|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5821 |
| Enzyme 1 Name |
Bile acid-CoA:amino acid N-acyltransferase |
| Enzyme 1 Synonyms |
- BACAT
- BAT
- Glycine N-choloyltransferase
- Long-chain fatty-acyl-CoA hydrolase
|
| Enzyme 1 Gene Name |
BAAT |
| Enzyme 1 Protein Sequence |
>Bile acid-CoA:amino acid N-acyltransferase
MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDL
NHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVAS
APKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASL
LASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQI
GLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFE
TTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGA
GHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL
|
| Enzyme 1 Number of Residues |
418 |
| Enzyme 1 Molecular Weight |
46298.9 |
| Enzyme 1 Theoretical pI |
7.00 |
| Enzyme 1 GO Classification |
| Function |
- CoA hydrolase activity
- acyl-CoA thioesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- palmitoyl-CoA hydrolase activity
- thiolester hydrolase activity
|
| Process |
- acyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in thiolester hydrolase activity |
| Enzyme 1 Specific Function |
Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs |
| Enzyme 1 Pathways |
- Bile Acid Biosynthesis (map00120
)
- Taurine and Hypotaurine Metabolism (map00430
)
|
| Enzyme 1 Reactions |
- palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q14032  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
BAAT_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1257 bp
ATGATCCAGTTGACAGCTACCCCTGTGAGTGCACTTGTTGATGAGCCAGTGCATATCCGA
GCTACAGGCCTGATTCCCTTTCAGATGGTGAGTTTTCAGGCATCACTGGAAGATGAAAAC
GGAGACATGTTTTATTCTCAAGCCCACTATAGGGCCAATGAATTCGGTGAGGTGGACCTG
AATCATGCTTCTTCACTTGGAGGGGATTATATGGGAGTCCACCCCATGGGTCTCTTCTGG
TCTCTGAAACCTGAAAAGCTATTAACAAGACTGTTGAAAAGAGATGTGATGAATAGGCCT
TTCCAGGTCCAAGTAAAACTTTATGACTTAGAGTTAATAGTGAACAATAAAGTTGCCAGT
GCTCCAAAGGCCAGCCTGACTTTGGAGAGGTGGTATGTGGCACCTGGTGTCACACGAATT
AAGGTTCGAGAAGGCCGCCTTCGAGGAGCTCTCTTTCTCCCTCCAGGAGAGGGTCTCTTC
CCAGGGGTAATTGATTTGTTTGGTGGTTTGGGTGGGCTGCTTGAATTTCGGGCCAGCCTC
CTAGCCAGTCGTGGCTTCGCCTCCTTGGCCTTGGCTTACCATAACTATGAAGACCTGCCC
CGCAAACCAGAAGTAACAGATTTGGAATATTTTGAGGAGGCTGCCAACTTTCTCCTGAGA
CATCCAAAGGTCTTTGGCTCAGGCGTTGGGGTAGTCTCTGTATGTCAAGGAGTACAGATT
GGACTATCTATGGCTATTTACCTAAAGCAAGTCACAGCCACGGTACTTATTAATGGGACC
AACTTTCCTTTTGGCATTCCACAGGTATATCATGGTCAGATCCATCAGCCCCTTCCCCAT
TCTGCACAATTAATATCCACCAATGCCTTGGGGTTACTAGAGCTCTATCGCACTTTTGAG
ACAACTCAAGTTGGGGCCAGTCAATATTTGTTTCCTATTGAAGAGGCCCAGGGGCAATTC
CTCTTCATTGTAGGAGAAGGTGATAAGACTATCAACAGCAAAGCACACGCTGAACAAGCC
ATAGGACAGCTGAAGAGACATGGGAAGAACAACTGGACCCTGCTATCTTACCCTGGGGCA
GGCCACCTGATAGAACCTCCCTATTCTCCTCTGTGCTGTGCCTCAACGACCCACGATTTG
AGGTTACACTGGGGAGGAGAGGTGATCCCACACGCAGCTGCACAGGAACATGCTTGGAAG
GAGATCCAGAGATTTCTCAGGAAGCACCTCATTCCAGATGTGACCAGTCAACTCTAA
|
| Enzyme 1 GenBank Gene ID |
L34081  |
| Enzyme 1 GeneCard ID |
BAAT  |
| Enzyme 1 GenAtlas ID |
BAAT  |
| Enzyme 1 HGNC ID |
HGNC:932  |
| Enzyme 1 Chromosome Location |
9 |
| Enzyme 1 Locus |
9q22.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Falany CN, Johnson MR, Barnes S, Diasio RB: Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase. J Biol Chem. 1994 Jul 29;269(30):19375-9. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- 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
]
- Johnson MR, Barnes S, Kwakye JB, Diasio RB: Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver. J Biol Chem. 1991 Jun 5;266(16):10227-33. [PubMed
]
- Sfakianos MK, Wilson L, Sakalian M, Falany CN, Barnes S: Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase. J Biol Chem. 2002 Dec 6;277(49):47270-5. Epub 2002 Sep 17. [PubMed
]
- O'Byrne J, Hunt MC, Rai DK, Saeki M, Alexson SE: The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine. J Biol Chem. 2003 Sep 5;278(36):34237-44. Epub 2003 Jun 16. [PubMed
]
- Carlton VE, Harris BZ, Puffenberger EG, Batta AK, Knisely AS, Robinson DL, Strauss KA, Shneider BL, Lim WA, Salen G, Morton DH, Bull LN: Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat Genet. 2003 May;34(1):91-6. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5975 |
| Enzyme 2 Name |
Glutamate decarboxylase 2 |
| Enzyme 2 Synonyms |
- 65 kDa glutamic acid decarboxylase
- GAD-65
- Glutamate decarboxylase 65 kDa isoform
|
| Enzyme 2 Gene Name |
GAD2 |
| Enzyme 2 Protein Sequence |
>Glutamate decarboxylase 2
MASPGSGFWSFGSEDGSGDSENPGTARAWCQVAQKFTGGIGNKLCALLYGDAEKPAESGG
SQPPRAAARKAACACDQKPCSCSKVDVNYAFLHATDLLPACDGERPTLAFLQDVMNILLQ
YVVKSFDRSTKVIDFHYPNELLQEYNWELADQPQNLEEILMHCQTTLKYAIKTGHPRYFN
QLSTGLDMVGLAADWLTSTANTNMFTYEIAPVFVLLEYVTLKKMREIIGWPGGSGDGIFS
PGGAISNMYAMMIARFKMFPEVKEKGMAALPRLIAFTSEHSHFSLKKGAAALGIGTDSVI
LIKCDERGKMIPSDLERRILEAKQKGFVPFLVSATAGTTVYGAFDPLLAVADICKKYKIW
MHVDAAWGGGLLMSRKHKWKLSGVERANSVTWNPHKMMGVPLQCSALLVREEGLMQNCNQ
MHASYLFQQDKHYDLSYDTGDKALQCGRHVDVFKLWLMWRAKGTTGFEAHVDKCLELAEY
LYNIIKNREGYEMVFDGKPQHTNVCFWYIPPSLRTLEDNEERMSRLSKVAPVIKARMMEY
GTTMVSYQPLGDKVNFFRMVISNPAATHQDIDFLIEEIERLGQDL
|
| Enzyme 2 Number of Residues |
585 |
| Enzyme 2 Molecular Weight |
65410.8 |
| Enzyme 2 Theoretical pI |
6.89 |
| Enzyme 2 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in carboxy-lyase activity |
| Enzyme 2 Specific Function |
Catalyzes the production of GABA |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- L-glutamate = 4-aminobutanoate + CO2 [RN:R00261]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
Not Available |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q05329  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
DCE2_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1758 bp
ATGGCATCTCCGGGCTCTGGCTTTTGGTCTTTCGGGTCGGAAGATGGCTCTGGGGATTCC
GAGAATCCCGGCACAGCGCGAGCCTGGTGCCAAGTGGCTCAGAAGTTCACGGGCGGCATC
GGAAACAAACTGTGCGCCCTGCTCTACGGAGACGCCGAGAAGCCGGCGGAGAGCGGCGGG
AGCCAACCCCCGCGGGCCGCCGCCCGGAAGGCCGCCTGCGCCTGCGACCAGAAGCCCTGC
AGCTGCTCCAAAGTGGATGTCAACTACGCGTTTCTCCATGCAACAGACCTGCTGCCGGCG
TGTGATGGAGAAAGGCCCACTTTGGCGTTTCTGCAAGATGTTATGAACATTTTACTTCAG
TATGTGGTGAAAAGTTTCGATAGATCAACCAAAGTGATTGATTTCCATTATCCTAATGAG
CTTCTCCAAGAATATAATTGGGAATTGGCAGACCAACCACAAAATTTGGAGGAAATTTTG
ATGCATTGCCAAACAACTCTAAAATATGCAATTAAAACAGGGCATCCTAGATACTTCAAT
CAACTTTCTACTGGTTTGGATATGGTTGGATTAGCAGCAGACTGGCTGACATCAACAGCA
AATACTAACATGTTCACCTATGAAATTGCTCCAGTATTTGTGCTTTTGGAATATGTCACA
CTAAAGAAAATGAGAGAAATCATTGGCTGGCCAGGGGGCTCTGGCGATGGGATATTTTCT
CCCGGTGGCGCCATATCTAACATGTATGCCATGATGATCGCACGCTTTAAGATGTTCCCA
GAAGTCAAGGAGAAAGGAATGGCTGCTCTTCCCAGGCTCATTGCCTTCACGTCTGAACAT
AGTCATTTTTCTCTCAAGAAGGGAGCTGCAGCCTTAGGGATTGGAACAGACAGCGTGATT
CTGATTAAATGTGATGAGAGAGGGAAAATGATTCCATCTGATCTTGAAAGAAGGATTCTT
GAAGCCAAACAGAAAGGGTTTGTTCCTTTCCTCGTGAGTGCCACAGCTGGAACCACCGTG
TACGGAGCATTTGACCCCCTCTTAGCTGTCGCTGACATTTGCAAAAAGTATAAGATCTGG
ATGCATGTGGATGCAGCTTGGGGTGGGGGATTACTGATGTCCCGAAAACACAAGTGGAAA
CTGAGTGGCGTGGAGAGGGCCAACTCTGTGACGTGGAATCCACACAAGATGATGGGAGTC
CCTTTGCAGTGCTCTGCTCTCCTGGTTAGAGAAGAGGGATTGATGCAGAATTGCAACCAA
ATGCATGCCTCCTACCTCTTTCAGCAAGATAAACATTATGACCTGTCCTATGACACTGGA
GACAAGGCCTTACAGTGCGGACGCCACGTTGATGTTTTTAAACTATGGCTGATGTGGAGG
GCAAAGGGGACTACCGGGTTTGAAGCGCATGTTGATAAATGTTTGGAGTTGGCAGAGTAT
TTATACAACATCATAAAAAACCGAGAAGGATATGAGATGGTGTTTGATGGGAAGCCTCAG
CACACAAATGTCTGCTTCTGGTACATTCCTCCAAGCTTGCGTACTCTGGAAGACAATGAA
GAGAGAATGAGTCGCCTCTCGAAGGTGGCTCCAGTGATTAAAGCCAGAATGATGGAGTAT
GGAACCACAATGGTCAGCTACCAACCCTTGGGAGACAAGGTCAATTTCTTCCGCATGGTC
ATCTCAAACCCAGCGGCAACTCACCAAGACATTGACTTCCTGATTGAAGAAATAGAACGC
CTTGGACAAGATTTATAA
|
| Enzyme 2 GenBank Gene ID |
M81882  |
| Enzyme 2 GeneCard ID |
GAD2  |
| Enzyme 2 GenAtlas ID |
GAD2  |
| Enzyme 2 HGNC ID |
HGNC:4093  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
10p11.23 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Karlsen AE, Hagopian WA, Grubin CE, Dube S, Disteche CM, Adler DA, Barmeier H, Mathewes S, Grant FJ, Foster D, et al.: Cloning and primary structure of a human islet isoform of glutamic acid decarboxylase from chromosome 10. Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8337-41. [PubMed
]
- Bu DF, Erlander MG, Hitz BC, Tillakaratne NJ, Kaufman DL, Wagner-McPherson CB, Evans GA, Tobin AJ: Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2115-9. [PubMed
]
- Bu DF, Tobin AJ: The exon-intron organization of the genes (GAD1 and GAD2) encoding two human glutamate decarboxylases (GAD67 and GAD65) suggests that they derive from a common ancestral GAD. Genomics. 1994 May 1;21(1):222-8. [PubMed
]
- Mauch L, Abney CC, Berg H, Scherbaum WA, Liedvogel B, Northemann W: Characterization of a linear epitope within the human pancreatic 64-kDa glutamic acid decarboxylase and its autoimmune recognition by sera from insulin-dependent diabetes mellitus patients. Eur J Biochem. 1993 Mar 1;212(2):597-603. [PubMed
]
- Kim J, Richter W, Aanstoot HJ, Shi Y, Fu Q, Rajotte R, Warnock G, Baekkeskov S: Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets. Diabetes. 1993 Dec;42(12):1799-808. [PubMed
]
- Namchuk M, Lindsay L, Turck CW, Kanaani J, Baekkeskov S: Phosphorylation of serine residues 3, 6, 10, and 13 distinguishes membrane anchored from soluble glutamic acid decarboxylase 65 and is restricted to glutamic acid decarboxylase 65alpha. J Biol Chem. 1997 Jan 17;272(3):1548-57. [PubMed
]
- Kanaani J, el-Husseini Ael-D, Aguilera-Moreno A, Diacovo JM, Bredt DS, Baekkeskov S: A combination of three distinct trafficking signals mediates axonal targeting and presynaptic clustering of GAD65. J Cell Biol. 2002 Sep 30;158(7):1229-38. [PubMed
]
- Corper AL, Stratmann T, Apostolopoulos V, Scott CA, Garcia KC, Kang AS, Wilson IA, Teyton L: A structural framework for deciphering the link between I-Ag7 and autoimmune diabetes. Science. 2000 Apr 21;288(5465):505-11. [PubMed
]
- Fenalti G, Law RH, Buckle AM, Langendorf C, Tuck K, Rosado CJ, Faux NG, Mahmood K, Hampe CS, Banga JP, Wilce M, Schmidberger J, Rossjohn J, El-Kabbani O, Pike RN, Smith AI, Mackay IR, Rowley MJ, Whisstock JC: GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop. Nat Struct Mol Biol. 2007 Apr;14(4):280-6. Epub 2007 Mar 25. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6005 |
| Enzyme 3 Name |
Gamma-glutamyltranspeptidase 1 |
| Enzyme 3 Synonyms |
- GGT 1
- Gamma-glutamyltransferase 1
- CD224 antigen
- Gamma-glutamyltranspeptidase 1 heavy chain
- Gamma-glutamyltranspeptidase 1 light chain
|
| Enzyme 3 Gene Name |
GGT1 |
| Enzyme 3 Protein Sequence |
>Gamma-glutamyltranspeptidase 1
MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRD
GGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFN
SSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALEN
KRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKD
IQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSR
ESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISD
DTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNE
MDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTA
TALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTF
IAVVQAIVRTAGGWAAASDSRKGGEPAGY
|
| Enzyme 3 Number of Residues |
569 |
| Enzyme 3 Molecular Weight |
61409.7 |
| Enzyme 3 Theoretical pI |
7.14 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- gamma-glutamyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in gamma-glutamyltransferase activity |
| Enzyme 3 Specific Function |
Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive |
| Enzyme 3 Pathways |
- Arachidonic acid metabolism (map00590
)
- Cyanoamino acid metabolism (map00460
)
- Glutathione Metabolism (map00480
)
- Selenoamino Acid Metabolism (map00450
)
- Taurine and Hypotaurine Metabolism (map00430
)
|
| Enzyme 3 Reactions |
- (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid [RN:R04159]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
183138  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P19440  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
GGT1_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1710 bp
ATGAAGAAGAAGTTAGTGGTGCTGGGCCTGCTGGCCGTGGTCCTGGTGCTGGTCATTGTC
GGCCTCTGTCTCTGGCTGCCCTCAGCCTCCAAGGAACCTGACAACCATGTGTACACCAGG
GCTGCCGTGGCCGCGGATGCCAAGCAGTGCTCGAAGATTGGGAGGGATGCACTGCGGGAC
GGTGGCTCTGCGGTGGATGCAGCCATTGCAGCCCTGTTGTGTGTGGGGCTCATGAATGCC
CACAGCATGGGCATCGGGGGTGGCCTCTTCCTCACCATCTACAACAGCACCACACGAAAA
GCTGAGGTCATCAACGCCCGCGAGGTGGCCCCCAGGCTGGCCTTTGCCACCATGTTCAAC
AGCTCGGAGCAGTCCCAGAAGGGGGGGCTGTCGGTGGCGGTGCCTGGGGAGATCCGAGGC
TATGAGCTGGCACACCAGCGGCATGGGCGGCTGCCCTGGGCTCGCCTCTTCCAGCCCAGC
ATCCAGCTGGCCCGCCAGGGCTTCCCCGTGGGCAAGGGCTTGGCGGCAGCCCTGGAAAAC
AAGCGGACCGTCATCGAGCAGCAGCCTGTCTTGTGTGAGGTGTTCTGCCGGGATAGAAAG
GTGCTTCGGGAGGGGGAGAGACTGACCCTGCCGCAGCTGGCTGACACCTACGAGACGCTG
GCCATCGAGGGTGCCCAGGCCTTCTACAACGGCAGCCTCACGGCCCAGATTGTGAAGGAC
ATCCAGGCGGCCGGGGGCATTGTGACAGCTGAGGACCTGAACAACTACCGTGCTGAGCTG
ATCGAGCACCCGCTGAACATCAGCCTGGGAGACGCGGTGCTGTACATGCCCAGTGCGCCG
CTCAGCGGGCCCGTGCTGGCCCTCATCCTCAACATCCTCAAAGGGTACAACTTCTCCCGG
GAGAGCGTGGAGAGCCCCGAGCAGAAGGGCCTGACGTACCACCGCATCGTAGAGGCTTTC
CGGTTTGCCTACGCCAAGAGGACCCTGCTTGGGGACCCCAAGTTTGTGGATGTGACTGAG
GTGGTCCGCAACATGACCTCCGAGTTCTTCGCTGCCCAGCTCCGGGCCCAGATCTCTGAC
GACACCACTCACCCGATCTCCTACTACAAGCCCGAGTTCTACACGCCGGATGACGGGGGC
ACTGCTCACCTGTCTGTCGTCGCAGAGGACGGCAGTGCTGTGTCCGCCACCAGCACCATC
AACCTCTACTTTGGCTCCAAGGTCCGCTCCCCGGTCAGCGGGATCCTGTTCAATAATGAA
ATGGACGACTTCAGCTCTCCCAGCATCACCAACGAGTTTGGGGTACCCCCCTCACCTGCC
AATTTCATCCAGCCAGGGAAGCAGCCGCTCTCGTCCATGTGCCCGACGATCATGGTGGGC
CAGGACGGCCAGGTCCGGATGGTGGTGGGAGCTGCTGGGGGCACACAGATCACCACGGCC
ACTGCACTGGCCATCATCTACAACCTCTGGTTCGGCTATGACGTGAAGCGGGCCGTGGAG
GAGCCCCGGCTGCACAACCAGCTTCTGCCCAACGTCACGACAGTGGAGAGAAACATTGAC
CAGGCAGTGACTGCAGCCCTGGAGACCCGGCACCATCACACCCAGATCGCGTCCACCTTC
ATCGCTGTGGTGCAAGCCATCGTCCGCACGGCTGGTGGCTGGGCAGCTGCCTCGGACTCC
AGGAAAGGCGGGGAGCCTGCCGGCTACTGA
|
| Enzyme 3 GenBank Gene ID |
J04131  |
| Enzyme 3 GeneCard ID |
GGT1  |
| Enzyme 3 GenAtlas ID |
GGT1  |
| Enzyme 3 HGNC ID |
HGNC:4250  |
| Enzyme 3 Chromosome Location |
2 |
| Enzyme 3 Locus |
22q11.23 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Rajpert-De Meyts E, Heisterkamp N, Groffen J: Cloning and nucleotide sequence of human gamma-glutamyl transpeptidase. Proc Natl Acad Sci U S A. 1988 Dec;85(23):8840-4. [PubMed
]
- Sakamuro D, Yamazoe M, Matsuda Y, Kangawa K, Taniguchi N, Matsuo H, Yoshikawa H, Ogasawara N: The primary structure of human gamma-glutamyl transpeptidase. Gene. 1988 Dec 15;73(1):1-9. [PubMed
]
- Pitot HC, Goodspeed D, Dunn T, Hendrich S, Maronpot RR, Moran S: Regulation of the expression of some genes for enzymes of glutathione metabolism in hepatotoxicity and hepatocarcinogenesis. Toxicol Appl Pharmacol. 1989 Jan;97(1):23-34. [PubMed
]
- Goodspeed DC, Dunn TJ, Miller CD, Pitot HC: Human gamma-glutamyl transpeptidase cDNA: comparison of hepatoma and kidney mRNA in the human and rat. Gene. 1989 Mar 15;76(1):1-9. [PubMed
]
- Pawlak A, Cohen EH, Octave JN, Schweickhardt R, Wu SJ, Bulle F, Chikhi N, Baik JH, Siegrist S, Guellaen G: An alternatively processed mRNA specific for gamma-glutamyl transpeptidase in human tissues. J Biol Chem. 1990 Feb 25;265(6):3256-62. [PubMed
]
- Courtay C, Oster T, Michelet F, Visvikis A, Diederich M, Wellman M, Siest G: Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues. Biochem Pharmacol. 1992 Jun 23;43(12):2527-33. [PubMed
]
- Wetmore LA, Gerard C, Drazen JM: Human lung expresses unique gamma-glutamyl transpeptidase transcripts. Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7461-5. [PubMed
]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- 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
]
- Tate SS, Khadse V, Wellner D: Renal gamma-glutamyl transpeptidases: structural and immunological studies. Arch Biochem Biophys. 1988 May 1;262(2):397-408. [PubMed
]
- Chikhi N, Holic N, Guellaen G, Laperche Y: Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species. Comp Biochem Physiol B Biochem Mol Biol. 1999 Apr;122(4):367-80. [PubMed
]
- Tate SS, Ross ME: Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit. J Biol Chem. 1977 Sep 10;252(17):6042-5. [PubMed
]
- Tate SS, Galbraith RA: In vitro translation and processing of human hepatoma cell (Hep G2) gamma-glutamyl transpeptidase. Biochem Biophys Res Commun. 1988 Aug 15;154(3):1167-73. [PubMed
]
- Ikeda Y, Fujii J, Taniguchi N: Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis. J Biol Chem. 1993 Feb 25;268(6):3980-5. [PubMed
]
- Ikeda Y, Fujii J, Taniguchi N, Meister A: Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit. J Biol Chem. 1995 May 26;270(21):12471-5. [PubMed
]
- Ikeda Y, Fujii J, Anderson ME, Taniguchi N, Meister A: Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase. J Biol Chem. 1995 Sep 22;270(38):22223-8. [PubMed
]
- Ikeda Y, Fujii J, Taniguchi N: Effects of substitutions of the conserved histidine residues in human gamma-glutamyl transpeptidase. J Biochem (Tokyo). 1996 Jun;119(6):1166-70. [PubMed
]
- Kristiansen TZ, Bunkenborg J, Gronborg M, Molina H, Thuluvath PJ, Argani P, Goggins MG, Maitra A, Pandey A: A proteomic analysis of human bile. Mol Cell Proteomics. 2004 Jul;3(7):715-28. Epub 2004 Apr 14. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6224 |
| Enzyme 4 Name |
Cysteine sulfinic acid decarboxylase |
| Enzyme 4 Synonyms |
- Cysteine-sulfinate decarboxylase
- Sulfinoalanine decarboxylase
|
| Enzyme 4 Gene Name |
CSAD |
| Enzyme 4 Protein Sequence |
>Cysteine sulfinic acid decarboxylase
MADSEALPSLAGDPVAVEALLRAVFGVVVDEAIQKGTSVSQKVCEWKEPEELKQLLDLEL
RSQGESQKQILERCRAVIRYSVKTGHPRFFNQLFSGLDPHALAGRIITESLNTSQYTYEI
APVFVLMEEEVLRKLRALVGWSSGDGIFCPGGSISNMYAVNLARYQRYPDCKQRGLRTLP
PLALFTSKECHYSIQKGAAFLGLGTDSVRVVKADERGKMVPEDLERQIGMAEAEGAVPFL
VSATSGTTVLGAFDPLEAIADVCQRHGLWLHVDAAWGGSVLLSQTHRHLLDGIQRADSVA
WNPHKLLAAGLQCSALLLQDTSNLLKRCHGSQASYLFQQDKFYDVALDTGDKVVQCGRRV
DCLKLWLMWKAQGDQGLERRIDQAFVLARYLVEEMKKREGFELVMEPEFVNVCFWFVPPS
LRGKQESPDYHERLSKVAPVLKERMVKEGSMMIGYQPHGTRGNFFRVVVANSALTCADMD
FLLNELERLGQDL
|
| Enzyme 4 Number of Residues |
493 |
| Enzyme 4 Molecular Weight |
55022.8 |
| Enzyme 4 Theoretical pI |
6.44 |
| Enzyme 4 GO Classification |
| Function |
- binding
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- cofactor binding
- lyase activity
- pyridoxal phosphate binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- metabolic process
- organic acid metabolic process
- oxoacid metabolic process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in carboxy-lyase activity |
| Enzyme 4 Specific Function |
3-sulfino-L-alanine = hypotaurine + CO(2) |
| Enzyme 4 Pathways |
- Taurine and Hypotaurine Metabolism (map00430
)
|
| Enzyme 4 Reactions |
- 3-sulfino-L-alanine = hypotaurine + CO2 [RN:R02466]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
4894560  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9Y600  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
CSAD_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1482 bp
ATGGCTGACTCAGAAGCACTCCCCTCCCTTGCTGGGGACCCAGTGGCTGTGGAAGCCTTG
CTCCGGGCCGTGTTTGGGGTTGTTGTGGATGAGGCCATTCAGAAAGGAACCAGTGTCTCC
CAGAAGGTCTGTGAGTGGAAGGAGCCTGAGGAGCTGAAGCAGCTGCTGGATTTGGAGCTG
CGGAGCCAGGGCGAGTCACAGAAGCAGATCCTGGAGCGGTGTCGGGCTGTGATTCGCTAC
AGTGTCAAGACTGGTCACCCTCGGTTCTTCAACCAGCTCTTCTCTGGGTTGGATCCCCAT
GCTCTGGCCGGGCGCATTATCACTGAGAGCCTCAACACCAGCCAGTACACATATGAAATC
GCCCCCGTGTTTGTGCTCATGGAAGAGGAGGTGCTGAGGAAACTGCGGGCCCTGGTGGGC
TGGAGCTCTGGGGACGGAATCTTCTGCCCTGGTGGCTCCATCTCCAACATGTATGCTGTA
AATCTGGCCCGCTATCAGCGCTACCCGGATTGCAAGCAGAGGGGCCTCCGCACACTGCCG
CCCCTGGCCCTATTCACATCGAAGGAGTGTCACTACTCCATCCAGAAGGGAGCTGCGTTT
CTGGGACTTGGCACCGACAGTGTCCGAGTGGTCAAGGCTGATGAGAGAGGGAAAATGGTC
CCCGAGGATCTGGAGAGGCAGATTGGTATGGCCGAGGCTGAGGGTGCTGTGCCGTTCCTG
GTCAGTGCCACCTCTGGCACCACTGTGCTAGGGGCCTTTGACCCCCTGGGGGCAATTGCT
GATGTGTGCCAGCGTCATGGGCTATGGCTGCATGTGGATGCTGCCTGGGGTGGGAGCGTC
CTGCTGTCACAGACACACAGGCATCTCCTGGATGGGATCCAGAGGGCTGACTCTGTGGCC
TGGAATCCCCACAAGCTCCTCGCAGCAGGCCTGCAATGCTCTGCACTTCTTCTCCAGGAT
ACCTCGAACCTGCTCAAGCGCTGCCATGGGTCCCAGGCCAGCTACCTTTTCCAGCAGGAC
AAGTTCTACGATGTGGCTCTGGACACGGGAGACAAGGTGGTGCAGTGTGGCCGCCGTGTG
GACTGTCTGAAGCTGTGGCTCATGTGGAAGGCACAGGGCGATCAAGGGCTGGAGCGGCGC
ATCGACCAGGCCTTTGTCCTTGCCCGGTACCTGGTGGAGGAAATGAAGAAGCGGGAAGGG
TTTGAGCTAGTCATGGAGCCTGAGTTTGTCAATGTGTGTTTCTGGTTCGTACCCCCCAGC
CTGCGAGGGAAGCAGGAGAGTCCAGATTACCACGAAAGGCTGTCAAAGGTGGCCCCCGTG
CTCAAGGAGCGCATGGTGAAGGAGGGCTCCATGATGATTGGCTACCAGCCCCACGGGACC
CGGGGCAACTTCTTCCGTGTGGTTGTGGCCAACTCTGCACTGACCTGTGCTGATATGGAC
TTCCTCCTCAACGAGCTGGAGCGGCTAGGCCAGGACCTGTGA
|
| Enzyme 4 GenBank Gene ID |
AF116547  |
| Enzyme 4 GeneCard ID |
CSAD  |
| Enzyme 4 GenAtlas ID |
CSAD  |
| Enzyme 4 HGNC ID |
HGNC:18966  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
12q13.11-q14.3 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
7966 |
| Enzyme 5 Name |
Hypothetical protein GAD1 |
| Enzyme 5 Synonyms |
Not Available |
| Enzyme 5 Gene Name |
GAD1 |
| Enzyme 5 Protein Sequence |
>Hypothetical protein GAD1
MASSTPSSSATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEK
SRLVSAFKERQSSKNLLSCENSDRDARFRRTETDFSNLFARDLLPAKNGEEQTVQFLLEV
VDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGV
RTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIVGWS
SKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEQSHYSIKKAGAA
LGFGTDNVILIKCNERGKIIPADFEAKILEAKQKGYVPFYVNATAGTTVYGAFDPIQEIA
DICEKYNLWLHVDAAWGGGLLMSRKHRHKLNGIERANSVTWNPHKMMGVLLQCSAILVKE
KGILQGCNQMCAGYLFQPDKQYDVSYDTGDKAIQCGRHVDIFKFWLMWKAKGTVGFENQI
NKCLELAEYLYAKIKNREEFEMVFNGEPEHTNVCFWYIPQSLRGVPDSPQRREKLHKVAP
KIKALMMESGTTMVGYQPQGDKANFFRMVISNPAATQSDIDFLIEEIERLGQDL
|
| Enzyme 5 Number of Residues |
594 |
| Enzyme 5 Molecular Weight |
66897 |
| Enzyme 5 Theoretical pI |
7.67 |
| Enzyme 5 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
|
| Process |
- amino acid and derivative metabolism
- amino acid metabolism
- cellular metabolism
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Amino acid transport and metabolism |
| Enzyme 5 Specific Function |
Not Available |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
62988850  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q53TQ7  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
Q53TQ7_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1785 bp
ATGGCGTCTTCGACCCCATCTTCGTCCGCAACCTCCTCGAACGCGGGAGCGGACCCCAAT
ACCACTAACCTGCGCCCCACAACGTACGATACCTGGTGCGGCGTGGCCCATGGATGCACC
AGAAAACTGGGGCTCAAGATCTGCGGCTTCTTGCAAAGGACCAACAGCCTGGAAGAGAAG
AGTCGCCTTGTGAGTGCCTTCAAGGAGAGGCAATCCTCCAAGAACCTGCTTTCCTGTGAA
AACAGCGACCGGGATGCCCGCTTCCGGCGCACAGAGACTGACTTCTCTAATCTGTTTGCT
AGAGATCTGCTTCCGGCTAAGAACGGTGAGGAGCAAACCGTGCAATTCCTCCTGGAAGTG
GTGGACATACTCCTCAACTATGTCCGCAAGACATTTGATCGCTCCACCAAGGTGCTGGAC
TTTCATCACCCACACCAGTTGCTGGAAGGCATGGAGGGCTTCAACTTGGAGCTCTCTGAC
CACCCCGAGTCCCTGGAGCAGATCCTGGTTGACTGCAGAGACACCTTGAAGTATGGGGTT
CGCACAGGTCATCCTCGATTTTTCAACCAGCTCTCCACTGGATTGGATATTATTGGCCTA
GCTGGAGAATGGCTGACATCAACGGCCAATACCAACATGTTTACATATGAAATTGCACCA
GTGTTTGTCCTCATGGAACAAATAACACTTAAGAAGATGAGAGAGATAGTTGGATGGTCA
AGTAAAGATGGTGATGGGATATTTTCTCCTGGGGGCGCCATATCCAACATGTACAGCATC
ATGGCTGCTCGCTACAAGTACTTCCCGGAAGTTAAGACAAAGGGCATGGCGGCTGTGCCT
AAACTGGTCCTCTTCACCTCAGAACAGAGTCACTATTCCATAAAGAAAGCTGGGGCTGCA
CTTGGCTTTGGAACTGACAATGTGATTTTGATAAAGTGCAATGAAAGGGGGAAAATAATT
CCAGCTGATTTTGAGGCAAAAATTCTTGAAGCCAAACAGAAGGGATATGTTCCCTTTTAT
GTCAATGCAACTGCTGGCACGACTGTTTATGGAGCTTTTGATCCGATACAAGAGATTGCA
GATATATGTGAGAAATATAACCTTTGGTTGCATGTCGATGCTGCCTGGGGAGGTGGGCTG
CTCATGTCCAGGAAGCACCGCCATAAACTCAACGGCATAGAAAGGGCCAACTCAGTCACC
TGGAACCCTCACAAGATGATGGGCGTGCTGTTGCAGTGCTCTGCCATTCTCGTCAAGGAA
AAGGGTATACTCCAAGGATGCAACCAGATGTGTGCAGGATACCTCTTCCAGCCAGACAAG
CAGTATGATGTCTCCTACGACACCGGGGACAAGGCAATTCAGTGTGGCCGCCACGTGGAT
ATCTTCAAGTTCTGGCTGATGTGGAAAGCAAAGGGCACAGTGGGATTTGAAAACCAGATC
AACAAATGCCTGGAACTGGCTGAATACCTCTATGCCAAGATTAAAAACAGAGAAGAATTT
GAGATGGTTTTCAATGGCGAGCCTGAGCACACAAACGTCTGTTTTTGGTATATTCCACAA
AGCCTCAGGGGTGTGCCAGACAGCCCTCAACGACGGGAAAAGCTACACAAGGTGGCTCCA
AAAATCAAAGCCCTGATGATGGAGTCAGGTACGACCATGGTTGGCTACCAGCCCCAAGGG
GACAAGGCCAACTTCTTCCGGATGGTCATCTCCAACCCAGCCGCTACCCAGTCTGACATT
GACTTCCTCATTGAGGAGATAGAAAGACTGGGCCAGGATCTGTAA
|
| Enzyme 5 GenBank Gene ID |
AC007405  |
| Enzyme 5 GeneCard ID |
GAD1  |
| Enzyme 5 GenAtlas ID |
GAD1  |
| Enzyme 5 HGNC ID |
HGNC:4092  |
| Enzyme 5 Chromosome Location |
2 |
| Enzyme 5 Locus |
2q31 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
Not Available |
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
8394 |
| Enzyme 6 Name |
Sodium- and chloride-dependent taurine transporter |
| Enzyme 6 Synonyms |
- Solute carrier family 6 member 6
|
| Enzyme 6 Gene Name |
SLC6A6 |
| Enzyme 6 Protein Sequence |
>Sodium- and chloride-dependent taurine transporter
MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVG
LGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEIIIGQYTSEGGITCWEKICPLF
SGIGYASVVIVSLLNVYYIVILAWATYYLFQSFQKELPWAHCNHSWNTPHCMEDTMRKNK
SVWITISSTNFTSPVIEFWERNVLSLSPGIDHPGSLKWDLALCLLLVWLVCFFCIWKGVR
STGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDITRLEDPQVWIDAGTQIFF
SYAICLGAMTSLGSYNKYKYNSYRDCMLLGCLNSGTSFVSGFAIFSILGFMAQEQGVDIA
DVAESGPGLAFIAYPKAVTMMPLPTFWSILFFIMLLLLGLDSQFVEVEGQITSLVDLYPS
FLRKGYRREIFIAFVCSISYLLGLTMVTEGGMYVFQLFDYYAASGVCLLWVAFFECFVIA
WIYGGDNLYDGIEDMIGYRPGPWMKYSWAVITPVLCVGCFIFSLVKYVPLTYNKTYVYPN
WAIGLGWSLALSSMLCVPLVIVIRLCQTEGPFLVRVKYLLTPREPNRWAVEREGATPYNS
RTVMNGALVKPTHIIVETMM
|
| Enzyme 6 Number of Residues |
620 |
| Enzyme 6 Molecular Weight |
69829.4 |
| Enzyme 6 Theoretical pI |
7.43 |
| Enzyme 6 GO Classification |
| Function |
- neurotransmitter transporter activity
- neurotransmitter:sodium symporter activity
- taurine:sodium symporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- establishment of localization
- neurotransmitter transport
- transport
|
| Component |
- cell part
- integral to membrane
- integral to plasma membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 6 General Function |
Involved in neurotransmitter:sodium symporter activity |
| Enzyme 6 Specific Function |
Required for the uptake of taurine. Transports both taurine and beta-alanine which requires sodium ions. Chloride ions are necessary for optimal uptake |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
- 50-70
78-97
122-142
218-236
245-262
298-315
327-348
381-400
430-448
465-485
506-525
545-563
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
197276623  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P31641  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
SC6A6_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1863 bp
ATGGCCACCAAGGAGAAGCTGCAGTGTCTGAAAGATTTCCACAAGGACATCCTGAAGCCC
TCACCAGGGAAGAGCCCAGGCACGCGGCCTGAGGACGAGGCTGAGGGAAAACCTCCGCAG
AGGGAGAAGTGGTCTAGCAAGATCGACTTTGTGCTCTCTGTGGCTGGCGGCTTCGTGGGC
TTGGGCAACGTCTGGCGCTTCCCGTACCTCTGCTACAAGAATGGTGGAGGTGCGTTTCTC
ATACCGTATTTTATTTTCCTGTTTGGGAGCGGCCTGCCTGTGTTTTTCTTGGAGATCATC
ATAGGCCAGTACACCTCTGAAGGGGGCATCACCTGCTGGGAAAAGATCTGCCCCTTGTTC
TCTGGTATCGGCTATGCCTCCGTTGTAATTGTGTCCCTCCTGAATGTCTACTACATCGTC
ATCCTGGCCTGGGCCACATACTACCTGTTCCAGTCCTTCCAGAAGGAGCTGCCCTGGGCA
CACTGCAACCACAGCTGGAACACACCTCACTGCATGGAGGACACCATGCGCAAGAACAAG
AGTGTCTGGATCACCATCAGCTCCACCAACTTCACCTCCCCTGTCATCGAGTTCTGGGAG
CGCAACGTGCTGAGCTTGTCCCCTGGAATCGACCACCCAGGCTCTCTGAAATGGGACCTC
GCTCTCTGCCTTCTTTTAGTCTGGCTAGTGTGTTTCTTCTGCATCTGGAAGGGCGTCAGG
TCCACTGGGAAGGTCGTCTACTTCACAGCCACTTTTCCATTCGCCATGCTCCTGGTGCTG
CTGGTCCGAGGGCTGACGCTGCCGGGCGCGGGCGCAGGCATCAAGTTCTATCTGTATCCT
GACATCACCCGCCTTGAGGACCCACAGGTGTGGATTGACGCTGGGACTCAGATATTCTTC
TCTTATGCCATCTGCCTGGGGGCTATGACCTCGCTGGGGAGCTACAACAAGTACAAGTAT
AACTCGTACAGGGACTGTATGCTGCTGGGATGCCTGAACAGTGGTACCAGTTTTGTGTCT
GGCTTCGCAATTTTTTCCATCCTGGGCTTCATGGCACAAGAGCAAGGGGTGGACATTGCT
GATGTGGCTGAGTCAGGTCCTGGCCTGGCCTTCATTGCCTACCCAAAAGCTGTGACAATG
ATGCCGCTGCCCACATTTTGGTCCATTCTTTTTTTTATTATGCTTCTCTTGCTTGGACTG
GATAGCCAGTTTGTTGAAGTTGAAGGACAGATCACATCCTTGGTTGATCTTTACCCATCC
TTCCTAAGGAAGGGTTATCGTCGGGAAATCTTCATCGCCTTCGTGTGTAGCATCAGCTAC
CTGCTGGGGCTGACGATGGTGACGGAGGGTGGCATGTATGTGTTTCAGCTCTTTGACTAC
TATGCAGCTAGCGGTGTATGCCTTTTGTGGGTTGCATTCTTTGAATGTTTTGTTATTGCC
TGGATATATGGAGGTGATAACCTTTATGATGGTATTGAGGACATGATTGGCTATCGGCCC
GGGCCCTGGATGAAGTACAGCTGGGCTGTGATCACTCCAGTTCTCTGTGTTGGATGTTTC
ATCTTCTCGCTCGTCAAGTACGTACCCCTGACCTACAACAAAACATACGTGTACCCCAAC
TGGGCCATTGGGCTGGGCTGGAGCCTGGCCCTTTCCTCCATGCTCTGCGTTCCCTTGGTC
ATCGTCATCCGCCTCTGCCAGACTGAGGGGCCGTTCCTTGTGAGAGTCAAGTACCTGCTG
ACCCCAAGGGAACCCAACCGCTGGGCTGTGGAGCGCGAGGGAGCCACACCTTACAACTCT
CGCACCGTCATGAACGGCGCTCTCGTGAAACCGACCCACATCATTGTGGAGACCATGATG
TGA
|
| Enzyme 6 GenBank Gene ID |
NM_001134367.1  |
| Enzyme 6 GeneCard ID |
SLC6A6  |
| Enzyme 6 GenAtlas ID |
SLC6A6  |
| Enzyme 6 HGNC ID |
HGNC:11052  |
| Enzyme 6 Chromosome Location |
3 |
| Enzyme 6 Locus |
3p25-p24 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Jhiang SM, Fithian L, Smanik P, McGill J, Tong Q, Mazzaferri EL: Cloning of the human taurine transporter and characterization of taurine uptake in thyroid cells. FEBS Lett. 1993 Mar 1;318(2):139-44. [PubMed
]
- Ramamoorthy S, Leibach FH, Mahesh VB, Han H, Yang-Feng T, Blakely RD, Ganapathy V: Functional characterization and chromosomal localization of a cloned taurine transporter from human placenta. Biochem J. 1994 Jun 15;300 ( Pt 3):893-900. [PubMed
]
- Miyamoto Y, Liou GI, Sprinkle TJ: Isolation of a cDNA encoding a taurine transporter in the human retinal pigment epithelium. Curr Eye Res. 1996 Mar;15(3):345-9. [PubMed
]
- Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
12987 |
| Enzyme 7 Name |
Gamma-glutamyltransferase 6 |
| Enzyme 7 Synonyms |
- GGT 6
- Gamma-glutamyltranspeptidase 6
- Gamma-glutamyltransferase 6 heavy chain
- Gamma-glutamyltransferase 6 light chain
|
| Enzyme 7 Gene Name |
GGT6 |
| Enzyme 7 Protein Sequence |
>Gamma-glutamyltransferase 6
MERAEEPVVYQKLLPWEPSLESEEEVEEEETSEALVLNPRRHQDSSRNKAGGLPGTWARV
VAALLLLAVGCSLAVRQLQNQGRSTGSLGSVAPPPGGHSHGPGVYHHGAIISPAGRELLV
AGGNVVDAGVGAALCLAVVHPHATGLGAMFWGLFHDSSSGNSTALTSGPAQTLAPGLGLP
AALPTLHLLHARFGRLPWPRLLVGPTTLAQEGFLVDTPLARALVARGTEGLCPLLCHADG
TPLGAGARATNPQLAAVLRSAALAPTSDLAGDALLSLLAGDLGVEVPSAVPRPTLEPAEQ
LPVPQGILFTTPSPSAGPELLALLEAALRSGAPIPDPCPPFLQTAVSPESSALAAVDSSG
SVLLLTSSLNCSFGSAHLSPSTGVLLSNLVAKSTTSAWACPLILRGSLDDTEADVLGLVA
SGTPDVARAMTHTLLRHLAARPPTQAQHQHQGQQEPTEHPSTCGQGTLLQVAAHTEHAHV
SSVPHACCPFQGF
|
| Enzyme 7 Number of Residues |
493 |
| Enzyme 7 Molecular Weight |
50508.8 |
| Enzyme 7 Theoretical pI |
6.04 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- gamma-glutamyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in gamma-glutamyltransferase activity |
| Enzyme 7 Specific Function |
Cleaves glutathione conjugates |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
- (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid [RN:R04159]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
171543825  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q6P531  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
GGT6_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1482 bp
ATGGAGCGGGCAGAAGAGCCCGTGGTCTATCAGAAGCTGCTGCCCTGGGAGCCAAGCTTG
GAGTCGGAGGAGGAAGTGGAGGAGGAGGAGACATCAGAGGCGCTGGTTCTAAACCCCCGG
AGGCACCAGGACTCTTCCAGGAACAAGGCTGGCGGGCTGCCCGGAACCTGGGCCCGTGTA
GTGGCAGCCCTGCTGCTGCTGGCTGTTGGCTGCTCCCTGGCTGTGAGGCAGCTCCAGAAT
CAGGGCAGGTCGACAGGAAGCTTGGGCTCTGTGGCCCCTCCACCCGGCGGACACTCCCAC
GGCCCTGGCGTATACCACCACGGTGCCATCATCAGCCCTGCAGGCCGAGAGCTGCTTGTT
GCCGGGGGCAACGTCGTGGATGCTGGAGTTGGAGCTGCATTGTGCCTGGCAGTGGTGCAT
CCTCATGCCACGGGGCTAGGTGCCATGTTTTGGGGCCTCTTCCACGATAGCTCCTCAGGC
AATTCCACGGCCCTGACATCAGGCCCAGCACAGACCCTGGCCCCCGGCCTGGGGCTGCCC
GCGGCTCTGCCCACCCTGCACCTGCTGCATGCACGCTTCGGCCGCCTGCCCTGGCCACGC
CTGCTAGTGGGCCCCACCACGCTGGCTCAGGAGGGCTTCCTGGTGGACACACCCCTGGCA
AGGGCTCTGGTGGCTCGGGGCACAGAAGGCCTCTGTCCACTACTTTGCCATGCTGATGGG
ACACCCCTGGGCGCTGGGGCCCGAGCCACCAACCCACAACTGGCAGCTGTGCTTCGCAGC
GCAGCCCTCGCTCCCACCTCAGACCTTGCTGGGGATGCTCTACTGAGTCTACTGGCGGGA
GACCTGGGGGTGGAGGTGCCCTCGGCTGTGCCCAGGCCCACTTTGGAACCAGCAGAGCAG
CTACCTGTGCCCCAGGGCATCCTGTTCACCACCCCCAGTCCCTCAGCTGGCCCAGAACTG
CTGGCACTGTTGGAGGCAGCCCTGCGCTCCGGGGCGCCCATCCCTGACCCCTGCCCACCG
TTCCTGCAGACTGCTGTGAGCCCCGAGAGCAGTGCCCTGGCCGCCGTGGACAGCAGCGGC
TCTGTGCTCCTTCTCACCTCCTCGCTCAACTGCTCCTTTGGCTCTGCACACCTGTCCCCA
AGCACTGGGGTTCTGCTCAGCAACCTGGTGGCCAAGTCTACCACTAGTGCCTGGGCCTGC
CCCCTCATCCTCCGTGGCAGCCTGGATGACACAGAGGCTGATGTGTTGGGGCTTGTGGCT
TCAGGGACCCCTGATGTGGCCAGGGCCATGACTCACACCCTACTCAGGCATCTGGCAGCA
AGGCCCCCTACCCAGGCCCAGCACCAGCATCAGGGTCAGCAAGAACCAACAGAGCATCCC
AGCACTTGTGGCCAAGGGACCCTGCTCCAGGTGGCAGCCCACACAGAGCACGCCCATGTC
TCCAGTGTCCCCCATGCCTGCTGCCCCTTCCAGGGGTTCTAA
|
| Enzyme 7 GenBank Gene ID |
NM_001122890.1  |
| Enzyme 7 GeneCard ID |
GGT6  |
| Enzyme 7 GenAtlas ID |
GGT6  |
| Enzyme 7 HGNC ID |
HGNC:26891  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
17p13.2 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
- Heisterkamp N, Groffen J, Warburton D, Sneddon TP: The human gamma-glutamyltransferase gene family. Hum Genet. 2008 May;123(4):321-32. Epub 2008 Mar 21. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
13927 |
| Enzyme 8 Name |
Glycine receptor subunit alpha-1 |
| Enzyme 8 Synonyms |
- Glycine receptor 48 kDa subunit
- Glycine receptor strychnine-binding subunit
|
| Enzyme 8 Gene Name |
GLRA1 |
| Enzyme 8 Protein Sequence |
>Glycine receptor subunit alpha-1
MYSFNTLRLYLWETIVFFSLAASKEAEAARSAPKPMSPSDFLDKLMGRTSGYDARIRPNF
KGPPVNVSCNIFINSFGSIAETTMDYRVNIFLRQQWNDPRLAYNEYPDDSLDLDPSMLDS
IWKPDLFFANEKGAHFHEITTDNKLLRISRNGNVLYSIRITLTLACPMDLKNFPMDVQTC
IMQLESFGYTMNDLIFEWQEQGAVQVADGLTLPQFILKEEKDLRYCTKHYNTGKFTCIEA
RFHLERQMGYYLIQMYIPSLLIVILSWISFWINMDAAPARVGLGITTVLTMTTQSSGSRA
SLPKVSYVKAIDIWMAVCLLFVFSALLEYAAVNFVSRQHKELLRFRRKRRHHKSPMLNLF
QEDEAGEGRFNFSAYGMGPACLQAKDGISVKGANNSNTTNPPPAPSKSPEEMRKLFIQRA
KKIDKISRIGFPMAFLIFNMFYWIIYKIVRREDVHNQ
|
| Enzyme 8 Number of Residues |
457 |
| Enzyme 8 Molecular Weight |
52623.4 |
| Enzyme 8 Theoretical pI |
9.04 |
| Enzyme 8 GO Classification |
| Function |
- amino acid binding
- binding
- carboxylic acid binding
- extracellular ligand-gated ion channel activity
- extracellular-glycine-gated chloride channel activity
- glycine binding
- inhibitory extracellular ligand-gated ion channel activity
- ion channel activity
- ion transmembrane transporter activity
- ligand-gated ion channel activity
- substrate-specific transmembrane transporter activity
- transmembrane transporter activity
- transmitter-gated ion channel activity
- transporter activity
|
| Process |
- anion transport
- chloride transport
- establishment of localization
- inorganic anion transport
- ion transport
- transport
|
| Component |
- cell part
- integral to membrane
- integral to plasma membrane
- intrinsic to membrane
- membrane
- membrane part
- postsynaptic membrane
|
|
| Enzyme 8 General Function |
Involved in ion transport |
| Enzyme 8 Specific Function |
The glycine receptor is a neurotransmitter-gated ion channel. Binding of glycine to its receptor increases the chloride conductance and thus produces hyperpolarization (inhibition of neuronal firing) |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
- 248-274
281-298
313-336
429-446
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
225903367  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P23415  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
GLRA1_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1374 bp
ATGTACAGCTTCAATACTCTTCGACTCTACCTTTGGGAGACCATTGTATTCTTCAGCCTT
GCTGCTTCTAAGGAGGCTGAAGCTGCTCGCTCCGCACCCAAGCCTATGTCACCCTCGGAT
TTCCTGGATAAGCTAATGGGGAGAACCTCCGGATATGATGCCAGGATCAGGCCCAATTTT
AAAGGTCCCCCAGTGAACGTGAGCTGCAACATTTTCATCAACAGCTTTGGTTCCATTGCT
GAGACAACCATGGACTATAGGGTCAACATCTTCCTGCGGCAGCAATGGAACGACCCCCGC
CTGGCCTATAATGAATACCCTGACGACTCTCTGGACCTGGACCCATCCATGCTGGACTCC
ATCTGGAAACCTGACCTGTTCTTTGCCAACGAGAAGGGGGCCCACTTCCATGAGATCACC
ACAGACAACAAATTGCTAAGGATCTCCCGGAATGGGAATGTCCTCTACAGCATCAGAATC
ACCCTGACACTGGCCTGCCCCATGGACTTGAAGAATTTCCCCATGGATGTCCAGACATGT
ATCATGCAACTGGAAAGCTTTGGATATACGATGAATGACCTCATCTTTGAGTGGCAGGAA
CAGGGAGCCGTGCAGGTAGCAGATGGACTAACTCTGCCCCAGTTTATCTTGAAGGAAGAG
AAGGACTTGAGATACTGCACCAAGCACTACAACACAGGTAAATTCACCTGCATTGAGGCC
CGGTTCCACCTGGAGCGGCAGATGGGTTACTACCTGATTCAGATGTATATTCCCAGCCTG
CTCATTGTCATCCTCTCATGGATCTCCTTCTGGATCAACATGGATGCTGCACCTGCTCGT
GTGGGCCTAGGCATCACCACTGTGCTCACCATGACCACCCAGAGCTCCGGCTCTCGAGCA
TCTCTGCCCAAGGTGTCCTATGTGAAAGCCATTGACATTTGGATGGCAGTTTGCCTGCTC
TTTGTGTTCTCAGCCCTATTAGAATATGCTGCCGTTAACTTTGTGTCTCGGCAACATAAG
GAGCTGCTCCGATTCAGGAGGAAGCGGAGACATCACAAGAGCCCCATGTTGAATCTATTC
CAGGAGGATGAAGCTGGAGAAGGCCGCTTTAACTTCTCTGCCTATGGGATGGGCCCAGCC
TGTCTACAGGCCAAGGATGGCATCTCAGTCAAGGGCGCCAACAACAGTAACACCACCAAC
CCCCCTCCTGCACCATCTAAGTCCCCAGAGGAGATGCGAAAACTCTTCATCCAGAGGGCC
AAGAAGATCGACAAAATATCCCGCATTGGCTTCCCCATGGCCTTCCTCATTTTCAACATG
TTCTACTGGATCATCTACAAGATTGTCCGTAGAGAGGACGTCCACAACCAGTGA
|
| Enzyme 8 GenBank Gene ID |
NM_001146040.1  |
| Enzyme 8 GeneCard ID |
GLRA1  |
| Enzyme 8 GenAtlas ID |
GLRA1  |
| Enzyme 8 HGNC ID |
HGNC:4326  |
| Enzyme 8 Chromosome Location |
5 |
| Enzyme 8 Locus |
5q32 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Grenningloh G, Schmieden V, Schofield PR, Seeburg PH, Siddique T, Mohandas TK, Becker CM, Betz H: Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes. EMBO J. 1990 Mar;9(3):771-6. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
- Vogel N, Kluck CJ, Melzer N, Schwarzinger S, Breitinger U, Seeber S, Becker CM: Mapping of disulfide bonds within the amino-terminal extracellular domain of the inhibitory glycine receptor. J Biol Chem. 2009 Dec 25;284(52):36128-36. Epub 2009 Oct 27. [PubMed
]
- Yushmanov VE, Mandal PK, Liu Z, Tang P, Xu Y: NMR structure and backbone dynamics of the extended second transmembrane domain of the human neuronal glycine receptor alpha1 subunit. Biochemistry. 2003 Apr 8;42(13):3989-95. [PubMed
]
- Ma D, Liu Z, Li L, Tang P, Xu Y: Structure and dynamics of the second and third transmembrane domains of human glycine receptor. Biochemistry. 2005 Jun 21;44(24):8790-800. [PubMed
]
- Shiang R, Ryan SG, Zhu YZ, Hahn AF, O'Connell P, Wasmuth JJ: Mutations in the alpha 1 subunit of the inhibitory glycine receptor cause the dominant neurologic disorder, hyperekplexia. Nat Genet. 1993 Dec;5(4):351-8. [PubMed
]
- Langosch D, Laube B, Rundstrom N, Schmieden V, Bormann J, Betz H: Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia. EMBO J. 1994 Sep 15;13(18):4223-8. [PubMed
]
- Schorderet DF, Pescia G, Bernasconi A, Regli F: An additional family with Startle disease and a G1192A mutation at the alpha 1 subunit of the inhibitory glycine receptor gene. Hum Mol Genet. 1994 Jul;3(7):1201. [PubMed
]
- Rees MI, Andrew M, Jawad S, Owen MJ: Evidence for recessive as well as dominant forms of startle disease (hyperekplexia) caused by mutations in the alpha 1 subunit of the inhibitory glycine receptor. Hum Mol Genet. 1994 Dec;3(12):2175-9. [PubMed
]
- Shiang R, Ryan SG, Zhu YZ, Fielder TJ, Allen RJ, Fryer A, Yamashita S, O'Connell P, Wasmuth JJ: Mutational analysis of familial and sporadic hyperekplexia. Ann Neurol. 1995 Jul;38(1):85-91. [PubMed
]
- Milani N, Dalpra L, del Prete A, Zanini R, Larizza L: A novel mutation (Gln266-->His) in the alpha 1 subunit of the inhibitory glycine-receptor gene (GLRA1) in hereditary hyperekplexia. Am J Hum Genet. 1996 Feb;58(2):420-2. [PubMed
]
- Elmslie FV, Hutchings SM, Spencer V, Curtis A, Covanis T, Gardiner RM, Rees M: Analysis of GLRA1 in hereditary and sporadic hyperekplexia: a novel mutation in a family cosegregating for hyperekplexia and spastic paraparesis. J Med Genet. 1996 May;33(5):435-6. [PubMed
]
- Seri M, Bolino A, Galietta LJ, Lerone M, Silengo M, Romeo G: Startle disease in an Italian family by mutation (K276E): The alpha-subunit of the inhibiting glycine receptor. Hum Mutat. 1997;9(2):185-7. [PubMed
]
- Vergouwe MN, Tijssen MA, Peters AC, Wielaard R, Frants RR: Hyperekplexia phenotype due to compound heterozygosity for GLRA1 gene mutations. Ann Neurol. 1999 Oct;46(4):634-8. [PubMed
]
- Saul B, Kuner T, Sobetzko D, Brune W, Hanefeld F, Meinck HM, Becker CM: Novel GLRA1 missense mutation (P250T) in dominant hyperekplexia defines an intracellular determinant of glycine receptor channel gating. J Neurosci. 1999 Feb 1;19(3):869-77. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
15189 |
| Enzyme 9 Name |
GGT7 protein |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
GGT7 |
| Enzyme 9 Protein Sequence |
>GGT7 protein
MAAENEASQESALGAYSPVDYMSITSFPRLPEDEPAPAAPLRGRKDEDAFLGDPDTDPDS
FLKSARLQRLPSSSSEMGSQDGSPLRETRKDPFSAAAAECSCRQDGLTVIVTACLTFATG
VTVALVMQIYFGDPQIFQQGAVVTDAARCTSLGIEVLSKQGSSVDAAVAAALCLGIVAPH
SSGLGGGGVMLVHDIRRNESHLIDFRESAPGALREETLQRSWETKPGLLVGVPGMVKGLH
EAHQLYGRLPWSQVLAFAAAVAQDGFNVTHDLARALAEQLPPNMSERFRETFLPSGRPPL
PGSLLHRPDLAEVLDVLGTSGPAAFYAGGNLTLEMVAEAQHAGGVITEEDFSNYSALVEK
PVCGVYRGHLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVAETLKIALALAS
RLGDPVYDSTITESMDDMLSKVEAAYLRGHINDSQAAPAPLLPVYELDGAPTAAQVLIMG
PDDFIVAMVSSLNQPFGSGLITPSGILLNSQMLDFSWPNRTANHSAPSLENSVQPGKRPL
SFLLPTVVRPAEGLCGTYLALGANGAARGLSGLTQVLLNVLTLNRNLSDSLA
|
| Enzyme 9 Number of Residues |
592 |
| Enzyme 9 Molecular Weight |
62565.3 |
| Enzyme 9 Theoretical pI |
4.64 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- gamma-glutamyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in gamma-glutamyltransferase activity |
| Enzyme 9 Specific Function |
Not Available |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
118600847  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
A0PJJ9  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
A0PJJ9_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1777 bp
ATGGCGGCGGAGAACGAGGCCAGCCAGGAGAGCGCCCTGGGCGCCTACTCGCCAGTGGAC
TACATGAGCATCACCAGCTTCCCGCGGCTGCCCGAGGACGAGCCGGCGCCCGCGGCCCCG
CTGAGGGGCCGCAAGGACGAGGACGCCTTTCTGGGAGACCCCGACACCGACCCGGACTCC
TTCCTGAAGTCTGCACGGCTGCAGCGGCTGCCATCGTCGTCGTCGGAGATGGGCAGCCAA
GACGGGTCGCCGCTACGCGAGACGCGCAAAGACCCGTTCTCCGCCGCAGCGGCCGAGTGC
TCCTGCCGCCAGGATGGGCTCACGGTCATCGTCACGGCCTGTCTCACCTTCGCTACCGGT
GTCACCGTGGCGCTGGTCATGCAGATCTACTTCGGGGACCCCCAGATCTTCCAGCAGGGT
GCCGTGGTGACCGATGCTGCCCGCTGCACTTCACTGGGCATCGAGGTGCTCAGTAAACAG
GGATCTTCTGTGGACGCAGCGGTGGCAGCAGCCTTGTGTTTGGGTATCGTGGCTCCACAC
AGTTCTGGCCTGGGCGGTGGGGGCGTGATGCTGGTACATGACATCCGACGAAATGAGAGC
CACCTAATTGATTTCCGGGAGTCCGCACCAGGGGCCCTCAGGGAAGAGACCCTGCAAAGA
TCCTGGGAGACCAAGCCTGGGCTCTTGGTGGGGGTTCCCGGAATGGTGAAAGGGCTACAT
GAAGCTCACCAGCTCTATGGCAGGCTGCCATGGTCCCAAGTCCTGGCCTTTGCAGCAGCT
GTGGCCCAAGATGGCTTCAACGTGACTCATGATCTAGCCCGTGCCCTGGCTGAACAGCTG
CCACCCAACATGTCCGAGCGCTTCCGGGAGACGTTCCTGCCATCGGGCCGCCCGCCACTA
CCTGGCTCGTTGCTGCATCGGCCCGACCTGGCTGAGGTGCTGGATGTACTTGGCACCTCC
GGCCCGGCTGCCTTCTACGCAGGTGGCAACCTCACACTGGAGATGGTGGCCGAGGCTCAG
CACGCAGGGGGTGTCATAACCGAAGAGGACTTCAGCAATTACAGCGCCCTTGTGGAGAAG
CCTGTGTGTGGCGTGTACAGAGGCCACCTGGTTCTTAGTCCCCCACCTCCGCACACGGGC
CCTGCCCTCATCAGTGCTCTCAACATCCTGGAGGGCTTCAATCTCACCAGCCTGGTATCC
CGAGAACAGGCTCTTCACTGGGTGGCAGAGACCCTGAAGATTGCATTAGCCCTGGCCAGC
AGACTGGGAGATCCCGTCTATGATTCTACCATCACTGAGAGCATGGATGACATGCTCAGC
AAGGTGGAGGCCGCCTACCTCCGGGGCCATATCAATGACTCCCAGGCAGCCCCTGCCCCA
CTCCTGCCTGTCTATGAACTAGACGGAGCTCCCACGGCTGCCCAGGTGCTGATCATGGGA
CCTGATGACTTCATTGTGGCCATGGTTAGCTCCCTGAACCAGCCCTTTGGCAGCGGCCTT
ATCACCCCCTCGGGGATCCTGCTCAACAGCCAGATGCTGGACTTCTCCTGGCCCAACCGG
ACAGCTAACCACTCTGCACCCAGCCTGGAGAATTCAGTGCAGCCAGGGAAGCGGCCACTC
TCTTTCCTGCTGCCCACAGTGGTCCGACCCGCGGAGGGGCTCTGTGGAACCTACCTCGCT
CTGGGGGCCAATGGAGCTGCGCGGGGCCTCAGCGGCCTGACACAGGTTCTGCTGAATGTC
CTGACCTTGAACCGGAACCTGAGTGACAGCCTGGCCC
|
| Enzyme 9 GenBank Gene ID |
BC033745  |
| Enzyme 9 GeneCard ID |
GGT7  |
| Enzyme 9 GenAtlas ID |
GGT7  |
| Enzyme 9 HGNC ID |
HGNC:4259  |
| Enzyme 9 Chromosome Location |
2 |
| Enzyme 9 Locus |
20q11.22 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- 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
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
15190 |
| Enzyme 10 Name |
Gamma-glutamyltransferase 5 |
| Enzyme 10 Synonyms |
Not Available |
| Enzyme 10 Gene Name |
GGT5 |
| Enzyme 10 Protein Sequence |
>Gamma-glutamyltransferase 5
MARGYGATVSLVLLGLGLALAVIVLAVVLSRHQAPCGPQAFAHAAVAADSKVCSDIGRAI
LQQQGSPVDATIAALVCTSVVNPQSMGLGGGVIFTIYNVTTGKVEVINARETVPASHAPS
LLDQCAQALPLGTGAQWIGVPGELRGYAEAHRRHGRLPWAQLFQPTIALLRGGHVVAPVL
SRFLHNSILRPSLQASTLRQLFFNGTEPLRPQDPLPWPALATTLETVATEGVEVFYTGRL
GQMLVEDIAKEGSQLTLQDLAKFQPEVVDALEVPLGDYTLYSPPPPAGGAILSFILNVLR
GFNFSTESMARPEGRVNVYHHLVETLKFAKGQRWRLGDPRSHPKLQNASRDLLGETLAQL
IRQQIDGRGDHQLSHYSLAEAWGHGTGTSHVSVLGEDGSAVAATSTINTPFGAMVYSPRT
GIILNNELLDLCERCPRGSGTTPSPAVSGDRVGGAPGRCWPPVPGERSPSSMVPSILINK
AQGSKLVIGGAGGELIISAVAQAIMSKLWLGFDLRAAIAAPILHVNSKGCVEYEPNFSQE
VQRGLQDRGQNQTQRPFFLNVVQAVSQEGACVYAVSDLRKSGEAAGY
|
| Enzyme 10 Number of Residues |
587 |
| Enzyme 10 Molecular Weight |
62331.8 |
| Enzyme 10 Theoretical pI |
7.59 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- gamma-glutamyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in gamma-glutamyltransferase activity |
| Enzyme 10 Specific Function |
Not Available |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
49256405  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q6GMP0  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
Q6GMP0_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1764 bp
ATGGCCCGGGGCTACGGGGCCACGGTCAGCCTAGTCCTGCTGGGTCTGGGGCTGGCGCTG
GCTGTCATTGTGCTGGCTGTGGTCCTCTCTCGACACCAGGCCCCATGTGGCCCCCAGGCC
TTTGCCCACGCTGCTGTTGCCGCCGACTCCAAGGTCTGCTCGGATATTGGACGAGCCATC
CTCCAGCAGCAGGGCTCACCCGTGGATGCCACCATCGCGGCTCTGGTCTGCACCAGCGTC
GTCAACCCTCAGAGCATGGGCCTGGGCGGAGGGGTCATCTTCACCATCTACAATGTGACA
ACAGGGAAGGTGGAGGTCATCAATGCCCGGGAGACGGTGCCGGCCAGCCACGCCCCGAGC
CTGCTGGACCAGTGTGCACAGGCTCTGCCACTGGGCACAGGGGCCCAGTGGATCGGGGTG
CCCGGGGAGCTCCGTGGCTATGCCGAGGCCCACCGCCGCCATGGCCGCCTGCCCTGGGCG
CAGCTGTTCCAGCCCACCATCGCGCTGCTCCGAGGGGGGCATGTGGTGGCCCCTGTCCTC
AGCCGTTTCCTGCACAACAGCATCCTGCGGCCTTCCTTGCAGGCGTCAACCCTGCGCCAG
CTCTTCTTCAACGGGACAGAACCCCTGAGGCCTCAGGACCCACTCCCATGGCCTGCACTG
GCCACCACCCTGGAGACCGTGGCCACAGAGGGCGTGGAGGTCTTCTACACGGGGAGGCTG
GGCCAGATGCTGGTGGAGGACATTGCCAAGGAAGGGAGCCAGCTGACGCTGCAGGACCTG
GCCAAGTTCCAGCCCGAGGTGGTGGATGCCCTGGAGGTGCCCCTGGGGGACTATACCCTG
TACTCACCACCGCCGCCTGCAGGGGGTGCCATTCTCAGCTTTATCCTCAACGTGCTAAGA
GGGTTCAACTTCTCAACAGAGTCTATGGCCAGGCCTGAAGGGAGGGTGAACGTGTACCAC
CACCTTGTAGAGACGCTCAAGTTTGCCAAGGGGCAGAGGTGGAGGCTGGGGGACCCTCGA
AGCCACCCGAAGCTCCAGAATGCCTCCCGGGACCTGCTGGGGGAGACCCTGGCCCAGCTC
ATCCGCCAACAGATCGATGGCCGGGGGGACCACCAGCTCAGCCACTACAGCTTGGCCGAG
GCCTGGGGCCACGGGACAGGCACGTCCCATGTGTCTGTGCTGGGGGAGGATGGCAGCGCC
GTGGCTGCCACCAGCACCATCAACACACCCTTTGGAGCGATGGTGTATTCACCACGGACA
GGCATCATCCTCAACAACGAGCTCCTGGACTTATGCGAGCGATGCCCCCGGGGTTCCGGC
ACCACCCCCTCACCTGCAGTGAGTGGAGACAGGGTGGGTGGAGCTCCCGGAAGGTGCTGG
CCCCCAGTTCCAGGCGAGCGTTCCCCATCCTCCATGGTGCCCTCCATCTTGATCAACAAA
GCCCAGGGGTCGAAGCTAGTGATTGGCGGGGCTGGCGGGGAGCTCATCATCTCTGCTGTG
GCCCAGGCCATCATGAGCAAGCTGTGGCTTGGCTTTGACCTGAGAGCGGCCATTGCAGCC
CCCATCCTGCATGTCAACAGCAAGGGCTGTGTGGAGTACGAGCCCAACTTCAGCCAGGAG
GTGCAGAGGGGACTCCAAGACCGTGGCCAGAACCAGACCCAGAGGCCCTTCTTCCTGAAC
GTGGTCCAGGCTGTGTCCCAGGAGGGGGCCTGTGTGTACGCCGTCTCGGACCTGAGGAAG
AGTGGGGAGGCCGCAGGCTACTAA
|
| Enzyme 10 GenBank Gene ID |
BC073999  |
| Enzyme 10 GeneCard ID |
GGT5  |
| Enzyme 10 GenAtlas ID |
GGT5  |
| Enzyme 10 HGNC ID |
HGNC:4260  |
| Enzyme 10 Chromosome Location |
2 |
| Enzyme 10 Locus |
22q11.23 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- 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
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
17008 |
| Enzyme 11 Name |
Transporter |
| Enzyme 11 Synonyms |
Not Available |
| Enzyme 11 Gene Name |
SLC6A6 |
| Enzyme 11 Protein Sequence |
>Transporter
MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVG
LGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEIIIGQYTSEGGITCWEKICPLF
SGIGYASVVIVSLLNVYYIVILAWATYYLFQSFQKELPWAHCNHSWNTPHCMEDTMRKNK
SVWITISSTNFTSPVIEFWE
|
| Enzyme 11 Number of Residues |
200 |
| Enzyme 11 Molecular Weight |
22744.2 |
| Enzyme 11 Theoretical pI |
7.80 |
| Enzyme 11 GO Classification |
| Function |
- neurotransmitter transporter activity
- neurotransmitter:sodium symporter activity
- taurine:sodium symporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- establishment of localization
- neurotransmitter transport
- transport
|
| Component |
- cell part
- integral to membrane
- integral to plasma membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 11 General Function |
Involved in neurotransmitter:sodium symporter activity |
| Enzyme 11 Specific Function |
Not Available |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
13623303  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9BRI2  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
Q9BRI2_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>603 bp
ATGGCCACCAAGGAGAAGCTGCAGTGTCTGAAAGATTTCCACAAGGACATCCTGAAGCCC
TCACCAGGGAAGAGCCCAGGCACGCGGCCTGAGGACGAGGCTGAGGGAAAACCTCCGCAG
AGGGAGAAGTGGTCTAGCAAGATCGACTTTGTGCTCTCTGTGGCTGGCGGCTTCGTGGGC
TTGGGCAACGTCTGGCGCTTCCCGTACCTCTGCTACAAGAATGGTGGAGGTGCGTTTCTC
ATACCGTATTTTATTTTCCTGTTTGGGAGCGGCCTGCCTGTGTTTTTCTTGGAGATCATC
ATAGGCCAGTACACCTCTGAAGGGGGCATCACCTGCTGGGAAAAGATCTGCCCCTTGTTC
TCTGGTATCGGCTATGCCTCCGTTGTAATTGTGTCCCTCCTGAATGTCTACTACATCGTC
ATCCTGGCCTGGGCCACATACTACCTGTTCCAGTCCTTCCAGAAGGAGCTGCCCTGGGCA
CACTGCAACCACAGCTGGAACACACCTCACTGCATGGAGGACACCATGCGCAAGAACAAG
AGTGTCTGGATCACCATCAGCTCCACCAACTTCACCTCCCCTGTCATCGAGTTCTGGGAG
TAA
|
| Enzyme 11 GenBank Gene ID |
BC006252  |
| Enzyme 11 GeneCard ID |
SLC6A6  |
| Enzyme 11 GenAtlas ID |
SLC6A6  |
| Enzyme 11 HGNC ID |
HGNC:11052  |
| Enzyme 11 Chromosome Location |
3 |
| Enzyme 11 Locus |
3p25-p24 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- 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
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
17009 |
| Enzyme 12 Name |
Transporter |
| Enzyme 12 Synonyms |
Not Available |
| Enzyme 12 Gene Name |
SLC6A6 |
| Enzyme 12 Protein Sequence |
>Transporter
MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVG
LGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEIIIGQYTSEGGITCWEKICPLF
SGIGYASVVIVSLLNVYYIVILAWATYYLFQSFQKELPWAHCNHSWNTPHCMEDTMRKNK
SVWITISSTNFTSPVIEFWERNVLSLSPGIDHPGSLKWDLALCLLLVWLVCFFCIWKGVR
STGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDITRLEDPQVWIDAGTQIFF
SYAICLGAMTSLGSYNKYKYNSYRDCMLLGCLNSGTSFVSGFAIFSILGFMAQEQGVDIA
DVAESGPGLAFIAYPKAVTMMPLPTFWSILFFIMLLLLGLDSQFVEVEGQITSLVDLYPS
FLRKGYRREIFIAFVCSISYLLGLTMVTEGGMYVFQLFDYYAASGVCLLWVAFFECFVIA
WIYGGDNLYDGIEDMIGYRPGPWMKYSWAVITPVLCVGCFIFSLVKYVPLTYNKTYVYPN
WAIGLGWSLALSSMLCVPLVIVIRLCQTEGPFLVRVKYLLTPREPNRWAVEREGATPYNS
RTVMNGALVKPTHIIVETMM
|
| Enzyme 12 Number of Residues |
620 |
| Enzyme 12 Molecular Weight |
69829.4 |
| Enzyme 12 Theoretical pI |
7.43 |
| Enzyme 12 GO Classification |
| Function |
- neurotransmitter transporter activity
- neurotransmitter:sodium symporter activity
- taurine:sodium symporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- establishment of localization
- neurotransmitter transport
- transport
|
| Component |
- cell part
- integral to membrane
- integral to plasma membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 12 General Function |
Involved in neurotransmitter:sodium symporter activity |
| Enzyme 12 Specific Function |
Not Available |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
Not Available |
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
187952517  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
B2RNU7  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
B2RNU7_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1863 bp
ATGGCCACCAAGGAGAAGCTGCAGTGTCTGAAAGATTTCCACAAGGACATCCTGAAGCCC
TCACCAGGGAAGAGCCCAGGCACGCGGCCTGAGGACGAGGCTGAGGGAAAACCTCCGCAG
AGGGAGAAGTGGTCTAGCAAGATCGACTTTGTGCTCTCTGTGGCTGGCGGCTTCGTGGGC
TTGGGCAACGTCTGGCGCTTCCCGTACCTCTGCTACAAGAATGGTGGAGGTGCGTTTCTC
ATACCGTATTTTATTTTCCTGTTTGGGAGCGGCCTGCCTGTGTTTTTCTTGGAGATCATC
ATAGGCCAGTACACCTCTGAAGGGGGCATCACCTGCTGGGAAAAGATCTGCCCCTTGTTC
TCTGGTATCGGCTATGCCTCCGTTGTAATTGTGTCCCTCCTGAATGTCTACTACATCGTC
ATCCTGGCCTGGGCCACATACTACCTGTTCCAGTCCTTCCAGAAGGAGCTGCCCTGGGCA
CACTGCAACCACAGCTGGAACACACCTCACTGCATGGAGGACACCATGCGCAAGAACAAG
AGTGTCTGGATCACCATCAGCTCCACCAACTTCACCTCCCCTGTCATCGAGTTCTGGGAG
CGCAACGTGCTGAGCTTGTCCCCTGGAATCGACCACCCAGGCTCTCTGAAATGGGACCTC
GCTCTCTGCCTTCTTTTAGTCTGGCTAGTGTGTTTCTTCTGCATCTGGAAGGGCGTCAGG
TCCACTGGGAAGGTCGTCTACTTCACAGCCACTTTTCCATTCGCCATGCTCCTGGTGCTG
CTGGTCCGAGGGCTGACGCTGCCGGGCGCGGGCGCAGGCATCAAGTTCTATCTGTATCCT
GACATCACCCGCCTTGAGGACCCACAGGTGTGGATTGACGCTGGGACTCAGATATTCTTC
TCTTATGCCATCTGCCTGGGGGCTATGACCTCGCTGGGGAGCTACAACAAGTACAAGTAT
AACTCGTACAGGGACTGTATGCTGCTGGGATGCCTGAACAGTGGTACCAGTTTTGTGTCT
GGCTTCGCAATTTTTTCCATCCTGGGCTTCATGGCACAAGAGCAAGGGGTGGACATTGCT
GATGTGGCTGAGTCAGGTCCTGGCCTGGCCTTCATTGCCTACCCAAAAGCTGTGACAATG
ATGCCGCTGCCCACATTTTGGTCCATTCTTTTTTTTATTATGCTTCTCTTGCTTGGACTG
GATAGCCAGTTTGTTGAAGTTGAAGGACAGATCACATCCTTGGTTGATCTTTACCCATCC
TTCCTAAGGAAGGGTTATCGTCGGGAAATCTTCATCGCCTTCGTGTGTAGCATCAGCTAC
CTGCTGGGGCTGACGATGGTGACGGAGGGTGGCATGTATGTGTTTCAGCTCTTTGACTAC
TATGCAGCTAGCGGTGTATGCCTTTTGTGGGTTGCATTCTTTGAATGTTTTGTTATTGCC
TGGATATATGGAGGTGATAACCTTTATGATGGTATTGAGGACATGATTGGCTATCGGCCC
GGGCCCTGGATGAAGTACAGCTGGGCTGTGATCACTCCAGTTCTCTGTGTTGGATGTTTC
ATCTTCTCGCTCGTCAAGTACGTACCCCTGACCTACAACAAAACATACGTGTACCCCAAC
TGGGCCATTGGGCTGGGCTGGAGCCTGGCCCTTTCCTCCATGCTCTGCGTTCCCTTGGTC
ATCGTCATCCGCCTCTGCCAGACTGAGGGGCCGTTCCTTGTGAGAGTCAAGTACCTGCTG
ACCCCAAGGGAACCCAACCGCTGGGCTGTGGAGCGCGAGGGAGCCACACCTTACAACTCT
CGCACCGTCATGAACGGCGCTCTCGTGAAACCGACCCACATCATTGTGGAGACCATGATG
TGA
|
| Enzyme 12 GenBank Gene ID |
BC137128  |
| Enzyme 12 GeneCard ID |
SLC6A6  |
| Enzyme 12 GenAtlas ID |
SLC6A6  |
| Enzyme 12 HGNC ID |
HGNC:11052  |
| Enzyme 12 Chromosome Location |
3 |
| Enzyme 12 Locus |
3p25-p24 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- 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
]
- 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
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
17010 |
| Enzyme 13 Name |
Transporter |
| Enzyme 13 Synonyms |
Not Available |
| Enzyme 13 Gene Name |
Not Available |
| Enzyme 13 Protein Sequence |
>Transporter
MATKEKLQCLKDFHKDILKPSPGKSPGTRPEDEAEGKPPQREKWSSKIDFVLSVAGGFVG
LGNVWRFPYLCYKNGGGAFLIPYFIFLFGSGLPVFFLEIIIGQYTSEGGITCWEKICPLF
SGIGYASVVIVSLLNVYYIVILAWATYYLFQSFQKELPWAHCNHSWNTPHCMEDTMRKNK
SVWITISSTNFTSPVIEFWGRNVLSLSPVIDHPGSLKWDLALCLLLVWLVCFFCIWKGVR
STGKVVYFTATFPFAMLLVLLVRGLTLPGAGAGIKFYLYPDITRLEDPQVWIDAGTQIFF
SYAICLGAMTSLGSYNKYKYNSYRSWPGLHCLPKSCDNDAAAHILVHSFFYYASLAWTG
|
| Enzyme 13 Number of Residues |
359 |
| Enzyme 13 Molecular Weight |
40485.8 |
| Enzyme 13 Theoretical pI |
8.39 |
| Enzyme 13 GO Classification |
| Function |
- neurotransmitter transporter activity
- neurotransmitter:sodium symporter activity
- taurine:sodium symporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- establishment of localization
- neurotransmitter transport
- transport
|
| Component |
- cell part
- integral to membrane
- integral to plasma membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 13 General Function |
Involved in neurotransmitter:sodium symporter activity |
| Enzyme 13 Specific Function |
Not Available |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
194383362  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
B4E140  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
B4E140_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1080 bp
ATGGCCACCAAGGAGAAGCTGCAGTGTCTGAAAGATTTCCACAAGGACATCCTGAAGCCC
TCACCAGGGAAGAGCCCAGGCACGCGGCCTGAGGACGAGGCTGAGGGAAAACCTCCGCAG
AGGGAGAAGTGGTCTAGCAAGATCGACTTTGTGCTCTCTGTGGCTGGCGGCTTCGTGGGC
TTGGGCAACGTCTGGCGCTTCCCGTACCTCTGCTACAAGAATGGTGGAGGTGCGTTTCTC
ATACCGTATTTTATTTTCCTGTTTGGGAGCGGCCTGCCTGTGTTTTTCTTGGAGATCATC
ATAGGCCAGTACACCTCTGAAGGGGGCATCACCTGTTGGGAAAAGATCTGCCCCTTGTTC
TCTGGTATCGGCTATGCCTCCGTTGTAATTGTGTCCCTCCTGAATGTCTACTACATCGTC
ATCCTGGCCTGGGCCACATACTACCTGTTCCAGTCCTTCCAGAAGGAGCTGCCCTGGGCA
CACTGCAACCACAGCTGGAACACACCTCACTGCATGGAGGACACCATGCGCAAGAACAAG
AGTGTCTGGATCACCATCAGCTCCACCAACTTCACCTCCCCTGTCATCGAGTTCTGGGGG
CGCAACGTGCTGAGCTTGTCCCCTGTAATCGACCACCCAGGCTCTCTGAAATGGGACCTC
GCTCTCTGCCTTCTTTTAGTCTGGCTAGTGTGTTTCTTCTGCATCTGGAAGGGCGTCAGG
TCCACTGGGAAGGTCGTCTACTTCACAGCCACTTTTCCATTCGCCATGCTCCTGGTGCTG
CTGGTCCGAGGGCTGACGCTGCCGGGCGCGGGCGCAGGCATCAAGTTCTATCTGTATCCT
GACATCACCCGCCTTGAGGACCCACAGGTGTGGATTGACGCTGGGACTCAGATATTCTTC
TCTTATGCCATCTGCCTGGGGGCTATGACCTCGCTGGGGAGCTACAACAAGTACAAGTAT
AACTCGTACAGGTCCTGGCCTGGCCTTCATTGCCTACCCAAAAGCTGTGACAATGATGCC
GCTGCCCACATTTTGGTCCATTCTTTTTTTTATTATGCTTCTCTTGCTTGGACTGGATAG
|
| Enzyme 13 GenBank Gene ID |
AK303649  |
| Enzyme 13 GeneCard ID |
Not Available |
| Enzyme 13 GenAtlas ID |
Not Available |
| Enzyme 13 HGNC ID |
HGNC:11052  |
| Enzyme 13 Chromosome Location |
Not Available |
| Enzyme 13 Locus |
Not Available |
| Enzyme 13 SNPs |
Not Available |
| Enzyme 13 General References |
Not Available |
| Enzyme 13 Metabolite References |
Not Available |