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Human Metabolome Database Version 2.5

 

Showing metabocard for Bilirubin diglucuronide (HMDB03325)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2006-07-26 11:28:39
Update Date 2009-05-21 16:32:18
Accession Number HMDB03325
Secondary Accession Numbers HMDB06518
Common Name Bilirubin diglucuronide
Description Bilirubin diglucuronide is a water soluble version of bilirubin. Conversion of bilirubin IX-alpha to a water-soluble form by disruption of the hydrogen bonds is essential for elimination by the liver and kidney. This is achieved by glucuronic acid conjugation of the propionic acid side chains of bilirubin. Bilirubin glucuronides are water-soluble and are readily excreted in bile. Bilirubin is primarily excreted in normal human bile as diglucuronide; unconjugated bilirubin accounts for only 1-4% of pigments in normal bile.
Synonyms
  1. (2S,3S,4S,5R,6S)-6-[3-[2-[[3-[2-[(2S,3R,4S,5S,6S)-6-carboxy-3,4,5-trihydroxy-oxan-2-yl]oxycarbonylethyl]-5-[(E)-(3-ethenyl-4-methyl-5-oxo-pyrrol-2-ylidene)methyl]-4-methyl-1H-pyrrol-2-yl]methyl]-5-[(E)-(4-ethenyl-3-methyl-5-oxo-pyrrol-2-ylidene)methyl]-4-methyl-1H-pyrrol-3-yl]propanoyloxy]-3,4,5-trihydroxy-oxane-2-carboxylate
  2. (2S,3S,4S,5R,6S)-6-[3-[2-[[3-[2-[(2S,3R,4S,5S,6S)-6-carboxy-3,4,5-trihydroxy-oxan-2-yl]oxycarbonylethyl]-5-[(E)-(3-ethenyl-4-methyl-5-oxo-pyrrol-2-ylidene)methyl]-4-methyl-1H-pyrrol-2-yl]methyl]-5-[(E)-(4-ethenyl-3-methyl-5-oxo-pyrrol-2-ylidene)methyl]-4-methyl-1H-pyrrol-3-yl]propanoyloxy]-3,4,5-trihydroxy-oxane-2-carboxylic acid
  3. Bilirubin-bisglucuronoside
  4. Bilirubin beta-diglucuronide
  5. bis(glucosyluronic acid)bilirubin
Chemical IUPAC Name (2S,3S,4S,5R,6S)-6-[3-[2-[[3-[2-[(2S,3R,4S,5S,6S)-6-carboxy-3,4,5-trihydroxy-oxan-2-yl]oxycarbonylethyl]-5-[(E)-(3-ethenyl-4-methyl-5-oxo-pyrrol-2-ylidene)methyl]-4-methyl-1H-pyrrol-2-yl]methyl]-5-[(E)-(4-ethenyl-3-methyl-5-oxo-pyrrol-2-ylidene)methyl]-4-methyl-1H-pyrrol-3-yl]propanoyloxy]-3,4,5-trihydroxy-oxane-2-carboxylic acid
Chemical Formula C45H52N4O18
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Carbohydrates and Carbohydrate conjugates
Class
  • Glucuronides
Sub Class
  • Fatty acid glucuronides
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • carboxylic acid
  • carboxylic acid ester
  • oxo(het)arene
  • alkene
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Waste products
Application
—
Source
  • Endogenous
Average Molecular Weight 936.910
Monoisotopic Molecular Weight 936.327637
Isomeric SMILES CC1=C(C=C)C(NC1=O)=C/C1=C(C)C(CCC(=O)O[C@@H]2O[C@@H]([C@@H](O)[C@H](O)[C@H]2O)C(O)=O)=C(CC2=C(CCC(=O)O[C@@H]3O[C@@H]([C@@H](O)[C@H](O)[C@H]3O)C(O)=O)C(C)=C(N2)C=C2NC(=O)C(C=C)=C2C)N1
Canonical SMILES CC1=C(C=C)C(NC1=O)=CC1=C(C)C(CCC(=O)OC2OC(C(O)C(O)C2O)C(O)=O)=C(CC2=C(CCC(=O)OC3OC(C(O)C(O)C3O)C(O)=O)C(C)=C(N2)C=C2NC(=O)C(C=C)=C2C)N1
KEGG Compound ID C05787 Link Image
BioCyc ID BILIRUBIN-BISGLUCURONOSIDE Link Image
BiGG ID 46500 Link Image
Wikipedia Link Bilirubin diglucuronide Link Image
NuGOwiki Link HMDB03325 Link Image
Metagene Link HMDB03325 Link Image
METLIN ID 6883 Link Image
PubChem Compound 5459911 Link Image
PubChem Substance 8143785 Link Image
ChEBI ID 18392 Link Image
CAS Registry Number 17459-92-6
InChI Identifier InChI=1/C45H52N4O18/c1-7-20-19(6)40(58)49-27(20)14-25-18(5)23(10-12-31(51)65-45-37(57)33(53)35(55)39(67-45)43(62)63)29(47-25)15-28-22(17(4)24(46-28)13-26-16(3)21(8-2)41(59)48-26)9-11-30(50)64-44-36(56)32(52)34(54)38(66-44)42(60)61/h7-8,13-14,32-39,44-47,52-57H,1-2,9-12,15H2,3-6H3,(H,48,59)(H,49,58)(H,60,61)(H,62,63)/b26-13+,27-14+/t32-,33-,34-,35-,36+,37+,38-,39-,44+,45+/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 0.126 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity 1.32 [Predicted by ALOGPS]; -0.782 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Porphyrin Metabolism SMP00024 Link Image map00860 Link Image
General References
  1. Mshelia DS, Buba AA: Point of care testing: a delight or a dilemma in the developing world?: an overview. Niger Postgrad Med J. 2005 Jun;12(2):136-9. [PubMed Link Image]
  2. Luo J, Lim CK: Isolation and characterization of new porphyrin metabolites in human porphyria cutanea tarda and in rats treated with hexachlorobenzene by HPTLC, HPLC and liquid secondary ion mass spectrometry. Biomed Chromatogr. 1995 May-Jun;9(3):113-22. [PubMed Link Image]
  3. Fevery J, Blanckaert N, Leroy P, Michiels R, Heirwegh KP: Analysis of bilirubins in biological fluids by extraction and thin-layer chromatography of the intact tetrapyrroles: application to bile of patients with Gilbert's syndrome, hemolysis, or cholelithiasis. Hepatology. 1983 Mar-Apr;3(2):177-83. [PubMed Link Image]
  4. Chowdhury JR, Chowdhury NR, Wu G, Shouval R, Arias IM: Bilirubin mono- and diglucuronide formation by human liver in vitro: assay by high-pressure liquid chromatography. Hepatology. 1981 Nov-Dec;1(6):622-7. [PubMed Link Image]
  5. Goresky CA, Gordon ER, Hinchey EJ, Fried GM: Bilirubin conjugate changes in the bile of gallbladders containing gallstones. Hepatology. 1995 Feb;21(2):373-82. [PubMed Link Image]
  6. Wikipedia Link Image
Metabolic Enzymes
  1. UDP-glucuronosyltransferase 2B28 precursor
  2. UDP-glucuronosyltransferase 2B4 precursor
  3. UDP-glucuronosyltransferase 1-4 precursor
  4. UDP-glucuronosyltransferase 2B15 precursor
  5. UDP-glucuronosyltransferase 2A1 precursor
  6. UDP-glucuronosyltransferase 1-1 precursor
  7. UDP-glucuronosyltransferase 1-9 precursor
  8. UDP-glucuronosyltransferase 1-3 precursor
  9. UDP-glucuronosyltransferase 2B17 precursor
  10. UDP-glucuronosyltransferase 1-6 precursor
  11. UDP-glucuronosyltransferase 1-5 precursor
  12. UDP-glucuronosyltransferase 2B11 precursor
  13. Beta-glucuronidase precursor
  14. UDP-glucuronosyltransferase 2A3 precursor
  15. UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
  16. UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
  17. UDP glycosyltransferase 1 family polypeptide A7
  18. cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b)
  19. cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
Enzyme 1 [top]
Enzyme 1 ID 5687
Enzyme 1 Name UDP-glucuronosyltransferase 2B28 precursor
Enzyme 1 Synonyms
  1. UDPGT
Enzyme 1 Gene Name UGT2B28
Enzyme 1 Protein Sequence >UDP-glucuronosyltransferase 2B28 precursor 
MALKWTSVLLLIHLGCYFSSGSCGKVLVWTGEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDAFTLKLEVYPTSLTKTEFENIIMQQVKRWSDIQKDSFWLYFSQEQEILWEFH
DIFRNFCKDVVSNKKVMKKLQESRFDIIFADAFFPCGELLAALLNIPFVYSLCFTPGYTI
ERHSGGLIFPPSYIPVVMSKLSDQMTFMERVKNMIYVLYFDFWFQMCDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNIDFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGLPKTRAFITHGGANGIYEAIYHGIPMVGIPLFWDQPDNIAHMKAKGAAVRLDFHTM
SSTDLLNALKTVINDPSYKENVMKLSIIQHDQPVKPLHRAVFWIEFVMCHKGAKHLRVAA
RDLTWFQYHSLDVIGFLLACVATVIFVVTKFCLFCFWKFARKGKKGKRD
Enzyme 1 Number of Residues 529
Enzyme 1 Molecular Weight 60907
Enzyme 1 Theoretical pI 8.80
Enzyme 1 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 1 General Function Carbohydrate transport and metabolism
Enzyme 1 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 1 Pathways
Enzyme 1 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-24
Enzyme 1 Transmembrane Regions
  • 495-517
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 13603476 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9BY64 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name UDB28_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 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 1 GenBank Gene ID AF177272 Link Image
Enzyme 1 GeneCard ID UGT2B28 Link Image
Enzyme 1 GenAtlas ID UGT2B28 Link Image
Enzyme 1 HGNC ID HGNC:13479 Link Image
Enzyme 1 Chromosome Location 4
Enzyme 1 Locus 4q13.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. 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 Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5696
Enzyme 2 Name UDP-glucuronosyltransferase 2B4 precursor
Enzyme 2 Synonyms
  1. UDPGT
  2. Hyodeoxycholic acid
  3. HLUG25
  4. UDPGTh-1
Enzyme 2 Gene Name UGT2B4
Enzyme 2 Protein Sequence >UDP-glucuronosyltransferase 2B4 precursor 
MSMKWTSALLLIQLSCYFSSGSCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLASSA
SISFDPNSPSTLKFEVYPVSLTKTEFEDIIKQLVKRWAELPKDTFWSYFSQVQEIMWTFN
DILRKFCKDIVSNKKLMKKLQESRFDVVLADAVFPFGELLAELLKIPFVYSLRFSPGYAI
EKHSGGLLFPPSYVPVVMSELSDQMTFIERVKNMIYVLYFEFWFQIFDMKKWDQFYSEVL
GRPTTLSETMAKADIWLIRNYWDFQFPHPLLPNVEFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSMVSNTSEERANVIASALAKIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGVPLFADQPDNIAHMKAKGAAVSLDFHTM
SSTDLLNALKTVINDPLYKENAMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVTGFLLACVATVIFIITKCLFCVWKFVRTGKKGKRD
Enzyme 2 Number of Residues 528
Enzyme 2 Molecular Weight 60513
Enzyme 2 Theoretical pI 8.75
Enzyme 2 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 2 General Function Carbohydrate transport and metabolism
Enzyme 2 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 2 Pathways
Enzyme 2 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • 1-23
Enzyme 2 Transmembrane Regions
  • 493-509
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 37589 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P06133 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name UDB4_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID Y00317 Link Image
Enzyme 2 GeneCard ID UGT2B4 Link Image
Enzyme 2 GenAtlas ID UGT2B4 Link Image
Enzyme 2 HGNC ID HGNC:12553 Link Image
Enzyme 2 Chromosome Location 4
Enzyme 2 Locus 4q13
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5719
Enzyme 3 Name UDP-glucuronosyltransferase 1-4 precursor
Enzyme 3 Synonyms
  1. UDP- glucuronosyltransferase 1A4
  2. UDPGT
  3. UGT1*4
  4. UGT1-04
  5. UGT1.4
  6. UGT- 1D
  7. UGT1D
  8. Bilirubin-specific UDPGT isozyme 2
  9. HUG-BR2
Enzyme 3 Gene Name UGT1A4
Enzyme 3 Protein Sequence >UDP-glucuronosyltransferase 1-4 precursor 
MARGLQVPLPRLATGLLLLLSVQPWAESGKVLVVPTDGSPWLSMREALRELHARGHQAVV
LTPEVNMHIKEEKFFTLTAYAVPWTQKEFDRVTLGYTQGFFETEHLLKRYSRSMAIMNNV
SLALHRCCVELLHNEALIRHLNATSFDVVLTDPVNLCGAVLAKYLSIPAVFFWRYIPCDL
DFKGTQCPNPSSYIPKLLTTNSDHMTFLQRVKNMLYPLALSYICHTFSAPYASLASELFQ
REVSVVDLVSYASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 3 Number of Residues 534
Enzyme 3 Molecular Weight 60026
Enzyme 3 Theoretical pI 8.68
Enzyme 3 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 3 General Function Carbohydrate transport and metabolism
Enzyme 3 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 3 Pathways
Enzyme 3 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-28
Enzyme 3 Transmembrane Regions
  • 492-508
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 340137 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID P22310 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name UD14_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >867 bp 
ATGGCCAGAGGACTCCAGGTTCCCCTGCCGCGGCTGGCCACAGGACTGCTGCTCCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGAAAGGTGTTGGTGGTGCCCACTGATGGCAGCCCC
TGGCTCAGCATGCGGGAGGCCTTGCGGGAGCTCCATGCCAGAGGCCACCAGGCGGTGGTC
CTCACCCCAGAGGTGAATATGCACATCAAAGAAGAGAAATTTTTCACCCTGACAGCCTAT
GCTGTTCCATGGACCCAGAAGGAATTTGATCGCGTTACGCTGGGCTACACTCAAGGGTTC
TTTGAAACAGAACATCTTCTGAAGAGATATTCTAGAAGTATGGCAATTATGAACAATGTA
TCTTTGGCCCTTCATAGGTGTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGAATGCTACTTCCTTTGATGTGGTTTTAACAGACCCCGTTAACCTCTGTGGGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTTTGGAGGTACATTCCATGTGACTTA
GACTTTAAGGGCACACAGTGTCCAAATCCTTCCTCCTATATTCCTAAGTTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACATTTGCCATACTTTTTCTGCCCCTTATGCAAGTCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCTATGCATCCGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGACTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAG
Enzyme 3 GenBank Gene ID M84128 Link Image
Enzyme 3 GeneCard ID UGT1A4 Link Image
Enzyme 3 GenAtlas ID UGT1A4 Link Image
Enzyme 3 HGNC ID HGNC:12536 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2q37
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
Enzyme 3 Metabolite References
  1. Meunier CJ, Verbeeck RK: Glucuronidation of R- and S-ketoprofen, acetaminophen, and diflunisal by liver microsomes of adjuvant-induced arthritic rats. Drug Metab Dispos. 1999 Jan;27(1):26-31. [PubMed Link Image]
Enzyme 4 [top]
Enzyme 4 ID 5722
Enzyme 4 Name UDP-glucuronosyltransferase 2B15 precursor
Enzyme 4 Synonyms
  1. UDPGT
  2. UDPGTh-3
  3. HLUG4
Enzyme 4 Gene Name UGT2B15
Enzyme 4 Protein Sequence >UDP-glucuronosyltransferase 2B15 precursor 
MSLKWTSVFLLIQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVTVLTSSA
STLVNASKSSAIKLEVYPTSLTKNDLEDSLLKILDRWIYGVSKNTFWSYFSQLQELCWEY
YDYSNKLCKDAVLNKKLMMKLQESKFDVILADALNPCGELLAELFNIPFLYSLRFSVGYT
FEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIHMLYFDFWFQIYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPVYKENVMKLSRIHHDQPMKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATVIFIITKFCLFCFRKLAKKGKKKKRD
Enzyme 4 Number of Residues 530
Enzyme 4 Molecular Weight 60989
Enzyme 4 Theoretical pI 9.04
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Carbohydrate transport and metabolism
Enzyme 4 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 4 Pathways
Enzyme 4 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • 1-23
Enzyme 4 Transmembrane Regions
  • 495-515
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 23955933 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P54855 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name UDB15_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 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 4 GenBank Gene ID AF548389 Link Image
Enzyme 4 GeneCard ID UGT2B15 Link Image
Enzyme 4 GenAtlas ID UGT2B15 Link Image
Enzyme 4 HGNC ID HGNC:12546 Link Image
Enzyme 4 Chromosome Location 4
Enzyme 4 Locus 4q13
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5724
Enzyme 5 Name UDP-glucuronosyltransferase 2A1 precursor
Enzyme 5 Synonyms Not Available
Enzyme 5 Gene Name UGT2A1
Enzyme 5 Protein Sequence >UDP-glucuronosyltransferase 2A1 precursor 
MLNNLLLFSLQISLIGTTLGGNVLIWPMEGSHWLNVKIIIDELIKKEHNVTVLVASGALF
ITPTSNPSLTFEIYKVPFGKERIEGVIKDFVSTWLENRPSPSTIWRFYQEMAKVIKDFHM
VSQEICDGVLKNQQLMAKLKKSKFEVLVSDPVFPCGDIVALKLGIPFMYSLRFSPASTVE
KHCGKVPYPPSYVPAVLSELTDQMSFTDRIRNFISYHLQDYMFETLWKSWDSYYSKALGR
PTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKEMEEFIQSSGKN
GVVVFSLGSMVKNLTEEKANLIASALAQIPQKVLWRYKGKKPATLGNNTQLFDWIPQNDL
LGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMFADQPDNIAHMKAKGAAVEVNLNTMTS
VDLLSALRTVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHD
LTWFQYHSLDVIGFLLVCVTTAIFLVIQCCLFSCQKFGKIGKKKKRE
Enzyme 5 Number of Residues 527
Enzyme 5 Molecular Weight 59873
Enzyme 5 Theoretical pI 9.29
Enzyme 5 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 5 General Function Carbohydrate transport and metabolism
Enzyme 5 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 5 Pathways
Enzyme 5 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-20
Enzyme 5 Transmembrane Regions
  • 491-507
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 4753766 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q9Y4X1 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name UDA1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 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 5 GenBank Gene ID AJ006054 Link Image
Enzyme 5 GeneCard ID UGT2A1 Link Image
Enzyme 5 GenAtlas ID UGT2A1 Link Image
Enzyme 5 HGNC ID HGNC:12542 Link Image
Enzyme 5 Chromosome Location 4
Enzyme 5 Locus 4q13
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. 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 Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5725
Enzyme 6 Name UDP-glucuronosyltransferase 1-1 precursor
Enzyme 6 Synonyms
  1. UDP- glucuronosyltransferase 1A1
  2. UDPGT
  3. UGT1*1
  4. UGT1-01
  5. UGT1.1
  6. UGT- 1A
  7. UGT1A
  8. Bilirubin-specific UDPGT isozyme 1
  9. HUG-BR1
Enzyme 6 Gene Name UGT1A1
Enzyme 6 Protein Sequence >UDP-glucuronosyltransferase 1-1 precursor 
MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVL
APDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDS
AMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLE
FEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQR
EVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEH
GIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDL
LGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTS
EDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHD
LTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 6 Number of Residues 533
Enzyme 6 Molecular Weight 59592
Enzyme 6 Theoretical pI 8.09
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 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 6 Pathways
Enzyme 6 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • 1-25
Enzyme 6 Transmembrane Regions
  • 491-507
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 184473 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P22309 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name UD11_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 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 6 GenBank Gene ID M57899 Link Image
Enzyme 6 GeneCard ID UGT1A1 Link Image
Enzyme 6 GenAtlas ID UGT1A1 Link Image
Enzyme 6 HGNC ID HGNC:12530 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 2q37
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
  6. 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 Link Image]
  7. 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 Link Image]
  8. 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 Link Image]
  9. 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 Link Image]
  10. 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 Link Image]
  11. 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 Link Image]
  12. 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 Link Image]
Enzyme 6 Metabolite References
  1. Meunier CJ, Verbeeck RK: Glucuronidation of R- and S-ketoprofen, acetaminophen, and diflunisal by liver microsomes of adjuvant-induced arthritic rats. Drug Metab Dispos. 1999 Jan;27(1):26-31. [PubMed Link Image]
Enzyme 7 [top]
Enzyme 7 ID 5726
Enzyme 7 Name UDP-glucuronosyltransferase 1-9 precursor
Enzyme 7 Synonyms
  1. UDP- glucuronosyltransferase 1A9
  2. UDPGT
  3. UGT1*9
  4. UGT1-9
  5. UGT1.9
  6. UGT- 1I
  7. UGT1I
  8. lugP4
Enzyme 7 Gene Name UGT1A9
Enzyme 7 Protein Sequence >UDP-glucuronosyltransferase 1-9 precursor 
MACTGWTSPLPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMRSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDLDREFKAFAHAQWKAQVRSIYSLLMGSYNDIFDLF
FSNCRSLFKDKKLVEYLKESSFDAVFLDPFDNCGLIVAKYFSLPSVVFARGILCHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLLCHRFFKNALEIASEILQTPVT
EYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 7 Number of Residues 530
Enzyme 7 Molecular Weight 59942
Enzyme 7 Theoretical pI 7.96
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 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 7 Pathways
Enzyme 7 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-25
Enzyme 7 Transmembrane Regions
  • 488-504
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 7690346 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID O60656 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name UD19_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID S55985 Link Image
Enzyme 7 GeneCard ID UGT1A9 Link Image
Enzyme 7 GenAtlas ID UGT1A9 Link Image
Enzyme 7 HGNC ID HGNC:12541 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5728
Enzyme 8 Name UDP-glucuronosyltransferase 1-3 precursor
Enzyme 8 Synonyms
  1. UDP- glucuronosyltransferase 1A3
  2. UDPGT
  3. UGT1*3
  4. UGT1-03
  5. UGT1.3
  6. UGT- 1C
  7. UGT1C
Enzyme 8 Gene Name UGT1A3
Enzyme 8 Protein Sequence >UDP-glucuronosyltransferase 1-3 precursor 
MATGLQVPLPWLATGLLLLLSVQPWAESGKVLVVPIDGSHWLSMREVLRELHARGHQAVV
LTPEVNMHIKEENFFTLTTYAISWTQDEFDRHVLGHTQLYFETEHFLKKFFRSMAMLNNM
SLVYHRSCVELLHNEALIRHLNATSFDVVLTDPVNLCAAVLAKYLSIPTVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFMQRVKNMLYPLALSYICHAFSAPYASLASELFQ
REVSVVDILSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANRKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 8 Number of Residues 534
Enzyme 8 Molecular Weight 60339
Enzyme 8 Theoretical pI 8.28
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
Enzyme 8 Pathways
Enzyme 8 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-28
Enzyme 8 Transmembrane Regions
  • 492-508
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 340135 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P35503 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name UD13_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >867 bp 
ATGGCCACAGGACTCCAGGTTCCCCTGCCGTGGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGAAAGGTGTTGGTGGTGCCCATTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGTCTTGCGGGAGCTCCATGCCAGAGGCCACCAGGCAGTGGTC
CTCACCCCAGAGGTGAATATGCACATCAAAGAAGAGAACTTTTTCACCCTGACAACCTAT
GCCATTTCGTGGACCCAGGATGAATTTGATCGCCATGTGCTGGGCCACACTCAACTGTAC
TTTGAAACAGAACATTTTCTGAAGAAATTTTTCAGAAGTATGGCAATGTTGAACAATATG
TCTTTGGTCTATCATAGGTCTTGTGTGGAGCTACTACATAATGAGGCCCTGATCAGGCAC
CTGAATGCTACTTCCTTTGATGTGGTTTTAACAGACCCCGTTAACCTCTGCGCGGCAGTG
CTGGCTAAGTACCTGTCGATTCCTACTGTGTTTTTTTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACAACC
AATTCAGACCACATGACATTCATGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACATTTGCCATGCTTTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATATTCTCAGTCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGACTACCCCAGGCCAATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACAGGAAGCCACTATCTCAG
Enzyme 8 GenBank Gene ID M84127 Link Image
Enzyme 8 GeneCard ID UGT1A3 Link Image
Enzyme 8 GenAtlas ID UGT1A3 Link Image
Enzyme 8 HGNC ID HGNC:12535 Link Image
Enzyme 8 Chromosome Location 2
Enzyme 8 Locus 2q37
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5731
Enzyme 9 Name UDP-glucuronosyltransferase 2B17 precursor
Enzyme 9 Synonyms
  1. UDPGT
  2. C19- steroid-specific UDP-glucuronosyltransferase
Enzyme 9 Gene Name UGT2B17
Enzyme 9 Protein Sequence >UDP-glucuronosyltransferase 2B17 precursor 
MSLKWMSVFLLMQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSA
SILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEY
SDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYT
VEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPIYKENIMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATMIFMITKCCLFCFRKLAKTGKKKKRD
Enzyme 9 Number of Residues 530
Enzyme 9 Molecular Weight 61096
Enzyme 9 Theoretical pI 8.73
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 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 9 Pathways
Enzyme 9 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-23
Enzyme 9 Transmembrane Regions
  • 495-515
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 3287473 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID O75795 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name UDB17_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 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 9 GenBank Gene ID U59209 Link Image
Enzyme 9 GeneCard ID UGT2B17 Link Image
Enzyme 9 GenAtlas ID UGT2B17 Link Image
Enzyme 9 HGNC ID HGNC:12547 Link Image
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5732
Enzyme 10 Name UDP-glucuronosyltransferase 1-6 precursor
Enzyme 10 Synonyms
  1. UDP- glucuronosyltransferase 1A6
  2. UDPGT
  3. UGT1*6
  4. UGT1-06
  5. UGT1.6
  6. UGT- 1F
  7. UGT1F
  8. Phenol-metabolizing UDP-glucuronosyltransferase
Enzyme 10 Gene Name UGT1A6
Enzyme 10 Protein Sequence >UDP-glucuronosyltransferase 1-6 precursor 
MACLLRSFQRISAGVFFLALWGMVVGDKLLVVPQDGSHWLSMKDIVEVLSDRGHEIVVVV
PEVNLLLKESKYYTRKIYPVPYDQEELKNRYQSFGNNHFAERSFLTAPQTEYRNNMIVIG
LYFINCQSLLQDRDTLNFFKESKFDALFTDPALPCGVILAEYLGLPSVYLFRGFPCSLEH
TFSRSPDPVSYIPRCYTKFSDHMTFSQRVANFLVNLLEPYLFYCLFSKYEELASAVLKRD
VDIITLYQKVSVWLLRYDFVLEYPRPVMPNMVFIGGINCKKRKDLSQEFEAYINASGEHG
IVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLL
GHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSE
DLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDL
TWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 10 Number of Residues 532
Enzyme 10 Molecular Weight 60751
Enzyme 10 Theoretical pI 8.55
Enzyme 10 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 10 General Function Carbohydrate transport and metabolism
Enzyme 10 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 10 Pathways
Enzyme 10 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-26
Enzyme 10 Transmembrane Regions
  • 490-506
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 340141 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID P19224 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name UD16_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >861 bp 
ATGGCCTGCCTCCTTCGCTCATTTCAGAGAATTTCTGCAGGGGTTTTCTTCTTAGCACTT
TGGGGCATGGTTGTAGGTGACAAGCTGCTGGTGGTCCCTCAGGACGGAAGCCACTGGCTT
AGTATGAAGGATATAGTTGAGGTTCTCAGTGACCGGGGTCATGAGATTGTAGTGGTGGTG
CCTGAAGTTAATTTGCTTTTGAAAGAATCCAAATACTACACAAGAAAAATCTATCCAGTG
CCGTATGACCAAGAAGAGCTGAAGAACCGTTACCAATCATTTGGAAACAATCACTTTGCT
GAGCGATCATTCCTAACTGCTCCTCAGACAGAGTACAGGAATAACATGATTGTTATTGGC
CTGTACTTCATCAACTGCCAGAGCCTCCTGCAGGACAGGGACACCCTGAACTTCTTTAAG
GAGAGCAAGTTTGATGCTCTTTTCACAGACCCAGCCTTACCCTGTGGGGTGATCCTGGCT
GAGTATTTGGGCCTACCATCTGTGTACCTCTTCAGGGGTTTTCCGTGTTCCCTGGAGCAT
ACATTCAGCAGAAGCCCAGACCCTGTGTCCTACATTCCCAGGTGCTACACAAAGTTTTCA
GACCACATGACTTTTTCCCAACGAGTGGCCAACTTCCTTGTTAATTTGTTGGAGCCCTAT
CTATTTTATTGTCTGTTTTCAAAGTATGAAGAACTCGCATCAGCTGTCCTCAAGAGAGAT
GTGGATATAATCACCTTATATCAGAAGGTCTCTGTTTGGCTGTTAAGATATGACTTTGTG
CTTGAATATCCTAGGCCGGTCATGCCCAACATGGTCTTCATTGGAGGTATCAACTGTAAG
AAGAGGAAAGACTTGTCTCAG
Enzyme 10 GenBank Gene ID M84130 Link Image
Enzyme 10 GeneCard ID UGT1A6 Link Image
Enzyme 10 GenAtlas ID UGT1A6 Link Image
Enzyme 10 HGNC ID HGNC:12538 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References
  1. 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 Link Image]
  2. 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 Link Image]
  3. 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 Link Image]
  4. 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 Link Image]
  5. 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 Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5733
Enzyme 11 Name UDP-glucuronosyltransferase 1-5 precursor
Enzyme 11 Synonyms
  1. UDP- glucuronosyltransferase 1A5
  2. UDPGT
  3. UGT1*5
  4. UGT1-05
  5. UGT1.5
  6. UGT- 1E
  7. UGT1E
Enzyme 11 Gene Name UGT1A5
Enzyme 11 Protein Sequence >UDP-glucuronosyltransferase 1-5 precursor 
MATGLQVPLPQLATGLLLLLSVQPWAESGKVLVVPTDGSHWLSMREALRDLHARGHQVVV
LTLEVNMYIKEENFFTLTTYAISWTQDEFDRLLLGHTQSFFETEHLLMKFSRRMAIMNNM
SLIIHRSCVELLHNEALIRHLHATSFDVVLTDPFHLCAAVLAKYLSIPAVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFLQRVKNMLYPLALSYLCHAVSAPYASLASELFQ
REVSVVDLVSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 11 Number of Residues 534
Enzyme 11 Molecular Weight 60072
Enzyme 11 Theoretical pI 8.14
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
Enzyme 11 Pathways
Enzyme 11 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-28
Enzyme 11 Transmembrane Regions
  • 492-508
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 340139 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P35504 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name UD15_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >867 bp 
ATGGCCACAGGACTCCAGGTTCCCCTGCCGCAGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGGAAGGTGCTGGTGGTGCCCACTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGCCTTGCGGGACCTCCATGCGAGAGGCCACCAGGTGGTGGTC
CTCACCCTGGAGGTGAATATGTACATCAAAGAAGAGAACTTTTTCACCCTGACAACGTAT
GCCATTTCATGGACCCAGGACGAATTTGATCGCCTTTTGCTGGGTCACACTCAATCGTTC
TTTGAAACAGAACATCTTCTGATGAAATTTTCTAGAAGAATGGCAATTATGAACAATATG
TCTTTGATCATACATAGGTCTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGCATGCTACTTCCTTTGATGTGGTTCTAACAGACCCCTTTCACCTCTGCGCGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTCTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACCTTTGCCATGCTGTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGATTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAG
Enzyme 11 GenBank Gene ID M84129 Link Image
Enzyme 11 GeneCard ID UGT1A5 Link Image
Enzyme 11 GenAtlas ID UGT1A5 Link Image
Enzyme 11 HGNC ID HGNC:12537 Link Image
Enzyme 11 Chromosome Location 2
Enzyme 11 Locus 2q37
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. 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 Link Image]
  2. 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 Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5734
Enzyme 12 Name UDP-glucuronosyltransferase 2B11 precursor
Enzyme 12 Synonyms
  1. UDPGT
Enzyme 12 Gene Name UGT2B11
Enzyme 12 Protein Sequence >UDP-glucuronosyltransferase 2B11 precursor 
MTLKWTSVLLLIHLSCYFSSGSCGKVLVWAAEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDASTLKFEVYPTSLTKTEFENIIMQQVKRWSDIRKDSFWLYFSQEQEILWELY
DIFRNFCKDVVSNKKVMKKLQESRFDIVFADAVFPCGELLAALLNIRFVYSLRFTPGYTI
ERHSGGLIFPPSYIPIVMSKLSDQMTFMERVKNMIYVLYFDFWFQMSDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNVDFVGGFHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRLDFNTM
SSTDLLNALKTVINDPLYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMPHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLACVATVIFIITKFCLFCFWKFARKGKKGKRD
Enzyme 12 Number of Residues 529
Enzyme 12 Molecular Weight 61039
Enzyme 12 Theoretical pI 9.29
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
Enzyme 12 Pathways
Enzyme 12 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-21
Enzyme 12 Transmembrane Regions
  • 493-513
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 3360273 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID O75310 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name UDB11_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 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 12 GenBank Gene ID AF016492 Link Image
Enzyme 12 GeneCard ID UGT2B11 Link Image
Enzyme 12 GenAtlas ID UGT2B11 Link Image
Enzyme 12 HGNC ID HGNC:12545 Link Image
Enzyme 12 Chromosome Location 4
Enzyme 12 Locus 4q13.2
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. 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 Link Image]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 6120
Enzyme 13 Name Beta-glucuronidase precursor
Enzyme 13 Synonyms
  1. Beta-G1
Enzyme 13 Gene Name GUSB
Enzyme 13 Protein Sequence >Beta-glucuronidase precursor 
MARGSAVAWAALGPLLWGCALGLQGGMLYPQESPSRECKELDGLWSFRADFSDNRRRGFE
EQWYRRPLWESGPTVDMPVPSSFNDISQDWRLRHFVGWVWYEREVILPERWTQDLRTRVV
LRIGSAHSYAIVWVNGVDTLEHEGGYLPFEADISNLVQVGPLPSRLRITIAINNTLTPTT
LPPGTIQYLTDTSKYPKGYFVQNTYFDFFNYAGLQRSVLLYTTPTTYIDDITVTTSVEQD
SGLVNYQISVKGSNLFKLEVRLLDAENKVVANGTGTQGQLKVPGVSLWWPYLMHERPAYL
YSLEVQLTAQTSLGPVSDFYTLPVGIRTVAVTKSQFLINGKPFYFHGVNKHEDADIRGKG
FDWPLLVKDFNLLRWLGANAFRTSHYPYAEEVMQMCDRYGIVVIDECPGVGLALPQFFNN
VSLHHHMQVMEEVVRRDKNHPAVVMWSVANEPASHLESAGYYLKMVIAHTKSLDPSRPVT
FVSNSNYAADKGAPYVDVICLNSYYSWYHDYGHLELIQLQLATQFENWYKKYQKPIIQSE
YGAETIAGFHQDPPLMFTEEYQKSLLEQYHLGLDQKRRKYVVGELIWNFADFMTEQSPTR
VLGNKKGIFTRQRQPKSAAFLLRERYWKIANETRYPHSVAKSQCLENSLFT
Enzyme 13 Number of Residues 651
Enzyme 13 Molecular Weight 74733
Enzyme 13 Theoretical pI 7.02
Enzyme 13 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • hydrolase activity, acting on glycosyl bonds
  • hydrolase activity, hydrolyzing O-glycosyl compounds
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
—
Enzyme 13 General Function Carbohydrate transport and metabolism
Enzyme 13 Specific Function Plays an important role in the degradation of dermatan and keratan sulfates
Enzyme 13 Pathways
Enzyme 13 Reactions
  • a beta-D-glucuronoside + H2O = D-glucuronate + an alcohol
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-22
Enzyme 13 Transmembrane Regions Not Available
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 183233 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P08236 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name BGLR_HUMAN Link Image
Enzyme 13 PDB ID 1BHG Link Image
Enzyme 13 PDB File Show
Enzyme 13 3D Structure
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1956 bp 
ATGGCCCGGGGGTCGGCGGTTGCCTGGGCGGCGCTCGGGCCGTTGTTGTGGGGCTGCGCG
CTGGGGCTGCAGGGCGGGATGCTGTACCCCCAGGAGAGCCCGTCGCGGGAGTGCAAGGAG
CTGGACGGCCTCTGGAGCTTCCGCGCCGACTTCTCTGACAACCGACGCCGGGGCTTCGAG
GAGCAGTGGTACCGGCGGCCGCTGTGGGAGTCAGGCCCCACCGTGGACATGCCAGTTCCC
TCCAGCTTCAATGACATCAGCCAGGACTGGCGTCTGCGGCATTTTGTCGGCTGGGTGTGG
TACGAACGGGAGGTGATCCTGCCGGAGCGATGGACCCAGGACCTGCGCACAAGAGTGGTG
CTGAGGATTGGCAGTGCCCATTCCTATGCCATCGTGTGGGTGAATGGGGTCGACACGCTA
GAGCATGAGGGGGGCTACCTCCCCTTCGAGGCCGACATCAGCAACCTGGTCCAGGTGGGG
CCCCTGCCCTCCCGGCTCCGAATCACTATCGCCATCAACAACACACTCACCCCCACCACC
CTGCCACCAGGGACCATCCAATACCTGACTGACACCTCCAAGTATCCCAAGGGTTACTTT
GTCCAGAACACATATTTTGACTTTTTCAACTACGCTGGACTGCAGCGGTCTGTACTTCTG
TACACGACACCCACCACCTACATCGATGACATCACCGTCACCACCAGCGTGGAGCAAGAC
AGTGGGCTGGTGAATTACCAGATCTCTGTCAAGGGCAGTAACCTGTTCAAGTTGGAAGTG
CGTCTTTTGGATGCAGAAAACAAAGTCGTGGCGAATGGGACTGGGACCCAGGGCCAACTT
AAGGTGCCAGGTGTCAGCCTCTGGTGGCCGTACCTGATGCACGAACGCCCTGCCTATCTG
TATTCATTGGAGGTGCAGCTGACTGCACAGACGTCACTGGGGCCTGTGTCTGACTTCTAC
ACACTCCCTGTGGGGATCCGCACTGTGGCTGTCACCAAGAGCCAGTTCCTCATCAATGGG
AAACCTTTCTATTTCCACGGTGTCAACAAGCATGAGGATGCGGACATCCGAGGGAAGGGC
TTCGACTGGCCGCTGCTGGTGAAGGACTTCAACCTGCTTCGCTGGCTTGGTGCCAACGCT
TTCCGTACCAGCCACTACCCCTATGCAGAGGAAGTGATGCAGATGTGTGACCGCTATGGG
ATTGTGGTCATCGATGAGTGTCCCGGCGTGGGCCTGGCGCTGCCGCAGTTCTTCAACAAC
GTTTCTCTGCATCACCACATGCAGGTGATGGAAGAAGTGGTGCGTAGGGACAAGAACCAC
CCCGCGGTCGTGATGTGGTCTGTGGCCAACGAGCCTGCGTCCCACCTAGAATCTGCTGGC
TACTACTTGAAGATGGTGATCGCTCACACCAAATCCTTGGACCCCTCCCGGCCTGTGACC
TTTGTGAGCAACTCTAACTATGCAGCAGACAAGGGGGCTCCGTATGTGGATGTGATCTGT
TTGAACAGCTACTACTCTTGGTATCACGACTACGGGCACCTGGAGTTGATTCAGCTGCAG
CTGGCCACCCAGTTTGAGAACTGGTATAAGAAGTATCAGAAGCCCATTATTCAGAGCGAG
TATGGAGCAGAAACGATTGCAGGGTTTCACCAGGATCCACCTCTGATGTTCACTGAAGAG
TACCAGAAAAGTCTGCTAGAGCAGTACCATCTGGGTCTGGATCAAAAACGCAGAAAATAT
GTGGTTGGAGAGCTCATTTGGAATTTTGCCGATTTCATGACTGAACAGTCACCGACGAGA
GTGCTGGGGAATAAAAAGGGGATCTTCACTCGGCAGAGACAACCAAAAAGTGCAGCGTTC
CTTTTGCGAGAGAGATACTGGAAGATTGCCAATGAAACCAGGTATCCCCACTCAGTAGCC
AAGTCACAATGTTTGGAAAACAGCCCGTTTACTTGA
Enzyme 13 GenBank Gene ID M15182 Link Image
Enzyme 13 GeneCard ID GUSB Link Image
Enzyme 13 GenAtlas ID GUSB Link Image
Enzyme 13 HGNC ID HGNC:4696 Link Image
Enzyme 13 Chromosome Location 7
Enzyme 13 Locus 7q21.11
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Oshima A, Kyle JW, Miller RD, Hoffmann JW, Powell PP, Grubb JH, Sly WS, Tropak M, Guise KS, Gravel RA: Cloning, sequencing, and expression of cDNA for human beta-glucuronidase. Proc Natl Acad Sci U S A. 1987 Feb;84(3):685-9. [PubMed Link Image]
  2. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  3. Shipley JM, Miller RD, Wu BM, Grubb JH, Christensen SG, Kyle JW, Sly WS: Analysis of the 5' flanking region of the human beta-glucuronidase gene. Genomics. 1991 Aug;10(4):1009-18. [PubMed Link Image]
  4. Tanaka J, Gasa S, Sakurada K, Miyazaki T, Kasai M, Makita A: Characterization of the subunits and sugar moiety of human placental and leukemic beta-glucuronidase. Biol Chem Hoppe Seyler. 1992 Jan;373(1):57-62. [PubMed Link Image]
  5. Guise KS, Korneluk RG, Waye J, Lamhonwah AM, Quan F, Palmer R, Ganschow RE, Sly WS, Gravel RA: Isolation and expression in Escherichia coli of a cDNA clone encoding human beta-glucuronidase. Gene. 1985;34(1):105-10. [PubMed Link Image]
  6. Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed Link Image]
  7. Jain S, Drendel WB, Chen ZW, Mathews FS, Sly WS, Grubb JH: Structure of human beta-glucuronidase reveals candidate lysosomal targeting and active-site motifs. Nat Struct Biol. 1996 Apr;3(4):375-81. [PubMed Link Image]
  8. Vervoort R, Lissens W, Liebaers I: Molecular analysis of a patient with hydrops fetalis caused by beta-glucuronidase deficiency, and evidence for additional pseudogenes. Hum Mutat. 1993;2(6):443-5. [PubMed Link Image]
  9. Wu BM, Sly WS: Mutational studies in a patient with the hydrops fetalis form of mucopolysaccharidosis type VII. Hum Mutat. 1993;2(6):446-57. [PubMed Link Image]
  10. Tomatsu S, Fukuda S, Sukegawa K, Ikedo Y, Yamada S, Yamada Y, Sasaki T, Okamoto H, Kuwahara T, Yamaguchi S, et al.: Mucopolysaccharidosis type VII: characterization of mutations and molecular heterogeneity. Am J Hum Genet. 1991 Jan;48(1):89-96. [PubMed Link Image]
  11. Shipley JM, Klinkenberg M, Wu BM, Bachinsky DR, Grubb JH, Sly WS: Mutational analysis of a patient with mucopolysaccharidosis type VII, and identification of pseudogenes. Am J Hum Genet. 1993 Mar;52(3):517-26. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 12970
Enzyme 14 Name UDP-glucuronosyltransferase 2A3 precursor
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name UGT2A3
Enzyme 14 Protein Sequence >UDP-glucuronosyltransferase 2A3 precursor 
MRSDKSALVFLLLQLFCVGCGFCGKVLVWPCDMSHWLNVKVILEELIVRGHEVTVLTHSK
PSLIDYRKPSALKFEVVHMPQDRTEENEIFVDLALNVLPGLSTWQSVIKLNDFFVEIRGT
LKMMCESFIYNQTLMKKLQETNYDVMLIDPVIPCGDLMAELLAVPFVLTLRISVGGNMER
SCGKLPAPLSYVPVPMTGLTDRMTFLERVKNSMLSVLFHFWIQDYDYHFWEEFYSKALGR
PTTLCETVGKAEIWLIRTYWDFEFPQPYQPNFEFVGGLHCKPAKALPKEMENFVQSSGED
GIVVFSLGSLFQNVTEEKANIIASALAQIPQKVLWRYKGKKPSTLGANTRLYDWIPQNDL
LGHPKTKAFITHGGMNGIYEAIYHGVPMVGVPIFGDQLDNIAHMKAKGAAVEINFKTMTS
EDLLRALRTVITDSSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRSAAHD
LTWFQHYSIDVIGFLLTCVATAIFLFTKCFLFSCQKFNKTRKIEKRE
Enzyme 14 Number of Residues 527
Enzyme 14 Molecular Weight 60285
Enzyme 14 Theoretical pI 8.04
Enzyme 14 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 14 General Function Carbohydrate transport and metabolism
Enzyme 14 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 14 Pathways
Enzyme 14 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 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-23
Enzyme 14 Transmembrane Regions
  • 492-512
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 44889644 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q6UWM9 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name UD2A3_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence Not Available
Enzyme 14 GenBank Gene ID AY542891 Link Image
Enzyme 14 GeneCard ID Q6UWM9 Link Image
Enzyme 14 GenAtlas ID UGT2A3 Link Image
Enzyme 14 HGNC ID HGNC:28528 Link Image
Enzyme 14 Chromosome Location Not Available
Enzyme 14 Locus Not Available
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. 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 Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 15056
Enzyme 15 Name UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
Enzyme 15 Synonyms Not Available
Enzyme 15 Gene Name UGT1A10
Enzyme 15 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f) 
MARAGWTSPVPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLERSLNCTVKTYSTSYTLEDQNREFMVFAHAQWKAQAQSIFSLLMSSSSGFLDLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDTCGLIVAKYFSLPSVVFTRGIFCHHLEEG
AQCPAPLSYVPNDLLGFSDAMTFKERVWNHIVHLEDHLFCQYLFRNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 15 Number of Residues 530
Enzyme 15 Molecular Weight 59810
Enzyme 15 Theoretical pI 7.31
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 Not Available
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • None
Enzyme 15 Transmembrane Regions
  • None
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 40849852 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q5DT02 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name Q5DT02_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 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 15 GenBank Gene ID AY435137 Link Image
Enzyme 15 GeneCard ID Q5DT02 Link Image
Enzyme 15 GenAtlas ID UGT1A10 Link Image
Enzyme 15 HGNC ID HGNC:12531 Link Image
Enzyme 15 Chromosome Location Not Available
Enzyme 15 Locus Not Available
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References Not Available
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 15057
Enzyme 16 Name UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
Enzyme 16 Synonyms Not Available
Enzyme 16 Gene Name UGT1A8
Enzyme 16 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e) 
MARTGWTSPIPLCVSLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGKSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVRSLFSLFLSSSNGFFNLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 16 Number of Residues 530
Enzyme 16 Molecular Weight 59742
Enzyme 16 Theoretical pI 7.73
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 Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • None
Enzyme 16 Transmembrane Regions
  • None
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 40849864 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q5DSZ6 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name Q5DSZ6_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 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 16 GenBank Gene ID AY435143 Link Image
Enzyme 16 GeneCard ID Q5DSZ6 Link Image
Enzyme 16 GenAtlas ID UGT1A8 Link Image
Enzyme 16 HGNC ID HGNC:12540 Link Image
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References Not Available
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 15058
Enzyme 17 Name UDP glycosyltransferase 1 family polypeptide A7
Enzyme 17 Synonyms Not Available
Enzyme 17 Gene Name UGT1A7
Enzyme 17 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A7 
MARAGWTGLLPLYVCLLLTCGFAKAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDQDREFMVFADARWTAPLRSAFSLLTSSSNGIFDLF
FSNCRSLFNDRKLVEYLKESCFDAVFLDPFDACGLIVAKYFSLPSVVFARGIFCHYLEEG
AQCPAPLSYVPRLLLGFSDAMTFKERVWNHIMHLEEHLFCPYFFKNVLEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLEYPKPVMPNMIFIGGINCHQGKPVPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 17 Number of Residues 530
Enzyme 17 Molecular Weight 59819
Enzyme 17 Theoretical pI 7.85
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 Not Available
Enzyme 17 Pathways Not Available
Enzyme 17 Reactions Not Available
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • None
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 40849862 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q5DSZ7 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name Q5DSZ7_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 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 17 GenBank Gene ID AY435142 Link Image
Enzyme 17 GeneCard ID Q5DSZ7 Link Image
Enzyme 17 GenAtlas ID UGT1A7 Link Image
Enzyme 17 HGNC ID HGNC:12539 Link Image
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References Not Available
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 15059
Enzyme 18 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 18 Synonyms Not Available
Enzyme 18 Gene Name UGT2B10
Enzyme 18 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 18 Number of Residues 528
Enzyme 18 Molecular Weight 60775
Enzyme 18 Theoretical pI 9.40
Enzyme 18 GO Classification Not Available
Enzyme 18 General Function Carbohydrate transport and metabolism
Enzyme 18 Specific Function Not Available
Enzyme 18 Pathways Not Available
Enzyme 18 Reactions Not Available
Enzyme 18 Pfam Domain Function Not Available
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • None
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 158258913 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID A8K9M3 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name A8K9M3_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 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 18 GenBank Gene ID AK292738 Link Image
Enzyme 18 GeneCard ID A8K9M3 Link Image
Enzyme 18 GenAtlas ID Not Available
Enzyme 18 HGNC ID Not Available
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References Not Available
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 16420
Enzyme 19 Name cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
Enzyme 19 Synonyms Not Available
Enzyme 19 Gene Name Not Available
Enzyme 19 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 19 Number of Residues 529
Enzyme 19 Molecular Weight 60721
Enzyme 19 Theoretical pI 8.45
Enzyme 19 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
—
Enzyme 19 General Function Carbohydrate transport and metabolism
Enzyme 19 Specific Function Not Available
Enzyme 19 Pathways Not Available
Enzyme 19 Reactions Not Available
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • None
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID B2R810 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name B2R810_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID AK313190 Link Image
Enzyme 19 GeneCard ID B2R810 Link Image
Enzyme 19 GenAtlas ID Not Available
Enzyme 19 HGNC ID Not Available
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs Not Available
Enzyme 19 General References Not Available
Enzyme 19 Metabolite References Not Available