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Human Metabolome Database Version 2.5

 

Showing metabocard for Formylanthranilic acid (HMDB04089)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-08-13 11:37:45
Update Date 2010-03-16 15:50:37
Accession Number HMDB04089
Secondary Accession Numbers Not Available
Common Name Formylanthranilic acid
Description Formylanthranilic acid is a polar acid metabolite of anthranilic acid, occasionally found in human urine. (PMID 7320161)
Synonyms
  1. 2-(Formylamino)-benzoic acid
  2. 2-(formylamino)benzoate
  3. 2-formamidobenzoate
  4. Formylanthranilate
  5. N-Formylanthranilate
  6. 2-(Formylamino)-benzoate
  7. 2-(formylamino)benzoic acid
  8. 2-formamidobenzoic acid
Chemical IUPAC Name 2-formamidobenzoate
Chemical Formula C8H7NO3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Aminobenzoates
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • secondary carboxylic acid amide
  • aromatic compound
Biofunction
  • Protein synthesis, amino acid biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 165.146
Monoisotopic Molecular Weight 165.042587
Isomeric SMILES OC(=O)C1=CC=CC=C1NC=O
Canonical SMILES OC(=O)C1=CC=CC=C1NC=O
KEGG Compound ID C05653 Link Image
BioCyc ID Not Available
BiGG ID 46205 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB04089 Link Image
Metagene Link HMDB04089 Link Image
METLIN ID Not Available
PubChem Compound 5459905 Link Image
PubChem Substance 8143772 Link Image
ChEBI ID 18410 Link Image
CAS Registry Number 3342-77-6
InChI Identifier InChI=1/C8H7NO3/c10-5-9-7-4-2-1-3-6(7)8(11)12/h1-5H,(H,9,10)(H,11,12)
Synthesis Reference Prashad, Mahavir; Har, Denis; Repic, Oljan; Blacklock, Thomas J.; Chin, Jefferson A.; Shapiro, Michael J. Reaction of benzoyleneurea and isatoic anhydride with the Vilsmeier reagent. Tetrahedron Letters (1997), 38(8), 1313-1316.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 2.33 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 0.28 [Predicted by ALOGPS] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Tryptophan Metabolism SMP00063 Link Image map00380 Link Image
General References Not Available
Metabolic Enzymes
  1. Probable arylformamidase
  2. Kynureninase (L-kynurenine hydrolase)
  3. AFMID protein
Enzyme 1 [top]
Enzyme 1 ID 13059
Enzyme 1 Name Probable arylformamidase
Enzyme 1 Synonyms
  1. Kynurenine formamidase
  2. KF
Enzyme 1 Gene Name AFMID
Enzyme 1 Protein Sequence >Probable arylformamidase
MMDVSGVGFPSKVPWKKMSAEELENQYCPSRWVVRLGAEEALRTYSQIGIEATTRARATR
KSLLHVPYGDGEGEKVDIYFPDESSEALPFFLFFHGGYWQSGSKDESAFMVHPLTAQGVA
VVIVAYGIAPKGTLDHMVDQVTRSVAFVQKRYPSNKGIYLCGHSAGAHLAAMMLLADWTK
HGVTPNLRGFFLVSGVFDLEPIVYTSQNVALQLTLEDAQRNSPQLKVAQAQPVDPTCRVL
VVVGQFDSPEFHRQSWEFYQTLCQGEWKASFEELHDVDHFEIVENLTQKDNVLTQIILKT
IFQ
Enzyme 1 Number of Residues 303
Enzyme 1 Molecular Weight 33991.5
Enzyme 1 Theoretical pI 5.78
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
  • metabolic process
Component
Enzyme 1 General Function Involved in hydrolase activity
Enzyme 1 Specific Function Catalyzes the hydrolysis of N-formyl-L-kynurenine to L- kynurenine, the second step in the conversion of tryptophan to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites
Enzyme 1 Pathways
Enzyme 1 Reactions
  • N-formyl-L-kynurenine + H2O = formate + L-kynurenine [RN:R01959]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 124375910 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q63HM1 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name AFMID_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >912 bp
ATGATGGATGTGTCTGGTGTGGGTTTCCCAAGCAAGGTTCCTTGGAAGAAGATGTCTGCA
GAGGAGCTGGAGAATCAGTACTGTCCCAGCCGATGGGTTGTCCGACTGGGAGCAGAGGAA
GCCTTGAGGACCTACTCACAGATAGGAATTGAAGCCACCACAAGGGCCCGGGCCACCAGG
AAGAGCCTGCTGCATGTCCCCTATGGAGACGGCGAAGGGGAGAAAGTGGACATTTACTTC
CCCGACGAGTCGTCTGAAGCCTTGCCTTTCTTCCTGTTCTTTCACGGAGGATACTGGCAG
AGCGGAAGTAAGGATGAGTCTGCCTTCATGGTCCACCCGCTGACGGCACAGGGAGTGGCC
GTGGTAATAGTGGCTTACGGCATCGCCCCCAAAGGCACCCTGGACCACATGGTAGACCAG
GTGACCCGCAGCGTTGCGTTTGTCCAGAAGCGGTATCCAAGCAACAAGGGAATTTACCTG
TGTGGACACTCAGCCGGGGCCCACCTGGCTGCCATGATGCTCCTGGCCGACTGGACCAAG
CATGGGGTCACGCCCAACCTCAGAGGCTTTTTCCTGGTGAGTGGGGTCTTTGACCTGGAG
CCCATCGTGTATACTTCACAGAACGTTGCTCTCCAGCTGACCCTGGAGGACGCTCAGAGG
AATAGCCCCCAGCTGAAGGTGGCCCAGGCACAGCCGGTGGACCCCACCTGCCGTGTGCTG
GTGGTCGTGGGCCAGTTCGACTCCCCCGAATTCCACCGACAGTCCTGGGAGTTTTACCAG
ACCCTGTGTCAAGGAGAGTGGAAAGCCTCATTTGAAGAGCTCCACGATGTGGACCACTTT
GAAATTGTTGAGAATCTGACCCAGAAGGACAACGTGCTCACCCAGATTATCTTGAAAACA
ATCTTCCAGTAG
Enzyme 1 GenBank Gene ID BC132824 Link Image
Enzyme 1 GeneCard ID AFMID Link Image
Enzyme 1 GenAtlas ID AFMID Link Image
Enzyme 1 HGNC ID HGNC:20910 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 17q25.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 13118
Enzyme 2 Name Kynureninase (L-kynurenine hydrolase)
Enzyme 2 Synonyms
  1. SubName: Kynureninase (L-kynurenine hydrolase), isoform CRA_a
Enzyme 2 Gene Name KYNU
Enzyme 2 Protein Sequence >Kynureninase (L-kynurenine hydrolase)
MEPSSLELPADTVQRIAAELKCHPTDERVALHLDEEDKLRHFRECFYIPKIQDLPPVDLS
LVNKDENAIYFLGNSLGLQPKMVKTYLEEELDKWAKIAAYGHEVGKRPWITGDESIVGLM
KDIVGANEKEIALMNALTVNLHLLMLSFFKPTPKRYKILLEAKAFPSDHYAIESQLQLHG
LNIEESMRMIKPREGEETLRIEDILEVIEKEGDSIAVILFSGVHFYTGQHFNIPAITKAG
QAKGCYVGFDLAHAVGNVELYLHDWGVDFACWCSYKYLNAGAGGIAGAFIHEKHAHTIKP
ARSEFFN
Enzyme 2 Number of Residues 307
Enzyme 2 Molecular Weight 34634.5
Enzyme 2 Theoretical pI 5.71
Enzyme 2 GO Classification
Function
  • binding
  • catalytic activity
  • cofactor binding
  • hydrolase activity
  • hydrolase activity, acting on acid carbon-carbon bonds
  • hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
  • kynureninase activity
  • pyridoxal phosphate binding
Process
  • NAD biosynthetic process
  • cellular amino acid and derivative metabolic process
  • cellular amino acid derivative metabolic process
  • cellular biogenic amine metabolic process
  • cellular metabolic process
  • coenzyme biosynthetic process
  • coenzyme metabolic process
  • cofactor metabolic process
  • indolalkylamine metabolic process
  • metabolic process
  • nicotinamide nucleotide biosynthetic process
  • pyridine nucleotide biosynthetic process
  • tryptophan catabolic process
  • tryptophan metabolic process
Component
  • cell part
  • cytoplasm
  • intracellular part
Enzyme 2 General Function Involved in metabolic process
Enzyme 2 Specific Function Not Available
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions Not Available
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 12654129 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q9BVW3 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name Q9BVW3_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >924 bp
ATGGAGCCTTCATCTCTTGAGCTGCCGGCTGACACAGTGCAGCGCATTGCGGCTGAACTC
AAATGCCACCCAACGGATGAGAGGGTGGCTCTCCACCTAGATGAGGAAGATAAGCTGAGG
CACTTCAGGGAGTGCTTTTATATTCCCAAAATACAGGATCTGCCTCCAGTTGATTTATCA
TTAGTGAATAAAGATGAAAATGCCATCTATTTCTTGGGAAATTCTCTTGGCCTTCAACCA
AAAATGGTTAAAACATATCTTGAAGAAGAACTAGATAAGTGGGCCAAAATAGCAGCCTAT
GGTCATGAAGTGGGGAAGCGTCCTTGGATTACAGGAGATGAGAGTATTGTAGGCCTTATG
AAGGACATTGTAGGAGCCAATGAGAAAGAAATAGCCCTAATGAATGCTTTGACTGTAAAT
TTACATCTTCTAATGTTATCATTTTTTAAGCCTACGCCAAAACGATATAAAATTCTTCTA
GAAGCCAAAGCCTTCCCTTCTGATCATTATGCTATTGAGTCACAACTACAACTTCACGGA
CTTAACATTGAAGAAAGTATGCGGATGATAAAGCCAAGAGAGGGGGAAGAAACCTTAAGA
ATAGAGGATATCCTTGAAGTAATTGAGAAGGAAGGAGACTCAATTGCAGTGATCCTGTTC
AGTGGGGTGCATTTTTACACTGGACAGCACTTTAATATTCCTGCCATCACAAAAGCTGGA
CAAGCGAAGGGTTGTTATGTTGGCTTTGATCTAGCACATGCAGTTGGAAATGTTGAACTC
TACTTACATGACTGGGGAGTTGATTTTGCCTGCTGGTGTTCCTACAAGTATTTAAATGCA
GGAGCAGGAGGAATTGCTGGTGCCTTCATTCATGAAAAGCATGCCCATACGATTAAACCT
GCGAGATCGGAGTTCTTTAATTAG
Enzyme 2 GenBank Gene ID BC000879 Link Image
Enzyme 2 GeneCard ID KYNU Link Image
Enzyme 2 GenAtlas ID KYNU Link Image
Enzyme 2 HGNC ID HGNC:6469 Link Image
Enzyme 2 Chromosome Location 2
Enzyme 2 Locus 2q22.2
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 15219
Enzyme 3 Name AFMID protein
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name AFMID
Enzyme 3 Protein Sequence >AFMID protein
MMDVSGVGFPSKVPWKKMSAEELENQYCPSRWVVRLGAEEALRTYSQIGIEATTRARATR
KSLLHVPYGDGEGEKVDIYFPDESSEALPFFLFFHGGYWQSGSKDESAFMVHPLTAQGVA
VVIVAYGIAPKGTLDHMVDQVTRSVAFVQKRYPSNKGIYLCGHSAGAHLAAMMLLADWTK
HGVTPNLRGFFLVSGVFDLEPIVYTSQNVALQLTLEDAQRNSPQLKVAQAQPVDPTCRVL
VVVGQFDSPEFHRQSWEFYQTLCQGEWKASFEELHDVDHFEIVENLTQKDNVLTQIILKT
IFQ
Enzyme 3 Number of Residues 303
Enzyme 3 Molecular Weight 33992
Enzyme 3 Theoretical pI 5.78
Enzyme 3 GO Classification Not Available
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function Not Available
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 124375910 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID A2RUB3 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name A2RUB3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >912 bp
ATGATGGATGTGTCTGGTGTGGGTTTCCCAAGCAAGGTTCCTTGGAAGAAGATGTCTGCA
GAGGAGCTGGAGAATCAGTACTGTCCCAGCCGATGGGTTGTCCGACTGGGAGCAGAGGAA
GCCTTGAGGACCTACTCACAGATAGGAATTGAAGCCACCACAAGGGCCCGGGCCACCAGG
AAGAGCCTGCTGCATGTCCCCTATGGAGACGGCGAAGGGGAGAAAGTGGACATTTACTTC
CCCGACGAGTCGTCTGAAGCCTTGCCTTTCTTCCTGTTCTTTCACGGAGGATACTGGCAG
AGCGGAAGTAAGGATGAGTCTGCCTTCATGGTCCACCCGCTGACGGCACAGGGAGTGGCC
GTGGTAATAGTGGCTTACGGCATCGCCCCCAAAGGCACCCTGGACCACATGGTAGACCAG
GTGACCCGCAGCGTTGCGTTTGTCCAGAAGCGGTATCCAAGCAACAAGGGAATTTACCTG
TGTGGACACTCAGCCGGGGCCCACCTGGCTGCCATGATGCTCCTGGCCGACTGGACCAAG
CATGGGGTCACGCCCAACCTCAGAGGCTTTTTCCTGGTGAGTGGGGTCTTTGACCTGGAG
CCCATCGTGTATACTTCACAGAACGTTGCTCTCCAGCTGACCCTGGAGGACGCTCAGAGG
AATAGCCCCCAGCTGAAGGTGGCCCAGGCACAGCCGGTGGACCCCACCTGCCGTGTGCTG
GTGGTCGTGGGCCAGTTCGACTCCCCCGAATTCCACCGACAGTCCTGGGAGTTTTACCAG
ACCCTGTGTCAAGGAGAGTGGAAAGCCTCATTTGAAGAGCTCCACGATGTGGACCACTTT
GAAATTGTTGAGAATCTGACCCAGAAGGACAACGTGCTCACCCAGATTATCTTGAAAACA
ATCTTCCAGTAG
Enzyme 3 GenBank Gene ID BC132824 Link Image
Enzyme 3 GeneCard ID A2RUB3 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location 17
Enzyme 3 Locus 17q25.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available