|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5303 |
| Enzyme 1 Name |
Aldo-keto reductase family 1 member C4 |
| Enzyme 1 Synonyms |
- Chlordecone reductase
- CDR
- 3-alpha-hydroxysteroid dehydrogenase type I
- 3-alpha-HSD1
- Dihydrodiol dehydrogenase 4
- DD4
- HAKRA
|
| Enzyme 1 Gene Name |
AKR1C4 |
| Enzyme 1 Protein Sequence |
>Aldo-keto reductase family 1 member C4
MDPKYQRVELNDGHFMPVLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPM
ALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEMILNKP
GLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLN
RNYRYVVMDFLMDHPDYPFSDEY
|
| Enzyme 1 Number of Residues |
323 |
| Enzyme 1 Molecular Weight |
37095 |
| Enzyme 1 Theoretical pI |
7.19 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Not Available |
| Enzyme 1 Specific Function |
Catalyzes the transformation of the potent androgen dihydrotestosterone (DHT) into the less active form, 5-alpha- androstan-3alpha,17beta-diol (3-alpha-diol). Also has some 20- alpha-hydroxysteroid dehydrogenase activity. The biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leads to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route |
| Enzyme 1 Pathways |
- Androgen and Estrogen Metabolism (map00150
)
- Bile Acid Biosynthesis (map00120
)
- C21 Steroid Hormone Metabolism (map00140
)
|
| Enzyme 1 Reactions |
- chlordecone alcohol + NADP+ = chlordecone + NADPH + H+
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
4261710  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P17516  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
AK1C4_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>972 bp
ATGGATCCCAAATATCAGCGTGTAGAGCTAAATGATGGTCATTTCATGCCCGTATTGGGA
TTTGGCACCTATGCACCTCCAGAGGTTCCGAGGAACAGAGCTGTAGAGGTCACCAAATTA
GCAATAGAAGCTGGCTTCCGCCATATTGATTCTGCTTATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTGCACTTTCTTTCAACCACAGATGGTCCAACCAGCCTTGGAA
AGCTCACTGAAAAAACTTCAACTGGACTATGTTGACCTCTATCTTCTTCATTTCCCAATG
GCTCTCAAGCCAGGTGAGACGCCACTACCAAAAGATGAAAATGGAAAAGTAATATTCGAC
ACAGTGGATCTCTCTGCCACATGGGAGGTCATGGAGAAGTGTAAGGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCAAACTTCAACTGCAGGCAGCTGGAGATGATCCTCAACAAGCCA
GGACTCAAGTACAAGCCTGTCTGCAACCAGGTAGAATGTCATCCTTACCTCAACCAGAGC
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCCACAGTGCTCTGGGA
ACCCAACGACATAAACTATGGGTGGACCCAAACTCCCCAGTTCTTTTGGAGGACCCAGTT
CTTTGTGCCTTAGCAAAGAAACACAAACGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGGATCAGAGAGAAC
ATCCAGGTTTTTGAATTCCAGTTGACATCAGAGGATATGAAAGTTCTAGATGGTCTAAAC
AGAAATTATCGATATGTTGTCATGGATTTTCTTATGGACCATCCTGATTATCCATTTTCA
GATGAATATTAG
|
| Enzyme 1 GenBank Gene ID |
S68287  |
| Enzyme 1 GeneCard ID |
AKR1C4  |
| Enzyme 1 GenAtlas ID |
AKR1C4  |
| Enzyme 1 HGNC ID |
HGNC:387  |
| Enzyme 1 Chromosome Location |
10 |
| Enzyme 1 Locus |
10p15-p14 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed
]
- Khanna M, Qin KN, Wang RW, Cheng KC: Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. J Biol Chem. 1995 Aug 25;270(34):20162-8. [PubMed
]
- Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed
]
- Kume T, Iwasa H, Shiraishi H, Yokoi T, Nagashima K, Otsuka M, Terada T, Takagi T, Hara A, Kamataki T: Characterization of a novel variant (S145C/L311V) of 3alpha-hydroxysteroid/dihydrodiol dehydrogenase in human liver. Pharmacogenetics. 1999 Dec;9(6):763-71. [PubMed
]
- Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed
]
- Dufort I, Labrie F, Luu-The V: Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution. J Clin Endocrinol Metab. 2001 Feb;86(2):841-6. [PubMed
]
- Winters CJ, Molowa DT, Guzelian PS: Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase. Biochemistry. 1990 Jan 30;29(4):1080-7. [PubMed
]
- Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A: Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem J. 1994 Apr 15;299 ( Pt 2):545-52. [PubMed
]
- Binstock JM, Iyer RB, Hamby CV, Fried VA, Schwartz IS, Weinstein BI, Southren AL: Human hepatic 3 alpha-hydroxysteroid dehydrogenase: possible identity with human hepatic chlordecone reductase. Biochem Biophys Res Commun. 1992 Sep 16;187(2):760-6. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5583 |
| Enzyme 2 Name |
Bile salt sulfotransferase |
| Enzyme 2 Synonyms |
- Hydroxysteroid Sulfotransferase
- HST
- Dehydroepiandrosterone sulfotransferase
- DHEA-ST
- ST2
- ST2A3
|
| Enzyme 2 Gene Name |
SULT2A1 |
| Enzyme 2 Protein Sequence |
>Bile salt sulfotransferase
MSDDFLWFEGIAFPTMGFRSETLRKVRDEFVIRDEDVIILTYPKSGTNWLAEILCLMHSK
GDAKWIQSVPIWERSPWVESEIGYTALSETESPRLFSSHLPIQLFPKSFFSSKAKVIYLM
RNPRDVLVSGYFFWKNMKFIKKPKSWEEYFEWFCQGTVLYGSWFDHIHGWMPMREEKNFL
LLSYEELKQDTGRTIEKICQFLGKTLEPEELNLILKNSSFQSMKENKMSNYSLLSVDYVV
DKAQLLRKGVSGDWKNHFTVAQAEDFDKLFQEKMADLPRELFPWE
|
| Enzyme 2 Number of Residues |
285 |
| Enzyme 2 Molecular Weight |
33780 |
| Enzyme 2 Theoretical pI |
5.76 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- sulfotransferase activity
- transferase activity
- transferase activity, transferring sulfur-containing groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 2 General Function |
Not Available |
| Enzyme 2 Specific Function |
Catalyzes the sulfation of steroids and bile acids in the liver and adrenal glands |
| Enzyme 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
- 3'-phosphoadenylyl sulfate + taurolithocholate = adenosine 3',5'-bisphosphate + taurolithocholate sulfate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
306702  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q06520  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
ST2A1_HUMAN  |
| Enzyme 2 PDB ID |
1OV4  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>858 bp
ATGTCGGACGATTTCTTATGGTTTGAAGGCATAGCTTTCCCTACTATGGGTTTCAGATCC
GAAACCTTAAGAAAAGTACGTGATGAGTTCGTGATAAGGGATGAAGATGTAATAATATTG
ACTTACCCCAAATCAGGAACAAACTGGTTGGCTGAGATTCTCTGCCTGATGCACTCCAAG
GGGGATGCCAAGTGGATCCAATCTGTGCCCATCTGGGAGCGATCACCCTGGGTAGAGAGT
GAGATTGGGTATACAGCACTCAGTGAAAGCGAGAGTCCACGTTTATTCTCCTCCCACCTC
CCCATCCAGTTATTCCCCAAGTCTTTCTTCAGTTCCAAGGCCAAGGTGATTTATCTCATG
AGAAATCCCAGAGATGTTTTGGTGTCTGGTTATTTTTTCTGGAAAAACATGAAGTTTATT
AAGAAACCAAAGTCATGGGAAGAATATTTTGAATGGTTTTGTCAAGGAACTGTGCTATAT
GGGTCATGGTTTGACCACATTCATGGCTGGATGCCCATGAGAGAGGAGAAAAACTTCCTG
TTACTGAGTTATGAGGAGCTGAAACAGGACACAGGAAGAACCATAGAGAAGATCTGTCAA
TTCCTGGGAAAGACGTTAGAACCCGAAGAACTGAACTTAATTCTCAAGAACAGCTCCTTT
CAGAGCATGAAAGAAAACAAGATGTCCAATTATTCCCTCCTGAGTGTTGATTATGTAGTG
GACAAAGCACAACTTCTGAGAAAAGGTGTATCTGGGGACTGGAAAAATCACTTCACAGTG
GCCCAAGCTGAAGACTTTGATAAATTGTTCCAAGAGAAGATGGCAGATCTTCCTCGAGAG
CTGTTCCCATGGGAATAA
|
| Enzyme 2 GenBank Gene ID |
L20000  |
| Enzyme 2 GeneCard ID |
SULT2A1  |
| Enzyme 2 GenAtlas ID |
SULT2A1  |
| Enzyme 2 HGNC ID |
HGNC:11458  |
| Enzyme 2 Chromosome Location |
19 |
| Enzyme 2 Locus |
19q13.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Comer KA, Falany JL, Falany CN: Cloning and expression of human liver dehydroepiandrosterone sulphotransferase. Biochem J. 1993 Jan 1;289 ( Pt 1):233-40. [PubMed
]
- Otterness DM, Wieben ED, Wood TC, Watson WG, Madden BJ, McCormick DJ, Weinshilboum RM: Human liver dehydroepiandrosterone sulfotransferase: molecular cloning and expression of cDNA. Mol Pharmacol. 1992 May;41(5):865-72. [PubMed
]
- Forbes KJ, Hagen M, Glatt H, Hume R, Coughtrie MW: Human fetal adrenal hydroxysteroid sulphotransferase: cDNA cloning, stable expression in V79 cells and functional characterisation of the expressed enzyme. Mol Cell Endocrinol. 1995 Jul;112(1):53-60. [PubMed
]
- Luu-The V, Dufort I, Paquet N, Reimnitz G, Labrie F: Structural characterization and expression of the human dehydroepiandrosterone sulfotransferase gene. DNA Cell Biol. 1995 Jun;14(6):511-8. [PubMed
]
- Otterness DM, Her C, Aksoy S, Kimura S, Wieben ED, Weinshilboum RM: Human dehydroepiandrosterone sulfotransferase gene: molecular cloning and structural characterization. DNA Cell Biol. 1995 Apr;14(4):331-41. [PubMed
]
- Kong AN, Yang L, Ma M, Tao D, Bjornsson TD: Molecular cloning of the alcohol/hydroxysteroid form (hSTa) of sulfotransferase from human liver. Biochem Biophys Res Commun. 1992 Aug 31;187(1):448-54. [PubMed
]
|
| Enzyme 2 Metabolite References |
- Chang HJ, Shi R, Rehse P, Lin SX: Identifying androsterone (ADT) as a cognate substrate for human dehydroepiandrosterone sulfotransferase (DHEA-ST) important for steroid homeostasis: structure of the enzyme-ADT complex. J Biol Chem. 2004 Jan 23;279(4):2689-96. Epub 2003 Oct 21. [PubMed
]
|
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5596 |
| Enzyme 3 Name |
Aldo-keto reductase family 1 member C3 |
| Enzyme 3 Synonyms |
- Trans-1,2- dihydrobenzene-1,2-diol dehydrogenase
- 3-alpha- hydroxysteroid dehydrogenase type 2
- 3-alpha-HSD type 2
- 3-alpha-HSD type II, brain
- Prostaglandin F synthase
- PGFS
- Estradiol 17-beta-dehydrogenase
- 17-beta-hydroxysteroid dehydrogenase type 5
- 17-beta-HSD 5
- Chlordecone reductase homolog HAKRb
- HA1753
- Dihydrodiol dehydrogenase type I
- Dihydrodiol dehydrogenase 3
- DD3
- DD-3
|
| Enzyme 3 Gene Name |
AKR1C3 |
| Enzyme 3 Protein Sequence |
>Aldo-keto reductase family 1 member C3
MDSKQQCVKLNDGHFMPVLGFGTYAPPEVPRSKALEVTKLAIEAGFRHIDSAHLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWSTFHRPELVRPALENSLKKAQLDYVDLYLIHSPM
SLKPGEELSPTDENGKVIFDIVDLCTTWEAMEKCKDAGLAKSIGVSNFNRRQLEMILNKP
GLKYKPVCNQVECHPYFNRSKLLDFCKSKDIVLVAYSALGSQRDKRWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTAEDMKAIDGLD
RNLHYFNSDSFASHPNYPYSDEY
|
| Enzyme 3 Number of Residues |
323 |
| Enzyme 3 Molecular Weight |
36845 |
| Enzyme 3 Theoretical pI |
8.06 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 Specific Function |
Catalyzes the conversion of aldehydes and ketones to alcohols. Catalyzes the reduction of prostaglandin (PG) D2, PGH2 and phenanthrenequinone (PQ) and the oxidation of 9alpha,11beta- PGF2 to PGD2. Functions as a bi-directional 3alpha-, 17beta- and 20alpha HSD. Can interconvert active androgens, estrogens and progestins with their cognate inactive metabolites. Preferentially transforms androstenedione (4-dione) to testosterone |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
4261711  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P42330  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
AK1C3_HUMAN  |
| Enzyme 3 PDB ID |
1XF0  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>972 bp
ATGGATTCCAAACAGCAGTGTGTAAAGCTAAATGATGGCCACTTCATGCCTGTATTGGGA
TTTGGCACCTATGCACCTCCAGAGGTTCCGAGAAGTAAAGCTTTGGAGGTCACAAAATTA
GCAATAGAAGCTGGGTTCCGCCATATAGATTCTGCTCATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTTGAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTCCACTTTTCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AACTCACTGAAGAAAGCTCAATTGGACTATGTTGACCTCTATCTTATTCATTCTCCAATG
TCTCTAAAGCCAGGTGAGGAACTTTCACCAACAGATGAAAATGGAAAAGTAATATTTGAC
ATAGTGGATCTCTGTACCACCTGGGAGGCCATGGAGAAGTGTAAGGATGCAGGATTGGCC
AAGTCCATTGGGGTATCAAACTTCAACCGCAGGCAGCTGGAGATCATCCTCAACAAGCCA
GGACTCAAGTACAAGCCTGTCTGCAACCAGGTAGAATGTCATCCGTATTTCAACCGGAGT
AAATTGCTAGATTTCTGCAAGTCGAAAGATATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCTCAACGAGACAAACGATGGGTGGACCCGAACTCCCCGGTCCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTTTTTGAGTTCCAGTTGACTGCAGAGGACATGAAAGCCATAGATGGCCTAGAC
AGAAATCTCCACTATTTTAACAGTGATAGTTTTGCTAGCCACCCTAATTATCCATATTCA
GATGAATATTAA
|
| Enzyme 3 GenBank Gene ID |
S68288  |
| Enzyme 3 GeneCard ID |
AKR1C3  |
| Enzyme 3 GenAtlas ID |
AKR1C3  |
| Enzyme 3 HGNC ID |
HGNC:386  |
| Enzyme 3 Chromosome Location |
10 |
| Enzyme 3 Locus |
10p15-p14 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed
]
- Khanna M, Qin KN, Wang RW, Cheng KC: Substrate specificity, gene structure, and tissue-specific distribution of multiple human 3 alpha-hydroxysteroid dehydrogenases. J Biol Chem. 1995 Aug 25;270(34):20162-8. [PubMed
]
- Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed
]
- Lin HK, Jez JM, Schlegel BP, Peehl DM, Pachter JA, Penning TM: Expression and characterization of recombinant type 2 3 alpha-hydroxysteroid dehydrogenase (HSD) from human prostate: demonstration of bifunctional 3 alpha/17 beta-HSD activity and cellular distribution. Mol Endocrinol. 1997 Dec;11(13):1971-84. [PubMed
]
- Suzuki-Yamamoto T, Nishizawa M, Fukui M, Okuda-Ashitaka E, Nakajima T, Ito S, Watanabe K: cDNA cloning, expression and characterization of human prostaglandin F synthase. FEBS Lett. 1999 Dec 3;462(3):335-40. [PubMed
]
- Griffin LD, Mellon SH: Selective serotonin reuptake inhibitors directly alter activity of neurosteroidogenic enzymes. Proc Natl Acad Sci U S A. 1999 Nov 9;96(23):13512-7. [PubMed
]
- Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed
]
- Penning TM, Burczynski ME, Jez JM, Lin HK, Ma H, Moore M, Ratnam K, Palackal N: Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3). Mol Cell Endocrinol. 2001 Jan 22;171(1-2):137-49. [PubMed
]
- Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al.: Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995;2(1):37-43. [PubMed
]
- Dufort I, Rheault P, Huang XF, Soucy P, Luu-The V: Characteristics of a highly labile human type 5 17beta-hydroxysteroid dehydrogenase. Endocrinology. 1999 Feb;140(2):568-74. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5623 |
| Enzyme 4 Name |
Aldo-keto reductase family 1 member C1 |
| Enzyme 4 Synonyms |
- 20-alpha- hydroxysteroid dehydrogenase
- 20-alpha-HSD
- Trans- 1,2-dihydrobenzene-1,2-diol dehydrogenase
- High- affinity hepatic bile acid-binding protein
- HBAB
- Chlordecone reductase homolog HAKRC
- Dihydrodiol dehydrogenase 1/2
- DD1/DD2
|
| Enzyme 4 Gene Name |
AKR1C1 |
| Enzyme 4 Protein Sequence |
>Aldo-keto reductase family 1 member C1
MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEATKLAIEAGFRHIDSAHLYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWCNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV
SVKPGEEVIPKDENGKILFDTVDLCATWEAVEKCKDAGLAKSIGVSNFNRRQLEMILNKP
GLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN
RNVRYLTLDIFAGPPNYPFSDEY
|
| Enzyme 4 Number of Residues |
323 |
| Enzyme 4 Molecular Weight |
36789 |
| Enzyme 4 Theoretical pI |
7.99 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
Converts progesterone to its inactive form, 20alpha- dihydroxyprogesterone (20alpha-OHP). In the liver and intestine, may have a role in the transport of bile. May have a role in monitoring the intrahepatic bile acid concentration. May play a role in myelin formation |
| Enzyme 4 Pathways |
- C21 Steroid Hormone Metabolism (map00140
)
|
| Enzyme 4 Reactions |
- trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
181549  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q04828  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
AK1C1_HUMAN  |
| Enzyme 4 PDB ID |
1MRQ  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>972 bp
ATGGATTCGAAATATCAGTGTGTGAAGCTGAATGATGGTCACTTCATGCCTGTCCTGGGA
TTTGGCACCTATGCGCCTGCAGAGGTTCCTAAAAGTAAAGCTTTAGAGGCCACCAAATTG
GCAATTGAAGCTGGCTTCCGCCATATTGATTCTGCTCATTTATACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGTGCAATTCCCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AGGTCACTGAAAAATCTTCAATTGGATTATGTTGACCTCTACCTTATTCATTTTCCAGTG
TCTGTAAAGCCAGGTGAGGAAGTGATCCCAAAAGATGAAAATGGAAAAATACTATTTGAC
ACAGTGGATCTCTGTGCCACGTGGGAGGCCGTGGAGAAGTGTAAAGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCCAACTTCAACCGCAGGCAGCTGGAGATGATCCTCAACAAGCCA
GGGCTCAAGTACAAGCCTGTCTGCAACCAGGTGGAATGTCATCCTTACTTCAACCAGAGA
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCCCACCGAGAAGAACCATGGGTGGACCCGAACTCCCCGGTGCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTACAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTGTTTGAATTCCAGTTGACTTCAGAGGAGATGAAAGCCATAGATGGCCTAAAC
AGAAATGTGCGATATTTGACCCTTGATATTTTTGCTGGCCCCCCTAATTATCCATTTTCT
GATGAATATTAA
|
| Enzyme 4 GenBank Gene ID |
M86609  |
| Enzyme 4 GeneCard ID |
AKR1C1  |
| Enzyme 4 GenAtlas ID |
AKR1C1  |
| Enzyme 4 HGNC ID |
HGNC:384  |
| Enzyme 4 Chromosome Location |
10 |
| Enzyme 4 Locus |
10p15-p14 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Stolz A, Hammond L, Lou H, Takikawa H, Ronk M, Shively JE: cDNA cloning and expression of the human hepatic bile acid-binding protein. A member of the monomeric reductase gene family. J Biol Chem. 1993 May 15;268(14):10448-57. [PubMed
]
- Lou H, Hammond L, Sharma V, Sparkes RS, Lusis AJ, Stolz A: Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding. J Biol Chem. 1994 Mar 18;269(11):8416-22. [PubMed
]
- Khanna M, Qin KN, Cheng KC: Distribution of 3 alpha-hydroxysteroid dehydrogenase in rat brain and molecular cloning of multiple cDNAs encoding structurally related proteins in humans. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):41-6. [PubMed
]
- Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed
]
- Zhang Y, Dufort I, Rheault P, Luu-The V: Characterization of a human 20alpha-hydroxysteroid dehydrogenase. J Mol Endocrinol. 2000 Oct;25(2):221-8. [PubMed
]
- Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed
]
- Deyashiki Y, Ogasawara A, Nakayama T, Nakanishi M, Miyabe Y, Sato K, Hara A: Molecular cloning of two human liver 3 alpha-hydroxysteroid/dihydrodiol dehydrogenase isoenzymes that are identical with chlordecone reductase and bile-acid binder. Biochem J. 1994 Apr 15;299 ( Pt 2):545-52. [PubMed
]
- Couture JF, Legrand P, Cantin L, Luu-The V, Labrie F, Breton R: Human 20alpha-hydroxysteroid dehydrogenase: crystallographic and site-directed mutagenesis studies lead to the identification of an alternative binding site for C21-steroids. J Mol Biol. 2003 Aug 15;331(3):593-604. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5624 |
| Enzyme 5 Name |
Aldo-keto reductase family 1 member C2 |
| Enzyme 5 Synonyms |
- Trans-1,2- dihydrobenzene-1,2-diol dehydrogenase
- Type III 3- alpha-hydroxysteroid dehydrogenase
- 3-alpha-HSD3
- Chlordecone reductase homolog HAKRD
- Dihydrodiol dehydrogenase/bile acid-binding protein
- DD/BABP
- Dihydrodiol dehydrogenase 2
- DD2
|
| Enzyme 5 Gene Name |
AKR1C2 |
| Enzyme 5 Protein Sequence |
>Aldo-keto reductase family 1 member C2
MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQ
VGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPV
SVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEMILNKP
GLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPV
LCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLN
RNVRYLTLDIFAGPPNYPFSDEY
|
| Enzyme 5 Number of Residues |
323 |
| Enzyme 5 Molecular Weight |
36736 |
| Enzyme 5 Theoretical pI |
7.55 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 5 General Function |
Not Available |
| Enzyme 5 Specific Function |
Works in concert with the 5alpha/5beta-steroid reductases to convert steroid hormones into the 3alpha/5alpha and 3alpha/5beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5alpha-DHT) to 5-alpha-androstane-3alpha,17beta-diol (3-alpha-diol) |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
- trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH + H+
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
531160  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P52895  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
AK1C2_HUMAN  |
| Enzyme 5 PDB ID |
1IHI  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>972 bp
ATGGATTCGAAATACCAGTGTGTGAAGCTGAATGATGGTCACTTCATGCCTGTCCTGGGA
TTTGGCACCTATGCGCCTGCAGAGGTTCCTAAAAGTAAAGCTCTAGAGGCCGTCAAATTG
GCAATAGAAGCCGGGTTCCACCATATTGATTCTGCACATGTTTACAATAATGAGGAGCAG
GTTGGACTGGCCATCCGAAGCAAGATTGCAGATGGCAGTGTGAAGAGAGAAGACATATTC
TACACTTCAAAGCTTTGGAGCAATTCCCATCGACCAGAGTTGGTCCGACCAGCCTTGGAA
AGGTCACTGAAAAATCTTCAATTGGACTATGTTGACCTCTATCTTATTCATTTTCCAGTG
TCTGTAAAGCCAGGTGAGGAAGTGATCCCAAAAGATGAAAATGGAAAAATACTATTTGAC
ACAGTGGATCTCTGTGCCACGTGGGAGGCCATGGAGAAGTGTAAAGATGCAGGATTGGCC
AAGTCCATCGGGGTGTCCAACTTCAACCACAGGCTGCTGGAGATGATCCTCAACAAGCCA
GGGCTCAAGTACAAGCCTGTCTGCAACCAGGTGGAATGTCATCCTTACTTCAACCAGAGA
AAACTGCTGGATTTCTGCAAGTCAAAAGACATTGTTCTGGTTGCCTATAGTGCTCTGGGA
TCCCATCGAGAAGAACCATGGGTGGACCCGAACTCCCCGGTGCTCTTGGAGGACCCAGTC
CTTTGTGCCTTGGCAAAAAAGCACAAGCGAACCCCAGCCCTGATTGCCCTGCGCTACCAG
CTGCAGCGTGGGGTTGTGGTCCTGGCCAAGAGCTACAATGAGCAGCGCATCAGACAGAAC
GTGCAGGTGTTTGAATTCCAGTTGACTTCAGAGGAGATGAAAGCCATAGATGGCCTAAAC
AGAAATGTGCGATATTTGACCCTTGATATTTTTGCTGGCCCCCCTAATTATCCATTTTCT
GATGAATATTAA
|
| Enzyme 5 GenBank Gene ID |
U05598  |
| Enzyme 5 GeneCard ID |
AKR1C2  |
| Enzyme 5 GenAtlas ID |
AKR1C2  |
| Enzyme 5 HGNC ID |
HGNC:385  |
| Enzyme 5 Chromosome Location |
10 |
| Enzyme 5 Locus |
10p15-p14 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Ciaccio PJ, Tew KD: cDNA and deduced amino acid sequences of a human colon dihydrodiol dehydrogenase. Biochim Biophys Acta. 1994 Jun 28;1186(1-2):129-32. [PubMed
]
- Qin KN, New MI, Cheng KC: Molecular cloning of multiple cDNAs encoding human enzymes structurally related to 3 alpha-hydroxysteroid dehydrogenase. J Steroid Biochem Mol Biol. 1993 Dec;46(6):673-9. [PubMed
]
- Qin KN, Khanna M, Cheng KC: Structure of a gene coding for human dihydrodiol dehydrogenase/bile acid-binding protein. Gene. 1994 Nov 18;149(2):357-61. [PubMed
]
- Shiraishi H, Ishikura S, Matsuura K, Deyashiki Y, Ninomiya M, Sakai S, Hara A: Sequence of the cDNA of a human dihydrodiol dehydrogenase isoform (AKR1C2) and tissue distribution of its mRNA. Biochem J. 1998 Sep 1;334 ( Pt 2):399-405. [PubMed
]
- Nishizawa M, Nakajima T, Yasuda K, Kanzaki H, Sasaguri Y, Watanabe K, Ito S: Close kinship of human 20alpha-hydroxysteroid dehydrogenase gene with three aldo-keto reductase genes. Genes Cells. 2000 Feb;5(2):111-25. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5687 |
| Enzyme 6 Name |
UDP-glucuronosyltransferase 2B28 precursor |
| Enzyme 6 Synonyms |
- UDPGT
|
| Enzyme 6 Gene Name |
UGT2B28 |
| Enzyme 6 Protein Sequence |
>UDP-glucuronosyltransferase 2B28 precursor
MALKWTSVLLLIHLGCYFSSGSCGKVLVWTGEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDAFTLKLEVYPTSLTKTEFENIIMQQVKRWSDIQKDSFWLYFSQEQEILWEFH
DIFRNFCKDVVSNKKVMKKLQESRFDIIFADAFFPCGELLAALLNIPFVYSLCFTPGYTI
ERHSGGLIFPPSYIPVVMSKLSDQMTFMERVKNMIYVLYFDFWFQMCDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNIDFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGLPKTRAFITHGGANGIYEAIYHGIPMVGIPLFWDQPDNIAHMKAKGAAVRLDFHTM
SSTDLLNALKTVINDPSYKENVMKLSIIQHDQPVKPLHRAVFWIEFVMCHKGAKHLRVAA
RDLTWFQYHSLDVIGFLLACVATVIFVVTKFCLFCFWKFARKGKKGKRD
|
| Enzyme 6 Number of Residues |
529 |
| Enzyme 6 Molecular Weight |
60907 |
| Enzyme 6 Theoretical pI |
8.80 |
| Enzyme 6 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Carbohydrate transport and metabolism |
| Enzyme 6 Specific Function |
UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme has glucuronidating capacity with steroid substrates such as 5-beta-androstane 3-alpha,17-beta- diol, estradiol, ADT, eugenol and bile acids. Only isoform 1 seems to be active |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
13603476  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q9BY64  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
UDB28_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1590 bp
ATGGCTCTGAAGTGGACTTCAGTTCTTCTGCTGATACATCTCGGTTGTTACTTTAGCTCT
GGGAGTTGTGGAAAGGTGCTGGTGTGGACCGGTGAATACAGCCATTGGATGAATATGAAG
ACAATCCTGAAAGAGCTTGTTCAGAGAGGTCATGAGGTGACTGTACTGGCATCTTCAGCT
TCCATTCTTTTTGATCCCAATGACGCATTCACTCTTAAACTCGAAGTTTATCCTACATCT
TTAACTAAAACTGAATTTGAGAATATCATCATGCAACAGGTTAAGAGATGGTCAGACATT
CAAAAAGATAGCTTTTGGTTATATTTTTCACAAGAACAAGAAATCCTGTGGGAATTTCAT
GACATATTTAGAAACTTCTGTAAAGATGTAGTTTCAAATAAGAAAGTTATGAAAAAACTA
CAAGAGTCAAGATTTGACATCATTTTTGCAGATGCTTTTTTTCCTTGTGGTGAGCTGCTG
GCTGCGCTACTTAACATACCGTTTGTGTACAGTCTCTGCTTCACTCCTGGCTACACAATT
GAAAGGCACAGTGGAGGACTGATTTTCCCTCCTTCCTACATACCTGTTGTTATGTCAAAA
TTAAGTGATCAAATGACTTTCATGGAGAGGGTAAAAAACATGATCTATGTGCTTTATTTT
GACTTTTGGTTCCAAATGTGTGATATGAAGAAGTGGGATCAGTTTTACAGTGAAGTTTTA
GGAAGACCCACTACCTTATTTGAGACAATGGGGAAAGCTGACATATGGCTTATGCGAAAC
TCCTGGAGTTTTCAATTTCCTCATCCATTCTTACCAAACATTGATTTTGTTGGAGGACTC
CACTGCAAACCTGCCAAACCCCTACCTAAGGAAATGGAGGAATTTGTACAGAGCTCTGGT
GAAAATGGTGTTGTGGTGTTTTCTCTGGGGTCAGTGATAAGTAACATGACAGCAGAAAGG
GCCAACGTAATTGCAACAGCCCTTGCCAAGATCCCACAAAAGGTTCTGTGGAGATTTGAT
GGGAATAAACCAGATGCCTTAGGTCTCAATACTCGGCTGTATAAGTGGATACCCCAGAAT
GACCTTCTAGGTCTTCCAAAAACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATC
TATGAGGCAATCTACCATGGGATCCCTATGGTAGGCATTCCATTGTTTTGGGATCAACCT
GATAACATTGCTCACATGAAGGCCAAGGGAGCAGCTGTTAGACTGGACTTCCACACAATG
TCGAGTACAGACCTGCTGAATGCACTGAAGACAGTAATTAATGATCCTTCATATAAAGAG
AATGTTATGAAATTATCAATAATTCAACATGATCAACCAGTAAAGCCCCTGCATCGAGCA
GTCTTCTGGATTGAATTTGTGATGTGCCACAAAGGAGCCAAACACCTTCGAGTTGCAGCC
CGTGACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGATTGGGTTTCTGCTGGCCTGT
GTGGCAACTGTGATATTTGTCGTCACAAAGTTTTGTCTGTTTTGTTTCTGGAAGTTTGCT
AGAAAAGGGAAGAAGGGAAAAAGAGATTAG
|
| Enzyme 6 GenBank Gene ID |
AF177272  |
| Enzyme 6 GeneCard ID |
UGT2B28  |
| Enzyme 6 GenAtlas ID |
UGT2B28  |
| Enzyme 6 HGNC ID |
HGNC:13479  |
| Enzyme 6 Chromosome Location |
4 |
| Enzyme 6 Locus |
4q13.2 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Levesque E, Turgeon D, Carrier JS, Montminy V, Beaulieu M, Belanger A: Isolation and characterization of the UGT2B28 cDNA encoding a novel human steroid conjugating UDP-glucuronosyltransferase. Biochemistry. 2001 Apr 3;40(13):3869-81. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5696 |
| Enzyme 7 Name |
UDP-glucuronosyltransferase 2B4 precursor |
| Enzyme 7 Synonyms |
- UDPGT
- Hyodeoxycholic acid
- HLUG25
- UDPGTh-1
|
| Enzyme 7 Gene Name |
UGT2B4 |
| Enzyme 7 Protein Sequence |
>UDP-glucuronosyltransferase 2B4 precursor
MSMKWTSALLLIQLSCYFSSGSCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLASSA
SISFDPNSPSTLKFEVYPVSLTKTEFEDIIKQLVKRWAELPKDTFWSYFSQVQEIMWTFN
DILRKFCKDIVSNKKLMKKLQESRFDVVLADAVFPFGELLAELLKIPFVYSLRFSPGYAI
EKHSGGLLFPPSYVPVVMSELSDQMTFIERVKNMIYVLYFEFWFQIFDMKKWDQFYSEVL
GRPTTLSETMAKADIWLIRNYWDFQFPHPLLPNVEFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSMVSNTSEERANVIASALAKIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGVPLFADQPDNIAHMKAKGAAVSLDFHTM
SSTDLLNALKTVINDPLYKENAMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVTGFLLACVATVIFIITKCLFCVWKFVRTGKKGKRD
|
| Enzyme 7 Number of Residues |
528 |
| Enzyme 7 Molecular Weight |
60513 |
| Enzyme 7 Theoretical pI |
8.75 |
| Enzyme 7 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Carbohydrate transport and metabolism |
| Enzyme 7 Specific Function |
UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme is active on polyhydroxylated estrogens (such as estriol, 4-hydroxyestrone and 2-hydroxyestriol) and xenobiotics (such as 4-methylumbelliferone, 1-naphthol, 4- nitrophenol, 2-aminophenol, 4-hydroxybiphenyl and menthol). It is capable of 6 alpha-hydroxyglucuronidation of hyodeoxycholic acid |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
37589  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P06133  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
UDB4_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>1587 bp
ATGTCTATGAAATGGACTTCAGCTCTTCTGCTGATACAGCTGAGCTGTTACTTTAGCTCT
GGGAGTTGTGGAAAGGTGCTGGTGTGGCCCACAGAATTCAGCCACTGGATGAATATAAAG
ACAATCCTGGATGAACTTGTCCAGAGAGGTCATGAGGTGACTGTATTGGCATCTTCAGCT
TCCATTTCTTTCGATCCCAACAGCCCATCTACTCTTAAATTTGAAGTTTATCCTGTATCT
TTAACTAAAACTGAGTTTGAGGATATTATCAAGCAGCTGGTTAAGAGATGGGCAGAACTT
CCAAAAGACACATTTTGGTCATATTTTTCACAAGTACAAGAAATCATGTGGACATTTAAT
GACATACTTAGAAAGTTCTGTAAGGATATAGTTTCAAATAAGAAACTTATGAAGAAACTA
CAGGAGTCAAGATTTGATGTTGTTCTTGCAGATGCTGTTTTCCCCTTTGGTGAGCTGCTG
GCCGAGTTACTTAAAATACCCTTTGTCTACAGGCCTCGCTTCTCTCCTGGCTACGCAATT
GAAAAGCATAGTGGAGGACTTCTGTTCCCTCCTTCCTATGTGCCTGTTGTTATGTCAGAA
CTAAGTGACCAAATGACTTTCATAGAGAGGGTAAAAAATATGATCTATGTGCTTTATTTT
GAATTTTGGTTCCAAATATTTGACATGAAGAAGTGGGATCAGTTCTACAGTGAAGTTCTA
GGAAGACCCACTACGTTATCTGAGACAATGGCAAAAGCTGACATATGGCTTATTCGAAAC
TACTGGGATTTTCAATTTCCTCACCCACTCTTACCAAATGTTGAGTTCGTTGGAGGACTC
CACTGCAAACCTGCCAAACCCCTACCGAAGGAAATGGAAGAGTTTGTCCAGAGCTCTGGA
GAAAATGGTGTTGTGGTGTTTTCTCTGGGGTCGATGGTCAGTAACACGTCAGAAGAAAGG
GCCAATGTAATTGCATCAGCCCTTGCCAAGATCCCACAAAAGGTTCTGTGGAGATTTGAT
GGGAATAAACCAGATACTTTAGGACTCAATACTCGGCTGTACAAGTGGATACCCCAGAAT
GATCTTCTTGGTCACCCAAAAACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATC
TATAAGGCAATCTCTCCTAGAATCCCTATGGTGGGCGTTCCATTGTTTGCAGATCAACCT
GATAACATTGCACACATGAAGGCCAAGGGAGCAGCTGTTAGTTTGGACTTCCACACAATG
TCGAGTACAGACTTACTCAATGCACTGAAGACAGTAATTAATGATCCTTTATATAAAGAG
AATGCTATGAAATTATCAAGAATTCATCATGATCAACCAGTGAAGCCCCTTGATCGAGCA
GTCTTCTGGATTGAATTTGTCATGCGCCATAAAGGAGCCAAGCACCTTCGGGTTGCAGCC
CACGACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGACTGGGTTCCTGCTGGCCTGT
GTGGCAACTGTGATATTCATCATCACAAAATGTCTGTTTTGTGTCTGGAAGTTTGTTAGA
ACAGGAAAGAAGGGGAAAAGAGATTAA
|
| Enzyme 7 GenBank Gene ID |
Y00317  |
| Enzyme 7 GeneCard ID |
UGT2B4  |
| Enzyme 7 GenAtlas ID |
UGT2B4  |
| Enzyme 7 HGNC ID |
HGNC:12553  |
| Enzyme 7 Chromosome Location |
4 |
| Enzyme 7 Locus |
4q13 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Jackson MR, McCarthy LR, Harding D, Wilson S, Coughtrie MW, Burchell B: Cloning of a human liver microsomal UDP-glucuronosyltransferase cDNA. Biochem J. 1987 Mar 1;242(2):581-8. [PubMed
]
- Jin CJ, Miners JO, Lillywhite KJ, Mackenzie PI: cDNA cloning and expression of two new members of the human liver UDP-glucuronosyltransferase 2B subfamily. Biochem Biophys Res Commun. 1993 Jul 15;194(1):496-503. [PubMed
]
- Levesque E, Beaulieu M, Hum DW, Belanger A: Characterization and substrate specificity of UGT2B4 (E458): a UDP-glucuronosyltransferase encoded by a polymorphic gene. Pharmacogenetics. 1999 Apr;9(2):207-16. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5719 |
| Enzyme 8 Name |
UDP-glucuronosyltransferase 1-4 precursor |
| Enzyme 8 Synonyms |
- UDP- glucuronosyltransferase 1A4
- UDPGT
- UGT1*4
- UGT1-04
- UGT1.4
- UGT- 1D
- UGT1D
- Bilirubin-specific UDPGT isozyme 2
- HUG-BR2
|
| Enzyme 8 Gene Name |
UGT1A4 |
| Enzyme 8 Protein Sequence |
>UDP-glucuronosyltransferase 1-4 precursor
MARGLQVPLPRLATGLLLLLSVQPWAESGKVLVVPTDGSPWLSMREALRELHARGHQAVV
LTPEVNMHIKEEKFFTLTAYAVPWTQKEFDRVTLGYTQGFFETEHLLKRYSRSMAIMNNV
SLALHRCCVELLHNEALIRHLNATSFDVVLTDPVNLCGAVLAKYLSIPAVFFWRYIPCDL
DFKGTQCPNPSSYIPKLLTTNSDHMTFLQRVKNMLYPLALSYICHTFSAPYASLASELFQ
REVSVVDLVSYASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
|
| Enzyme 8 Number of Residues |
534 |
| Enzyme 8 Molecular Weight |
60026 |
| Enzyme 8 Theoretical pI |
8.68 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Carbohydrate transport and metabolism |
| Enzyme 8 Specific Function |
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
340137  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P22310  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
UD14_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>867 bp
ATGGCCAGAGGACTCCAGGTTCCCCTGCCGCGGCTGGCCACAGGACTGCTGCTCCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGAAAGGTGTTGGTGGTGCCCACTGATGGCAGCCCC
TGGCTCAGCATGCGGGAGGCCTTGCGGGAGCTCCATGCCAGAGGCCACCAGGCGGTGGTC
CTCACCCCAGAGGTGAATATGCACATCAAAGAAGAGAAATTTTTCACCCTGACAGCCTAT
GCTGTTCCATGGACCCAGAAGGAATTTGATCGCGTTACGCTGGGCTACACTCAAGGGTTC
TTTGAAACAGAACATCTTCTGAAGAGATATTCTAGAAGTATGGCAATTATGAACAATGTA
TCTTTGGCCCTTCATAGGTGTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGAATGCTACTTCCTTTGATGTGGTTTTAACAGACCCCGTTAACCTCTGTGGGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTTTGGAGGTACATTCCATGTGACTTA
GACTTTAAGGGCACACAGTGTCCAAATCCTTCCTCCTATATTCCTAAGTTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACATTTGCCATACTTTTTCTGCCCCTTATGCAAGTCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCTATGCATCCGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGACTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAG
|
| Enzyme 8 GenBank Gene ID |
M84128  |
| Enzyme 8 GeneCard ID |
UGT1A4  |
| Enzyme 8 GenAtlas ID |
UGT1A4  |
| Enzyme 8 HGNC ID |
HGNC:12536  |
| Enzyme 8 Chromosome Location |
2 |
| Enzyme 8 Locus |
2q37 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Ritter JK, Crawford JM, Owens IS: Cloning of two human liver bilirubin UDP-glucuronosyltransferase cDNAs with expression in COS-1 cells. J Biol Chem. 1991 Jan 15;266(2):1043-7. [PubMed
]
- Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS: A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem. 1992 Feb 15;267(5):3257-61. [PubMed
]
- Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [PubMed
]
- Bosma PJ, Chowdhury JR, Huang TJ, Lahiri P, Elferink RP, Van Es HH, Lederstein M, Whitington PF, Jansen PL, Chowdhury NR: Mechanisms of inherited deficiencies of multiple UDP-glucuronosyltransferase isoforms in two patients with Crigler-Najjar syndrome, type I. FASEB J. 1992 Jul;6(10):2859-63. [PubMed
]
- Aono S, Yamada Y, Keino H, Hanada N, Nakagawa T, Sasaoka Y, Yazawa T, Sato H, Koiwai O: Identification of defect in the genes for bilirubin UDP-glucuronosyl-transferase in a patient with Crigler-Najjar syndrome type II. Biochem Biophys Res Commun. 1993 Dec 30;197(3):1239-44. [PubMed
]
- Moghrabi N, Clarke DJ, Boxer M, Burchell B: Identification of an A-to-G missense mutation in exon 2 of the UGT1 gene complex that causes Crigler-Najjar syndrome type 2. Genomics. 1993 Oct;18(1):171-3. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5721 |
| Enzyme 9 Name |
UDP-glucuronosyltransferase 2B7 precursor |
| Enzyme 9 Synonyms |
- UDPGT
- 3,4- catechol estrogen specific
- UDPGTh-2
|
| Enzyme 9 Gene Name |
UGT2B7 |
| Enzyme 9 Protein Sequence |
>UDP-glucuronosyltransferase 2B7 precursor
MSVKWTSVILLIQLSFCFSSGNCGKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSA
SILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRWSDLPKDTFWLYFSQVQEIMSIFG
DITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTF
EKHSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSEVL
GRPTTLSETMGKADVWLIRNSWNFQFPHPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSG
ENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFADQPDNIAHMKARGAAVRVDFNTM
SSTDLLNALKRVINDPSYKENVMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLVCVATVIFIVTKCCLFCFWKFARKAKKGKND
|
| Enzyme 9 Number of Residues |
529 |
| Enzyme 9 Molecular Weight |
60695 |
| Enzyme 9 Theoretical pI |
8.45 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Carbohydrate transport and metabolism |
| Enzyme 9 Specific Function |
Its unique specificity for 3,4-catechol estrogens and estriol suggests it may play an important role in regulating the level and activity of these potent and active estrogen metabolites |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
340080  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P16662  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
UDB7_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1590 bp
ATGTCTGTGAAATGGACTTCAGTAATTTTGCTAATACAACTGAGCTTTTGCTTTAGCTCT
GGGAATTGTGGAAAGGTGCTGGTGTGGGCAGCAGAATACAGCCATTGGATGAATATAAAG
ACAATCCTGGATGAGCTTATTCAGAGAGGTCATGAGGTGACTGTACTGGCATCTTCAGCT
TCCATTCTTTTTGATCCCAACAACTCATCCGCTCTTAAAATTGAAATTTATCCCACATCT
TTAACTAAAACTGAGTTGGAGAATTTCATCATGCAACAGATTAAGAGATGGTCAGACCTT
CCAAAAGATACATTTTGGTTATATTTTTCACAAGTACAGGAAATCATGTCAATATTTGGT
GACATAACTAGAAAGTTCTGTAAAGATGTAGTTTCAAATAAGAAATTTATGAAAAAAGTA
CAAGAGTCAAGATTTGACGTCATTTTTGCAGATGCTATTTTTCCCTGTAGTGAGCTGCTG
GCTGAGCTATTTAACATACCCTTTGTGTACAGTCTCAGCTTCTCTCCTGGCTACACTTTT
GAAAAGCATAGTGGAGGATTTATTTTCCCTCCTTCCTACGTACCTGTTGTTATGTCAGAA
TTAACTGATCAAATGACTTTCATGGAGAGGGTAAAAAATATGATCTATGTGCTTTACTTT
GACTTTTGGTTCGAAATATTTGACATGAAGAAGTGGGATCAGTTTTATAGTGAAGTTCTA
GGAAGACCCACTACGTTATCTGAGACAATGGGGAAAGCTGACGTATGGCTTATTCGAAAC
TCCTGGAATTTTCAGTTTCCTCATCCACTCTTACCAAATGTTGATTTTGTTGGAGGACTC
CACTGCAAACCTGCCAAACCCCTGCCTAAGGAAATGGAAGACTTTGTACAGAGCTCTGGA
GAAAATGGTGTTGTGGTGTTTTCTCTGGGGTCAATGGTCAGTAACATGACAGAAGAAAGG
GCCAACGTAATTGCATCAGCCCTGGCCCAGATCCCACAAAAGGTTCTGTGGAGATTTGAT
GGGAATAAACCAGATACCTTAGGTCTCAATACTCGGCTGTATAAGTGGATACCCCAGAAT
GACCTTCTAGGTCATCCAAAGACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATC
TACGAGGCAATCTACCATGGGATCCCTATGGTGGGGATTCCATTGTTTGCCGATCAACCT
GATAACATTGCTCACATGAAGGCCAGGGGAGCAGCTGTTAGAGTGGACTTCAACACAATG
TCGAGTACAGACTTGCTGAATGCATTGAAGAGAGTAATTAATGATCCTTCATATAAAGAG
AATGTTATGAAATTATCAAGAATTCAACATGATCAACCAGTGAAGCCCCTGGATCGAGCA
GTCTTCTGGATTGAATTTGTCATGCGCCACAAAGGAGCTAAACACCTTCGGGTTGCAGCC
CACGACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGATTGGGTTCCTGCTGGTCTGT
GTGGCAACTGTGATATTTATCGTCACAAAATGTTGTCTGTTTTGTTTCTGGAAGTTTGCT
AGAAAAGCAAAGAAGGGAAAAAATGATTAG
|
| Enzyme 9 GenBank Gene ID |
J05428  |
| Enzyme 9 GeneCard ID |
UGT2B7  |
| Enzyme 9 GenAtlas ID |
UGT2B7  |
| Enzyme 9 HGNC ID |
HGNC:12554  |
| Enzyme 9 Chromosome Location |
4 |
| Enzyme 9 Locus |
4q13 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Ritter JK, Sheen YY, Owens IS: Cloning and expression of human liver UDP-glucuronosyltransferase in COS-1 cells. 3,4-catechol estrogens and estriol as primary substrates. J Biol Chem. 1990 May 15;265(14):7900-6. [PubMed
]
- Bhasker CR, McKinnon W, Stone A, Lo AC, Kubota T, Ishizaki T, Miners JO: Genetic polymorphism of UDP-glucuronosyltransferase 2B7 (UGT2B7) at amino acid 268: ethnic diversity of alleles and potential clinical significance. Pharmacogenetics. 2000 Nov;10(8):679-85. [PubMed
]
|
| Enzyme 9 Metabolite References |
- Coffman BL, King CD, Rios GR, Tephly TR: The glucuronidation of opioids, other xenobiotics, and androgens by human UGT2B7Y(268) and UGT2B7H(268). Drug Metab Dispos. 1998 Jan;26(1):73-7. [PubMed
]
|
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5722 |
| Enzyme 10 Name |
UDP-glucuronosyltransferase 2B15 precursor |
| Enzyme 10 Synonyms |
- UDPGT
- UDPGTh-3
- HLUG4
|
| Enzyme 10 Gene Name |
UGT2B15 |
| Enzyme 10 Protein Sequence |
>UDP-glucuronosyltransferase 2B15 precursor
MSLKWTSVFLLIQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVTVLTSSA
STLVNASKSSAIKLEVYPTSLTKNDLEDSLLKILDRWIYGVSKNTFWSYFSQLQELCWEY
YDYSNKLCKDAVLNKKLMMKLQESKFDVILADALNPCGELLAELFNIPFLYSLRFSVGYT
FEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIHMLYFDFWFQIYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPVYKENVMKLSRIHHDQPMKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATVIFIITKFCLFCFRKLAKKGKKKKRD
|
| Enzyme 10 Number of Residues |
530 |
| Enzyme 10 Molecular Weight |
60989 |
| Enzyme 10 Theoretical pI |
9.04 |
| Enzyme 10 GO Classification |
Not Available |
| Enzyme 10 General Function |
Carbohydrate transport and metabolism |
| Enzyme 10 Specific Function |
UDPGTs are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isozyme displays activity toward several classes of xenobiotic substrates, including simple phenolic compounds, 7-hydroxylated coumarins, flavonoids, anthraquinones, and certain drugs and their hydroxylated metabolites. It also catalyzes the glucuronidation of endogenous estrogens and androgens |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 10 Pfam Domain Function |
Not Available |
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
23955933  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P54855  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
UDB15_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1593 bp
ATGTCTCTGAAATGGACGTCAGTCTTTCTGCTGATACAGCTCAGTTGTTACTTTAGCTCT
GGAAGCTGTGGAAAGGTGCTAGTGTGGCCCACAGAATACAGCCATTGGATAAATATGAAG
ACAATCCTGGAAGAGCTTGTTCAGAGGGGTCATGAGGTGACTGTGTTGACATCTTCGGCT
TCTACTCTTGTCAATGCCAGTAAATCATCTGCTATTAAATTAGAAGTTTATCCTACATCT
TTAACTAAAAATGATTTGGAAGATTCTCTTCTGAAAATTCTCGATAGATGGATATATGGT
GTTTCAAAAAATACATTTTGGTCATATTTTTCACAATTACAAGAATTGTGTTGGGAATAT
TATGACTACAGTAACAAGCTCTGTAAAGATGCAGTTTTGAATAAGAAACTTATGATGAAA
CTACAAGAGTCAAAGTTTGATGTCATTCTGGCAGATGCCCTTAATCCCTGTGGTGAGCTA
CTGGCTGAACTATTTAACATACCCTTTCTGTACAGTCTTCGATTCTCTGTTGGCTACACA
TTTGAGAAGAATGGTGGAGGATTTCTGTTCCCTCCTTCCTATGTACCTGTTGTTATGTCA
GAATTAAGTGATCAAATGATTTTCATGGAGAGGATAAAAAATATGATACATATGCTTTAT
TTTGACTTTTGGTTTCAAATTTATGATCTGAAGAAGTGGGACCAGTTTTATAGTGAAGTT
CTAGGAAGACCCACTACATTATTTGAGACAATGGGGAAAGCTGAAATGTGGCTCATTCGA
ACCTATTGGGATTTTGAATTTCCTCGCCCATTCTTACCAAATGTTGATTTTGTTGGAGGA
CTTCACTGTAAACCAGCCAAACCCCTGCCTAAGGAAATGGAAGAGTTTGTGCAGAGCTCT
GGAGAAAATGGTATTGTGGTGTTTTCTCTGGGGTCGATGATCAGTAACATGTCAGAAGAA
AGTGCCAACATGATTGCATCAGCCCTTGCCCAGATCCCACAAAAGGTTCTATGGAGATTT
GATGGCAAGAAGCCAAATACTTTAGGTTCCAATACTCGACTGTACAAGTGGTTACCCCAG
AATGACCTTCTTGGTCATCCCAAAACCAAAGCTTTTATAACTCATGGTGGAACCAATGGC
ATCTATGAGGCGATCTACCATGGGATCCCTATGGTGGGCATTCCCTTGTTTGCGGATCAA
CATGATAACATTGCTCACATGAAAGCCAAGGGAGCAGCCCTCAGTGTGGACATCAGGACC
ATGTCAAGTAGAGATTTGCTCAATGCATTGAAGTCAGTCATTAATGACCCTGTCTATAAA
GAGAATGTCATGAAATTATCAAGAATTCATCATGACCAACCAATGAAGCCCCTGGATCGA
GCAGTCTTCTGGATTGAGTTTGTCATGCGCCACAAAGGAGCCAAGCACCTTCGAGTCGCA
GCTCACAACCTCACCTGGATCCAGTACCACTCTTTGGATGTGATAGCATTCCTGCTGGCC
TGCGTGGCAACTGTGATATTTATCATCACAAAATTTTGCCTGTTTTGTTTCCGAAAGCTT
GCCAAAACAGGAAAGAAGAAGAAAAGAGATTAG
|
| Enzyme 10 GenBank Gene ID |
AF548389  |
| Enzyme 10 GeneCard ID |
UGT2B15  |
| Enzyme 10 GenAtlas ID |
UGT2B15  |
| Enzyme 10 HGNC ID |
HGNC:12546  |
| Enzyme 10 Chromosome Location |
4 |
| Enzyme 10 Locus |
4q13 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Green MD, Oturu EM, Tephly TR: Stable expression of a human liver UDP-glucuronosyltransferase (UGT2B15) with activity toward steroid and xenobiotic substrates. Drug Metab Dispos. 1994 Sep-Oct;22(5):799-805. [PubMed
]
- Levesque E, Beaulieu M, Green MD, Tephly TR, Belanger A, Hum DW: Isolation and characterization of UGT2B15(Y85): a UDP-glucuronosyltransferase encoded by a polymorphic gene. Pharmacogenetics. 1997 Aug;7(4):317-25. [PubMed
]
- Coffman BL, Tephly TR, Irshaid YM, Green MD, Smith C, Jackson MR, Wooster R, Burchell B: Characterization and primary sequence of a human hepatic microsomal estriol UDPglucuronosyltransferase. Arch Biochem Biophys. 1990 Aug 15;281(1):170-5. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5724 |
| Enzyme 11 Name |
UDP-glucuronosyltransferase 2A1 precursor |
| Enzyme 11 Synonyms |
Not Available |
| Enzyme 11 Gene Name |
UGT2A1 |
| Enzyme 11 Protein Sequence |
>UDP-glucuronosyltransferase 2A1 precursor
MLNNLLLFSLQISLIGTTLGGNVLIWPMEGSHWLNVKIIIDELIKKEHNVTVLVASGALF
ITPTSNPSLTFEIYKVPFGKERIEGVIKDFVSTWLENRPSPSTIWRFYQEMAKVIKDFHM
VSQEICDGVLKNQQLMAKLKKSKFEVLVSDPVFPCGDIVALKLGIPFMYSLRFSPASTVE
KHCGKVPYPPSYVPAVLSELTDQMSFTDRIRNFISYHLQDYMFETLWKSWDSYYSKALGR
PTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKEMEEFIQSSGKN
GVVVFSLGSMVKNLTEEKANLIASALAQIPQKVLWRYKGKKPATLGNNTQLFDWIPQNDL
LGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMFADQPDNIAHMKAKGAAVEVNLNTMTS
VDLLSALRTVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHD
LTWFQYHSLDVIGFLLVCVTTAIFLVIQCCLFSCQKFGKIGKKKKRE
|
| Enzyme 11 Number of Residues |
527 |
| Enzyme 11 Molecular Weight |
59873 |
| Enzyme 11 Theoretical pI |
9.29 |
| Enzyme 11 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 11 General Function |
Carbohydrate transport and metabolism |
| Enzyme 11 Specific Function |
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform is active on odorants and seems to be involved in olfaction; it could help clear lipophilic odorant molecules from the sensory epithelium |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
4753766  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9Y4X1  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
UDA1_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1584 bp
ATGTTAAACAACCTTCTGCTGTTCTCCCTTCAGATAAGTCTCATAGGAACCACTCTTGGT
GGGAATGTTTTGATTTGGCCAATGGAAGGTAGTCATTGGCTAAATGTTAAGATAATTATA
GATGAGCTCATTAAAAAGGAGCATAATGTGACTGTCCTAGTTGCCTCTGGTGCACTTTTC
ATCACACCAACCTCTAACCCATCTCTGACATTTGAAATATATAAGGTGCCCTTTGGCAAA
GAAAGAATAGAAGGAGTAATTAAGGACTTCGTTTCGACATGGCTGGAAAATAGACCATCT
CCTTCAACCATTTGGAGATTCTATCAGGAGATGGCCAAAGTAATCAAGGACTTCCACATG
GTGTCTCAGGAGATCTGTGATGGCGTTCTTAAAAACCAACAGCTGATGGCAAAGCTAAAG
AAAAGCAAGTTTGAAGTCCTGGTGTCTGATCCAGTATTTCCTTGTGGCGATATAGTAGCT
TTAAAACTTGGAATTCCATTTATGTACTCCTTGAGGTTTTCTCCAGCCTCAACAGTGGAA
AAGCACTGTGGGAAGGTACCATACCCTCCTTCCTATGTTCCTGCTGTTTTATCAGAACTC
ACCGACCAAATGTCTTTCACTGACAGAATAAGAAATTTCATCTCCTACCACCTACAGGAC
TACATGTTTGAAACTCTTTGGAAATCATGGGATTCATACTATAGTAAAGCTTTAGGAAGA
CCCACTACGTTATGTGAGACTATGGGGAAAGCTGAAATTTGGTTAATCCGAACATATTGG
GATTTTGAATTTCCTCGTCCATACTTACCTAATTTTGAGTTTGTTGGAGGATTGCACTGC
AAACCTGCCAAACCTTTACCTAAGGAAATGGAAGAATTTATCCAGAGCTCAGGTAAAAAT
GGTGTTGTGGTGTTTTCTCTGGGATCAATGGTCAAAAACCTTACAGAAGAAAAGGCCAAT
CTTATTGCCTCAGCCCTTGCCCAGATTCCACAGAAGGTTTTATGGAGATACAAAGGAAAG
AAACCAGCCACATTAGGAAACAATACTCAGCTCTTTGATTGGATACCCCAGAATGATCTT
CTTGGACATCCCAAAACCAAAGCTTTTATCACTCATGGTGGAACTAATGGGATCTACGAA
GCTATTTACCACGGAGTCCCTATGGTGGGAGTTCCCATGTTTGCTGATCAGCCTGATAAC
ATTGCTCACATGAAGGCCAAAGGAGCAGCTGTGGAAGTGAACCTAAACACAATGACAAGT
GTGGATTTGCTTAGCGCTTTGAGAACAGTCATTAATGAACCTTCTTATAAAGAGAATGCT
ATGAGGTTATCAAGAATTCACCATGATCAACCTGTAAAGCCCCTGGATCGAGCAGTCTTC
TGGATCGAGTTTGTCATGCGCCACAAAGGAGCCAAGCACCTTCGGGTTGCAGCCCATGAC
CTCACCTGGTTCCAGTACCACTCTTTGGATGTAATTGGGTTCTTGCTGGTCTGTGTGACA
ACGGCTATATTTTTGGTCATACAATGTTGTTTGTTTTCCTGTCAAAAATTTGGTAAGATA
GGAAAGAAGAAAAAAAGAGAATAG
|
| Enzyme 11 GenBank Gene ID |
AJ006054  |
| Enzyme 11 GeneCard ID |
UGT2A1  |
| Enzyme 11 GenAtlas ID |
UGT2A1  |
| Enzyme 11 HGNC ID |
HGNC:12542  |
| Enzyme 11 Chromosome Location |
4 |
| Enzyme 11 Locus |
4q13 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Jedlitschky G, Cassidy AJ, Sales M, Pratt N, Burchell B: Cloning and characterization of a novel human olfactory UDP-glucuronosyltransferase. Biochem J. 1999 Jun 15;340 ( Pt 3):837-43. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5725 |
| Enzyme 12 Name |
UDP-glucuronosyltransferase 1-1 precursor |
| Enzyme 12 Synonyms |
- UDP- glucuronosyltransferase 1A1
- UDPGT
- UGT1*1
- UGT1-01
- UGT1.1
- UGT- 1A
- UGT1A
- Bilirubin-specific UDPGT isozyme 1
- HUG-BR1
|
| Enzyme 12 Gene Name |
UGT1A1 |
| Enzyme 12 Protein Sequence |
>UDP-glucuronosyltransferase 1-1 precursor
MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVL
APDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDS
AMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLE
FEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQR
EVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEH
GIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDL
LGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTS
EDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHD
LTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
|
| Enzyme 12 Number of Residues |
533 |
| Enzyme 12 Molecular Weight |
59592 |
| Enzyme 12 Theoretical pI |
8.09 |
| Enzyme 12 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Carbohydrate transport and metabolism |
| Enzyme 12 Specific Function |
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
184473  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P22309  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
UD11_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1602 bp
ATGGCTGTGGAGTCCCAGGGCGGACGCCCACTTGTCCTGGGCCTGCTGCTGTGTGTGCTG
GGCCCAGTGGTGTCCCATGCTGGGAAGATACTGTTGATCCCAGTGGATGGCAGCCACTGG
CTGAGCATGCTTGGGGCCATCCAGCAGCTGCAGCAGAGGGGACATGAAATAGTTGTCCTA
GCACCTGACGCCTCGTTGTACATCAGAGACGGAGCATTTTACACCTTGAAGACGTACCCT
GTGCCATTCCAAAGGGAGGATGTGAAAGAGTCTTTTGTTAGTCTCGGGCATAATGTTTTT
GAGAATGATTCTTTCCTGCAGCGTGTGATCAAAACATACAAGAAAATAAAAAAGGACTCT
GCTATGCTTTTGTCTGGCTGTTCCCACTTACTGCACAACAAGGAGCTCATGGCCTCCCTG
GCAGAAAGCAGCTTTGATGTCATGCTGACGGACCCTTTCCTTCCTTGCAGCCCCATCGTG
GCCCAGTACCTGTCTCTGCCCACTGTATTCTTCTTGCATGCACTGCCATGCAGCCTGGAA
TTTGAGGCTACCCAGTGCCCCAACCCATTCTCCTACGTGCCCAGGCCTCTCTCCTCTCAT
TCAGATCACATGACCTTCCTGCAGCGGGTGAAGAACATGCTCATTGCCTTTTCACAGAAC
TTTCTGTGCGACGTGGTTTATTCCCCGTATGCAACCCTTGCCTCAGAATTCCTTCAGAGA
GAGGTGACTGTCCAGGACCTATTGAGCTCTGCATCTGTCTGGCTGTTTAGAAGTGACTTT
GTGAAGGATTACCCTAGGCCCATCATGCCCAATATGGTTTTTGTTGGTGGAATCAACTGC
CTTCACCAAAATCCACTATCCCAGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACAT
GGAATTGTGGTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATG
GCAATTGCTGATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACC
CGACCATCGAATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTG
CTTGGTCACCCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAA
AGCATATGCAATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAAT
GCAAAGCGCATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCT
GAAGATTTAGAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATC
ATGCGCCTCTCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTC
TGGGTGGAGTTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGAC
CTCACCTGGTACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTG
ACAGTGGCCTTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAA
AAAGGGCGAGTTAAGAAAGCCCACAAATCCAAGACCCATTGA
|
| Enzyme 12 GenBank Gene ID |
M57899  |
| Enzyme 12 GeneCard ID |
UGT1A1  |
| Enzyme 12 GenAtlas ID |
UGT1A1  |
| Enzyme 12 HGNC ID |
HGNC:12530  |
| Enzyme 12 Chromosome Location |
2 |
| Enzyme 12 Locus |
2q37 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Ritter JK, Crawford JM, Owens IS: Cloning of two human liver bilirubin UDP-glucuronosyltransferase cDNAs with expression in COS-1 cells. J Biol Chem. 1991 Jan 15;266(2):1043-7. [PubMed
]
- Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS: A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem. 1992 Feb 15;267(5):3257-61. [PubMed
]
- Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [PubMed
]
- Bosma PJ, Chowdhury JR, Huang TJ, Lahiri P, Elferink RP, Van Es HH, Lederstein M, Whitington PF, Jansen PL, Chowdhury NR: Mechanisms of inherited deficiencies of multiple UDP-glucuronosyltransferase isoforms in two patients with Crigler-Najjar syndrome, type I. FASEB J. 1992 Jul;6(10):2859-63. [PubMed
]
- Aono S, Yamada Y, Keino H, Hanada N, Nakagawa T, Sasaoka Y, Yazawa T, Sato H, Koiwai O: Identification of defect in the genes for bilirubin UDP-glucuronosyl-transferase in a patient with Crigler-Najjar syndrome type II. Biochem Biophys Res Commun. 1993 Dec 30;197(3):1239-44. [PubMed
]
- Moghrabi N, Clarke DJ, Boxer M, Burchell B: Identification of an A-to-G missense mutation in exon 2 of the UGT1 gene complex that causes Crigler-Najjar syndrome type 2. Genomics. 1993 Oct;18(1):171-3. [PubMed
]
- Ritter JK, Yeatman MT, Kaiser C, Gridelli B, Owens IS: A phenylalanine codon deletion at the UGT1 gene complex locus of a Crigler-Najjar type I patient generates a pH-sensitive bilirubin UDP-glucuronosyltransferase. J Biol Chem. 1993 Nov 5;268(31):23573-9. [PubMed
]
- Labrune P, Myara A, Hadchouel M, Ronchi F, Bernard O, Trivin F, Chowdhury NR, Chowdhury JR, Munnich A, Odievre M: Genetic heterogeneity of Crigler-Najjar syndrome type I: a study of 14 cases. Hum Genet. 1994 Dec;94(6):693-7. [PubMed
]
- Seppen J, Bosma PJ, Goldhoorn BG, Bakker CT, Chowdhury JR, Chowdhury NR, Jansen PL, Oude Elferink RP: Discrimination between Crigler-Najjar type I and II by expression of mutant bilirubin uridine diphosphate-glucuronosyltransferase. J Clin Invest. 1994 Dec;94(6):2385-91. [PubMed
]
- Aono S, Adachi Y, Uyama E, Yamada Y, Keino H, Nanno T, Koiwai O, Sato H: Analysis of genes for bilirubin UDP-glucuronosyltransferase in Gilbert's syndrome. Lancet. 1995 Apr 15;345(8955):958-9. [PubMed
]
- Yamamoto K, Soeda Y, Kamisako T, Hosaka H, Fukano M, Sato H, Fujiyama Y, Adachi Y, Satoh Y, Bamba T: Analysis of bilirubin uridine 5'-diphosphate (UDP)-glucuronosyltransferase gene mutations in seven patients with Crigler-Najjar syndrome type II. J Hum Genet. 1998;43(2):111-4. [PubMed
]
- Maruo Y, Sato H, Yamano T, Doida Y, Shimada M: Gilbert syndrome caused by a homozygous missense mutation (Tyr486Asp) of bilirubin UDP-glucuronosyltransferase gene. J Pediatr. 1998 Jun;132(6):1045-7. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5726 |
| Enzyme 13 Name |
UDP-glucuronosyltransferase 1-9 precursor |
| Enzyme 13 Synonyms |
- UDP- glucuronosyltransferase 1A9
- UDPGT
- UGT1*9
- UGT1-9
- UGT1.9
- UGT- 1I
- UGT1I
- lugP4
|
| Enzyme 13 Gene Name |
UGT1A9 |
| Enzyme 13 Protein Sequence |
>UDP-glucuronosyltransferase 1-9 precursor
MACTGWTSPLPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMRSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDLDREFKAFAHAQWKAQVRSIYSLLMGSYNDIFDLF
FSNCRSLFKDKKLVEYLKESSFDAVFLDPFDNCGLIVAKYFSLPSVVFARGILCHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLLCHRFFKNALEIASEILQTPVT
EYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
|
| Enzyme 13 Number of Residues |
530 |
| Enzyme 13 Molecular Weight |
59942 |
| Enzyme 13 Theoretical pI |
7.96 |
| Enzyme 13 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 13 General Function |
Carbohydrate transport and metabolism |
| Enzyme 13 Specific Function |
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
7690346  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
O60656  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
UD19_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1593 bp
ATGGCTTGCACAGGGTGGACCAGCCCCCTTCCTCTATGTGTGTGTCTGCTGCTGACCTGT
GGCTTTGCCGAGGCAGGGAAGCTAGTGGTAGTGCCCATGGATGGGAGCCACTGGTTCACC
ATGAGGTCGGTGGTGGAGAAACTCATTCTCAGGGGGCATGAGGTGGTTGTAGTCAGTGCC
AGAGGTGAGTTGGCAACTGGGAAGATCAATGAATTGCACAGTGAAGACTTATTCAACTTC
ATATACCTGGAGGATCTGGACCGGGAGTTCAAGGCTTTTGCCCATGCTCAATGGAAAGCA
CAAGTACGAAGTATATATTCTCTATTAATGGGTTCATACAATGACATTTTTGACTTATTT
TTTTCAAATTGCAGGAGTTTGTTTAAAGACAAAAAATTAGTAGAATACTTAAAGGAGAGT
TCTTTTGATGCAGTGTTTCTCGATCCTTTTGATAACTGTGGCTTAATTGTTGCCAAATAT
TTCTCCCTCCCCTCCGTGGTCTTCGCCAGGGGAATACTTTGCCACTATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAGAATTCTCTTAGGGTTCTCAGATGAC
ATGACTTTCAAGGAGAGAGTACGGAACCACATCATGCACTTGGAGGAACATTTATTATGC
CACCGTTTTTTCAAAAATGCCCTAGAAATAGCCTCTGAAATTCTCCAAACACCTGTTACG
GAGTATGATCTCTACAGCCACACATCAATTTGGTTGTTGCGAACGGACTTTGTTTTGGAC
TATCCCAAACCCGTGATGCCCAACATGATCTTCATTGGTGGTATCAACTGCCATGAGAGG
AAAGCGTTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GGTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATGC
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCAGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCATGAATGTTCTGGAAATGACTTCTGAAGAATTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTTATGAGGCACAAGGGCGCGACACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGCCGTGCTGACAGTGGCC
TTCATCACCTGTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
|
| Enzyme 13 GenBank Gene ID |
S55985  |
| Enzyme 13 GeneCard ID |
UGT1A9  |
| Enzyme 13 GenAtlas ID |
UGT1A9  |
| Enzyme 13 HGNC ID |
HGNC:12541  |
| Enzyme 13 Chromosome Location |
Not Available |
| Enzyme 13 Locus |
Not Available |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Wooster R, Sutherland L, Ebner T, Clarke D, Da Cruz e Silva O, Burchell B: Cloning and stable expression of a new member of the human liver phenol/bilirubin: UDP-glucuronosyltransferase cDNA family. Biochem J. 1991 Sep 1;278 ( Pt 2):465-9. [PubMed
]
- Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5728 |
| Enzyme 14 Name |
UDP-glucuronosyltransferase 1-3 precursor |
| Enzyme 14 Synonyms |
- UDP- glucuronosyltransferase 1A3
- UDPGT
- UGT1*3
- UGT1-03
- UGT1.3
- UGT- 1C
- UGT1C
|
| Enzyme 14 Gene Name |
UGT1A3 |
| Enzyme 14 Protein Sequence |
>UDP-glucuronosyltransferase 1-3 precursor
MATGLQVPLPWLATGLLLLLSVQPWAESGKVLVVPIDGSHWLSMREVLRELHARGHQAVV
LTPEVNMHIKEENFFTLTTYAISWTQDEFDRHVLGHTQLYFETEHFLKKFFRSMAMLNNM
SLVYHRSCVELLHNEALIRHLNATSFDVVLTDPVNLCAAVLAKYLSIPTVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFMQRVKNMLYPLALSYICHAFSAPYASLASELFQ
REVSVVDILSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANRKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
|
| Enzyme 14 Number of Residues |
534 |
| Enzyme 14 Molecular Weight |
60339 |
| Enzyme 14 Theoretical pI |
8.28 |
| Enzyme 14 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Carbohydrate transport and metabolism |
| Enzyme 14 Specific Function |
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
340135  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P35503  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
UD13_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>867 bp
ATGGCCACAGGACTCCAGGTTCCCCTGCCGTGGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGAAAGGTGTTGGTGGTGCCCATTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGTCTTGCGGGAGCTCCATGCCAGAGGCCACCAGGCAGTGGTC
CTCACCCCAGAGGTGAATATGCACATCAAAGAAGAGAACTTTTTCACCCTGACAACCTAT
GCCATTTCGTGGACCCAGGATGAATTTGATCGCCATGTGCTGGGCCACACTCAACTGTAC
TTTGAAACAGAACATTTTCTGAAGAAATTTTTCAGAAGTATGGCAATGTTGAACAATATG
TCTTTGGTCTATCATAGGTCTTGTGTGGAGCTACTACATAATGAGGCCCTGATCAGGCAC
CTGAATGCTACTTCCTTTGATGTGGTTTTAACAGACCCCGTTAACCTCTGCGCGGCAGTG
CTGGCTAAGTACCTGTCGATTCCTACTGTGTTTTTTTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACAACC
AATTCAGACCACATGACATTCATGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACATTTGCCATGCTTTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATATTCTCAGTCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGACTACCCCAGGCCAATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACAGGAAGCCACTATCTCAG
|
| Enzyme 14 GenBank Gene ID |
M84127  |
| Enzyme 14 GeneCard ID |
UGT1A3  |
| Enzyme 14 GenAtlas ID |
UGT1A3  |
| Enzyme 14 HGNC ID |
HGNC:12535  |
| Enzyme 14 Chromosome Location |
2 |
| Enzyme 14 Locus |
2q37 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS: A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem. 1992 Feb 15;267(5):3257-61. [PubMed
]
- Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5731 |
| Enzyme 15 Name |
UDP-glucuronosyltransferase 2B17 precursor |
| Enzyme 15 Synonyms |
- UDPGT
- C19- steroid-specific UDP-glucuronosyltransferase
|
| Enzyme 15 Gene Name |
UGT2B17 |
| Enzyme 15 Protein Sequence |
>UDP-glucuronosyltransferase 2B17 precursor
MSLKWMSVFLLMQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSA
SILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEY
SDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYT
VEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPIYKENIMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATMIFMITKCCLFCFRKLAKTGKKKKRD
|
| Enzyme 15 Number of Residues |
530 |
| Enzyme 15 Molecular Weight |
61096 |
| Enzyme 15 Theoretical pI |
8.73 |
| Enzyme 15 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Carbohydrate transport and metabolism |
| Enzyme 15 Specific Function |
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. The major substrates of this isozyme are eugenol > 4-methylumbelliferone > dihydrotestosterone (DHT) > androstane-3alpha,17beta-diol (3alpha-diol) > testosterone > androsterone (ADT) |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
3287473  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
O75795  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
UDB17_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1593 bp
ATGTCTCTGAAATGGATGTCAGTCTTTCTGCTGATGCAGCTCAGTTGTTACTTTAGCTCT
GGGAGTTGTGGAAAGGTGCTGGTGTGGCCCACAGAATACAGCCATTGGATAAATATGAAG
ACAATCCTGGAAGAGCTTGTTCAGAGGGGTCATGAGGTGATTGTGTTGACATCTTCGGCT
TCTATTCTTGTCAATGCCAGTAAATCATCTGCTATTAAATTAGAAGTTTATCCTACATCT
TTAACTAAAAATGATTTGGAAGATTTTTTTATGAAAATGTTCGATAGATGGACATATAGT
ATTTCAAAAAATACATTTTGGTCATATTTTTCACAACTACAAGAATTGTGTTGGGAATAT
TCTGACTATAATATAAAGCTCTGTGAAGATGCAGTTTTGAACAAGAAACTTATGAGAAAA
CTACAAGAGTCAAAATTTGATGTCCTTCTGGCAGATGCCGTTAATCCCTGTGGTGAGCTG
CTGGCTGAACTACTTAACATACCCTTTCTGTACAGTCTCCGCTTCTCTGTTGGCTACACA
GTTGAGAAGAATGGTGGAGGATTTCTGTTCCCTCCTTCCTATGTACCTGTTGTTATGTCA
GAATTAAGTGATCAAATGATTTTCATGGAGAGGATAAAAAATATGATATATATGCTTTAT
TTTGACTTTTGGTTTCAAGCATATGATCTGAAGAAGTGGGACCAGTTTTATAGTGAAGTT
CTAGGAAGACCCACTACATTATTTGAGACAATGGGGAAAGCTGAAATGTGGCTCATTCGA
ACCTATTGGGATTTTGAATTTCCTCGCCCATTCTTACCAAATGTTGATTTTGTTGGAGGA
CTTCACTGTAAACCAGCCAAACCCTTGCCTAAGGAAATGGAAGAGTTTGTGCAGAGCTCT
GGAGAAAATGGTATTGTGGTGTTTTCTCTGGGGTCGATGATCAGTAACATGTCAGAAGAA
AGTGCCAACATGATTGCATCAGCCCTTGCCCAGATCCCACAAAAGGTTCTATGGAGATTT
GATGGCAAGAAGCCAAATACTTTAGGTTCCAATACTCGACTGTATAAGTGGTTACCCCAG
AATGACCTTCTTGGTCATCCCAAAACCAAAGCTTTTATAACTCATGGTGGAACCAATGGC
ATCTATGAGGCGATCTACCATGGGATCCCTATGGTGGGCATTCCCTTGTTTGCGGATCAA
CATGATAACATTGCTCACATGAAAGCCAAGGGAGCAGCCCTCAGTGTGGACATCAGGACC
ATGTCAAGTAGAGATTTGCTCAATGCATTGAAGTCAGTCATTAATGACCCTATCTATAAA
GAGAATATCATGAAATTATCAAGAATTCATCATGATCAACCGGTGAAGCCCCTGGATCGA
GCAGTCTTCTGGATTGAGTTTGTCATGCGCCATAAAGGAGCCAAGCACCTTCGGGTCGCA
GCCCACAACCTCACCTGGATCCAGTACCACTCTTTGGATGTGATAGCATTCCTGCTGGCC
TGCGTGGCAACTATGATATTTATGATCACAAAATGTTGCCTGTTTTGTTTCCGAAAGCTT
GCCAAAACAGGAAAGAAGAAGAAAAGGGATTAG
|
| Enzyme 15 GenBank Gene ID |
U59209  |
| Enzyme 15 GeneCard ID |
UGT2B17  |
| Enzyme 15 GenAtlas ID |
UGT2B17  |
| Enzyme 15 HGNC ID |
HGNC:12547  |
| Enzyme 15 Chromosome Location |
Not Available |
| Enzyme 15 Locus |
Not Available |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Beaulieu M, Levesque E, Hum DW, Belanger A: Isolation and characterization of a novel cDNA encoding a human UDP-glucuronosyltransferase active on C19 steroids. J Biol Chem. 1996 Sep 13;271(37):22855-62. [PubMed
]
- Beaulieu M, Levesque E, Tchernof A, Beatty BG, Belanger A, Hum DW: Chromosomal localization, structure, and regulation of the UGT2B17 gene, encoding a C19 steroid metabolizing enzyme. DNA Cell Biol. 1997 Oct;16(10):1143-54. [PubMed
]
|
| Enzyme 15 Metabolite References |
- Beaulieu M, Levesque E, Tchernof A, Beatty BG, Belanger A, Hum DW: Chromosomal localization, structure, and regulation of the UGT2B17 gene, encoding a C19 steroid metabolizing enzyme. DNA Cell Biol. 1997 Oct;16(10):1143-54. [PubMed
]
|
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5732 |
| Enzyme 16 Name |
UDP-glucuronosyltransferase 1-6 precursor |
| Enzyme 16 Synonyms |
- UDP- glucuronosyltransferase 1A6
- UDPGT
- UGT1*6
- UGT1-06
- UGT1.6
- UGT- 1F
- UGT1F
- Phenol-metabolizing UDP-glucuronosyltransferase
|
| Enzyme 16 Gene Name |
UGT1A6 |
| Enzyme 16 Protein Sequence |
>UDP-glucuronosyltransferase 1-6 precursor
MACLLRSFQRISAGVFFLALWGMVVGDKLLVVPQDGSHWLSMKDIVEVLSDRGHEIVVVV
PEVNLLLKESKYYTRKIYPVPYDQEELKNRYQSFGNNHFAERSFLTAPQTEYRNNMIVIG
LYFINCQSLLQDRDTLNFFKESKFDALFTDPALPCGVILAEYLGLPSVYLFRGFPCSLEH
TFSRSPDPVSYIPRCYTKFSDHMTFSQRVANFLVNLLEPYLFYCLFSKYEELASAVLKRD
VDIITLYQKVSVWLLRYDFVLEYPRPVMPNMVFIGGINCKKRKDLSQEFEAYINASGEHG
IVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLL
GHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSE
DLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDL
TWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
|
| Enzyme 16 Number of Residues |
532 |
| Enzyme 16 Molecular Weight |
60751 |
| Enzyme 16 Theoretical pI |
8.55 |
| Enzyme 16 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 16 General Function |
Carbohydrate transport and metabolism |
| Enzyme 16 Specific Function |
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
340141  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P19224  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
UD16_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>861 bp
ATGGCCTGCCTCCTTCGCTCATTTCAGAGAATTTCTGCAGGGGTTTTCTTCTTAGCACTT
TGGGGCATGGTTGTAGGTGACAAGCTGCTGGTGGTCCCTCAGGACGGAAGCCACTGGCTT
AGTATGAAGGATATAGTTGAGGTTCTCAGTGACCGGGGTCATGAGATTGTAGTGGTGGTG
CCTGAAGTTAATTTGCTTTTGAAAGAATCCAAATACTACACAAGAAAAATCTATCCAGTG
CCGTATGACCAAGAAGAGCTGAAGAACCGTTACCAATCATTTGGAAACAATCACTTTGCT
GAGCGATCATTCCTAACTGCTCCTCAGACAGAGTACAGGAATAACATGATTGTTATTGGC
CTGTACTTCATCAACTGCCAGAGCCTCCTGCAGGACAGGGACACCCTGAACTTCTTTAAG
GAGAGCAAGTTTGATGCTCTTTTCACAGACCCAGCCTTACCCTGTGGGGTGATCCTGGCT
GAGTATTTGGGCCTACCATCTGTGTACCTCTTCAGGGGTTTTCCGTGTTCCCTGGAGCAT
ACATTCAGCAGAAGCCCAGACCCTGTGTCCTACATTCCCAGGTGCTACACAAAGTTTTCA
GACCACATGACTTTTTCCCAACGAGTGGCCAACTTCCTTGTTAATTTGTTGGAGCCCTAT
CTATTTTATTGTCTGTTTTCAAAGTATGAAGAACTCGCATCAGCTGTCCTCAAGAGAGAT
GTGGATATAATCACCTTATATCAGAAGGTCTCTGTTTGGCTGTTAAGATATGACTTTGTG
CTTGAATATCCTAGGCCGGTCATGCCCAACATGGTCTTCATTGGAGGTATCAACTGTAAG
AAGAGGAAAGACTTGTCTCAG
|
| Enzyme 16 GenBank Gene ID |
M84130  |
| Enzyme 16 GeneCard ID |
UGT1A6  |
| Enzyme 16 GenAtlas ID |
UGT1A6  |
| Enzyme 16 HGNC ID |
HGNC:12538  |
| Enzyme 16 Chromosome Location |
Not Available |
| Enzyme 16 Locus |
Not Available |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS: A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem. 1992 Feb 15;267(5):3257-61. [PubMed
]
- Harding D, Fournel-Gigleux S, Jackson MR, Burchell B: Cloning and substrate specificity of a human phenol UDP-glucuronosyltransferase expressed in COS-7 cells. Proc Natl Acad Sci U S A. 1988 Nov;85(22):8381-5. [PubMed
]
- Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [PubMed
]
- Munzel PA, Lehmkoster T, Bruck M, Ritter JK, Bock KW: Aryl hydrocarbon receptor-inducible or constitutive expression of human UDP glucuronosyltransferase UGT1A6. Arch Biochem Biophys. 1998 Feb 1;350(1):72-8. [PubMed
]
- Ciotti M, Marrone A, Potter C, Owens IS: Genetic polymorphism in the human UGT1A6 (planar phenol) UDP-glucuronosyltransferase: pharmacological implications. Pharmacogenetics. 1997 Dec;7(6):485-95. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5733 |
| Enzyme 17 Name |
UDP-glucuronosyltransferase 1-5 precursor |
| Enzyme 17 Synonyms |
- UDP- glucuronosyltransferase 1A5
- UDPGT
- UGT1*5
- UGT1-05
- UGT1.5
- UGT- 1E
- UGT1E
|
| Enzyme 17 Gene Name |
UGT1A5 |
| Enzyme 17 Protein Sequence |
>UDP-glucuronosyltransferase 1-5 precursor
MATGLQVPLPQLATGLLLLLSVQPWAESGKVLVVPTDGSHWLSMREALRDLHARGHQVVV
LTLEVNMYIKEENFFTLTTYAISWTQDEFDRLLLGHTQSFFETEHLLMKFSRRMAIMNNM
SLIIHRSCVELLHNEALIRHLHATSFDVVLTDPFHLCAAVLAKYLSIPAVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFLQRVKNMLYPLALSYLCHAVSAPYASLASELFQ
REVSVVDLVSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
|
| Enzyme 17 Number of Residues |
534 |
| Enzyme 17 Molecular Weight |
60072 |
| Enzyme 17 Theoretical pI |
8.14 |
| Enzyme 17 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 17 General Function |
Carbohydrate transport and metabolism |
| Enzyme 17 Specific Function |
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
340139  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P35504  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
UD15_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>867 bp
ATGGCCACAGGACTCCAGGTTCCCCTGCCGCAGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGGAAGGTGCTGGTGGTGCCCACTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGCCTTGCGGGACCTCCATGCGAGAGGCCACCAGGTGGTGGTC
CTCACCCTGGAGGTGAATATGTACATCAAAGAAGAGAACTTTTTCACCCTGACAACGTAT
GCCATTTCATGGACCCAGGACGAATTTGATCGCCTTTTGCTGGGTCACACTCAATCGTTC
TTTGAAACAGAACATCTTCTGATGAAATTTTCTAGAAGAATGGCAATTATGAACAATATG
TCTTTGATCATACATAGGTCTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGCATGCTACTTCCTTTGATGTGGTTCTAACAGACCCCTTTCACCTCTGCGCGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTCTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACCTTTGCCATGCTGTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGATTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAG
|
| Enzyme 17 GenBank Gene ID |
M84129  |
| Enzyme 17 GeneCard ID |
UGT1A5  |
| Enzyme 17 GenAtlas ID |
UGT1A5  |
| Enzyme 17 HGNC ID |
HGNC:12537  |
| Enzyme 17 Chromosome Location |
2 |
| Enzyme 17 Locus |
2q37 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Ritter JK, Chen F, Sheen YY, Tran HM, Kimura S, Yeatman MT, Owens IS: A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J Biol Chem. 1992 Feb 15;267(5):3257-61. [PubMed
]
- Gong QH, Cho JW, Huang T, Potter C, Gholami N, Basu NK, Kubota S, Carvalho S, Pennington MW, Owens IS, Popescu NC: Thirteen UDPglucuronosyltransferase genes are encoded at the human UGT1 gene complex locus. Pharmacogenetics. 2001 Jun;11(4):357-68. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5734 |
| Enzyme 18 Name |
UDP-glucuronosyltransferase 2B11 precursor |
| Enzyme 18 Synonyms |
- UDPGT
|
| Enzyme 18 Gene Name |
UGT2B11 |
| Enzyme 18 Protein Sequence |
>UDP-glucuronosyltransferase 2B11 precursor
MTLKWTSVLLLIHLSCYFSSGSCGKVLVWAAEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDASTLKFEVYPTSLTKTEFENIIMQQVKRWSDIRKDSFWLYFSQEQEILWELY
DIFRNFCKDVVSNKKVMKKLQESRFDIVFADAVFPCGELLAALLNIRFVYSLRFTPGYTI
ERHSGGLIFPPSYIPIVMSKLSDQMTFMERVKNMIYVLYFDFWFQMSDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNVDFVGGFHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRLDFNTM
SSTDLLNALKTVINDPLYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMPHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLACVATVIFIITKFCLFCFWKFARKGKKGKRD
|
| Enzyme 18 Number of Residues |
529 |
| Enzyme 18 Molecular Weight |
61039 |
| Enzyme 18 Theoretical pI |
9.29 |
| Enzyme 18 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Carbohydrate transport and metabolism |
| Enzyme 18 Specific Function |
UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
3360273  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
O75310  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
UDB11_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1590 bp
ATGACTCTGAAATGGACTTCAGTTCTTCTGCTGATACATCTCAGTTGTTACTTTAGCTCT
GGGAGTTGTGGAAAAGTGCTGGTGTGGGCCGCAGAATACAGCCATTGGATGAATATGAAG
ACAATCCTGAAAGAGCTTGTTCAGAGAGGTCATGAGGTGACTGTACTGGCATCTTCAGCT
TCCATTCTTTTTGATCCCAATGATGCATCCACTCTTAAATTTGAAGTTTATCCTACATCT
TTAACTAAAACTGAATTTGAGAATATCATCATGCAACAGGTTAAGAGATGGTCAGACATT
CGAAAAGATAGCTTTTGGTTATATTTTTCACAAGAACAAGAAATCCTGTGGGAATTATAT
GACATATTTAGAAACTTCTGTAAAGATGTAGTTTCAAATAAGAAAGTTATGAAAAAACTA
CAAGAGTCAAGATTTGACATCGTTTTTGCAGATGCTGTTTTTCCCTGTGGTGAGCTGCTG
GCTGCGCTACTTAACATACGGTTTGTGTACAGTCTCCGCTTTACTCCTGGCTACACAATT
GAAAGGCACAGTGGAGGACTGATTTTCCCTCCTTCCTACATACCTATTGTTATGTCAAAA
TTAAGTGATCAAATGACTTTCATGGAGAGGGTAAAAAATATGATCTATGTGCTTTATTTT
GACTTTTGGTTCCAAATGTCTGATATGAAGAAGTGGGATCAGTTTTACAGTGAAGTTTTA
GGAAGACCCACTACCTTATTTGAGACAATGGGAAAAGCTGACATATGGCTTATGCGAAAC
TCCTGGAGTTTTCAATTTCCTCATCCATTCTTACCAAACGTTGATTTTGTTGGAGGATTC
CACTGCAAACCTGCCAAACCCCTACCTAAGGAAATGGAGGAGTTTGTACAGAGCTCTGGA
GAAAATGGTGTTGTGGTGTTTTCTCTGGGGTCAGTGATAAGTAACATGACAGCAGAAAGG
GCCAATGTAATTGCAACAGCCCTTGCCAAGATCCCACAAAAGGTTCTGTGGAGATTTGAC
GGGAATAAACCAGATGCCTTAGGTCTCAATACTCGGCTGTACAAGTGGATACCCCAGAAT
GACCTTCTAGGTCATCCAAAAACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATC
TATGAGGCAATCTACCATGGGATCCCTATGGTGGGCATTCCATTGTTTTTTGATCAACCT
GATAACATTGCTCACATGAAGGCCAAGGGAGCAGCTGTTAGATTGGACTTCAACACAATG
TCGAGTACAGACCTGCTGAATGCACTGAAGACAGTAATTAATGATCCTTTATATAAAGAG
AATATTATGAAATTATCAAGAATTCAACATGATCAACCAGTAAAGCCCCTGGATCGAGCA
GTCTTCTGGATTGAATTTGTCATGCCCCACAAAGGAGCCAAACACCTTCGAGTTGCAGCC
CATGACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGATTGGGTTTCTGCTGGCCTGT
GTGGCAACTGTGATATTTATCATCACAAAGTTTTGTCTGTTTTGTTTCTGGAAGTTTGCT
AGAAAAGGGAAGAAGGGAAAAAGAGATTAG
|
| Enzyme 18 GenBank Gene ID |
AF016492  |
| Enzyme 18 GeneCard ID |
UGT2B11  |
| Enzyme 18 GenAtlas ID |
UGT2B11  |
| Enzyme 18 HGNC ID |
HGNC:12545  |
| Enzyme 18 Chromosome Location |
4 |
| Enzyme 18 Locus |
4q13.2 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Beaulieu M, Levesque E, Hum DW, Belanger A: Isolation and characterization of a human orphan UDP-glucuronosyltransferase, UGT2B11. Biochem Biophys Res Commun. 1998 Jul 9;248(1):44-50. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
6947 |
| Enzyme 19 Name |
Androgen receptor |
| Enzyme 19 Synonyms |
- Dihydrotestosterone receptor
|
| Enzyme 19 Gene Name |
AR |
| Enzyme 19 Protein Sequence |
>Androgen receptor
MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLLQQQ
QQQQQQQQQQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSA
LECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLK
DILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDNAKELCKA
VSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKS
TEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSR
DYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGP
GSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGGGGGGGGGGGGEAGAVAPY
GYTRPPQGLAGQESDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLE
TARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRND
CTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETTQKLT
VSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAK
ALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRM
YSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDR
IIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIIS
VQVPKILSGKVKPIYFHTQ
|
| Enzyme 19 Number of Residues |
919 |
| Enzyme 19 Molecular Weight |
98990 |
| Enzyme 19 Theoretical pI |
6.38 |
| Enzyme 19 GO Classification |
| Function |
- DNA binding
- androgen receptor activity
- binding
- ligand-dependent nuclear receptor activity
- nucleic acid binding
- receptor activity
- signal transducer activity
- steroid binding
- steroid hormone receptor activity
- transcription factor activity
|
| Process |
- regulation of biological process
- regulation of cellular metabolism
- regulation of metabolism
- regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- regulation of physiological process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bound organelle
- membrane-bound organelle
- nucleus
- organelle
|
|
| Enzyme 19 General Function |
Not Available |
| Enzyme 19 Specific Function |
The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Activated, but not phosphorylated, by HIPK3 |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
Not Available |
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
178628  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
P10275  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
ANDR_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>2760 bp
ATGGAAGTGCAGTTAGGGCTGGGAAGGGTCTACCCTCGGCCGCCGTCCAAGACCTACCGA
GGAGCTTTCCAGAATCTGTTCCAGAGCGTGCGCGAAGTGATCCAGAACCCGGGCCCCAGG
CACCCAGAGGCCGCGAGCGCAGCACCTCCCGGCGCCAGTTTGCTGCTGCTGCAGCAGCAG
CAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAGCAAGAGACT
AGCCCCAGGCAGCAGCAGCAGCAGCAGGGTGAGGATGGTTCTCCCCAAGCCCATCGTAGA
GGCCCCACAGGCTACCTGGTCCTGGATGAGGAACAGCAACCTTCACAGCCGCAGTCGGCC
CTGGAGTGCCACCCCGAGAGAGGTTGCGTCCCAGAGCCTGGAGCCGCCGTGGCCGCCAGC
AAGGGGCTGCCGCAGCAGCTGCCAGCACCTCCGGACGAGGATGACTCAGCTGCCCCATCC
ACGTTGTCCCTGCTGGGCCCCACTTTCCCCGGCTTAAGCAGCTGCTCCGCTGACCTTAAA
GACATCCTGAGCGAGGCCAGCACCATGCAACTCCTTCAGCAACAGCAGCAGGAAGCAGTA
TCCGAAGGCAGCAGCAGCGGGAGAGCGAGGGAGGCCTCGGGGGCTCCCACTTCCTCCAAG
GACAATTACTTAGGGGGCACTTCGACCATTTCTGACAACGCCAAGGAGTTGTGTAAGGCA
GTGTCGGTGTCCATGGGCCTGGGTGTGGAGGCGTTGGAGCATCTGAGTCCAGGGGAACAG
CTTCGGGGGGATTGCATGTACGCCCCACTTTTGGGAGTTCCACCCGCTGTGCGTCCCACT
CCTTGTGCCCCATTGGCCGAATGCAAAGGTTCTCTGCTAGACGACAGCGCAGGCAAGAGC
ACTGAAGATACTGCTGAGTATTCCCCTTTCAAGGGAGGTTACACCAAAGGGCTAGAAGGC
GAGAGCCTAGGCTGCTCTGGCAGCGCTGCAGCAGGGAGCTCCGGGACACTTGAACTGCCG
TCTACCCTGTCTCTCTACAAGTCCGGAGCACTGGACGAGGCAGCTGCGTACCAGAGTCGC
GACTACTACAACTTTCCACTGGCTCTGGCCGGACCGCCGCCCCCTCCGCCGCCTCCCCAT
CCCCACGCTCGCATCAAGCTGGAGAACCCGCTGGACTACGGCAGCGCCTGGGCGGCTGCG
GCGGCGCAGTGCCGCTATGGGGACCTGGCGAGCCTGCATGGCGCGGGTGCAGCGGGACCC
GGTTCTGGGTCACCCTCAGCCGCCGCTTCCTCATCCTGGCACACTCTCTTCACAGCCGAA
GAAGGCCAGTTGTATGGACCGTGTGGTGGTGGTGGGGGTGGTGGCGGCGGCGGCGGCGGC
GGCGGCGGCGGCGGCGGCGGCGGCGGCGGCGGCGGCGAGGCGGGAGCTGTAGCCCCCTAC
GGCTACACTCGGCCCCCTCAGGGGCTGGCGGGCCAGGAAAGCGACTTCACCGCACCTGAT
GTGTGGTACCCTGGCGGCATGGTGAGCAGAGTGCCCTATCCCAGTCCCACTTGTGTCAAA
AGCGAAATGGGCCCCTGGATGGATAGCTACTCCGGACCTTACGGGGACATGCGTTTGGAG
ACTGCCAGGGACCATGTTTTGCCCATTGACTATTACTTTCCACCCCAGAAGACCTGCCTG
ATCTGTGGAGATGAAGCTTCTGGGTGTCACTATGGAGCTCTCACATGTGGAAGCTGCAAG
GTCTTCTTCAAAAGAGCCGCTGAAGGGAAACAGAAGTACCTGTGCGCCAGCAGAAATGAT
TGCACTATTGATAAATTCCGAAGGAAAAATTGTCCATCTTGTCGTCTTCGGAAATGTTAT
GAAGCAGGGATGACTCTGGGAGCCCGGAAGCTGAAGAAACTTGGTAATCTGAAACTACAG
GAGGAAGGAGAGGCTTCCAGCACCACCAGCCCCACTGAGGAGACAACCCAGAAGCTGACA
GTGTCACACATTGAAGGCTATGAATGTCAGCCCATCTTTCTGAATGTCCTGGAAGCCATT
GAGCCAGGTGTAGTGTGTGCTGGACACGACAACAACCAGCCCGACTCCTTTGCAGCCTTG
CTCTCTAGCCTCAATGAACTGGGAGAGAGACAGCTTGTACACGTGGTCAAGTGGGCCAAG
GCCTTGCCTGGCTTCCGCAACTTACACGTGGACGACCAGATGGCTGTCATTCAGTACTCC
TGGATGGGGCTCATGGTGTTTGCCATGGGCTGGCGATCCTTCACCAATGTCAACTCCAGG
ATGCTCTACTTCGCCCCTGATCTGGTTTTCAATGAGTACCGCATGCACAAGTCCCGGATG
TACAGCCAGTGTGTCCGAATGAGGCACCTCTCTCAAGAGTTTGGATGGCTCCAAATCACC
CCCCAGGAATTCCTGTGCATGAAAGCACTGCTACTCTTCAGCATTATTCCAGTGGATGGG
CTGAAAAATCAAAAATTCTTTGATGAACTTCGAATGAACTACATCAAGGAACTCGATCGT
ATCATTGCATGCAAAAGAAAAAATCCCACATCCTGCTCAAGACGCTTCTACCAGCTCACC
AAGCTCCTGGACTCCGTGCAGCCTATTGCGAGAGAGCTGCATCAGTTCACTTTTGACCTG
CTAATCAAGTCACACATGGTGAGCGTGGACTTTCCGGAAATGATGGCAGAGATCATCTCT
GTGCAAGTGCCCAAGATCCTTTCTGGGAAAGTCAAGCCCATCTATTTCCACACCCAGTGA
|
| Enzyme 19 GenBank Gene ID |
M20132  |
| Enzyme 19 GeneCard ID |
AR  |
| Enzyme 19 GenAtlas ID |
AR  |
| Enzyme 19 HGNC ID |
HGNC:644  |
| Enzyme 19 Chromosome Location |
X |
| Enzyme 19 Locus |
Xq11.2-q12 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Lubahn DB, Joseph DR, Sar M, Tan J, Higgs HN, Larson RE, French FS, Wilson EM: The human androgen receptor: complementary deoxyribonucleic acid cloning, sequence analysis and gene expression in prostate. Mol Endocrinol. 1988 Dec;2(12):1265-75. [PubMed
]
- Lubahn DB, Brown TR, Simental JA, Higgs HN, Migeon CJ, Wilson EM, French FS: Sequence of the intron/exon junctions of the coding region of the human androgen receptor gene and identification of a point mutation in a family with complete androgen insensitivity. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9534-8. [PubMed
]
- Govindan MV: Specific region in hormone binding domain is essential for hormone binding and trans-activation by human androgen receptor. Mol Endocrinol. 1990 Mar;4(3):417-27. [PubMed
]
- Chang CS, Kokontis J, Liao ST: Structural analysis of complementary DNA and amino acid sequences of human and rat androgen receptors. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7211-5. [PubMed
]
- Rao MA, Cheng H, Quayle AN, Nishitani H, Nelson CC, Rennie PS: RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor. J Biol Chem. 2002 Dec 13;277(50):48020-7. Epub 2002 Oct 1. [PubMed
]
- Tilley WD, Marcelli M, Wilson JD, McPhaul MJ: Characterization and expression of a cDNA encoding the human androgen receptor. Proc Natl Acad Sci U S A. 1989 Jan;86(1):327-31. [PubMed
]
- Marcelli M, Tilley WD, Wilson CM, Griffin JE, Wilson JD, McPhaul MJ: Definition of the human androgen receptor gene structure permits the identification of mutations that cause androgen resistance: premature termination of the receptor protein at amino acid residue 588 causes complete androgen resistance. Mol Endocrinol. 1990 Aug;4(8):1105-16. [PubMed
]
- Faber PW, Kuiper GG, van Rooij HC, van der Korput JA, Brinkmann AO, Trapman J: The N-terminal domain of the human androgen receptor is encoded by one, large exon. Mol Cell Endocrinol. 1989 Feb;61(2):257-62. [PubMed
]
- Chang CS, Kokontis J, Liao ST: Molecular cloning of human and rat complementary DNA encoding androgen receptors. Science. 1988 Apr 15;240(4850):324-6. [PubMed
]
- Trapman J, Klaassen P, Kuiper GG, van der Korput JA, Faber PW, van Rooij HC, Geurts van Kessel A, Voorhorst MM, Mulder E, Brinkmann AO: Cloning, structure and expression of a cDNA encoding the human androgen receptor. Biochem Biophys Res Commun. 1988 May 31;153(1):241-8. [PubMed
]
- Kuiper GG, Faber PW, van Rooij HC, van der Korput JA, Ris-Stalpers C, Klaassen P, Trapman J, Brinkmann AO: Structural organization of the human androgen receptor gene. J Mol Endocrinol. 1989 May;2(3):R1-4. [PubMed
]
- Lubahn DB, Joseph DR, Sullivan PM, Willard HF, French FS, Wilson EM: Cloning of human androgen receptor complementary DNA and localization to the X chromosome. Science. 1988 Apr 15;240(4850):327-30. [PubMed
]
- Ris-Stalpers C, Trifiro MA, Kuiper GG, Jenster G, Romalo G, Sai T, van Rooij HC, Kaufman M, Rosenfield RL, Liao S, et al.: Substitution of aspartic acid-686 by histidine or asparagine in the human androgen receptor leads to a functionally inactive protein with altered hormone-binding characteristics. Mol Endocrinol. 1991 Oct;5(10):1562-9. [PubMed
]
- Sleddens HF, Oostra BA, Brinkmann AO, Trapman J: Trinucleotide repeat polymorphism in the androgen receptor gene (AR). Nucleic Acids Res. 1992 Mar 25;20(6):1427. [PubMed
]
- Giovannucci E, Stampfer MJ, Krithivas K, Brown M, Dahl D, Brufsky A, Talcott J, Hennekens CH, Kantoff PW: The CAG repeat within the androgen receptor gene and its relationship to prostate cancer. Proc Natl Acad Sci U S A. 1997 Apr 1;94(7):3320-3. [PubMed
]
- Waragai M, Lammers CH, Takeuchi S, Imafuku I, Udagawa Y, Kanazawa I, Kawabata M, Mouradian MM, Okazawa H: PQBP-1, a novel polyglutamine tract-binding protein, inhibits transcription activation by Brn-2 and affects cell survival. Hum Mol Genet. 1999 Jun;8(6):977-87. [PubMed
]
- Hsiao PW, Lin DL, Nakao R, Chang C: The linkage of Kennedy's neuron disease to ARA24, the first identified androgen receptor polyglutamine region-associated coactivator. J Biol Chem. 1999 Jul 16;274(29):20229-34. [PubMed
]
- Oettgen P, Finger E, Sun Z, Akbarali Y, Thamrongsak U, Boltax J, Grall F, Dube A, Weiss A, Brown L, Quinn G, Kas K, Endress G, Kunsch C, Libermann TA: PDEF, a novel prostate epithelium-specific ets transcription factor, interacts with the androgen receptor and activates prostate-specific antigen gene expression. J Biol Chem. 2000 Jan 14;275(2):1216-25. [PubMed
]
- Sharma M, Zarnegar M, Li X, Lim B, Sun Z: Androgen receptor interacts with a novel MYST protein, HBO1. J Biol Chem. 2000 Nov 10;275(45):35200-8. [PubMed
]
- Wong CW, McNally C, Nickbarg E, Komm BS, Cheskis BJ: Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade. Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14783-8. Epub 2002 Nov 1. [PubMed
]
- Niki T, Takahashi-Niki K, Taira T, Iguchi-Ariga SM, Ariga H: DJBP: a novel DJ-1-binding protein, negatively regulates the androgen receptor by recruiting histone deacetylase complex, and DJ-1 antagonizes this inhibition by abrogation of this complex. Mol Cancer Res. 2003 Feb;1(4):247-61. [PubMed
]
- Matias PM, Donner P, Coelho R, Thomaz M, Peixoto C, Macedo S, Otto N, Joschko S, Scholz P, Wegg A, Basler S, Schafer M, Egner U, Carrondo MA: Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations. J Biol Chem. 2000 Aug 25;275(34):26164-71. [PubMed
]
- Matias PM, Carrondo MA, Coelho R, Thomaz M, Zhao XY, Wegg A, Crusius K, Egner U, Donner P: Structural basis for the glucocorticoid response in a mutant human androgen receptor (AR(ccr)) derived from an androgen-independent prostate cancer. J Med Chem. 2002 Mar 28;45(7):1439-46. [PubMed
]
- Pinsky L, Trifiro M, Kaufman M, Beitel LK, Mhatre A, Kazemi-Esfarjani P, Sabbaghian N, Lumbroso R, Alvarado C, Vasiliou M, et al.: Androgen resistance due to mutation of the androgen receptor. Clin Invest Med. 1992 Oct;15(5):456-72. [PubMed
]
- Brown TR, Scherer PA, Chang YT, Migeon CJ, Ghirri P, Murono K, Zhou Z: Molecular genetics of human androgen insensitivity. Eur J Pediatr. 1993;152 Suppl 2:S62-9. [PubMed
]
- Sultan C, Lumbroso S, Poujol N, Belon C, Boudon C, Lobaccaro JM: Mutations of androgen receptor gene in androgen insensitivity syndromes. J Steroid Biochem Mol Biol. 1993 Nov;46(5):519-30. [PubMed
]
- Patterson MN, Hughes IA, Gottlieb B, Pinsky L: The androgen receptor gene mutations database. Nucleic Acids Res. 1994 Sep;22(17):3560-2. [PubMed
]
- Brinkmann AO, Jenster G, Ris-Stalpers C, van der Korput JA, Bruggenwirth HT, Boehmer AL, Trapman J: Androgen receptor mutations. J Steroid Biochem Mol Biol. 1995 Jun;53(1-6):443-8. [PubMed
]
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- Melo KF, Latronico AC, Costa EM, Billerbeck AE, Mendonca BB, Arnhold IJ: A novel point mutation (R840S) in the androgen receptor in a Brazilian family with partial androgen insensitivity syndrome. Hum Mutat. 1999 Oct;14(4):353. [PubMed
]
- Gottlieb B, Vasiliou DM, Lumbroso R, Beitel LK, Pinsky L, Trifiro MA: Analysis of exon 1 mutations in the androgen receptor gene. Hum Mutat. 1999;14(6):527-39. [PubMed
]
- Chen CP, Chern SR, Wang TY, Wang W, Wang KL, Jeng CJ: Androgen receptor gene mutations in 46,XY females with germ cell tumours. Hum Reprod. 1999 Mar;14(3):664-70. [PubMed
]
- Kanayama H, Naroda T, Inoue Y, Kurokawa Y, Kagawa S: A case of complete testicular feminization: laparoscopic orchiectomy and analysis of androgen receptor gene mutation. Int J Urol. 1999 Jun;6(6):327-30. [PubMed
]
- Shkolny DL, Beitel LK, Ginsberg J, Pekeles G, Arbour L, Pinsky L, Trifiro MA: Discordant measures of androgen-binding kinetics in two mutant androgen receptors causing mild or partial androgen insensitivity, respectively. J Clin Endocrinol Metab. 1999 Feb;84(2):805-10. [PubMed
]
- Wallen MJ, Linja M, Kaartinen K, Schleutker J, Visakorpi T: Androgen receptor gene mutations in hormone-refractory prostate cancer. J Pathol. 1999 Dec;189(4):559-63. [PubMed
]
- Zhao XY, Boyle B, Krishnan AV, Navone NM, Peehl DM, Feldman D: Two mutations identified in the androgen receptor of the new human prostate cancer cell line MDA PCa 2a. J Urol. 1999 Dec;162(6):2192-9. [PubMed
]
- Ong YC, Wong HB, Adaikan G, Yong EL: Directed pharmacological therapy of ambiguous genitalia due to an androgen receptor gene mutation. Lancet. 1999 Oct 23;354(9188):1444-5. [PubMed
]
- Peters I, Weidemann W, Romalo G, Knorr D, Schweikert HU, Spindler KD: An androgen receptor mutation in the direct vicinity of the proposed C-terminal alpha-helix of the ligand binding domain containing the AF-2 transcriptional activating function core is associated with complete androgen insensitivity. Mol Cell Endocrinol. 1999 Feb 25;148(1-2):47-53. [PubMed
]
- Nazareth LV, Stenoien DL, Bingman WE 3rd, James AJ, Wu C, Zhang Y, Edwards DP, Mancini M, Marcelli M, Lamb DJ, Weigel NL: A C619Y mutation in the human androgen receptor causes inactivation and mislocalization of the receptor with concomitant sequestration of SRC-1 (steroid receptor coactivator 1) Mol Endocrinol. 1999 Dec;13(12):2065-75. [PubMed
]
- Holterhus PM, Wiebel J, Sinnecker GH, Bruggenwirth HT, Sippell WG, Brinkmann AO, Kruse K, Hiort O: Clinical and molecular spectrum of somatic mosaicism in androgen insensitivity syndrome. Pediatr Res. 1999 Dec;46(6):684-90. [PubMed
]
- Yaegashi N, Uehara S, Senoo M, Sato J, Fujiwara J, Funato T, Sasaki T, Yajima A: Point mutations in the steroid-binding domain of the androgen receptor gene of five Japanese patients with androgen insensitivity syndrome. Tohoku J Exp Med. 1999 Mar;187(3):263-72. [PubMed
]
- Nordenskjold A, Friedman E, Tapper-Persson M, Soderhall C, Leviav A, Svensson J, Anvret M: Screening for mutations in candidate genes for hypospadias. Urol Res. 1999;27(1):49-55. [PubMed
]
- Marcelli M, Ittmann M, Mariani S, Sutherland R, Nigam R, Murthy L, Zhao Y, DiConcini D, Puxeddu E, Esen A, Eastham J, Weigel NL, Lamb DJ: Androgen receptor mutations in prostate cancer. Cancer Res. 2000 Feb 15;60(4):944-9. [PubMed
]
- Ahmed SF, Cheng A, Dovey L, Hawkins JR, Martin H, Rowland J, Shimura N, Tait AD, Hughes IA: Phenotypic features, androgen receptor binding, and mutational analysis in 278 clinical cases reported as androgen insensitivity syndrome. J Clin Endocrinol Metab. 2000 Feb;85(2):658-65. [PubMed
]
- Chavez B, Mendez JP, Ulloa-Aguirre A, Larrea F, Vilchis F: Eight novel mutations of the androgen receptor gene in patients with androgen insensitivity syndrome. J Hum Genet. 2001;46(10):560-5. [PubMed
]
- Sills ES, Sholes TE, Perloe M, Kaplan CR, Davis JG, Tucker MJ: Characterization of a novel receptor mutation A-->T at exon 4 in complete androgen insensitivity syndrome and a carrier sibling via bidirectional polymorphism sequence analysis. Int J Mol Med. 2002 Jan;9(1):45-8. [PubMed
]
|
| Enzyme 19 Metabolite References |
- Peterziel H, Culig Z, Stober J, Hobisch A, Radmayr C, Bartsch G, Klocker H, Cato AC: Mutant androgen receptors in prostatic tumors distinguish between amino-acid-sequence requirements for transactivation and ligand binding. Int J Cancer. 1995 Nov 15;63(4):544-50. [PubMed
]
|
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
8106 |
| Enzyme 20 Name |
Dehydrogenase/reductase SDR family member 9 precursor |
| Enzyme 20 Synonyms |
- 3- alpha hydroxysteroid dehydrogenase
- 3alpha-HSD
- RDH-E2
- Short-chain dehydrogenase/reductase retSDR8
- NADP-dependent retinol dehydrogenase/reductase
- RDHL
|
| Enzyme 20 Gene Name |
DHRS9 |
| Enzyme 20 Protein Sequence |
>Dehydrogenase/reductase SDR family member 9 precursor
MLFWVLGLLILCGFLWTRKGKLKIEDITDKYIFITGCDSGFGNLAARTFDKKGFHVIAAC
LTESGSTALKAETSERLRTVLLDVTDPENVKRTAQWVKNQVGEKGLWGLINNAGVPGVLA
PTDWLTLEDYREPIEVNLFGLISVTLNMLPLVKKAQGRVINVSSVGGRLAIVGGGYTPSK
YAVEGFNDSLRRDMKAFGVHVSCIEPGLFKTNLADPVKVIEKKLAIWEQLSPDIKQQYGE
GYIEKSLDKLKGNKSYVNMDLSPVVECMDHALTSLFPKTHYAAGKDAKIFWIPLSHMPAA
LQDFLLLKQKAELANPKAV
|
| Enzyme 20 Number of Residues |
319 |
| Enzyme 20 Molecular Weight |
35227 |
| Enzyme 20 Theoretical pI |
8.89 |
| Enzyme 20 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 20 General Function |
Lipid transport and metabolism |
| Enzyme 20 Specific Function |
3-alpha-hydroxysteroid dehydrogenase that converts 3- alpha-tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and 3-alpha-androstanediol to dihydroxyprogesterone. May play a role in the biosynthesis of retinoic acid from retinaldehyde, but seems to have low activity with retinoids. Can utilize both NADH and NADPH |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
Not Available |
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
13649974  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q9BPW9  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
DHRS9_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>960 bp
ATGCTCTTTTGGGTGCTAGGCCTCCTAATCCTCTGTGGTTTTCTGTGGACTCGTAAAGGA
AAACTAAAGATTGAAGACATCACTGATAAGTACATTTTTATCACTGGATGTGACTCGGGC
TTTGGAAACTTGGCAGCCAGAACTTTTGATAAAAAGGGATTTCATGTAATCGCTGCCTGT
CTGACTGAATCAGGATCAACAGCTTTAAAGGCAGAAACCTCAGAGAGACTTCGTACTGTG
CTTCTGGATGTGACCGACCCAGAGAATGTCAAGAGGACTGCCCAGTGGGTGAAGAACCAA
GTTGGGGAGAAAGGTCTCTGGGGTCTGATCAATAATGCTGGTGTTCCCGGCGTGCTGGCT
CCCACTGACTGGCTGACACTAGAGGACTACAGAGAACCTATTGAAGTGAACCTGTTTGGA
CTCATCAGTGTGACACTAAATATGCTTCCTTTGGTCAAGAAAGCTCAAGGGAGAGTTATT
AATGTCTCCAGTGTTGGAGGTCGCCTTGCAATCGTTGGAGGGGGCTATACTCCATCCAAA
TATGCAGTGGAAGGTTTCAATGACAGCTTAAGACGGGACATGAAAGCTTTTGGTGTGCAC
GTCTCATGCATTGAACCAGGATTGTTCAAAACAAACTTGGCAGATCCAGTAAAGGTAATT
GAAAAAAAACTCGCCATTTGGGAGCAGCTGTCTCCAGACATCAAACAACAATATGGAGAA
GGTTACATTGAAAAAAGTCTAGACAAACTGAAAGGCAATAAATCCTATGTGAACATGGAC
CTCTCTCCGGTGGTAGAGTGCATGGACCACGCTCTAACAAGTCTCTTCCCTAAGACTCAT
TATGCCGCTGGAAAAGATGCCAAAATTTTCTGGATACCTCTGTCTCACATGCCAGCAGCT
TTGCAAGACTTTTTATTGTTGAAACAGAAAGCAGAGCTGGCTAATCCCAAGGCAGTGTGA
|
| Enzyme 20 GenBank Gene ID |
AF343729  |
| Enzyme 20 GeneCard ID |
DHRS9  |
| Enzyme 20 GenAtlas ID |
DHRS9  |
| Enzyme 20 HGNC ID |
HGNC:16888  |
| Enzyme 20 Chromosome Location |
2 |
| Enzyme 20 Locus |
2q31.1 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Chetyrkin SV, Belyaeva OV, Gough WH, Kedishvili NY: Characterization of a novel type of human microsomal 3alpha -hydroxysteroid dehydrogenase: unique tissue distribution and catalytic properties. J Biol Chem. 2001 Jun 22;276(25):22278-86. Epub 2001 Apr 9. [PubMed
]
- Soref CM, Di YP, Hayden L, Zhao YH, Satre MA, Wu R: Characterization of a novel airway epithelial cell-specific short chain alcohol dehydrogenase/reductase gene whose expression is up-regulated by retinoids and is involved in the metabolism of retinol. J Biol Chem. 2001 Jun 29;276(26):24194-202. Epub 2001 Apr 13. [PubMed
]
- Markova NG, Pinkas-Sarafova A, Karaman-Jurukovska N, Jurukovski V, Simon M: Expression pattern and biochemical characteristics of a major epidermal retinol dehydrogenase. Mol Genet Metab. 2003 Feb;78(2):119-35. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Haeseleer F, Palczewski K: Short-chain dehydrogenases/reductases in retina. Methods Enzymol. 2000;316:372-83. [PubMed
]
|
| Enzyme 20 Metabolite References |
- Klein J, Thomas H, Post K, Worner W, Oesch F: Dihydrodiol dehydrogenase activities of rabbit liver are associated with hydroxysteroid dehydrogenases and aldo-keto reductases. Eur J Biochem. 1992 May 1;205(3):1155-62. [PubMed
]
|
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
8526 |
| Enzyme 21 Name |
Sterol/retinol dehydrogenase |
| Enzyme 21 Synonyms |
Not Available |
| Enzyme 21 Gene Name |
Not Available |
| Enzyme 21 Protein Sequence |
>Sterol/retinol dehydrogenase
MWLYLAVFVGLYYLLHWYRERQVLSHLRDKYVFITGCDSGFGKLLARQLDARGLRVLAAC
LTEKGAEQLRGQTSDRLETVTLDVTKTESVAAAAQWVKECVRDKGLWGLVNNAGISLPTA
PNELLTKQDFVTILDVNLLGVIDVTLSLLPLVRKARGRVVNVSSVMGRVSLFGGGYCISK
YGVEAFSDSLRRELSYFGVKVAMIEPGYFKTAVTSKERFLKSFLEIWDRSSPEVKEAYGE
KFVADYKKSAEQMEQKCTQDLSLVTNCMEHALIACHPRTRYSAGWDAKLLYLPMSYMPTF
LVDAIMYWVSPSPAKAL
|
| Enzyme 21 Number of Residues |
317 |
| Enzyme 21 Molecular Weight |
35646 |
| Enzyme 21 Theoretical pI |
8.77 |
| Enzyme 21 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Lipid transport and metabolism |
| Enzyme 21 Specific Function |
Not Available |
| Enzyme 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
Not Available |
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
Not Available |
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
3372592  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
O75452  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
O75452_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>954 bp
ATGTGGCTCTACCTGGCGGTTTTCGTGGGCCTGTACTACCTTCTGCACTGGTACCGGGAG
AGGCAGGTGCTGAGCCACCTGAGAGATAAGTATGTGTTCATCACGGGCTGTGACTCTGGC
TTCGGGAAACTGCTGGCCAGACAGCTGGATGCACGAGGCTTGCGGGTGCTGGCTGCATGT
CTGACGGAGAAAGGAGCCGAGCAGCTGAGGGGCCAGACTTCAGACAGGCTGGAGACGGTG
ACCCTGGATGTTACCAAGACAGAGAGCGTTGCTGCAGCCGCCCAGTGGGTGAAGGAGTGC
GTGAGAGACAAAGGACTCTGGGGCCTGGTGAATAATGCTGGCATCTCCTTGCCCACGGCT
CCCAATGAGTTGCTCACCAAGCAGGACTTCGTGACCATACTGGACGTGAACTTGTTGGGG
GTGATTGATGTGACTCTGAGCCTGCTGCCCTTAGTGAGGAAGGCCAGGGGCCGTGTGGTC
AACGTCTCCAGTGTCATGGGCCGGGTGTCACTTTTTGGTGGAGGCTACTGCATCTCCAAG
TATGGCGTGGAAGCCTTCTCTGACTCCCTCAGGAGGGAACTCTCCTACTTTGGGGTGAAG
GTGGCTATGATTGAACCTGGCTATTTCAAGACTGCTGTGACCAGTAAGGAGAGATTCTTA
AAGAGCTTCCTGGAGATTTGGGACCGGTCCAGTCCAGAGGTCAAGGAGGCCTATGGCGAG
AAGTTTGTTGCAGACTATAAGAAATCAGCTGAACAAATGGAGCAGAAGTGCACACAGGAT
CTGTCGTTGGTGACCAACTGCATGGAGCATGCGCTGATTGCCTGCCACCCCCGTACTCGC
TACTCAGCTGGCTGGGATGCCAAGCTTCTCTACCTCCCCATGAGCTACATGCCCACCTTC
CTGGTGGATGCCATTATGTACTGGGTCTCTCCAAGCCCGGCCAAGGCTCTATGA
|
| Enzyme 21 GenBank Gene ID |
AF057034  |
| Enzyme 21 GeneCard ID |
Not Available |
| Enzyme 21 GenAtlas ID |
Not Available |
| Enzyme 21 HGNC ID |
HGNC:29674  |
| Enzyme 21 Chromosome Location |
Not Available |
| Enzyme 21 Locus |
Not Available |
| Enzyme 21 SNPs |
Not Available |
| Enzyme 21 General References |
- Gough WH, VanOoteghem S, Sint T, Kedishvili NY: cDNA cloning and characterization of a new human microsomal NAD+-dependent dehydrogenase that oxidizes all-trans-retinol and 3alpha-hydroxysteroids. J Biol Chem. 1998 Jul 31;273(31):19778-85. [PubMed
]
|
| Enzyme 21 Metabolite References |
- Karlsson T, Vahlquist A, Kedishvili N, Torma H: 13-cis-retinoic acid competitively inhibits 3 alpha-hydroxysteroid oxidation by retinol dehydrogenase RoDH-4: a mechanism for its anti-androgenic effects in sebaceous glands? Biochem Biophys Res Commun. 2003 Mar 28;303(1):273-8. [PubMed
]
|
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
12970 |
| Enzyme 22 Name |
UDP-glucuronosyltransferase 2A3 precursor |
| Enzyme 22 Synonyms |
Not Available |
| Enzyme 22 Gene Name |
UGT2A3 |
| Enzyme 22 Protein Sequence |
>UDP-glucuronosyltransferase 2A3 precursor
MRSDKSALVFLLLQLFCVGCGFCGKVLVWPCDMSHWLNVKVILEELIVRGHEVTVLTHSK
PSLIDYRKPSALKFEVVHMPQDRTEENEIFVDLALNVLPGLSTWQSVIKLNDFFVEIRGT
LKMMCESFIYNQTLMKKLQETNYDVMLIDPVIPCGDLMAELLAVPFVLTLRISVGGNMER
SCGKLPAPLSYVPVPMTGLTDRMTFLERVKNSMLSVLFHFWIQDYDYHFWEEFYSKALGR
PTTLCETVGKAEIWLIRTYWDFEFPQPYQPNFEFVGGLHCKPAKALPKEMENFVQSSGED
GIVVFSLGSLFQNVTEEKANIIASALAQIPQKVLWRYKGKKPSTLGANTRLYDWIPQNDL
LGHPKTKAFITHGGMNGIYEAIYHGVPMVGVPIFGDQLDNIAHMKAKGAAVEINFKTMTS
EDLLRALRTVITDSSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRSAAHD
LTWFQHYSIDVIGFLLTCVATAIFLFTKCFLFSCQKFNKTRKIEKRE
|
| Enzyme 22 Number of Residues |
527 |
| Enzyme 22 Molecular Weight |
60285 |
| Enzyme 22 Theoretical pI |
8.04 |
| Enzyme 22 GO Classification |
| Function |
- binding
- catalytic activity
- ion binding
- metal ion binding
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- cation transport
- cellular physiological process
- ion transport
- metabolism
- metal ion transport
- physiological process
- transport
|
| Component |
| — |
|
| Enzyme 22 General Function |
Carbohydrate transport and metabolism |
| Enzyme 22 Specific Function |
UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds |
| Enzyme 22 Pathways |
- Androgen and Estrogen Metabolism (map00150
)
- Metabolism of xenobiotics by cytochrome P450 (map00980
)
- Porphyrin Metabolism (map00860
)
- Starch and Sucrose Metabolism (map00500
)
|
| Enzyme 22 Reactions |
- UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383] ALL_REAC R01383 > R02358 R02389 R02478 R02502 R02902 R03091 R04352 R04353 R04354 R04683 R07106
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
44889644  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q6UWM9  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
UD2A3_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
Not Available |
| Enzyme 22 GenBank Gene ID |
AY542891  |
| Enzyme 22 GeneCard ID |
Q6UWM9  |
| Enzyme 22 GenAtlas ID |
UGT2A3  |
| Enzyme 22 HGNC ID |
HGNC:28528  |
| Enzyme 22 Chromosome Location |
Not Available |
| Enzyme 22 Locus |
Not Available |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
15056 |
| Enzyme 23 Name |
UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f) |
| Enzyme 23 Synonyms |
Not Available |
| Enzyme 23 Gene Name |
UGT1A10 |
| Enzyme 23 Protein Sequence |
>UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
MARAGWTSPVPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLERSLNCTVKTYSTSYTLEDQNREFMVFAHAQWKAQAQSIFSLLMSSSSGFLDLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDTCGLIVAKYFSLPSVVFTRGIFCHHLEEG
AQCPAPLSYVPNDLLGFSDAMTFKERVWNHIVHLEDHLFCQYLFRNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
|
| Enzyme 23 Number of Residues |
530 |
| Enzyme 23 Molecular Weight |
59810 |
| Enzyme 23 Theoretical pI |
7.31 |
| Enzyme 23 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 23 General Function |
Carbohydrate transport and metabolism |
| Enzyme 23 Specific Function |
Not Available |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
Not Available |
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
40849852  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q5DT02  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
Q5DT02_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>1593 bp
ATGGCTCGCGCAGGGTGGACCAGCCCCGTTCCTTTATGTGTGTGTCTACTGCTGACCTGT
GGCTTTGCCGAGGCAGGGAAGCTGCTGGTAGTGCCCATGGATGGGAGTCACTGGTTCACC
ATGCAGTCGGTGGTGGAGAAACTTATCCTCAGGGGGCATGAGGTGGTTGTAGTCATGCCA
GAGGTGAGTTGGCAACTGGAAAGATCACTGAATTGCACAGTGAAGACTTACTCAACCTCG
TACACTCTGGAAGATCAGAACCGGGAATTCATGGTTTTCGCCCATGCTCAATGGAAAGCA
CAGGCACAAAGTATATTTTCTCTATTAATGAGTTCATCCAGTGGTTTTCTTGACTTATTT
TTTTCGCATTGCAGGAGTTTGTTTAATGACCGAAAATTAGTAGAATACTTAAAGGAGAGT
TCTTTTGATGCAGTGTTTCTGGATCCTTTTGATACCTGTGGCTTAATTGTTGCTAAATAT
TTCTCCCTCCCCTCTGTGGTCTTCACCAGGGGAATATTTTGCCACCATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAATGATCTCTTAGGGTTCTCAGATGCC
ATGACTTTCAAGGAGAGAGTATGGAACCACATCGTGCACTTGGAGGACCATTTATTTTGC
CAGTATCTTTTTAGAAATGCCCTAGAAATAGCCTCTGAAATTCTCCAAACCCCTGTCACG
GCATATGATCTCTACAGTCACACATCAATTTGGTTGTTGCGAACGGACTTTGTTTTGGAC
TATCCCAAACCCGTGATGCCCAACATGATCTTCATTGGTGGTATCAACTGTCATCAGGGA
AAGCCATTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATCG
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAAGATTTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACAGTGGCC
TTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
|
| Enzyme 23 GenBank Gene ID |
AY435137  |
| Enzyme 23 GeneCard ID |
Q5DT02  |
| Enzyme 23 GenAtlas ID |
UGT1A10  |
| Enzyme 23 HGNC ID |
HGNC:12531  |
| Enzyme 23 Chromosome Location |
Not Available |
| Enzyme 23 Locus |
Not Available |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
Not Available |
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
15057 |
| Enzyme 24 Name |
UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e) |
| Enzyme 24 Synonyms |
Not Available |
| Enzyme 24 Gene Name |
UGT1A8 |
| Enzyme 24 Protein Sequence |
>UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
MARTGWTSPIPLCVSLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGKSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVRSLFSLFLSSSNGFFNLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
|
| Enzyme 24 Number of Residues |
530 |
| Enzyme 24 Molecular Weight |
59742 |
| Enzyme 24 Theoretical pI |
7.73 |
| Enzyme 24 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 24 General Function |
Carbohydrate transport and metabolism |
| Enzyme 24 Specific Function |
Not Available |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
Not Available |
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
40849864  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q5DSZ6  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
Q5DSZ6_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>1593 bp
ATGGCTCGCACAGGGTGGACCAGCCCCATTCCCCTATGTGTTTCTCTGCTGCTGACCTGT
GGCTTTGCTGAGGCAGGGAAGCTGCTGGTAGTGCCCATGGATGGGAGTCACTGGTTCACC
ATGCAGTCGGTGGTGGAGAAACTTATCCTCAGGGGGCATGAGGTGGTTGTAGTCATGCCA
GAGGTGAGTTGGCAACTGGGAAAATCACTGAATTGCACAGTGAAGACTTACTCAACCTCA
TACACTCTGGAGGATCTGGACCGGGAATTCATGGATTTCGCCGATGCTCAATGGAAAGCA
CAAGTACGAAGTTTGTTTTCTCTATTTCTGAGTTCATCCAATGGTTTTTTTAACTTATTT
TTTTCGCATTGCAGGAGTTTGTTTAATGACCGAAAATTAGTAGAATACTTAAAGGAGAGT
TCTTTTGATGCGGTGTTTCTTGATCCTTTTGATGCCTGTGGCTTAATTGTTGCCAAATAT
TTCTCCCTCCCCTCTGTGGTCTTCGCCAGGGGAATAGCTTGCCACTATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAGAATTCTCTTAGGGTTCTCAGATGCC
ATGACTTTCAAGGAGAGAGTACGGAACCACATCATGCACTTGGAGGAACATTTATTTTGC
CAGTATTTTTCCAAAAATGCCCTAGAAATAGCCTCTGAAATTCTCCAAACACCTGTCACA
GCATATGATCTCTACAGCCACACATCAATTTGGTTGTTGCGAACAGACTTTGTTTTGGAC
TATCCCAAACCCGTGATGCCCAATATGATCTTCATTGGTGGTATCAACTGCCATCAGGGA
AAGCCATTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATCG
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAAGATTTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACAGTGGCC
TTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
|
| Enzyme 24 GenBank Gene ID |
AY435143  |
| Enzyme 24 GeneCard ID |
Q5DSZ6  |
| Enzyme 24 GenAtlas ID |
UGT1A8  |
| Enzyme 24 HGNC ID |
HGNC:12540  |
| Enzyme 24 Chromosome Location |
Not Available |
| Enzyme 24 Locus |
Not Available |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
Not Available |
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
15058 |
| Enzyme 25 Name |
UDP glycosyltransferase 1 family polypeptide A7 |
| Enzyme 25 Synonyms |
Not Available |
| Enzyme 25 Gene Name |
UGT1A7 |
| Enzyme 25 Protein Sequence |
>UDP glycosyltransferase 1 family polypeptide A7
MARAGWTGLLPLYVCLLLTCGFAKAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDQDREFMVFADARWTAPLRSAFSLLTSSSNGIFDLF
FSNCRSLFNDRKLVEYLKESCFDAVFLDPFDACGLIVAKYFSLPSVVFARGIFCHYLEEG
AQCPAPLSYVPRLLLGFSDAMTFKERVWNHIMHLEEHLFCPYFFKNVLEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLEYPKPVMPNMIFIGGINCHQGKPVPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
|
| Enzyme 25 Number of Residues |
530 |
| Enzyme 25 Molecular Weight |
59819 |
| Enzyme 25 Theoretical pI |
7.85 |
| Enzyme 25 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 25 General Function |
Carbohydrate transport and metabolism |
| Enzyme 25 Specific Function |
Not Available |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
Not Available |
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
40849862  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q5DSZ7  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
Q5DSZ7_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1593 bp
ATGGCTCGTGCAGGGTGGACTGGCCTCCTTCCCCTATATGTGTGTCTACTGCTGACCTGT
GGCTTTGCCAAGGCAGGGAAGCTGCTGGTAGTGCCCATGGATGGGAGCCACTGGTTCACC
ATGCAGTCGGTGGTGGAGAAACTCATCCTCAGGGGGCATGAGGTGGTCGTAGTCATGCCA
GAGGTGAGTTGGCAACTGGGAAGATCACTGAATTGCACAGTGAAGACTTACTCAACCTCA
TACACTCTGGAGGATCAGGACCGGGAGTTCATGGTTTTTGCCGATGCTCGCTGGACGGCA
CCATTGCGAAGTGCATTTTCTCTATTAACAAGTTCATCCAATGGTATTTTTGACTTATTT
TTTTCAAATTGCAGGAGTTTGTTTAATGACCGAAAATTAGTAGAATACTTAAAGGAGAGT
TGTTTTGATGCAGTGTTTCTCGATCCTTTTGATGCCTGTGGCTTAATTGTTGCCAAATAT
TTCTCCCTCCCCTCTGTGGTCTTCGCCAGGGGAATATTTTGCCACTATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAGACTTCTCTTAGGGTTCTCAGACGCC
ATGACTTTCAAGGAGAGAGTATGGAACCACATCATGCACTTGGAGGAACATTTATTTTGC
CCCTATTTTTTCAAAAATGTCTTAGAAATAGCCTCTGAAATTCTCCAAACCCCTGTCACG
GCATATGATCTCTACAGCCACACATCAATTTGGTTGTTGCGAACTGACTTTGTTTTGGAG
TATCCCAAACCCGTGATGCCCAATATGATCTTCATTGGTGGTATCAACTGTCATCAGGGA
AAGCCAGTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATCG
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAAGATTTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACAGTGGCC
TTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
|
| Enzyme 25 GenBank Gene ID |
AY435142  |
| Enzyme 25 GeneCard ID |
Q5DSZ7  |
| Enzyme 25 GenAtlas ID |
UGT1A7  |
| Enzyme 25 HGNC ID |
HGNC:12539  |
| Enzyme 25 Chromosome Location |
Not Available |
| Enzyme 25 Locus |
Not Available |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
Not Available |
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
15059 |
| Enzyme 26 Name |
cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b) |
| Enzyme 26 Synonyms |
Not Available |
| Enzyme 26 Gene Name |
UGT2B10 |
| Enzyme 26 Protein Sequence |
>cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b)
MALKWTTVLLIQLSFYFSSGSCGKVLVWAAEYSLWMNMKTILKELVQRGHEVTVLASSAS
ILFDPNDSSTLKLEVYPTSLTKTEFENIIMQLVKRLSEIQKDTFWLPFSQEQEILWAIND
IIRNFCKDVVSNKKLMKKLQESRFDIVFADAYLPCGELLAELFNIPFVYSHSFSPGYSFE
RHSGGFIFPPSYVPVVMSKLSDQMTFMERVKNMLYVLYFDFWFQIFNMKKWDQFYSEVLG
RPTTLSETMRKADIWLMRNSWNFKFPHPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGE
NGVVVFSLGSMVSNMTEERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQND
LLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRVDFNTMS
STDLLNALKTVINDPSYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAH
NLTWFQYHSLDVIGFLLACVATVLFIITKCCLFCFWKFARKGKKGKRD
|
| Enzyme 26 Number of Residues |
528 |
| Enzyme 26 Molecular Weight |
60775 |
| Enzyme 26 Theoretical pI |
9.40 |
| Enzyme 26 GO Classification |
Not Available |
| Enzyme 26 General Function |
Carbohydrate transport and metabolism |
| Enzyme 26 Specific Function |
Not Available |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
Not Available |
| Enzyme 26 Pfam Domain Function |
Not Available |
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
158258913  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
A8K9M3  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
A8K9M3_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>1587 bp
ATGGCTCTGAAATGGACTACAGTTCTGCTGATACAACTCAGTTTTTACTTTAGCTCTGGG
AGTTGTGGAAAGGTGCTGGTATGGGCCGCAGAATACAGCCTTTGGATGAATATGAAGACA
ATCCTGAAAGAACTTGTTCAGAGAGGTCATGAGGTGACTGTACTGGCATCTTCAGCTTCC
ATTCTTTTTGATCCCAACGACTCATCCACTCTTAAACTTGAAGTTTATCCTACATCTTTA
ACTAAAACTGAATTTGAGAATATCATCATGCAATTGGTTAAGAGATTGTCAGAAATTCAA
AAAGATACATTTTGGTTACCTTTTTCACAAGAACAAGAAATCCTGTGGGCAATTAATGAC
ATAATTAGAAACTTCTGTAAAGATGTAGTTTCAAATAAGAAACTTATGAAAAAACTACAA
GAGTCAAGATTTGACATCGTTTTTGCAGATGCTTATTTACCCTGTGGTGAGCTGCTGGCT
GAGCTATTTAACATACCCTTTGTGTACAGTCACAGCTTCAGTCCTGGCTACTCATTTGAA
AGGCACAGTGGAGGATTTATTTTCCCTCCTTCCTACGTACCTGTTGTTATGTCAAAATTA
AGTGATCAAATGACTTTCATGGAGAGGGTAAAAAATATGCTCTATGTGCTTTATTTTGAC
TTTTGGTTCCAAATATTTAATATGAAGAAGTGGGATCAGTTTTACAGTGAAGTTTTAGGA
AGACCCACTACATTATCTGAGACAATGAGGAAAGCTGACATATGGCTTATGCGAAACTCC
TGGAATTTTAAATTTCCTCATCCATTCTTACCAAATGTTGATTTTGTTGGAGGACTCCAC
TGCAAACCTGCCAAACCCCTACCTAAGGAAATGGAGGAGTTTGTACAGAGCTCTGGAGAA
AATGGTGTTGTGGTGTTTTCTCTGGGGTCAATGGTCAGTAACATGACAGAAGAAAGGGCC
AACGTAATTGCAACAGCCCTTGCCAAGATCCCACAAAAGGTTCTTTGGAGATTTGATGGG
AATAAACCAGATGCCTTAGGTCTCAATACTCGACTGTACAAGTGGATACCCCAGAATGAC
CTTCTAGGTCATCCAAAAACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATCTAT
GAGGCAATCTACCATGGGATCCCTATGGTGGGCATTCCATTGTTTTTTGATCAACCTGAT
AATATTGCTCACATGAAGGCCAAGGGAGCAGCTGTTAGAGTGGACTTCAACACAATGTCG
AGTACAGACCTGCTGAATGCACTGAAGACAGTAATTAATGATCCTTCATATAAAGAGAAT
ATTATGAAATTATCAAGAATTCAACATGATCAACCAGTGAAGCCCCTGGATCGAGCAGTC
TTCTGGATTGAATTTGTCATGCGCCACAAAGGAGCCAAACATCTTCGAGTTGCAGCCCAC
AACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGATTGGGTTCCTGCTGGCTTGTGTG
GCAACCGTGCTATTTATCATCACAAAGTGTTGTCTGTTTTGTTTCTGGAAGTTTGCTAGA
AAAGGAAAGAAGGGAAAAAGGGATTAG
|
| Enzyme 26 GenBank Gene ID |
AK292738  |
| Enzyme 26 GeneCard ID |
A8K9M3  |
| Enzyme 26 GenAtlas ID |
Not Available |
| Enzyme 26 HGNC ID |
Not Available |
| Enzyme 26 Chromosome Location |
Not Available |
| Enzyme 26 Locus |
Not Available |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
Not Available |
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
16420 |
| Enzyme 27 Name |
cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA |
| Enzyme 27 Synonyms |
Not Available |
| Enzyme 27 Gene Name |
Not Available |
| Enzyme 27 Protein Sequence |
>cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
MSVKWTSVILLIQLSFCFSSGNCGKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSA
SILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRWSDLPKDTFWLYFSQVQEIMSIFG
DITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTF
EKHSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSEVL
GRPTTLSETMGKADVWLIRNSWNFQFPYPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSG
ENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFADQPDNIAHMKARGAAVRVDFNTM
SSTDLLNALKRVINDPSYKENVMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLVCVATVIFIVTKCCLFCFWKFARKAKKGKND
|
| Enzyme 27 Number of Residues |
529 |
| Enzyme 27 Molecular Weight |
60721 |
| Enzyme 27 Theoretical pI |
8.45 |
| Enzyme 27 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 27 General Function |
Carbohydrate transport and metabolism |
| Enzyme 27 Specific Function |
Not Available |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
Not Available |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
B2R810  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
B2R810_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
Not Available |
| Enzyme 27 GenBank Gene ID |
AK313190  |
| Enzyme 27 GeneCard ID |
B2R810  |
| Enzyme 27 GenAtlas ID |
Not Available |
| Enzyme 27 HGNC ID |
Not Available |
| Enzyme 27 Chromosome Location |
Not Available |
| Enzyme 27 Locus |
Not Available |
| Enzyme 27 SNPs |
Not Available |
| Enzyme 27 General References |
Not Available |
| Enzyme 27 Metabolite References |
Not Available |