RTI.Ma Rattus norvegicus retinol dehydrogenase type II mRNA, 2125 18302 033500 General com lete cds 2126 25599 034897 y Rattus norvegicus GTP-binding 2127 1394 037099 h protein rab 3C) mRNA, complete cds EST, Weakly similar to actin-filament binding protein Frabin [ R.norvegicus],Rattus norvegicus cytosolic phospholipase A2 mRNA, 2128 244 038376 n complete cds Rattus norvegicus Cys2/His2 zinc f inger protein (rKr1 ) mRNA, complete 2129 1623 041164 h c ds f,t,x, 2130 15851 042719 GeneralComplement Complement component component 4 Rattus norvegicus apoptosis-r egulating basic protein mRNA, 2131 17886 047315 s,z c om lete cds i,t, estrogen-responsive uterine 2132 21654 053184 Generaltranscript strogen-res onsive e uterine transcript Rattus norvegicus FceRl gamma-c hain interacting protein SH2-B
(SH2-2133 1439 057391 w B) mRNA, complete cds solute carrierolute carrier family family 16 16 s (monocarboxylicmonocarboxylic acid ( acid transporters), 2134 725 062316 bb traps orters),member 7 mem b,cc, 2137 2153 075404 General ESTs Rattus norvegicus cell adhesion r egulator (CAR1 ) mRNA, complete 2139 4956 076714 j, c ds 2140 4477 077829 I,m ESTs Rattus norvegicus RCL (Rcl) mRNA, 2141 21703 082591 z c om late cds Rattus norvegicus putative cell 2142 977 089744 s s urface antigen mRNA, complete cds 2143 23282 090725 h lipo rotein-bindingipoprotein-bindin rotein l rotein Rattus norvegicus liver mRNA, 2144 22005 096490 m c om late cds TABLE MM~4RY /Att~y. Docket 1: No. 44921-5U89W0 SU

Doe. No. 1798397.1 ,i y 'Sequence GenBank Model Aeel 1D No. dentifierRef. Seq Code Gene Name Unigene Csluster I . If7 Title Aldolase B,fructose-2146 819 X02284 j,z biphosphate Aldolase B, fructose-biphosphate Aldolase B, fructose-2147 818 X02291 e,j,zbiphosphate Aldolase B, fructose-biphosphate glutathione S-transferase, pi 2148 20818 X02904 n,q 2 glutathione S-transferase, pi 2 2149 16401 X04979 c Rat apolipo rotein a mrna Pyruvate kinase, liver and 2150 20513 X05684 o,r RBC P ruvate kinase, liver and RBC

2151 25084 X06769 cc 2152 672 X13722 h Rat mRNA for LDL-receptor 2153 25675 X14181 n ESTs, Highly similar to 60S

RIBOSOMAL PROTEIN

2153 20810 X14181 n,q,w[ R.norvegicus]

ESTs, Highly similar to RL26 RAT 60S

RIBOSOMAL PROTEIN

2154 18541 X14671 y [ R.norvegicus]

2155 25679 X15013 q ESTs, Highly similar to RL7A_HUMAN

2155 19244 X15013 c,q,w R.norvegicus ESTs. Highly similar to RS16_HUMAN

2156 15626 X17665 a [ R.norvegicus]

phospholipase phospholipase A2, A2, group group IIA
IIA

2157 1893 X51529 t (platelets, platelets, synovial s novial fluid)fluid) ( 2158 25686 X51536 bb ESTs, Highly similar to RS3 MOUSE

2158 10819 X51536 aa,bb R.norvegicus]

ESTs, Highly similar to RL9 RAT 60S

RIBOSOMAL PROTEIN

2159 18250 X51706 a,q,wribosomal proteinR.norvegicus]
L9 [

ESTs, Highly similar to RS19 RAT

2160 20872 X51707 a ribosomal proteinR.norvegicus]
S19 [

2161 516 X52711 c Rat mRNA for Mx1 protein Rattus norvegicus ribosomal protein 2163 20427 X53378 w S13 (RPS13) mRNA, 3' end ESTs, Highly similar to 60S

RIBOSOMAL PROTEIN

2164 8606 X53504 General[ R.norve icus]

d,u, Rat mRNA for preprocathepsin D (EC

2165 463 X54467 General 3.4.23.5) ESTs, Highly similar to 60S ACIDIC

RIBOSOMAL PROTEIN

2166 24577 X55153 a,v R.norvegicus LOCUS NOTCH HOMOLOG

2167 0344 X57405 ',m Drosophila R.norvegicus]
1 Notch homolog ESTs, Highly similar to RS18_HUMAN

2168 5106 X57529 g,n, R.norvegicus]

2169 5667 X58200 ,bb ribosomal protein ESTs, Highly similar to RL23_HUMAN

2169 8611 X58200 a,v ribosomal roteinR.norvegicus]
1 L23 ( R.norvegicus ASI
mRNA for mammalian equivalent of bacterial 2170 7175 X58389 w l ar a ribosomal 1 subunit rotein 2171 25702 X58465 w 2171 0109 X58465 c,q Ribosomal roteinRibosomal rotein c,i,aa, 2172 25705 X59375 General TABLE M AR Atty. Docket o.
1: 44931-5U89W0 SU

_ Doe. No. 1798397.1 Sequence GenBank Model Ace/-ID No. dentifierRef. Seq Code Gene Name l~l ~igene Cluster I ID Title 2173 25709 X59737 a 2174 18354 X59859 Generaldecorin decorin 2174 18355 X59859 t decorin decorin Rattus norvegicus interferon-inducible protein variant 10 mRNA, complete 2175 21657 X61381 General cds bb, 2176 25718 X62145 Generalribosomal rotein LS

ESTs, Highly similar to RL8_HUMAN

L

2176 15875 X62145 a,q,vribosomal rotein[R.norvegicus]

ESTs, Highly similar to RL3 RAT 60S

RIBOSOMAL PROTEIN

2177 13646 X62166 bb R.norvegicus ESTs, Highly similar to HIGH

MOBILITY GROUP
PROTEIN HMG-Y

2179 16012 X62875 m,s,z [M.musculus]

2180 25730 X63369 cc 2181 25089 X63594 General cc, 2181 25090 X63594 General ESTs, Highly similar to RL2B_HUMAN

2182 20844 X65228 n,w [R.norvegicus]

2183 20879 X65296 ',y carboxylesterasecarbox lesterase 2184 25736 X68782 c 2185 16426 X70369 c procollagen, procollagen, type t pe III, III, alpha 1 alpha 1 2186 16300 X70706 a plastin 3 (T-isoform)lastin 3 (T-isoform) 2187 24232 X75207 c c clip D1 c clin D1 R.norvegicus (Sprague Dawley) alpha 2188 16272 X76456 n,p albumin gene 2189 25741 X76489 a prolyl 4-hydroxylase alpha 2190 23302 X78949 h subunit prol I 4-h drox lase alpha subunit 2191 25747 X81448 General ESTs, Highly similar to K1 CS RAT

KERATIN,TYPEICYTOSKELETAL

2192 24115 X81449 a 19 [R.norve icus]

2193 25754 X89696 g 2194 25097 X90642 ,z ESTs, Highly similar to RADIATION-cc, INDUCIBLE IMMEDIATE-EARLY

2195 2978 X96437 General GENE IEX-1 [M.musculus]

Rattus norvegicus mRNA Best5 2197 594 Y07704 c protein 9.P, 2198 25777 Y08355 Generaloxidative stressoxidative stress induced induced Rattus norvegicus mRNA for putative bb, i ntegral membrane transport protein 2199 5986 Y09945 General (USTIr Rattus norvegicus mRNA for D6.1A

2200 20890 Y13275 k protein 2201 21914 Y13336 d Rattus norvegicus DAD-1 gene R.norvegicus mRNA
encoding 45kDa protein which binds to heymann 2202 06 211995 o,General nephritis antigen 4 gp330 2203 8352 212298 t decorin decorin 2204 7481 249761 k R.norvegicus mRNA
1 for RTl.Ma ESTs, Moderately similar to T17342 hypothetical protein DKFZp586K1924.1 [H.sapiens],Heat 2205 8664 275029 r,v Heat shock shock protein 70-1 protein 70-1 2206 459 AA964755 cc ESTs 2207 3830 AA956638 as ESTs 2208 100 X73524 x desmin desmin TABLE MMARY Atty. Docket No.
1: 44921-5U89W0 SU

Doe. No. 798597.1 5equenee GenBank Model Aee/

ID No. dentifierRef. Seq Code Gene Name Unigene Cluster I ID Tittle Bone morphogenetic protein 2209 439 222607 w 4 Bone morphogenetic protein 4 ESTs, Moderately similar to T17342 hypothetical protein DKFZp586K1924.1 [H.sapiens],Heat 2210 8665 A1071965 v Heat shock shock protein 70-1 protein 70-1 2211 155 U32681 cr -ductin crp-ductin t Rattus norvegicus mRNA for thiol-specific antioxidant protein (1-Cys 2212 19252 AA892041 s HMm:peroxiredoxinperoxiredoxin) Rat mitochondrial 3-hydroxy-3-methylglutaryl-CoA
synthase mRNA, 2213 15582 AI232320 q complete cds Epoxide hydrolase ( microsomal Epoxide hydrolase xenobiotic 1 (microsomal 2214 17541 M26125 n hydrolase) xenobiotic h drolase) Rat Ly6-B antigen mRNA, complete 2215 18609 M30689 cds i 2216 6262 A1177125 g ESTs 2217 23859 A1072161 ESTs f Glutathione-S-transferase,Glutathione-S-transferase, mu type 2 2218 21011 H32189 a mu pe 2(Yb2 (Yb2) 2220 2572 A1177143 b ESTs 2221 25419 M22922 a TABLE THV1'(fAlfS Atty. ocket No. 44'921-508911f10 2: D Doe. No. 1798397.1 PA enB'ank dentifierAcel odel Sequence Ref. Seq. Code athway4s, 1D No. ID No.

1 6949 AA012785 q 2 25098 AA108277 h,v 3 17312 AA108308 r 6049 AA685178 y 6 4426 AA685974 I,m 7 21815 AA686423 g 8 1600 AA686470 i 8 1599 AA686470 i 9 21997 AA799325 a 18396 AA799330 v 11 6581 AA799412 f,1 12 16538 AA799449 k 13 23294 AA799472 a 14 18290 AA799497 r 18981 AA799523 a 16 20843 AA799545 h 17 16993 AA799560 b 18 16576 AA799570 d 19 18361 AA799591 i 17712 AA799598 z 22 18346 AA799718 f 24 11687 AA799732 w 18349 AA799744 a 26 17494 AA799751 n 27 18360 AA799771 General 28 18880 AA799801 w 29 20998 AA799803 z 21006 AA799861 c 31 15011 AA799893 General 32 20811 AA799899 a 33 23202 AA799971 General 34 4832 AA800190 b 21656 AA800202 d 36 18433 AA800218 j,y,z 37 6386 AA800235 a 38 18442 AA800258 h,k 39 21092 AA800380 y 17325 AA800587 General 41 13930 AA800613 cc,General 42 21372 AA800693 v 42 21373 AA800693 s 43 18161 AA800701 k 44 6595 AA800753 w 13348 AA800928 General 46 23115 AA801165 0, 47 12399 AA801307 General 48 7543 AA801395 General 49 24237 AA817726 t,General 51 5985 AA818005 g 52 11338 AA818016 x 53 2845 AA818026 k,General 54 16756 AA818089 i,k,General 17771 AA818224 e,g,p,General 56 6522 AA818261 g,m 58 7806 AA818421 b,aa 59 8237 AA818512 v 17434 AA818574 h 61 8728 AA818615 General 62 j 6054 AA818658 b,v,cc,General T~B'LE TIiInIAYS Atty. Docket No. 44'921-5U'8'91'NO
2: _ Doc. No. 179839 .1' PA GenBank Accl _ dentifierRef. Seq. odel Pathways , y '~t Sequence ID No. Code ID No.

63 11590 AA818721 d 64 4291 AA818741 q,General 65 4330 AA818747 o,General 66 19723 AA818761 v,General 67 13684 AA818770 h,j,l,m 68 6322 AA818801 k 69 7690 AA818875 General 70 4952 AA818907 q,General 71 6094 AA818911 t 72 10985 AA818998 o,General 73 6120 AA819008 t 74 2586 AA819081 c 77 24721 AA819306 d,w 78 6250 AA819376 o,y j j 82 6551 AA819558 t 83 6723 AA819653 r 84 14958 AA819744 as 85 19433 AA819776 v 86 6204 AA819889 as 87 22820 AA848315 General Purine metabolism 88 6614 AA848389 bb 89 21125 AA848437 General 90 23504 AA848496 q 91 18532 AA848675 g 92 21140 AA848738 c 94 22923 AA848929 g 95 17339 AA849497 General I

97 21275 AA849796 ,I,m,General i 98 16678 AA849827 as 99 8515 AA849917 a 100 18447 AA849939 General 101 12130 AA850037 p 102 23981 AA850040 x,aa t 105 2637 AA850893 x 106 22093 AA850909 d 107 21766 AA850916 c 108 2847 AA850919 w 109 12162 AA850975 h 110 9514 AA850978 General 111 3924 AA851017 e,q 111 3925 AA851017 o,General 112 4490 AA851184 a,k 113 19187 AA851230 General 114 9189 AA851237 c 115 5386 AA851241 m 116 21462 AA851261 g,I,General 117 21471 AA851343 General Oxidative phosphorylation,Ubiquinone 118 6902 AA851379 p biosynthesis 119 23376 AA851392 ,x i x 120 3349 AA851417 General 121 1527 AA851733 ,u 2 r 122 048 AA851814 ,o,u,General 4 i 123 0561 AA851871 bb 124 7411 AA858621 ,y 1 - j 125 _ AA858636 ,s,x,bb 1 801 k TAf3'LETIiINAIfS Atty. Docket No. 44'921-5U'8'9f1f10 2: Uoc. No. 17 8397.1 PA enBank Acc/
entifierRef. Seq. odel Pathways Sequence18350 I~ No. Code ID No. AA858674 p I

127 19484 AA858693 a 128 6360 AA858696 d 129 17334 AA858704 p 130 6380 AA858758 q 131 13219 AA858759 a 132 6384 AA858788 ,m,General I

134 13412 AA858830 p f t Alanine and aspartate 137 5867 AA858953 v,Generalmetabolism,Aminoacyl-tRNA
biosynthesis r t 140 17361 AA859114 o,General 141 21025 AA859241 General 142 10076 AA859271 c 143 21791 AA859333 k 144 16314 AA859348 cc,General f r 147 19894 AA859581 s 148 14353 AA859585 h 149 16318 AA859648 h 150 17316 AA859652 General 151 19067 AA859663 n,q 152 22406 AA859680 n 153 20599 AA859690 x 154 14261 AA859693 a 155 14138 AA859700 v Porphyrin and chlorophyll metabolism 155 14139 AA859700 v Porphyrin and chloroph II metabolism I

158 22385 AA859805 b,k 159 22773 AA859885 n 160 22816 AA859898 k,x,z 161 11891 AA859926 x 162 23070 AA859942 k 163 23121 AA859948 k 164 23166 AA859954 cc,General 165 18468 AA859966 as 166 23336 AA859981 q I nositol phosphate metabolism 167 4222 AA860024 a,bb 168 13974 AA860030 u,x,General 169 7090 AA860039 x 170 23769 AA860055 k,x 171 16323 AA866240 w 172 4462 AA866264 General 173 15884 AA866276 k Phenylalanine metabolism,Tyrosine 174 17742 AA866302 c,y metabolism 175 16333 AA866414 a,h 176 18918 AA866444 p,q 177 16853 AA866454 ,l,m,y,z j 178 18995 AA866459 h,m 179 16013 AA866482 s r 181 16059 AA874857 h r f 184 16192 AA874995 w j 186 16312 AA875032 cc,General 187 20701 AA875097 b T~B'~E TFII~IfIAYS Atty. Dosk'et No. 4'4929-50'8'91N0 2: Doc. No. 1798397.1 PA enBank~4ccl entifierRef. Seq. odel Pathways Sequence6416 ID No. Code 'ID AA875098 bb -No.
I

189 6419 AA875102 bb 190 5313 AA875126 ,m,General 191 0936 AA875146 w 192 8084 AA875186 h 193 5371 AA875205 a 194 5401 AA875257 ,z 1 x Oxidative phosphorylation,Ubiquinone 195 5410 AA875268 p,s biosynthesis 1 f 197 5446 AA875327 ,w 1 s 198 7936 AA875495 b,General 199 7314 AA875509 ,1,m 1 i 200 24472 AA875523 k 1 j 202 5617 AA875620 General 202 5618 AA875620 General 203 5384 AA891041 ,cc,General f 204 24814 AA891209 ,p f 205 21930 AA891322 d 206 7225 AA891553 h 207 7522 AA891571 ,m j 208 9071 AA891578 b 209 19321 AA891666 a 210 17693 AA891737 ,l,m,n,y,z j 211 17256 AA891739 General 213 18269 AA891769 General 214 9905 AA891774 s,bb,General 215 17061 AA891812 d 216 7050 AA891824 h 217 4463 AA891831 General i 219 20523 AA891842 ,cc r 220 17779 AA891914 g,s,z 221 17438 AA891943 General 222 22862 AA891944 p 223 1159 AA891949 e,z 224 4473 AA891965 General 225 6362 AA892053 ,j,l,m f 226 9037 AA892066 y 227 19469 AA892112 General 228 14595 AA892128 o,t,v 229 16527 AA892154 cc 230 4482 AA892173 bb 231 20917 AA892238 h 232 2357 AA892268 d 233 18183 AA892271 h 234 6523 AA892299 d 236 13647 AA892367 a 237 3473 AA892378 v 238 17682 AA892382 ,p,s,x, j General Carbon fixation,Fructose and mannose metabolism,Glycolysis 39 20 A892395 ,s /
Gluconeogenesis,lnositol metabolism,Pentose phosphate cycle 240 14754 AA892414 a f 242 16469 AA892462 p 243 13609 AA892468 ,General i 243 13610 AA892468 n,v,General 244 9254 AA892470 n,u 245 11991 AA892483 s f TAI3'LETIifNIAYS Atty. ocket No. 44921-5U8~9fNO
2: D Doc. No. 1798397.1 PA enl3ank entifierAccl odel Code Sequence11994 Ref. Seq. as athways ID No. ID No.

248 23888 AA892520 w 248 23889 AA892520 h 250 15154 AA892532 p 251 17468 AA892545 r 252 11203 AA892554 f,h 253 18906 AA892561 a,bb,General 254 19327 AA892562 f,j,y,z 255 18274 AA892572 p 256 4512 AA892578 cc 257 15876 AA892582 w 258 19085 AA892598 General 258 19086 AA892598 General 260 20088 AA892666 a,n 261 23783 AA892773 n 262 17549 AA892776 f,z 263 13542 AA892798 b Glyoxylate 264 22537 AA892799 General and dicarboxylate metabolism,Pyruvate metabolism Glyoxylate 264 22539 AA892799 v and dicarboxylate metabolism,Pyruvate metabolism Glyoxylate 264 22538 AA892799 General and dicarboxylate metabolism,Pyruvate metabolism 265 6951 AA892820 h 266 23322 AA892821 j,z 267 17923 AA892843 f 268 22871 AA892859 m 269 9053 AA892861 p,v,General 270 16482 AA892940 w 271 12020 AA893035 j,y 272 3863 AA893060 General 273 13332 AA893080 i,General 274 21305 AA893082 General 275 16591 AA893191 j,z 276 17447 AA893192 General 277 3876 AA893205 n 278 3878 AA893230 General 279 20986 AA893242 q Fatty acid metabolism 280 16168 AA893280 i,z,General 281 3886 AA893289 j,m,y 282 15209 AA893327 y 283 17800 AA893436 cc 284 17836 AA893626 h 285 9084 AA893717 x 286 22731 AA893743 d Aminoacyl-tRNA
287 12031 AA893860 v biosynthesis,Glycine, serine and threonine metabolism 288 17897 AA893905 k 289 3447 AA893982 d 290 22583 AA894009 n 291 10540 AA894027 j 292 4569 AA894059 x 293 18419 AA894130 d 294 17336 AA894297 j 295 19120 AA894318 f,j 296 19762 AA899113 i 297 18286 AA899219 a 298 22051 AA899498 w 298 22052 AA899498 q 299 21628 AA899563 as 300 4262 AA899590 i TABLE TIiIIUAIfS A~tty. No. 44921-5U'8'91N0 2: Docket Doe. No.
PA enf3ank 1798397.1 entifierAcef odel Gode Sequence4661 Ref. Seq. t,Generalathway',s !ID ID N~o.' No. AA899709 I

302 21354 AA899721 q 303 7905 AA899762 General 304 5231 AA899840 r 305 23778 AA899854 c,k,x 306 22060 AA899898 b 307 9114 AA899951 v,General 308 8988 AA900148 f 309 11841 AA900247 v 310 4725 AA900290 cc 311 4747 AA900465 General 313 3822 AA900863 b,g,General 315 12420 AA901017 b 316 4849 AA901155 s 317 3959 AA901338 General 318 22846 AA923982 a,d 319 4895 AA923999 k 320 21546 AA924188 cc,General 321 24192 AA924210 n,General 322 4933 AA924301 g,I,General 323 4944 AA924405 (,General 324 4948 AA924428 r 325 4949 AA924432 General 326 18891 AA924598 a Glyoxylate 327 22540 AA924630 v,Generaland dicarboxylate metabolism,Pyruvate metabolism Glyoxylate 327 22541 AA924630 General and dicarboxylate metabolism,Pyruvate metabolism 328 14759 AA924766 k 329 23123 AA924794 x 330 4067 AA924813 g,p 331 2888 AA924902 r,General 332 18130 AA924964 d 333 23141 AA925019 r 334 23195 AA925026 General 335 21458 AA925049 f,aa,General 336 5073 AA925061 m 337 14790 AA925087 o,General 338 5089 AA925126 g 339 23261 AA925145 k,General 340 17363 AA925150 a 342 23159 AA925318 a 343 21500 AA925353 k 344 22479 AA925418 t 345 21151 AA925539 b 346 16944 AA925541 f 346 16945 AA925541 t 347 17514 AA925554 bb Oxidative phosphorylation 348 5183 AA925662 i,General 349 23189 AA925844 r 350 23190 AA925863 as 351 5252 AA926051 General 352 22967 AA926080 h,cc 353 17157 AA926129 b 354 13411 AA926196 u,General 355 5295 AA926247 General 356 22928 AA926262 General 357 8948 AA926316 r 358 21798 AA926365 as 359 9942 AA942697 s 360 6039 AA942716 x,General TAB't!ETIiIIUAYS Atty. Docket No. 44921-5U8~911V0 2: Doc. No. 1798397.1 PA enBank entifierAccl odel CodePathways Sequence11174 Ref. Seq. g,o,w ID No. ID No.

362 23005 AA942770 g 363 21318 AA942774 General 364 6615 AA942889 v 365 6691 AA943028 c 366 22142 AA943066 p 367 21993 AA943149 v,General 368 9061 AA943508 General 369 24390 AA943531 b,j,n,y 370 13976 AA943532 f,s,x 371 22248 AA943537 cc,General 372 22257 AA943558 m 373 12673 AA943773 u,cc,General 374 13641 AA944154 a 375 2658 AA944155 f 376 12770 AA944161 d 377 20903 AA944180 i,x 378 13507 AA944244 v 379 15596 AA944353 General 380 22681 AA944413 i,v,cc,General 381 6711 AA944439 General 382 14763 AA944481 i,q,General 383 22466 AA944605 h 384 12301 AA944727 b Purine metabolism,Pyrimidine 385 7023 AA944792 d,m,aa metabolism,RNA polymerase 386 22536 AA944803 bb 387 22501 AA944811 g,1 388 23967 AA944831 s 389 26084 AA944922 i 390 11974 AA944958 General 391 22547 AA944970 as 392 22554 AA945076 z,General 393 14352 AA945181 General 395 1798 AA945569 General 396 22050 AA945604 i.aa 397 19731 AA945615 d,o 398 22612 AA945624 a,General 399 22618 AA945656 as 400 11871 AA945679 v 401 22656 AA945818 General 402 6720 AA945828 p 403 22351 AA945867 m 404 22665 AA945877 f 405 24243 AA945950 b 406 22689 AA945962 General 407 22692 AA945986 d 408 22696 AA945996 c,General 408 22697 AA945996 c,o 409 22658 AA945998 w 410 20832 AA946040 s Oxidative phosphorylation 411 8337 AA946046 General 412 825 AA946108 General 413 8639 AA946221 e,cc,General 414 23237 AA946224 f 415 5600 AA946250 o,aa 416 9387 AA946275 t 417 6351 AA946344 d 418 22057 AA946348 a 419 22069 AA946349 as 420 3962 AA946351 General 421 8280 AA946361 g 422 8944 AA946391 v TABLE TIiIIUAYS Atty. ~ cket No. 44'921-SU'8~9f1f10 2: Doc. No. 1798397.1 PA enBank t entifierAccl odel Pathways Sequence21410 Ref. Seq. Code ID No. ID No.

425 643 AA946439 0, 426 20736 AA946443 x r 428 21947 AA946451 bb 429 17499 AA946467 General 430 1809 AA946503 x,General f 432 23471 AA955162 General 433 9452 AA955206 b,General 434 23512 AA955282 General 435 22596 AA955298 General 436 23283 AA955391 h 437 23546 AA955393 General 438 12404 AA955408 b 439 23626 AA955540 as 441 17540 AA955914 bb 442 24277 AA955962 General 443 19939 AA955980 General i 445 11050 AA956164 s,v 446 498 AA956278 a,General 447 23409 AA956294 q 449 23773 AA956476 ,x f 450 23799 AA956530 d 451 23800 AA956534 as 452 23834 AA956659 cc,General 453 16425 AA956688 ,x f 454 23847 AA956723 s 455 23852 AA956746 ,l,m,z j 456 5989 AA956907 g,s 456 5990 AA956907 General 457 23957 AA957123 u,General 458 22357 AA957264 General g,l,m,p,v,cc, 459 23314 AA957270 General 460 23995 AA957292 a,b Aminoacyl-tRNA biosynthesis,Glycine, 461 2702 AA957307 General serine and threonine metabolism 462 24040 AA957422 c 463 12478 AA957554 m 464 21306 AA957811 v t 466 24178 AA957905 d 467 17034 AA963071 a 468 24053 AA963092 General 470 2022 AA963259 g 471 2126 AA963488 d 472 24246 AA963703 b 473 2195 AA963746 General i 475 2282 AA964147 a 476 2284 AA964152 x 478 2350 AA964368 g,General 479 18830 AA964496 as 480 2392 AA964541 b 481 2395 AA964554 General 482 2410 AA964589 ,aa i t 484 2424 AA964617 g 485 3107 AA964687 General 486 2457 AA964752 q,t TABLE TIiINAIfS Atty. Docket No. 44'9'21-5U'8'9~IflO
2: Uoe. No. 1798397.1 P'A enBank Accl entifierRef. Seq. odel Fath'w,~ays Sequence6778 ID No. Code ID No. AA964763 b I

I

Glutamate metabolism,Glutathione 490 2469 AA964814 w metabolism 491 12561 AA964815 General 492 2326 AA964892 as 493 21339 AA964962 General 494 21390 AA964988 General 495 12569 AA965023 g 496 2583 AA965166 bb r 499 2905 AA996727 b,I,m,u,General 500 2915 AA996782 u,bb 501 2920 AA996813 d 502 19525 AA996856 aa,General 503 2984 AA997015 c 504 2986 AA997028 General 505 3145 AA997237 General 506 19249 AA997342 m 507 16883 AA997345 General 508 12598 AA997362 s 509 3470 AA997374 p t 511 3245 AA997608 General t 513 3269 AA997800 x,aa f 515 23992 AA998164 k,x 516 17470 AA998264 b 517 3773 AA998356 General 518 19623 AA998422 General 519 3572 AA998516 x 520 2782 AA998565 c 521 26119 AA998576 ,r,w,General i 522 22737 AA998660 as 523 3696 AA999030 a 524 3079 AA999169 k,x,General 525 3081 AA999171 e,p,r 526 3082 AA999172 General Glutamate metabolism,Purine metabolism 527 17337 A8000717 k 528 1535 AB000778 a 529 1382 AB002406 k 530 20184 AB003753 d 531 4312 AB010635 c,i,j,k,y,z 532 21666 AB012214 k Methionine metabolism 533 15772 AB015645 g 534 1183 AF013144 h 535 1582 AF015911 h,z 536 11483 AF020618 u,cc,General 537 20295 AF024712 as 538 19077 AF030358 y,z 539 23044 AF034218 General 540 25178 AF035955 d 541 1564 AF035963 x,bb,General f 543 21817 AF036537 k 544 21145 AF038571 General 545 22602 AF044574 General 546 13464 AF047707 h 547 24024 AF052695 x 548 12259 AF061266 h 549 4589 AF062389 y,z t TABLE TH1NAYS After. Docket No. 44'9'21-50'8911110 2: Doc. No. 1798397.1 PA enBan Accl entifierRef. Seq. Model Pathways Sequence15761 ID No. Code ID No. AF062741 a I

552 17426 AF073839 p 553 18615 AF074608 s 554 15797 AF084205 f 555 12932 AF102552 s 556 18603 A1007649 x 557 22733 A1007668 r 558 22746 A1007672 r 559 24109 A1007725 General 560 15848 A1007820 n,v 561 10108 A1007857 f 562 6804 A1007877 General 563 20099 A1007893 f,u 564 11368 A1007948 d 565 15849 A1008074 h 566 3121 A1008160 General 567 16646 A1008190 t 568 12683 A1008203 x 569 22018 A1008309 b 570 23917 A1008441 n 571 22599 A1008458 General 572 22698 A1008578 p,General 573 14405 A1008579 r,x 574 4086 A1008629 x 575 3808 A1008643 i,v,General 577 7785 A1008758 as 578 16701 A1008838 q 579 21789 A1008930 k 580 21895 A1008971 General 581 410 A1008974 i,aa,General 582 21632 A1009167 General 583 21596 A1009168 General 584 22801 A1009197 General 585 11876 A1009321 cc,General 586 2506 A1009341 General 587 6382 A1009362 General 588 14370' A1009427 k 589 19275 A1009460 x 590 4154 A1009467 g 591 3464 A1009589 cc 592 3926 A1009592 a 593 19358 A1009675 c 594 22545 A1009747 g 595 15089 A1009752 cc, General 596 5458 A1009756 h 597 6844 A1009770 e,r,cc 598 15627 A1009810 as 599 22619 A1009825 d 600 7857 A1009898 j,l,m,z 601 13259 A1009946 r 602 21105 A1010067 General 603 24627 A1010102 as 604 12716 A1010178 General 605 18757 A1010216 as 606 2912 A1010220 aa,General 607 3316 A1010237 t 608 15644 A1010256 General 609 657 A1010262 b 610 3271 A1010303 b 611 11081 A1010407 bb 612 16521 A1010470 c,s,t,GeneralPorphyrin and chlorophyll metabolism 613 6927 A1010542 General TA~BaLETFIIIfIAYS iKtty. Docket No. 44'9'21-5U8'91N0 2: Doc. No. 1798397.1 PA enBank Accl i entifierRef. Seq. odel Pathway',s Iv''' Sequence17524 I~ No. Code 'ID A1010568 a,j,y,General No.
I

615 6946 A1010642 n 616 23509 A1010962 as t 619 21779 A1011380 cc 621 12534 A1011460 cc 622 12629 A1011492 e,f f 624 3941 A1011598 General 625 17550 A1011607 ,General j 626 10636 A1011634 a 627 3995 A1011678 General 628 16112 A1011706 h 629 13354 A1011757 c 630 12745 A1011799 cc t 632 4205 A1011982 b 633 6518 A1012114 General 634 17407 A1012145 General r f 637 21796 A1012221 d,General 638 3981 A1012235 ,General i 639 6606 A1012308 ,r i 640 3417 A1012337 w 641 24200 A1012356 b,t,General 642 7471 A1012379 cc 643 7247 A1012438 g 644 7127 A1012464 p,General 645 3304 A1012471 b 646 2311 A1012485 as 647 20817 A1012589 g,n,q Glutathione metabolism 648 3493 A1012590 v,General 649 8975 A1012613 General j 651 21409 A1012637 General 652 8015 A1012638 as 653 8476 A1012647 w 654 4232 A1012958 e,p,General 655 23128 A1013011 General 656 20086 A1013260 General 657 11969 A1013273 k 658 26147 A1013387 as 659 8815 A1013437 p 660 19722 A1013508 k 661 6674 A1013568 General 662 23145 A1013647 o,t 663 15130 A1013676 w 664 7274 A1013715 as 665 7276 A1013730 a 666 7278 A1013738 y,z,aa 667 22592 A1013740 s,x,bb,General 668 16584 A1013765 w 669 24143 A1013804 ,l j 670 15928 A1013829 a,General 671 21950 A1013861 Valine, leucine and j isoleucine degradation t 673 2708 A1013882 d,q i 675 7299 A1013911 p,r,t,General 676 15904 A1013971 General 677 12781 A1014023 w TABLE THWAYS A~fty. Docket No. 44'921-5U8~91N0 2: Doc. No. 1798397.
PA enBank Accl dentifiesRef. Seq. odel Pathways 'Sequence ID No. Code ID No.

678 19372 A1014135 as 679 4241 A1014140 w 680 15247 A1014169 c,u _ 7315 A1028831 682 16631 A1028856 General 683 23297 A1028953 x 684 11326 A1029015 b 685 2866 A1029058 n,y 686 12812 A1029126 General 687 17602 A1029156 p 688 7392 A1029185 as 689 6517 A1029264 d,k,x 690 7639 A1029292 b 691 3874 A1029428 ,General i f 693 7452 A1029466 r 694 7493 A1029608 b 696 7537 A1029829 o,General 697 2310 A1029969 v 698 7585 A1030023 x 699 7586 A1030024 b,n 700 14492 A1030091 cc f 702 7615 A1030163 o,r 703 2370 A1030179 General 704 7681 A1030449 n 705 11559 A1030472 General 706 7665 A1030668 ,bb t 707 24222 A1030704 k 708 10740 A1030743 h 709 10742 A1030773 a 711 16169 A1030932 General f r 714 3167 A1031012 a 715 5350 A1043611 a t 717 10784 A1043678 d 718 9180 A1043694 as 719 7867 A1043695 as Glutamate metabolism,Purine metabolism 720 7584 A1043724 General 721 7895 A1043768 a 722 7903 A1043805 General 723 7913 A1043849 cc I

f 726 10818 A1043990 g,I,m,General f 728 5393 A1044170 p 729 5398 A1044177 q 730 5425 A1044237 a,d r i 733 5461 A1044338 g,p,General i 735 3359 A1044347 as 737 2695 A1044396 b 738 5494 A1044425 General 740 9882 A1044588 ,m j 741 5575 A1044688 g 742 2348 A1044794 General 743 18205 A1044836 n X744 _ A10448~ u I -~

TABLE TIifNAYS Atty. DocketNo. 44'9'21-5U'89V110 2: Doe. No.
PA enBank Accl 1798397.1 entifierRef. Seq. odel athways, Sequence5630 ID No. Code ID No. A1044869 I f 746 5634 A1044883 General 747 4047 A1044947 ,m I

748 5654 A1044976 w r 750 19235 A1045074 General 751 5689 A1045075 ,aa,General i 752 5711 A1045151 General 753 19237 A1045153 c f f 756 5474 A1045477 a,General 757 5811 A1045502 d,e 758 5819 A1045537 General i 760 6808 A1045600 s 761 17755 A1045608 y 763 10020 A1045632 a 764 5855 A1045669 General i 766 5897 A1045862 General 767 5900 A1045866 y,z 768 7540 A1045882 o,t,General 769 5329 A1045970 p 770 15093 A1058285 d i 772 8017 A1058341 c 773 6828 A1058359 General 774 8177 A1058603 as 775 3090 A1058730 as 776 10093 A1058746 g 777 8143 A1058759 General f 779 8163 A1058837 as 780 4789 A1058889 General 781 8221 A1059061 General 782 10159 A1059147 d 783 8245 A1059154 b 784 8283 A1059290 n 785 8314 A1059386 g,General i s 788 18359 A1059675 n 789 10281 A1059947 b,t 790 8494 A1059968 as 791 8495 A1059971 General 792 8496 A1059974 General i 794 8548 A1060176 k t 796 18322 A1060279 ,y,z i r 799 17506 A1070068 cc 800 9067 A1070087 General 801 3551 A1070122 a 802 4967 A1070179 k 803 18 A1070195 General 804 24197 A1070314 General r 806 8874 A1070336 b,cc 807 10417 A1070410 m 808 8901 A1070419 as TABLE THfNAIfS Atty. Docket No. 44921-5U'8'9f1110 2: Doe. No. 1798397.1 FA enBank Acci entifierRef. Seq. odel Pathways Sequence14424 ID Ne. Code ID No. A1070421 ,p,General I I

810 10434 A1070497 General 811 8927 A1070523 v 812 8946 A1070611 q 813 8950 A1070621 w 814 8972 A1070673 General 815 8981 A1070715 bb 816 26184 A1070784 ,l i 817 3007 A1070824 w 818 8999 A1070839 p 819 10477 A1070868 e,f 820 24301 A1070911 k 821 8721 A1071024 General 822 9212 A1071098 x 823 1831 A1071137 c r 825 9104 A1071173 ,m j 826 9583 A1071185 General 827 9644 A1071410 c 828 16058 A1071490 General Sphingoglycolipid metabolism 829 11057 A1071509 ,o f 831 5695 A1071566 bb 832 9671 A1071568 w 833 22929 A1071578 General 834 9673 A1071581 General 835 9699 A1071646 General 837 9799 A1072008 q,y,z 838 9808 A1072050 d 839 22796 A1072213 General 840 9271 A1072405 v 841 10869 A1072425 w 842 21797 A1072439 General r j 845 10893 A1072559 x 846 1501 A1072634 cc,General 847 6548 A1072658 General 848 9363 A1072695 d 850 9409 A1072841 n 851 9410 A1072842 w 852 9468 A1073021 General f 854 11183 A1100768 Nitrogen metabolism t 855 9190 AI100835 a 856 2029 A1100842 p 857 5687 A1101006 a 858 15192 A1101099 g,cc 860 9339 A1101160 ,m,o I

861 6321 AI101256 General 862 5421 AI101270 c 863 11910 A1101323 General 864 23140 AI101608 a 865 4119 A1101901 General 866 16324 AI102009 b 868 19373 A1102044 a 869 7051 A1102055 h 870 6544 A1102064 c 871 10227 A1102248 w 872 23849 A1102318 e,q 873 11954 A1102505 ,j,s Oxidative phosphorylation g 874 2125 AI102519 c,k TABLE THIIUfAYS Atty . cket No. 44921-5U'8'91N0 2: DoDoc. No.1798397.1 FA enBan Aee/
entifierRef. Seq. odel athways Se~~que~nce ID No. Code SID
No.
I

875 5967 AI102520 y 875 5969 A1102520 p,w 876 11563 AI102560 General 877 15190 AI102562 b,g,n,p,v 878 19769 AI102570 bb 879 22487 A1102578 General 880 19011 A1102618 General 881 23837 AI102620 q,t 882 23538 A1102727 g,General 883 17234 A1102741 c 884 5891 A1102745 k 885 6796 A1102753 General 886 8837 AI102849 o,p i 888 3533 A1102877 g 889 13222 A1102977 General 890 6806 AI103018 o,u 891 10659 AI103059 w,cc,General 892 17400 AI103097 a 893 3584 A1103106 x,aa 894 13298 A1103143 r 895 15981 A1103150 ,x i 896 3475 AI103245 w 898 23619 A1103314 p 899 24181 A1103320 a 901 4355 A1103410 General 902 7622 AI103472 General 903 20918 A1103552 n 904 21579 A1103572 General 906 2752 A1103641 a i 908 8990 A1103719 ,m,y,z I

r 910 22885 A1103828 e,General 911 15853 A1103841 x 912 15050 A1103911 ,y Oxidative j phosphorylation 913 12376 AI103939 a 914 22271 A1103947 o,y 915 20833 A1104035 ,q Oxidative f phosphorylation 916 7010 AI104099 w 917 22101 A1104251 General 918 22833 AI104258 General 919 22211 AI104279 g,m I

i 922 10991 A1104342 a 923 18831 A1104357 p 924 7223 A1104373 a 925 23574 A1104520 e,g,s Oxidative phosphorylation 926 8509 AI104528 q 927 11680 A1104605 v 928 2342 A1104658 w r 930 15377 A1104821 o,cc 931 22957 A1104897 General Oxidative 932 8451 AI104953 o,s phosphorylation,Type protein secretion system 933 24375 AI104979 n,General 934 8278 A1105080 bb 935 2196 A1105243 g 936 5199 A1105272 bb,General 937 2901 AI105301 o,s TABi!E TH1NAYS Aft~y. Docket No. 44921-5U'8911V0 2: Doc. No. 1798397.1 PA enBank dentifierAeel odel Pathways Sequence Ref. Seq. Code SID ID No.
No.

938 7 AI105383 cc,General 939 _ AI105398 a -940 22931 A1105417 e,General Fatty acid metabolism,Lysine 941 23596 AI105435 bb degradation,Tryptophan metabolism 943 12660 A1111492 c 944 4479 A1111599 General 945 24211 AI111853 k 946 2539 A1111960 r 947 5729 A1111990 k 948 4049 A1112012 ,q,u,General i i 950 20041 A1112161 t 951 12937 A1112462 General 952 3713 AI112571 b 953 12921 A1112636 General 954 12965 AI112926 General 955 7499 AI112986 General 956 4969 AI113008 r f 959 11165 A1136372 c 960 4045 A1136460 cc 961 12782 A1136493 k 962 6850 A1136665 h Purine metabolism,Pyrimidine metabolism 963 20920 AI136891 p,v i 966 13111 A1137224 o,General 967 15969 AI137302 a 968 14349 AI137303 d 969 9166 AI137406 General r 971 6638 A1137579 General 972 7414 AI137586 General 973 11321 AI137752 z I

i 976 13467 A1138034 cc 977 11377 A1138105 y 978 6790 A1144801 d,h 979 6506 AI144919 ,1,y j i 982 14458 AI145095 General 983 7476 AI145202 g 984 17545 A1145384 a r r 987 8634 A1145722 g 988 8339 A1145761 ,General 989 2059 AI146005 h,General 991 5232 A1168942 bb Valine, leucine and isoleucine degradation 992 18472 AI168975 a 992 18473 A1168975 a r 994 11618 A1169115 0, ,General 996 0984 A1169156 o,u a 1 a X ~ c TAB'L!ETIi171lAYS A~tty. Docket No. 44921-5U'8'91'11'IO
2: Doc. No. 798397.1 PA enBank Acel dentifierRef. Seq. odel Pathways Sequence I~ No. Code Oxidative phosphorylation,Type ID No. 22661 III protein A1169265 s,z secretion s stem 1001 13239 AI169278 g,j,l,y,z 1002 24162 AI169279 m 1004 24213 A1169289 p 1005 13240 A1169311 cc 1006 5931 A1169324 b 1007 20891 A1169337 d 1008 11979 A1169365 cc 1009 10947 A1169372 s 1010 20697 A1169494 o,u 1011 8234 AI169517 z 1013 10839 A1169655 ,m I

1014 24146 A1169668 ,l j 1015 22575 A1169728 r 1016 804 A1169756 cc 1017 8213 A1169883 p 1018 3916 A1169947 ,bb i 1019 3733 AI170053 u,General 1020 14179 AI170224 cc 1021 11406 A1170263 r 1022 3547 A1170279 General 1023 11524 AI170340 ,y,z j 1024 2729 AI170363 e,i i 1026 22524 A1170542 h 1027 24048 A1170570 a,g 1028 5968 AI170692 y,aa 1029 9757 A1170693 b 1030 18905 A1170770 e,s i 1032 7089 A1171185 c 1033 17591 A1171354 b 1034 13285 A1171361 h Oxidative phosphorylation,Ubiquinone 1035 4428 AI171362 a biosynthesis 1036 18126 AI171369 w 1038 4584 A1171492 m,General 1039 11158 AI171542 ,s r I

1041 21183 A1171676 k i i 1044 2625 A1171800 cc 1045 23579 A1171802 v 1046 11708 A1171807 ,t I

Oxidative phosphorylation,Type 1047 17204 AI171844 s,y,z III protein s ecretion system 1048 4420 AI171916 m 1049 3266 A1171948 ,m I

t 1051 1205 A1172057 a,q,bb 1052 6057 A1172102 b 1053 9128 AI172103 m 1 z 1055 6630 A1172184 n 1056 1968 A1172208 bb 1057 6974 A1172263 ,m I

__ 23313 AI172271 1058 d 1059 2140 AI172272 General X ~

TABLE 2: PATHfIfIAYS Atty. U cket No. 449'29-5U'8'9fN10 Uoc. No. 1798397.1 Sequence e Bank Ace/
'ID No. IdentifiesRef. Seq. odel P thw~ays 1060 15382 ID No. Code A1172302 ,p,General I

I

1063 3042 A1172447 General Citrate cycle (TCA
cycle),Glutathione 064 17291 I172491 b ( metabolism,Reductive carboxylate cycle C02 fixation) 1065 26222 AI172506 p r 1067 8795 A1172618 General 1068 6454 AI175342 ,l,m,y j x 1071 3418 A1175475 m 1072 18507 A1175551 bb 1073 10217 A1175628 w 1074 7262 A1175833 ,m,x j r 1076 22352 A1175959 ,General ( 1077 7022 AI176041 h,n t 1079 18581 A1176160 General 1080 14159 A1176169 g 1081 21742 A1176172 w 1082 10182 A1176185 v 1083 22765 A1176265 General 1084 6905 AI176275 a 1085 12999 A1176276 cc 1086 16438 A1176294 a 1087 21130 A1176298 y 1088 3014 A1176362 a r 1090 19006 A1176393 x 1092 12174 A1176435 ,m j 1093 15191 A1176456 b,o,t,v,cc 1094 24236 AI176473 d,General 1095 16518 A1176546 v 1096 2161 A1176592 General 1097 12436 AI176610 General 1098 2536 AI176616 ,v,General I

1099 18525 AI176792 a 1100 23449 A1176828 g 1101 23299 A1176839 General 1102 3580 AI176848 a 1103 22103 A1176849 d,General f 1105 15588 A1176916 General t 1107 16124 A1176963 cc 1108 15146 A1176969 b,General f 1110 2852 A1177059 c 1112 3156 A1177092 g 1113 14384 A1177096 a Purine metabolism 1114 13310 AI177119 General 1115 24049 AI177341 g,p,s,u 1116 15964 A1177360 o,General 1117 14989 A1177366 a 1118 7975 A1177374 as 1119 3006 A1177395 k 1120 17570 A1177683 r 1121 9521 A1177706 b 1122 14425 A1177755 g,General TABLE TIiI'N,AYS Atty. Docket No. 44'9-29-SU'8'91'A'10 2: Doc. No. 1798397.1 PA enBank Acci entifierRef. Seq. odel Pathw,~ays Sequence10611 ID No. Code ID No. A1177790 ,m I j 1124 5356 A1177813 cc 1125 11791 A1177843 General 1126 14484 AI177867 General 1127 5780 AI177869 General 1128 19184 AI178025 General 1129 6059 AI178245 c,General 1130 23248 AI178267 y 1132 7838 AI178291 a 1133 18996 AI178326 y 1134 22488 A1178392 b 1135 18800 A1178504 n,p,aa 1136 22197 AI178527 g,General 1137 3401 A1178684 bb 1138 17713 A1178700 m 1139 14874 A1178735 a 1140 23567 A1178746 v,General 1141 18907 AI178971 c i 1143 5887 A1179099 q,t 1144 8477 AI179167 b,e,General 1145 3348 AI179288 u,v 1146 13608 A1179314 a 1147 8849 A1179315 g,p 1148 13611 A1179378 v,General 1149 15438 AI179399 m,x 1150 13614 A1179407 e,t,General 1151 15042 AI179422 b,General 1152 2768 A1179481 ,General i 1153 24041 AI179580 b,i 1154 19822 A1179599 o,General 1155 23270 AI179601 q,General 1156 5901 AI179605 a 1157 16081 A1179610 g,i,p Porphyrin and chlorophyll metabolism 1158 14564 AI179717 k 1159 7918 AI179750 General 1160 6647 A1179795 g 1161 9097 A1179875 o,General 1162 23989 AI179953 a 1163 12899 A1179967 b 1164 1687 A1179971 c 1165 22569 A1179979 General 1166 23514 AI179986 o,GeneralGlycine, serine and threonine metabolism 1167 15892 AI179988 c,General 1168 12402 AI180004 g 1169 5443 A1180165 General 1170 5481 AI180170 General I

1172 17089 A1180281 g 1173 3701 A1180306 as 1174 3352 AI180334 m 1175 24368 A1180392 ,m I

1176 14337 A1180414 c 1177 19080 A1227647 ,y,z j 1178 22838 AI227667 as 1179 6765 A1227761 ,General i 1180 24054 AI227867 General i 1182 23898 A1227987 d 1183 1651 A1228068 n,w 1184 14237 A1228128 a 1185 14242 A1228197 General TA~B'LETH1'NtAYS Atty. Doe ~et No. 44929-5U'891'NO
2: Doe. N.o31t7~983.9t7~11 PA GenBank Aac/
dentifier Ref. odel Pathways SequenceSeq. ID No. Code ID No. 16913 AI228236 0 I

r 1188 8917 A1228301 General 1189 15879 A1228313 ,General r 1190 13727 A1228326 o,General 1191 6102 A1228335 General 1192 13730 AI228356 a 1193 13745 A1228494 b,cc 1194 4217 A1228587 s 1195 16053 A1228596 cc 1196 3557 A1228672 a 1197 11605 A1228682 a r 1199 13771 A1228848 g 1200 5918 A1229036 r 1201 8235 A1229154 k r 1203 13826 A1229304 a 1204 13144 A1229320 g 1205 4640 A1229404 x,aa I

1207 15426 A1229497 s 1208 15193 A1229508 bb 1209 19243 A1229638 x 1210 23078 A1229647 p Oxidative phosphorylation,Ubiquinone 1211 3099 AI229680 o biosynthesis 1212 19508 AI229698 bb 1213 13977 A1229707 x 1214 23983 A1229708 v 1215 2688 A1229793 a 1216 13874 A1229832 g 1217 12587 A1229979 General 1218 20591 A1229993 ,m I

1219 24042 A1230002 a,b,d,General 1220 13880 AI230042 a Oxidative phosphorylation,Ubiquinone 1221 17672 AI230074 d biosynthesis 1222 3652 AI230113 General 1223 18650 A1230121 as 1224 13025 A1230173 c 1225 4280 A1230247 z 1226 18528 A1230284 General 1227 7084 A1230362 p 1228 20895 A1230549 b,n 1229 12961 AI230554 General r 1231 4121 A1230647 j ,m 1232 14388 A1230702 General 1233 18529 A1230716 x,General 1234 13618 A1230724 General 1235 8304 A1230746 cc 1236 4731 A1230773 a 1237 14430 A1230798 c,k,x 1238 16627 AI230822 bb Glycoprotein biosynthesis 1239 3125 AI231028 General 1240 633 A1231127 k 1241 20846 A1231140 p 1242 6743 A1231219 d 1244 26292 A1231391 k 1245 12343 A1231433 w 1246 7337 A1231465 as 1247 16321 A1231506 General TABLE TIiIIfIAIfS A~tty. Docket No. 44921-5U'8'9fNO
2: Doe. No. 1798397.
PA enBank Accl entifierRef. Seq. odel Pathwa~y~s Sequence8004 I~ No. Code ID No. A1231532 ,l I j 1249 15171 AI231792 g i 1252 14227 A1231999 a 1253 24501 A1232006 w,y,bb g,q,z,cc, 1254 3434 A1232014 General 1255 19094 AI232021 n,General 1256 14020 A1232076 a 1257 6726 A1232157 d 1258 11549 A1232174 ,m I

1259 23125 A1232266 ,s j 1260 2085 A1232270 bb 1262 14304 A1232281 g 1263 15955 A1232294 u,bb,General 1264 15122 A1232303 y 1265 4716 A1232313 y 1266 15246 A1232332 ,u t 1268 16172 A1232341 d 1269 11411 A1232346 h 1270 19287 A1232379 pdgf f 1271 5601 A1232461 n,General 1272 14051 AI232489 ,m I

1273 5572 A1232490 ,t i 1274 11157 A1232494 cc 1276 20350 A1232552 ,v,y j 1277 14069 AI232631 a 1278 4440 A1232643 w 1279 17695 A1232784 a 1280 15796 A1232874 v 1281 12467 A1232924 General i r 1284 18794 A1233121 c 1285 3823 A1233147 b,g,General 1286 11967 AI233155 c,k,General 1287 11561 AI233182 d 1288 3471 A1233183 g i 1290 13598 A1233194 g,p,y 1291 15552 A1233195 y 1292 17907 A1233224 bb 1293 14111 A1233269 cc 1294 12894 A1233365 d 1295 7161 A1233407 General 1296 15906 AI233425 q 1297 14120 A1233433 d 1298 14095 A1233468 a,d 1299 3075 AI233494 u,aa 1300 6046 A1233530 General 1301 18900 A1233570 General Aminoacyl-tRNA biosynthesis,Arginine 1302 7888 AI233583 General and proline metabolism 1303 16709 AI233602 General Purine metabolism y 1305 7243 A1233717 General g 1307 13023 A1233740 ,h,General d g 1309 7469 A1233767 cc TABLE THiNAYS Att~y. Docket No. 44'929-5U'8'9V1IO
2: Doc. No. 1798397.
PA enBa~nk entifierA~ c~cl odel Pathways Sequence7804 Ref. Seq. Code !ID ID No. b No. A1233771 I

1311 13563 A1233773 a 1312 2154 A1233818 k,cc 1313 16616 AI234079 h 1314 13393 A1234100 a,d,General 1315 7071 AI234162 r 1316 14677 A1234620 General 1317 4443 AI234629 m 1318 22453 A1234678 b 1319 23964 A1234748 ,General t f 1321 22152 A1234822 o,General 1322 18942 AI234865 d Oxidative phosphorylation,Type 1323 22662 AI234939 as III protein secretion system 1324 3875 AI235047 o,General 1326 14906 AI235192 g 1327 14718 A1235210 a 1328 15004 A1235224 b,General 1329 6632 A1235277 v 1330 14722 A1235284 x,z 1331 1462 AI235585 u,General 1332 21061 AI235631 ,m I

1333 14665 A1235646 m t gf-beta 1334 19940 AI235689 General 1335 5698 AI235692 a 1336 23745 AI235732 k 1337 11164 A1235739 General 1338 5212 AI235745 d 1339 14768 A1235912 h 1340 14776 A1235950 m 1341 3091 A1236027 n,General r 1343 14862 A1236048 a 1344 16943 A1236097 p I

1346 23230 A1236146 v 1347 22855 A1236150 a i r 1350 5051 AI236332 General 1351 19298 AI236338 bb 1352 0667 A1236366 b f 1354 9407 A1236402 as 1355 26335 A1236460 General 1356 17950 AI236590 ,General t 1357 8259 A1236601 h,v 1358 1445 A1236613 ,y 1 j 1359 7248 AI236635 o,aa 1360 6859 A1236753 ,General 1 t 1361 5208 AI236754 g 1362 24388 A1236772 e,General 1363 5850 AI236795 n,v,w 1364 4800 AI236856 w 1366 1404 A1237002 m 1367 8151 AI237212 o,General 1368 21653 A1237535 ,General t 1369 1208 AI237586 z 1370 2 AI237713 ,k,aa 1893 i _ _ A1237724 -1371 4842 r ~ - -~1372 3467 A1237835 X ~ General -~

TABLE THVI'IAIfS Aft~y. Docket No. 44'9'21-5U'8~9fNO
2: Doc. No. 1798397.1 PA enBank Aee/
entifierRef Seq. odel Pathways Sequence25840 ID No. Code ID No. A1638972 a I

1374 17108 A1639017 i r 1375 16676 A1639082 c,k,x 1376 12400 AI639107 k 1377 19952 A1639108 q,v 1379 25907 A1639167 o,w 1381 18533 A1639231 n 1382 18353 A1639233 ,aa t 1384 15330 AI639285 General 1385 20026 AI639354 g 1386 25971 A1639365 r 1388 19152 A1639387 u,General 1390 18338 A1639422 y 1392 20082 A1639488 ,m i 1394 20056 A1639504 a,bb,General 1395 4713 A1639518 q 1396 14332 AJ001044 bb 1397 7602 AJ001929 k 1398 9867 AJ005424 a 1400 16351 AJ011811 General 1401 20116 AJ011969 ,General ( 1402 17635 AJ223355 v,w 1403 18686 D00729 q Fatty acid metabolism 1404 5049 D10655 n,w 1405 25257 D13623 j 1405 15281 D13623 h 1406 11434 D14014 cc 1407 1613 D14076 x Bile acid biosynthesis,Fatty acid q biosynthesis (path 2),Fatty acid 08 28 6479 metabolism,Phenylalanine metabolism,Valine, leucine and isoleucine degradation 1409 3015 D16554 c,s,v,z 1410 472 D26111 d,s,bb 1412 16233 D29960 j ,l 1413 9029 D30804 n 1414 1485 D38222 y,z 1415 9135 D45247 s Proteasome 1416 16354 D50564 a Cysteine metabolism 1417 1884 D50695 I ,m,bb 1418 21147 D63772 General 1419 826 D82928 f GI cerolipid metabolism 1420 25306 D84485 a 1421 18867 D88250 t 1423 22543 H31117 r ,v,General 1424 12360 H31456 w 1425 20514 H31489 h,j 1426 11358 H31610 h 1427 4360 H31813 bb,General 1429 4386 H33093 h,w 1430 4415 H33636 h 1432 17159 J00797 u,General 1433 16260 J01878 f 1434 17284 J02827 bb Valine, leucine and isoleucine degradation 1435 15017 J03752 n 1436 44 J03819 p,s 1437 21014 J03914 e,r,GeneralGlutathione metabolism Androgen and estrogen 1438 20429 J05035 f metabolism,Bile acid biosynthesis TABLE TFI1111AYS Afty. Docket No. 44'929-5U'8'9fNO
2: Doe. No. 1798397.1 f'A enB~ank lentifie~Accl odel Pathways Sequence Ref. Seq. Code Glutamate metabolism,Glutathione ID No. 1247 ID No. metabolism I J ,l,m,s,y,z 05181 j 1440 10464 05510 n,u,General J

1441 20149 K03243 q 1442 17758 K03249 q 1443 381 L00124 w 1444 2048 L00382 k,x 1445 10500 L04619 s 1447 108 L14002 p 1448 25366 L14003 t 1449 109 L14004 c,p 1450 20414 L14323 General 1451 25369 L14937 y 1452 16119 L16532 k 1453 25377 L25387 h 1453 12058 L25387 h 1455 21146 L35558 General 1456 106 L37203 w 1458 13682 L38482 f ,j,k,m,z Glutamate metabolism,Glutathione 1459 6405 L38615 p metabolism 1461 15189 M11794 n,v 1462 17086 M13011 j 1465 25405 M18330 j ,l 1466 25415 M19648 a 1468 14967 M22366 w 1469 20481 M22631 bb 1471 15048 M24542 q Oxidative phosphorylation 1472 20921 M29853 m 1473 1224 M31931 a 1474 15579 M33648 q 1474 15580 M33648 q 1475 17211 M34331 g,n,q,v 1476 20699 M35601 b,x,bb 1476 20700 M35601 b,t,bb 1479 1585 M57728 j ,m, 1480 24844 M58040 c 1481 25057 M58495 h 1482 457 M60666 d,General 1483 1223 M75281 f 1484 5733 M81855 i ,k,aa 1485 4198 M83143 m 1485 4199 M83143 m 1486 24651 M83678 k,x,z Histidine metabolism,Phenylalanine metabolism,Tryptophan 487 430 84648 eneral metabolism,T rosine metabolism Arginine and proline 1488 25467 M93297 c metabolism,Urea cycle and metabolism of amino groups 1489 729 M95762 a,y Bile acid biosynthesis,Fatty acid q biosynthesis (path 2),Fatty acid 90 698 012489 metabolism,Phenylalanine metabolism,Valine, leucine and isoleucine degradation Bile acid biosynthesis,Fatty acid q biosynthesis (path 2),Fatty acid 90 699 012489 metabolism,Phenylalanine metabolism,Valine, leucine and isoleucine degradation TABl!E THI7fIAYS Atty. Docket No. 44'921-508'911110 2: Doe. No. 17 8391.1 PA enBank Accl entifierRef. Seq. odel Pathways i Sequence ID No. Code Carbon fixation,Fructose ID No. and mannose I metabolism,Glycolysis 062 q /
M 012495 Gluconeogenesis,lnositol metabolism,Pentose 491 phosphate c cle Fructose and mannose metabolism,Galactose metabolism,Glycerolipid i metabolism,Pentose 92 511 012498 and glucuronate nterconversions,P ruvate metabolism 1494 7427 NM 012515 General i Arginine and proline 1496 4467 NM 012529 d metabolism,Urea cycle and metabolism of amino groups 1497 16520 NM 012532 General Porphyrin and chlorophyll metabolism 1498 225 NM 012544 x,z Histidine metabolism,Phenylalanine metabolism,Tryptophan 499 431 M 012545 eneral metabolism,Tyrosine metabolism 1500 23868 NM 012551 ,m,v,General I

1500 23872 NM 012551 ,v,cc,General I

1500 23869 NM 012551 v,General Glycolysis /
z Gluconeogenesis,Phenylalanine, 501 9407 M 012554 tyrosine and tryptophan biosynthesis Glycolysis /
Gluconeogenesis,Phenylalanine, 501 9408 M 012554 ,s, ,z tyrosine and tryptophan biosynthesis 1502 21836 NM 012555 k Carbon fixation,Fructose and mannose 503 6895 M 012558 ,s metabolism,Glycolysis /
Gluconeogenesis,Pentose phosphate cycle 1504 25317 NM 012559 bb 1504 6477 NM 012559 b,bb 1504 6478 NM 012559 bb 1505 11731 NM 012561 k 1507 4254 NM 012564 a r r r 1509 16080 NM 012580 g,m Porphyrin and chlorophyll metabolism 1510 15098 NM 012588 bb 1511 4450 NM 012592 bb Valine, leucine and isoleucine degradation 1511 4451 NM 012592 ,bb Valine, leucine and i isoleucine degradation 1511 4452 NM 012592 bb Valine, leucine and isoleucine degradation 1512 17198 NM 012593 a,x 1512 17197 NM 012593 x 1513 18749 NM 012600 a,h Carbon fixation,Pyruvate metabolism 1514 2628 NM 012603 General 1514 2629 NM 012603 x,General 1515 16849 NM 012608 n,o,q 1517 15540 NM 012620 General 1518 24568 NM 012630 General 1518 24566 NM 012630 General 1519 18553 NM 012631 k 1520 1844 NM 012637 General f 1522 18632 NM 012645 a 1523 25435 NM 012647 g 1524 9423 NM 012649 b,cc 1525 24496 NM 012654 n 1526 7101 NM 012679 x,bb,General Fatty acid metabolism,Tryptophan 1527 24707 NM 012693 metabolism i TABLE TIifIfIAYS Atty. Doc~t No. 44921-50'8~9fNO
2: Doc. No. 1798397.1 PA enBank entifierAcc/ odel CodeFathways Sequence1850 Ref. Seq. t ID No. ID No.

1528 1854 NM 012696 t 1529 1603 NM 012697 General Aminosugars metabolism,Fructose and a mannose metabolism,Galactose metabolism,Glycolysis Gluconeogenesis,Starch and sucrose metabolism Alanine and aspartate 1531 1478 NM 012744 bb,Generalmetabolism,Citrate cycle (TCA cycle),Pyruvate metabolism 1532 343 NM 012747 h,t 1533 8829 NM 012749 General 1534 20828 NM 012752 General 1534 20829 NM 012752 i,General 1534 20830 NM 012752 i,General 1535 15174 NM 012756 b 1536 21685 NM 012760 j,m,n 1537 18068 NM 012762 t 1538 1246 NM 012770 a,GeneralPurine metabolism 1539 1348 NM 012776 f 1540 18135 NM 012791 w Arginine and proline metabolism,Glycine, 541 6947 M 012793 ,bb serine and threonine metabolism,Urea cycle and metabolism of amino groups 1542 960 NM 012796 a Glutathione metabolism 1543 260 NM 012798 f,u 1544 556 NM 012803 d 1545 21729 NM 012804 q 1546 15032 NM 012816 General 1547 24895 NM 012817 General 1548 18109 NM 012823 u,General 1549 373 NM 012833 h,I,q,General 1550 2855 NM 012838 a 1551 11136 NM 012839 s 1552 20885 NM 012842 a egf 1552 20884 NM 012842 a,bb egf 1553 18770 NM 012857 a 1554 20674 NM 012861 i 1555 13151 NM 012862 a,r,General 1556 24617 NM 012870 General 1557 20945 NM 012875 a,v 1558 15872 NM 012879 o,r 1559 495 NM 012880 z 1559 494 NM 012880 c 1560 23651 NM 012881 d,u,General 1562 19477 NM 012891 q 1563 18564 NM 012899 v,GeneralPorphyrin and chlorophyll metabolism 1564 7197 NM 012904 f,r,cc,General 1564 7196 NM 012904 v,cc,General 1565 20202 NM 012909 b,r 1566 16581 NM 012911 c,j 1566 16582 NM 012911 c 1567 24431 NM 012912 General 1568 18118 NM 012913 p Oxidative phosphorylation 1569 6108 NM 012915 n 1570 20757 NM 012923 c,i,aa 1570 20755 NM 012923 i 1571 2830 NM 012925 f 1571 2831 NM 012925 f Fatty acid metabolism,Glycerolipid 1572 1977 NM 012930 q metabolism 1573 18694 NM 012931 j,l,m,z 1574 13723 NM 012935 n TA'B'LETI11NAYS Atty. Docket No. 44'929-5U'8'91'N'10 2: Doc. No. 1798397.1 PA enBank Accl entifierRef. Seq. odel Pathways Sequence9109 ID No. Code ID No. NM 012939 ,y,z I j 1575 19398 NM 012939 as 1576 223 NM 012945 b,cc 1577 15058 NM 012950 cc 1579 19111 NM 012963 g 1580 19374 NM 012964 x t 1581 2555 NM 012967 ,cc,General t 1582 24528 NM 012973 c 1583 956 NM 012976 c 1584 16417 NM 012991 g 1585 17393 NM 012992 d 1586 23544 NM 013013 s 1587 1588 NM 013026 k 1588 17894 NM 013027 m 1589 18300 NM 013030 s,v,General 1589 18076 NM 013030 g,s,z 1589 18078 NM 013030 s 1589 18077 NM 013030 e,s,z 1591 730 NM 013040 w 1592 17401 NM 013043 ,o,General i 1593 16684 NM 013052 General 1594 14421 NM 013053 a 1595 15254 NM 013058 k 1596 14997 NM 013059 s,z Folate biosynthesis,Glycerolipid metabolism 1596 14996 NM 013059 General Folate biosynthesis,Glycerolipid metabolism 1597 25676 NM 013069 as 1598 24748 NM 013070 h,q 1599 1529 NM 013082 d,General 1600 1521 NM 013091 ,I,z,General j 1601 1685 NM 013096 c,aa 1601 26150 NM 013096 c,i.

1601 1688 NM 013096 p 1601 1689 NM 013096 c,p 1601 1684 NM 013096 c,s,aa 1602 20886 NM 013097 u,x,bb 1602 20887 NM 013097 u,x,bb Galactose metabolism,Glycolysis c /
603 321 M 013098 Gluconeogenesis,Starch and sucrose metabolism 1604 15296 NM 013102 ,m I

1606 23709 NM 013113 o,s,z,aa 1606 23711 NM 013113 p 1606 23710 NM 013113 s 1607 1976 N M 013118 a 1609 870 NM 013130 h 1610 16650 NM 013132 u,General 1611 650 NM 013134 h Sterol biosynthesis 1611 651 NM 013134 h,j,l Sterol biosynthesis 1612 1712 NM 013138 General 1613 16982 NM 013144 o,v,General 1614 21683 NM 013154 ,cc,General t 1614 21682 NM 013154 cc 1615 3431 NM 013156 b,g,n 1615 25567 NM 013156 v,General 1615 3430 NM 013156 General 1616 1309 NM 013159 w 1616 1310 NM 013159 w 1617 21723 NM 013174 w 1618 1314 NM 013181 m 1619 17357 NM 013183 p,bb,General Tl.IB'l!ETHIIfIAYS Atty. Docket No. 44921-5U'89fIVO
2: Uoc. No. 1798397.1 PA enBank entifierAccl MocJel Pathw~y~
Sequence Ref. Seq. Code Fructose and mannose 1D No. ID No. metabolism,Galactose I metabolism,Glycolysis 300 y /
Gluconeogenesis,Pentose M 013190 phosphate cycle 1621 16448 NM 013197 c Glycine, serine and threonine metabolism Fatty acid metabolism,Glycerolipid 1622 20856 NM 013200 b metabolism 1623 397 NM 013214 f 1624 20864 NM 013215 g,n,y 1625 20728 NM 013217 v ~

1626 1396 NM 013222 j 1627 815 NM 013224 w 1628 18305 NM 013226 v Fatty acid metabolism,Propanoate d metabolism,Valine, 629 1078 M 016986 leucine and isoleucine degradation,beta-Alanine metabolism 1630 24649 NM 016988 v Riboflavin metabolism 1631 15239 NM 016989 q,w 1632 45 NM 016996 General Fatty acid metabolism,Tryptophan 1633 20714 NM 016999 t metabolism Fatty acid metabolism,Tryptophan 1633 20713 NM 016999 t metabolism Fatty acid metabolism,Tryptophan 1633 20711 NM 016999 q,t metabolism Fatty acid metabolism,Tryptophan 1633 20715 NM 016999 q,t metabolism 1634 1698 NM 017000 e,n,p,GeneralSterol biosynthesis Glutathione metabolism,Pentose 1635 1399 NM 017006 h,n,Generalphosphate cycle 1637 18989 NM 017013 n Glutathione metabolism 1638 21013 NM 017014 e,f Glutathione metabolism 1638 21015 NM 017014 e,GeneralGlutathione metabolism 1639 11836 NM 017023 b 1639 5475 NM 017023 b 1639 25546 NM 017023 b,bb Cysteine metabolism,Glycolysis /
640 7807 M 017025 ,General Gluconeogenesis,Propanoate metabolism,Pyruvate metabolism 1641 24597 NM 017040 a 1642 24696 NM 017048 f,j,z 1643 24695 NM 017049 a 1644 20876 NM 017050 j,n,z 1645 910 NM 017059 f,l,m 1645 912 NM 017059 i 1646 1946 NM 017061 h 1646 1942 NM 017061 t,General 1646 1943 NM 017061 t 1647 6062 NM 017066 d 1648 6654 NM 017068 w 1649 11153 NM 017073 s Glutamate metabolism,Nitrogen metabolism 1650 923 NM 017076 General 1651 1523 NM 017079 s Androgen and estrogen 1652 23660 NM 017080 s metabolism,C21-Steroid hormone metabolism Androgen and estrogen 1653 275 NM 017081 b,d,Generalmetabolism,C21-Steroid hormone metabolism 1654 16211 NM 017082 j,s,z 1655 1552 NM 017084 j Glycine, serine and threonine metabolism 1655 1550 NM 017084 y GI cine, serine and threonine metabolism 1656 22552 NM 017087 a,k,x 1657 8888 NM 017090 m Purine metabolism 1658 10887 NM 017094 a,General TABLE TIiINAIfS Atty. Docket No. 44'9'21-508~91IV0 2: Doc. No. 1798397.1 PA enBamk Acc/
entifierRef. Seq. odel Pathways Sequence4393 ID No. Code ID No. NM 017101 a,y I

1660 24770 NM 017111 d 1661 20745 NM 017113 a 1661 20746 NM 017113 a 1662 1375 NM 017122 w 1663 12903 NM 017124 k 1664 24885 NM 017138 r 1664 24886 NM 017138 d,q 1665 15363 NM 017147 n,u 1666 13392 NM 017148 u,General 1667 5351 NM 017150 q 1668 16954 NM 017151 a,n 1669 21643 NM 017152 g 1670 1694 NM 017153 a,q 1671 17104 NM 017160 bb,General 1671 17106 NM 017160 a 1671 17107 NM 017160 d,e 1672 17686 NM 017165 n,q Glutathione metabolism 1673 20702 NM 017166 c 1674 3513 NM 017177 Glycerolipid metabolism r 1675 19031 NM 017180 v,General 1676 15437 NM 017187 x,z 1676 15433 NM 017187 y 1676 15434 NM 017187 x,z 1677 24437 NM 017190 p 1678 1542 NM 017193 ,l,m,z j 1679 14695 NM 017202 q,s Oxidative phosphorylation 1679 14694 NM 017202 s,z Oxidative phosphorylation 1680 1428 NM 017213 m 1681 1622 NM 017216 g,j,s,z 1682 13642 NM 017220 v 1682 19976 NM 017220 w 1683 1510 NM 017224 General 1684 1811 NM 017228 ,l,m,z j 1686 17563 NM 017245 a,c,e,q r 1687 17501 NM 017248 x 1688 19 NM 017258 v,General 1689 15300 NM 017259 ,v,cc,General i I ,m,v,aa,cc, 1689 15301 NM 017259 General 1689 15299 NM 017259 ,y,cc,General I

1690 5224 NM 017264 d 1691 3987 NM 017280 bb Proteasome 1692 1447 NM 017281 Proteasome I

1693 5535 NM 017283 s,bb Proteasome 1694 12349 NM 017290 General Oxidative phosphorylation 1695 5819 NM 017298 p 1696 23825 NM 017299 v 1696 23826 NM 017299 v Glutamate metabolism,Glutathione 1697 4003 NM 017305 ,l,m,y,zmetabolism 1 j 1698 26109 NM 017306 q,s 1698 8687 NM 017306 q,t Fat acid metabolism 1699 8142 NM 017314 g,s,aa 1 t 1701 20809 NM 017326 a 1702 355 NM 017334 cc 1703 6148 NM 017340 q,s Fatt acid metabolism 1703 6150 NM 017340 a Fatty acid metabolism 1704 20849 NM 017343 ,u,General r 1704 20848 NM 01 b,General 1705 606 _ TABLE TI11111A1fS Atty. Docket No. 44921-5U'8'911V0 2PA Doe. No. 179&397.1 enf3ank SequenceentifierAcel odel Pathways ID No. 1581 Ref. Seq. Code I ID No. General 1707 455 NM 019131 x 1707 456 NM 019131 ,z 1708 4532 NM 019134 b 1709 1608 NM 019166 ,y,z j 1710 7489 NM 019169 c,General 1711 17066 NM 019170 p Prostaglandin and leukotriene metabolism 1712 23924 NM 019174 bb Nitrogen metabolism 1713 24019 NM 019186 t 1714 22063 N M 019195 d 1715 2079 NM 019220 ,k,z j 1716 16284 NM 019229 ,m I

1717 985 NM 019233 b,cc 1718 15503 NM 019237 k,x 1718 15504 NM 019237 k,x -1719 17908 NM 019242 ,v,cc,General I

1720 11218 NM 019247 c 1721 15259 NM 019259 d,f 1722 21443 NM 019262 aa,General 1722 21444 NM 019262 ,General t 1723 117 NM 019266 o,bb 1724 1145 NM 019280 w Bile acid biosynthesis, Fatty acid c metabolism,Glycerolipid 725 2220 M 019286 metabolism,Glycolysis /
Gluconeogenesis,Tyrosine metabolism 1726 10015 NM 019289 ,m,t,x,General I

1726 10016 NM 019289 bb,General 1727 21651 NM 019296 c,f,x 1728 20751 NM 019301 s 1729 645 NM 019345 bb 1730 1301 NM 019349 c 1731 3776 NM 019354 a,u 1732 4592 NM 019356 General 1733 1324 NM 019371 w 1734 19577 NM 019377 a 1735 24626 NM 019381 s 1736 744 NM 019622 p Fatty acid metabolism,Tryptophan 1737 20716 NM 019623 c metabolism 1738 20709 NM 019904 x 1739 574 NM 019905 u,GeneralGlyoxylate and dicarboxylate metabolism j 1741 20457 NM 020073 ,General i 1741 20458 NM 020073 General 1741 20460 NM 020073 General 1742 18713 NM 020075 r 1742 18715 NM 020075 r 1743 20493 NM 020076 p Tryptophan metabolism 1744 16375 NM 020976 g 1745 20816 NM 021261 k,General 1746 15335 NM 021264 a 1747 18729 NM 021578 k,z 1748 19060 NM 021587 cc 1749 17324 NM 021593 o,General 1750 19679 NM 021653 General 1750 19678 NM 021653 a,v,General 1751 19665 NM 021688 u,General 1752 19667 NM 021690 m 1754 22916 NM 021740 a t 1 t 1756 19712 NM 021745 r TABLE 'THI'NAYS Atty. ~ocket No. 44'9'29-5U'8'9111'10 2: floc. No. 1798397.1 PA enBank Accl entifierRef. Seq. odel Pathway~,s Sequence1962 ID No. Code 'ID NM 021750 ,k,y,z No. j I

1757 19824 NM 021750 a,bb Taurine and h potaurine metabolism 1758 25198 NM 021754 h 1758 20035 NM 021754 b,n,s,v,General 1759 20090 NM 021757 m 1760 17885 NM 021765 as 1762 20161 NM 021836 cc,General 1764 1203 NM 021997 k,z 1765 23151 NM 022005 b Aminosugars metabolism, Fructose and mannose metabolism,Galactose b metabolism,Glycolysis Gluconeogenesis,Starch and sucrose metabolism Aminosugars metabolism,Fructose and mannose metabolism,Galactose b metabolism,Glycolysis Gluconeogenesis,Starch and sucrose metabolism 1768 20257 NM 022180 w,General i 1768 10860 NM 022180 p 1769 23780 NM 022183 k,x 1771 6585 NM 022266 d,p,cc 1772 17161 NM 022298 ,v,cc,General i 1772 17162 NM 022298 a 1772 17160 NM 022298 a 1772 17158 NM 022298 q 1773 11454 NM 022381 ,aa,General i 1773 11455 NM 022381 ,General ( 1774 13480 NM 022390 s Folate biosynthesis 1775 15184 NM 022391 z 1776 22413 NM 022392 h 1776 22414 NM 022392 n t 1779 24537 NM 022399 a 1779 24539 NM 022399 y 1780 1141 NM 022401 o,General 1781 1069 NM 022402 g 1782 8211 NM 022500 ,n,s j 1782 8212 NM 022500 n,s 1783 6815 NM 022503 s Oxidative phosphorylation 1784 4259 NM 022504 q,w j Butanoate metabolism, Fatty acid 786 236 M 022512 ,z metabolism,Valine, leucine and isoleucine degradation 1787 3026 NM 022514 a 1787 3027 NM 022514 a,q,r,aa 1788 2696 NM 022515 a,d 1788 2697 NM 022515 n,w,aa 1789 3900 NM 022516 h Arginine and proline 1791 4242 NM 022521 c metabolism,Urea cycle and metabolism of amino groups 1793 6641 NM 022533 General 1794 8097 NM 022536 a 1795 8597 NM 022538 c,r,u 1795 8598 NM 022538 a 1797 21063 NM 022585 h TA'B'LETIiINAYS Atty. Docket No. 44921-Sti8~9fIVO
2: Doe. No. 179839 .1 PA enBamk entifierAccl odel CodePathways Sequence20781 Ref. S",e~,q.z ID No. ID No.

1800 20803 NM 022592 n Carbon fixation,Pentose phosphate cycle 1801 20925 N M 022594q 1802 20944 N M 022597as 1803 21024 NM 022599 o,General 1804 2250 NM 022643 General 1805 17567 NM 022672 a, 1806 17661 NM 022674 bb 1807 24563 N M 022676b 1807 24564 NM 022676 b,x 1809 20508 N M 022688g 1810 17586 N M 022694k 1811 17730 N M 022697a 1811 17729 N M 022697q 1812 154 N M 022849t 1813 127 N M 022855h 1814 152 N M 022858j 1816 18101 N M 022948z 1816 18103 NM 022948 a 1817 21491 N M 022951w 1818 15742 N M 022958y 1819 9286 NM 023027 t,w 1820 23215 N M 023102z 1821 21238 NM 024125 cc,Generall6,interact6-1 i 1821 21239 NM 024125 cc,Generall6,interact6-1 i 1822 353 NM 024127 i,n,General 1822 354 NM 024127 i,n,General 1822 352 NM 024127 h,General 1823 17227 N M 024131x 1825 1162 NM 024153 d Porphyrin and chlorophyll metabolism Oxidative phosphorylation,Type 1826 7863 NM 024156 c III protein secretion system 1827 22079 N M 024157x 1828 16476 NM 024162 General 1829 17765 NM 024351 b,s,v 1830 8879 NM 024360 h 1831 20772 N M 024363x Butanoate metabolism,Synthesis and 832 812 M 024386 l degradation of ketone bodies,Valine, eucine and isoleucine degradation 1833 335 NM 024387 j,y Porphyrin and chlorophyll metabolism 1834 21 NM 024388 cc 1834 22 NM 024388 cc 1836 9929 NM 024392 f Androgen and estrogen metabolism 1837 3582 NM 024396 as 1838 19993 NM 024398 e,p,s,aa 1840 22626 NM 024400 cc,General 1841 13633 NM 024403 g,General 1841 13634 NM 024403 g,General 1842 23387 NM 024404 b,General 1843 21038 NM 024484 h Glycine, serine and threonine metabolism 1844 1853 NM 030826 s Glutathione metabolism 1845 15111 NM 030827 e,General 1845 15112 NM 030827 y,z 1845 15110 NM 030827 General 1846 808 NM 030837 k,m 1847 4057 NM 030844 k 1848 1221 NM 030845 t 1849 21509 NM 030847 x 1850 1928 NM 030872 v TAf3'LETIiI7fIAYS ~Att~y. Docket No.
2: 449'21-5U'8~9f111~
PA enBank Acc/ Doc. No. 1798397.1 entifierRef. Seq. odel Is Sequence7342 ID No. Code Pathways ID No. NM 030873 a I

1852 24648 NM 030985 a 1852 25453 NM 030985 General 185 21802 NM 030987 h _ Glycerolipid metabolism,Glycolysis _ /
1854 3109 M 031000 s,z i Gluconeogenesis,Pentose f and glucuronate nterconversions 1855 34 NM 031003 a,u 1857 845 NM 031010 Prostaglandin and leukotriene 1 t metabolism 1857 25517 NM 031010 c,t Prostaglandin and leukotriene metabolism f f 1860 1719 NM 031024 n 1861 1350 NM 031030 h Arginine and proline metabolism,Glycine, 862 6775 M 031031 eneral serine and threonine metabolism,Urea cycle and metabolism of amino groups 1863 691 NM 031034 w 1864 15886 NM 031035 z 1866 3608 NM 031044 k,GeneralHistidine metabolism 1866 3610 NM 031044 d,GeneralHistidine metabolism 1867 15137 NM 031051 s 1868 514 NM 031056 General I nositol metabolism,Propanoate metabolism,Valine, 869 7269 M 031057 General leucine and isoleucine degradation 1870 11849 NM 031065 a 1871 1855 NM 031074 h 1872 4683 NM 031083 d 1873 15202 NM 031093 a 1873 15201 NM 031093 a,n 1874 12639 NM 031099 as 1875 20812 NM 031100 a 1876 16938 NM 031103 w 1877 19268 NM 031104 q 1878 16929 NM 031108 q 1879 10878 NM 031110 q,bb 1880 19162 NM 031111 as 1880 19161 NM 031111 a,bb 1881 24615 NM 031112 a,y 1882 20839 NM 031113 a,q 1883 19040 NM 031114 ,m,General I

1884 16349 NM 031115 a 1885 14970 NM 031127 General 1886 1814 NM 031134 n,q 1887 13359 NM 031135 General 1888 15052 NM 031136 a 1888 19359 NM 031136 a 1889 15185 NM 031140 General 1890 21625 NM 031144 a,e 1891 238 NM 031152 bb 1891 240 NM 031152 bb 1892 15277 NM 031237 g 1893 18083 NM 031315 q 1893 1858 NM 031315 q 1894 15663 NM 031318 General 1895 1422 NM 031324 bb,General Nucleotide sugars metabolism,Pentose and 896 8597 M 031325 ,bb glucuronate interconversions,Starch and sucrose metabolism 1897 11259 NM 031327 ,cc,General i 1898 4235 NM 031330 General TABLE TFiINAYS Atty. Docket No. 44'921-5U'8'9fIVO
2: Uoc. No. 1798397.1 PA enBank entifierAccl odel CodePathway's, Sequence8375 Ref. Seq. I,m ID No. D No.

1900 3519 NM 031334 cc 1901 20698 N M 031357b 1903 634 NM 031509 n Glutathione metabolism 1903 25525 NM 031509 n Glutathione metabolism 1903 25069 NM 031509 b,n,w 1903 635 NM 031509 z Glutathione metabolism 1904 848 N M 031517t 1905 872 NM 031523 a 1905 6245 NM 031523 a,d,u 1905 6244 NM 031523 a 1906 9370 NM 031527 w 1907 20448 NM 031530 General 1907 20449 NM 031530 General Androgen and estrogen i metabolism,Pentose and glucuronate 908 633 M 031533 a nterconversions,Porphyrin 1 and chlorophyll metabolism,Starch and sucrose metabolism 1909 6048 NM 031541 f ' Fatty acid metabolism,Tryptophan 1910 4011 NM 031543 c,q metabolism Fatty acid metabolism,Tryptophan 1910 4010 NM 031543 c,q metabolism Fatty acid metabolism,Tryptophan 1910 4012 NM 031543 q metabolism 1911 28 NM 031546 General 1912 24640 NM 031548 h,cc 1913 17149 NM 031549 x 1913 17151 NM 031549 x 1914 13105 NM 031552 w Fatty acid metabolism,Glycerolipid 1915 15411 NM 031559 d,r metabolism 1916 16164 NM 031563 a, 1917 9621 NM 031570 bb 1917 9620 NM 031570 w,bb 1918 546 NM 031573 f 1919 1921 NM 031576 f 1919 1920 NM 031576 r 1920 24219 NM 031579 i,General 1921 770 NM 031584 k,x 1922 18008 NM 031588 cc 1922 18005 NM 031588 h 1922 18011 NM 031588 cc,General 1923 1584 NM 031595 k 1924 24235 NM 031614 v Pyrimidine metabolism 1924 24234 NM 031614 General Pyrimidine metabolism 1925 1639 NM 031627 j,l,v 1926 1727 NM 031642 m,General 1929 1993 NM 031655 k,I,m,General 1930 2057 NM 031660 a 1931 15039 NM 031672 k,General Butanoate metabolism,Fatty acid biosynthesis (path b 2),Fatty acid 32 175 031682 metabolism,Lysine degradation,Tryptophan metabolism,Valine, leucine and isoleucine degradation 1933 1004 NM 031685 v 1934 19727 NM 031687 a,q,s 1935 20404 NM 031700 j,r,y 1935 20405 NM 031700 a,r TABLE THI'NAIfS A~tty. Docket No. 44'9'21-5U'8'9W0 2: floc. No. 1798397.1 FA enBank Accl entifierRef. Seq. oelel Pathways Sequence ID N-o:' Code Pantothenate and CoA
ID No. j~ : biosynthesis,Pyrimidine I 11 metabolism,beta-eneral Alanine metabolism Pantothenate and CoA
biosynthesis,Pyrimidine 936 12 M 031705 ,v,bb,Generalmetabolism,beta-Alanine metabolism 1937 16204 NM 031706 q,bb 1937 16205 NM 031706 a,y 1938 24081 NM 031708 m 1939 16918 NM 031709 a,q 1940 1081 NM 031712 General Fructose and mannose metabolism,Galactose ,n,u,cc,metabolism,Glycolysis 941 340 M 031715 General /
Gluconeogenesis,Pentose phosphate cycle Arginine and proline metabolism,Ascorbate and aldarate metabolism,Bile acid l biosynthesis,Butanoate metabolism,Fatty acid metabolism,Glycerolipid metabolism,Histidine s metabolism,Lysine 2 84 31731 j degradation,Propanoate metabolism,Pyruvate metabolism,Tryptophan metabolism,Valine, eucine and isoleucine degradation,beta-Alanine metabolism 1943 10241 NM 031740 d 1944 1214 NM 031741 r 1944 1215 NM 031741 r 1945 20724 NM 031753 h 1946 20753 NM 031763 h 1946 20752 NM 031763 y 1947 14953 NM 031774 p 1948 14184 NM 031776 ,GeneralPurine metabolism t 1948 14185 NM 031776 d,o,t,GeneralPurine metabolism 1949 1169 NM 031789 c 1950 16155 NM 031810 d,z 1950 16156 NM 031810 d 1951 17194 NM 031814 z 1952 17535 NM 031816 bb 1953 2655 NM 031821 ,l,m,aa i i 1955 22321 NM 031832 o,t,u,General 1956 4748 NM 031834 e,t 1956 4749 NM 031834 e,t Alanine and aspartate 1957 7914 NM 031835 a metabolism,Glycine, serine and threonine metabolism 1958 8385 NM 031836 h 1958 8384 NM 031836 h 1959 10268 NM 031838 a 1959 10269 NM 031838 as 1959 10267 NM 031838 n,aa 1960 15077 NM 031841 b 1961 16726 NM 031855 x Fructose and mannose metabolism 1962 25802 NM 031969 a 1962 19191 NM 031969 c r 1962 19190 NM 031969 p 1963 17734 NM 031970 v,General 1964 1475 NM 031971 v f 1966 18502 NM 031984 c 1967 19768 NM 031986 v,aa,General 1968 723 NM 032084 n TABI!E TH1I11AYS Atty. Docket No. 44'921-5U'89f11'10 2: Doc. No. 1798397~1j PA enBank Aecl entifierRef. Seq. ocJelode athways Sequence17935 ID No. a ID No. NM 032615 I

1970 16831 NM 033095 n 1971 25468 NM 033234 c,z 1971 25469 NM 033234 c 1971 17832 NM 033234 c,p 1971 17829 NM 033234 c,z 1972 4723 NM 033235 z 1973 1409 NM 033349 p,General P ruvate metabolism 1974 19998 NM 033352 General 1975 1410 NM 052798 d Cysteine 1976 15028 NM 052809 metabolism,Taurine f and hypotaurine metabolism 1977 5176 NM 053297 a i 1979 5117 NM 053310 p 1981 17473 NM 053319 a,v 1982 25480 NM 053329 g 1982 21977 NM 053329 y f 1983 14929 NM 053330 e,General 1984 16407 NM 053332 c,e 1985 15790 NM 053341 ,x j 1986 6154 NM 053356 p i 1988 6416 NM 053380 General 1989 19113 NM 053395 a 1990 2242 NM 053433 n,General 1991 5561 NM 053438 y 1992 14670 NM 053439 n,General 1993 17102 NM 053440 w 1994 24762 NM 053442 General 1995 8085 NM 053453 General 1996 4622 NM 053463 d 1997 21866 NM 053472 p 1998 9573 NM 053475 h 1999 16137 NM 053480 k 2000 15556 NM 053483 y 2001 16394 NM 053485 General 2002 4290 NM 053487 ,y j 2004 18826 NM 053523 d 2005 7764 NM 053525 as 2006 14199 NM 053538 c 2007 1058 NM 053539 c,d 2008 4327 NM 053563 General 2009 1342 NM 053573 h Methane 2010 19254 NM 053576 h,s metabolism,Phenylalanine metabolism Methane 2010 19253 NM 053576 h metabolism,Phenylalanine metabolism 2011 3049 NM 053582 p,cc,General 2011 3050 NM 053582 o,General 2012 21423 NM 053586 s,y Oxidative phosphorylation 2013 21445 NM 053587 ,v t 2014 20871 NM 053591 ,l j I

2015 21044 NM 053594 d 2016 21709 NM 053596 k 2016 21708 NM 053596 z t 2018 5565 NM 053618 General 2019 13004 NM 053623 Fatty t acid metabolism TABLE THWAYS A'tty. Docket No. 44'921-5U891N0 2: Doe. No. 1798397.1 PA enBank entifier~cc/ NoeJel Pathwiay~s Sequence Ref. Seq. Code Arginine and proline ID No. 1U No. metabolism,D-Arginine I 127 g and D-ornithine metabolism,Glycine, serine M 053626 and threonine metabolism 2021 18644 NM 053648 n 2022 21637 NM 053653 p 2023 3454 NM 053662 cc 2024 16121 NM 053698 h,j,z 2024 16122 NM 053698 h,j,z 2025 25379 NM 053713 General 2025 13622 NM 053713 General 2026 15376 NM 053747 h 2027 1218 NM 053748 b 2028 1137 NM 053763 y 2029 15996 NM 053769 cc 2030 8652 NM 053774 g 2031 14664 NM 053806 General 2032 4361 NM 053812 k 2034 15002 NM 053819 b,x,bb,General b,l,x,bb, 2034 15003 NM 053819 General 2035 16173 NM 053822 t 2036 17154 NM 053835 j,z 2037 20868 NM 053843 t 2037 20869 NM 053843 t 2040 714 NM 053863 y 2041 19781 NM 053883 b 2041 19780 NM 053883 b 2042 1454 NM 053887 General 2043 1660 NM 053891 g 2044 712 NM 053896 k 2045 753 NM 053897 k 2046 794 NM 053902 General Tryptophan metabolism 2047 17937 NM 053911 f 2048 8188 NM 053927 General 2050 1628 NM 053936 h 2051 13954 NM 053955 General 2052 408 NM 053961 General 2052 19991 NM 053961 a 2052 16190 NM 053961 q 2052 21355 NM 053961 j,1, ,z 2055 15136 NM 053971 as 2055 15135 NM 053971 d 2056 1764 NM 053974 h 2058 15468 NM 053982 q 2059 15642 NM 053985 General 2060 21066 NM 054001 t 2061 17327 NM 054008 cc 2061 17329 NM 054008 g,o,cc 2062 25253 NM 057099 j,l,m, ,z 2062 22849 NM 057099 j,1 2063 19657 NM 057103 b,cc Androgen and estrogen i metabolism,Pentose and glucuronate 064 492 M 057105 w nterconversions,Porphyrin and chlorophyll metabolism,Starch and sucrose metabolism Androgen and estrogen i metabolism,Pentose and glucuronate 064 126 M 057105 r nterconversions,Porphyrin 1 and chlorophyll metabolism,Starch and sucrose metabolism TABLE TIiINAYS Atty. Docket No. 4492'1-508~9fIVO
2: Doc. No.1798397.1 FA enBank Accl entifierRef. Seq. odel Pathways j"'~
Sequence ID No. Code Androgen and estrogen ~ID metabolism,Pentose No. i and glucuronate I 5125 nterconversions,Porphyrin M 057105 s and chlorophyll metabolism,Starch and sucrose metabolism 2066 15391 NM 057114 n 2067 727 NM 057123 m 2068 915 NM 057124 s 2069 15151 NM 057131 k 2070 1892 NM 057144 b f 2071 12331 NM 057155 v,General 2071 12332 NM 057155 ,General f 2072 17477 NM 057194 a,General 2073 15408 NM 057197 p,t t 2074 7866 NM 057198 h Glutamate metabolism,Purine metabolism 2075 14125 NM 057208 h,j,y,z 2076 1743 NM 057210 k,s 2077 10498 NM 078617 a 2078 8820 NM 080399 n 2079 15701 NM 080581 ,m,y,z j 2079 20105 NM 080581 as 2080 16109 NM 080585 c 2081 1757 NM 080766 d 2082 7108 NM 080778 y 2083 132 NM 080782 k 2084 20122 NM 080887 General 2085 6143 NM 080892 a 2086 9952 NM 080902 h 2087 17546 NM 130401 b 2088 21695 NM 130411 c,x 2089 21391 NM 130416 x,General 2090 20694 NM 130430 General 2090 19818 NM 130430 cc 2090 18810 NM 130430 e,s Bile acid biosynthesis, Fatty acid q biosynthesis (path 2),Fatty acid 91 293 130433 metabolism,Phenylalanine metabolism,Valine, leucine and isoleucine degradation 2092 25064 S45392 a,n 2093 3244 S63519 a 2094 25501 S63521 q 2095 16248 S68135 h 2096 18647 S69316 q 2097 24351 S74257 v 2098 25066 S75280 d j ~l,m,x,Y, 2099 1460 S76054 General 2100 25539 S76742 v 2101 16400 S76779 c 2102 24469 S77858 n 2103 25545 S77900 k,s 2103 21583 S77900 k 2104 10260 S81497 s 2105 3609 S82579 k Histidine metabolism 2106 111 002506 a 2107 4959 003390 a,q,General 2109 2010 005675 b,x,bb 2110 15462 006230 d 2112 1583 007201 s,General 2113 627 009229 h TA~B'LETH111t/AYS Atty. Docket No. 44'921-5U'89fNO
2: Doe. No. 1798397.1 PA enBank Aeel entifierRef. Seq. odel Path~w bays ~ I
~Sequenee809 ID No. Code ID No. 017035 General I

2115 16675 017565 k,x,bb 2116 25587 020110 r 2117 90 020796 r 2118 25589 021718 h,aa 2119 22196 021719 h 2120 17118 025746 s 2121 1537 027518 g,h,n 2122 1558 028504 bb 2123 16193 030831 n 2124 17480 031598 z 2125 18302 033500 General 2126 25599 034897 y 2127 1394 037099 h 2128 244 038376 n 2129 1623 041164 h 2130 15851 042719 f ,t,x,General 2131 17886 047315 s,z 2132 21654 053184 i ,t,General 2133 1439 057391 w 2134 725 062316 bb 2137 2153 075404 b,cc,General 2139 4956 076714 j ,y 2140 4477 077829 I ,m 2141 21703 082591 z 2142 977 089744 s 2143 23282 090725 h 2144 22005 096490 m Carbon fixation,Fructose and mannose metabolism,Glycolysis 146 19 02284 j z /
Gluconeogenesis,lnositol metabolism,Pentose phosphate cycle Carbon fixation,Fructose and mannose metabolism,Glycolysis 147 18 02291 ,j,z /
Gluconeogenesis,lnositol metabolism,Pentose phosphate cycle 2148 20818 X02904 n,q Glutathione metabolism 2149 16401 X04979 c Carbon fixation,Glycolysis /
150 0513 05684 ,r Gluconeogenesis,Purine metabolism,Pyruvate metabolism 2151 25084 X06769 cc 2152 672 X13722 h 2153 25675 X14181 n 2153 20810 X14181 n,q,w 2154 18541 X14671 y 2155 25679 X15013 q 2155 19244 X15013 c,q,w 2156 15626 X17665 a Glycerolipid metabolism,Phospholipid degradation,Prostaglandin 157 893 51529 t and leukotriene metabolism 2158 25686 X51536 bb 2158 10819 X51536 aa,bb 2159 18250 X51706 a,q,w 2160 20872 X51707 a 2161 516 X52711 c 2162 25689 X52815 g 2163 20427 X53378 w 2164 18606 X53504 General 2165 1463 X54467 d,u,General 2166 2 X55153 a,v X2167 _ X57405 j ,m ~ - _ -. 10344 J

TABLE THfNAIfS A~tiy. Docket No. 44'921-508~9V1'IO
2: Doc. No. 1798397.1 PA enBank Accl entifierRef. Seq. odel Pathways ~ , Sequence15106 ID No. Code ID No. X57529 g,n,q I

2169 5667 X58200 q,bb 2169 18611 X58200 a,v 2170 17175 X58389 w 2171 25702 X58465 w 2171 10109 X58465 c,q 2172 25705 X59375 c,i,aa,General 2173 25709 X59737 a 2174 18354 X59859 General 2174 18355 X59859 t 2175 21657 X61381 General 2176 25718 X62145 bb,General 2176 15875 X62145 a,q,v 2177 13646 X62166 bb 2178 25721 X62325 p 2179 16012 X62875 m,s,z 2180 25730 X63369 cc 2181 25089 X63594 General 2181 25090 X63594 cc,General 2182 20844 X65228 n,w 2183 20879 X65296 j ,y 2184 25736 X68782 c 2185 16426 X70369 c 2186 16300 X70706 a 2187 24232 X75207 c 2188 16272 X76456 n,p 2189 25741 X76489 a 2190 23302 X78949 h 2191 25747 X81448 General 2192 24115 X81449 a 2193 25754 X89696 g 2194 25097 X90642 ,z 2195 12978 X96437 cc,General 2197 4594 Y07704 c 2198 25777 Y08355 g,p,General 2199 15986 Y09945 bb,General 2200 20890 Y13275 k 2201 21914 Y13336 d 2202 406 211995 o,General 2203 18352 212298 t 2204 17481 249761 k 2205 8664 275029 r ,v 2206 2459 AA964755 cc 2207 23830 AA956638 as 2208 6100 X73524 x 2209 439 222607 w 2210 8665 A1071965 v 2211 155 U32681 t Methane metabolism,Phenylalanine 2212 19252 AA892041 s metabolism 2213 15582 AI232320 q 2214 17541 M26125 n 2215 18609 M30689 i 2216 6262 A1177125 g f 2218 21011 H32189 a Glutathione metabolism 2220 2572 AI17 b 2221 2541g _ I
- ~ ~ M22922 -I

TABLE 3: OMOLOGUE N~TA1'1~NS A tt~y. Docket No.

Uoe. No. 1798397.1' aSeq. 1U GenBank Homologous Aee.! Gene No. IdentifierRef. Seq.Model Name Hom~,oklogous Cluster 1U No: Code Name 1 6949 AA012785 q 2 25098 AA108277 h;y -EST, Moderately similar to A
Chain A, Mdm2 Bound To The Transactivation Domain Of {SUB

[H.sapiensj, mouse double minute 2, human homolog of;
p53-binding 3 17312 AA108308 r protein NADH
dehydrogenase (ubiquinone) 4 16882 AA684537 o beta subcomplex, (16kD, SGDH) EST, Weakly similar to nascent polypeptide-associated complex alpha chain, non-muscle splice form -mouse [M.musculusj, FKSG17, Homo Sapiens alpha-NAC

gene for nascent polypeptide-associated complex component, protein, expressed sequence AL022831, nascent-polypeptide-associated complex alpha 6049 AA685178 pol peptide 6 4426 AA685974 I,m EST, Weakly similar to hypothetical protein DKFZp434C1920.1 [H.sapiensj, hepatocellular carcinoma-associated 7 21815 AA686423 g antigen DNA-damage inducible transcript 3, EST, Moderately similar to GA15_HUMAN
GROWTH
ARREST

DNA-damage AND
inducible DNA-DAMAGE-INDUCIBLE

transcript PROTEIN
3, DNA-damage-GADD153 [H.sapiens], 8 1600 AA686470 i inducible myozenin transcript DNA-damage inducible transcript 3, EST, Moderately similar to GA15_HUMAN
GROWTH
ARREST

DNA-damage AND
inducible DNA-DAMAGE-INDUCIBLE

transcript PROTEIN
3, DNA-damage-GADD153 [H.sapiens], 8 1599 AA686470 i inducible myozenin transcript 9 21997 AA799325 a 18396 AA799330 v ESTs, Highly similar to ERR3_HUMAN

ESTROGEN-RELATED
RECEPTOR

GAMMA
[H.sapiens], Untitled, e strogen related receptor, alpha, e strogen related receptor, beta, 11 6581 AA799412 f,1 e strogen-related receptor beta ESTs, Moderately similar to NPL4_HUMAN
NUCLEOSOME

ASSEMBLY
PROTEIN

( H.sapiens], ESTs, Weakly similar to NPL4_HUMAN
NUCLEOSOME

ASSEMBLY
PROTEIN

[ H.sapiens], SET
translocation, n ucleosome assembly protein 1-like 1, 12 16538 AA799449 k n ucleosome assembl rotein 1-like 13 23294 AA799472 a CGI-116 rotein X14 - - AA799497 r 18290 ~ - ~

TABLEHUMAN OMOLOGUE N~TATI~N8 ~ltty. Doeke No.
3: H AN 44921-5U89W0 Doe. No. 1798397.1 Seq. GenBank Homologous 1U Aee./ Gene Tlo. IdentifierRef. Seq.MocJel Name 9 Ho",rn,~ologo,~",us 1U No. Code Cluster Name DAZ
associated protein 1, ESTs, Highly similar to RAT

HETEROGENEOUS
NUCLEAR

RIBONUCLEOPROTEIN

[R.norvegicus], ESTs, Moderately similar to Up1, The Two Rna-Recognition Motif Domain Of Hnmp {SUB

[H.sapiens], ESTs, Weakly similar to RAT

HETEROGENEOUS
NUCLEAR

RIBONUCLEOPROTEIN

[R.norvegicus], ESTs, Weakly similar to MOUSE
HETEROGENEOUS

NUCLEAR
RIBONUCLEOPROTEINS

[M.musculus], RIKEN
cDNA

gene, Ras-GTPase activating protein domain-binding protein 2, Ras-GTPase-activating protein SH3-domain binding protein, cell death regulator aven, heterogeneous nuclear ribonucleoprotein A1, heterogeneous 15 18981 AA799523 a nuclear ribonucleoprotein EST, Moderately similar to ring complex protein TRiC5 [H.sapiens], T-complex 1, chaperonin containing TCP1, subunit (gamma), expressed sequence AI528772, t-i6 20843 AA799545 h complex 1, t-complex rotein 17 16993 AA799560 b 18 16576 AA799570 d EST, Moderately similar to beta tubulin [H.sapiens], ESTs, Highly similar to beta-tubulin [H.sapiens], ESTs, Highly similar to tubulin beta chain [H.sapiens], ESTs, Highly similar to RAT

TUBULIN
BETA
CHAIN

[R.norvegicus], ESTs, Moderately similar to beta-tubulin [H.sapiens].
RIKEN
cDNA

gene, RIKEN
cDNA

gene, RIKEN
cDNA

gene, Rat mRNA
for beta t ubulin T
beta15, beta tubulin 1, class 19 18361 AA799591 VI, i tubulin, beta 3, tubulin, beta, 20 17712 AA799598 z f I

DiGeorge syndrome chromosome region 6, DiGeorge syndrome critical region gene 6, DiGeorge syndrome 24 11687 AA799732 w critical re ion gene like 25 18349 AA799744 a 26 17494 AA799751 n 27 18360 AA799771 General 28 18880 AA799801 w EST, Moderately similar to MAS2_HUMAN
MANNAN-BINDING

LECTIN
SERINE
PROTEASE

PRECURSOR
[H.sapiens], Rattus norvegicus mRNA
for serine protease, complete cds, complement r-like proteinase precursor"
complement component 1, r subcomponent, complement component 1, s 29 20998 AA799803 subcom z onent, rotein C

TABLE 3: OMOLOGUE N~TATIONS ~tt~y. Docket No.

Doe. No. 1798397.

_ GenBank Hornologo Seq. ID Aec.l s Gene ~

No. IdentifierRef. Seq.Model Name Homo~,lrog~s Cluster ID No. Code Name 30 21006 AA799861 c interferon re ulato factor 7 ESTs, Moderately similar to Up1, The Two Rna-Recognition Motif Domain Of Hnrnp A1 {SUB 3-184 [H.sapiens], ESTs, Weakly similar to ROA1 RAT

HETEROGENEOUS NUCLEAR

RIBONUCLEOPROTEIN

[R.norvegicus], ESTs, Weakly similar to heterogeneous ribonuclear particle protein A1 [H.sapiens], Human DNA

sequence from clone RP11-51N22 on chromosome 13 Contains ESTs, STSs and GSSs. Contains an HNRPA1 (heterogeneous nuclear ribonucleoprotein A1) pseudogene, RIKEN cDNA 4930547K05 gene, heterogeneous nuclear 31 15011 AA799893 General ribonucleoprotein EST, Moderately similar to RLiX_HUMAN 60S RIBOSOMAL

PROTEIN L18A [H.sapiens], EST, Weakly similar to RL1X_HUMAN 60S

RIBOSOMAL PROTEIN

[H.sapiens], EST, Weakly similar to S47353 ribosomal protein LlBa, cytosolic [H.sapiens], ESTs, Highly similar to RL1X_HUMAN

RIBOSOMAL PROTEIN

[H.sapiens], RIKEN
cDNA 2510019J09 32 20811 AA799899 a gene, ribosomal protein L18a 33 23202 AA799971 General ESTs, Moderately similar to 1701409A

glycogen phosphorylase [H.sapiens], ESTs, Weakly similar to 1701409A

glycogen phosphorylase [H.sapiens], 34 4832 AA800190 b hospho lase, g1 cogen; brain 35 21656 AA800202 d 36 18433 AA800218 . ,z j 37 6386 AA800235 a 38 18442 AA800258 h,k DNA segment, Chr 14, University of California at Los Angeles 2, Hydroxysteroid dehydrogenase,ll beta type 1, expressed sequence C79874, hydroxysteroid (11-beta) dehydrogenase 1, hydroxysteroid beta dehydrogenase 1, hydroxysteroid 17-beta dehydrogenase 11, retinal short-chain dehydrogenase/reductase 39 21092 AA800380 retSDR2 ESTs, Highly similar to GSHG_MOUSE GLUTATHIONE

PEROXIOASE-GASTROINTESTINAL

(GSHPX-GI) [M.musculus], Glutathione peroxidase 1, glutathione peroxidase 1, glutathione peroxidase 2 40 17325 AA800587 General (gastrointestinal zinc finger protein 36, zinc finger protein homologous to Zfp-36 in 41 13930 AA800613 cc, General mouse 42 21372 AA800693 v 42 21373 AA800693 s 43 18161 AA800701 k 44 6595 AA800753 w 45 13348 AA800928 General -1 as-TABLE: HUMANOMOLOGUE NOTATIONS Atty. Docket No.

Uoc. No. 1798397.1 ~Seq. GenBank Homologous ID Aee.l Gene No. IdentifierRef. Seq. Model Narne Homologo~,","aus ID No. Code Cluster Name EST, Weakly similar to H2AL_HUMAN

HISTONE H2A.L (H2A/L) [H.sapiens], H2A histone family, member L, similar t o H2A histone family, member A (H.

46 23115 AA801165 0, Sapiens) 47 12399 AA801307 General 48 7543 AA801395 General 49 24237 AA817726 ,General t 51 5985 AA818005 g EST, Weakly similar to RB6K MOUSE

RABKINESIN-6 [M.musculus], i nteracting, kinesin-like (rabkinesin 6), RIKEN cDNA 3110001D19 gene, 52 11338 AA818016 x Rab6, kinesin-like COP9 (constitutive photomorphogenic), subunit 6 ( Arabidopsis), Homo Sapiens cDNA

FLJ14833 fis, clone OVARC1001171, moderately similar to Homo Sapiens t ranslation initiation factor 3 47 kDa subunit mRNA, IFP38, RIKEN cDNA

0610037M02 gene, eukaryotic t ranslation initiation factor 3, subunit ( epsilon, 47kD), hypothetical protein MGC13045, proteasome (prosome, macropain) 26S subunit, non-ATPase, 53 2845 AA818026 k,General 7 54 16756 AA818089 ,k,General glycyl-tRNA s nthetase i EST, Weakly similar to S45140 tubulin beta chain [H.sapiens], RIKEN cDNA

2410129E14 gene, RIKEN cDNA

4930542603 gene, tubulin, beta 2, t ubulin, beta 5, tubulin, beta 55 17771 AA818224 e,g,p,General of peptide, tubulin, beta, 2 56 6522 AA818261 g,m 58 7806 AA818421 b,aa 59 8237 AA818512 v 60 17434 AA818574 h 61 8728 AA818615 General d iphtheria toxin receptor ( heparin-bindingiphtheria toxin epidermal receptor (heparin-d growth factor-likebinding epidermal growth growth factor-like f actor), heparinrowth factor), expressed binding g sequence epidermal AW047313, heparin growth factor-binding epidermal 62 6054 AA818658 b,v,cc,Generalike growth rowth factor-like l factor g growth factor 63 11590 AA818721 d 64 4291 AA818741 ,General 65 4330 AA818747 o,General 66 19723 AA818761 v,General 67 13684 AA818770 h,j,l,m 68 6322 AA818801 k e xpressed sequence AV066530, g uanylate cyclase activator 2B

( uroguanylin), guanylate cyclase 69 7690 AA818875 General a ctivator 2b (retina) 70 4952 AA818907 q,General t 72 10985 AA818998 o,General t TABLEHUMAN OMOLOGUE N~TATI~N~S Attsy. Docket tJo.
3: H AN 44921-5U89W0 Doe. No. 1798397.

Seq. GenBank Homologous ID Aee.! Gene No. dentifierRef. Seq.Model Name Homol_ogp~us Cluster I I~ No. Code Name CocoaCrisp, ESTs, Weakly similar to J C5308 testis-specific, vespid, and pathogenesis-related protein 1 precursor [H.sapiens], Homo Sapiens, Similar to RIKEN
cDNA 1700011E04 gene, clone MGC:26856 I MAGE:4822995, mRNA, complete c ds, RIKEN cDNA 1200009H11 gene, RIKEN cDNA 1700011 E04 gene, RIKEN cDNA 4921508011 gene, acidic epididymal glycoprotein-like 1, glioma pathogenesis-related protein, s pecific granule protein (28 kDa), testis s pecific gene 1, testis specific protein 1 , testis specific protein 1 (probe 74 2586 AA819081 c p3-1 77 24721 AA819306 d,w ESTs, Weakly similar to T17246 hypothetical protein DKFZp586M0617.1 [H.sapiens], KIAA0263 gene product, mammalian 78 6250 AA819376 o,y i nositol hexakis hos hate kinase HYA22 protein, conserved gene amplified in osteosarcoma, nuclear 80 6281 AA819517 LIM interactor-interacting factor 82 6551 AA819558 t 83 6723 AA819653 r 84 14958 AA819744 as ESTs, Highly similar to HS9B RAT

HEAT SHOCK PROTEIN

BETA [R.norvegicus], expressed s equence AL024080,expressed s equence C81438, heat shock 90kD

protein 1, beta, heat shock protein, 85 19433 AA819776 v kDa 1 86 6204 AA819889 as GMPR2 for guanosine monophosphate r eductase isolog, IMP (inosine monophosphate) dehydrogenase 2, RIKEN cDNA 2310004P21 gene, RIKEN cDNA 5730544D12 gene, expressed sequence AA959850, guanosine monophosphate reductase, 87 22820 AA848315 General i nosine 5'- hosphate deh drogenase 2 88 6614 AA848389 bb 89 21125 AA848437 General ESTs, Moderately similar to I F4B_HUMAN EUKARYOTIC

TRANSLATION INITIATION
FACTOR

4 B [H.sapiens], eukaryotic translation 90 23504 AA848496 i nitiation factor ESTs, Highly similar to FM02_HUMAN

DIMETHYLANILINE

MONOOXYGENASE [H.sapiens], Flavin-containing monooxygenase 1, fl avin containing monooxygenase 1, fl avin containing monooxygenase 2, fl avin containing monooxygenase 3, 91 18532 AA848675 g hypothetical protein 92 21140 AA848738 c 94 22923 AA848929 g 95 17339 AA849497 General 97 21275 AA849796 i,I,m,General -1 ss-TABLE: HUMANOMOLOGUE N~TATI~NS Att~y. Docket No.

Doe. No. 1798597.1 3Seq. GenBanl Homologous ID Acc.l Gene .No. IdentifierRef. SeqeModel Name Homoho~go,~us Cluwter ID No. Code Narne 98 16678 AA849827 as 99 8515 AA849917 a 100 18447 AA849939 General RIKEN cDNA 2810452609 gene, adenylyl cyclase-associated CAP

protein homolog 1 (S. cerevisiae, S.

pombe), adenylyl cyclase-associated 102 23981 AA850040 ,aa protein x t 105 2637 AA850893 DKFZP434O125 protein x 106 22093 AA850909 d 107 21766 AA850916 c ESTs, Highly similar to LB4D_HUMAN

NADP-DEPENDENT
LEUKOTRIENE

[H.sapiens], ESTs, Weakly similar to FAS RAT FATTY ACID
SYNTHASE

[R.norvegicus], ESTs, Weakly similar to LB4D_HUMAN NADP-DEPENDENT

HYDROXYDEHYDROGENASE

[H.sapiens], crystallin, zeta, fatty acid 108 2847 AA850919 w s nthase 109 12162 AA850975 h 110 9514 AA850978 General 111 3924 AA851017 e,q 111 3925 AA851017 o,General 112 4490 AA851184 a,k cathepsin Z

113 19187 AA851230 General RIKEN cDNA 1110058H21 gene, 114 19189 AA851237 c ubiquitin s ecific protease 18 breast cancer metastasis-suppressor 115 15386 AA851241 m 1, h pothetical protein MGC11296 116 21462 AA851261 g,I,General ART-4 rotein 117 21471 AA851343 General NADH dehydrogenase (ubiquinone) Fe S protein 8 (23kD) (NADH-coenzyme 118 16902 AA851379 p Q reductase) 119 23376 AA851392 ,x kinesin-like 4 i 119 23377 AA851392 kinesin-like 4 x 120 13349 AA851417 General 121 21527 AA851733 ,u r EST, Moderately similar to PM17 MOUSE MELANOCYTE
PROTEIN

[M.musculus], Homo sapiens, Similar to glycoprotein (transmembrane) nmb, clone MGC:1696 IMAGE:3345861, mRNA, complete cds, glycoprotein 122 4048 AA851814 ,o,u,General (transmembrane) i nmb, silver signal sequence receptor, alpha 123 10561 AA851871 bb (translocon-associated protein al ha) ESTs, Weakly similar to A60021 tropomyosin-related protein, neuronal -rat [R.norvegicus], RIKEN cDNA

0710005K15 gene, expressed sequence 875279, reticulon 1, 124 17411 AA858621 reticulon 3 expressed sequence AI747533, mini chromosome maintenance deficient 7 (S. cerevisiae), minichromosome 125 1801 AA858636 k,s,x,bb maintenance deficient (S. cerevisiae) 126 18350 AA858674 p 127 19484 AA858693 a 128 6360 AA858696 d -18s-TABLEHUMAN OMOLOGUE N~'fAT'IONB Att~y. Uoe et No.
3: H AN 44921-SU89W~

Doe. No. 1798397.1 ~Seq. GenBank Homologous ID Aec./ Gene C

No. IdentifierRef. Seq.iModel Name Hom~olo4gous ID No. Code luster Name exostoses (multiple) 1, exostoses (multiple)-like 1, expressed sequence 130 6380 AA858758 q 131 13219 AA858759 a 132 6384 AA858788 I,m,General LanC (bacterial lantibiotic synthetase component C)-like, LanC (bacterial lantibiotic synthetase component C)-134 13412 AA858830 p like 1, RIKEN cDNA
1700003F10 gene 135 7279 AA858892 f 136 18217 AA858930 t asparaginyl-tRNA
synthetase, 137 5867 AA858953 v,General by othetical protein Interleukin 1 receptor accessory protein, Mus musculus IL-1Rrp2 mRNA, complete cds, interleukin 1 receptor accessory protein-like 2, interleukin 1 receptor, type I, 138 14479 AA858969 r interleukin 18 receptor 139 6431 AA859085 t 140 17361 AA859114 o,General EST, Highly similar to OM25_RAT

MITOCHONDRIAL OUTER

MEMBRANE PROTEIN
25 (NPW16) [R.norvegicus], EST, Weakly similar to OM25_RAT MITOCHONDRIAL

OUTER MEMBRANE PROTEIN

(NPW16) [R.norvegicus], Erbb2 i nteracting protein, discs, large homolog 4 (Drosophila), expressed sequence AI118201, hypothetical protein FLJ11271, synaptojanin 2 141 21025 AA859241 General binding protein 142 10076 AA859271 c EST, Moderately similar to CYSR
RAT

CYSTEINE-RICH PROTEIN

[R.norvegicus], ESTs, Weakly similar to S12658 cysteine-rich protein [H.sapiens], cysteine and glycine-rich protein 1, cysteine and glycine-rich protein 3 (cardiac LIM protein), cysteine rich protein, cysteine-rich protein 2, cysteine-rich protein 3, 143 21791 AA859333 k t h mus LIM rotein 144 16314 AA859348 cc,General 145 18862 AA859520 f 146 15059 AA859545 r EST, Highly similar to SPERM-COATING GLYCOPROTEIN

PRECURSOR [R.norvegicus], ESTs, Weakly similar to JC4131 glioma pathogenesis-related protein [ H.sapiens], Human DNA sequence f rom clone RP5-881 L22 on chromosome 20 Contains ESTs, GSSs, STSs and CpG
islands.

Contains a gene for a novel protein similar to a trypsin inhibitor and four other genes for novel proteins, RIKEN

cDNA 1810049K24 gene, RIKEN

cDNA 2410114014 gene, RIKEN

cDNA 9230112K08 gene, acidic epididymal glycoprotein 1, acidic epididymal glycoprotein 2, epididymal glycoprotein, glioma pathogenesis-147 9894 AA859581 s r elated rotein TABLE 3: OMOLOGUE OTATIONS Atty. Docket No.

Doe. No. 1798397.

~5eq. ID GenBan Homologous Aec.l Gene No. IdentifierRef. Seq. Model Name Homologous Cluster I~ No. Code Name h DnaJ (Hsp40) homolog, subfamily B, member 1, DnaJ (Hsp40) homolog, s ubfamily B, member 5, DnaJ (Hsp40) h omolog, subfamily B, member 6, DnaJ (Hsp40) homolog, subfamily B, member 8, ESTs, Weakly similar to DnaJ-like protein [M.musculus], ESTs, Weakly similar to [ R.norvegicus], Homo sapiens cDNA

FLJ13992 fis, clone Y79AA1002139, weakly similar to DNAJ PROTEIN

HOMOLOG 1, RIKEN
cDNA

1 700029A20 gene, RIKEN cDNA

149 16318 AA859648 2010306619 ene h 150 17316 AA859652 General 151 19067 AA859663 n,q 152 22406 AA859680 n x 154 14261 AA859693 a 155 14138 AA859700 v rotoporphyrinogen oxidase 155 14139 AA859700 v rotoporph rinogen oxidase I

ESTs, Weakly similar to PROTEIN-PRECURSOR

[ R.norvegicus], Lysyl oxidase, lysyl oxidase, lysyl oxidase-like, lysyl 158 22385 AA859805 b,k oxidase-like 1, I s I oxidase-like 159 22773 AA859885 n 160 22816 AA859898 k,x,z 161 11891 AA859926 x EST, Weakly similar to JC1343 glycylpeptide N-t etradecanoyltransferase [H.sapiens], 162 23070 AA859942 k N-m ristoyltransferase 163 23121 AA859948 k 164 23166 AA859954 cc,General Homo Sapiens cDNA
FLJ14666 fis, clone NT2RP2003000, weakly similar t o TUMOR NECROSIS
FACTOR, ALPHA-INDUCED PROTEIN
1, Homo Sapiens polymerase delta-interacting protein 1 mRNA, complete cds, MSTP028 protein, tumor necrosis f actor, alpha-induced protein 1 165 18468 AA859966 as ( endothelial) ESTs, Moderately similar to A Chain A, I nositol Monophosphatase [H.sapiens], I nositol (myo)-1(or4)-monophosphatase 1, RIKEN cDNA

2900059K10 gene, bisphosphate 3'-nucleotidase 1, inositol (myo)-1(or4)-monophosphatase 1, inositol (myo)-1 (or 4)-monophosphatase 2, i nositol(myo)-1 (or 4)-monophosphatase 1, inositol(myo)-166 23336 AA859981 q 1 (or 4)-monophosphatase EST, Moderately similar to EF1G_HUMAN ELONGATION

FACTOR 1-GAMMA [H.sapiens], ESTs, Highly similar to EF1G_HUMAN

ELONGATION FACTOR

[ H.sapiens], Homo Sapiens cDNA

FLJ11216 fis, clone PLACE1008002, eukaryotic translation elongation factor 167 4222 AA860024 a,bb 1 gamma TABLE: HUMANHOMOLOGUEN~TATIONS Atty. Docket No.

Doe. No. 1798597.1 ~Seq. GenBanl _ Homologous 1U Acc./ ~ Gene No. IdentifierRef. Seq.Model Narne Homo~,~,,",",lo~
I~ No. Code gnus CIuster Name EST, Moderately similar to 138369 beta t ubulin [H.sapiens], EST, Weakly similar to 138369 beta-tubulin [ H.sapiens], EST, Weakly similar to [ M.musculus], ESTs, Highly similar to A25113 tubulin beta chain 15 - rat [ R.norvegicus], FK506-binding protein 1A (12kD), RIKEN
cDNA 2310061K05 gene, RIKEN cDNA

gene, tubulin, beta 2, tubulin, beta 5, 168 13974 AA860030 u,x,Generalt ubulin, beta pol peptide Mus musculus 12 days embryo male wolffian duct includes surrounding r egion cDNA, RIKEN
full-length enriched library, clone:6720466F14, f ull insert sequence, RIKEN cDNA

hyaluronan 0610027D24 gene, mediated TRAF4 associated motility receptoractor 1, hyaluronan (RHAMM), mediated motility f hyaluronan-mediatedeceptor (RHAMM), r hyaluronan-169 7090 AA860039 x motilit receptormediated motili (RHAMM) receptor (RHAMM) DKFZP547E2110 protein, hypothetical 170 23769 AA860055 k,x protein FLJ10604 171 16323 AA866240 w EST, Weakly similar to PE2R RAT 20-ALPHA-HYDROXYSTEROID

DEHYDROGENASE [R.norvegicus], Mus musculus 10 days embryo cDNA, RIKEN full-length enriched library, clone:2610528B18, full insert sequence, RIKEN
cDNA 9430025F20 gene, Rattus norvegicus mRNA for 20-alpha-hydroxysteroid dehydrogenase ( 20-alpha-HSD), complete cds, aldo-keto reductase family 1, member C1, aldo-keto reductase family 1, member C4 (chlordecone reductase; 3-alpha hydroxysteroid dehydrogenase, type I;

dihydrodiol dehydrogenase 4), expressed sequence AI315367, expressed sequence AI503553, hydroxysteroid (17-beta) 172 4462 AA866264 General deh drogenase 5 ESTs, Highly similar to A54602 microtubule-associated serine/threonine protein kinase MAST205 - mouse [M.musculus], ESTs, Moderately similar to A54602 microtubule-associated serine/threonine protein kinase MAST205 - mouse [M.musculus], Homo sapiens cDNA:
FLJ21699 fis, clone COL09829, KIAA0303 protein, KIAA0807 protein, Mus musculus adult male cecum cDNA, RIKEN full-length enriched library, clone:9130026D18, f ull insert sequence, microtubule associated testis specific serine/threonine protein kinase, syntrophin associated serine/threonine 173 15884 AA866276 k kinase TABLEHUMAN OMOLOGUE NOTATIONS Atty. Docket No.
3: H AN 44921-5U89W0 Uoe. No 1798397.1 -~Seq. GenBank ~ Homologous I~ Aee./ Gene No. dentifierRef. Seq.Model Name Homolo~gyus Clus I ID No. Code er Name 4-hydroxyphenylpyruvate dioxygenase, 4-hydroxyphenylpyruvic acid dioxygenase, ESTs, Weakly similar to HPPD

HYDROXYPHENYLPYRUVATE

4-hydroxyphenylpyruvateDIOXYGENASE [M.musculus], ESTs, dioxygenase, Weakly similar to 4- S32820 alloantigen F

hydroxyphenylpyruvic- rat [R.norvegicus], acid hypothetical 174 17742 AA866302 c, diox genase protein MGC15668 ESTs, Highly similar to BAND 3 ANION EXCHANGE PROTEIN

[M.musculus], ESTs, Weakly similar to solute carrierB3HU band 3 anion family 4 transport protein, (anion exchanger),erythrocyte [H.sapiens], solute carrier member 1, family 4 (anion solute carrierexchanger), member 1, family 4, solute carrier family anion exchanger,4, anion member 1 (erythrocyteexchanger, member 1 (erythrocyte membrane proteinmembrane protein band 3, band 3, Diego blood 175 16333 AA866414 a,h Diego blood group) group) 176 18918 AA866444 p,q 177 16853 AA866454 ,l,m,y,z j 178 18995 AA866459 h,m ESTs, Highly similar to FGDi_HUMAN

GUANINE

NUCLEOTIDE EXCHANGE
FACTOR

[H.sapiens], ESTs, Weakly similar to RHO/RAC

GUANINE NUCLEOTIDE
EXCHANGE

FACTOR [M.musculus], ESTs, Weakly similar to FGD1_HUMAN
PUTATIVE

RHO/RAC GUANINE
NUCLEOTIDE

EXCHANGE FACTOR
[H.sapiens], FGD1 family, member 3, RIKEN cDNA

5830461 L01 gene, faciogenital dysplasia (Aarskog-Scott syndrome), faciogenital dysplasia homolog, faciogenital dysplasia homolog 2 179 16013 AA866482 s (human) r 181 16059 AA874857 h r ESTs, Weakly similar to RNA binding 183 21633 AA874951 rotein [H.sa iens]
f 184 16192 AA874995 w 185 16254 AA875025 cellular retinoic j acid-binding protein 186 16312 AA875032 cc,General Homo sapiens clone H00582, expressed sequence AI303526, fibrinogen, fibrinogen, A alpha A alpha polypeptide, 187 20701 AA875097 b pol pe tide fibrinogen, gamma pol peptide ADP-ribosylation factor 3, RIKEN

cDNA 5430400P17 gene, Rattus norvegicus ADP-ribosylation factor 3 mRNA, complete cds, expressed 188 6416 AA875098 bb sequence AA408731 expressed sequence AL022645, expressed sequence C76690, small nuclear ribonucleoprotein E, small nuclear ribonucleoprotein polypeptide 189 6419 AA875102 bb E

190 5313 AA875126 ,m,General 191 0936 AA875146 w 192 8084 AA875186 h ESTs, Weakly similar to IF39_HUMAN

EUKARYOTIC TRANSLATION

I NITIATION FACTOR

193 5371 AA875205 a H.sa ions TABLE3: HUMANOMOLOGUE 01'ATIONS Atty. Docket No.
H AN 44921-5U89W~

Doc. N
o. 1798397.1 Seq.__ GenBank Homologous _ ID ~~~~~ Acc./ Gene ~

No. IdentifierRef. Seq. Model Name . Hom_o_logqus Cluster I~ No. Code Name 194 15401 AA875257 x,z NADH dehydrogenase (ubiquinone) Fe S protein 7 (20kD) (NADH-coenzyme 195 15410 AA875268 p,s O reductase) f 197 15446 AA875327 s,w 198 7936 AA875495 b,General EST, Moderately similar to A Chain A, Mdm2 Bound To The Transactivation Domain Of P53 {SUB

[H.sapiens], mouse double minute 2, human homolog of;
p53-binding 199 17314 AA875509 ,1,m protein i EST, Weakly similar to MOHU6N

myosin alkali light chain 6, nonmuscle form [H.sapiens], myosin light chain, alkali, nonmuscle, myosin, light polypeptide 6, alkali, smooth muscle 200 24472 AA875523 k and non-muscle j 202 15617 AA875620 General 202 15618 AA875620 General Jun-B oncogene, jun B proto-203 5384 AA891041 ,cc,General oncogene f 204 24814 AA891209 , f EST, Moderately similar to JH0148 nucleolin - rat [R.norvegicusJ, EST, Weakly similar to NUCL_HUMAN

NUCLEOLIN [H.sapiens], ESTs, Highly similar to FUS_HUMAN
RNA-BINDING

PROTEIN FUS [H.sapiens], ESTs, Weakly similar to T17210 hypothetical protein DKFZp434N041.1 [H.sapiens], RIKEN cDNA 2700022N21 gene, fusion, derived from t(12;16) malignant l iposarcoma, poly(A) binding protein, nuclear 1, small nuclear ribonucleoprotein 70kD polypeptide 205 21930 AA891322 d (RNP antigen) EST, Weakly similar to IF37 MOUSE

EUKARYOTIC TRANSLATION

INITIATION FACTOR

[M.musculus], eukaryotic translation . i nitiation factor 3, subunit 7 (zeta, 66/67 kDa), eukaryotic translation i nitiation factor 3, subunit 7 (zeta, 206 17225 AA891553 h 66/67kD

207 7522 AA891571 ,m j 208 9071 AA891578 b Homo Sapiens, Similar to neurofilament, heavy polypeptide (200kD), clone MGC:20701 I MAGE:4634024, mRNA, complete cds, MAGE-E1 protein, protein, Neurofilament, heavy polypeptide, RIKEN
cDNA

2010107K23 gene, RIKEN cDNA

3830417A13 gene, general t ranscription factor IIH, polypeptide (62kD subunit), melanoma antigen, f amily D, 1, melanoma antigen, family D, 2, necdin, neurofilament, heavy melanoma antigen,polypeptide, neurofilament, family heavy 209 19321 AA891666 D, 1 0l peptide 200kD) a 210 17693 AA891737 ,l,m,n, j ,z 211 17256 AA891739 General TABLE3: OMOLOGUE NOTATI~NS Atty, Docket No.

H

Doe. No. 1798897.1 ~Seq. GenBan Homologous .
ID Aee.l Gene ,~"

, 'No. IdentifierRef. Seq.Model Narne ~
1U No. Code Hoin'~ol~o~ go~u~s Cluster Name ESTs, Highly similar to S03917 fibronectin ED-A
[H.sapiens), ESTs, Moderately similar to Fourth And Fifth Fibronectin Type I Module Pair {SUB

183-275 [H.sapiens], Fibronectin 1, 213 18269 AA891769 General fibronectin 1 214 9905 AA891774 s,bb,General 215 17061 AA891812 d ESTs, Highly similar to 2013348A Ser kinase SRPK1 [H.sapiens], Mus musculus 13 days embryo head cDNA, RIKEN full-length enriched library, clone:3110005M20, full insert sequence, Mus musculus adult male lung cDNA, RIKEN
full-length enriched library, clone:1200011 B22, full insert sequence, SFRS protein kinase 1, SFRS protein kinase 2, serine/arginine rich protein specific kinase 2, 216 7050 AA891824 h serine/threonine kinase 23 EST, Weakly similar to PE2R RAT 20-ALPHA-HYDROXYSTEROID

DEHYDROGENASE [R.norvegicus], Mus musculus 10 days embryo cDNA, RIKEN full-length enriched library, clone:2610528B18, full insert sequence, RIKEN
cDNA 9430025F20 gene, Rattus norvegicus mRNA for 20-alpha-hydroxysteroid dehydrogenase (20-alpha-HSD), complete cds, aldo-keto reductase family 1, member C1, aldo-keto reductase family 1, member C4 (chlordecone reductase; 3-alpha hydroxysteroid dehydrogenase, type I;

dihydrodiol dehydrogenase 4), expressed sequence AI315367, expressed sequence A1503553, hydroxysteroid (17-beta) 217 4463 AA891831 General deh drogenase 5 i 219 20523 AA891842 ,cc r EST, Weakly similar to ACY1_HUMAN

AMINOACYLASE-1 [H.sapiens], 220 17779 AA891914 g,s,z aminoac lase 1 221 17438 AA891943 General 223 1159 AA891949 e,z 224 4473 AA891965 General 225 6362 AA892053 ,j,l,m f EST, Weakly similar to PROD_HUMAN PROLINE
OXIDASE, MITOCHONDRIAL PRECURSOR

[H.sapiens], Homo sapiens mRNA for KIAA1653 protein, partial cds, proline dehydrogenase, proline dehydrogenase (proline oxidase), proline oxidase 1, proline oxidase 227 19469 AA892112 General homolog 228 14595 AA892128 o,t,v 229 16527 AA892154 c c 230 4482 AA892173 bb h Met proto-oncogene, RYK receptor-like tyrosine kinase, macrophage stimulating 1 receptor (c-met-related 232 2357 AA892268 t rosine kinase d , met roto-oncogene TABLEHUMAN OMOLOGUE NOTATIONS Atty. Docket No.
3: H AN 44931-5U89W~

Doc. No. 1798397.1 Seq. GenBank Homologous ID Acc.l Gene ~No. dentifierRef. Seq.Model .Name Homologous Cluster I 1U No. Code Name 233 8183 AA892271 h 234 6523 AA892299 d EST, Weakly similar to 60S

RIBOSOMAL PROTEIN

[R.norvegicus], EST, Weakly similar to 1 84501 ribosomal protein L3 [H.sapiens], ESTs, Moderately similar t o 60S RIBOSOMAL

[R.norvegicus], ESTs, Moderately similar to 184501 ribosomal protein [H.sapiens], ESTs, Weakly similar to PROTEIN L3 [M.musculus], RIKEN

cDNA 1110057H16 gene, ribosomal 236 3647 AA892367 a protein L3, ribosomal 1 protein L3-like 237 3473 AA892378 v ESTs, Weakly similar to T44342 hypothetical protein [H.sapiens], kidney-and liver-specific gene, putative N-acetyltransferase 238 7682 AA892382 , ,s,x,General Camello 2 aldolase 2, B isoform, aldolase B, fructose-239 820 AA892395 g,s bisphos hate 240 14754 AA892414 a f ubiquinol-cytochrome c reductase 242 16469 AA892462 p (6.4kD) subunit EST, Weakly similar to MAST CELL

[M.musculus], ESTs, Weakly similar to PRECURSOR [R.norvegicus], RIKEN

cDNA 2410039E18 gene, RIKEN

cDNA 4933401 F05 gene, marapsin, mast cell protease 7, protease, serine, 21 (testisin), protease, serine, 22, protease, serine, 8 (prostasin), 243 13609 AA892468 ,General t tase delta 1, i t ptase, alpha EST, Weakly similar to MAST CELL

[M.musculus], ESTs, Weakly similar to PRECURSOR [R.norvegicus], RIKEN

cDNA 2410039E18 gene, RIKEN

cDNA 4933401 F05 gene, marapsin, mast cell protease 7, protease, serine, 21 (testisin), protease, serine, 22, protease, serine, 8 (prostasin), 243 13610 AA892468 n,v,Generalt ryptase delta 1, t ptase, al ha EST, Weakly similar to histone H2A.F/Z variant (H.sapiens]. H2A

histone family, member Z, RIKEN

cDNA C530002L11 gene, histone 244 9254 AA892470 n,u H2A.F/Z variant 245 11991 AA892483 s EST, Weakly similar to A32609 alpha-glucosidase [H.sapiens], ESTs, Weakly similar to LYAG MOUSE

LYSOSOMAL ALPHA-GLUCOSIDASE

PRECURSOR [M.musculus], alpha glucosidase 2, alpha neutral subunit, 246 1522 AA892486 glucosidase, alpha, f acid ESTs, Highly similar to DS1_HUMAN

DS-1 PROTEI [H.sapiens], immature 247 11994 AA892507 as colon carcinoma transcript 1 248 23888 AA892520 w TABLEHUMAN OMOLOGUE N~TATIONS ~tt~y. Docket No.
3: H N 44921-5U89W0 Doe. Ne. 1798397.

Seq. GenBank Homologous ID Ace./ Gene r l ~

No. IdentifierRef. Seq.Model Name ~ ornologous Cluster I~ No. Code ~ Narne 248 23889 AA892520 h expressed sequence A1987846, expressed sequence AL023058, expressed sequence 077895, hypothetical protein MGC3178, protein disulfide isomerase-related protein, 250 15154 AA892532 p quiescin Q6 r 252 11203 AA892554 ,h f 253 18906 AA892561 a,bb,General ESTs, Moderately similar to DKC1 RAT DYSKERIN [R.norvegicus], ESTs, Weakly similar to DKC1_HUMAN

DYSKERIN [H.sapiens], RIKEN cDNA

9030425013 gene, dyskeratosis congenita 1, dyskerin, hypothetical protein, MGC:7014, nuclear factor of kappa light polypeptide gene enhancer 254 19327 AA892562 ,j, ,z in B-cells inhibitor-like f 1 255 18274 AA892572 p 256 4512 AA892578 cc EST, Highly similar to 60S

RIBOSOMAL PROTEIN

[R.norvegicus], EST, Moderately similar to 60S
RIBOSOMAL PROTEIN

L8 [R.norvegicus], EST, Weakly similar to JN0923 ribosomal protein L8, cytosolic [H.sapiens], ESTs, Highly similar to 60S
RIBOSOMAL PROTEIN

L8 [R.norvegicus], ESTs, Highly similar to RL8_HUMAN 60S
RIBOSOMAL

PROTEIN L [M.musculus], ESTs, Moderately similar to RLS_HUMAN

L

[M.musculus], expressed sequence 257 15876 AA892582 w AL024098, ribosomal rotein L8 258 19085 AA892598 General 258 19086 AA892598 General EST, Highly similar to HISTONE H4 [R.norvegicus], ESTs, Highly similar to HISTONE H4 [R.norvegicus], histone family, member D, H4 histone family, member H, H4 histone family, member I, H4 histone family, member K, Mus musculus 10 day old male pancreas cDNA, RIKEN full-length enriched library, clone:1810029H14, full insert sequence, Mus musculus 10 days embryo cDNA, RIKEN full-length enriched library, clone:2610027B07, full insert sequence, Mus musculus adult male testis cDNA, RIKEN full-length enriched library, clone:4930558J22, full insert sequence, Mus musculus adult male tongue cDNA, RIKEN
full-length enriched library, clone:2310067E17, 259 20065 AA892647 full insert se I uence, histone 4 rotein 260 20088 AA892666 a,n 261 23783 AA892773 n TABLEHUMAN OMOLOGUE NOTATI~NS Atty. Docket No.
3: H AN 44921-5U89W0 Doe. No. 1798397.1 Seq. _ _ GenBank _ _ Homologous _ ID . Aec.l ~ .~~ Gene .

No. IdentifierRef. Seq.Model Name Homologous Cluster ID No. Code Name Mus musculus, Similar to solute carrier f amily 25 (mitochondria) carrier;

phosphate carrier), member 3, clone MGC:7631, mRNA, complete cds, expressed sequence W51672, solute carrier family 25 (mitochondria) carrier;

262 17549 AA892776 ,z phosphate carrier), f member 3 263 13542 AA892798 b 3-phosphoglycerate dehydrogenase, EST, Weakly similar to SERA RAT D-3 PHOSPHOGLYCERATE

DEHYDROGENASE [R.norvegicus], ESTs, Moderately similar to SERA_HUMAN D-3-PHOSPHOGLYCERATE

DEHYDROGENASE [H.sapiensJ, Mus musculus adult male testis cDNA, RIKEN full-length enriched library, clone:4930404C15, full insert sequence, RIKEN
cDNA 1110059D05 gene, RIKEN cDNA
6430629L09 gene, glyoxylate reductase/hydroxypyruvate r eductase, phosphoglycerate 264 22537 AA892799 General deh drogenase 3-phosphoglycerate dehydrogenase, EST, Weakly similar to SERA RAT D-3 PHOSPHOGLYCERATE

DEHYDROGENASE [R.norvegicus], ESTs, Moderately similar to SERA_HUMAN D-3-PHOSPHOGLYCERATE

DEHYDROGENASE [H.sapiens], Mus musculus adult male testis cDNA, RIKEN full-length enriched library, clone:4930404C15, full insert s equence, RIKEN
cDNA 1110059D05 gene, RIKEN cDNA
6430629L09 gene, glyoxylate reductase/hydroxypyruvate r eductase, phosphoglycerate 264 22539 AA892799 deh drogenase v 3-phosphoglycerate dehydrogenase, EST, Weakly similar to SERA RAT D-3 PHOSPHOGLYCERATE

DEHYDROGENASE [R.norvegicus], ESTs, Moderately similar to SERA_HUMAN D-3-PHOSPHOGLYCERATE

DEHYDROGENASE [H.sapiens], Mus musculus adult male testis cDNA, RIKEN full-length enriched library, c lone:4930404C15, full insert s equence, RIKEN
cDNA 1110059D05 g ene, RIKEN cDNA
6430629L09 gene, g lyoxylate reductase/hydroxypyruvate r eductase, phosphoglycerate 264 22538 AA892799 General d eh drogenase h -1 ss-TABLE 3: OMOLOGUE N~TATI~NS Atty. Do ket No.

Doe. Ne. 1798397.1 Seq. ID GenBank Homologous Aec.l Gene No. IdentifierRef. Seq.Model N.. ame, Horno,lofg~ous I~ No. Code Cluster Narne ESTs, Highly similar to AR72_HUMAN

REDUCTASE 1 (AFB1-AR
1 ) (ALDOKETOREDUCTASE
7) [H.sapiens], ESTs, Moderately similar to AFAR RAT AFLATOXIN

ALDEHYDE REDUCTASE

[R.norvegicus], RIKEN cDNA

0610025K21 gene, aflatoxin B1 aldehyde reductase, aldo-keto reductase family 7, member A2 (aflatoxin aldehyde reductase), aldo-keto reductase family 7, member 266 23322 AA892821 ,z (aflatoxin aldeh ' de reductase) f RIKEN cDNA 2410042F05 gene, procollagen-lysine, 2-oxoglutarate dioxygenase (lysine hydroxylase) 2, procollagen-lysine, 2-oxoglutarate dioxygenase (lysine hydroxylase, Ehlers-Danlos syndrome type VI), procollagen-lysine, 2-oxoglutarate 268 22871 AA892859 m diox genase 1 269 9053 AA892861 p,v,General EST, Weakly similar to EFHU2 translation elongation factor eEF-2 [H.sapiens], ESTs, Highly similar to ELONGATION FACTOR

[R.norvegicus], U5 snRNP-specific protein, 116 kD, eukaryotic translation elongation factor 2, expressed sequence AI451340, hypothetical 270 16482 AA892940 w protein FLJ21661 271 12020 AA893035 ,y j 272 3863 AA893060 General 273 13332 AA893080 ,General i 274 21305 AA893082 General 275 16591 AA893191 ,z j 276 17447 AA893192 General 277 3876 AA893205 n Calmodulin 1 (phosphorylase kinase, delta), Calmodulin III, ESTs, Highly similar to A Chain A, Calmodulin Complexed With Calmodulin-Binding Peptide From Smooth Muscle Myosin Light Chain Kinase {SUB 2-148 [H.sapiens], RIKEN
cDNA

2310068022 gene, calmodulin, calmodulin 1, calmodulin (phosphorylase kinase, delta), calmodulin 2, calmodulin (phosphorylase kinase, delta), 278 3878 AA893230 General calmodulin 3. calmodulin-like TABLEHUMAN OMOLOGUE N~TATI~NS Atty. Docket No.
3: H AN 44921-5U89W0 Doe. No. 1798397.1 Seq. GenBank Homologous ID Aee.l Gene No. dentifierRef. Seq.Model Name Homologous Cluster I ID No. Code Name ESTs, Weakly similar to LCFB MOUSE

LONG-CHAIN-FATTY-ACID--COA

LIGASE 2 [M.musculus], Mus musculus, Similar to fatty-acid-Coenzyme A ligase, long-chain 6, clone MGC:28744 IMAGE:4481949, mRNA, complete cds, Rattus norvegicus gonadotropin-regulated long chain acyl-CoA
synthetase (GR-LACS) mRNA, complete cds, fatty acid Coenzyme A ligase, long chain 2, fatty f atty acid acid Coenzyme A
Coenzyme ligase, long chain A 5, l igase, long fatty-acid-Coenzyme chain 2, A ligase, long-fatty-acid-Coenzymechain 1, fatty-acid-Coenzyme A ligase, A ligase, 279 20986 AA893242 q l ong-chain long-chain 2, lipidosin RIKEN cDNA 1300012015 gene, RIKEN cDNA 2310076L09 gene, adipose differentiation related protein, 280 16168 AA893280 i,z,General adipose differentiation-related protein 281 3886 AA893289 j,m, 282 15209 AA893327 y 283 17800 AA893436 cc Guanine nucleotide-binding protein beta 1, Homo sapiens mRNA for FLJ00083 protein, partial cds, Mus musculus, clone MGC:7934 IMAGE:3583848, mRNA, complete cds, RIKEN cDNA
5930415H02 gene, WD repeat domain 5, guanine nucleotide binding protein (G protein), beta polypeptide 1, guanine nucleotide binding protein beta subunit 4, guanine nucleotide binding protein, beta 1, guanine nucleotide binding protein, beta 4, hypothetical protein, 284 7836 AA893626 h recombination protein 285 9084 AA893717 x 286 22731 AA893743 d ESTs, Highly similar to YSHUT

threonine--tRNA
ligase [H.sapiens], ESTs, Moderately similar to YSHUT

t hreonine--tRNA
ligase [H.sapiens], hypothetical protein FLJ12528, 287 2031 AA893860 v threon I-tRNA s 1 nthetase 288 7897 AA893905 k 289 3447 AA893982 d 290 22583 AA894009 n 291 0540 AA894027.

292 569 AA894059 x 4 ~

f~lAnt~~~~ 31 ~
1'AB~LEHUMAN OMO OGUE NOTATION-S ~1'X~'~-~'~
3: H AN l~tty. Docket No~,44921-5U89W0 Do~c. No 1798397 ~Seq. GenBank Homologous .
ID Acc.l Gene ~ e= ' ';'~~~, v ~~

No. dentifierRef. Seq.Model Narne - HomologousCluster;Name I 1U No. Gode .n=T

Amyloid protein precursor-like protein 2, EST, Weakly similar to AMYLOID-PRECURSOR

[R.norvegicus], Human DNA sequence from clone RP3-461P17 on chromosome 20q12-13.2.
Contains two novel genes, gene HE4 for Major Epididymis-specific protein E4 precursor (Epididymis Secretory protein E4), RPLS
(60S Ribosomal Protein L5), COX6C
(Cytochrome C

Oxidase subunit VIC) and HSPD1 (HSP60, Mitochondrial Matrix Protein P1 precursor, Heat Shock Protein 60, GROEL, HUCHA60) pseudogenes, the SPINT3 gene for Kunitz type serine protease inhibitor 3 (HKIB9), two genes for novel Kunitz/Bovine pancreatic trypsin inhibitor and WAP-type (Whey Acidic Protein) 'four-disulfide core' domains containing proteins and the gene for Eppin-1, and -3. Contains ESTs, STSs, GSSs and a CpG island, RIKEN cDNA

1700024E17 gene, amyloid beta (A4) precursor-like protein 2, serine protease inhibitor, Kunitz type 2, tissue factor pathway inhibitor, tissue factor 293 18419 AA894130 d pathwa inhibitor 295 19120 AA894318 ,j f i EST, Weakly similar to S45140 tubulin beta chain [H.sapiens], ESTs, Highly similar to T08726 tubulin beta chain [H.sapiens], ESTs, Highly similar to BETA CHAIN

[R.norvegicus], ESTs, Moderately similar to 138370 beta-tubulin [H.sapiens], ESTs, Moderately similar to TBB1 RAT TUBULIN
BETA CHAIN

[R.norvegicus], RIKEN cDNA

2410129E14 gene, RIKEN cDNA

4930447K03 gene, RIKEN cDNA

4930542603 gene, tubulin, beta 3, 297 18286 AA899219 a tubulin, beta pol eptide 298 22051 AA899498 w 298 22052 AA899498 q 299 21628 AA899563 as i receptor (calcitonin)receptor (calcitonin) activity modifying 301 4661 AA899709 ,General activit modifprotein 3 t ing rotein EST, Moderately similar to EGFR_HUMAN EPIDERMAL

GROWTH FACTOR RECEPTOR

PRECURSOR [H.sapiens], Epidermal growth factor receptor, formerly avian erythroblastic leukemia viral (v-erb8) oncogene homolog (Erbb1), avian erythroblastosis oncogene B 3, epidermal growth factor receptor, epidermal growth factor receptor (avian erythroblastic leukemia viral (v-303 17905 AA899762 General erb-b) oncogene homology 304 15231 AA899840 r TABLE HUMANOMOLOGUE NOT TIONS Aftjl~Uo'e'ket N~44921-5U89W0 3: H AN

. 17983971.
~ Doe. No ~Seq. _ __ Homologous _ ID G~en"~IBank Genes Ace.l No. dentifierRef~~, Model Name ~; ~Homolyogous Cluster I Seq; ID Code ~~,~ Name No.

ESTs, Moderately similar to A40493 DNA topoisomerase [H.sapiens], ESTs, Moderately similar to TP2A

MOUSE DNA TOPOISOMERASE
II, ALPHA [M.musculus], topoisomerase t opoisomerase(DNA) II alpha, (DNA) II topoisomerase (DNA) II

alpha, topoisomerasebeta, topoisomerase (DNA) II beta 305 23778AA899854 c,k,x DNA) II alpha(180kD) ( (170kD) 306 22060AA899898 b 307 9114 AA899951 v,General f ESTs, Highly similar to IEFS_HUMAN

TRANSFORMATION-SENSITIVE

PROTEIN IEF SSP
3521 [H.sapiens], 309 1841 AA900247 v hypothetical protein Alpha-2-macroglobulin, ESTs, Moderately similar to A2M2 MOUSE

PRECURSOR

[M.musculus], RIKEN
cDNA

2610307121 gene, alpha-2-macroglobulin, carbon catabolite repression 4 homolog (S. cerevisiae), expressed sequence AW456442, 310 725 AA900290 cc pregnanc -zone rotein 311 747 AA900465 General DNA segment, Chr 17, human D6S81 E 1, ESTs, Highly similar to S33681 translation initiation factor eIF-4A.1 [H.sapiens], HLA-B associated transcript 1, Human clone 23933 mRNA sequence, eukaryotic translation initiation factor 4A, isoform 1, mitochondrial DEAD-box polypeptide 28, nuclear RNA helicase, 313 3822 AA900863 b,g,General DECD variant of DEAD box famil Mus musculus, Similar to aspartyl-tRNA synthetase, clone MGC:6719 IMAGE:3586278. mRNA, complete cds, asparaginyl-tRNA
synthetase, aspartyl-tRNA synthetase, hypothetical protein FLJ10514, hypothetical protein 315 2420 AA901017 b FLJ23441 316 849 AA901155 s 317 959 AA901338 General succinate-CoA ligase, ADP-forming, 318 22846AA923982 a,d beta subunit 319 895 AA923999 k 320 21546AA924188 cc,General 321 24192AA924210 n,General 322 933 AA924301 g,I,General ESTs, Weakly similar to NEUROFILAMENT TRIPLET
H

PROTEIN [M.musculus], RIKEN cDNA

0610009L18 gene, RIKEN cDNA

1300003A17 gene, RIKEN cDNA

2410142614 gene, nucleolar protein 323 944 AA924405 ,General (KKE/D repeat) 4 ( 4 r TABLEHUMAN OMOLOGUE NOTATIONS Atty. D diet N'o.
3: H AN 449315U88W0 ~oe. No. 1798897 Seq. GenBan Homologous ID Aee./ Gene ~

No. IdentifierRef. Seq.Model Name L~~,~ ~~om~l.~gous CI_uster ID No. ode ~; Nams ESTs, Weakly similar to NPT2_HUMAN RENAL
SODIUM-DEPENDENT PHOSPHATE

TRANSPORT PROTEIN
2 [H.sapiens], Homo sapiens, Similar to solute carrier family 34 (sodium phosphate), membe 1, clone MGC:18179 IMAGE:4155326, mRNA, complete cds, Rattus norvegicus mRNA
for NaPi-2 alpha, complete cds, Solute carrier family (sodium/hydrogen exchanger), member 2, expressed sequence AI649385, solute carrier family (sodium phosphate), member 1, solute carrier family 34 (sodium phosphate), 325 4949 AA924432 General member 2 326 18891 AA924598 a 3-phosphoglycerate dehydrogenase, EST, Weakly similar to SERA RAT D-3 PHOSPHOGLYCERATE

DEHYDROGENASE [R.norvegicus], ESTs, Moderately similar to SERA_HUMAN D-3-PHOSPHOGLYCERATE

DEHYDROGENASE [H.sapiens], Mus musculus adult male testis cDNA, RIKEN full-length enriched library, clone:4930404C15, full insert sequence, RIKEN
cDNA 1110059D05 gene, RIKEN cDNA
6430629L09 gene, glyoxylate reductase/hydroxypyruvate reductase, phosphoglycerate 327 22540 AA924630 v,General deh drogenase 3-phosphoglycerate dehydrogenase, EST, Weakly similar to SERA RAT D-3 PHOSPHOGLYCERATE

DEHYDROGENASE [R.norvegicus], ESTs, Moderately similar to SERA_HUMAN D-3-PHOSPHOGLYCERATE

DEHYDROGENASE [H.sapiens], Mus musculus adult male testis cDNA, RIKEN full-length enriched library, clone:4930404C15, full insert sequence, RIKEN
cDNA 1110059D05 gene, RIKEN cDNA
6430629L09 gene, glyoxylate reductase/hydroxypyruvate reductase, phosphoglycerate 327 22541 AA924630 General deh drogenase 328 14759 AA924766 k x 330 4067 AA924813 g,p 331 2888 AA924902 ,General r d r ESTs, Weakly similar to A35863 tryptase [H.sapiens], ESTs, Weakly similar to MCT7 RAT MAST CELL

[R.norvegicus], RIKEN cDNA

4733401 N09 gene, mast cell protease 7, tryptase delta 1, tryptase gamma 1, 334 23195 AA925026 General t ptase, al ha 335 21458 AA925049 ,aa,General f 336 5073 AA925061 m 337 14790 AA925087 o,General TABLE: HUMAN~MOLOGUE NOTATIONS Atty. Doclief~No.

Doe. No1798397 Seq. GenBank Homologous ~1 ID Aec.l Gerie ~

No. IdentifierRef. Seq.Model Name Homologous ClusterENarne I~ No. Code Homo sapiens, clone IMAGE:3940519, mRNA, partial cds, hypothetical protein 338 5089 AA925126 g DKFZp7620076 Mus musculus adult male testis cDNA, RIKEN full-length enriched library, clone:4930572N12, full insert sequence, betaine-homocysteine methyltransferase, betaine-339 23261 AA925145 k,General homoc steine meth Itransferase 2 KIAA0438 gene product, Rattus norvegicus mRNA
for neurodegeneration associated protein 1, complete cds, expressed sequence AL022700, g1-related zinc finger protein, hypothetical protein, hypothetical protein FLJ11830 similar to Praja1, hypothetical protein, similar 340 17363 AA925150 a to (U06944) PRAJA1, rajal I

EST, Weakly similar to TRI9_HUMAN

THYROID RECEPTOR
INTERACTING

PROTEIN 9 [H.sapiens], ESTs, Highly similar to A44437 regenerating liver i nhibitory factor RUIF-1 - rat [R.norvegicus], ESTs, Weakly similar t o I-kappa B alpha chain [M.musculus], nuclear factor of kappa light chain gene enhancer in B-cells inhibitor, alpha, nuclear factor of kappa light chain gene enhancer in B-cells i nhibitor, beta, nuclear factor of kappa l ight polypeptide gene enhancer in B-cells inhibitor, alpha, nuclear factor of kappa light polypeptide gene enhancer i n B-cells inhibitor, beta, nuclear factor of kappa light polypeptide gene 342 23159 AA925318 a enhancer in B-cells inhibitor, epsilon 343 21500 AA925353 k t 345 21151 AA925539 b EST, Moderately similar to 1604358A

nuclear RNP protein L [H.sapiens], ESTs, Highly similar to 1604358A

nuclear RNP protein L [H.sapiens], ESTs, Moderately similar to 1604358A

nuclear RNP protein L [H.sapiens], heterogeneousheterogeneous nuclear nuclear 346 16944 AA925541 ribonucleoproteinibonucleoprotein f L r L

EST, Moderately similar to 1604358A

nuclear RNP protein L [H.sapiens], ESTs, Highly similar to 1604358A

nuclear RNP protein L [H.sapiens], ESTs, Moderately similar to 1604358A

nuclear RNP protein L [H.sapiens], heterogeneousheterogeneous nuclear nuclear 346 16945 AA925541 ribonucleoproteinibonucleo rotein t L r L

ESTs, Moderately similar to JX0336 succinate dehydrogenase [H.sapiens], succinate dehydrogenase complex, 347 17514 AA925554 b subunit A, flavoprotein b (F ) 348 5183 AA925662 ,General i r TABLE: HUMANOMOLOGUE NOTATIONS Attsy. Docket No.

Doe. No. 1798397.

~Seq. GenBank omologous Gene ID Aee./

No. IdentifierRef. Seq.Model Name Homoloag~o"us Cluster 1U No. Code Name EST, Weakly similar to IMB3_HUMAN

SUBUNIT

[H.sapiens], Homo Sapiens cDNA

FLJ12978 fis, clone NT2RP2006321, RAN binding protein 6, karyopherin 350 23190 AA925863 as (im ortin) beta 351 5252 AA926051 General 352 22967 AA926080 h,cc 353 17157 AA926129 b 354 13411 AA926196 u,General potassium channel, subfamily K, member 1 (TWIK-1), potassium channel, subfamily K, member 3 (TASK-1), potassium channel, subfamily K, member 6 (TWIK-2), potassium channel, subfamily K, 355 5295 AA926247 General member 7 DNA segment, human D4S114, P311 356 22928 AA926262 General protein 357 8948 AA926316 r CGI-69 protein, EST, Moderately similar to T43493 hypothetical protein DKFZp434C119.1 [H.sapiens], mitochondrial carrier family protein, 358 21798 AA926365 as mitochondria) solute carrier 359 9942 AA942697 s DNA segment, Chr 17, ERATO Doi 441, expressed, hematological and 360 6039 AA942716 x,General neurological expressed 361 11174 AA942745 g,o,w 362 23005 AA942770 g 363 21318 AA942774 General 364 6615 AA942889 v RAT MACROPHAGE
COLONY

STIMULATING FACTOR
I

RECEPTOR PRECURSOR

[R.norvegicus], colony stimulating factor 1 receptor, colony stimulating factor 1 receptor, formerly McDonough feline sarcoma viral (v-fms) oncogene 365 6691 AA943028 c homolog DEAD (aspartate-glutamate-alanine-aspartate) box polypeptide 5, DEAD/H

(Asp-Glu-Ala-Asp/His) box polypeptide 17 (72kD), KIAA0801 gene product, RIKEN cDNA 2610007K22 gene, RIKEN cDNA 4921506D17 gene, RIKEN cDNA 9130430L19 gene, RNA

helicase, Rattus norvegicus RNA

helicase with arginine-serine-rich domain mRNA, complete cds, expressed sequence AI325430, hypothetical protein, prp28, U5 snRNP

366 22142 AA943066 p 100 kd protein ALEX1 protein, ALEX3 protein, armadillo repeat protein ALEX2, 367 21993 AA943149 v,General h othetical protein TU3A protein, hypothetical protein 368 9061 AA943508 General MGC11034 ESTs, Weakly similar to VIL1 MOUSE

VILLIN [M.musculus], actin binding LIM protein 1, advillin, erythrocyte membrane protein band 4.9 (dematin), 369 24390 AA943531 b,',n, a throe to rotein band 4.9, villin TABLE: HUMANOMOLOGUE NOTATIONS Atty. D cket No.

Doe. No. 1798397.1 Seq. GenBank _ I~ Aee.l Homologous Gene .No. 'IdentifierRef. Seq.Model Name , Homologues Cluster ID No. Code Narne EST, Moderately similar to 138369 beta tubulin [H.sapiens], EST, Weakly similar to 138369 beta-tubulin [H.sapiens], EST, Weakly similar to [M.musculus], ESTs, Highly similar to A25113 tubulin beta chain 15 - rat [R.norvegicus], FK506-binding protein 1A (l2kD), RIKEN
cDNA 2310061K05 gene, RIKEN cDNA

gene, tubulin, beta 2, tubulin, beta 5, 370 13976 AA943532 ,s,x tubulin, beta pol f eptide ajuba, expressed sequence AI481106, 371 22248 AA943537 cc,General expressed se uence 875157, z xin TATA box binding protein (TBP)-associated factor, RNA polymerase II, 372 22257 AA943558 m J,20kD

373 12673 AA943773 u,cc,General 374 13641 AA944154 a f 376 12770 AA944161 d CDC28 protein kinase 2, RIKEN cDNA

1110038L14 gene, expressed 377 20903 AA944180 ,x sequence A1047807 i 378 13507 AA944244 v 379 15596 AA944353 General 380 22681 AA944413 ,v,cc,General i 381 6711 AA944439 General ESTs, Highly similar to AGP2_RAT

ANGIOPOIETIN-2 (ANG-2) [R.norvegicus], angiopoietin 1, angiopoietin 2, angiopoietin-like 3, angiopoietin-like 4, angiopoietin-like 382 14763 AA944481 ,q,General factor i 383 22466 AA944605 h B-cell CLUlymphoma 3, B-cell leukemia/lymphoma 3, ESTs, Highly ' similar to A44437 regenerating liver inhibitory factor RUIF-1 - rat [R.norvegicus], ESTs, Weakly similar to I-kappa B alpha chain [M.musculus], molecule possessing ankyrin repeats induced by lipopolysaccharide (MAIL), homolog of mouse, nuclear factor of kappa light chain gene enhancer in B-cells 1, p105, nuclear factor of kappa light chain gene enhancer in B-cells inhibitor, alpha, nuclear factor of kappa light polypeptide gene enhancer in B-cells 2, p49/p100, nuclear factor of ' kappa light polypeptide gene enhancer in B-cells inhibitor, alpha, nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, epsilon, testis-specific ankyrin motif containing 384 12301 AA944727 b protein 385 7023 AA944792 d,m,aa 386 22536 AA944803 bb CGI-89 protein, hypothetical protein DKFZp667O2416, hypothetical protein FLJ20984, leukocyte receptor cluster 387 22501 AA944811 g,1 (LRC) member 4 388 23967 AA944831 s i 390 11974 AA944958 General 391 22547 AA944970 as -2os-TABLE : HUMANOMOLOGUE NOTATIONS Atty. Doeket No.

Doe. No. 1798397.1 ~Seq. GenBan Homologous ID Aee.l Gene No. IdentifierRef. Seq.Model Name Horno.logo~us Cluster 1U No. Code Name 392 22554 AA945076 z,General 393 14352 AA945181 General 395 1798 AA945569 General 396 22050 AA945604 ,aa i 397 19731 AA945615 d,o Diaphorase (NADH/NADPH), NAD(P)H

menadione oxidoreductase 2, dioxin i nducible, NAD(P)H
menadione oxidoreductase 2, dioxin-inducible, diaphorase (NADH/NADPH) ( cytochrome b-5 reductase), 398 22612 AA945624 a,General diaphorase 4 (NADH/NADPH) 399 22618 AA945656 as 400 11871 AA945679 v 401 22656 AA945818 General 402 6720 AA945828 p 403 22351 AA945867 m f 405 24243 AA945950 b 406 22689 AA945962 General 407 22692 AA945986 d 408 22696 AA945996 c,General 408 22697 AA945996 c,o 409 22658 AA945998 w ESTs. Weakly similar to COXG

MOUSE CYTOCHROME
C OXIDASE

POLYPEPTIDE VIB
[M.musculus], Human DNA sequence from clone RP4-591 N18 on chromosome 22q13.1 13.2 Contains a COX6B (Cytochrome C Oxidase subunit Vlb (EC 1.9.3.1 )) pseudogene, ESTs, GSSs and two putative CpG islands, RIKEN cDNA

2010000605 gene, cytochrome c 410 20832 AA946040 s oxidase subunit Vlb 411 18337 AA946046 General EST, Highly similar to LMA3_HUMAN

CHAIN

PRECURSOR [H.sapiens], ESTs, Highly similar to LMA3_HUMAN

CHAIN

PRECURSOR [H.sapiens], Homo s apiens cDNA: FLJ21236 fis, clone COL01111, expressed sequence AI853660, laminin, alpha 3 (nicein ( 150kD), kalinin (165kD), BM600 412 825 AA946108 General ( 150kD , a ilegrin) 413 8639 AA946221 e,cc,General f 415 15600 AA946250 o,aa a ctin related protein 2/3 complex, 416 19387 AA946275 s ubunit 3 (21 kD) t EST, Weakly similar to JC5111 cyclin-d ependent kinase-related protein 1 b -r at [R.norvegicus], EST, Weakly s imilar to S10889 proline-rich protein [ H.sapiens], ESTs, Highly similar to J C5111 cyclin-dependent kinase-r elated protein 1 b - rat [R.norvegicus], Homo sapiens ALS2CR7 mRNA, c omplete cds, PCTAIRE
protein kinase 1 , PCTAIRE-motif protein kinase 1, 417 6351 AA946344 PFTAIRE protein d kinase 1 418 22057 AA946348 a 419 22069 AA946349 as 420 13962 AA946351 General TABLE HUMAN OMOLOGUE NOTATION'S Atty: Docket N''"o.
3: H AN 44921-SU89W0 DocNo. 1798397.1 5eq. GenBank Homologous ' ID Aee./ Gene Na. dentifiercf. Seq. Model Name Hornologo~usyClu_ster I 1U No. Code Name EST, Moderately similar to 1923401A

protein CBP [M.musculus], EST, Weakly similar to 1923401A protein CBP [M.musculus], ESTs, Highly similar to 1923401A
protein CBP

[ M.musculus], ESTs, Weakly similar to 1923401A protein CBP [M.musculus], bromodomain, testis-specific, 421 18280 AA946361 g bromodomain-containing 422 18944 AA946391 v t EST, Highly similar to HISTONE H4 [ R.norvegicus], H4 histone family, member D, H4 histone family, member H, H4 histone family, member I, H4 histone family, member K, Mus musculus 10 day old male pancreas cDNA, RIKEN full-length enriched l ibrary, clone:1810029H14, full insert sequence, Mus musculus 10 days embryo cDNA, RIKEN
full-length enriched library, clone:2610027B07, f ull insert sequence, Mus musculus adult male testis cDNA, RIKEN full-l ength enriched library, clone:4930558J22, full insert sequence, Mus musculus adult male t ongue cDNA, RIKEN
full-length enriched library, clone:2310067E17, f ull insert sequence, germinal histone 425 643 AA946439 0, H4 gene, histone 4 protein EST, Weakly similar to NPD1 HUMAN

NEURAL PROLIFERATION

DIFFERENTIATION
AND CONTROL

(NPDC-1 PROTEIN) [H.sapiens], expressed sequence AI314472, neural proliferation, differentiation and control gene 1, neural proliferation, 426 20736 AA946443 d ifferentiation x and control, 1 r EST, Highly similar to AF151863 1 CGI

428 21947 AA946451 bb 1 05 protein H.sa iens 429 17499 AA946467 General 430 1809 AA946503 ,General x f 432 23471 AA955162 General 433 9452 AA955206 b,General 434 23512 AA955282 General 435 22596 AA955298 General h igh density lipoprotein binding protein 436 23283 AA955391 h ( vigilin) 437 23546 AA955393 General ESTs, Weakly similar to SX10 RAT

TRANSCRIPTION FACTOR

[ R.norvegicus], SRY (sex determining r egion Y)-box 10, SRY (sex d etermining region Y)-box 9 ( campomelic dysplasia, autosomal sex r eversal), SRY-box containing gene 438 12404 AA955408 b 1 0, expressed sequence 439 23626 AA955540 s a -2os-TABLE 3: OMOLOGUE N~TATIONS Att~y. Docket No.

Doc~. No. 1798897.1 vSeq. I~ GenBank Homologoi _ ~ Aee.l s Gene No. IdentifierRef. Seq. Model Name P ~,~~ Homologous Cluster 1l7 No. Code Name EST, Highly similar to FBRL MOUSE

FIBRILLARIN [M.musculus], EST, Weakly similar to A38712 fibrillarin [H.sapiens], ESTs, Highly similar to A38712 fibrillarin [H.sapiens], ESTs, Weakly similar to FBRL MOUSE

FIBRILLARIN [M.musculus], expressed sequence AL022665, 441 17540 AA955914 bb fibrillarin 442 24277 AA955962 General 443 19939 AA955980 General ESTs, Weakly similar to PC83_MOUSE POLY(RC)-BINDING

PROTEIN 3 (ALPHA-CP3) [ M.musculus], ESTs, Weakly similar to ROK_HUMAN HETEROGENEOUS

NUCLEAR RIBONUCLEOPROTEIN
K

[ R.norvegicus], IGF-II
mRNA-binding protein 3, RIKEN
cDNA 2610101 N11 gene, coding region determinant-binding protein, heterogeneous nuclea r ibonucleoprotein K, poly(rC)-binding 444 24000 AA956005 protein 3, poly(rC)-binding i protein 4 EST, Weakly similar to T-COMPLEX

PROTEIN 1, EPSILON
SUBUNIT

[ M.musculus], ESTs, Moderately similar to T-COMPLEX
PROTEIN 1, EPSILON SUBUNIT
[M.musculus], T-complex 1, chaperonin containing TCP1, subunit 5 (epsilon), chaperonin subunit 5 (epsilon), expressed sequence AI528772, t-complex 1, t-445 11050 AA956164 s,v com lex protein 446 498 AA956278 a,General 447 23409 AA956294 q 449 23773 AA956476 ,x f 450 23799 AA956530 d ESTs, Weakly similar to PROTEIN

[ H.sapiens], ring finger protein 1, ring 451 23800 AA956534 as f inger protein 2 452 23834 AA956659 cc,General gene rich cluster, C8 gene, 453 16425 AA956688 ,x h pothetical protein f MGC2577 454 23847 AA956723 s ESTs, Weakly similar to CHD4_HUMAN CHROMODOMAIN

HELICASE-DNA-BINDING
PROTEIN

4 [H.sapiens], KIAA1416 protein, KIAA1696 protein, chromodomain 455 23852 AA956746 ,l,m,z h elicase DNA binding j protein 4 DnaJ (Hsp40) homolog, subfamily C, member 8, Homo Sapiens mRNA;

c DNA DKFZp434C2016 (from clone DKFZp434C2016), eukaryotic t ranslation initiation factor 3, e ukaryotic translation initiation factor 3, subunit 10 (theta, 150/170kD), e xpressed sequence C85189, g uanylate kinase membrane-a ssociated inverted 1, hypothetical p rotein DKFZp434B227, n asopharyngeal epithelium specific 456 5989 AA956907 ,s rotein 1 g -2os-TABLEHUMAN OMOLOGUE NOTATI~NS Atty. Docket No.
3: H AN 44931-SU89W0 ~oc. No. 1798897.1 ~Seq. GenBan Homologous ID Acc.l Gene No. IdentifierRef. Seq.Model Name ~ H.ornologous Cluster IL) No. Code Name DnaJ (Hsp40) homolog, subfamily C, member 8, Homo Sapiens mRNA;

cDNA DKFZp434C2016 (from clone DKFZp434C2016), eukaryotic translation initiation factor 3, eukaryotic translation initiation factor 3, subunit 10 (theta, 150/170kD), expressed sequence C85189, guanylate kinase membrane-associated inverted 1, hypothetical protein DKFZp434B227, nasopharyngeal epithelium specific 456 5990 AA956907 General protein 1 X-linked protein, brain expressed, X-linked 1, hypothetical protein FLJ10097, nerve growth factor receptor (TNFRSF16) associated 457 23957 AA957123 u,General protein 1 EST, Weakly similar to T12456 hypothetical protein DKFZp564M2423.1 [H.sapiens], ESTs, Highly similar to T12456 hypothetical protein DKFZp564M2423.1 [H.sapiens], PAI-1 mRNA-binding protein, intracellular hyaluronan-458 22357 AA957264 General binding rotein g,I,m,p,v,cc,Gene 459 23314 AA957270 al r 460 23995 AA957292 a,b EST, Moderately similar to 601026 serine--tRNA ligase [H.sapiens], hypothetical protein FLJ20450, seryl-tRNA synthetase, uncharacterized 461 2702 AA957307 General gastric protein CD3 antigen, zeta polypeptide, CD3Z

antigen, zeta polypeptide (TiT3 complex), Fc fragment of IgE, high affinity I, receptor for; gamma polypeptide, Fc receptor, IgE, high affinity I, gamma polypeptide, 462 24040 AA957422 c expressed se uence EST, Weakly similar to S01696 gene P3 protein [H.sapiens], ESTs, Highly similar to P3 PROTEIN
[M.musculus], 463 12478 AA957554 m Protein P3 464 21306 AA957811 v t 466 24178 AA957905 d EST, Moderately similar to COPE_HUMAN COATOMER

EPSILON SUBUNIT
[H.sapiens], ESTs, Highly similar to COPE_HUMAN

COATOMER EPSILON
SUBUNIT

[H.sapiens], coatomer protein complex, subunit epsilon, hypothetical 467 17034 AA963071 a rotein FLJ13241 X-linked protein, brain expressed, X-linked 1, hypothetical protein FLJ10097, nerve growth factor receptor (TNFRSF16) associated 468 24053 AA963092 General rotein 1 470 2022 AA963259 g 471 2126 AA963488 d 472 24246 AA963703 b 473 2195 AA963746 General 474 19370 63797 ~ I
~

TABLEHUMAN OMOLOGUE N~TATI~NS " Att Docket No.
3: H AN 44921-5U89W0 l7oc. No. 798397.1 ~Seq. GenBank Homologous 1U Aee.l Gene No. dentifierRef. Seq;Model Name Hornologou~s Cluster I ID No. Code Name 475 282 AA964147 a 2 x ubiquitin specific protease 14 (tRNA-478 350 AA964368 g,General guanine transgl 2 cos lase) ESTs, Weakly similar to A29861 actin gamma [H.sapiens], ESTs, Weakly similar to 139393 alpha-actin [H.sapiens], ESTs, Weakly similar to S38782 actin beta' chain [H.sapiens], Homo Sapiens mRNA;
cDNA

DKFZp434B2115 (from clone DKFZp434B2115), RIKEN cDNA

1700052K15 gene, RIKEN cDNA

1700061J02 gene, actin-like 7a, expressed sequence AL023024, expressed sequence AV259599, melanoma X-actin, uncharacterized 479 8830 AA964496 as h pothalamus protein 480 2392 AA964541 b 481 2395 AA964554 General 482 2410 AA964589 ,aa i 1 t 484 2424 AA964617 g 485 3107 AA964687 General 486 2457 AA964752 q,t 487 6778 AA964763 b I

ESTs, Highly similar to GSHO_HUMAN

GLUTAMATE--CYSTEINE
LIGASE

glutamate-cysteineREGULATORY SUBUNIT
ligase , [H.sapiens], modifier subunit,glutamate-cysteine glutamate ligase , modifier cysteine ligase,subunit, glutamate-cysteine modifier ligase, 490 2469 AA964814 w subunit modifier subunit 491 12561 AA964815 General EST, Weakly similar to PROCOLLAGEN ALPHA
1(1V) CHAIN

PRECURSOR [M.musculus], collagen, type IV, alpha 1, procollagen, type IV, alpha 1, procollagen, type IV, alpha 3, 492 2326 AA964892 as procollagen, type IV, alpha 5 ATP-binding cassette, sub-family A

(ABC1 ), member 1, ATP-binding cassette, sub-family A (ABC1), member 12, ATP-binding cassette, sub family A (ABC1 ), member 7, EST, Moderately similar to ABC1_HUMAN

ATP-BINDING CASSETTE, SUB-FAMILY A, MEMBER
1 [H.sapiens], EST, Weakly similar to ABC1 MOUSE

ATP-BINDING CASSETTE, SUB-FAMILY A, MEMBER
1 [M.musculus], 493 21339 AA964962 General RIKEN cDNA 1810036E22 gene 494 21390 AA964988 General 495 12569 AA965023 g Homo Sapiens, clone MGC:8857 IMAGE:3866266, mRNA, complete cds, inorganic pyrophosphatase, 496 2583 AA965166 bb ro hosphatase (inorganic) EST, Highly similar to T14795 hypothetical protein DKFZp434E171.1 497 15885 AA965207 [H.sa lens]
r 499 2905 AA996727 b,I,m,u,General ESTs, Moderately similar to LAMIN

[M.musculus], hypothetical protein 500 2915 AA996782 u,bb MGC2721, lamin 81, lamin B2 50 2920 AA996813 d 502 19525 AA996856 aa,General TABLEHUMAN OMOLOGUE N~TA'T~I~N-S. ~,~E- Atty. ~ocket No.
3: H AN 44921-5U89W~

~oe. No. 1798S9f7,1 ~Seq. GenBank Homologo s " '.
ID Aec.l Gene I

No. dentifieref. Seq. Model Name ~.~,3~a,~..Ho~o,~9ous Cluster I ID No. Code ~ Name 503 2984 AA997015 c 504 2986 AA997028 General 505 3145 AA997237 General 506 19249 AA997342 m 507 16883 AA997345 General methylene tetrahydrofolate dehydrogenase (NAD+
dependent), methenyltetrahydrofolate 508 12598 AA997362 s cycloh drolase, protease, serine, EST, Weakly similar to LIS1 MOUSE

PLATELET-ACTIVATING
FACTOR

ACETYLHYDROLASEIB
ALPHA

SUBUNIT [R.norvegicus], ESTs, Weakly similar to PLATELET-ACTIVATING
FACTOR

ACETYLHYDROLASEIB
ALPHA

SUBUNIT [R.norvegicus], WD repeat domain 3, f-box and WD-40 domain protein 2, hypothetical protein MGC2655, platelet-activating factor acetylhydrolase beta subunit (PAF-AH

beta), platelet-activating factor acetylhydrolase, isoform 1b, beta1 subunit, platelet-activating factor acetylhydrolase, isoform Ib, alpha 509 3470 AA997374 p subunit(45kD

t EST, Weakly similar to PLASMINOGEN ACTIVATOR

INHIBITOR-2, TYPE
A [R.norvegicus], expressed sequence AI876477, expressed sequence C76171, 'plasminogen activator inhibitor 2 type A, serine (or cysteine) proteinase inhibitor, Glade B (ovalbumin), member 2, serine (or cysteine) proteinase inhibitor, Glade B (ovalbumin), member 511 3245 AA997608 General 6, serine rotease inhibitor 12 t Homo sapiens, clone IMAGE:4810400, mRNA, antigen identified by 513 3269 AA997800 ,aa monoclonal antibod x Ki 67 f DNA segment, Chr 4, ERATO Doi 639, expressed, EST, Moderately similar to SPECIFIC CYCLIN
B2 [M.musculus], ESTs, Weakly similar to CGB1_HUMAN G2/MITOTIC-SPECIFIC CYCLIN
B [H.sapiens], 515 23992 AA998164 k,x c clin B1 biliverdin reductase B (flavin reductase 516 17470 AA998264 b (NADPH)) B-cell CLL/lymphoma 3, molecule possessing ankyrin repeats induced by lipopolysaccharide (MAIL), homolog of mouse, nuclear factor of kappa light polypeptide gene enhancer in B-cells 517 3773 AA998356 General inhibitor, epsilon 518 19623 AA998422 General ESTs, Weakly similar to G2/MITOTIC-SPECIFIC CYCLIN
B1 [R.norvegicus], cyclin A2, cyclin B1, cyclin B1, related 519 3572 AA998516 se uence 1, c clin x B2 cyclin-dependent kinase inhibitor (P57), cyclin-dependent kinase 520 2782 AA998565 inhibitor 1C ( 57, c Ki 2 TABLE 3' OMOLOGUE NOTATIONS Atty. Docket No.

Doc. No. 1798897.1 Seq. ID GenBank Homologous E i No. IdentifierAee./ Model Gene ~Homolo'I'go~us Ref. Seq. Code Name Cluster Name 1U No.

521 26119 AA998576 ,r,w,General i 522 22737 AA998660 as 523 3696 AA999030 a 524 3079 AA999169 k,x,General Signal transducer and activator of transcription 3, expressed sequence AA408197, signal transducer and activator of transcription 1, signal transducer and activator of transcription 1, 91kD, signal transducer and activator of transcription 2, signal transducer and signal transduceractivator of transcription and 3, signal activator transducer and activator of transcriptionof 1, signal transducertranscription 3 and (acute-phase response activator factor), signal of transcriptiontransducer and 1, activator 525 3081 AA999171 e,p,r 9lkD of transcription ESTs, Moderately similar to A54847 GMP synthase [H.sapiens], guanine 526 3082 AA999172 General monphosphate s nthetase 527 17337 AB000717 k phospholipase D1, phophatidylcholine-528 1535 AB000778 a specific, phos holi ase D2 Homer, neuronal immediate early gene, 1B, Homer, neuronal immediate early gene, 2, homer, neuronal RuvB (E coli immediate early homology-likegene, 1, homer, 529 1382 AB002406 k 1, RuvB-like neuronal immediate protein 1 earl gene, 2 530 20184 AB003753 d EST, Weakly similar to JC5408 carboxylesterase [H.sapiens], ESTs, Moderately similar to ES22 MOUSE

LIVER CARBOXYLESTERASE

PRECURSOR [M.musculus], ESTs, Weakly similar to carboxylesterase [H.sapiens], ESTs, Weakly similar to carboxylesterase [H.sapiens], T-complex expressed gene 5, carboxylesterase 1, carboxylesterase 2 (intestine, liver), carboxylesterase 3, carboxylesterase 3 (brain), 531 4312 AB010635 c,i,j,k, h othetical protein ,z FLJ21736 DNA (cytosine-5-)-methyltransferase 1, DNA (cytosine-5-)-methyltransferase 2, DNA

methyltransferase (cytosine-5) 1, EST, Weakly similar to [R.norvegicus], Mus musculus DNA

cytosine methyltransferase mRNA, f-box and leucine-rich repeat protein 11, 532 21666 AB012214 k protein containing CXXC domain 2 Mus musculus mouse-thyrotropin-releasing hormone receptor 2 (TRH-R2) mRNA, complete cds, thyrotropin releasing hormone receptor, 533 15772 AB015645 g th rotro in-releasing hormone rece for TABLEHUMAN OMOLOGUE N~TATIONS "i4ttyD~ocket No.
3: H AN 44921-5U89~W0 Doc. No. 1798597.1 Seq. GenBank Homologous ID Aee.l Gene No. dentifierRef. Seq. Model Name , ~~ Homologo,.u_s Cluster I I~ No. Code Name ESTs, Weakly similar to DUSB_HUMAN DUAL
SPECIFICITY

PROTEIN PHOSPHATASE

[H.sapiens], Human DNA sequence from clone RP11-243J16 on chromosome 20 Contains parts of 2 isoforms of the BCL2L1 (BCL2-like 1 ) gene, the gene for a novel protein (FLS353), the gene for a protein similar to MYLK
(myosin, light polypeptide kinase), the FKHL18 (forkhead (Drosophila)-like 18) gene, part of three novel genes, ESTs, STSs, GSSs and CpG
islands, KIAA1725 protein, dual specificity phosphatase 13.
dual specificity phosphatase 14, dual specificity phosphatase 5, expressed sequence BB104621, expressed sequence 079103, protein tyrosine phosphatase, 534 1183 AF013144 h non-receptor t a B-cell CLUlymphoma 6, member B

(zinc finger protein), ESTs, Moderately similar to zinc finger protein [H.sapiens], Homo sapiens, Similar to RIKEN cDNA 0610020102 gene, clone MGC:23427 IMAGE:4654320, mRNA, 535 1582 AF015911 h,z com lete cds 536 11483 AF020618 u,cc,General HLA-G histocompatibility antigen, 537 20295 AF024712 s class I, G
a hypothetical protein, clone 1-53, small inducible cytokine subfamily D (Cys-X3 Cys), member 1 (fractalkine, neurotactin), small inducible cytokine 538 19077 AF030358 ,z subfamily D, 1 RIKEN cDNA 4632428M18 gene, hyaluronidase 1, hyaluronidase 2, hyaluronoglucosaminidase 1, hyaluronoglucosaminidase 2, hyaluronoglucosaminidase 3, sperm 539 23044 AF034218 General adhesion molecule d ESTs, Moderately similar to hepatitis A

virus cellular receptor 1 [H.sapiens], ESTs, Moderately similar to kidney injury molecule-1 [R.norvegicus], ESTs, Weakly similar to kidney injury 541 1564 AF035963 ,bb,General molecule-1 R.norvegicus x ESTs, Moderately similar to NR54_HUMAN 54 KDA
NUCLEAR

RNA-BINDING PROTEIN
[H.sapiens], ESTs, Moderately similar to p54nrb [H.sapiens], ESTs, Weakly similar to A54691 octamer-binding protein NonO

- mouse [M.musculus], ESTs, Weakly similar to PSF_HUMAN
PTB-ASSOCIATED SPLICING
FACTOR

[H.sapiens], RIKEN
cDNA

5730470009 gene, RIKEN cDNA

9030402K04 gene, non-POU-domain-542 8426 AF036335 containin , octamer-bindin f rotein TABLE: HUMANOMOLOGUE NOTATI~NS ~4ttvy. Docket No.

Uoe. No. 1798897.1 ~Seq. GenBank Homologous,,~Gene IU Aee.l No. IdentifierRef. Seq. Model Name~~ Hod ~oloclous Cluster I~ No. Code Name E

ESTs, Highly similar to A55318 serine/threonine protein kinase [M.musculus], ESTs, Weakly similar to RIP MOUSE SERINE/THREONINE

PROTEIN KINASE RIP
[M.musculus], Human DNA sequence from clone RP5-1182A14 on chromosome Contains part of a gene similar to rat Espin, a pseudogene similar to KIAA0454, a gene similar to MST1 (macrophage stimulating 1 (hepatocyte growth factor-like)), a pseudogene similar to KIAA0445, two isoforms of a novel gene (isoform 2 is the gene for KIAA1245 protein), ESTs, STSs, GSSs and CpG islands, ankyrin repeat domain 3, cerebral cavernous malformations 1, mitogen activated protein kinase kinase kinase 12, mitogen-activated protein kinase kinase kinase 12, receptor (TNFRSF)-interacting serine-threonine kinase 1, receptor interacting protein 3, receptor-543 21817 AF036537 k interactin serine-threonine kinase 2 solute carrier family 1 ( neuronal/epithelial high affinity glutamate t ransporter, system Xag), member 1, solute carrier 544 21145 AF038571 General amil 1, member f 1 2,4-dienoyl CoA
reductase 1, mitochondrial, 2,4-dienoyl CoA

reductase 2, peroxisomal, 2-4-dienoyl-Coenzyme A reductase 2, peroxisomal, ESTs, Weakly similar to S11021 2,4-dienoyl-CoA
reductase [R.norvegicus], Homo Sapiens AS10 protein mRNA, partial cds, RIKEN

cDNA 1200012F07 gene, RIKEN

cDNA 2400003818 gene, hydroxyprostaglandin dehydrogenase 15 (NAD), hydroxysteroid (17-beta) dehydrogenase 10, peroxisomal traps 2-enoyl CoA reductase;
putative short 545 22602 AF044574 General chain alcohol dehydrogenase UDP-glucose ceramide 546 13464 AF047707 h lucosyltransferase x EST, Highly similar to JC5807 trp3 protein - rat [R.norvegicus], EST, Weakly similar to TRP1_MOUSE

TRANSIENT RECEPTOR
POTENTIAL

CHANNEL 1 (TRANSIENT

RECEPTOR PROTEIN
1) (MTRP1) (TRP-RELATED PROTEIN
1) [M.musculus], transient receptor potential channel 1, transient receptor protein 1, transient receptor protein 3, transient receptor protein 4, transient 548 12259 AF061266 rece for rotein h 5 TABLE: HllMAOMOLOGUE N~TATI'~NvS Atty. Docket No.

Doe. N~1t7~9$39t7~1.

Seq. GenBank Homologous ID Aee./ Gene No. IdentifierRef. Seq. Model Narne Hom ~o~lo~,gwous ID No. Code Cluster Name EST, Highly similar to A61209 hypertension-associated protein SA -rat [R.norvegicus], ESTs, Highly similar to A61209 hypertension-associated protein SA - rat [R.norvegicus], ESTs, Weakly similar to 154401 hypertension-associated protein SA [H.sapiens], protein, SA (rat hypertension-associated) homolog, SA rat hypertension-associated homolog, expressed sequence AI788978, hypothetical protein FLJ20581, medium-chain acyl-CoA
synthetase, solute carrier family 27 (fatty acid transporter), member 1, solute carrier family 27 (fatty acid transporter), 549 4589 AF062389 ,z member 4 ESTs, Highly similar to 2008109A set gene [R.norvegicus], ESTs, Highly similar to SET_HUMAN
SET PROTEIN

[H.sapiens], SET
translocation, SET

translocation (myeloid leukemia-associated), nucleosome assembly protein 1-like 1, nucleosome assembly nucleosome protein 1-like 2, assembly nucleosome assembly 550 16007 AF062594 rotein 1-likerotein 1-like 4 t 1 KIAA1348 protein, protein phosphatase 1 G
(formerly 2C), magnesium-dependent, gamma 551 15761 AF062741 a isoform 552 17426 AF073839 p 553 18615 AF074608 s ESTs, Moderately similar to T17365 serine/threonine protein kinase rat (R.norvegicus], ESTs, Weakly similar to ST25_MOUSE

SERINE/THREONINE
PROTEIN

KINASE 25 (STERILE

STRESS-RESPONSE
KINASE 1) (STE20/OXIDANT STRESS

) (SOK-1 ) (STE20-LIKE KINASE) [M.musculus], KIAA1361 protein, STE20-like kinase, expressed sequence AU020252, prostate derived STE20-like kinase PSK, serine/threonine kinase 10, thousand and one amino acid protein 554 15797 AF084205 kinase f ESTs, Moderately similar to A55575 ankyrin 3, long splice form [H.sapiens], RIKEN cDNA 2310026615 gene, RIKEN cDNA 2410004E01 gene, RIKEN cDNA 2410197A17 gene, RIKEN cDNA 4933400N19 gene, RIKEN cDNA 8430401 K06 gene, RIKEN cDNA C430011 H06 gene, ankyrin 3, node of Ranvier (ankyrin G), hypothetical protein FLJ20189, phospholipase A2, group VI, phospholipase A2, group VI (cytosolic, calcium-independent), proteasome (prosome, macropain) 26S subunit, 555 12932 AF102552 s non-ATPase, 10 TABLE: HUMANOMOLOGUE NOTATIONS]f _Atty. ~ocket No.

Uoe. No. 1798397.1 Seq. GenBank Homologous ID Aee.l Gene No. IdentifierRef. Seq.Model Name ~;jY, Hornohogous Cluster I~ No: Code Narne EST, Moderately similar to A49013 tumor cell suppression protein HTS1 [H.sapiens], KIAA1277 protein, hypothetical protein FLJ22457, 556 18603 A1007649 x suppression of tumorigenicit 557 22733 A1007668 r 558 22746 A1007672 r 559 24109 A1007725 General EST, Highly similar to HS9B RAT

HEAT SHOCK PROTEIN

BETA [R.norvegicus], EST, Weakly similar to HHMS84 heat shock protein 84 - mouse [M.musculus], ESTs, Highly similar to T46243 hypothetical protein DKFZp761K0511.1 [H.sapiens], expressed sequence AL022974,expressed sequence C81438, heat shock 90kD protein 1, 560 15848 A1007820 n,v beta, heat shock protein, 84 kDa HGF-regulated tyrosine kinase substrate, Homo Sapiens cDNA

FLJ13428 fis, clone PLACE1002493, highly similar to Homo Sapiens signal transducing adaptor molecule 2A

(STAM2) mRNA, Mouse 31-kDa proline-rich salivary protein, complete cds of clone pUMP125, Mus musculus, Similar to proline-rich protein BstNl subfamily 2, clone MGC:18611 IMAGE:4165240, mRNA, complete cds, RIKEN cDNA
1700120F24 gene, RIKEN cDNA 4930406E12 gene, Rattus norvegicus proline-rich proteoglycan (PRPG2) mRNA, complete cds, proline-rich protein Haelll subfamily 2, signal transducing adaptor molecule (SH3 domain and 561 10108 A1007857 f ITAM motif) 2 562 6804 A1007877 General 563 20099 A1007893 f,u 564 11368 A1007948 d EST, Highly similar to HS9B RAT

HEAT SHOCK PROTEIN

BETA [R.norvegicus], EST, Weakly similar to HHMS84 heat shock protein 84 - mouse [M.musculus], ESTs, Highly similar to T46243 hypothetical protein DKFZp761K0511.1 [H.sapiens], expressed sequence AL022974,expressed sequence C81438, heat shock 90kD protein 1, 565 15849 A1008074 h beta, heat shock protein, 84 kDa 566 3121 A1008160 General CGI-83 rotein TABLE: HUMANOMOL~GUE NOTATIONS Atty. Docket No.

Uo e. No. 1798397.

Seq. GenBank _ _ ID Acc.l Homologous Gene No. 'Identifier~f. Seq. Model Name Homologo,~s Cluster ' I~ No. Code Name :

EST, Highly similar to JC7290 guanine nucleotide binding protein G gamma chain [H.sapiens], EST, Weakly similar to GBG9 RAT GUANINE

NUCLEOTIDE-BINDING
PROTEIN

G(I)/G(S)/G(O) GAMMA-9 SUBUNIT

[M.musculus], EST, Weakly similar to JC7290 guanine nucleotide binding protein G gamma 2 chain [H.sapiens], RIKEN cDNA 1110003P13 gene, guanine nucleotide binding protein (G

protein), gamma 12, guanine nucleotide binding protein (G protein), gamma 2, guanine nucleotide binding protein (G protein), gamma 2 subunit, guanine nucleotide binding protein (G

protein), gamma 3 subunit, guanine nucleotide binding protein (G protein), gamma 4 subunit, guanine nucleotide 567 16646 A1008190 binding rotein 4 t EST, Moderately similar to CGB2 CYCLIN B2 [M.musculus], ESTs, Weakly similar to SPECIFIC CYCLIN
B1 [R.norvegicus], Homo sapiens cDNA
FLJ13342 fis, clone OVARC1001950, cyclin A1, cyclin B1, cyclin B1, related sequence 568 12683 A1008203 x 1, c clin B2 ESTs, Highly similar to PROTO-ONCOGENE SERINE/THREONINE-[M.musculus], ESTs, Highly similar to S55333 protein kinase pim-2 [M.musculus], ESTs, Moderately similar to S55333 protein kinase pim-2 [M.musculus], Pim-1 oncogene, pim-1 oncogene, pim-2 oncogene, proviral integration site 1, serine threonine 569 22018 A1008309 b kinase im3 570 23917 A1008441 n phos hogluconate deh drogenase 571 22599 A1008458 General 572 22698 A1008578 p,General 573 14405 A1008579 ,x r EST, Weakly similar to JH0446 75K

autoantigen [H.sapiens], polymyositis/scleroderma autoantigen 574 4086 A1008629 1 75kD) x DnaJ (Hsp40) homolog, subfamily B, member 1, DnaJ (Hsp40) homolog, subfamily B, member 12, DnaJ

(Hsp40) homolog, subfamily B, member 4, DnaJ (Hsp40) homolog, subfamily B, member 5, ESTs, Weakly similar to HS4L_HUMAN
HEAT

HOMOLOG [H.sapiens].
RIKEN cDNA

1700029A20 gene, RIKEN cDNA

575 3808 A1008643 ,v,General 2010306619 gene i I

DEMANDE OU BREVET VOLUMINEUX
LA PRESENTE PARTIE DE CETTE DEMANDE OU CE BREVET COMPREND
PLUS D'UN TOME.

NOTE : Pour les tomes additionels, veuillez contacter 1e Bureau canadien des brevets JUMBO APPLICATIONS/PATENTS
THIS SECTION OF THE APPLICATION/PATENT CONTAINS MORE THAN ONE
VOLUME

NOTE: For additional volumes, please contact the Canadian Patent Office NOM DU FICHIER / FILE NAME
NOTE POUR LE TOME / VOLUME NOTE:

Claims (59)

WE CLAIM:

1. A method of predicting at least one toxic effect of a compound, comprising:
(a) preparing a gene expression profile of a tissue or cell sample exposed to the compound; and (b) comparing the gene expression profile to a database comprising at least part of the data or information of Tables 1-5.

2. A method of claim 1, wherein the gene expression profile prepared from the tissue or cell sample comprises the level of expression for at least one gene.

3. A method of claim 2, wherein the level of expression is compared to a Tox Mean and/or NonTox Mean value in Tables 5-5CC.

4. A method of claim 3, wherein the level of expression is normalized prior to comparison.

5. A method of claim 1, wherein the database comprises substantially all of the data or information in Tables 5-5CC.

6. A method of predicting at least one toxic effect of a compound, comprising:
(a) detecting the level of expression in a tissue or cell sample exposed to the compound of two or more genes from Tables 1-5; wherein differential expression of the genes in Tables 1-5 is indicative of at least one toxic effect.

7. A method of predicting the progression of a toxic effect of a compound, comprising:
(a) detecting the level of expression in a tissue or cell sample exposed to the compound of two or more genes from Tables 1-5; wherein differential expression of the genes in Tables 1-5 is indicative of toxicity progression.

8. A method of predicting the renal toxicity of a compound, comprising:
(a) detecting the level of expression in a tissue or cell sample exposed to the compound of two or more genes from Tables 1-5; wherein differential expression of the genes in Tables 1-5 is indicative of renal toxicity.

9. A method of identifying an agent that modulates the onset or progression of a toxic response, comprising:
(a) exposing a cell to the agent and a known toxin; and (b) detecting the expression level of two or more genes from Tables 1-5;
wherein differential expression of the genes in Tables 1-5 is indicative of toxicity.

10. A method of predicting the cellular pathways that a compound modulates in a cell, comprising:
(a) detecting the level of expression in a tissue or cell sample exposed to the compound of two or more genes from Tables 1-5; wherein differential expression of the genes in Tables 1-5 is associated the modulation of at least one cellular pathway.

11. The method of any one of claims 6-10, wherein the expression levels of at least 3 genes are detected.

12. The method of any one of claims 6-10, wherein the expression levels of at least 4 genes are detected.

13. The method of any one of claims 6-10, wherein the expression levels of at least 5 genes are detected.

14. The method of any one of claims 6-10, wherein the expression levels of at least 6 genes are detected.

15. The method of any one of claims 6-10, wherein the expression levels of at least 7 genes are detected.

16. The method of any one of claims 6-10, wherein the expression levels of at least 8 genes are detected.

17. The method of any one of claims 6-10, wherein the expression levels of at least 9 genes are detected.

18. The method of any one of claims 6-10, wherein the expression levels of at least genes are detected.

19. A method of claim 6 or 7, wherein the effect is selected from the group consisting of nephritis, kidney necrosis, glomerular and tubular injury, and focal segmental glomerulosclerosis.

20. A method of claim 8, wherein the renal toxicity is associated with at least one kidney disease pathology selected from the group consisting of nephritis, kidney necrosis, glomerular and tubular injury, and focal segmental glomerulosclerosis.

21. A method of claim 10, wherein the cellular pathway is modulated by a toxin selected from the group consisting of cephaloridine, cisplatin, puromycin aminonucleoside (PAN), bromoethylamine hydrobromide (BEA), gentamicin, ifosfamide, cyclophosphamide, carboplatin, AY-25329, indomethacin, acyclovir, citrinin, mercuric chloride, diflunisal, cidofovir, pamidronate, lithium, hydralazine, colchicine, sulfadiazine, and adriamycin.

22. A set of at least two probes, wherein each of the probes comprises a sequence that specifically hybridizes to a gene in Tables 1-5.

23. A set of probes according to claim 22, wherein the set comprises probes that hybridize to at least 3 genes.

24. A set of probes according to claim 22, wherein the set comprises probes that hybridize to at least 5 genes.

25. A set of probes according to claim 22, wherein the set comprises probes that hybridize to at least 7 genes.

26. A set of probes according to claim 22, wherein the set comprises probes that hybridize to at least 10 genes.

27. A set of probes according to any one of claims 22-26, wherein the probes are attached to a solid support.

28. A set of probes according to claim 27, wherein the solid support is selected from the group consisting of a membrane, a glass support and a silicon support.

29. A solid support comprising at least two probes, wherein each of the probes comprises a sequence that specifically hybridizes to a gene in Tables 1-5.

30. A solid support of claim 29, wherein the solid support is an array comprising at least 10 different oligonucleotides in discrete locations per square centimeter.

31. A solid support of claim 29, wherein the array comprises at least about different oligonucleotides in discrete locations per square centimeter.

32. A solid support of claim 29, wherein the array comprises at least about different oligonucleotides in discrete locations per square centimeter.

33. A solid support of claim 29, wherein the array comprises at least about 10,000 different oligonucleotides in discrete locations per square centimeter.

34. A computer system comprising:
(a) a database containing information identifying the expression level in a tissue or cell sample exposed to a renal toxin of a set of genes comprising at least two genes in Tables 1-5; and (b) a user interface to view the information.

35. A computer system of claim 34, wherein the database further comprises sequence information for the genes.

36. A computer system of claim 34, wherein the database further comprises information identifying the expression level for the set of genes in the tissue or cell sample before exposure to a renal toxin.

37. A computer system of claim 34, wherein the database further comprises information identifying the expression level of the set of genes in a tissue or cell sample exposed to at least a second renal toxin.

38. A computer system of any of claims 34-37, further comprising records including descriptive information from an external database, which information correlates said genes to records in the external database.

39. A computer system of claim 38, wherein the external database is GenBank.

40. A method of using a computer system of any one of claims 34-37 to present information identifying the expression level in a tissue or cell of at least one gene in Tables 1-5, comprising:
comparing the expression level of at least one gene in Tables 1-5 in a tissue or cell exposed to a test agent to the level of expression of the gene in the database.

41. A method of claim 40, wherein the expression levels of at least two genes are compared.

42. A method of claim 40, wherein the expression levels of at least five genes are compared.

43. A method of claim 40, wherein the expression levels of at least ten genes are compared.

44. A method of claim 40, further comprising the step of displaying the level of expression of at least one gene in the tissue or cell sample compared to the expression level when exposed to a toxin.

45. A method of claim 9, wherein the known toxin is a renal toxin.

46. A method of claim 42, wherein the renal toxin is selected from the group consisting of cephaloridine, cisplatin, puromycin aminonucleoside (Pale, bromoethylamine hydrobromide (BEA), gentamicin, ifosfamide, cyclophosphamide, carboplatin, AY-25329, indomethacin, acyclovir, citrinin, mercuric chloride, diflunisal, cidofovir, pamidronate, lithium, hydralazine, colchicine, sulfadiazine, and adriamycin.

47. A method of any one of claims 6-10, wherein nearly all of the genes in Tables 1-5 are detected.

48. A method of claim 47, wherein all of the genes in at least one of Tables 5-are detected.

49. A kit comprising at least one solid support of any one of claims 29-33 packaged with gene expression information for said genes.

50. A kit of claim 49, wherein the gene expression information comprises gene expression levels in a tissue or cell sample exposed to a renal toxin.

51. A kit of claim 50, wherein the gene expression information is in an electronic format.

52. A method of any one of claims 6-10, wherein the compound exposure is in vivo or in vitro.

53. A method of any one of claims 6-10, wherein the level of expression is detected by an amplification or hybridization assay.

54. A method of claim 53, wherein the amplification assay is quantitative or semi-quantitative PCR.

55. A method of claim 53, wherein the hybridization assay is selected from the group consisting of Northern blot, dot or slot blot, nuclease protection and microarray assays.

56. A method of identifying an agent that modulates at least one activity of a protein encoded by a gene in Tables 1-5 comprising:
(a) exposing the protein to the agent; and (b) assaying at least one activity of said protein.

57. A method of claim 56, wherein the agent is exposed to a cell expressing the protein.

58. A method of claim 57, wherein the cell is exposed to a known toxin.

59. A method of claim 58 wherein the toxin modulates the expression of the protein.