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Human Metabolome Database Version 2.5

 

Showing metabocard for Uridine diphosphate glucuronic acid (HMDB00935)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:23
Accession Number HMDB00935
Secondary Accession Numbers HMDB01384
Common Name Uridine diphosphate glucuronic acid
Description Uridine diphosphate glucuronic acid is a nucleoside diphosphate sugar which serves as a source of glucuronic acid for polysaccharide biosynthesis. It may also be epimerized to UDP Iduronic acid, which donates Iduronic acid to polysaccharides. In animals, UDP glucuronic acid is used for formation of many glucosiduronides with various aglycones. The transfer of glucuronic acid from UDP-alpha-D-glucuronic acid onto a terminal galactose residue is done by beta1,3-glucuronosyltransferases, responsible for the completion of the protein-glycosaminoglycan linkage region of proteoglycans and of the HNK1 epitope of glycoproteins and glycolipids. In humans the enzyme galactose-beta-1,3-glucuronosyltransferase I completes the synthesis of the common linker region of glycosaminoglycans (GAGs) by transferring glucuronic acid (GlcA) onto the terminal galactose of the glycopeptide primer of proteoglycans. The GAG chains of proteoglycans regulate major biological processes such as cell proliferation and recognition, extracellular matrix deposition, and morphogenesis. (PMID: 16815917)
Synonyms
  1. UDP glucuronate
  2. UDP-D-glucuronate
  3. UDP-D-glucuronic acid
  4. UDP-GlcUA
  5. UDP-alpha-D-glucuronate
  6. UDP-delta-glucuronate
  7. UDP-delta-glucuronic acid
  8. UDP-glucuronate
  9. UDP-glucuronic acid
  10. UDPGA
  11. UDPglucuronate
  12. UGA
  13. Udp glucuronic acid
  14. Uridine 5'-diphospho-a-D-glucuronate
  15. Uridine 5'-diphospho-a-D-glucuronic acid
  16. Uridine 5'-diphospho-alpha-delta-glucuronate
  17. Uridine 5'-diphospho-alpha-delta-glucuronic acid
  18. Uridine 5'-diphospho-glucuronic acid
  19. Uridine 5'-diphosphoglucuronate
  20. Uridine 5'-diphosphoglucuronic acid
  21. Uridine diphosphate glucuronate
  22. Uridine diphosphate glucuronic acid
  23. Uridine diphosphate-glucuronate
  24. Uridine diphospho-D-glucuronate
  25. Uridine diphospho-D-glucuronic acid
  26. Uridine diphospho-delta-glucuronate
  27. Uridine diphospho-delta-glucuronic acid
  28. Uridine diphosphoglucuronate
  29. Uridine diphosphoglucuronic acid
  30. Uridine pyrophosphoglucuronate
  31. Uridine pyrophosphoglucuronic acid
  32. Uridinediphosphoglucuronic acid
  33. a-D-Glucopyranuronic acid 1->5'-ester with uridine 5'-(trihydrogen pyrophosphate)
  34. a-D-Glucopyranuronic acid ester with uridine 5'-pyrophosphate
  35. alpha-D-Glucopyranuronic acid 1-P'-ester with uridine 5'-(trihydrogen diphosphate)
  36. uridine 5'-[3-(D-glucopyranosyloxyuronic acid) dihydrogen diphosphate]
  37. Glucopyranuronic acid 1-ester with uridine 5'-pyrophosphate
  38. UDP-alpha-delta-glucuronate
  39. alpha-delta-Glucopyranuronic acid 1->5'-ester with uridine 5'-(trihydrogen pyrophosphate)
  40. alpha-delta-Glucopyranuronic acid ester with uridine 5'-pyrophosphate
  41. alpha-delta-Glucopyranuronic acid 1-P'-ester with uridine 5'-(trihydrogen diphosphate)
Chemical IUPAC Name (2S,3S,4R,5R,6R)-6-[[[(2S,3S,4R,5R)-5-(2,4-dioxopyrimidin-1-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-hydroxy-phosphoryl]oxy-3,4,5-trihydroxy-oxane-2-carboxylic
Chemical Formula C15H22N2O18P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide diphosphates
Family
  • Mammalian Metabolite
Species
  • secondary alcohol
  • 1,2-diol
  • carboxylic acid
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Nucleotide sugars metabolism
  • Component of Starch and sucrose metabolism
Application
Source
  • Endogenous
Average Molecular Weight 580.285
Monoisotopic Molecular Weight 580.034302
Isomeric SMILES O[C@@H]1[C@@H](COP(O)(=O)OP(O)(=O)O[C@H]2O[C@@H]([C@@H](O)[C@H](O)[C@H]2O)C(O)=O)O[C@H]([C@@H]1O)N1C=CC(=O)NC1=O
Canonical SMILES OC1C(COP(O)(=O)OP(O)(=O)OC2OC(C(O)C(O)C2O)C(O)=O)OC(C1O)N1C=CC(=O)NC1=O
KEGG Compound ID C00167 Link Image
BioCyc ID UDP-GLUCURONATE Link Image
BiGG ID 34117 Link Image
Wikipedia Link Uridine diphosphate glucuronic acid Link Image
NuGOwiki Link HMDB00935 Link Image
Metagene Link HMDB00935 Link Image
METLIN ID 5884 Link Image
PubChem Compound 17473 Link Image
PubChem Substance 837291 Link Image
ChEBI ID 17200 Link Image
CAS Registry Number 2616-64-0
InChI Identifier InChI=1/C15H22N2O18P2/c18-5-1-2-17(15(26)16-5)12-9(22)6(19)4(32-12)3-31-36(27,28)35-37(29,30)34-14-10(23)7(20)8(21)11(33-14)13(24)25/h1-2,4,6-12,14,19-23H,3H2,(H,24,25)(H,27,28)(H,29,30)(H,16,18,26)/t4-,6-,7+,8+,9-,10-,11+,12-,14-/m1/s1
Synthesis Reference Simon, Ethan S.; Grabowski, Sven; Whitesides, George M. Convenient syntheses of cytidine 5'-triphosphate, guanosine 5'-triphosphate, and uridine 5'-triphosphate and their use in the preparation of UDP-glucose, UDP-glucuronic acid, and GDP-mannose. Journal
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 18.099998 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.21 [Predicted by ALOGPS]; -6.2 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
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)
  • endoplasmic reticulum
  • golgi apparatus
Biofluid Location Not Available
Tissue Location
Tissue References
Liver
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Nucleotide Sugars Metabolism SMP00010 Link Image map00520 Link Image
Starch and Sucrose Metabolism SMP00058 Link Image map00500 Link Image
General References
  1. Quintus J, Kovar KA, Link P, Hamacher H: Urinary excretion of arbutin metabolites after oral administration of bearberry leaf extracts. Planta Med. 2005 Feb;71(2):147-52. [PubMed Link Image]
  2. Cappiello M, Giuliani L, Rane A, Pacifici GM: Uridine 5'-diphosphoglucuronic acid (UDPGLcUA) in the human fetal liver, kidney and placenta. Eur J Drug Metab Pharmacokinet. 2000 Jul-Dec;25(3-4):161-3. [PubMed Link Image]
  3. Clinical Guide to Laboratory Tests, 2nd Ed. Norbert W. Tietz 1990
  4. Ghosal A, Hapangama N, Yuan Y, Achanfuo-Yeboah J, Iannucci R, Chowdhury S, Alton K, Patrick JE, Zbaida S: Identification of human UDP-glucuronosyltransferase enzyme(s) responsible for the glucuronidation of ezetimibe (Zetia). Drug Metab Dispos. 2004 Mar;32(3):314-20. [PubMed Link Image]
  5. Huskey SW, Doss GA, Miller RR, Schoen WR, Chiu SH: N-glucuronidation reactions. II. Relative N-glucuronidation reactivity of methylbiphenyl tetrazole, methylbiphenyl triazole, and methylbiphenyl imidazole in rat, monkey, and human hepatic microsomes. Drug Metab Dispos. 1994 Jul-Aug;22(4):651-8. [PubMed Link Image]
  6. Alkharfy KM, Frye RF: High-performance liquid chromatographic assay for acetaminophen glucuronide in human liver microsomes. J Chromatogr B Biomed Sci Appl. 2001 Apr 5;753(2):303-8. [PubMed Link Image]
  7. Hagenauer B, Salamon A, Thalhammer T, Kunert O, Haslinger E, Klingler P, Senderowicz AM, Sausville EA, Jager W: In vitro glucuronidation of the cyclin-dependent kinase inhibitor flavopiridol by rat and human liver microsomes: involvement of UDP-glucuronosyltransferases 1A1 and 1A9. Drug Metab Dispos. 2001 Apr;29(4 Pt 1):407-14. [PubMed Link Image]
  8. Cappiello M, Giuliani L, Pacifici GM: Distribution of UDP-glucuronosyltransferase and its endogenous substrate uridine 5'-diphosphoglucuronic acid in human tissues. Eur J Clin Pharmacol. 1991;41(4):345-50. [PubMed Link Image]
  9. 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. UDP-glucose 6-dehydrogenase
  14. Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
  15. Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
  16. Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
  17. Chondroitin sulfate synthase 3
  18. Chondroitin sulfate synthase 2
  19. Chondroitin sulfate synthase 1
  20. Hyaluronan synthase 1
  21. Hyaluronan synthase 3
  22. Hyaluronan synthase 2
  23. UDP-glucuronic acid decarboxylase 1
  24. UDP-glucuronosyltransferase 2A3 precursor
  25. UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
  26. UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
  27. UDP glycosyltransferase 1 family polypeptide A7
  28. cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b)
  29. cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
  30. Chondroitin synthase-3 (Chondroitin sulfate glucuronyltransferase, isoform CRA_b)
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 Not Available
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 Not Available
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 6195
Enzyme 13 Name UDP-glucose 6-dehydrogenase
Enzyme 13 Synonyms
  1. UDP-Glc dehydrogenase
  2. UDP-GlcDH
  3. UDPGDH
Enzyme 13 Gene Name UGDH
Enzyme 13 Protein Sequence >UDP-glucose 6-dehydrogenase
MFEIKKICCIGAGYVGGPTCSVIAHMCPEIRVTVVDVNESRINAWNSPTLPIYEPGLKEV
VESCRGKNLFFSTNIDDAIKEADLVFISVNTPTKTYGMGKGRAADLKYIEACARRIVQNS
NGYKIVTEKSTVPVRAAESIRRIFDANTKPNLNLQVLSNPEFLAEGTAIKDLKNPDRVLI
GGDETPEGQRAVQALCAVYEHWVPREKILTTNTWSSELSKLAANAFLAQRISSINSISAL
CEATGADVEEVATAIGMDQRIGNKFLKASVGFGGSCFQKDVLNLVYLCEALNLPEVARYW
QQVIDMNDYQRRRFASRIIDSLFNTVTDKKIAILGFAFKKDTGDTRESSSIYISKYLMDE
GAHLHIYDPKVPREQIVVDLSHPGVSEDDQVSRLVTISKDPYEACDGAHAVVICTEWDMF
KELDYERIHKKMLKPAFIFDGRRVLDGLHNELQTIGFQIETIGKKVSSKRIPYAPSGEIP
KFSLQDPPNKKPKV
Enzyme 13 Number of Residues 494
Enzyme 13 Molecular Weight 55025
Enzyme 13 Theoretical pI 7.13
Enzyme 13 GO Classification
Function
Process
  • cellular metabolism
  • electron transport
  • generation of precursor metabolites and energy
  • metabolism
  • physiological process
Component
Enzyme 13 General Function Cell wall/membrane/envelope biogenesis
Enzyme 13 Specific Function Involved in the biosynthesis of glycosaminoglycans; hyaluronan, chondroitin sulfate, and heparan sulfate
Enzyme 13 Pathways
Enzyme 13 Reactions
  • UDP-glucose + 2 NAD+ + H2O = UDP-glucuronate + 2 NADH + 2 H+
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • None
Enzyme 13 Transmembrane Regions
  • None
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 3127127 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID O60701 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name UGDH_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1485 bp
ATGTTTGAAATTAAGAAGATCTGTTGCATCGGTGCAGGCTATGTTGGAGGACCCACATGT
AGTGTCATTGCTCATATGTGTCCTGAAATCAGGGTAACGGTTGTTGATGTCAATGAATCA
AGAATCAATGCGTGGAATTCTCCTACACTTCCTATTTATGAGCCAGGACTAAAAGAAGTG
GTAGAATCCTGTCGAGGAAAAAATCTTTTTTTTTCTACCAATATTGATGATGCCATCAAA
GAAGCTGATCTTGTATTTATTTCTGTGAATACTCCAACAAAAACCTATGGAATGGGGAAA
GGCCGGGCAGCAGATCTGAAGTATATTGAAGCTTGTGCTAGACGCATTGTGCAAAACTCA
AATGGGTACAAAATTGTGACTGAGAAAAGCACAGTTCCAGTGCGGGCAGCAGAAAGTATC
CGTCGCATATTTGATGCAAACACAAAACCCAACTTGAATTTACAGGTGCTGTCCAACCCT
GAGTTTCTGGCAGAGGGAACAGCCATCAAGGACCTAAAGAACCCAGACAGAGTACTGATT
GGAGGGGATGAAACTCCAGAGGGCCAGAGAGCTGTGCAGGCCCTGTGTGCTGTATATGAG
CACTGGGTTCCCAGAGAAAAGATCCTCACCACTAATACTTGGTCTTCAGAGCTTTCCAAA
CTGGCAGCAAATGCTTTTCTTGCCCAGAGAATAAGCAGCATTAACTCCATAAGTGCTCTG
TGTGAAGCAACAGGAGCTGATGTAGAAGAGGTAGCAACAGCGATTGGAATGGACCAGAGA
ATTGGAAACAAGTTTCTAAAAGCCAGTGTTGGGTTTGGTGGGAGCTGTTTCCAAAAGGAT
GTTCTGAATTTGGTTTATCTCTGTGAGGCTCTGAATTTGCCAGAAGTAGCTCGTTATTGG
CAGCAGGTCATAGACATGAATGACTACCAGAGGAGGAGGTTTGCTTCCCGGATCATAGAT
AGTCTGTTTAATACAGTAACTGATAAGAAGATAGCTATTTTGGGATTTGCATTCAAAAAG
GACACTGGTGATACAAGAGAATCTTCTAGTATATATATTAGCAAATATTTGATGGATGAA
GGTGCACATCTACATATATATGATCCAAAAGTACCTAGGGAACAAATAGTTGTGGATCTT
TCTCATCCAGGTGTTTCAGAGGATGACCAAGTGTCCCGGCTCGTGACCATTTCCAAGGAT
CCATATGAAGCATGTGATGGTGCCCATGCTGTTGTTATTTGCACTGAGTGGGACATGTTT
AAGGAATTGGATTATGAACGCATTCATAAAAAAATGCTAAAGCCAGCCTTTATCTTCGAT
GGACGGCGTGTCCTGGATGGGCTCCACAATGAACTACAAACCATTGGCTTCCAGATTGAA
ACAATTGGCAAAAAGGTGTCTTCAAAGAGAATTCCATATGCTCCTTCTGGTGAAATTCCG
AAGTTTAGTCTTCAAGATCCACCTAACAAGAAACCTAAAGTGTAG
Enzyme 13 GenBank Gene ID AF061016 Link Image
Enzyme 13 GeneCard ID UGDH Link Image
Enzyme 13 GenAtlas ID UGDH Link Image
Enzyme 13 HGNC ID HGNC:12525 Link Image
Enzyme 13 Chromosome Location 4
Enzyme 13 Locus 4p15.1
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Spicer AP, Kaback LA, Smith TJ, Seldin MF: Molecular cloning and characterization of the human and mouse UDP-glucose dehydrogenase genes. J Biol Chem. 1998 Sep 25;273(39):25117-24. [PubMed Link Image]
  2. Peng HL, Lou MD, Chang ML, Chang HY: cDNA cloning and expression analysis of the human UDPglucose dehydrogenase. Proc Natl Sci Counc Repub China B. 1998 Oct;22(4):166-72. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 6221
Enzyme 14 Name Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
Enzyme 14 Synonyms
  1. Beta-1,3-glucuronyltransferase 3
  2. Glucuronosyltransferase-I
  3. GlcAT-I
  4. UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase
  5. GlcUAT-I
Enzyme 14 Gene Name B3GAT3
Enzyme 14 Protein Sequence >Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
MKLKLKNVFLAYFLVSIAGLLYALVQLGQPCDCLPPLRAAAEQLRQKDLRISQLQAELRR
PPPAPAQPPEPEALPTIYVVTPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAEGPTPL
VSGLLAASGLLFTHLVVLTPKAQRLREGEPGWVHPRGVEQRNKALDWLRGRGGAVGGEKD
PPPPGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDGRVVGFH
TAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTAPRGHLESSLLSHLVDPKDLEPRAAN
CTRVLVWHTRTEKPKMKQEEQLQRQGRGSDPAIEV
Enzyme 14 Number of Residues 335
Enzyme 14 Molecular Weight 37122
Enzyme 14 Theoretical pI 8.47
Enzyme 14 GO Classification
Function
  • UDP-glycosyltransferase activity
  • catalytic activity
  • galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
  • glucuronosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
Component
  • cell
  • membrane
Enzyme 14 General Function Not Available
Enzyme 14 Specific Function Glycosaminoglycans biosynthesis. Involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. Transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal beta 1-3Gal beta 1-4Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. Can also play a role in the biosynthesis of l2/HNK- 1 carbohydrate epitope on glycoproteins. Shows strict specificity for Gal beta1-3Gal beta1-4Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O- benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc
Enzyme 14 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 14 Reactions
  • UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-23
Enzyme 14 Transmembrane Regions Not Available
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 3892640 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID O94766 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name B3GA3_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 Gene Sequence >1008 bp
ATGAAGCTGAAGCTGAAGAACGTGTTTCTCGCCTACTTCCTGGTGTCGATCGCCGGCCTC
CTCTACGCGCTGGTACAGCTCGGCCAGCCATGTGACTGCCTTCCTCCCCTGCGGGCAGCA
GCCGAGCAGCTACGGCAGAAGGATCTGAGGATTTCCCAGCTGCAAGCGGAACTCCGACGG
CCACCCCCTGCCCCTGCCCAGCCCCCTGAACCCGAGGCCCTGCCTACTATCTATGTTGTT
ACCCCCACCTATGCCAGGCTGGTACAGAAGGCAGAGCTGGTACGACTGTCCCAGACACTG
AGCCTGGTGCCCCGGCTGCATTGGCTGCTGGTGGAGGATGCTGAGGGTCCCACCCCGCTG
GTCTCAGGGCTGCTGGCTGCCTCTGGCCTCCTCTTCACACACCTGGTGGTCCTCACGCCC
AAAGCCCAGCGGCTTCGGGAGGGCGAGCCTGGCTGGGTTCATCCCCGTGGTGTCGAGCAG
CGGAACAAGGCCCTGGACTGGCTCCGGGGCAGAGGGGGTGCTGTGGGTGGGGAGAAGGAC
CCACCACCACCAGGGACCCAAGGAGTCGTTTACTTTGCTGACGATGACAACACCTACAGC
CGGGAGCTGTCTGAGGAGATGCGCTGGACCCGTGGTGTCTCAGTGTGGCCTGTGGGGCTG
GTGGGCGGCCTGCGATTCGAGGGCCCTCAGGTACAGGACGGCCGGGTAGTGGGCTTCCAC
ACAGCATGGGAGCCCAGCAGGCCCTTCCCTGTGGATATGGCTGGATTTGCCGTGGCCCTG
CCCTTGCTGTTAGATAAGCCCAATGCCCAATTTGATTCCACCGCTCCCCGGGGCCACCTG
GAGAGCAGTCTTCTGAGCCACCTTGTGGATCCCAAGGACCTGGAGCCACGGGCTGCCAAC
TGCACTCGGGTACTGGTGTGGCATACTCGGACAGAGAAGCCCAAGATGAAGCAGGAGGAG
CAGCTGCAGCGGCAGGGCCGGGGCTCAGACCCAGCAATTGAGGTGTGA
Enzyme 14 GenBank Gene ID AB009598 Link Image
Enzyme 14 GeneCard ID B3GAT3 Link Image
Enzyme 14 GenAtlas ID B3GAT3 Link Image
Enzyme 14 HGNC ID HGNC:923 Link Image
Enzyme 14 Chromosome Location 11
Enzyme 14 Locus 11q12.3
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 General References
  1. Kitagawa H, Tone Y, Tamura J, Neumann KW, Ogawa T, Oka S, Kawasaki T, Sugahara K: Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. J Biol Chem. 1998 Mar 20;273(12):6615-8. [PubMed Link Image]
  2. Ouzzine M, Gulberti S, Netter P, Magdalou J, Fournel-Gigleux S: Structure/function of the human Ga1beta1,3-glucuronosyltransferase. Dimerization and functional activity are mediated by two crucial cysteine residues. J Biol Chem. 2000 Sep 8;275(36):28254-60. [PubMed Link Image]
  3. Herman T, Horvitz HR: Three proteins involved in Caenorhabditis elegans vulval invagination are similar to components of a glycosylation pathway. Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):974-9. [PubMed Link Image]
  4. Tone Y, Kitagawa H, Imiya K, Oka S, Kawasaki T, Sugahara K: Characterization of recombinant human glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans. FEBS Lett. 1999 Oct 15;459(3):415-20. [PubMed Link Image]
  5. Pedersen LC, Tsuchida K, Kitagawa H, Sugahara K, Darden TA, Negishi M: Heparan/chondroitin sulfate biosynthesis. Structure and mechanism of human glucuronyltransferase I. J Biol Chem. 2000 Nov 3;275(44):34580-5. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 6222
Enzyme 15 Name Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
Enzyme 15 Synonyms
  1. Beta-1,3-glucuronyltransferase 2
  2. Glucuronosyltransferase-S
  3. GlcAT-S
  4. UDP-glucuronosyltransferase-S
  5. GlcAT-D
Enzyme 15 Gene Name B3GAT2
Enzyme 15 Protein Sequence >Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
MKSALFTRFFILLPWILIVIIMLDVDTRRPVPPLTPRPYFSPYAVGRGGARLPLRRGGPA
HGTQKRNQSRPQPQPEPQLPTIYAITPTYSRPVQKAELTRLANTFRQVAQLHWILVEDAA
ARSELVSRFLARAGLPSTHLHVPTPRRYKRPGLPRATEQRNAGLAWLRQRHQHQRAQPGV
LFFADDDNTYSLELFQEMRTTRKVSVWPVGLVGGRRYERPLVENGKVVGWYTGWRADRPF
AIDMAGFAVSLQVILSNPKAVFKRRGSQPGMQESDFLKQITTVEELEPKANNCTKVLVWH
TRTEKVNLANEPKYHLDTVKIEV
Enzyme 15 Number of Residues 323
Enzyme 15 Molecular Weight 36919
Enzyme 15 Theoretical pI 11.20
Enzyme 15 GO Classification
Function
  • UDP-glycosyltransferase activity
  • catalytic activity
  • galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
  • glucuronosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
Component
  • cell
  • membrane
Enzyme 15 General Function Not Available
Enzyme 15 Specific Function Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins
Enzyme 15 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 15 Reactions
  • UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-27
Enzyme 15 Transmembrane Regions Not Available
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 18086555 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9NPZ5 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name B3GA2_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >972 bp
ATGAAGTCCGCGCTTTTCACCCGCTTCTTTATCCTCCTGCCCTGGATCCTAATTGTCATC
ATCATGCTCGACGTGGACACGCGCAGGCCAGTGCCCCCGCTCACCCCGCGCCCCTACTTC
TCTCCCTACGCGGTGGGCCGCGGGGGCGCCCGACTCCCGCTCCGCAGGGGCGGCCCGGCT
CACGGGACCCAAAAGCGCAACCAGTCTCGGCCGCAGCCACAGCCGGAGCCGCAGCTGCCC
ACCATCTATGCCATCACGCCCACCTACAGCCGCCCGGTGCAGAAAGCGGAGCTGACCCGC
CTGGCCAACACGTTCCGCCAGGTGGCGCAGCTGCACTGGATCCTGGTGGAGGACGCGGCG
GCGCGCAGCGAGCTGGTGAGCCGCTTCCTGGCGCGGGCCGGGCTGCCCAGCACTCACCTG
CACGTGCCCACGCCGCGGCGCTACAAGCGGCCCGGGCTGCCGCGCGCCACTGAGCAGCGC
AACGCGGGCCTCGCCTGGCTGCGCCAGAGGCACCAGCACCAGCGCGCGCAGCCCGGCGTG
CTCTTCTTCGCTGACGACGACAACACCTATAGTCTGGAGCTCTTCCAGGAGATGCGAACC
ACCCGCAAGGTCTCCGTCTGGCCTGTGGGCCTGGTTGGTGGGCGGCGCTACGAACGTCCG
CTGGTGGAAAACGGCAAAGTTGTTGGCTGGTACACCGGCTGGAGAGCAGACAGGCCTTTT
GCCATCGACATGGCAGGATTTGCTGTAAGTCTTCAAGTCATTTTGTCCAATCCAAAAGCT
GTATTTAAGCGTCGTGGATCCCAGCCAGGGATGCAAGAATCTGACTTTCTCAAACAGATA
ACAACAGTCGAAGAACTGGAACCGAAAGCAAATAACTGCACTAAGGTTCTCGTGTGGCAC
ACTCGGACAGAGAAGGTTAATCTAGCCAACGAGCCAAAGTACCACCTGGACACAGTGAAA
ATTGAGGTATAA
Enzyme 15 GenBank Gene ID AY070019 Link Image
Enzyme 15 GeneCard ID B3GAT2 Link Image
Enzyme 15 GenAtlas ID B3GAT2 Link Image
Enzyme 15 HGNC ID HGNC:922 Link Image
Enzyme 15 Chromosome Location 6
Enzyme 15 Locus 6q13
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Marcos I, Galan JJ, Borrego S, Antinolo G: Cloning, characterization, and chromosome mapping of the human GlcAT-S gene. J Hum Genet. 2002;47(12):677-80. [PubMed Link Image]
  2. Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed Link Image]
  3. Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 6223
Enzyme 16 Name Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
Enzyme 16 Synonyms
  1. Beta-1,3-glucuronyltransferase 1
  2. Glucuronosyltransferase-P
  3. GlcAT-P
  4. UDP-GlcUA:glycoprotein beta- 1,3-glucuronyltransferase
  5. GlcUAT-P
Enzyme 16 Gene Name B3GAT1
Enzyme 16 Protein Sequence >Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
MPKRRDILAIVLIVLPWTLLITVWHQSTLAPLLAVHKDEGSDPRRETPPGADPREYCTSD
RDIVEVVRTEYVYTRPPPWSDTLPTIHVVTPTYSRPVQKAELTRMANTLLHVPNLHWLVV
EDAPRRTPLTARLLRDTGLNYTHLHVETPRNYKLRGDARDPRIPRGTMQRNLALRWLRET
FPRNSSQPGVVYFADDDNTYSLELFEEMRSTRRVSVWPVAFVGGLRYEAPRVNGAGKVVR
WKTVFDPHRPFAIDMAGFAVNLRLILQRSQAYFKLRGVKGGYQESSLLRELVTLNDLEPK
AANCTKILVWHTRTEKPVLVNEGKKGFTDPSVEI
Enzyme 16 Number of Residues 334
Enzyme 16 Molecular Weight 38356
Enzyme 16 Theoretical pI 10.13
Enzyme 16 GO Classification
Function
  • UDP-glycosyltransferase activity
  • catalytic activity
  • galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
  • glucuronosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
Component
  • cell
  • membrane
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo- orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity:stearoyl- sphingomyelin was the most effective, followed by palmitoyl- sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group
Enzyme 16 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 16 Reactions
  • UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-29
Enzyme 16 Transmembrane Regions Not Available
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 8051678 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q9P2W7 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name B3GA1_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1005 bp
ATGCCGAAGAGACGGGACATCCTAGCGATCGTCCTCATCGTGCTGCCCTGGACTCTGCTC
ATCACTGTCTGGCACCAGAGCACCCTCGCACCCCTGCTCGCGGTACATAAGGATGAGGGC
AGTGACCCCCGACGCGAAACGCCGCCCGGCGCCGACCCCAGGGAGTACTGCACGTCTGAC
CGCGACATCGTGGAGGTGGTGCGCACCGAGTACGTGTACACGCGGCCCCCGCCATGGTCC
GACACGCTGCCCACCATCCACGTGGTGACGCCCACCTACAGCCGCCCGGTGCAGAAGGCC
GAGCTGACGCGCATGGCCAACACGCTGCTGCACGTGCCCAACCTCCACTGGCTGGTGGTG
GAGGATGCGCCGCGCCGGACGCCGCTGACCGCGCGCCTGCTGCGCGACACCGGCCTCAAC
TACACGCACCTGCACGTGGAGACGCCCCGCAACTACAAGCTGCGCGGAGACGCCCGCGAC
CCACGCATCCCGCGGGGCACCATGCAGCGCAACCTGGCCCTGCGCTGGCTGCGCGAGACC
TTCCCGCGCAACTCCAGCCAGCCTGGCGTGGTCTACTTCGCCGACGACGACAACACCTAC
AGCCTGGAGCTCTTCGAAGAGATGCGCAGCACCAGGAGGGTGTCCGTGTGGCCCGTCGCC
TTCGTGGGTGGCCTGCGGTACGAGGCCCCACGGGTGAACGGGGCAGGGAAGGTGGTCCGC
TGGAAGACGGTGTTTGACCCCCACCGGCCATTTGCAATAGACATGGCTGGATTTGCCGTC
AACCTGCGGCTCATTCTGCAGCGAAGCCAGGCCTACTTCAAGCTGCGAGGTGTGAAGGGA
GGCTACCAGGAAAGCAGCCTCCTTCGAGAACTTGTCACCCTCAACGACCTGGAGCCCAAG
GCAGCCAACTGCACCAAGATCCTGGTGTGGCACACACGGACAGAGAAGCCAGTGCTGGTG
AATGAGGGCAAGAAGGGCTTCACTGACCCCTCGGTGGAGATCTGA
Enzyme 16 GenBank Gene ID AB029396 Link Image
Enzyme 16 GeneCard ID B3GAT1 Link Image
Enzyme 16 GenAtlas ID B3GAT1 Link Image
Enzyme 16 HGNC ID HGNC:921 Link Image
Enzyme 16 Chromosome Location 11
Enzyme 16 Locus 11q25
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Mitsumoto Y, Oka S, Sakuma H, Inazawa J, Kawasaki T: Cloning and chromosomal mapping of human glucuronyltransferase involved in biosynthesis of the HNK-1 carbohydrate epitope. Genomics. 2000 Apr 15;65(2):166-73. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 6392
Enzyme 17 Name Chondroitin sulfate synthase 3
Enzyme 17 Synonyms
  1. Glucuronosyl-N- acetylgalactosaminyl-proteoglycan 4-beta-N- acetylgalactosaminyltransferase II
  2. Chondroitin synthase 2
  3. N- acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase II
  4. Chondroitin glucuronyltransferase II
  5. N- acetylgalactosaminyltransferase II
  6. Carbohydrate synthase 2
Enzyme 17 Gene Name CSS3
Enzyme 17 Protein Sequence >Chondroitin sulfate synthase 3
MAVRSRRPWMSVALGLVLGFTAASWLIAPRVAELSERKRRGSSLCSYYGRSAAGPRAGAQ
QPLPQPQSRPRQEQSPPPARQDLQGPPLPEAAPGITSFRSSPWQQPPPLQQRRRGREPEG
ATGLPGAPAAEGEPEEEDGGAAGQRRDGRPGSSHNGSGDGGAAAPSARPRDFLYVGVMTA
QKYLGSRALAAQRTWARFIPGRVEFFSSQQPPNAGQPPPPLPVIALPGVDDSYPPQKKSF
MMIKYMHDHYLDKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQTGLGNIEELGKL
GLEPGENFCMGGPGMIFSREVLRRMVPHIGECLREMYTTHEDVEVGRCVRRFGGTQCVWS
YEMQQLFHENYEHNRKGYIQDLHNSKIHAAITLHPNKRPAYQYRLHNYMLSRKISELRYR
TIQLHRESALMSKLSNTEVSKEDQQLGVIPSFNHFQPRERNEVIEWEFLTGKLLYSAAEN
QPPRQSLSSILRTALDDTVLQVMEMINENAKSRGRLIDFKEIQYGYRRVNPMHGVEYILD
LLLLYKRHKGRKLTVPVRRHAYLQQLFSKPFFRETEELDVNSLVESINSETQSFSFISNS
LKILSSFQGAKEMGGHNEKKVHILVPLIGRYDIFLRFMENFENMCLIPKQNVKLVIILFS
RDSGQDSSKHIELIKGYQNKYPKAEMTLIPMKGEFSRGLGLEMASAQFDNDTLLLFCDVD
LIFREDFLQRCRDNTIQGQQVYYPIIFSQYDPKVTNGGNPPTDDYFIFSKKTGFWRDYGY
GITCIYKSDLLGAGGFDTSIQGWGLEDVDLYNKVILSGLRPFRSQEVGVVHIFHPVHCDP
NLDPKQYKMCLGSKASTFASTMQLAELWLEKHLGVRYNRTLS
Enzyme 17 Number of Residues 882
Enzyme 17 Molecular Weight 100286
Enzyme 17 Theoretical pI 8.97
Enzyme 17 GO Classification Not Available
Enzyme 17 General Function Not Available
Enzyme 17 Specific Function Has both beta-1,3-glucuronic acid and beta-1,4-N- acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer. Specific activity is much reduced compared to CHSY1
Enzyme 17 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 17 Reactions
  • UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-23
Enzyme 17 Transmembrane Regions Not Available
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 37573674 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q70JA7 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name CHSS3_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >2649 bp
ATGGCTGTGCGCTCTCGCCGCCCGTGGATGAGCGTGGCATTAGGGCTGGTGCTGGGCTTC
ACCGCCGCGTCCTGGCTCATCGCCCCCAGGGTGGCGGAGCTGAGCGAGAGGAAGAGACGT
GGCTCCAGCCTCTGCTCCTACTACGGTCGCTCTGCTGCTGGCCCCCGCGCCGGCGCTCAG
CAGCCGCTCCCCCAGCCCCAGTCCCGACCACGGCAGGAGCAGTCGCCGCCCCCCGCGCGC
CAGGATCTCCAGGGGCCACCGCTGCCCGAGGCAGCACCCGGGATCACCAGTTTTCGAAGC
AGCCCCTGGCAGCAGCCACCTCCGCTGCAGCAGCGGCGGCGAGGACGCGAGCCTGAGGGC
GCGACGGGGCTTCCCGGTGCTCCAGCGGCCGAGGGGGAGCCCGAGGAGGAGGACGGGGGC
GCGGCTGGGCAGCGGAGAGACGGCCGGCCGGGGAGTAGCCACAACGGCAGCGGGGACGGG
GGCGCTGCCGCCCCGAGCGCCCGACCCCGGGACTTCCTGTACGTGGGGGTGATGACCGCG
CAGAAGTACCTGGGCAGCCGCGCGCTGGCCGCGCAGCGGACCTGGGCGCGTTTCATCCCG
GGCCGCGTGGAGTTCTTTTCCAGCCAGCAGCCCCCCAACGCCGGCCAGCCCCCGCCACCC
CTGCCTGTCATCGCGCTACCGGGTGTGGACGACTCCTATCCTCCCCAGAAAAAGTCCTTC
ATGATGATCAAGTACATGCACGACCACTACCTGGACAAGTATGAGTGGTTCATGCGCGCC
GACGACGATGTCTACATCAAAGGTGACAAATTAGAAGAGTTTCTTAGATCGCTAAACAGC
AGTAAGCCTCTCTACCTGGGACAGACTGGCCTGGGGAATATTGAAGAGCTTGGAAAGCTG
GGACTGGAGCCTGGGGAAAACTTCTGTATGGGAGGACCTGGCATGATCTTTAGCCGAGAA
GTTCTCAGGAGGATGGTGCCACATATTGGTGAATGCCTTAGAGAAATGCACACGACTCAT
GAGGATGTGGAAGTAGGAAGATGCGTTCGCCGCTTTGGTAGGGCTCAGTGTGTGTGGTCT
TTTCAGATGCAACAACTGTTCCATGAAAATTATGAACACAATCGGAAGGGTTACATCCAA
GACCTTCACAATAGCAAAATCCATGCAGCCATAACACTTCATCCCAACAAAAGGCCTGCA
TACCAATACAGGCTGCATAATTACATGCTCAGCCGCAAAATTTCTGAACTTCGCTACCGC
ACCATCCAGCTCCACAGGGAAAGTGCCCTGATGAGCAAGCTCAGTAACACAGAAGTGAGC
AAAGAGGACCAGCAGCTGGGAGTGATACCTTCTTTCAACCACTTCCAGCCTCGGGAGAGA
AATGAAGTGATAGAATGGGAGTTCCTGACAGGGAAGCTTCTATACTCAGCAGCTGAGAAC
CAGCCCCCTCGACAGAGCCTCAGTAGCATTTTAAGAACAGCACTGGATGATACCGTCCTA
CAGGTGATGGAGATGATCAATGAGAATGCCAAGAGCAGAGGACGGCTCATTGACTTCAAG
GAAATTCAGTATGGCTACCGCAGAGTTAACCCCATGCACGGGGTGGAGTACATTTTGGAT
TTACTCCTTTTATACAAAAGACACAAGGGAAGGAAACTGACTGTGCCAGTGAGACGTCAT
GCCTATCTTCAGCAGTTGTTCAGCAAGCCTTTCTTCAGAGAGACCGAAGAGCTAGATGTC
AACAGTCTTGTGGAGAGTATTAACAGTGAAACTCAGTCATTCTCCTTTATATCTAATTCT
TTAAAGATATTATCTTCTTTTCAAGGTGCCAAAGAAATGGGAGGGCACAATGAAAAGAAA
GTACACATTCTCGTTCCTCTCATCGGAAGGTATGACATTTTCTTGAGATTCATGGAGAAC
TTTGAAAACATGTGTCTTATCCCAAAGCAGAATGTAAAGTTGGTCATTATCCTTTTCAGT
AGGGATTCTGGCCAAGACTCCAGCAAGCATATTGAGCTGATAAAAGGGTACCAGAACAAG
TACCCCAAAGCAGAAATGACCCTGATCCCAATGAAGGGAGAGTTTTCCAGAGGTCTTGGT
CTTGAAATGGCTTCTGCCCAGTTTGACAATGACACTTTGCTGCTATTTTGTGATGTTGAC
TTGATCTTCAGAGAAGATTTTCTCCAACGATGTAGAGACAATACAATTCAGGGACAACAG
GTGTACTATCCCATCATCTTTAGCCAGTATGACCCAAAGGTAACAAACGGGGGAAATCCT
CCCACTGATGATTACTTCATATTCTCAAAAAAGACTGGATTTTGGAGAGACTATGGATAT
GGCATCACCTGTATTTACAAAAGTGATCTTCTAGGTGCAGGTGGATTTGATACCTCAATA
CAAGGCTGGGGACTAGAAGATGTAGATCTCTACAATAAAGTCATTCTATCTGGCTTAAGG
CCATTCAGAAGCCAAGAAGTAGGAGTGGTGCATATTTTCCATCCAGTTCATTGTGATCCT
AACTTGGACCCTAAGCAGTATAAGATGTGCTTAGGATCCAAGGCAAGTACTTTCGCCTCA
ACCATGCAACTGGCTGAACTCTGGCTTGAAAAACATTTAGGTGTCAGGTACAATCGAACT
CTCTCCTGA
Enzyme 17 GenBank Gene ID AB086062 Link Image
Enzyme 17 GeneCard ID Not Available
Enzyme 17 GenAtlas ID Not Available
Enzyme 17 HGNC ID Not Available
Enzyme 17 Chromosome Location 5
Enzyme 17 Locus 5q23.3
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Yada T, Sato T, Kaseyama H, Gotoh M, Iwasaki H, Kikuchi N, Kwon YD, Togayachi A, Kudo T, Watanabe H, Narimatsu H, Kimata K: Chondroitin sulfate synthase-3. Molecular cloning and characterization. J Biol Chem. 2003 Oct 10;278(41):39711-25. Epub 2003 Aug 7. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 6393
Enzyme 18 Name Chondroitin sulfate synthase 2
Enzyme 18 Synonyms
  1. Glucuronosyl-N- acetylgalactosaminyl-proteoglycan 4-beta-N- acetylgalactosaminyltransferase II
  2. N-acetylgalactosaminyl- proteoglycan 3-beta-glucuronosyltransferase II
  3. Chondroitin glucuronyltransferase II
  4. N- acetylgalactosaminyltransferase
  5. Chondroitin-polymerizing factor
Enzyme 18 Gene Name CSS2
Enzyme 18 Protein Sequence >Chondroitin sulfate synthase 2
MRASLLLSVLRPAGPVAVGISLGFTLSLLSVTWVEEPCGPGPPQPGDSELPPRGNTNAAR
RPNSVQPGAEREKPGAGEGAGENWEPRVLPYHPAQPGQAAKKAVRTRYISTELGIRQRLL
VAVLTSQTTLPTLGVAVNRTLGHRLERVVFLTGARGRRAPPGMAVVTLGEERPIGHLHLA
LRHLLEQHGDDFDWFFLVPDTTYTEAHGLARLTGHLSLASAAHLYLGRPQDFIGGEPTPG
RYCHGGFGVLLSRMLLQQLRPHLEGCRNDIVSARPDEWLGRCILDATGVGCTGDHEGVHY
SHLELSPGEPVQEGDPHFRSALTAHPVRDPVHMYQLHKAFARAELERTYQEIQELQWEIQ
NTSHLAVDGDRAAAWPVGIPAPSRPASRFEVLRWDYFTEQHAFSCADGSPRCPLRGADRA
DVADVLGTALEELNRRYHPALRLQKQQLVNGYRRFDPARGMEYTLDLQLEALTPQGGRRP
LTRRVQLLRPLSRVEILPVPYVTEASRLTVLLPLAAAERDLAPGFLEAFATAALEPGDAA
AALTLLLLYEPRQAQRVAHADVFAPVKAHVAELERRFPGARVPWLSVQTAAPSPLRLMDL
LSKKHPLDTLFLLAGPDTVLTPDFLNRCRMHAISGWQAFFPMHFQAFHPAVAPPQGPGPP
ELGRDTGRFDRQAASEACFYNSDYVAARGRLAAASEQEEELLESLDVYELFLHFSSLHVL
RAVEPALLQRYRAQTCSARLSEDLYHRCLQSVLEGLGSRTQLAMLLFEQEQGNST
Enzyme 18 Number of Residues 775
Enzyme 18 Molecular Weight 85496
Enzyme 18 Theoretical pI 6.99
Enzyme 18 GO Classification Not Available
Enzyme 18 General Function Not Available
Enzyme 18 Specific Function Has both beta-1,3-glucuronic acid and beta-1,4-N- acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer
Enzyme 18 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 18 Reactions
  • UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-34
Enzyme 18 Transmembrane Regions Not Available
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 32170677 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q8IZ52 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name CHSS2_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >2328 bp
ATGCGGGCATCGCTGCTGCTGTCGGTGCTGCGGCCCGCAGGGCCCGTGGCCGTGGGCATC
TCCCTGGGCTTCACCCTGAGCCTGCTCAGCGTCACCTGGGTGGAGGAGCCGTGCGGCCCA
GGCCCGCCCCAACCTGGAGACTCTGAGCTGCCGCCGCGCGGCAACACCAACGCGGCGCGC
CGGCCCAACTCGGTGCAGCCCGGAGCGGAGCGCGAGAAGCCCGGGGCCGGCGAAGGCGCC
GGGGAGAATTGGGAGCCGCGCGTCTTGCCCTACCACCCTGCACAGCCCGGCCAGGCCGCC
AAAAAGGCCGTCAGGACCCGCTACATCAGCACGGAGCTGGGCATCAGGCAGAGGCTGCTG
GTGGCGGTGCTGACCTCTCAGACCACGCTGCCCACGCTGGGCGTGGCCGTGAACCGCACG
CTGGGGCACCGGCTGGAGCGTGTGGTGTTCCTGACGGGCGCACGGGGCCGCCGGGCCCCA
CCTGGCATGGCAGTGGTGACGCTGGGCGAGGAGCGACCCATTGGACACCTGCACCTGGCG
CTGCGCCACCTGCTGGAGCAGCACGGCGACGACTTTGACTGGTTCTTCCTGGTGCCTGAC
ACCACCTACACCGAGGCGCACGGCCTGGCACGCCTAACTGGCCACCTCAGCCTGGCCTCC
GCCGCCCACCTGTACCTGGGCCGGCCCCAGGACTTCATCGGCGGAGAGCCCACCCCCGGC
CGCTACTGCCACGGAGGCTTTGGGGTGCTGCTGTCGCGCATGCTGCTGCAACAACTGCGC
CCCCACCTGGAAGGCTGCCGCAACGACATCGTCAGTGCGCGCCCTGACGAGTGGCTGGGT
CGCTGCATTCTCGATGCCACCGGGGTGGGCTGCACTGGTGACCACGAGGGGGTGCACTAT
AGCCATCTGGAGCTGAGCCCTGGGGAGCCAGTGCAGGAGGGGGACCCTCATTTCCGAAGT
GCCCTGACAGCCCACCCTGTGCGTGACCCTGTGCACATGTACCAGCTGCACAAAGCTTTC
GCCCGAGCTGAACTGGAACGCACGTACCAGGAGATCCAGGAGTTACAGTGGGAGATCCAG
AATACCAGCCATCTGGCCGTTGATGGGGACCGGGCAGCTGCTTGGCCCGTGGGTATTCCA
GCACCATCCCGCCCGGCCTCCCGCTTTGAGGTGCTGCGCTGGGACTACTTCACGGAGCAG
CACGCTTTCTCCTGCGCCGATGGCTCACCCCGCTGCCCACTGCGTGGGGCTGACCGGGCT
GATGTGGCCGATGTTCTGGGGACAGCTCTAGAGGAGCTGAACCGCCGCTACCACCCGGCC
TTGCGGCTCCAGAAGCAGCAGCTGGTGAATGGCTACCGACGCTTTGATCCGGCCCGGGGT
ATGGAATACACGCTGGACTTGCAGCTGGAGGCACTGACCCCCCAGGGAGGCCGCCGGCCC
CTCACTCGCCGAGTGCAGCTGCTCCGGCCGCTGAGCCGCGTGGAGATCTTGCCTGTGCCC
TATGTCACTGAGGCCTCACGTCTCACTGTGCTGCTGCCTCTAGCTGCGGCTGAGCGTGAC
CTGGCCCCTGGCTTCTTGGAGGCCTTTGCCACTGCAGCACTGGAGCCTGGTGATGCTGCG
GCAGCCCTGACCCTGCTGCTACTGTATGAGCCGCGCCAGGCCCAGCGCGTGGCCCATGCA
GATGTCTTCGCACCTGTCAAGGCCCACGTGGCAGAGCTGGAGCGGCGTTTCCCCGGTGCC
CGGGTGCCATGGCTCAGTGTGCAGACAGCCGCACCCTCACCACTGCGCCTCATGGATCTA
CTCTCCAAGAAGCACCCGCTGGACACACTGTTCCTGCTGGCCGGGCCAGACACGGTGCTC
ACGCCTGACTTCCTGAACCGCTGCCGCATGCATGCCATCTCCGGCTGGCAGGCCTTCTTT
CCCATGCATTTCCAAGCCTTCCACCCAGCTGTGGCCCCACCACAAGGGCCTGGGCCCCCA
GAGCTGGGCCGTGACACTGGCCGCTTTGATCGCCAGGCAGCCAGCGAGGCCTGCTTCTAC
AACTCCGACTACGTGGCAGCCCGTGGGCGCCTGGCGGCAGCCTCAGAACAAGAAGAGGAG
CTGCTGGAGAGCCTGGATGTGTACGAGCTGTTCCTCCACTTCTCCAGTCTGCATGTGCTG
CGGGCGGTGGAGCCGGCGCTGCTGCAGCGCTACCGGGCCCAGACGTGCAGCGCGAGGCTC
AGTGAGGACCTGTACCACCGCTGCCTCCAGAGCGTGCTTGAGGGCCTCGGCTCCCGAACC
CAGCTGGCCATGCTACTCTTTGAACAGGAGCAGGGCAACAGCACCTGA
Enzyme 18 GenBank Gene ID AB095813 Link Image
Enzyme 18 GeneCard ID Not Available
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
  1. Kitagawa H, Izumikawa T, Uyama T, Sugahara K: Molecular cloning of a chondroitin polymerizing factor that cooperates with chondroitin synthase for chondroitin polymerization. J Biol Chem. 2003 Jun 27;278(26):23666-71. Epub 2003 Apr 25. [PubMed Link Image]
  2. Yada T, Gotoh M, Sato T, Shionyu M, Go M, Kaseyama H, Iwasaki H, Kikuchi N, Kwon YD, Togayachi A, Kudo T, Watanabe H, Narimatsu H, Kimata K: Chondroitin sulfate synthase-2. Molecular cloning and characterization of a novel human glycosyltransferase homologous to chondroitin sulfate glucuronyltransferase, which has dual enzymatic activities. J Biol Chem. 2003 Aug 8;278(32):30235-47. Epub 2003 May 20. [PubMed Link Image]
  3. 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]
  4. Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 6394
Enzyme 19 Name Chondroitin sulfate synthase 1
Enzyme 19 Synonyms
  1. Glucuronosyl-N- acetylgalactosaminyl-proteoglycan 4-beta-N- acetylgalactosaminyltransferase 1
  2. N-acetylgalactosaminyl- proteoglycan 3-beta-glucuronosyltransferase 1
  3. Chondroitin glucuronyltransferase II
  4. N- acetylgalactosaminyltransferase II
Enzyme 19 Gene Name CHSY1
Enzyme 19 Protein Sequence >Chondroitin sulfate synthase 1
MAARGRRAWLSVLLGLVLGFVLASRLVLPRASELKRAGPRRRASPEGCRSGQAAASQAGG
ARGDARGAQLWPPGSDPDGGPRDRNFLFVGVMTAQKYLQTRAVAAYRTWSKTIPGKVQFF
SSEGSDTSVPIPVVPLRGVDDSYPPQKKSFMMLKYMHDHYLDKYEWFMRADDDVYIKGDR
LENFLRSLNSSEPLFLGQTGLGTTEEMGKLALEPGENFCMGGPGVIMSREVLRRMVPHIG
KCLREMYTTHEDVEVGRCVRRFAGVQCVWSYEMQQLFYENYEQNKKGYIRDLHNSKIHQA
ITLHPNKNPPYQYRLHSYMLSRKISELRHRTIQLHREIVLMSKYSNTEIHKEDLQLGIPP
SFMRFQPRQREEILEWEFLTGKYLYSAVDGQPPRRGMDSAQREALDDIVMQVMEMINANA
KTRGRIIDFKEIQYGYRRVNPMYGAEYILDLLLLYKKHKGKKMTVPVRRHAYLQQTFSKI
QFVEHEELDAQELAKRINQESGSLSFLSNSLKKLVPFQLPGSKSEHKEPKDKKINILIPL
SGRFDMFVRFMGNFEKTCLIPNQNVKLVVLLFNSDSNPDKAKQVELMRDYRIKYPKADMQ
ILPVSGEFSRALALEVGSSQFNNESLLFFCDVDLVFTTEFLQRCRANTVLGQQIYFPIIF
SQYDPKIVYSGKVPSDNHFAFTQKTGFWRNYGFGITCIYKGDLVRVGGFDVSIQGWGLED
VDLFNKVVQAGLKTFRSQEVGVVHVHHPVFCDPNLDPKQYKMCLGSKASTYGSTQQLAEM
WLEKNDPSYSKSSNNNGSVRTA
Enzyme 19 Number of Residues 802
Enzyme 19 Molecular Weight 91786
Enzyme 19 Theoretical pI 9.63
Enzyme 19 GO Classification Not Available
Enzyme 19 General Function Not Available
Enzyme 19 Specific Function Has both beta-1,3-glucuronic acid and beta-1,4-N- acetylgalactosamine transferase activity. Transfers glucuronic acid (GlcUA) from UDP-GlcUA and N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of the elongating chondroitin polymer
Enzyme 19 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 19 Reactions
  • UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-23
Enzyme 19 Transmembrane Regions Not Available
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 15617453 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q86X52 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name CHSS1_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >2409 bp
ATGGCCGCGCGCGGCCGGCGCGCCTGGCTCAGCGTGCTGCTCGGGCTCGTCCTGGGCTTC
GTGCTGGCCTCGCGGCTCGTCCTGCCCCGGGCTTCCGAGCTGAAGCGAGCGGGCCCACGG
CGCCGCGCCAGCCCCGAGGGCTGCCGGTCCGGGCAGGCGGCGGCTTCCCAGGCCGGCGGG
GCGCGCGGCGATGCGCGCGGGGCGCAGCTCTGGCCGCCCGGCTCGGACCCAGATGGCGGC
CCGCGCGACAGGAACTTTCTCTTCGTGGGAGTCATGACCGCCCAGAAATACCTGCAGACT
CGGGCCGTGGCCGCCTACAGAACATGGTCCAAGACAATTCCTGGGAAAGTTCAGTTCTTC
TCAAGTGAGGGTTCTGACACATCTGTACCAATTCCAGTAGTGCCACTACGGGGTGTGGAC
GACTCCTACCCGCCCCAGAAGAAGTCCTTCATGATGCTCAAGTACATGCACGACCACTAC
TTGGACAAGTATGAATGGTTTATGAGAGCAGATGATGACGTGTACATCAAAGGAGACCGT
CTGGAGAACTTCCTGAGGAGTTTGAACAGCAGCGAGCCCCTCTTTCTTGGGCAGACAGGC
CTGGGCACCACGGAAGAAATGGGAAAACTGGCCCTGGAGCCTGGTGAGAACTTCTGCATG
GGGGGGCCTGGCGTGATCATGAGCCGGGAGGTGCTTCGGAGAATGGTGCCGCACATTGGC
AAGTGTCTCCGGGAGATGTACACCACCCATGAGGACGTGGAGGTGGGAAGGTGTGTCCGG
AGGTTTGCAGGGGTGCAGTGTGTCTGGTCTTATGAGATGCAGCAGCTTTTTTATGAGAAT
TACGAGCAGAACAAAAAGGGGTACATTAGAGATCTCCATAACAGTAAAATTCACCAAGCT
ATCACATTACACCCCAACAAAAACCCACCCTACCAGTACAGGCTCCACAGCTACATGCTG
AGCCGCAAGATATCCGAGCTCCGCCATCGCACAATACAGCTGCACCGCGAAATTGTCCTG
ATGAGCAAATACAGCAACACAGAAATTCATAAAGAGGACCTCCAGCTGGGAATCCCTCCC
TCCTTCATGAGGTTTCAGCCCCGCCAGCGAGAGGAGATTCTGGAATGGGAGTTTCTGACT
GGAAAATACTTGTATTCGGCAGTTGACGGCCAGCCCCCTCGAAGAGGAATGGACTCCGCC
CAGAGGGAAGCCTTGGACGACATTGTCATGCAGGTCATGGAGATGATCAATGCCAACGCC
AAGACCAGAGGGCGCATCATTGACTTCAAAGAGATCCAGTACGGCTACCGCCGGGTGAAC
CCCATGTATGGGGCTGAGTACATCCTGGACCTGCTGCTTCTGTACAAAAAGCACAAAGGG
AAGAAAATGACGGTCCCTGTGAGGAGGCACGCGTATTTACAGCAGACTTTCAGCAAAATC
CAGTTTGTGGAGCATGAGGAGCTGGATGCACAAGAGTTGGCCAAGAGAATCAATCAGGAA
TCTGGATCCTTGTCCTTTCTCTCAAACTCCCTGAAGAAGCTCGTCCCCTTTCAGCTCCCT
GGGTCGAAGAGTGAGCACAAAGAACCCAAAGATAAAAAGATAAACATACTGATTCCTTTG
TCTGGGCGTTTCGACATGTTTGTGAGATTTATGGGAAACTTTGAGAAGACGTGTCTTATC
CCCAATCAGAACGTCAAGCTCGTGGTTCTGCTTTTCAATTCTGACTCCAACCCTGACAAG
GCCAAACAAGTTGAACTGATGACAGATTACCGCATTAAGTACCCTAAAGCCGACATGCAG
ATTTTGCCTGTGTCTGGAGAGTTTTCAAGAGCCCTGGCCCTGGAAGTAGGATCCTCCCAG
TTTAACAATGAATCTTTGCTCTTCTTCTGCGACGTCGACCTCGTCTTTACTACAGAATTC
CTTCAGCGATGTCGAGCAAATACAGTTCTGGGCCAACAAATATATTTTCCAATCATCTTC
AGCCAGTATGACCCAAAGATTGTTTATAGTGGGAAAGTTCCCAGTGACAACCATTTTGCC
TTTACTCAGAAAACTGGCTTCTGGAGAAACTATGGGTTTGGCATCACGTGTATTTATAAG
GGAGATCTTGTCCGAGTGGGTGGCTTTGATGTTTCCATCCAAGGCTGGGGGCTGGAGGAT
GTGGACCTTTTCAACAAGGTTGTCCAGGCAGGTTTGAAGACGTTTAGGAGCCAGGAAGTA
GGAGTAGTCCACGTCCACCATCCTGTCTTTTGTGATCCCAATCTTGACCCCAAACAGTAC
AAAATGTGCTTGGGGTCCAAAGCATCGACCTATGGGTCCACACAGCAGCTGGCTGAGATG
TGGCTGGAAAAAAATGATCCAAGTTACAGTAAAAGCAGCAATAATAATGGCTCAGTGAGG
ACAGCCTAA
Enzyme 19 GenBank Gene ID AB071402 Link Image
Enzyme 19 GeneCard ID CHSY1 Link Image
Enzyme 19 GenAtlas ID CHSY1 Link Image
Enzyme 19 HGNC ID HGNC:17198 Link Image
Enzyme 19 Chromosome Location 15
Enzyme 19 Locus 15q26.3
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed Link Image]
  2. 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]
  3. Kitagawa H, Izumikawa T, Uyama T, Sugahara K: Molecular cloning of a chondroitin polymerizing factor that cooperates with chondroitin synthase for chondroitin polymerization. J Biol Chem. 2003 Jun 27;278(26):23666-71. Epub 2003 Apr 25. [PubMed Link Image]
  4. Yada T, Sato T, Kaseyama H, Gotoh M, Iwasaki H, Kikuchi N, Kwon YD, Togayachi A, Kudo T, Watanabe H, Narimatsu H, Kimata K: Chondroitin sulfate synthase-3. Molecular cloning and characterization. J Biol Chem. 2003 Oct 10;278(41):39711-25. Epub 2003 Aug 7. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 7038
Enzyme 20 Name Hyaluronan synthase 1
Enzyme 20 Synonyms
  1. Hyaluronate synthase 1
  2. Hyaluronic acid synthase 1
  3. HA synthase 1
  4. HuHAS1
Enzyme 20 Gene Name HAS1
Enzyme 20 Protein Sequence >Hyaluronan synthase 1
MRQQDAPKPTPAARRCSGLARRVLTIAFALLILGLMTWAYAAGVPLASDRYGLLAFGLYG
AFLSAHLVAQSLFAYLEHRRVAAAARGPLDAATARSVALTISAYQEDPAYLRQCLASARA
LLYPRARLRVLMVVDGNRAEDLYMVDMFREVFADEDPATYVWDGNYHQPWEPAAAGAVGA
GAYREVEAEDPGRLAVEALVRTRRCVCVAQRWGGKREVMYTAFKALGDSVDYVQVCDSDT
RLDPMALLELVRVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFH
CVSCISGPLGLYRNNLLQQFLEAWYNQKFLGTHCTFGDDRHLTNRMLSMGYATKYTSRSR
CYSETPSSFLRWLSQQTRWSKSYFREWLYNALWWHRHHAWMTYEAVVSGLFPFFVAATVL
RLFYAGRPWALLWVLLCVQGVALAKAAFAAWLRGCLRMVLLSLYAPLYMCGLLPAKFLAL
VTMNQSGWGTSGRRKLAANYVPLLPLALWALLLLGGLVRSVAHEARADWSGPSRAAEAYH
LAAGAGAYVGYWVAMLTLYWVGVRRLCRRRTGGYRVQV
Enzyme 20 Number of Residues 578
Enzyme 20 Molecular Weight 64886
Enzyme 20 Theoretical pI 9.47
Enzyme 20 GO Classification Not Available
Enzyme 20 General Function Cell wall/membrane/envelope biogenesis
Enzyme 20 Specific Function Plays a role in hyaluronan/hyaluronic acid (HA) synthesis. Also able to catalyze the synthesis of chito- oligosaccharide depending on the substrate
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions
  • n UDP-N-acetyl-D-glucosamine + n UDP-D-glucuronate = [beta-N-acetyl-D-glucosaminyl(1-> 4)beta-D-glucuronosyl(1-> 3)]n+ 2n UDP
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 26-46 53-73 400-420 431-451 458-478 498-518 541-561
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 1556465 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q92839 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name HAS1_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1737 bp
ATGAGACAGCAGGACGCGCCCAAGCCCACTCCTGCAGCCCGCCGCTGCTCCGGCCTGGCC
CGGAGGGTGCTGACCATCGCCTTCGCCCTGCTCATCCTGGGCCTCATGACCTGGGCCTAC
GCCGCCGGGGTGCCGCTGGCCTCCGATCGCTACGGCCTCCTGGCCTTCGGCCTCTACGGG
GCCTTCCTTTCAGCGCACCTGGTGGCGCAGAGCCTCTTCGCGTACCTGGAGCACCGGCGG
GTGGCGGCGGCGGCGCGGGGGCCGCTGGATGCAGCCACCGCGCGCAGTGTGGCGCTGACC
ATCTCCGCCTACCAGGAGGACCCCGCGTACCTGCGCCAGTGCCTGGCGTCCGCCCGCGCC
CTGCTGTACCCGCGCGCGCGGCTGCGCGTCCTCATGGTGGTGGATGGCAACCGCGCCGAG
GACCTCTACATGGTCGACATGTTCCGCGAGGTCTTCGCTGACGAGGACCCCGCCACGTAC
GTGTGGGACGGCAACTACCACCAGCCCTGGGAACCCGCGGCGGCGGGCGCGGTGGGCGCC
GGAGCCTATCGGGAGGTGGAGGCGGAGGATCCTGGGCGGCTGGCAGTGGAGGCGCTGGTG
AGGACTCGCAGGTGCGTGTGCGTGGCGCAGCGCTGGGGCGGCAAGCGCGAGGTCATGTAC
ACAGCCTTCAAGGCGCTCGGAGATTCGGTGGACTACGTGCAGGTCTGTGACTCGGACACA
AGGTTGGACCCCATGGCACTGCTGGAGCTCGTGCGGGTACTGGACGAGGACCCCCGGGTA
GGGGCTGTTGGTGGGGACGTGCGGATCCTTAACCCTCTGGACTCCTGGGTCAGCTTCCTA
AGCAGCCTGCGATACTGGGTAGCCTTCAATGTGGAGCGGGCTTGTCAGAGCTACTTCCAC
TGTGTATCCTGCATCAGCGGTCCTCTAGGCCTATATAGGAATAACCTCTTGCAGCAGTTT
CTTGAGGCCTGGTACAACCAGAAGTTCCTGGGTACCCACTGTACTTTTGGGGATGACCGG
CACCTCACCAACCGCATGCTCAGCATGGGTTATGCTACCAAGTACACCTCCAGGTCCCGC
TGCTACTCAGAGACGCCCTCGTCCTTCCTGCGGTGGCTGAGCCAGCAGACACGCTGGTCC
AAGTCGTACTTCCGTGAGTGGCTGTACAACGCGCTCTGGTGGCACCGGCACCATGCGTGG
ATGACCTACGAGGCGGTGGTCTCCGGCCTGTTCCCCTTCTTCGTGGCGGCCACTGTGCTG
CGTCTGTTCTACGCGGGCCGCCCTTGGGCGCTGCTGTGGGTGCTGCTGTGCGTGCAGGGC
GTGGCACTGGCCAAGGCGGCCTTCGCGGCCTGGCTGCGGGGCTGCCTGCGCATGGTGCTT
CTCTCGCTCTACGCGCCCCTCTACATGTGTGGCCTCCTGCCTGCCAAGTTCCTGGCGCTA
GTCACCATGAACCAGAGTGGCTGGGGCACCTCGGGCCGGCGGAAGCTGGCCGCTAACTAC
GTCCCTCTGCTGCCCCTGGCGCTCTGGGCGCTGCTGCTGCTTGGGGGCCTGGTCCGCAGC
GTAGCACACGAGGCCAGGGCCGACTGGAGCGGCCCTTCCCGCGCAGCCGAGGCCTACCAC
TTGGCCGCGGGGGCCGGCGCCTACGTGGGCTACTGGGTGGCCATGTTGACGCTGTACTGG
GTGGGCGTGCGGAGGCTTTGCCGGCGGCGGACCGGGGGCTACCGCGTCCAGGTGTGA
Enzyme 20 GenBank Gene ID U59269 Link Image
Enzyme 20 GeneCard ID HAS1 Link Image
Enzyme 20 GenAtlas ID HAS1 Link Image
Enzyme 20 HGNC ID HGNC:4818 Link Image
Enzyme 20 Chromosome Location 19
Enzyme 20 Locus 19q13.4
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Shyjan AM, Heldin P, Butcher EC, Yoshino T, Briskin MJ: Functional cloning of the cDNA for a human hyaluronan synthase. J Biol Chem. 1996 Sep 20;271(38):23395-9. [PubMed Link Image]
  2. Itano N, Kimata K: Molecular cloning of human hyaluronan synthase. Biochem Biophys Res Commun. 1996 May 24;222(3):816-20. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 7046
Enzyme 21 Name Hyaluronan synthase 3
Enzyme 21 Synonyms
  1. Hyaluronate synthase 3
  2. Hyaluronic acid synthase 3
  3. HA synthase 3
Enzyme 21 Gene Name HAS3
Enzyme 21 Protein Sequence >Hyaluronan synthase 3
MPVQLTTALRVVGTSLFALAVLGGILAAYVTGYQFIHTEKHYLSFGLYGAILGLHLLIQS
LFAFLEHRRMRRAGQALKLPSPRRGSVALCIAAYQEDPDYLRKCLRSAQRISFPDLKVVM
VVDGNRQEDAYMLDIFHEVLGGTEQAGFFVWRSNFHEAGEGETEASLQEGMDRVRDVVRA
STFSCIMQKWGGKREVMYTAFKALGDSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGG
VGGDVQILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLE
DWYHQKFLGSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKS
YFREWLYNSLWFHKHHLWMTYESVVTGFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVG
IIKATYACFLRGNAEMIFMSLYSLLYMSSLLPAKIFAIATINKSGWGTSGRKTIVVNFIG
LIPVSIWVAVLLEGLAYTAYCQDLFSETELAFLVSGAILYGCYWVALLMLYLAIIARRCG
KKPEQYSLAFAEV
Enzyme 21 Number of Residues 553
Enzyme 21 Molecular Weight 63071
Enzyme 21 Theoretical pI 8.48
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Cell wall/membrane/envelope biogenesis
Enzyme 21 Specific Function Plays a role in hyaluronan/hyaluronic acid (HA) synthesis
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions
  • n UDP-N-acetyl-D-glucosamine + n UDP-D-glucuronate = [beta-N-acetyl-D-glucosaminyl(1-> 4)beta-D-glucuronosyl(1-> 3)]n+ 2n UDP
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • 1-27
Enzyme 21 Transmembrane Regions Not Available
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 7110558 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID O00219 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name HAS3_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1662 bp
ATGCCGGTGCAGCTGACGACAGCCCTGCGTGTGGTGGGCACCAGCCTGTTTGCCCTGGCA
GTGCTGGGTGGCATCCTGGCAGCCTATGTGACGGGCTACCAGTTCATCCACACGGAAAAG
CACTACCTGTCCTTCGGCCTGTACGGCGCCATCCTGGGCCTGCACCTGCTCATTCAGAGC
CTTTTTGCCTTCCTGGAGCACCGGCGCATGCGACGTGCCGGCCAGGCCCTGAAGCTGCCC
TCCCCGCGGCGGGGCTCGGTGGCACTGTGCATTGCCGCATACCAGGAGGACCCTGACTAC
TTGCGCAAGTGCCTGCGCTCGGCCCAGCGCATCTCCTTCCCTGACCTCAAGGTGGTCATG
GTGGTGGATGGCAACCGCCAGGAGGACGCCTACATGCTGGACATCTTCCACGAGGTGCTG
GGCGGCACCGAGCAGGCCGGCTTCTTTGTGTGGCGCAGCAACTTCCATGAGGCAGGCGAG
GGTGAGACGGAGGCCAGCCTGCAGGAGGGCATGGACCGTGTGCGGGATGTGGTGCGGGCC
AGCACCTTCTCGTGCATCATGCAGAAGTGGGGAGGCAAGCGCGAGGTCATGTACACGGCC
TTCAAGGCCCTCGGCGATTCGGTGGACTACATCCAGGTGTGCGACTCTGACACTGTGCTG
GATCCAGCCTGCACCATCGAGATGCTTCGAGTCCTGGAGGAGGATCCCCAAGTAGGGGGA
GTCGGGGGAGATGTCCAGATCCTCAACAAGTACGACTCATGGATTTCCTTCCTGAGCAGC
GTGCGGTACTGGATGGCCTTCAACGTGGAGCGGGCCTGCCAGTCCTACTTTGGCTGTGTG
CAGTGTATTAGTGGGCCCTTGGGCATGTACCGCAACAGCCTCCTCCAGCAGTTCCTGGAG
GACTGGTACCATCAGAAGTTCCTAGGCAGCAAGTGCAGCTTCGGGGATGACCGGCACCTC
ACCAACCGAGTCCTGAGCCTTGGCTACCGAACTAAGTATACCGCGCGCTCCAAGTGCCTC
ACAGAGACCCCCACTAAGTACCTCCGGTGGCTCAACCAGCAAACCCGCTGGAGCAAGTCT
TACTTCCGGGAGTGGCTCTACAACTCTCTGTGGTTCCATAAGCACCACCTCTGGATGACC
TACGAGTCAGTGGTCACGGGTTTCTTCCCCTTCTTCCTCATTGCCACGGTTATACAGCTT
TTCTACCGGGGCCGCATCTGGAACATTCTCCTCTTCCTGCTGACGGTGCAGCTGGTGGGC
ATTATCAAGGCCACCTACGCCTGCTTCCTTCGGGGCAATGCAGAGATGATCTTCATGTCC
CTCTACTCCCTCCTCTATATGTCCAGCCTTCTGCCGGCCAAGATCTTTGCCATTGCTACC
ATCAACAAATCTGGCTGGGGCACCTCTGGCCGAAAAACCATTGTGGTGAACTTCATTGGC
CTCATTCCTGTGTCCATCTGGGTGGCAGTTCTCCTGGAGGGGCTGGCCTACACAGCTTAT
TGCCAGGACCTGTTCAGTGAGACAGAGCTAGCCTTCCTTGTCTCTGGGGCTATACTGTAT
GGCTGCTACTGGGTGGCCCTCCTCATGCTATATCTGGCCATCATCGCCCGGCGATGTGGG
AAGAAGCCGGAGCAGTACAGCTTGGCTTTTGCTGAGGTGTGA
Enzyme 21 GenBank Gene ID AF232772 Link Image
Enzyme 21 GeneCard ID HAS3 Link Image
Enzyme 21 GenAtlas ID HAS3 Link Image
Enzyme 21 HGNC ID HGNC:4820 Link Image
Enzyme 21 Chromosome Location 16
Enzyme 21 Locus 16q22.1
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References
  1. Spicer AP, Olson JS, McDonald JA: Molecular cloning and characterization of a cDNA encoding the third putative mammalian hyaluronan synthase. J Biol Chem. 1997 Apr 4;272(14):8957-61. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 7269
Enzyme 22 Name Hyaluronan synthase 2
Enzyme 22 Synonyms
  1. Hyaluronate synthase 2
  2. Hyaluronic acid synthase 2
  3. HA synthase 2
Enzyme 22 Gene Name HAS2
Enzyme 22 Protein Sequence >Hyaluronan synthase 2
MHCERFLCILRIIGTTLFGVSLLLGITAAYIVGYQFIQTDNYYFSFGLYGAFLASHLIIQ
SLFAFLEHRKMKKSLETPIKLNKTVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKVVMVI
DGNSEDDLYMMDIFSEVMGRDKSATYIWKNNFHEKGPGETDESHKESSQHVTQLVLSNKS
ICIMQKWGGKREVMYTAFRALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGG
DVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWY
NQEFMGNQCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFR
EWLYNAMWFHKHHLWMTYEAIITGFFPFFLIATVIQLFYRGKIWNILLFLLTVQLVGLIK
SSFASCLRGNIVMVFMSLYSVLYMSSLLPAKMFAIATINKAGWGTSGRKTIVVNFIGLIP
VSVWFTILLGGVIFTIYKESKRPFSESKQTVLIVGTLLYACYWVMLLTLYVVLINKCGRR
KKGQQYDMVLDV
Enzyme 22 Number of Residues 552
Enzyme 22 Molecular Weight 63567
Enzyme 22 Theoretical pI 8.74
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Cell wall/membrane/envelope biogenesis
Enzyme 22 Specific Function Plays a role in hyaluronan/hyaluronic acid (HA) synthesis
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions
  • n UDP-N-acetyl-D-glucosamine + n UDP-D-glucuronate = [beta-N-acetyl-D-glucosaminyl(1-> 4)beta-D-glucuronosyl(1-> 3)]n+ 2n UDP
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • 1-29
Enzyme 22 Transmembrane Regions Not Available
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 1543068 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q92819 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name HAS2_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >1659 bp
ATGCATTGTGAGAGGTTTCTATGTATCCTGAGAATAATTGGAACCACACTCTTTGGAGTC
TCTCTCCTCCTTGGAATCACAGCTGCTTATATTGTTGGCTACCAGTTTATCCAAACGGAT
AATTACTATTTCTCTTTTGGACTGTATGGTGCCTTTTTGGCATCACACCTCATCATCCAA
AGCCTGTTTGCCTTTTTGGAGCACCGAAAAATGAAAAAATCCCTAGAAACCCCCATAAAG
TTGAACAAAACAGTTGCCCTTTGCATCGCTGCCTATCAAGAAGATCCAGACTACTTAAGG
AAATGTTTGCAATCTGTGAAAAGGCTAACCTACCCTGGGATTAAAGTTGTCATGGTCATA
GATGGGAACTCAGAAGATGACCTTTACATGATGGACATCTTCAGTGAAGTCATGGGCAGA
GACAAATCAGCCACTTATATCTGGAAGAACAACTTCCACGAAAAGGGTCCCGGTGAGACA
GATGAGTCACATAAAGAAAGCTCGCAACACGTAACGCAATTGGTCTTGTCCAACAAAAGT
ATCTGCATCATGCAAAAATGGGGTGGAAAAAGAGAAGTCATGTACACAGCCTTCAGAGCA
CTGGGACGAAGTGTGGATTATGTACAGGTTTGTGATTCAGACACTATGCTTGACCCAGCC
TCATCTGTGGAGATGGTAAAAGTTTTAGAAGAAGATCCCATGGTTGGAGGTGTTGGGGGA
GATGTCCAGATTTTAAACAAGTACGATTCCTGGATCTCATTCCTCAGCAGTGTAAGATAT
TGGATGGCTTTTAATATAGAAAGGGCCTGTCAGTCTTATTTTGGGTGTGTTCAGTGCATT
AGTGGACCTCTGGGAATGTACAGAAACTCCTTGTTGCATGAGTTTGTGGAAGATTGGTAC
AATCAAGAATTTATGGGCAACCAATGTAGCTTTGGTGATGACAGGCATCTCACGAACCGG
GTGCTGAGCCTGGGCTATGCAACAAAATACACAGCTCGATCTAAGTGCCTTACTGAAACA
CCTATAGAGTATCTCAGATGGCTAAACCAGCAGACCCGTTGGAGCAAGTCCTACTTCCGA
GAATGGCTGTACAATGCAATGTGGTTTCACAAACATCACTTGTGGATGACCTACGAAGCG
ATTATCACTGGATTCTTTCCTTTCTTTCTCATTGCCACAGTAATCCAGCTCTTCTACCGG
GGTAAAATTTGGAACATTCTCCTCTTCTTGTTAACTGTCCAGCTAGTAGGTCTCATAAAA
TCATCTTTTGCCAGCTGCCTTAGAGGAAATATCGTCATGGTCTTCATGTCTCTCTACTCA
GTGTTATACATGTCGAGTTTACTTCCCGCCAAGATGTTTGCAATTGCAACAATAAACAAA
GCTGGGTGGGGCACATCAGGAAGGAAAACCATTGTTGTTAATTTCATAGGACTCATTCCA
GTATCAGTTTGGTTTACAATCCTCCTGGGTGGTGTGATTTTCACCATTTATAAGGAGTCT
AAAAGGCCATTTTCAGAATCCAAACAGACAGTTCTAATTGTTGGAACGTTGCTCTATGCA
TGCTATTGGGTCATGCTTTTGACGCTGTATGTAGTTCTCATCAATAAGTGTGGCAGGCGG
AAGAAGGGACAACAATATGACATGGTGCTTGATGTATGA
Enzyme 22 GenBank Gene ID U54804 Link Image
Enzyme 22 GeneCard ID HAS2 Link Image
Enzyme 22 GenAtlas ID HAS2 Link Image
Enzyme 22 HGNC ID HGNC:4819 Link Image
Enzyme 22 Chromosome Location 8
Enzyme 22 Locus 8q24.12
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References
  1. Watanabe K, Yamaguchi Y: Molecular identification of a putative human hyaluronan synthase. J Biol Chem. 1996 Sep 20;271(38):22945-8. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 8701
Enzyme 23 Name UDP-glucuronic acid decarboxylase 1
Enzyme 23 Synonyms
  1. UDP-glucuronate decarboxylase 1
  2. UGD
  3. UXS-1
Enzyme 23 Gene Name UXS1
Enzyme 23 Protein Sequence >UDP-glucuronic acid decarboxylase 1
MVSKALLRLVSAVNRRRMKLLLGIALLAYVASVWGNFVNMRSIQENGELKIESKIEEMVE
PLREKIRDLEKSFTQKYPPVKFLSEKDRKRILITGGAGFVGSHLTDKLMMDGHEVTVVDN
FFTGRKRNVEHWIGHENFELINHDVVEPLYIEVDQIYHLASPASPPNYMYNPIKTLKTNT
IGTLNMLGLAKRVGARLLLASTSEVYGDPEVHPQSEDYWGHVNPIGPRACYDEGKRVAET
MCYAYMKQEGVEVRVARIFNTFGPRMHMNDGRVVSNFILQALQGEPLTVYGSGSQTRAFQ
YVSDLVNGLVALMNSNVSSPVNLGNPEEHTILEFAQLIKNLVGSGSEIQFLSEAQDDPQK
RKPDIKKAKLMLGWEPVVPLEEGLNKAIHYFRKELEYQANNQYIPKPKPARIKKGRTRHS
Enzyme 23 Number of Residues 420
Enzyme 23 Molecular Weight 47577
Enzyme 23 Theoretical pI 9.35
Enzyme 23 GO Classification
Function
  • NAD binding
  • binding
  • catalytic activity
  • coenzyme binding
  • cofactor binding
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleotide-sugar metabolism
  • physiological process
Component
Enzyme 23 General Function Cell wall/membrane/envelope biogenesis
Enzyme 23 Specific Function Catalyzes the NAD-dependent decarboxylation of UDP- glucuronic acid to UDP-xylose. Necessary for the biosynthesis of the core tetrasaccharide in glycosaminoglycan biosynthesis
Enzyme 23 Pathways
Enzyme 23 Reactions
  • UDP-D-glucuronate = UDP-D-xylose + CO2
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-35
Enzyme 23 Transmembrane Regions
  • 20-40
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 24061784 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q8NBZ7 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name UXS1_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1263 bp
ATGGTGAGCAAGGCGCTGCTGCGCCTCGTGTCTGCCGTCAACCGCAGGAGGATGAAGCTG
CTGCTGGGCATCGCCTTGCTGGCCTACGTCGCCTCTGTTTGGGGCAACTTCGTTAATATG
AGGTCTATCCAGGAAAATGGTGAACTAAAAATTGAAAGCAAGATTGAAGAGATGGTTGAA
CCACTAAGAGAGAAAATCAGAGATTTAGAAAAAAGCTTTACCCAGAAATACCCACCAGTA
AAGTTTTTATCAGAAAAGGATCGGAAAAGAATTTTGATAACAGGAGGCGCAGGGTTCGTG
GGCTCCCATCTAACTGACAAACTCATGATGGACGGCCACGAGGTGACCGTGGTGGACAAT
TTCTTCACGGGCAGGAAGAGAAACGTGGAGCACTGGATCGGACATGAGAACTTCGAGTTG
ATTAACCACGACGTGGTGGAGCCCCTCTACATCGAGGTTGACCAGATATACCATCTGGCA
TCTCCAGCCTCCCCTCCAAACTACATGTATAATCCTATCAAGACATTAAAGACCAATACG
ATTGGGACATTAAACATGTTGGGGCTGGCAAAACGAGTCGGTGCCCGTCTGCTCCTGGCC
TCCACATCGGAGGTGTATGGAGATCCTGAAGTCCACCCTCAAAGTGAGGATTACTGGGGC
CACGTGAATCCAATAGGACCTCGGGCCTGCTACGATGAAGGCAAACGTGTTGCAGAGACC
ATGTGCTATGCCTACATGAAGCAGGAAGGCGTGGAAGTGCGAGTGGCCAGAATCTTCAAC
ACCTTTGGGCCACGCATGCACATGAACGATGGGCGAGTAGTCAGCAACTTCATCCTGCAG
GCGCTCCAGGGGGAGCCACTCACGGTATACGGATCCGGGTCTCAGACAAGGGCGTTCCAG
TACGTCAGCGATCTAGTGAATGGCCTCGTGGCTCTCATGAACAGCAACGTCAGCAGCCCG
GTCAACCTGGGGAACCCAGAAGAACACACAATCCTAGAATTTGCTCAGTTAATTAAAAAC
CTTGTTGGTAGCGGAAGTGAAATTCAGTTTCTCTCCGAAGCCCAGGATGACCCACAGAAA
AGAAAACCAGACATCAAAAAAGCAAAGCTGATGCTGGGGTGGGAGCCCGTGGTCCCGCTG
GAGGAAGGTTTAAACAAAGCAATTCACTACTTCCGTAAAGAACTCGAGTACCAGGCAAAT
AATCAGTACATCCCCAAACCAAAGCCTGCCAGAATAAAGAAAGGACGGACTCGCCACAGC
TGA
Enzyme 23 GenBank Gene ID AY147934 Link Image
Enzyme 23 GeneCard ID UXS1 Link Image
Enzyme 23 GenAtlas ID UXS1 Link Image
Enzyme 23 HGNC ID HGNC:17729 Link Image
Enzyme 23 Chromosome Location 2
Enzyme 23 Locus 2q12.2
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Hwang HY, Horvitz HR: The SQV-1 UDP-glucuronic acid decarboxylase and the SQV-7 nucleotide-sugar transporter may act in the Golgi apparatus to affect Caenorhabditis elegans vulval morphogenesis and embryonic development. Proc Natl Acad Sci U S A. 2002 Oct 29;99(22):14218-23. Epub 2002 Oct 21. [PubMed Link Image]
  2. 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 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 12970
Enzyme 24 Name UDP-glucuronosyltransferase 2A3 precursor
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name UGT2A3
Enzyme 24 Protein Sequence >UDP-glucuronosyltransferase 2A3 precursor
MRSDKSALVFLLLQLFCVGCGFCGKVLVWPCDMSHWLNVKVILEELIVRGHEVTVLTHSK
PSLIDYRKPSALKFEVVHMPQDRTEENEIFVDLALNVLPGLSTWQSVIKLNDFFVEIRGT
LKMMCESFIYNQTLMKKLQETNYDVMLIDPVIPCGDLMAELLAVPFVLTLRISVGGNMER
SCGKLPAPLSYVPVPMTGLTDRMTFLERVKNSMLSVLFHFWIQDYDYHFWEEFYSKALGR
PTTLCETVGKAEIWLIRTYWDFEFPQPYQPNFEFVGGLHCKPAKALPKEMENFVQSSGED
GIVVFSLGSLFQNVTEEKANIIASALAQIPQKVLWRYKGKKPSTLGANTRLYDWIPQNDL
LGHPKTKAFITHGGMNGIYEAIYHGVPMVGVPIFGDQLDNIAHMKAKGAAVEINFKTMTS
EDLLRALRTVITDSSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRSAAHD
LTWFQHYSIDVIGFLLTCVATAIFLFTKCFLFSCQKFNKTRKIEKRE
Enzyme 24 Number of Residues 527
Enzyme 24 Molecular Weight 60285
Enzyme 24 Theoretical pI 8.04
Enzyme 24 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 24 General Function Carbohydrate transport and metabolism
Enzyme 24 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 24 Pathways
Enzyme 24 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 24 Pfam Domain Function
Enzyme 24 Signals
  • 1-23
Enzyme 24 Transmembrane Regions
  • 492-512
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 44889644 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID Q6UWM9 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name UD2A3_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence Not Available
Enzyme 24 GenBank Gene ID AY542891 Link Image
Enzyme 24 GeneCard ID Q6UWM9 Link Image
Enzyme 24 GenAtlas ID UGT2A3 Link Image
Enzyme 24 HGNC ID HGNC:28528 Link Image
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 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 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 15056
Enzyme 25 Name UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
Enzyme 25 Synonyms Not Available
Enzyme 25 Gene Name UGT1A10
Enzyme 25 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
MARAGWTSPVPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLERSLNCTVKTYSTSYTLEDQNREFMVFAHAQWKAQAQSIFSLLMSSSSGFLDLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDTCGLIVAKYFSLPSVVFTRGIFCHHLEEG
AQCPAPLSYVPNDLLGFSDAMTFKERVWNHIVHLEDHLFCQYLFRNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 25 Number of Residues 530
Enzyme 25 Molecular Weight 59810
Enzyme 25 Theoretical pI 7.31
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
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 40849852 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID Q5DT02 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name Q5DT02_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 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 25 GenBank Gene ID AY435137 Link Image
Enzyme 25 GeneCard ID Q5DT02 Link Image
Enzyme 25 GenAtlas ID UGT1A10 Link Image
Enzyme 25 HGNC ID HGNC:12531 Link Image
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References Not Available
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 15057
Enzyme 26 Name UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
Enzyme 26 Synonyms Not Available
Enzyme 26 Gene Name UGT1A8
Enzyme 26 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
MARTGWTSPIPLCVSLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGKSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVRSLFSLFLSSSNGFFNLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 26 Number of Residues 530
Enzyme 26 Molecular Weight 59742
Enzyme 26 Theoretical pI 7.73
Enzyme 26 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
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
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 40849864 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q5DSZ6 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name Q5DSZ6_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 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 26 GenBank Gene ID AY435143 Link Image
Enzyme 26 GeneCard ID Q5DSZ6 Link Image
Enzyme 26 GenAtlas ID UGT1A8 Link Image
Enzyme 26 HGNC ID HGNC:12540 Link Image
Enzyme 26 Chromosome Location Not Available
Enzyme 26 Locus Not Available
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 15058
Enzyme 27 Name UDP glycosyltransferase 1 family polypeptide A7
Enzyme 27 Synonyms Not Available
Enzyme 27 Gene Name UGT1A7
Enzyme 27 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A7
MARAGWTGLLPLYVCLLLTCGFAKAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDQDREFMVFADARWTAPLRSAFSLLTSSSNGIFDLF
FSNCRSLFNDRKLVEYLKESCFDAVFLDPFDACGLIVAKYFSLPSVVFARGIFCHYLEEG
AQCPAPLSYVPRLLLGFSDAMTFKERVWNHIMHLEEHLFCPYFFKNVLEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLEYPKPVMPNMIFIGGINCHQGKPVPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 27 Number of Residues 530
Enzyme 27 Molecular Weight 59819
Enzyme 27 Theoretical pI 7.85
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
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 40849862 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q5DSZ7 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name Q5DSZ7_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 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 27 GenBank Gene ID AY435142 Link Image
Enzyme 27 GeneCard ID Q5DSZ7 Link Image
Enzyme 27 GenAtlas ID UGT1A7 Link Image
Enzyme 27 HGNC ID HGNC:12539 Link Image
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus Not Available
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References Not Available
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 15059
Enzyme 28 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 28 Synonyms Not Available
Enzyme 28 Gene Name UGT2B10
Enzyme 28 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 28 Number of Residues 528
Enzyme 28 Molecular Weight 60775
Enzyme 28 Theoretical pI 9.40
Enzyme 28 GO Classification Not Available
Enzyme 28 General Function Carbohydrate transport and metabolism
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function Not Available
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 158258913 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID A8K9M3 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name A8K9M3_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 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 28 GenBank Gene ID AK292738 Link Image
Enzyme 28 GeneCard ID A8K9M3 Link Image
Enzyme 28 GenAtlas ID Not Available
Enzyme 28 HGNC ID Not Available
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus Not Available
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References Not Available
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 16420
Enzyme 29 Name cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
Enzyme 29 Synonyms Not Available
Enzyme 29 Gene Name Not Available
Enzyme 29 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 29 Number of Residues 529
Enzyme 29 Molecular Weight 60721
Enzyme 29 Theoretical pI 8.45
Enzyme 29 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 29 General Function Carbohydrate transport and metabolism
Enzyme 29 Specific Function Not Available
Enzyme 29 Pathways Not Available
Enzyme 29 Reactions Not Available
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein Not Available
Enzyme 29 UniProtKB/Swiss-Prot ID B2R810 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name B2R810_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence Not Available
Enzyme 29 GenBank Gene ID AK313190 Link Image
Enzyme 29 GeneCard ID B2R810 Link Image
Enzyme 29 GenAtlas ID Not Available
Enzyme 29 HGNC ID Not Available
Enzyme 29 Chromosome Location Not Available
Enzyme 29 Locus Not Available
Enzyme 29 SNPs Not Available
Enzyme 29 General References Not Available
Enzyme 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 16554
Enzyme 30 Name Chondroitin synthase-3 (Chondroitin sulfate glucuronyltransferase, isoform CRA_b)
Enzyme 30 Synonyms Not Available
Enzyme 30 Gene Name ChSy-3
Enzyme 30 Protein Sequence >Chondroitin synthase-3 (Chondroitin sulfate glucuronyltransferase, isoform CRA_b)
MRLSSLLALLRPALPLILGLSLGCSLSLLRVSWIQGEGEDPCVEAVGERGGPQNPDSRAR
LDQSDEDFKPRIVPYYRDPNKPYKKVLRTRYIQTELGSRERLLVAVLTSRATLSTLAVAV
NRTVAHHFPRLLYFTGQRGARAPAGMQVVSHGDERPAWLMSETLRHLHTHFGADYDWFFI
MQDDTYVQAPRLAALAGHLSINQDLYLGRAEEFIGAGEQARYCHGGFGYLLSRSLLLRLR
PHLDGCRGDILSARPDEWLGRCLIDSLGVGCVSQHQGQQYRSFELAKNRDPEKEGSSAFL
SAFAVHPVSEGTLMYRLHKRFSALELERAYSEIEQLQAQIRNLTVLTPEGEAGLSWPVGL
PAPFTPHSRFEVLGWDYFTEQHTFSCADGAPKCPLQGASRADVGDALETALEQLNRRYQP
RLRFQKQRLLNGYRRFDPARGMEYTLDLLLECVTQRGHRRALARRVSLLRPLSRVEILPM
PYVTEATRVQLVLPLLVAEAAAAPAFLEAFAANVLEPREHALLTLLLVYGPREGGRGAPD
PFLGVKAAAAELERRYPGTRLAWLAVRAEAPSQVRLMDVVSKKHPVDTLFFLTTVWTRPG
PEVLNRCRMNAISGWQAFFPVHFQEFNPALSPQRSPPGPPGAGPDPPSPPGADPSRGAPI
GGRFDRQASAEGCFYNADYLAARARLAGELAGQEEEEALEGLEVMDVFLRFSGLHLFRAV
EPGLVQKFSLRDCSPRLSEELYHRCRLSNLEGLGGRAQLAMALFEQEQANST
Enzyme 30 Number of Residues 772
Enzyme 30 Molecular Weight 85949
Enzyme 30 Theoretical pI 7.88
Enzyme 30 GO Classification Not Available
Enzyme 30 General Function Not Available
Enzyme 30 Specific Function Not Available
Enzyme 30 Pathways Not Available
Enzyme 30 Reactions Not Available
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein Not Available
Enzyme 30 UniProtKB/Swiss-Prot ID B2DBD8 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name B2DBD8_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence Not Available
Enzyme 30 GenBank Gene ID AB095812 Link Image
Enzyme 30 GeneCard ID B2DBD8 Link Image
Enzyme 30 GenAtlas ID Not Available
Enzyme 30 HGNC ID Not Available
Enzyme 30 Chromosome Location Not Available
Enzyme 30 Locus Not Available
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References Not Available
Enzyme 30 Metabolite References Not Available