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Human Metabolome Database Version 2.5

 

Showing metabocard for Uridine 5'-diphosphate (HMDB00295)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-24 16:23:22
Accession Number HMDB00295
Secondary Accession Numbers Not Available
Common Name Uridine 5'-diphosphate
Description A uracil nucleotide containing a pyrophosphate group esterified to C5 of the sugar moiety. UDP is an important extracellular pyrimidine signaling molecule that mediates diverse biological effects via P1 and P2 purinergic receptors, such as the uptake of thymidine and proliferation of gliomas. (PMID: 14558596) UDP induces intracellular Ca(2+) responses and oscillations in HeLa cells, due to the activation of P2Ys (G-protein coupled ATP receptors). (PMID: 1257952)
Synonyms
  1. 5'-UDP
  2. UDP
  3. Uridine 5'-diphosphate
  4. Uridine 5'-diphosphic acid
  5. Uridine 5'-pyrophosphate
  6. Uridine 5'-pyrophosphorate
  7. Uridine 5'-pyrophosphoric acid
  8. Uridine diphosphate
  9. Uridine pyrophosphate
Chemical IUPAC Name Uridine 5'-(trihydrogen diphosphate)
Chemical Formula C9H14N2O12P2
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
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 404.161
Monoisotopic Molecular Weight 404.002197
Isomeric SMILES O[C@@H]1[C@@H](COP(O)(=O)OP(O)(O)=O)O[C@H]([C@@H]1O)N1C=CC(=O)NC1=O
Canonical SMILES OC1C(COP(O)(=O)OP(O)(O)=O)OC(C1O)N1C=CC(=O)NC1=O
KEGG Compound ID C00015 Link Image
BioCyc ID UDP Link Image
BiGG ID 33518 Link Image
Wikipedia Link UDP Link Image
NuGOwiki Link HMDB00295 Link Image
Metagene Link HMDB00295 Link Image
METLIN ID Not Available
PubChem Compound 6031 Link Image
PubChem Substance 11538182 Link Image
ChEBI ID 17659 Link Image
CAS Registry Number 58-98-0
InChI Identifier InChI=1/C9H14N2O12P2/c12-5-1-2-11(9(15)10-5)8-7(14)6(13)4(22-8)3-21-25(19,20)23-24(16,17)18/h1-2,4,6-8,13-14H,3H2,(H,19,20)(H,10,12,15)(H2,16,17,18)/t4-,6-,7-,8-/m1/s1
Synthesis Reference Zeng, Bin; Rao, Linfan; Li, Gaowo. Method for manufacturing uridine diphosphate. Faming Zhuanli Shenqing Gongkai Shuomingshu (2007), 14pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 65.5 mg/mL [MEYLAN,WM et al. (1996)]; 8.89 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -0.94 [Predicted by ALOGPS]; -5 [Predicted by PubChem via XLOGP]; -3.12 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • endoplasmic reticulum
  • Extracellular
  • golgi apparatus
  • lysosome
  • mitochondria
  • nucleus
Biofluid Location
  • Blood
Tissue Location
Tissue References
Placenta
Thyroid Gland
Concentrations (Normal)
Biofluid Blood
Value 41.0 +/- 12.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Geigy Scientific Tables, 8th Rev edition, pp. 165-177. Edited by C. Lentner, West Cadwell, N.J.: Medical education Div., Ciba-Geigy Corp., Basel, Switzerland c1981-1992.
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Lactose Synthesis SMP00444 Link Image
Pyrimidine Metabolism SMP00046 Link Image map00240 Link Image
General References
  1. Brouwer A, Morse DC, Lans MC, Schuur AG, Murk AJ, Klasson-Wehler E, Bergman A, Visser TJ: Interactions of persistent environmental organohalogens with the thyroid hormone system: mechanisms and possible consequences for animal and human health. Toxicol Ind Health. 1998 Jan-Apr;14(1-2):59-84. [PubMed Link Image]
  2. Kamisako T, Kobayashi Y, Takeuchi K, Ishihara T, Higuchi K, Tanaka Y, Gabazza EC, Adachi Y: Recent advances in bilirubin metabolism research: the molecular mechanism of hepatocyte bilirubin transport and its clinical relevance. J Gastroenterol. 2000;35(9):659-64. [PubMed Link Image]
  3. Syme MR, Paxton JW, Keelan JA: Drug transfer and metabolism by the human placenta. Clin Pharmacokinet. 2004;43(8):487-514. [PubMed Link Image]
  4. Collier AC, Tingle MD, Paxton JW, Mitchell MD, Keelan JA: Metabolizing enzyme localization and activities in the first trimester human placenta: the effect of maternal and gestational age, smoking and alcohol consumption. Hum Reprod. 2002 Oct;17(10):2564-72. [PubMed Link Image]
  5. Wikipedia Link Image
Metabolic Enzymes
  1. Ectonucleoside triphosphate diphosphohydrolase 1
  2. Soluble calcium-activated nucleotidase 1
  3. Nucleoside diphosphate kinase, mitochondrial precursor
  4. Ribonucleoside-diphosphate reductase large subunit
  5. Nucleoside diphosphate kinase A
  6. Ribonucleoside-diphosphate reductase M2 subunit
  7. Nucleoside diphosphate kinase B
  8. Nucleoside diphosphate kinase 6
  9. Alpha-lactalbumin precursor
  10. UDP-glucuronosyltransferase 2B28 precursor
  11. UDP-glucuronosyltransferase 2B4 precursor
  12. UDP-glucuronosyltransferase 1-4 precursor
  13. UDP-glucuronosyltransferase 2B15 precursor
  14. UDP-glucuronosyltransferase 2A1 precursor
  15. UDP-glucuronosyltransferase 1-1 precursor
  16. UDP-glucuronosyltransferase 1-9 precursor
  17. UDP-glucuronosyltransferase 1-3 precursor
  18. UDP-glucuronosyltransferase 2B17 precursor
  19. UDP-glucuronosyltransferase 1-6 precursor
  20. UDP-glucuronosyltransferase 1-5 precursor
  21. UDP-glucuronosyltransferase 2B11 precursor
  22. GTP:AMP phosphotransferase mitochondrial
  23. 6-phosphofructokinase type C
  24. 6-phosphofructokinase, liver type
  25. 6-phosphofructokinase, muscle type
  26. Pyruvate kinase isozymes R/L
  27. Ceramide glucosyltransferase
  28. Beta-1,4 N-acetylgalactosaminyltransferase 1
  29. Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
  30. Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
  31. Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
  32. Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
  33. Polypeptide N-acetylgalactosaminyltransferase 4
  34. Polypeptide N-acetylgalactosaminyltransferase 3
  35. Polypeptide N-acetylgalactosaminyltransferase-like protein 2
  36. Polypeptide N-acetylgalactosaminyltransferase 10
  37. Putative polypeptide N-acetylgalactosaminyltransferase-like protein 4
  38. Polypeptide N-acetylgalactosaminyltransferase 6
  39. Polypeptide N-acetylgalactosaminyltransferase 14
  40. Polypeptide N-acetylgalactosaminyltransferase 2
  41. Polypeptide N-acetylgalactosaminyltransferase 12
  42. Polypeptide N-acetylgalactosaminyltransferase 1
  43. Beta-1,4-galactosyltransferase 3
  44. UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1
  45. Glycogen [starch] synthase, liver
  46. Glycogenin-1
  47. Glycogen [starch] synthase, muscle
  48. Glycogenin-2
  49. Histo-blood group ABO system transferase
  50. Chondroitin sulfate synthase 3
  51. Chondroitin sulfate synthase 2
  52. Chondroitin sulfate synthase 1
  53. Polyribonucleotide nucleotidyltransferase 1, mitochondrial precursor
  54. Hyaluronan synthase 1
  55. Exostosin-like 3
  56. Exostosin-2
  57. Exostosin-like 1
  58. N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase
  59. Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase V
  60. UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
  61. Hyaluronan synthase 3
  62. Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
  63. Hyaluronan synthase 2
  64. Uridine-cytidine kinase 2
  65. N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
  66. OTTHUMP00000018263
  67. Polypeptide N-acetylgalactosaminyltransferase 14
  68. ENTPD4 protein
  69. Beta-1,3-N-acetylglucosaminyltransferase bGnT-2
  70. Polypeptide N-acetylgalactosaminyltransferase 9
  71. Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
  72. Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
  73. UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
  74. UDP-glucuronosyltransferase 2A3 precursor
  75. Ribonucleoside-diphosphate reductase subunit M2 B
  76. LOC129607 protein
  77. Uridine/cytidine kinase-like 1
  78. Ectonucleoside triphosphate diphosphohydrolase 8
  79. Polypeptide N-acetylgalactosaminyltransferase 17
  80. Putative polypeptide N-acetylgalactosaminyltransferase-like protein 5
  81. UDP glycosyltransferase 1 family polypeptide A10 (HCG2039726, isoform CRA_f)
  82. UDP glycosyltransferase 1 family polypeptide A8 (HCG2039726, isoform CRA_e)
  83. UDP glycosyltransferase 1 family polypeptide A7
  84. cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b)
  85. cDNA FLJ76131, highly similar to Homo sapiens non-metastatic cells 7, protein expressed in (nucleoside-diphosphate kinase) (NME7), transcript variant 1, mRNA (Non-metastatic cells 7, protein expressed in (Nucleoside-diphosphate kinase), isoform CRA_a)
  86. Uridine-cytidine kinase 1 (Uridine-cytidine kinase 1, isoform CRA_e)
  87. Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
  88. Ectonucleoside triphosphate diphosphohydrolase 5 (Ectonucleoside triphosphate diphosphohydrolase 5, isoform CRA_d)
  89. cDNA FLJ75238, highly similar to Homo sapiens asparagine-linked glycosylation 14 homolog (yeast) (ALG14), mRNA (Asparagine-linked glycosylation 14 homolog (Yeast), isoform CRA_b)
  90. cDNA FLJ78031, highly similar to Homo sapiens beta3GnT6 beta-1,3-N- acetylglucosaminyltransferase 6 (HCG2018639)
  91. UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (EC 5.1.3.14) (Glucosamine (UDP-N-acetyl)-2-epimerase/N- acetylmannosamine kinase, isoform CRA_a)
  92. UDP-N-acetyl-alpha-D-galactosamine:polypeptide N- acetylgalactosaminyltransferase 5 (GalNAc-T5) (cDNA FLJ75131, highly similar to Homo sapiens UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 5 (GalNAc-T5) (GALNT5), mRNA)
  93. UDP-N-acetyl-alpha-D-galactosamine:polypeptide N- acetylgalactosaminyltransferase-like 1 (cDNA FLJ76743, highly similar to Homo sapiens UDP-N-acetyl-alpha-D-galactosamine:polypeptide N- acetylgalactosaminyltransferase-like 1 (GALNTL1), mRNA)
  94. Pp-GalNAc-transferase 20 (Williams-Beuren syndrome chromosome region 17, isoform CRA_d) (Williams-Beuren syndrome chromosome region 17) (cDNA FLJ76765, highly similar to Homo sapiens Williams-Beuren syndrome chromosome region 17 (WBSCR17), mRNA)
  95. cDNA FLJ78450, highly similar to Homo sapiens globoside alpha-1,3-N- acetylgalactosaminyltransferase 1 (GBGT1), mRNA (Globoside alpha-1,3- N-acetylgalactosaminyltransferase 1, isoform CRA_c)
  96. cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
  97. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  98. cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
  99. cDNA, FLJ93218, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 1 (B4GALT1), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 1, isoform CRA_a)
  100. cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-)
  101. cDNA, FLJ95212, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 4 (B4GALT4), mRNA (UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4, isoform CRA_a)
  102. Glycosyltransferase 28 domain containing 1, isoform CRA_b
  103. cDNA FLJ31605 fis, clone NT2RI2002729, highly similar to Alpha-1,6-mannosyl-glycoprotein2-beta-N- acetylglucosaminyltransferase (Mannosyl (Alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase)
  104. cDNA, FLJ93340, Homo sapiens exostoses (multiple)-like 2 (EXTL2), mRNA (Exostoses (Multiple)-like 2, isoform CRA_a)
  105. cDNA, FLJ93616, highly similar to Homo sapiens exostoses (multiple) 1 (EXT1), mRNA (Exostoses (Multiple) 1)
  106. UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 8 (GalNAc-T8)
  107. cDNA PSEC0182 fis, clone OVARC1001636, highly similar to N-acetylgalactosaminyltransferase 7 (EC 2.4.1.-)
  108. cDNA FLJ42944 fis, clone BRSTN2004863, highly similar to PolypeptideN-acetylgalactosaminyltransferase 11 (EC 2.4.1.41)
  109. cDNA FLJ46085 fis, clone TESTI2007490, highly similar to 2-hydroxyacylsphingosine1-beta-galactosyltransferase (EC 2.4.1.45)
  110. cDNA FLJ90831 fis, clone Y79AA1001795, highly similar to Beta-1,3-galactosyltransferase 4 (EC 2.4.1.62)
  111. Chondroitin synthase-3 (Chondroitin sulfate glucuronyltransferase, isoform CRA_b)
  112. cDNA, FLJ93377, Homo sapiens alpha 1,4-galactosyltransferase (A4GALT), mRNA (Alpha 1,4-galactosyltransferase) (Globotriaosylceramide synthase)
Enzyme 1 [top]
Enzyme 1 ID 5313
Enzyme 1 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 1 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase
  3. ATPDase
  4. Lymphoid cell activation antigen
  5. Ecto-apyrase
  6. CD39 antigen
Enzyme 1 Gene Name ENTPD1
Enzyme 1 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
Enzyme 1 Number of Residues 510
Enzyme 1 Molecular Weight 57965
Enzyme 1 Theoretical pI 6.29
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 17-37 479-499
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 765256 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID P49961 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name ENTP1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1533 bp
ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG
Enzyme 1 GenBank Gene ID S73813 Link Image
Enzyme 1 GeneCard ID ENTPD1 Link Image
Enzyme 1 GenAtlas ID ENTPD1 Link Image
Enzyme 1 HGNC ID HGNC:3363 Link Image
Enzyme 1 Chromosome Location 10
Enzyme 1 Locus 10q24
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed Link Image]
  2. Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed Link Image]
  3. Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed Link Image]
  4. Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed Link Image]
  5. Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed Link Image]
  6. Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed Link Image]
  7. Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed Link Image]
  8. Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5314
Enzyme 2 Name Soluble calcium-activated nucleotidase 1
Enzyme 2 Synonyms
  1. SCAN-1
  2. Apyrase homolog
  3. Putative NF-kappa-B-activating protein 107
  4. Putative MAPK-activating protein PM09
Enzyme 2 Gene Name CANT1
Enzyme 2 Protein Sequence >Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
Enzyme 2 Number of Residues 401
Enzyme 2 Molecular Weight 44840
Enzyme 2 Theoretical pI 5.98
Enzyme 2 GO Classification Not Available
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP
Enzyme 2 Pathways
Enzyme 2 Reactions
  • A nucleoside diphosphate + H2O = a nucleotide + phosphate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 45-62
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 22218108 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q8WVQ1 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name CANT1_HUMAN Link Image
Enzyme 2 PDB ID 1S1D Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1116 bp
ATGACCAAGGCCGCGGACCCCCGCTTCCGCCCCCGCTGGAAGGTGATCCTGACGTTCTTT
GTGGGTGCTGCCATCCTCTGGCTGCTCTGCTCCCACCGCCCGGCCCCCGGCAGGCCCCCC
ACCCACAATGCACACAACTGGAGGCTCGGCCAGGCGCCCGCCAACTGGTACAATGACACC
TACCCCCTGTCTCCCCCACAAAGGACACCGGCTGGGATTCGGTATCGAATCGCAGTTATC
GCAGACCTGGACACAGAGTCAAGGGCCCAAGAGGAAAACACCTGGTTCAGTTACCTGAAA
AAGGGCTACCTGACCCTGTCAGACAGTGGGGACAAGGTGGCCGTGGAATGGGACAAAGAC
CATGGGGTCCTGGAGTCCCACCTGGCGGAGAAGGGGAGAGGCATGGAGCTATCCGACCTG
ATTGTTTTCAATGGGAAACTCTACTCCGTGGATGACCGGACGGGGGTCGTCTACCAGATC
GAAGGCAGCAAAGCCGTGCCCTGGGTGATTCTGTCCGACGGCGACGGCACCGTGGAGAAA
GGCTTCAAGGCCGAATGGCTGGCAGTGAAGGACGAGCGTCTGTACGTGGGCGGCCTGGGC
AAGGAGTGGACGACCACTACGGGTGATGTGGTGAACGAGAACCCGGAGTGGGTGAAGGTG
GTGGGCTACAAGGGCAGCGTGGACCACGAGAACTGGGTGTCCAACTACAACGCCCTGCGG
GCTGCTGCCGGCATCCAGCCGCCAGGCTACCTCATCCATGAGTCTGCCTGCTGGAGTGAC
ACGCTGCAGCGCTGGTTCTTCCTGCCGCGCCGCGCCAGCCAGGAGCGCTACAGCGAGAAG
GACGACGAGCGCAAGGGCGCCAACCTGCTGCTGAGCGCCTCCCCTGACTTCGGCGACATC
GCTGTGAGCCACGTCGGGGCGGTGGTCCCCACTCACGGCTTCTCGTCCTTCAAGTTCATC
CCCAACACCGACGACCAGATCATTGTGGCCCTCAAATCCGAGGAGGACAGCGGCAGAGTC
GCCTCCTACATCATGGCCTTCACGCTGGACGGGCGCTTCCTGTTGCCGGAGACCAAGATC
GGAAGCGTGAAATACGAAGGCATCGAGTTCATTTAA
Enzyme 2 GenBank Gene ID AF328554 Link Image
Enzyme 2 GeneCard ID CANT1 Link Image
Enzyme 2 GenAtlas ID CANT1 Link Image
Enzyme 2 HGNC ID HGNC:19721 Link Image
Enzyme 2 Chromosome Location 17
Enzyme 2 Locus 17q25.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed Link Image]
  2. Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed Link Image]
  3. Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5338
Enzyme 3 Name Nucleoside diphosphate kinase, mitochondrial precursor
Enzyme 3 Synonyms
  1. NDP kinase, mitochondrial
  2. NDK
  3. nm23-H4
  4. Nucleoside diphosphate kinase D
  5. NDPKD
Enzyme 3 Gene Name NME4
Enzyme 3 Protein Sequence >Nucleoside diphosphate kinase, mitochondrial precursor
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
Enzyme 3 Number of Residues 187
Enzyme 3 Molecular Weight 20659
Enzyme 3 Theoretical pI 10.75
Enzyme 3 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 3 General Function Nucleotide transport and metabolism
Enzyme 3 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-15
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 1945762 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O00746 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name NDKM_HUMAN Link Image
Enzyme 3 PDB ID 1EHW Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCA
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
Enzyme 3 GenBank Gene ID Y07604 Link Image
Enzyme 3 GeneCard ID NME4 Link Image
Enzyme 3 GenAtlas ID NME4 Link Image
Enzyme 3 HGNC ID HGNC:7852 Link Image
Enzyme 3 Chromosome Location 16
Enzyme 3 Locus 16p13.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Milon L, Rousseau-Merck MF, Munier A, Erent M, Lascu I, Capeau J, Lacombe ML: nm23-H4, a new member of the family of human nm23/nucleoside diphosphate kinase genes localised on chromosome 16p13. Hum Genet. 1997 Apr;99(4):550-7. [PubMed Link Image]
  2. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed Link Image]
  3. Milon L, Meyer P, Chiadmi M, Munier A, Johansson M, Karlsson A, Lascu I, Capeau J, Janin J, Lacombe ML: The human nm23-H4 gene product is a mitochondrial nucleoside diphosphate kinase. J Biol Chem. 2000 May 12;275(19):14264-72. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5340
Enzyme 4 Name Ribonucleoside-diphosphate reductase large subunit
Enzyme 4 Synonyms
  1. Ribonucleoside-diphosphate reductase M1 subunit
  2. Ribonucleotide reductase large chain
Enzyme 4 Gene Name RRM1
Enzyme 4 Protein Sequence >Ribonucleoside-diphosphate reductase large subunit
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS
Enzyme 4 Number of Residues 792
Enzyme 4 Molecular Weight 90071
Enzyme 4 Theoretical pI 7.16
Enzyme 4 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH2 groups
  • oxidoreductase activity, acting on CH2 groups, disulfide as acceptor
  • ribonucleoside-diphosphate reductase activity
Process
  • DNA metabolism
  • DNA replication
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
  • protein complex
  • ribonucleoside-diphosphate reductase complex
Enzyme 4 General Function Nucleotide transport and metabolism
Enzyme 4 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Enzyme 4 Pathways
Enzyme 4 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 36065 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID P23921 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name RIR1_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >2379 bp
ATGCATGTGATCAAGCGAGATGGCCGCCAAGAACGAGTCATGTTTGACAAAATTACATCT
CGAATCCAGAAGCTTTGTTATGGACTCAATATGGATTTTGTTGATCCTGCTCAGATCACC
ATGAAAGTAATCCAAGGCTTGTACAGTGGGGTCACCACAGTGGAACTAGATACTTTGGCT
GCTGAAACAGCTGCAACCTTGACTACTAAGCACCCTGACTATGCTATCCTGGCAGCCAGG
ATCGCTGTCTCTAACTTGCACAAAGAAACAAAGAAAGTGTTCAGTGATGTGATGGAAGAC
CTCTATAACTACATAAATCCACATAATGGCAAACACTCTCCCATGGTGGCCAAGTCAACA
TTGGATATTGTTCTGGCCAATAAAGATCGCCTGAATTCTGCTATTATCTATGACCGAGAT
TTCTCTTACAATTACTTCGGCTTTAAGACGCTAGAGCGGTCTTATTTGTTGAAGATCAAT
GGAAAAGTGGCTGAAAGACCACAACATATGTTGATGAGAGTATCTGTTGGGATCCACAAA
GAAGACATTGATGCAGCAATTGAAACATATAATCTTCTTTCTGAGAGGTGGTTTACTCAT
GCTTCGCCCACTCTCTTCAATGCTGGTACCAACCGCCCACAACTTTCTAGCTGTTTTCTT
CTGAGTATGAAAGATGACAGCATTGAAGGCATTTATGACACTCTAAAGCAATGTGCATTG
ATTTCTAAGTCTGCTGGAGGAATTGGTGTTGCTGTGAGTTGTATTCGGGCTACTGGCAGC
TACATTGCTGGGACTAATGGCAATTCCAATGGCCTTGTACCGATGCTGAGAGTATATAAC
AACACAGCTCGATATGTGGATCAAGGTGGGAACAAGCGTCCTGGGGCATTTGCTATTTAC
CTGGAGCCTTGGCATTTAGACATCTTTGAATTCCTTGATTTAAAGAAGAACACAGGAAAG
GAAGAGCAGCGTGCCAGAGATCTTTTCTTTGCTCTTTGGATTCCGGATCTCTTCATGAAA
CGAGTGGAGACTAATCAGGACTGGTCTTTGATGTGTCCAAATGAGTGTCCTGGTCTGGAT
GAGGTTTGGGGAGAGGAATTTGAGAAACTATATGCAAGTTATGAGAAACAAGGTCGTGTC
CGCAAAGTTGTAAAAGCTCAGCAGCTTTGGTATGCCATCATTGAGTCTCAGACGGAAACA
GGCACCCCGTATATGCTCTACAAAGATTCCTGTAATCGAAAGAGCAACCAGCAGAACCTG
GGAACCATCAAATGCAGCAACCTGTGCACAGAAATAGTGGAGTACACCAGCAAAGATGAG
GTTGCTGTTTGTAATTTGGCTTCCCTGGCCCTGAATATGTATGTCACATCAGAACACACA
TACGACTTTAAGAAGTTGGCTGAAGTCACTAAAGTCGTTGTCCGAAACTTGAATAAAATT
ATTGATATAAACTACTATCCTGTACCAGAGGCATGCCTATCAAATAAACGCCATCGCCCC
ATTGGAATTGGGGTACAAGGTCTGGCAGATGCTTTTATCCTGATGAGATACCCTTTTGAG
AGTGCAGAAGCCCAGTTACTGAATAAGCAGATCTTTGAAACTATTTATTATGGTGCTCTG
GAAGCCAGCTGTGACCTTGCCAAGGAGCAGGGCCCATACGAAACCTATGAGGGCTCTCCA
GTTAGCAAAGGAATTCTTCAGTATGATATGTGGAATGTTACTCCTACAGACCTATGGGAC
TGGAAGGTTCTCAAGGAGAAGATTGCAAAGTATGGTATAAGAAACAGTTTACTTATTGCC
CCGATGCCTACAGCTTCCACTGCTCAGATCCTGGGGAATAATGAGTCCATTGAACCTTAC
ACCAGCAACATCTATACTCGCAGAGTCTTGTCAGGAGAATTTCAGATTGTAAATCCTCAC
TTATTGAAAGATCTTACCGAGCGGGGCCTATGGCATGAAGAGATGAAAAACCAGATTATT
GCATGCAATGGCTCTATTCAGAGCATACCAGAAATTCCTGATGACCTGAAGCAACTTTAT
AAAACTGTGTGGGAAATCTCTCAGAAAACTGTTCTCAAGATGGCAGCTGAGAGAGGTGCT
TTCATTGATCAAAGCCAATCTTTGAACATCCACATTGCTGAGCCTAACTATGGCAAACTC
ACTAGTATGCACTTCTACGGCTGGAAGCAGGGTTTGAAGACTGGGATGTATTATTTAAGG
ACGAGACCAGCAGCTAATCCAATCCAGTTCACTCTAAATAAGGAGAAGCTAAAAGATAAA
GAAAAGGTATCAAAAGAGGAAGAAGAGAAGGAGAGGAACACAGCAGCCATGGTGTGCTCT
TTGGAGAATAGAGATGAATGTCTGATGTGTGGATCCTGA
Enzyme 4 GenBank Gene ID X59543 Link Image
Enzyme 4 GeneCard ID RRM1 Link Image
Enzyme 4 GenAtlas ID RRM1 Link Image
Enzyme 4 HGNC ID HGNC:10451 Link Image
Enzyme 4 Chromosome Location 11
Enzyme 4 Locus 11p15.5
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Parker NJ, Begley CG, Fox RM: Human M1 subunit of ribonucleotide reductase: cDNA sequence and expression in stimulated lymphocytes. Nucleic Acids Res. 1991 Jul 11;19(13):3741. [PubMed Link Image]
  2. Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed Link Image]
  3. Bepler G, O'briant KC, Kim YC, Schreiber G, Pitterle DM: A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region. Genomics. 1999 Jan 15;55(2):164-75. [PubMed Link Image]
  4. Parker NJ, Begley CG, Fox RM: Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking region of the gene. Genomics. 1994 Jan 1;19(1):91-6. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5341
Enzyme 5 Name Nucleoside diphosphate kinase A
Enzyme 5 Synonyms
  1. NDK A
  2. NDP kinase A
  3. Tumor metastatic process-associated protein
  4. Metastasis inhibition factor nm23
  5. nm23-H1
  6. Granzyme A-activated DNase
  7. GAAD
Enzyme 5 Gene Name NME1
Enzyme 5 Protein Sequence >Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
Enzyme 5 Number of Residues 152
Enzyme 5 Molecular Weight 17149
Enzyme 5 Theoretical pI 6.11
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 5 General Function Nucleotide transport and metabolism
Enzyme 5 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 5 Pathways
Enzyme 5 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 35068 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P15531 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name NDKA_HUMAN Link Image
Enzyme 5 PDB ID 1JXV Link Image
Enzyme 5 PDB File Show
Enzyme 5 3D Structure
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >543 bp
TGCTGCGAACCACGTGGGTCCCGGGCGCGTTTCGGGTGCTGGCGGCTGCAGCCGGAGTTC
AAACCTAAGCAGCTGGAAGGAACCATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAA
CCAGATGGGGTCCAGCGGGGTCTTGTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGA
TTCCGCCTTGTTGGTCTGAAATTCATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTAC
GTTGACCTGAAGGACCGTCCATTCTTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCG
GTAGTTGCCATGGTCTGGGAGGGGCTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGG
GAGACCAACCCTGCAGACTCCAAGCCTGGGACCATCCGTGGAGACTTCTGCATACAAGTT
GGCAGGAACATTATACATGGCAGTGATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTG
TGGTTTCACCCTGAGGAACTGGTAGATTACACGAGCTGTGCTCAGAACTGGATCTATGAA
TGA
Enzyme 5 GenBank Gene ID X17620 Link Image
Enzyme 5 GeneCard ID NME1 Link Image
Enzyme 5 GenAtlas ID NME1 Link Image
Enzyme 5 HGNC ID HGNC:7849 Link Image
Enzyme 5 Chromosome Location 17
Enzyme 5 Locus 17q21.3
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Rosengard AM, Krutzsch HC, Shearn A, Biggs JR, Barker E, Margulies IM, King CR, Liotta LA, Steeg PS: Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. Nature. 1989 Nov 9;342(6246):177-80. [PubMed Link Image]
  2. Dooley S, Seib T, Engel M, Theisinger B, Janz H, Piontek K, Zang KD, Welter C: Isolation and characterization of the human genomic locus coding for the putative metastasis control gene nm23-H1. Hum Genet. 1994 Jan;93(1):63-6. [PubMed Link Image]
  3. Wang L, Patel U, Ghosh L, Chen HC, Banerjee S: Mutation in the nm23 gene is associated with metastasis in colorectal cancer. Cancer Res. 1993 Feb 15;53(4):717-20. [PubMed Link Image]
  4. Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed Link Image]
  5. Hailat N, Keim DR, Melhem RF, Zhu XX, Eckerskorn C, Brodeur GM, Reynolds CP, Seeger RC, Lottspeich F, Strahler JR, et al.: High levels of p19/nm23 protein in neuroblastoma are associated with advanced stage disease and with N-myc gene amplification. J Clin Invest. 1991 Jul;88(1):341-5. [PubMed Link Image]
  6. Manda R, Kohno T, Matsuno Y, Takenoshita S, Kuwano H, Yokota J: Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display. Genomics. 1999 Oct 1;61(1):5-14. [PubMed Link Image]
  7. Min K, Song HK, Chang C, Kim SY, Lee KJ, Suh SW: Crystal structure of human nucleoside diphosphate kinase A, a metastasis suppressor. Proteins. 2002 Feb 15;46(3):340-2. [PubMed Link Image]
  8. Chen Y, Gallois-Montbrun S, Schneider B, Veron M, Morera S, Deville-Bonne D, Janin J: Nucleotide binding to nucleoside diphosphate kinases: X-ray structure of human NDPK-A in complex with ADP and comparison to protein kinases. J Mol Biol. 2003 Sep 26;332(4):915-26. [PubMed Link Image]
  9. Fan Z, Beresford PJ, Oh DY, Zhang D, Lieberman J: Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Cell. 2003 Mar 7;112(5):659-72. [PubMed Link Image]
  10. Chang CL, Zhu XX, Thoraval DH, Ungar D, Rawwas J, Hora N, Strahler JR, Hanash SM, Radany E: Nm23-H1 mutation in neuroblastoma. Nature. 1994 Aug 4;370(6488):335-6. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5343
Enzyme 6 Name Ribonucleoside-diphosphate reductase M2 subunit
Enzyme 6 Synonyms
  1. Ribonucleotide reductase small subunit
  2. Ribonucleotide reductase small chain
Enzyme 6 Gene Name RRM2
Enzyme 6 Protein Sequence >Ribonucleoside-diphosphate reductase M2 subunit
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF
Enzyme 6 Number of Residues 389
Enzyme 6 Molecular Weight 44878
Enzyme 6 Theoretical pI 5.05
Enzyme 6 GO Classification
Function
  • catalytic activity
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH2 groups
  • oxidoreductase activity, acting on CH2 groups, disulfide as acceptor
  • ribonucleoside-diphosphate reductase activity
Process
  • cellular metabolism
  • deoxyribonucleoside diphosphate metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside diphosphate metabolism
  • nucleotide metabolism
  • physiological process
Component
Enzyme 6 General Function Nucleotide transport and metabolism
Enzyme 6 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Enzyme 6 Pathways
Enzyme 6 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 36155 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P31350 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name RIR2_HUMAN Link Image
Enzyme 6 PDB ID 1H0N Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1170 bp
ATGCTCTCCCTCCGTGTCCCGCTCGCGCCCATCACGGACCCGCAGCAGCTGCAGCTCTCG
CCGCTGAAGGGGCTCAGCTTGGTCGACAAGGAGAACACGCCGCCGGCCCTGAGCGGGACC
CGCGTCCTGGCCAGCAAGACCGCGAGGAGGATCTTCCAGGAGCCCACGGAGCCGAAAACT
AAAGCAGCTGCCCCCGGCGTGGAGGATGAGCCGCTGCTGAGAGAAAACCCCCGCCGCTTT
GTCATCTTCCCCATCGAGTACCATGATATCTGGCAGATGTATAAGAAGGCAGAGGCTTCC
TTTTGGACCGCCGAGGAGGTTGACCTCTCCAAGGACATTCAGCACTGGGAATCCCTGAAA
CCCGAGGAGAGATATTTTATATCCCATGTTCTGGCTTTCTTTGCAGCAAGCGATGGCATA
GTAAATGAAAACTTGGTGGAGCGATTTAGCCAAGAAGTTCAGATTACAGAAGCCCGCTGT
TTCTATGGCTTCCAAATTGCCATGGAAAACATACATTCTGAAATGTATAGTCTTCTTATT
GACACTTACATAAAAGATCCCAAAGAAAGGGAATTTCTCTTCAATGCCATTGAAACGATG
CCTTGTGTCAAGAAGAAGGCAGACTGGGCCTTGCGCTGGATTGGGGACAAAGAGGCTACC
TATGGTGAACGTGTTGTAGCCTTTGCTGCAGTGGAAGGCATTTTCTTTTCCGGTTCTTTT
GCGTCGATATTCTGGCTCAAGAAACGAGGACTGATGCCTGGCCTCACATTTTCTAATGAA
CTTATTAGCAGAGATGAGGGTTTACACTGTGATTTTGCTTGCCTGATGTTCAAACACCTG
GTACACAAACCATCGGAGGAGAGAGTAAGAGAAATAATTATCAATGCTGTTCGGATAGAA
CAGGAGTTCCTCACTGAGGCCTTGCCTGTGAAGCTCATTGGGATGAATTGCACTCTAATG
AAGCAATACATTGAGTTTGTGGCAGACAGACTTATGCTGGAACTGGGTTTTAGCAAGGTT
TTCAGAGTAGAGAACCCATTTGACTTTATGGAGAATATTTCACTGGAAGGAAAGACTAAC
TTCTTTGAGAAGAGAGTAGGCGAGTATCAGAGGATGGGAGTGATGTCAAGTCCAACAGAG
AATTCTTTTACCTTGGATGCTGACTTCTAA
Enzyme 6 GenBank Gene ID X59618 Link Image
Enzyme 6 GeneCard ID RRM2 Link Image
Enzyme 6 GenAtlas ID RRM2 Link Image
Enzyme 6 HGNC ID HGNC:10452 Link Image
Enzyme 6 Chromosome Location 2
Enzyme 6 Locus 2p25-p24
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References
  1. Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed Link Image]
  2. Zhou B, Yen Y: Characterization of the human ribonucleotide reductase M2 subunit gene; genomic structure and promoter analyses. Cytogenet Cell Genet. 2001;95(1-2):52-9. [PubMed Link Image]
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5344
Enzyme 7 Name Nucleoside diphosphate kinase B
Enzyme 7 Synonyms
  1. NDK B
  2. NDP kinase B
  3. nm23-H2
  4. C-myc purine-binding transcription factor PUF
Enzyme 7 Gene Name NME2
Enzyme 7 Protein Sequence >Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
Enzyme 7 Number of Residues 152
Enzyme 7 Molecular Weight 17298
Enzyme 7 Theoretical pI 8.69
Enzyme 7 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 7 General Function Nucleotide transport and metabolism
Enzyme 7 Specific Function Acts as a transcriptional activator of the c-Myc gene; binds DNA nonspecifically (Ref.3)
Enzyme 7 Pathways
Enzyme 7 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 4467843 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P22392 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name NDKB_HUMAN Link Image
Enzyme 7 PDB ID 1NSK Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
Enzyme 7 GenBank Gene ID X58965 Link Image
Enzyme 7 GeneCard ID NME2 Link Image
Enzyme 7 GenAtlas ID NME2 Link Image
Enzyme 7 HGNC ID HGNC:7850 Link Image
Enzyme 7 Chromosome Location 17
Enzyme 7 Locus 17q21.3
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References
  1. Gilles AM, Presecan E, Vonica A, Lascu I: Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. J Biol Chem. 1991 May 15;266(14):8784-9. [PubMed Link Image]
  2. Stahl JA, Leone A, Rosengard AM, Porter L, King CR, Steeg PS: Identification of a second human nm23 gene, nm23-H2. Cancer Res. 1991 Jan 1;51(1):445-9. [PubMed Link Image]
  3. Postel EH, Berberich SJ, Flint SJ, Ferrone CA: Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. Science. 1993 Jul 23;261(5120):478-80. [PubMed Link Image]
  4. Webb PA, Perisic O, Mendola CE, Backer JM, Williams RL: The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. J Mol Biol. 1995 Aug 25;251(4):574-87. [PubMed Link Image]
  5. Morera S, Lacombe ML, Xu Y, LeBras G, Janin J: X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. Structure. 1995 Dec 15;3(12):1307-14. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5346
Enzyme 8 Name Nucleoside diphosphate kinase 6
Enzyme 8 Synonyms
  1. NDK 6
  2. NDP kinase 6
  3. nm23-H6
  4. Inhibitor of p53-induced apoptosis-alpha
  5. IPIA-alpha
Enzyme 8 Gene Name NME6
Enzyme 8 Protein Sequence >Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
Enzyme 8 Number of Residues 186
Enzyme 8 Molecular Weight 21142
Enzyme 8 Theoretical pI 8.49
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • ion binding
  • magnesium ion binding
  • metal ion binding
  • nucleoside diphosphate kinase activity
  • nucleotide binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthesis
  • GTP biosynthesis
  • UTP biosynthesis
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • nucleoside triphosphate biosynthesis
  • nucleoside triphosphate metabolism
  • nucleotide metabolism
  • physiological process
  • purine nucleoside triphosphate biosynthesis
  • purine nucleotide biosynthesis
  • purine nucleotide metabolism
  • purine ribonucleoside triphosphate biosynthesis
  • pyrimidine ribonucleoside triphosphate biosynthesis
  • ribonucleoside triphosphate biosynthesis
Component
Enzyme 8 General Function Nucleotide transport and metabolism
Enzyme 8 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Inhibitor of p53-induced apoptosis
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-24
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 3228530 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID O75414 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NDK6_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
Enzyme 8 GenBank Gene ID AF051941 Link Image
Enzyme 8 GeneCard ID NME6 Link Image
Enzyme 8 GenAtlas ID NME6 Link Image
Enzyme 8 HGNC ID HGNC:20567 Link Image
Enzyme 8 Chromosome Location 3
Enzyme 8 Locus 3p21
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. Mehus JG, Deloukas P, Lambeth DO: NME6: a new member of the nm23/nucleoside diphosphate kinase gene family located on human chromosome 3p21.3. Hum Genet. 1999 Jun;104(6):454-9. [PubMed Link Image]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5608
Enzyme 9 Name Alpha-lactalbumin precursor
Enzyme 9 Synonyms
  1. Lactose synthase B protein
  2. Lysozyme- like protein 7
Enzyme 9 Gene Name LALBA
Enzyme 9 Protein Sequence >Alpha-lactalbumin precursor
MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAI
VENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGI
DYWLAHKALCTEKLEQWLCEKL
Enzyme 9 Number of Residues 142
Enzyme 9 Molecular Weight 16225
Enzyme 9 Theoretical pI 4.60
Enzyme 9 GO Classification
Function
  • UDP-galactosyltransferase activity
  • UDP-glycosyltransferase activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • lactose synthase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • cellular carbohydrate metabolism
  • disaccharide metabolism
  • lactose biosynthesis
  • lactose metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • extracellular region
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • 1-19
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 307104 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID P00709 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name LALBA_HUMAN Link Image
Enzyme 9 PDB ID 1HML Link Image
Enzyme 9 PDB File Show
Enzyme 9 3D Structure
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >429 bp
ATGAGGTTCTTTGTCCCTCTGTTCCTGGTGGGCATCCTGTTCCCTGCCATCCTGGCCAAG
CAATTCACAAAATGTGAGCTGTCCCAGCTGCTGAAAGACATAGATGGTTATGGAGGCATC
GCTTTGCCTGAATTGATCTGTACCATGTTTCACACCAGTGGTTATGACACACAAGCCATA
GTTGAAAACAATGAAAGCACGGAATATGGACTCTTCCAGATCAGTAATAAGCTTTGGTGC
AAGAGCAGCCAGGTCCCTCAGTCAAGGAACATCTGTGACATCTCCTGTGACAAGTTCCTG
GATGATGACATTACTGATGACATAATGTGTGCCAAGAAGATCCTGGATATTAAAGGAATT
GACTACTGGTTGGCCCATAAAGCCCTCTGCACTGAGAAGCTGGAACAGTGGCTTTGTGAG
AAGTTGTGA
Enzyme 9 GenBank Gene ID J00270 Link Image
Enzyme 9 GeneCard ID LALBA Link Image
Enzyme 9 GenAtlas ID LALBA Link Image
Enzyme 9 HGNC ID HGNC:6480 Link Image
Enzyme 9 Chromosome Location 12
Enzyme 9 Locus 12q13
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References
  1. Hall L, Craig RK, Edbrooke MR, Campbell PN: Comparison of the nucleotide sequence of cloned human and guinea-pig pre-alpha-lactalbumin cDNA with that of chick pre-lysozyme cDNA suggests evolution from a common ancestral gene. Nucleic Acids Res. 1982 Jun 11;10(11):3503-15. [PubMed Link Image]
  2. Hall L, Emery DC, Davies MS, Parker D, Craig RK: Organization and sequence of the human alpha-lactalbumin gene. Biochem J. 1987 Mar 15;242(3):735-42. [PubMed Link Image]
  3. Findlay JB, Brew K: The complete amino-acid sequence of human -lactalbumin. Eur J Biochem. 1972 May;27(1):65-86. [PubMed Link Image]
  4. Acharya KR, Ren JS, Stuart DI, Phillips DC, Fenna RE: Crystal structure of human alpha-lactalbumin at 1.7 A resolution. J Mol Biol. 1991 Sep 20;221(2):571-81. [PubMed Link Image]
  5. Ren J, Stuart DI, Acharya KR: Alpha-lactalbumin possesses a distinct zinc binding site. J Biol Chem. 1993 Sep 15;268(26):19292-8. [PubMed Link Image]
  6. Chandra N, Brew K, Acharya KR: Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin. Biochemistry. 1998 Apr 7;37(14):4767-72. [PubMed Link Image]
  7. Harata K, Abe Y, Muraki M: Crystallographic evaluation of internal motion of human alpha-lactalbumin refined by full-matrix least-squares method. J Mol Biol. 1999 Mar 26;287(2):347-58. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5687
Enzyme 10 Name UDP-glucuronosyltransferase 2B28 precursor
Enzyme 10 Synonyms
  1. UDPGT
Enzyme 10 Gene Name UGT2B28
Enzyme 10 Protein Sequence >UDP-glucuronosyltransferase 2B28 precursor
MALKWTSVLLLIHLGCYFSSGSCGKVLVWTGEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDAFTLKLEVYPTSLTKTEFENIIMQQVKRWSDIQKDSFWLYFSQEQEILWEFH
DIFRNFCKDVVSNKKVMKKLQESRFDIIFADAFFPCGELLAALLNIPFVYSLCFTPGYTI
ERHSGGLIFPPSYIPVVMSKLSDQMTFMERVKNMIYVLYFDFWFQMCDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNIDFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGLPKTRAFITHGGANGIYEAIYHGIPMVGIPLFWDQPDNIAHMKAKGAAVRLDFHTM
SSTDLLNALKTVINDPSYKENVMKLSIIQHDQPVKPLHRAVFWIEFVMCHKGAKHLRVAA
RDLTWFQYHSLDVIGFLLACVATVIFVVTKFCLFCFWKFARKGKKGKRD
Enzyme 10 Number of Residues 529
Enzyme 10 Molecular Weight 60907
Enzyme 10 Theoretical pI 8.80
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 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 10 Pathways
Enzyme 10 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • 1-24
Enzyme 10 Transmembrane Regions
  • 495-517
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 13603476 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q9BY64 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name UDB28_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 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 10 GenBank Gene ID AF177272 Link Image
Enzyme 10 GeneCard ID UGT2B28 Link Image
Enzyme 10 GenAtlas ID UGT2B28 Link Image
Enzyme 10 HGNC ID HGNC:13479 Link Image
Enzyme 10 Chromosome Location 4
Enzyme 10 Locus 4q13.2
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5696
Enzyme 11 Name UDP-glucuronosyltransferase 2B4 precursor
Enzyme 11 Synonyms
  1. UDPGT
  2. Hyodeoxycholic acid
  3. HLUG25
  4. UDPGTh-1
Enzyme 11 Gene Name UGT2B4
Enzyme 11 Protein Sequence >UDP-glucuronosyltransferase 2B4 precursor
MSMKWTSALLLIQLSCYFSSGSCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLASSA
SISFDPNSPSTLKFEVYPVSLTKTEFEDIIKQLVKRWAELPKDTFWSYFSQVQEIMWTFN
DILRKFCKDIVSNKKLMKKLQESRFDVVLADAVFPFGELLAELLKIPFVYSLRFSPGYAI
EKHSGGLLFPPSYVPVVMSELSDQMTFIERVKNMIYVLYFEFWFQIFDMKKWDQFYSEVL
GRPTTLSETMAKADIWLIRNYWDFQFPHPLLPNVEFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSMVSNTSEERANVIASALAKIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGVPLFADQPDNIAHMKAKGAAVSLDFHTM
SSTDLLNALKTVINDPLYKENAMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVTGFLLACVATVIFIITKCLFCVWKFVRTGKKGKRD
Enzyme 11 Number of Residues 528
Enzyme 11 Molecular Weight 60513
Enzyme 11 Theoretical pI 8.75
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 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 11 Pathways
Enzyme 11 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-23
Enzyme 11 Transmembrane Regions
  • 493-509
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 37589 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P06133 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name UDB4_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 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 11 GenBank Gene ID Y00317 Link Image
Enzyme 11 GeneCard ID UGT2B4 Link Image
Enzyme 11 GenAtlas ID UGT2B4 Link Image
Enzyme 11 HGNC ID HGNC:12553 Link Image
Enzyme 11 Chromosome Location 4
Enzyme 11 Locus 4q13
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5719
Enzyme 12 Name UDP-glucuronosyltransferase 1-4 precursor
Enzyme 12 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 12 Gene Name UGT1A4
Enzyme 12 Protein Sequence >UDP-glucuronosyltransferase 1-4 precursor
MARGLQVPLPRLATGLLLLLSVQPWAESGKVLVVPTDGSPWLSMREALRELHARGHQAVV
LTPEVNMHIKEEKFFTLTAYAVPWTQKEFDRVTLGYTQGFFETEHLLKRYSRSMAIMNNV
SLALHRCCVELLHNEALIRHLNATSFDVVLTDPVNLCGAVLAKYLSIPAVFFWRYIPCDL
DFKGTQCPNPSSYIPKLLTTNSDHMTFLQRVKNMLYPLALSYICHTFSAPYASLASELFQ
REVSVVDLVSYASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 12 Number of Residues 534
Enzyme 12 Molecular Weight 60026
Enzyme 12 Theoretical pI 8.68
Enzyme 12 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 12 General Function Carbohydrate transport and metabolism
Enzyme 12 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate
Enzyme 12 Pathways
Enzyme 12 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-28
Enzyme 12 Transmembrane Regions
  • 492-508
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 340137 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P22310 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name UD14_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >867 bp
ATGGCCAGAGGACTCCAGGTTCCCCTGCCGCGGCTGGCCACAGGACTGCTGCTCCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGAAAGGTGTTGGTGGTGCCCACTGATGGCAGCCCC
TGGCTCAGCATGCGGGAGGCCTTGCGGGAGCTCCATGCCAGAGGCCACCAGGCGGTGGTC
CTCACCCCAGAGGTGAATATGCACATCAAAGAAGAGAAATTTTTCACCCTGACAGCCTAT
GCTGTTCCATGGACCCAGAAGGAATTTGATCGCGTTACGCTGGGCTACACTCAAGGGTTC
TTTGAAACAGAACATCTTCTGAAGAGATATTCTAGAAGTATGGCAATTATGAACAATGTA
TCTTTGGCCCTTCATAGGTGTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGAATGCTACTTCCTTTGATGTGGTTTTAACAGACCCCGTTAACCTCTGTGGGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTTTGGAGGTACATTCCATGTGACTTA
GACTTTAAGGGCACACAGTGTCCAAATCCTTCCTCCTATATTCCTAAGTTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACATTTGCCATACTTTTTCTGCCCCTTATGCAAGTCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCTATGCATCCGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGACTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAG
Enzyme 12 GenBank Gene ID M84128 Link Image
Enzyme 12 GeneCard ID UGT1A4 Link Image
Enzyme 12 GenAtlas ID UGT1A4 Link Image
Enzyme 12 HGNC ID HGNC:12536 Link Image
Enzyme 12 Chromosome Location 2
Enzyme 12 Locus 2q37
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 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 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5722
Enzyme 13 Name UDP-glucuronosyltransferase 2B15 precursor
Enzyme 13 Synonyms
  1. UDPGT
  2. UDPGTh-3
  3. HLUG4
Enzyme 13 Gene Name UGT2B15
Enzyme 13 Protein Sequence >UDP-glucuronosyltransferase 2B15 precursor
MSLKWTSVFLLIQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVTVLTSSA
STLVNASKSSAIKLEVYPTSLTKNDLEDSLLKILDRWIYGVSKNTFWSYFSQLQELCWEY
YDYSNKLCKDAVLNKKLMMKLQESKFDVILADALNPCGELLAELFNIPFLYSLRFSVGYT
FEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIHMLYFDFWFQIYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPVYKENVMKLSRIHHDQPMKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATVIFIITKFCLFCFRKLAKKGKKKKRD
Enzyme 13 Number of Residues 530
Enzyme 13 Molecular Weight 60989
Enzyme 13 Theoretical pI 9.04
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Carbohydrate transport and metabolism
Enzyme 13 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 13 Pathways
Enzyme 13 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 13 Pfam Domain Function Not Available
Enzyme 13 Signals
  • 1-23
Enzyme 13 Transmembrane Regions
  • 495-515
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 23955933 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID P54855 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name UDB15_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 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 13 GenBank Gene ID AF548389 Link Image
Enzyme 13 GeneCard ID UGT2B15 Link Image
Enzyme 13 GenAtlas ID UGT2B15 Link Image
Enzyme 13 HGNC ID HGNC:12546 Link Image
Enzyme 13 Chromosome Location 4
Enzyme 13 Locus 4q13
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5724
Enzyme 14 Name UDP-glucuronosyltransferase 2A1 precursor
Enzyme 14 Synonyms Not Available
Enzyme 14 Gene Name UGT2A1
Enzyme 14 Protein Sequence >UDP-glucuronosyltransferase 2A1 precursor
MLNNLLLFSLQISLIGTTLGGNVLIWPMEGSHWLNVKIIIDELIKKEHNVTVLVASGALF
ITPTSNPSLTFEIYKVPFGKERIEGVIKDFVSTWLENRPSPSTIWRFYQEMAKVIKDFHM
VSQEICDGVLKNQQLMAKLKKSKFEVLVSDPVFPCGDIVALKLGIPFMYSLRFSPASTVE
KHCGKVPYPPSYVPAVLSELTDQMSFTDRIRNFISYHLQDYMFETLWKSWDSYYSKALGR
PTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKEMEEFIQSSGKN
GVVVFSLGSMVKNLTEEKANLIASALAQIPQKVLWRYKGKKPATLGNNTQLFDWIPQNDL
LGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMFADQPDNIAHMKAKGAAVEVNLNTMTS
VDLLSALRTVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHD
LTWFQYHSLDVIGFLLVCVTTAIFLVIQCCLFSCQKFGKIGKKKKRE
Enzyme 14 Number of Residues 527
Enzyme 14 Molecular Weight 59873
Enzyme 14 Theoretical pI 9.29
Enzyme 14 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 14 General Function Carbohydrate transport and metabolism
Enzyme 14 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. 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 14 Pathways
Enzyme 14 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-20
Enzyme 14 Transmembrane Regions
  • 491-507
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 4753766 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q9Y4X1 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name UDA1_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 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 14 GenBank Gene ID AJ006054 Link Image
Enzyme 14 GeneCard ID UGT2A1 Link Image
Enzyme 14 GenAtlas ID UGT2A1 Link Image
Enzyme 14 HGNC ID HGNC:12542 Link Image
Enzyme 14 Chromosome Location 4
Enzyme 14 Locus 4q13
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5725
Enzyme 15 Name UDP-glucuronosyltransferase 1-1 precursor
Enzyme 15 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 15 Gene Name UGT1A1
Enzyme 15 Protein Sequence >UDP-glucuronosyltransferase 1-1 precursor
MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVL
APDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDS
AMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLE
FEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQR
EVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEH
GIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDL
LGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTS
EDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHD
LTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 15 Number of Residues 533
Enzyme 15 Molecular Weight 59592
Enzyme 15 Theoretical pI 8.09
Enzyme 15 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 15 General Function Carbohydrate transport and metabolism
Enzyme 15 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform glucuronidates bilirubin IX- alpha to form both the IX-alpha-C8 and IX-alpha-C12 monoconjugates and diconjugate
Enzyme 15 Pathways
Enzyme 15 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-25
Enzyme 15 Transmembrane Regions
  • 491-507
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 184473 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID P22309 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name UD11_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 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 15 GenBank Gene ID M57899 Link Image
Enzyme 15 GeneCard ID UGT1A1 Link Image
Enzyme 15 GenAtlas ID UGT1A1 Link Image
Enzyme 15 HGNC ID HGNC:12530 Link Image
Enzyme 15 Chromosome Location 2
Enzyme 15 Locus 2q37
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 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 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5726
Enzyme 16 Name UDP-glucuronosyltransferase 1-9 precursor
Enzyme 16 Synonyms
  1. UDP- glucuronosyltransferase 1A9
  2. UDPGT
  3. UGT1*9
  4. UGT1-9
  5. UGT1.9
  6. UGT- 1I
  7. UGT1I
  8. lugP4
Enzyme 16 Gene Name UGT1A9
Enzyme 16 Protein Sequence >UDP-glucuronosyltransferase 1-9 precursor
MACTGWTSPLPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMRSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDLDREFKAFAHAQWKAQVRSIYSLLMGSYNDIFDLF
FSNCRSLFKDKKLVEYLKESSFDAVFLDPFDNCGLIVAKYFSLPSVVFARGILCHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLLCHRFFKNALEIASEILQTPVT
EYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 16 Number of Residues 530
Enzyme 16 Molecular Weight 59942
Enzyme 16 Theoretical pI 7.96
Enzyme 16 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 16 General Function Carbohydrate transport and metabolism
Enzyme 16 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. This isoform has specificity for phenols
Enzyme 16 Pathways
Enzyme 16 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-25
Enzyme 16 Transmembrane Regions
  • 488-504
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 7690346 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID O60656 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name UD19_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 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 16 GenBank Gene ID S55985 Link Image
Enzyme 16 GeneCard ID UGT1A9 Link Image
Enzyme 16 GenAtlas ID UGT1A9 Link Image
Enzyme 16 HGNC ID HGNC:12541 Link Image
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 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 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5728
Enzyme 17 Name UDP-glucuronosyltransferase 1-3 precursor
Enzyme 17 Synonyms
  1. UDP- glucuronosyltransferase 1A3
  2. UDPGT
  3. UGT1*3
  4. UGT1-03
  5. UGT1.3
  6. UGT- 1C
  7. UGT1C
Enzyme 17 Gene Name UGT1A3
Enzyme 17 Protein Sequence >UDP-glucuronosyltransferase 1-3 precursor
MATGLQVPLPWLATGLLLLLSVQPWAESGKVLVVPIDGSHWLSMREVLRELHARGHQAVV
LTPEVNMHIKEENFFTLTTYAISWTQDEFDRHVLGHTQLYFETEHFLKKFFRSMAMLNNM
SLVYHRSCVELLHNEALIRHLNATSFDVVLTDPVNLCAAVLAKYLSIPTVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFMQRVKNMLYPLALSYICHAFSAPYASLASELFQ
REVSVVDILSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANRKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 17 Number of Residues 534
Enzyme 17 Molecular Weight 60339
Enzyme 17 Theoretical pI 8.28
Enzyme 17 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 17 General Function Carbohydrate transport and metabolism
Enzyme 17 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 17 Pathways
Enzyme 17 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-28
Enzyme 17 Transmembrane Regions
  • 492-508
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 340135 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P35503 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name UD13_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >867 bp
ATGGCCACAGGACTCCAGGTTCCCCTGCCGTGGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGAAAGGTGTTGGTGGTGCCCATTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGTCTTGCGGGAGCTCCATGCCAGAGGCCACCAGGCAGTGGTC
CTCACCCCAGAGGTGAATATGCACATCAAAGAAGAGAACTTTTTCACCCTGACAACCTAT
GCCATTTCGTGGACCCAGGATGAATTTGATCGCCATGTGCTGGGCCACACTCAACTGTAC
TTTGAAACAGAACATTTTCTGAAGAAATTTTTCAGAAGTATGGCAATGTTGAACAATATG
TCTTTGGTCTATCATAGGTCTTGTGTGGAGCTACTACATAATGAGGCCCTGATCAGGCAC
CTGAATGCTACTTCCTTTGATGTGGTTTTAACAGACCCCGTTAACCTCTGCGCGGCAGTG
CTGGCTAAGTACCTGTCGATTCCTACTGTGTTTTTTTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACAACC
AATTCAGACCACATGACATTCATGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACATTTGCCATGCTTTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATATTCTCAGTCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGACTACCCCAGGCCAATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACAGGAAGCCACTATCTCAG
Enzyme 17 GenBank Gene ID M84127 Link Image
Enzyme 17 GeneCard ID UGT1A3 Link Image
Enzyme 17 GenAtlas ID UGT1A3 Link Image
Enzyme 17 HGNC ID HGNC:12535 Link Image
Enzyme 17 Chromosome Location 2
Enzyme 17 Locus 2q37
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5731
Enzyme 18 Name UDP-glucuronosyltransferase 2B17 precursor
Enzyme 18 Synonyms
  1. UDPGT
  2. C19- steroid-specific UDP-glucuronosyltransferase
Enzyme 18 Gene Name UGT2B17
Enzyme 18 Protein Sequence >UDP-glucuronosyltransferase 2B17 precursor
MSLKWMSVFLLMQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSA
SILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEY
SDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYT
VEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPIYKENIMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATMIFMITKCCLFCFRKLAKTGKKKKRD
Enzyme 18 Number of Residues 530
Enzyme 18 Molecular Weight 61096
Enzyme 18 Theoretical pI 8.73
Enzyme 18 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 18 General Function Carbohydrate transport and metabolism
Enzyme 18 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. The major substrates of this isozyme are eugenol > 4-methylumbelliferone > dihydrotestosterone (DHT) > androstane-3alpha,17beta-diol (3alpha-diol) > testosterone > androsterone (ADT)
Enzyme 18 Pathways
Enzyme 18 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-23
Enzyme 18 Transmembrane Regions
  • 495-515
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 3287473 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID O75795 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name UDB17_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 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 18 GenBank Gene ID U59209 Link Image
Enzyme 18 GeneCard ID UGT2B17 Link Image
Enzyme 18 GenAtlas ID UGT2B17 Link Image
Enzyme 18 HGNC ID HGNC:12547 Link Image
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5732
Enzyme 19 Name UDP-glucuronosyltransferase 1-6 precursor
Enzyme 19 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 19 Gene Name UGT1A6
Enzyme 19 Protein Sequence >UDP-glucuronosyltransferase 1-6 precursor
MACLLRSFQRISAGVFFLALWGMVVGDKLLVVPQDGSHWLSMKDIVEVLSDRGHEIVVVV
PEVNLLLKESKYYTRKIYPVPYDQEELKNRYQSFGNNHFAERSFLTAPQTEYRNNMIVIG
LYFINCQSLLQDRDTLNFFKESKFDALFTDPALPCGVILAEYLGLPSVYLFRGFPCSLEH
TFSRSPDPVSYIPRCYTKFSDHMTFSQRVANFLVNLLEPYLFYCLFSKYEELASAVLKRD
VDIITLYQKVSVWLLRYDFVLEYPRPVMPNMVFIGGINCKKRKDLSQEFEAYINASGEHG
IVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLL
GHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSE
DLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDL
TWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 19 Number of Residues 532
Enzyme 19 Molecular Weight 60751
Enzyme 19 Theoretical pI 8.55
Enzyme 19 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 19 General Function Carbohydrate transport and metabolism
Enzyme 19 Specific Function 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 19 Pathways
Enzyme 19 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-26
Enzyme 19 Transmembrane Regions
  • 490-506
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 340141 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID P19224 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name UD16_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence >861 bp
ATGGCCTGCCTCCTTCGCTCATTTCAGAGAATTTCTGCAGGGGTTTTCTTCTTAGCACTT
TGGGGCATGGTTGTAGGTGACAAGCTGCTGGTGGTCCCTCAGGACGGAAGCCACTGGCTT
AGTATGAAGGATATAGTTGAGGTTCTCAGTGACCGGGGTCATGAGATTGTAGTGGTGGTG
CCTGAAGTTAATTTGCTTTTGAAAGAATCCAAATACTACACAAGAAAAATCTATCCAGTG
CCGTATGACCAAGAAGAGCTGAAGAACCGTTACCAATCATTTGGAAACAATCACTTTGCT
GAGCGATCATTCCTAACTGCTCCTCAGACAGAGTACAGGAATAACATGATTGTTATTGGC
CTGTACTTCATCAACTGCCAGAGCCTCCTGCAGGACAGGGACACCCTGAACTTCTTTAAG
GAGAGCAAGTTTGATGCTCTTTTCACAGACCCAGCCTTACCCTGTGGGGTGATCCTGGCT
GAGTATTTGGGCCTACCATCTGTGTACCTCTTCAGGGGTTTTCCGTGTTCCCTGGAGCAT
ACATTCAGCAGAAGCCCAGACCCTGTGTCCTACATTCCCAGGTGCTACACAAAGTTTTCA
GACCACATGACTTTTTCCCAACGAGTGGCCAACTTCCTTGTTAATTTGTTGGAGCCCTAT
CTATTTTATTGTCTGTTTTCAAAGTATGAAGAACTCGCATCAGCTGTCCTCAAGAGAGAT
GTGGATATAATCACCTTATATCAGAAGGTCTCTGTTTGGCTGTTAAGATATGACTTTGTG
CTTGAATATCCTAGGCCGGTCATGCCCAACATGGTCTTCATTGGAGGTATCAACTGTAAG
AAGAGGAAAGACTTGTCTCAG
Enzyme 19 GenBank Gene ID M84130 Link Image
Enzyme 19 GeneCard ID UGT1A6 Link Image
Enzyme 19 GenAtlas ID UGT1A6 Link Image
Enzyme 19 HGNC ID HGNC:12538 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 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 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5733
Enzyme 20 Name UDP-glucuronosyltransferase 1-5 precursor
Enzyme 20 Synonyms
  1. UDP- glucuronosyltransferase 1A5
  2. UDPGT
  3. UGT1*5
  4. UGT1-05
  5. UGT1.5
  6. UGT- 1E
  7. UGT1E
Enzyme 20 Gene Name UGT1A5
Enzyme 20 Protein Sequence >UDP-glucuronosyltransferase 1-5 precursor
MATGLQVPLPQLATGLLLLLSVQPWAESGKVLVVPTDGSHWLSMREALRDLHARGHQVVV
LTLEVNMYIKEENFFTLTTYAISWTQDEFDRLLLGHTQSFFETEHLLMKFSRRMAIMNNM
SLIIHRSCVELLHNEALIRHLHATSFDVVLTDPFHLCAAVLAKYLSIPAVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFLQRVKNMLYPLALSYLCHAVSAPYASLASELFQ
REVSVVDLVSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 20 Number of Residues 534
Enzyme 20 Molecular Weight 60072
Enzyme 20 Theoretical pI 8.14
Enzyme 20 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 20 General Function Carbohydrate transport and metabolism
Enzyme 20 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 20 Pathways
Enzyme 20 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • 1-28
Enzyme 20 Transmembrane Regions
  • 492-508
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 340139 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID P35504 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name UD15_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >867 bp
ATGGCCACAGGACTCCAGGTTCCCCTGCCGCAGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGGAAGGTGCTGGTGGTGCCCACTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGCCTTGCGGGACCTCCATGCGAGAGGCCACCAGGTGGTGGTC
CTCACCCTGGAGGTGAATATGTACATCAAAGAAGAGAACTTTTTCACCCTGACAACGTAT
GCCATTTCATGGACCCAGGACGAATTTGATCGCCTTTTGCTGGGTCACACTCAATCGTTC
TTTGAAACAGAACATCTTCTGATGAAATTTTCTAGAAGAATGGCAATTATGAACAATATG
TCTTTGATCATACATAGGTCTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGCATGCTACTTCCTTTGATGTGGTTCTAACAGACCCCTTTCACCTCTGCGCGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTCTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACCTTTGCCATGCTGTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGATTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAG
Enzyme 20 GenBank Gene ID M84129 Link Image
Enzyme 20 GeneCard ID UGT1A5 Link Image
Enzyme 20 GenAtlas ID UGT1A5 Link Image
Enzyme 20 HGNC ID HGNC:12537 Link Image
Enzyme 20 Chromosome Location 2
Enzyme 20 Locus 2q37
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5734
Enzyme 21 Name UDP-glucuronosyltransferase 2B11 precursor
Enzyme 21 Synonyms
  1. UDPGT
Enzyme 21 Gene Name UGT2B11
Enzyme 21 Protein Sequence >UDP-glucuronosyltransferase 2B11 precursor
MTLKWTSVLLLIHLSCYFSSGSCGKVLVWAAEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDASTLKFEVYPTSLTKTEFENIIMQQVKRWSDIRKDSFWLYFSQEQEILWELY
DIFRNFCKDVVSNKKVMKKLQESRFDIVFADAVFPCGELLAALLNIRFVYSLRFTPGYTI
ERHSGGLIFPPSYIPIVMSKLSDQMTFMERVKNMIYVLYFDFWFQMSDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNVDFVGGFHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRLDFNTM
SSTDLLNALKTVINDPLYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMPHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLACVATVIFIITKFCLFCFWKFARKGKKGKRD
Enzyme 21 Number of Residues 529
Enzyme 21 Molecular Weight 61039
Enzyme 21 Theoretical pI 9.29
Enzyme 21 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 21 General Function Carbohydrate transport and metabolism
Enzyme 21 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 21 Pathways
Enzyme 21 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • 1-21
Enzyme 21 Transmembrane Regions
  • 493-513
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 3360273 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID O75310 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name UDB11_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 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 21 GenBank Gene ID AF016492 Link Image
Enzyme 21 GeneCard ID UGT2B11 Link Image
Enzyme 21 GenAtlas ID UGT2B11 Link Image
Enzyme 21 HGNC ID HGNC:12545 Link Image
Enzyme 21 Chromosome Location 4
Enzyme 21 Locus 4q13.2
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5845
Enzyme 22 Name GTP:AMP phosphotransferase mitochondrial
Enzyme 22 Synonyms
  1. Adenylate kinase 3
  2. AK3
  3. Adenylate kinase 3 alpha-like 1
Enzyme 22 Gene Name AK3
Enzyme 22 Protein Sequence >GTP:AMP phosphotransferase mitochondrial
MGASARLLRAVIMGAPGSGKGTVSSRITTHFELKHLSSGDLLRDNMLRGTEIGVLAKAFI
DQGKLIPDDVMTRLALHELKNLTQYSWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEV
IKQRLTARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDDKPETVIKRLKAYEDQT
KPVLEYYQKKGVLETFSGTETNKIWPYVYAFLQTKVPQRSQKASVTP
Enzyme 22 Number of Residues 227
Enzyme 22 Molecular Weight 25566
Enzyme 22 Theoretical pI 9.64
Enzyme 22 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenylate kinase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleotide binding
  • nucleotide kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular metabolism
  • metabolism
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolism
  • physiological process
Component
Enzyme 22 General Function Nucleotide transport and metabolism
Enzyme 22 Specific Function NTP + AMP = NDP + ADP
Enzyme 22 Pathways
Enzyme 22 Reactions
  • nucleoside triphosphate + AMP = nucleoside diphosphate + ADP
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 6518533 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID Q9UIJ7 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name KAD3_HUMAN Link Image
Enzyme 22 PDB ID 2AK3 Link Image
Enzyme 22 PDB File Show
Enzyme 22 3D Structure
Enzyme 22 Cellular Location Not Available
Enzyme 22 Gene Sequence >684 bp
ATGGGGGCGTCGGGGCGGCTGCTGCGAGCGGTGATCATGGGGGCCCCGGGCTCGGGCAAG
GGCACCGTGTCGTCCCGCATCACTACACACTTCGAGCTGAAGCACCTCTCCCGCGGGGAC
CTGCTCCGGGACAACATGCTGCGGGGCACAGAAATTGGCGTGTTAGCCCAGGCTTTCATT
GACCAAGGGAAACTCATCCCAGATTATGTCACGACTCGGCTGGCCCTTCATGAGCTGAAA
AACCTCACCCAGTATAGCTGGCTGTTGGATGGTTTTCCAAGGACACTTCCACAGGCAGAA
GCCCTAGATAGAGCTTATCAGATCGACACAGTGATTAACCTGAATGTGCCCTTTGAGGTC
ATTAAACAACGCCTTACTGCTCGCTGGATTCATCCCGCCAGTGGCCGAGTCTATAACATT
GAATTCAACCCTCCCAAAACTGTGGGCATTGATGACCTGACTGGGGAGCCTCTCATTCAG
CGTGAGGATGATAAACCAGAGACGGTTATCAAGAGACTAAAGGCTTATGAAGACCAAACA
AAGCCAGTCCTGGAATATTACCAGAAAAAAGGGGTGTTGGAAACATTCTCCGGAACAGAA
ACCAACAAGATTTGGCCCTATGTATATGCTTTCCTACAAACTAAAGTTCCACAAAGAAGC
CAGAAAGCTTCAGTTACTCCATGA
Enzyme 22 GenBank Gene ID AB021870 Link Image
Enzyme 22 GeneCard ID AK3 Link Image
Enzyme 22 GenAtlas ID AK3 Link Image
Enzyme 22 HGNC ID HGNC:17376 Link Image
Enzyme 22 Chromosome Location 9
Enzyme 22 Locus 9p24.1-p24.3
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 General References Not Available
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 6009
Enzyme 23 Name 6-phosphofructokinase type C
Enzyme 23 Synonyms
  1. Phosphofructokinase 1
  2. Phosphohexokinase
  3. Phosphofructo-1-kinase isozyme C
  4. PFK-C
  5. 6- phosphofructokinase, platelet type
Enzyme 23 Gene Name PFKP
Enzyme 23 Protein Sequence >6-phosphofructokinase type C
MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFI
YEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGIT
NLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCG
TDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLP
ESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDT
RVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMEC
VQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGA
PAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTK
RVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVS
NNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGA
DAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKG
VFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVL
GISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQ
PWSV
Enzyme 23 Number of Residues 784
Enzyme 23 Molecular Weight 85597
Enzyme 23 Theoretical pI 7.60
Enzyme 23 GO Classification
Function
  • 6-phosphofructokinase activity
  • catalytic activity
  • phosphofructokinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • 6-phosphofructokinase complex
  • cell
  • cytoplasm
  • intracellular
  • protein complex
Enzyme 23 General Function Carbohydrate transport and metabolism
Enzyme 23 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 23 Pathways
Enzyme 23 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 560105 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID Q01813 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name K6PP_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >2355 bp
ATGGACGCGGACGACTCCCGGGCCCCCAAGGGCTCCTTGCGGAAGTTCCTGGAGCACCTC
TCCGGGGCCGGCAAGGCCATCGGCGTGCTGACCAGCGGCGGGGATGCTCAAGGTATGAAC
GCTGCCGTCCGTGCCGTGGTGCGCATGGGTATCTACGTGGGGGCCAAGGTGTACTTCATC
TACGAGGGCTACCAGGGCATGGTGGACGGAGGCTCAAACATCGCAGAGGCCGACTGGGAG
AGTGTCTCCAGCATCCTGCAAGTGGGCGGGACGATCATTGGCAGTGCGCGGTGCCAGGCC
TTCCGCACGCGGGAAGGCCGCCTGAAGGCTGCTTGCAACCTGCTGCAGCGCGGCATCACC
AACCTGTGTGTGATCGGCGGGGACGGGAGCCTCACCGGGGCCAACCTCTTCCGGAAGGAG
TGGAGTGGGCTGCTGGAGGAGCTGGCCAGGAACGGCCAGATCGATAAGGAGGCCGTGCAG
AAGTACGCCTACCTCAACGTGGTGGGCATGGTGGGCTCCATCGACAATGATTTCTGCGGC
ACCGACATGACCATCGGCACGGACTCCGCCCTGCACAGGATCATCGAGGTCGTCGACGCC
ATCATGACCACGGCCCAGAGCCACCAGAGGACCTTCGTTCTGGAGGTGATGGGACGACAC
TGTGGGTACCTGGCCCTGGTGAGTGCCTTGGCCTGCGGTGCGGACTGGGTGTTCCTTCCA
GAATCTCCACCAGAGGAAGGCTGGGAGGAGCAGATGTGTGTCAAACTCTCGGAGAACCGT
GCCCGGAAAAAAAGGCTGAATATTATTATTGTGGCTGAAGGAGCAATTGATACCCAAAAT
AAACCCATCACCTCTGAGAAAATCAAAGAGCTTGTCGTCACGCAGCTGGGCTATGACACA
CGTGTGACCATCCTCGGGCACGTGCAGAGAGGAGGGACCCCTTCGGCATTCGACAGGATC
TTGGCCAGCCGCATGGGAGTGGAGGCAGTCATCGCCTTGCTAGAGGCCACCCCGGACACC
CCAGCTTGCGTCGTGTCACTGAACGGGAACCACGCCGTGCGCCTGCCGCTGATGGAGTGC
GTGCAGATGACTCAGGATGTGCAGAAGGCGATGGACGAGAGGAGATTTCAAGATGCGGTT
CGACTCCGAGGGAGGAGCTTTGCGGGCAACCTGAACACCTACAAGCGACTTGCCATCAAG
CTGCCGGATGATCAGATCCCAAAGACCAATTGCAACGTAGCTGTCATCAACGTGGGGGCA
CCCGCGGCTGGGATGAACGCGGCCGTACGCTCAGCTGTGCGCGTGGGCATTGCCGACGGC
CACAGGATGCTCGCCATCTATGATGGCTTTGACGGCTTCGCCAAGGGCCAGATCAAAGAA
ATCGGCTGGACAGATGTCGGGGGCTGGACCGGCCAAGGAGGCTCCATTCTTGGGACAAAA
CGCGTTCTCCCGGGGAAGTACTTGGAAGAGATCGCCACACAGATGCGCACGCACAGCATC
AACGCGCTGCTGATCATCGGTGGATTCGAGGCCTACCTGGGACTCCTGGAGCTGTCAGCC
GCCCGGGAGAAGCACGAGGAGTTCTGTGTCCCCATGGTCATGGTTCCCGCTACTGTGTCC
AACAATGTGCCGGGTTCCGATTTCAGCATCGGGGCAGACACCGCCCTGAACACTATCACC
GACACCTGCGACCGCATCAAGCAGTCCGCCAGCGGAACCAAGCGGCGCGTGTTCATCATC
GAGACCATGGGCGGCTACTGTGGCTACCTGGCCAACATGGGGGGGCTCGCGGCCGGAGCT
GATGCCGCATACATTTTCGAAGAGCCCTTCGACATCAGGGATCTGCAGTCCAACGTGGAG
CACCTGACGGAGAAAATGAAGACCACCATCCAGAGAGGCCTTGTGCTCAGAAATGAGAGC
TGCAGTGAAAACTACACCACCGACTTCATTTACCAGCTGTATTCAGAAGAGGGCAAAGGC
GTGTTTGACTGCAGGAAGAACGTGCTGGGTCACATGCAGCAGGGTGGGGCACCCTCTCCA
TTTGATAGAAACTTTGGAACCAAAATCTCTGCCAGAGCTATGGAGTGGATCACTGCAAAA
CTCAAGGAGGCCCGGGGCAGAGGAAAAAAATTTACCACCGATGATTCCATTTGTGTGCTG
GGAATAAGCAAAAGAAACGTTATTTTTCAACCTGTGGCAGAGCTGAAGAAGCAAACGGAT
TTTGAGCACAGGATTCCCAAAGAACAGTGGTGGCTCAAGCTACGGCCCCTCATGAAAATC
CTGGCCAAGTACAAGGCCAGCTATGACGTGTCGGACTCAGGCCAGCTGGAACATGTGCAG
CCCTGGAGTGTCTGA
Enzyme 23 GenBank Gene ID D25328 Link Image
Enzyme 23 GeneCard ID PFKP Link Image
Enzyme 23 GenAtlas ID PFKP Link Image
Enzyme 23 HGNC ID HGNC:8878 Link Image
Enzyme 23 Chromosome Location 10
Enzyme 23 Locus 10p15.3-p15.2
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References
  1. Eto K, Sakura H, Yasuda K, Hayakawa T, Kawasaki E, Moriuchi R, Nagataki S, Yazaki Y, Kadowaki T: Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet. Biochem Biophys Res Commun. 1994 Feb 15;198(3):990-8. [PubMed Link Image]
  2. Simpson CJ, Fothergill-Gilmore LA: Isolation and sequence of a cDNA encoding human platelet phosphofructokinase. Biochem Biophys Res Commun. 1991 Oct 15;180(1):197-203. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 6033
Enzyme 24 Name 6-phosphofructokinase, liver type
Enzyme 24 Synonyms
  1. Phosphofructokinase 1
  2. Phosphohexokinase
  3. Phosphofructo-1-kinase isozyme B
  4. PFK-B
Enzyme 24 Gene Name PFKL
Enzyme 24 Protein Sequence >6-phosphofructokinase, liver type
MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVE
GGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDG
SLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDS
ALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWE
NFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQ
RGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQK
AMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRS
AVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESI
VENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLG
SDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFN
IHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGH
LQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFS
PVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF
Enzyme 24 Number of Residues 780
Enzyme 24 Molecular Weight 85020
Enzyme 24 Theoretical pI 7.54
Enzyme 24 GO Classification
Function
  • 6-phosphofructokinase activity
  • catalytic activity
  • phosphofructokinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • 6-phosphofructokinase complex
  • cell
  • cytoplasm
  • intracellular
  • protein complex
Enzyme 24 General Function Carbohydrate transport and metabolism
Enzyme 24 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 24 Pathways
Enzyme 24 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 35431 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P17858 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name K6PL_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >2343 bp
ATGGCCGCGGTGGACCTGGAGAAGCTGCGGGCGTCGGGCGCGGGCAAGGCCATCGGCGTC
CTGACCAGCGGCGGCGACCGGCAAGGCATGAACGCTGCTGTCCGGGCTGTGACGCGCATG
GGCATTTATGTGGGTGCCAAAGTCTTCCTCATCTACGAGGGCTATGAGGGCCTCGTGGAG
GGAGGTGAGAACATCAAGCAGGCCAACTGGCTGAGCGTCTCCAACATCATCCAGCTGGGC
GGCACTATCATTGGCAGCGCTCGCTCGAAGGCCTTTACCACCAGGGAGGGGCGCCGGGCA
GCGGCCTACAACCTGGTCCAGCACGGCATCACCAACCTGTGCGTCATCGGCGGGGATGGC
AGCCTCACAGGTGCCAACATCTTCCGCAGCGAGTGGGGCAGCCTGCTGGAGGAGCTGGTG
GCGGAAGGTAAGATCTCAGAGACTACAGCCTGGACCTACTCGCACCTGAACATCGCGGGC
CTAGTGGGCTCCATCGATAACGACTTCTGCGGCACCGACATGACCATCGGCACGGACTCG
GCCCTCCACCGCATCATGGAGGTCATCGATGCCATCACCACCACTGCCCAGAGCCACCAG
AGGACCTTCGTGCTGGAAGTGATGGGCCGGCACTGCGGGTACCTGGCGCTGGTATCTGCA
CTGGCCTCAGGGGCCGACTGGCTGTTCATCCCCGAGGCTCCACCCGAGGACGGCTGGGAG
AACTTCATGTGTGAGAGGCTGGGTGAGACTCGGAGCCGTGGGTCCCGACTGAACATCATC
ATCATCGCTGAGGGTGCCATTGACCGCAACGGGAAGCCCATCTCGTCCAGCTACGTGAAG
GACCTGGTGGTTCAGAGGCTGGGCTTCGACACCCGTGTAACTGTGCTGGGCCACGTGCAG
CGGGGAGGGACGCCCTCTGCCTTCGACCGGATCCTGAGCAGCAAGATGGGCATGGAGGCG
GTGATGGCGCTGCTGGAAGCCACGCCTGACACGCCGGCCTGCGTGGTCACCCTCTCGGGG
AACCAGTCAGTGCGGCTGCCCCTCATGGAGTGCGTGCAGATGACCAAGGAAGTGCAGAAA
GCCATGGATGACAAGAGGTTTGACGAGGCCACCCAGCTCCGTGGTGGGAGCTTCGAGAAC
AACTGGAACATTTACAAGCTCCTCACCCACCAGAAGCCCCCCAAGGAGAAGTCTAACTTC
TCCCTGGCCATCCTGAATGTGGGGGCCCCGGCGGCTGGCATGAATGCGGCCGTGCGCTCG
GCGGTGCGGACCGGCATCTCCCATGGACACACAGTATACGTGGTGCACGATGGCTTCGAA
GGCCTAGCCAAGGGTCAGGTGCAAGAAGTAGGCTGGCACGACGTGGCCGGCTGGTTGGGG
CGTGGTGGCTCCATGCTGGGGACCAAGAGGACCCTGCCCAAGGGCCAGCTGGAGTCCATT
GTGGAGAACATCCGCATCTATGGTATTCACGCCCTGCTGGTGGTCGGTGGGTTTGAGGCC
TATGAAGGGGTGCTGCAGCTGGTGGAGGCTCGCGGGCGCTACGAGGAGCTCTGCATCGTC
ATGTGTGTCATCCCAGCCACCATCAGCAACAACGTCCCTGGCACCGACTTCAGCCTGGGC
TCCGACACTGCTGTAAATGCCGCCATGGAGAGCTGTGACCGCATCAAACAGTCTGCCTCG
GGGACCAAGCGCCGTGTGTTCATCGTGGAGACCATGGGGGGTTACTGTGGCTACCTGGCC
ACCGTGACTGGCATTGCTGTGGGGGCCGACGCCGCCTACGTCTTCGAGGACCCTTTCAAC
ATCCACGACTTAAAGGTCAACGTGGAGCACATGACGGAGAAGATGAAGACAGACATTCAG
AGGGGCCTGGTGCTGCGGAACGAGAAGTGCCATGACTACTACACCACGGAGTTCCTGTAC
AACCTGTACTCATCAGAGGGCAAGGGCGTCTTCGACTGCAGGACCAATGTCCTGGGCCAC
CTGCAGCAGGGTGGCGCTCCAACCCCCTTTGACCGGAACTATGGGACCAAGCTGGGGGTG
AAGGCCATGCTGTGGTTGTCGGAGAAGCTGCGCGAGGTTTACCGCAAGGGACGGGTGTTC
GCCAATGCCCCAGACTCGGCCTGCGTGATCGGCCTGAAGAAGAAGGCGGTGGCCTTCAGC
CCCGTCACTGAGCTCAAGAAAGACACTGATTTCGAGCACCGCATGCCACGGGAGCAGTGG
TGGCTGAGCCTGCGGCTCATGCTGAAGATGCTGGCACAATACCGCATCAGTATGGCCGCC
TACGTGTCAGGGGAGCTGGAGCACGTGACCCGCCGCACCCTGAGCATGGACAAGGGCTTC
TGA
Enzyme 24 GenBank Gene ID X15573 Link Image
Enzyme 24 GeneCard ID PFKL Link Image
Enzyme 24 GenAtlas ID PFKL Link Image
Enzyme 24 HGNC ID HGNC:8876 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. Levanon D, Danciger E, Dafni N, Bernstein Y, Elson A, Moens W, Brandeis M, Groner Y: The primary structure of human liver type phosphofructokinase and its comparison with other types of PFK. DNA. 1989 Dec;8(10):733-43. [PubMed Link Image]
  2. Elson A, Levanon D, Brandeis M, Dafni N, Bernstein Y, Danciger E, Groner Y: The structure of the human liver-type phosphofructokinase gene. Genomics. 1990 May;7(1):47-56. [PubMed Link Image]
  3. Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [PubMed Link Image]
  4. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 6037
Enzyme 25 Name 6-phosphofructokinase, muscle type
Enzyme 25 Synonyms
  1. Phosphofructokinase 1
  2. Phosphohexokinase
  3. Phosphofructo-1-kinase isozyme A
  4. PFK-A
  5. Phosphofructokinase-M
Enzyme 25 Gene Name PFKM
Enzyme 25 Protein Sequence >6-phosphofructokinase, muscle type
MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVD
GGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDG
SLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDS
ALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWE
EHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQ
RGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTK
AMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVR
STVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQ
ISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSV
GADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPF
TIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLG
HMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVF
QPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV
Enzyme 25 Number of Residues 780
Enzyme 25 Molecular Weight 85184
Enzyme 25 Theoretical pI 8.07
Enzyme 25 GO Classification
Function
  • 6-phosphofructokinase activity
  • catalytic activity
  • phosphofructokinase activity
  • phosphotransferase activity, alcohol group as acceptor
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
  • 6-phosphofructokinase complex
  • cell
  • cytoplasm
  • intracellular
  • protein complex
Enzyme 25 General Function Carbohydrate transport and metabolism
Enzyme 25 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 25 Pathways
Enzyme 25 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 1101758 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID P08237 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name K6PF_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence >2343 bp
ATGACCCATGAAGAGCACCATGCAGCCAAAACCCTGGGGATTGGCAAAGCCATTGCTGTC
TTAACCTCTGGTGGAGATGCCCAAGGTATGAATGCTGCTGTCAGGGCTGTGGTTCGAGTT
GGTATCTTCACCGGTGCCCGTGTCTTCTTTGTCCATGAGGGTTATCAAGGCCTGGTGGAT
GGTGGAGATCACATCAAGGAAGCCACCTGGGAGAGCGTTTCGATGATGCTTCAGCTGGGA
GGCACGGTGATTGGAAGTGCCCGGTGCAAGGACTTTCGGGAACGAGAAGGACGACTCCGA
GCTGCCTACAACCTGGTGAAGCGTGGGATCACCAATCTCTGTGTCATTGGGGGTGATGGC
AGCCTCACTGGGGCTGACACCTTCCGTTCTGAGTGGAGTGACTTGTTGAGTGACCTCCAG
AAAGCAGGTAAGATCACAGATGAGGAGGCTACGAAGTCCAGCTACCTGAACATTGTGGGC
CTGGTTGGGTCAATTGACAATGACTTCTGTGGCACTGATATGACCATTGGCACTGACTCT
GCCCTGCATCGGATCATGGAAATTGTAGATGCCATCACTACCACTGCCCAGAGCCACCAG
AGGACATTTGTGTTAGAAGTAATGGGCCGCCACTGTGGATACCTGGCCCTTGTCACCTCT
CTGTCCTGTGGGGCCGACTGGGTTTTTATTCCTGAATGTCCACCAGATGACGACTGGGAG
GAACACCTTTGTCGCCGACTCAGCGAGACAAGGACCCGTGGTTCTCGTCTCAACATCATC
ATTGTGGCTGAGGGTGCAATTGACAAGAATGGAAAACCAATCACCTCAGAAGACATCAAG
AATCTGGTGGTTAAGCGTCTGGGATATGACACCCGGGTTACTGTCTTGGGGCATGTGCAG
AGGGGTGGGACGCCATCAGCCTTTGACAGAATTCTGGGCAGCAGGATGGGTGTGGAAGCA
GTGATGGCACTTTTGGAGGGGACCCCAGATACCCCAGCCTGTGTAGTGAGCCTCTCTGGT
AACCAGGCTGTGCGCCTGCCCCTCATGGAATGTGTCCAGGTGACCAAAGATGTGACCAAG
GCCATGGATGAGAAGAAATTTGACGAAGCCCTGAAGCTGAGAGGCCGGAGCTTCATGAAC
AACTGGGAGGTGTACAAGCTTCTAGCTCATGTCAGACCCCCGGTATCTAAGAGTGGTTCG
CACACAGTGGCTGTGATGAACGTGGGGGCTCCGGCTGCAGGCATGAATGCTGCTGTTCGC
TCCACTGTGAGGATTGGCCTTATCCAGGGCAACCGAGTGCTCGTTGTCCATGATGGTTTC
GAGGGCCTGGCCAAGGGGCAGATAGAGGAAGCTGGCTGGAGCTATGTTGGGGGCTGGACT
GGCCAAGGTGGCTCTAAACTTGGGACTAAAAGGACTCTACCCAAGAAGAGCTTTGAACAG
ATCAGTGCCAATATAACTAAGTTTAACATTCAGGGCCTTGTCATCATTGGGGGCTTTGAG
GCTTACACAGGGGGCCTGGAACTGATGGAGGGCAGGAAGCAGTTTGATGAGCTCTGCATC
CCATTTGTGGTCATTCCTGCTACAGTCTCCAACAATGTCCCTGGCTCAGACTTCAGCGTT
GGGGCTGACACAGCACTCAATACTATCTGCACAACCTGTGACCGCATCAAGCAGTCAGCA
GCTGGCACCAAGCGTCGGGTGTTTATCATTGAGACTATGGGTGGCTACTGTGGCTACCTG
GCTACCATGGCTGGACTGGCAGCTGGGGCCGATGCTGCCTACATTTTTGAGGAGCCCTTC
ACCATTCGAGACCTGCAGGCAAATGTTGAACATCTGGTGCAAAAGATGAAAACAACTGTG
AAAAGGGGCTTGGTGTTAAGGAATGAAAAGTGCAATGAGAACTATACCACTGACTTCATT
TTCAACCTGTACTCTGAGGAGGGGAAGGGCATCTTCGACAGCAGGAAGAATGTGCTTGGT
CACATGCAGCAGGGTGGGAGCCCAACCCCATTTGATAGGAATTTTGCCACTAAGATGGGC
GCCAAGGCTATGAACTGGATGTCTGGGAAAATCAAAGAGAGTTACCGTAATGGGCGGATC
TTTGCCAATACTCCAGATTCGGGCTGTGTTCTGGGGATGCGTAAGAGGGCTCTGGTCTTC
CAACCAGTGGCTGAGCTGAAGGACCAGACAGATTTTGAGCATCGAATCCCCAAGGAACAG
TGGTGGCTGAAACTGAGGCCCATCCTCAAAATCCTAGCCAAGTACGAGATTGACTTGGAC
ACTTCAGACCATGCCCACCTGGAGCACATCACCCGGAAGCGGTCCGGGGAAGCTGCCGTC
TAA
Enzyme 25 GenBank Gene ID M59741 Link Image
Enzyme 25 GeneCard ID PFKM Link Image
Enzyme 25 GenAtlas ID PFKM Link Image
Enzyme 25 HGNC ID HGNC:8877 Link Image
Enzyme 25 Chromosome Location 12
Enzyme 25 Locus 12q13.3
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References
  1. Yamasaki T, Nakajima H, Kono N, Hotta K, Yamada K, Imai E, Kuwajima M, Noguchi T, Tanaka T, Tarui S: Structure of the entire human muscle phosphofructokinase-encoding gene: a two-promoter system. Gene. 1991 Aug 15;104(2):277-82. [PubMed Link Image]
  2. Sharma PM, Reddy GR, Vora S, Babior BM, McLachlan A: Cloning and expression of a human muscle phosphofructokinase cDNA. Gene. 1989 Apr 15;77(1):177-83. [PubMed Link Image]
  3. Nakajima H, Noguchi T, Yamasaki T, Kono N, Tanaka T, Tarui S: Cloning of human muscle phosphofructokinase cDNA. FEBS Lett. 1987 Oct 19;223(1):113-6. [PubMed Link Image]
  4. Sharma PM, Reddy GR, Babior BM, McLachlan A: Alternative splicing of the transcript encoding the human muscle isoenzyme of phosphofructokinase. J Biol Chem. 1990 Jun 5;265(16):9006-10. [PubMed Link Image]
  5. Valdez BC, Chen Z, Sosa MG, Younathan ES, Chang SH: Human 6-phosphofructo-1-kinase gene has an additional intron upstream of start codon. Gene. 1989 Mar 15;76(1):167-9. [PubMed Link Image]
  6. Raben N, Sherman JB: Mutations in muscle phosphofructokinase gene. Hum Mutat. 1995;6(1):1-6. [PubMed Link Image]
  7. Tsujino S, Servidei S, Tonin P, Shanske S, Azan G, DiMauro S: Identification of three novel mutations in non-Ashkenazi Italian patients with muscle phosphofructokinase deficiency. Am J Hum Genet. 1994 May;54(5):812-9. [PubMed Link Image]
  8. Raben N, Exelbert R, Spiegel R, Sherman JB, Nakajima H, Plotz P, Heinisch J: Functional expression of human mutant phosphofructokinase in yeast: genetic defects in French Canadian and Swiss patients with phosphofructokinase deficiency. Am J Hum Genet. 1995 Jan;56(1):131-41. [PubMed Link Image]
  9. Hamaguchi T, Nakajima H, Noguchi T, Nakagawa C, Kuwajima M, Kono N, Tarui S, Matsuzawa Y: Novel missense mutation (W686C) of the phosphofructokinase-M gene in a Japanese patient with a mild form of glycogenosis VII. Hum Mutat. 1996;8(3):273-5. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 6041
Enzyme 26 Name Pyruvate kinase isozymes R/L
Enzyme 26 Synonyms
  1. R-type/L-type pyruvate kinase
  2. Red cell/liver pyruvate kinase
  3. Pyruvate kinase 1
Enzyme 26 Gene Name PKLR
Enzyme 26 Protein Sequence >Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
Enzyme 26 Number of Residues 574
Enzyme 26 Molecular Weight 61831
Enzyme 26 Theoretical pI 7.83
Enzyme 26 GO Classification
Function
  • catalytic activity
  • kinase activity
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • metabolism
  • monosaccharide metabolism
  • physiological process
Component
Enzyme 26 General Function Carbohydrate transport and metabolism
Enzyme 26 Specific Function ATP + pyruvate = ADP + phosphoenolpyruvate
Enzyme 26 Pathways
Enzyme 26 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 3327365 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID P30613 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name KPYR_HUMAN Link Image
Enzyme 26 PDB ID 1LIU Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >1725 bp
ATGTCGATCCAGGAGAACATATCATCCCTGCAGCTTCGGTCATGGGTCTCTAAGTCCCAA
AGAGACTTAGCAAAGTCCATCCTGATTGGGGCTCCAGGAGGGCCAGCGGGGTATCTGCGG
CGGGCCAGTGTGGCCCAACTGACCCAGGAGCTGGGCACTGCCTTCTTCCAGCAGCAGCAG
CTGCCAGCTGCTATGGCAGACACCTTCCTGGAACACCTCTGCCTACTGGACATTGACTCC
GAGCCCGTGGCTGCTCGCAGTACCAGCATCATTGCCACCATCGGGCCAGCATCTCGCTCC
GTGGAGCGCCTCAAGGAGATGATCAAGGCCGGGATGAACATTGCGCGACTCAACTTCTCC
CACGGCTCCCACGAGTACCATGCTGAGTCCATCGCCAACGTCCGGGAGGCGGTGGAGAGC
TTTGCAGGTTCCCCACTCAGCTACCGGCCCGTGGCCATCGCCCTGGACACCAAGGGACCG
GAGATCCGCACTGGGATCCTGCAGGGGGGTCCAGAGTCGGAAGTGGAGCTGGTGAAGGGC
TCCCAGGTGCTGGTGACTGTGGACCCCGCGTTCCGGACGCGGGGGAACGCGAACACCGTG
TGGGTGGACTACCCCAATATTGTCCGGGTCGTGCCGGTGGGGGGCCGCATCTACATTGAC
GACGGGCTCATCTCCCTAGTGGTCCAGAAAATCGGCCCAGAGGGACTGGTGACCCAAGTG
GAGAACGGCGGCGTCCTGGGCAGCCGGAAGGGCGTGAACTTGCCAGGGGCCCAGGTGGAC
TTGCCCGGGCTGTCCGAGCAGGACGTCCGAGACCTGCGCTTCGGGGTGGAGCATGGGGTG
GACATCGTCTTTGCCTCCTTTGTGCGGAAAGCCAGCGACGTGGCTGCCGTCAGGGCTGCT
CTGGGTCCGGAAGGACACGGCATCAAGATCATCAGCAAAATTGAGAACCACGAAGGCGTG
AAGAGGTTTGATGAAATCCTGGAGGTGAGCGACGGCATCATGGTGGCACGGGGGGACCTA
GGCATCGAGATCCCAGCAGAGAAGGTTTTCCTGGCTCAGAAGATGATGATTGGGCGCTGC
AACTTGGCGGGCAAGCCTGTTGTCTGTGCCACACAGATGCTGGAGAGCATGATTACCAAG
CCCCGGCCAACGAGGGCAGAGACAAGCGATGTCGCCAATGCTGTGCTGGATGGGGCTGAC
TGCATCATGCTGTCAGGGGAGACTGCCAAGGGCAACTTCCCTGTGGAAGCGGTGAAGATG
CAGCATGCGATTGCCCGGGAGGCAGAGGCCGCAGTGTACCACCGGCAGCTGTTTGAGGAG
CTACGTCGGGCAGCGCCACTAAGCCGTGATCCCACTGAGGTCACCGCCATTGGTGCTGTG
GAGGCTGCCTTCAAGTGCTGTGCTGCTGCCATCATTGTGCTGACCACAACTGGCCGCTCA
GCCCAGCTTCTGTCTCGGTACCGACCTCGGGCAGCAGTCATTGCTGTCACCCGCTCTGCC
CAGGCTGCCCGCCAGGTCCACTTATGCCGAGGAGTCTTCCCCTTGCTTTACCGTGAACCT
CCAGAAGCCATCTGGGCAGATGATGTAGATCGCCGGGTGCAATTTGGCATTGAAAGTGGA
AAGCTCCGTGGCTTCCTCCGTGTTGGAGACCTGGTGATTGTGGTGACAGGCTGGCGACCT
GGCTCCGGCTACACCAACATCATGAGGGTGCTAAGCATATCCTGA
Enzyme 26 GenBank Gene ID AB015983 Link Image
Enzyme 26 GeneCard ID PKLR Link Image
Enzyme 26 GenAtlas ID PKLR Link Image
Enzyme 26 HGNC ID HGNC:9020 Link Image
Enzyme 26 Chromosome Location 1
Enzyme 26 Locus 1q21
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Kanno H, Fujii H, Hirono A, Miwa S: cDNA cloning of human R-type pyruvate kinase and identification of a single amino acid substitution (Thr384----Met) affecting enzymatic stability in a pyruvate kinase variant (PK Tokyo) associated with hereditary hemolytic anemia. Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8218-21. [PubMed Link Image]
  2. Tani K, Fujii H, Nagata S, Miwa S: Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells. Proc Natl Acad Sci U S A. 1988 Mar;85(6):1792-5. [PubMed Link Image]
  3. Tani K, Fujii H, Tsutsumi H, Sukegawa J, Toyoshima K, Yoshida MC, Noguchi T, Tanaka T, Miwa S: Human liver type pyruvate kinase: cDNA cloning and chromosomal assignment. Biochem Biophys Res Commun. 1987 Mar 13;143(2):431-8. [PubMed Link Image]
  4. Kanno H, Fujii H, Tsujino G, Miwa S: Molecular basis of impaired pyruvate kinase isozyme conversion in erythroid cells: a single amino acid substitution near the active site and decreased mRNA content of the R-type PK. Biochem Biophys Res Commun. 1993 Apr 15;192(1):46-52. [PubMed Link Image]
  5. Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed Link Image]
  6. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase. Blood Cells Mol Dis. 1996;22(1):85-9. [PubMed Link Image]
  7. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (1st update). Blood Cells Mol Dis. 1996;22(3):259-64. [PubMed Link Image]
  8. Baronciani L, Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (2nd update). Blood Cells Mol Dis. 1998 Sep;24(3):273-9. [PubMed Link Image]
  9. Bianchi P, Zanella A: Hematologically important mutations: red cell pyruvate kinase (Third update). Blood Cells Mol Dis. 2000 Feb;26(1):47-53. [PubMed Link Image]
  10. Neubauer B, Lakomek M, Winkler H, Parke M, Hofferbert S, Schroter W: Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency. Blood. 1991 May 1;77(9):1871-5. [PubMed Link Image]
  11. Kanno H, Fujii H, Hirono A, Omine M, Miwa S: Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia. Blood. 1992 Mar 1;79(5):1347-50. [PubMed Link Image]
  12. Kanno H, Fujii H, Miwa S: Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused by a single amino acid substitution (426 Arg-->Gln) associated with hereditary hemolytic anemia. Blood. 1993 May 1;81(9):2439-41. [PubMed Link Image]
  13. Baronciani L, Beutler E: Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia. Proc Natl Acad Sci U S A. 1993 May 1;90(9):4324-7. [PubMed Link Image]
  14. Kanno H, Ballas SK, Miwa S, Fujii H, Bowman HS: Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish. Blood. 1994 Apr 15;83(8):2311-6. [PubMed Link Image]
  15. Lenzner C, Nurnberg P, Thiele BJ, Reis A, Brabec V, Sakalova A, Jacobasch G: Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia. Blood. 1994 May 15;83(10):2817-22. [PubMed Link Image]
  16. Baronciani L, Beutler E: Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia. J Clin Invest. 1995 Apr;95(4):1702-9. [PubMed Link Image]
  17. Beutler E, Westwood B, van Zwieten R, Roos D: G-->T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP. Hum Mutat. 1997;9(3):282-5. [PubMed Link Image]
  18. Zarza R, Alvarez R, Pujades A, Nomdedeu B, Carrera A, Estella J, Remacha A, Sanchez JM, Morey M, Cortes T, Perez Lungmus G, Bureo E, Vives Corrons JL: Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients. Red Cell Pathology Group of the Spanish Society of Haematology (AEHH). Br J Haematol. 1998 Nov;103(2):377-82. [PubMed Link Image]
  19. Cohen-Solal M, Prehu C, Wajcman H, Poyart C, Bardakdjian-Michau J, Kister J, Prome D, Valentin C, Bachir D, Galacteros F: A new sickle cell disease phenotype associating Hb S trait, severe pyruvate kinase deficiency (PK Conakry), and an alpha2 globin gene variant (Hb Conakry). Br J Haematol. 1998 Dec;103(4):950-6. [PubMed Link Image]
  20. Pastore L, Della Morte R, Frisso G, Alfinito F, Vitale D, Calise RM, Ferraro F, Zagari A, Rotoli B, Salvatore F: Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy. Hum Mutat. 1998;11(2):127-34. [PubMed Link Image]
  21. Zanella A, Bianchi P, Fermo E, Iurlo A, Zappa M, Vercellati C, Boschetti C, Baronciani L, Cotton F: Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients. Br J Haematol. 2001 Apr;113(1):43-8. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6126
Enzyme 27 Name Ceramide glucosyltransferase
Enzyme 27 Synonyms
  1. Glucosylceramide synthase
  2. GCS
  3. UDP-glucose:N-acylsphingosine D-glucosyltransferase
  4. UDP- glucose ceramide glucosyltransferase
  5. GLCT-1
Enzyme 27 Gene Name UGCG
Enzyme 27 Protein Sequence >Ceramide glucosyltransferase
MALLDLALEGMAVFGFVLFLVLWLMHFMAIIYTRLHLNKKATDKQPYSKLPGVSLLKPLK
GVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVG
INPKINNLMPGYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTEKVGLVHGLPYVADRQGF
AATLEQVYFGTSHPRYYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMA
KAIADRGWRFAMSTQVAMQNSGSYSISQFQSRMIRWTKLRINMLPATIICEPISECFVAS
LIIGWAAHHVFRWDIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVAWFIRESMT
IYIFLSALWDPTISWRTGRYRLRCGGTAEEILDV
Enzyme 27 Number of Residues 394
Enzyme 27 Molecular Weight 44854
Enzyme 27 Theoretical pI 7.86
Enzyme 27 GO Classification Not Available
Enzyme 27 General Function Cell wall/membrane/envelope biogenesis
Enzyme 27 Specific Function May serve as a "flippase" as well as a glucosyltransferase that transfers glucose to ceramide
Enzyme 27 Pathways
Enzyme 27 Reactions
  • UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • 1-29
Enzyme 27 Transmembrane Regions Not Available
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein 1325917 Link Image
Enzyme 27 UniProtKB/Swiss-Prot ID Q16739 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name CEGT_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence >1185 bp
ATGGCGCTGCTGGACCTGGCCTTGGAGGGAATGGCCGTCTTCGGGTTCGTCCTCTTCTTG
GTGCTGTGGCTGATGCATTTCATGGCTATCATCTACACCCGATTACACCTCAACAAGAAG
GCAACTGACAAACAGCCTTATAGCAAGCTCCCAGGTGTCTCTCTTCTGAAACCACTGAAA
GGGGTAGATCCTAACTTAATCAACAACCTGGAAACATTCTTTGAATTGGATTATCCCAAA
TATGAAGTGCTCCTTTGTGTACAAGATCATGATGATCCAGCCATTGATGTATGTAAGAAG
CTTCTTGGAAAATATCCAAATGTTGATGCTAGATTGTTTATAGGTGGTAAAAAAGTTGGC
ATTAATCCTAAAATTAATAATTTAATGCCAGGATATGAAGTTGCAAAGTATGATCTTATA
TGGATTTGTGATAGTGGAATAAGAGTAATTCCAGATACGCTTACTGACATGGTGAATCAA
ATGACAGAAAAAGTAGGCTTGGTTCACGGGCTGCCTTACGTAGCAGACAGACAGGGCTTT
GCTGCCACCTTAGAGCAGGTATATTTTGGAACTTCACATCCAAGATACTATATCTCTGCC
AATGTAACTGGTTTCAAATGTGTGACAGGAATGTCTTGTTTAATGAGAAAAGATGTGTTG
GATCAAGCAGGAGGACTTATAGCTTTTGCTCAGTACATTGCCGAAGATTACTTTATGGCC
AAAGCGATAGCTGACCGAGGTTGGAGGTTTGCAATGTCCACTCAAGTTGCAATGCAAAAC
TCTGGCTCATATTCAATTTCTCAGTTTCAATCCAGAATGATCAGGTGGACCAAACTACGA
ATTAACATGCTTCCTGCTACAATAATTTGTGAGCCAATTTCAGAATGCTTTGTTGCCAGT
TTAATTATTGGATGGGCAGCCCACCATGTGTTCAGATGGGATATTATGGTATTTTTCATG
TGTCATTGCCTGGCATGGTTTATATTTGACTACATTCAACTCAGGGGTGTCCAGGGTGGC
ACACTGTGTTTTTCAAAACTTGATTATGCAGTCGCCTGGTTCATCCGCGAATCCATGACA
ATATACATTTTTTTGTCTGCATTATGGGACCCAACTATAAGCTGGAGAACTGGTCGCTAC
AGATTACGCTGTGGGGGTACAGCAGAGGAAATCCTAGATGTATAA
Enzyme 27 GenBank Gene ID D50840 Link Image
Enzyme 27 GeneCard ID UGCG Link Image
Enzyme 27 GenAtlas ID UGCG Link Image
Enzyme 27 HGNC ID HGNC:12524 Link Image
Enzyme 27 Chromosome Location 9
Enzyme 27 Locus 9q31
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References
  1. Ichikawa S, Sakiyama H, Suzuki G, Hidari KI, Hirabayashi Y: Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis. Proc Natl Acad Sci U S A. 1996 May 14;93(10):4638-43. [PubMed Link Image]
  2. Ichikawa S, Sakiyama H, Suzuki G, Hidari KI, Hirabayashi Y: Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis. Proc Natl Acad Sci U S A. 1996 Oct 29;93(22):12654. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6155
Enzyme 28 Name Beta-1,4 N-acetylgalactosaminyltransferase 1
Enzyme 28 Synonyms
  1. (N- acetylneuraminyl-galactosylglucosylceramide
  2. GM2/GD2 synthase
  3. GalNAc-T
Enzyme 28 Gene Name B4GALNT1
Enzyme 28 Protein Sequence >Beta-1,4 N-acetylgalactosaminyltransferase 1
MWLGRRALCALVLLLACASLGLLYASTRDAPGLRLPLAPWAPPQSPRRPELPDLAPEPRY
AHIPVRIKEQVVGLLAWNNCSCESSGGGLPLPFQKQVRAIDLTKAFDPAELRAASATREQ
EFQAFLSRSQSPADQLLIAPANSPLQYPLQGVEVQPLRSILVPGLSLQAASGQEVYQVNL
TASLGTWDVAGEVTGVTLTGEGQADLTLVSPGLDQLNRQLQLVTYSSRSYQTNTADTVRF
STEGHEAAFTIRIRHPPNPRLYPPGSLPQGAQYNISALVTIATKTFLRYDRLRALITSIR
RFYPTVTVVIADDSDKPERVSGPYVEHYLMPFGKGWFAGRNLAVSQVTTKYVLWVDDDFV
FTARTRLERLVDVLERTPLDLVGGAVREISGFATTYRQLLSVEPGAPGLGNCLRQRRGFH
HELVGFPGCVVTDGVVNFFLARTDKVREVGFDPRLSRVAHLEFFLDGLGSLRVGSCSDVV
VDHASKLKLPWTSRDAGAETYARYRYPGSLDESQMAKHRLLFFKHRLQCMTSQ
Enzyme 28 Number of Residues 533
Enzyme 28 Molecular Weight 58883
Enzyme 28 Theoretical pI 8.82
Enzyme 28 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • lipid glycosylation
  • lipid modification
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Involved in the biosynthesis of gangliosides GM2, GD2 and GA2
Enzyme 28 Pathways
Enzyme 28 Reactions
  • UDP-N-acetyl-D-galactosamine + (N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide = UDP + N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • 1-25
Enzyme 28 Transmembrane Regions Not Available
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 431033 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID Q00973 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name B4GN1_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence >1602 bp
ATGTGGCTGGGCCGCCGGGCCCTGTGCGCTCTGGTCCTTCTGCTCGCCTGCGCCTCGCTG
GGGCTCCTGTACGCGAGCACCCGGGACGCGCCCGGCCTCCGGCTACCTCTTGCGCCGTGG
GCGCCCCCGCAAAGCCCCCGCAGGCCCGAGCTGCCAGATCTTGCTCCTGAGCCCCGCTAC
GCACACATCCCGGTCAGGATCAAGGAGCAAGTAGTGGGGCTGCTGGCTTGGAACAACTGC
AGTTGTGAGTCCAGTGGGGGGGGCCTCCCCCTCCCCTTCCAGAAACAAGTCCGAGCTATT
GACCTCACCAAGGCCTTTGACCCTGCAGAGCTGAGGGCTGCCTCTGCCACAAGAGAGCAG
GAGTTCCAGGCCTTTCTGTCGAGGAGCCAGTCCCCAGCTGACCAGCTGCTCATAGCCCCT
GCCAACTCCCCGCTCCAGTACCCCCTACAGGGTGTGGAAGTTCAGCCCCTCAGGAGCATC
TTGGTGCCAGGGCTGAGCCTTCAGGCAGCTTCTGGTCAGGAGGTATACCAGGTGAACCTG
ACTGCCTCCCTAGGCACCTGGGACGTGGCAGGGGAAGTGACTGGAGTTACTCTCACTGGA
GAGGGTCAGGCAGATCTCACCCTTGTCAGCCCAGGGCTGGACCAACTCAACAGGCAACTA
CAACTGGTCACTTACAGCAGCCGAAGCTACCAGACCAACACAGCAGACACAGTCCGGTTC
TCCACCGAGGGACATGAGGCTGCTTTCACTATCCGCATAAGACACCCGCCCAACCCTCGG
CTGTACCCACCTGGGTCTCTACCCCAGGGAGCCCAGTACAACATCAGCGCTCTAGTCACG
ATTGCCACCAAGACCTTCCTCCGTTATGATCGGCTACGGGCTCTCATCACCAGTATCCGC
CGCTTCTACCCAACGGTTACCGTGGTCATCGCTGACGACAGCGACAAGCCAGAGCGCGTT
AGTGGCCCCTACGTGGAACACTATCTCATGCCCTTCGGCAAGGGCTGGTTCGCAGGCCGG
AACCTGGCCGTGTCTCAAGTAACCACCAAGTACGTGCTGTGGGTGGACGACGACTTCGTC
TTCACGGCGCGGACGCGGCTGGAGAGGCTTGTGGACGTGCTGGAGCGGACGCCGCTGGAC
CTGGTGGGGGGCGCGGTGCGCGAGATCTCCGGCTTTGCCACCACTTATCGGCAGCTGCTG
AGCGTGGAGCCCGGCGCCCCAGGCCTCGGGAACTGCCTCCGGCAAAGGCGCGGCTTCCAC
CACGAGCTCGTCGGCTTCCCAGGCTGCGTGGTCACCGACGGCGTGGTTAACTTCTTCCTG
GCGCGGACTGACAAGGTGCGCGAGGTCGGTTTCGACCCCCGCCTCAGCCGCGTGGCTCAT
CTGGAATTCTTCTTGGATGGGCTTGGTTCCCTTCGGGTTGGCTCCTGCTCCGACGTCGTG
GTGGATCATGCATCCAAACTGAAGCTGCCTTGGACATCAAGGGATGCCGGAGCAGAGACT
TACGCCCGGTACCGTTACCCAGGATCACTGGACGAGAGCCAGATGGCCAAACACCGGCTG
CTCTTCTTCAAACACCGGCTGCAGTGCATGACCTCCCAGTGA
Enzyme 28 GenBank Gene ID M83651 Link Image
Enzyme 28 GeneCard ID B4GALNT1 Link Image
Enzyme 28 GenAtlas ID B4GALNT1 Link Image
Enzyme 28 HGNC ID HGNC:4117 Link Image
Enzyme 28 Chromosome Location 12
Enzyme 28 Locus 12q13.3
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References
  1. Nagata Y, Yamashiro S, Yodoi J, Lloyd KO, Shiku H, Furukawa K: Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase cDNAs that determine the expression of GM2 and GD2 gangliosides. J Biol Chem. 1992 Jun 15;267(17):12082-9. [PubMed Link Image]
  2. Nagata Y, Yamashiro S, Yodoi J, Lloyd KO, Shiku H, Furukawa K: Expression cloning of beta 1,4 N-acetylgalactosaminyltransferase cDNAs that determine the expression of GM2 and GD2 gangliosides. J Biol Chem. 1994 Mar 4;269(9):7045. [PubMed Link Image]
  3. Li J, Yen TY, Allende ML, Joshi RK, Cai J, Pierce WM, Jaskiewicz E, Darling DS, Macher BA, Young WW Jr: Disulfide bonds of GM2 synthase homodimers. Antiparallel orientation of the catalytic domains. J Biol Chem. 2000 Dec 29;275(52):41476-86. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 6221
Enzyme 29 Name Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
Enzyme 29 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 29 Gene Name B3GAT3
Enzyme 29 Protein Sequence >Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
MKLKLKNVFLAYFLVSIAGLLYALVQLGQPCDCLPPLRAAAEQLRQKDLRISQLQAELRR
PPPAPAQPPEPEALPTIYVVTPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAEGPTPL
VSGLLAASGLLFTHLVVLTPKAQRLREGEPGWVHPRGVEQRNKALDWLRGRGGAVGGEKD
PPPPGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDGRVVGFH
TAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTAPRGHLESSLLSHLVDPKDLEPRAAN
CTRVLVWHTRTEKPKMKQEEQLQRQGRGSDPAIEV
Enzyme 29 Number of Residues 335
Enzyme 29 Molecular Weight 37122
Enzyme 29 Theoretical pI 8.47
Enzyme 29 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 29 General Function Not Available
Enzyme 29 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 29 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 29 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 29 Pfam Domain Function
Enzyme 29 Signals
  • 1-23
Enzyme 29 Transmembrane Regions Not Available
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 3892640 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID O94766 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name B3GA3_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >1008 bp
ATGAAGCTGAAGCTGAAGAACGTGTTTCTCGCCTACTTCCTGGTGTCGATCGCCGGCCTC
CTCTACGCGCTGGTACAGCTCGGCCAGCCATGTGACTGCCTTCCTCCCCTGCGGGCAGCA
GCCGAGCAGCTACGGCAGAAGGATCTGAGGATTTCCCAGCTGCAAGCGGAACTCCGACGG
CCACCCCCTGCCCCTGCCCAGCCCCCTGAACCCGAGGCCCTGCCTACTATCTATGTTGTT
ACCCCCACCTATGCCAGGCTGGTACAGAAGGCAGAGCTGGTACGACTGTCCCAGACACTG
AGCCTGGTGCCCCGGCTGCATTGGCTGCTGGTGGAGGATGCTGAGGGTCCCACCCCGCTG
GTCTCAGGGCTGCTGGCTGCCTCTGGCCTCCTCTTCACACACCTGGTGGTCCTCACGCCC
AAAGCCCAGCGGCTTCGGGAGGGCGAGCCTGGCTGGGTTCATCCCCGTGGTGTCGAGCAG
CGGAACAAGGCCCTGGACTGGCTCCGGGGCAGAGGGGGTGCTGTGGGTGGGGAGAAGGAC
CCACCACCACCAGGGACCCAAGGAGTCGTTTACTTTGCTGACGATGACAACACCTACAGC
CGGGAGCTGTCTGAGGAGATGCGCTGGACCCGTGGTGTCTCAGTGTGGCCTGTGGGGCTG
GTGGGCGGCCTGCGATTCGAGGGCCCTCAGGTACAGGACGGCCGGGTAGTGGGCTTCCAC
ACAGCATGGGAGCCCAGCAGGCCCTTCCCTGTGGATATGGCTGGATTTGCCGTGGCCCTG
CCCTTGCTGTTAGATAAGCCCAATGCCCAATTTGATTCCACCGCTCCCCGGGGCCACCTG
GAGAGCAGTCTTCTGAGCCACCTTGTGGATCCCAAGGACCTGGAGCCACGGGCTGCCAAC
TGCACTCGGGTACTGGTGTGGCATACTCGGACAGAGAAGCCCAAGATGAAGCAGGAGGAG
CAGCTGCAGCGGCAGGGCCGGGGCTCAGACCCAGCAATTGAGGTGTGA
Enzyme 29 GenBank Gene ID AB009598 Link Image
Enzyme 29 GeneCard ID B3GAT3 Link Image
Enzyme 29 GenAtlas ID B3GAT3 Link Image
Enzyme 29 HGNC ID HGNC:923 Link Image
Enzyme 29 Chromosome Location 11
Enzyme 29 Locus 11q12.3
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 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 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 6222
Enzyme 30 Name Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
Enzyme 30 Synonyms
  1. Beta-1,3-glucuronyltransferase 2
  2. Glucuronosyltransferase-S
  3. GlcAT-S
  4. UDP-glucuronosyltransferase-S
  5. GlcAT-D
Enzyme 30 Gene Name B3GAT2
Enzyme 30 Protein Sequence >Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
MKSALFTRFFILLPWILIVIIMLDVDTRRPVPPLTPRPYFSPYAVGRGGARLPLRRGGPA
HGTQKRNQSRPQPQPEPQLPTIYAITPTYSRPVQKAELTRLANTFRQVAQLHWILVEDAA
ARSELVSRFLARAGLPSTHLHVPTPRRYKRPGLPRATEQRNAGLAWLRQRHQHQRAQPGV
LFFADDDNTYSLELFQEMRTTRKVSVWPVGLVGGRRYERPLVENGKVVGWYTGWRADRPF
AIDMAGFAVSLQVILSNPKAVFKRRGSQPGMQESDFLKQITTVEELEPKANNCTKVLVWH
TRTEKVNLANEPKYHLDTVKIEV
Enzyme 30 Number of Residues 323
Enzyme 30 Molecular Weight 36919
Enzyme 30 Theoretical pI 11.20
Enzyme 30 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 30 General Function Not Available
Enzyme 30 Specific Function Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins
Enzyme 30 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 30 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 30 Pfam Domain Function
Enzyme 30 Signals
  • 1-27
Enzyme 30 Transmembrane Regions Not Available
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 18086555 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID Q9NPZ5 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name B3GA2_HUMAN Link Image
Enzyme 30 PDB ID Not Available
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >972 bp
ATGAAGTCCGCGCTTTTCACCCGCTTCTTTATCCTCCTGCCCTGGATCCTAATTGTCATC
ATCATGCTCGACGTGGACACGCGCAGGCCAGTGCCCCCGCTCACCCCGCGCCCCTACTTC
TCTCCCTACGCGGTGGGCCGCGGGGGCGCCCGACTCCCGCTCCGCAGGGGCGGCCCGGCT
CACGGGACCCAAAAGCGCAACCAGTCTCGGCCGCAGCCACAGCCGGAGCCGCAGCTGCCC
ACCATCTATGCCATCACGCCCACCTACAGCCGCCCGGTGCAGAAAGCGGAGCTGACCCGC
CTGGCCAACACGTTCCGCCAGGTGGCGCAGCTGCACTGGATCCTGGTGGAGGACGCGGCG
GCGCGCAGCGAGCTGGTGAGCCGCTTCCTGGCGCGGGCCGGGCTGCCCAGCACTCACCTG
CACGTGCCCACGCCGCGGCGCTACAAGCGGCCCGGGCTGCCGCGCGCCACTGAGCAGCGC
AACGCGGGCCTCGCCTGGCTGCGCCAGAGGCACCAGCACCAGCGCGCGCAGCCCGGCGTG
CTCTTCTTCGCTGACGACGACAACACCTATAGTCTGGAGCTCTTCCAGGAGATGCGAACC
ACCCGCAAGGTCTCCGTCTGGCCTGTGGGCCTGGTTGGTGGGCGGCGCTACGAACGTCCG
CTGGTGGAAAACGGCAAAGTTGTTGGCTGGTACACCGGCTGGAGAGCAGACAGGCCTTTT
GCCATCGACATGGCAGGATTTGCTGTAAGTCTTCAAGTCATTTTGTCCAATCCAAAAGCT
GTATTTAAGCGTCGTGGATCCCAGCCAGGGATGCAAGAATCTGACTTTCTCAAACAGATA
ACAACAGTCGAAGAACTGGAACCGAAAGCAAATAACTGCACTAAGGTTCTCGTGTGGCAC
ACTCGGACAGAGAAGGTTAATCTAGCCAACGAGCCAAAGTACCACCTGGACACAGTGAAA
ATTGAGGTATAA
Enzyme 30 GenBank Gene ID AY070019 Link Image
Enzyme 30 GeneCard ID B3GAT2 Link Image
Enzyme 30 GenAtlas ID B3GAT2 Link Image
Enzyme 30 HGNC ID HGNC:922 Link Image
Enzyme 30 Chromosome Location 6
Enzyme 30 Locus 6q13
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 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 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 6223
Enzyme 31 Name Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
Enzyme 31 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 31 Gene Name B3GAT1
Enzyme 31 Protein Sequence >Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
MPKRRDILAIVLIVLPWTLLITVWHQSTLAPLLAVHKDEGSDPRRETPPGADPREYCTSD
RDIVEVVRTEYVYTRPPPWSDTLPTIHVVTPTYSRPVQKAELTRMANTLLHVPNLHWLVV
EDAPRRTPLTARLLRDTGLNYTHLHVETPRNYKLRGDARDPRIPRGTMQRNLALRWLRET
FPRNSSQPGVVYFADDDNTYSLELFEEMRSTRRVSVWPVAFVGGLRYEAPRVNGAGKVVR
WKTVFDPHRPFAIDMAGFAVNLRLILQRSQAYFKLRGVKGGYQESSLLRELVTLNDLEPK
AANCTKILVWHTRTEKPVLVNEGKKGFTDPSVEI
Enzyme 31 Number of Residues 334
Enzyme 31 Molecular Weight 38356
Enzyme 31 Theoretical pI 10.13
Enzyme 31 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 31 General Function Not Available
Enzyme 31 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 31 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 31 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 31 Pfam Domain Function
Enzyme 31 Signals
  • 1-29
Enzyme 31 Transmembrane Regions Not Available
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein 8051678 Link Image
Enzyme 31 UniProtKB/Swiss-Prot ID Q9P2W7 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name B3GA1_HUMAN Link Image
Enzyme 31 PDB ID Not Available
Enzyme 31 Cellular Location Not Available
Enzyme 31 Gene Sequence >1005 bp
ATGCCGAAGAGACGGGACATCCTAGCGATCGTCCTCATCGTGCTGCCCTGGACTCTGCTC
ATCACTGTCTGGCACCAGAGCACCCTCGCACCCCTGCTCGCGGTACATAAGGATGAGGGC
AGTGACCCCCGACGCGAAACGCCGCCCGGCGCCGACCCCAGGGAGTACTGCACGTCTGAC
CGCGACATCGTGGAGGTGGTGCGCACCGAGTACGTGTACACGCGGCCCCCGCCATGGTCC
GACACGCTGCCCACCATCCACGTGGTGACGCCCACCTACAGCCGCCCGGTGCAGAAGGCC
GAGCTGACGCGCATGGCCAACACGCTGCTGCACGTGCCCAACCTCCACTGGCTGGTGGTG
GAGGATGCGCCGCGCCGGACGCCGCTGACCGCGCGCCTGCTGCGCGACACCGGCCTCAAC
TACACGCACCTGCACGTGGAGACGCCCCGCAACTACAAGCTGCGCGGAGACGCCCGCGAC
CCACGCATCCCGCGGGGCACCATGCAGCGCAACCTGGCCCTGCGCTGGCTGCGCGAGACC
TTCCCGCGCAACTCCAGCCAGCCTGGCGTGGTCTACTTCGCCGACGACGACAACACCTAC
AGCCTGGAGCTCTTCGAAGAGATGCGCAGCACCAGGAGGGTGTCCGTGTGGCCCGTCGCC
TTCGTGGGTGGCCTGCGGTACGAGGCCCCACGGGTGAACGGGGCAGGGAAGGTGGTCCGC
TGGAAGACGGTGTTTGACCCCCACCGGCCATTTGCAATAGACATGGCTGGATTTGCCGTC
AACCTGCGGCTCATTCTGCAGCGAAGCCAGGCCTACTTCAAGCTGCGAGGTGTGAAGGGA
GGCTACCAGGAAAGCAGCCTCCTTCGAGAACTTGTCACCCTCAACGACCTGGAGCCCAAG
GCAGCCAACTGCACCAAGATCCTGGTGTGGCACACACGGACAGAGAAGCCAGTGCTGGTG
AATGAGGGCAAGAAGGGCTTCACTGACCCCTCGGTGGAGATCTGA
Enzyme 31 GenBank Gene ID AB029396 Link Image
Enzyme 31 GeneCard ID B3GAT1 Link Image
Enzyme 31 GenAtlas ID B3GAT1 Link Image
Enzyme 31 HGNC ID HGNC:921 Link Image
Enzyme 31 Chromosome Location 11
Enzyme 31 Locus 11q25
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 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 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6229
Enzyme 32 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
Enzyme 32 Synonyms
  1. GlcNAc-PI synthesis protein
  2. Phosphatidylinositol- glycan biosynthesis class A protein
  3. PIG-A
Enzyme 32 Gene Name PIGA
Enzyme 32 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCL
IERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRE
RVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNH
IICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGI
DLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLV
QGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLE
KAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHC
GPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEI
SETR
Enzyme 32 Number of Residues 484
Enzyme 32 Molecular Weight 54127
Enzyme 32 Theoretical pI 8.41
Enzyme 32 GO Classification
Function
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 32 General Function Cell wall/membrane/envelope biogenesis
Enzyme 32 Specific Function Necessary for the synthesis of N-acetylglucosaminyl- phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis
Enzyme 32 Pathways Not Available
Enzyme 32 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 422-442
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein 219994 Link Image
Enzyme 32 UniProtKB/Swiss-Prot ID P37287 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name PIGA_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 Gene Sequence >1455 bp
ATGGCCTGTAGAGGAGGAGCTGGGAATGGCCACCGTGCCTCAGCTACACTCTCTCGGGTT
AGCCCTGGAAGTCTTTACACATGTAGAACCCGTACCCATAATATATGCATGGTATCTGAC
TTTTTCTACCCAAATATGGGAGGCGTGGAAAGCCACATTTACCAGCTCTCTCAGTGCCTG
ATTGAAAGAGGGCATAAGGTTATAATTGTCACCCATGCTTATGGAAATCGAAAAGGCATC
CGTTACCTCACCAGTGGCCTCAAAGTCTATTACTTGCCTCTGAAAGTCATGTACAACCAG
TCTACAGCCACGACCCTCTTTCACAGTCTGCCATTGCTCAGGTACATATTTGTTCGGGAG
AGAGTCACGATAATCCATTCACATAGTTCTTTTTCTGCTATGGCCCATGATGCTCTCTTC
CACGCCAAGACAATGGGGCTTCAGACAGTCTTCACGGACCATTCCCTTTTTGGATTTGCT
GATGTCAGCTCGGTGCTTACAAACAAGCTTCTAACCGTGTCTCTTTGTGATACAAACCAC
ATCATTTGTGTGTCTTATACTAGTAAGGAAAATACTGTACTAAGAGCAGCACTGAATCCT
GAAATAGTGTCCGTCATTCCTAATGCTGTAGATCCTACTGACTTCACTCCAGACCCATTT
AGAAGGCATGATAGTATAACTATTGTTGTTGTCAGCAGACTTGTTTACAGAAAAGGGATC
GATTTGCTTAGTGGTATAATACCTGAACTCTGTCAGAAATATCCAGATTTAAATTTCATA
ATTGGAGGAGAGGGACCAAAGAGAATCATTTTGGAAGAAGTTCGGGAAAGATACCAGCTG
CATGACAGGGTGCGTCTTTTGGGAGCTTTAGAACACAAGGATGTTAGAAATGTCTTAGTT
CAAGGACATATTTTTCTGAATACCTCCCTTACTGAAGCATTCTGCATGGCGATCGTGGAA
GCAGCCAGTTGTGGTTTACAGGTTGTAAGTACCAGAGTTGGTGGAATTCCTGAGGTGCTT
CCAGAAAACCTTATTATTTTATGTGAGCCTTCAGTAAAATCTTTGTGTGAAGGATTGGAA
AAGGCTATTTTCCAACTGAAGTCAGGGACATTGCCAGCTCCAGAAAACATCCATAACATA
GTAAAGACTTTCTACACCTGGAGGAATGTTGCAGAAAGAACTGAAAAGGTATATGACCGG
GTATCAGTGGAAGCTGTGTTGCCAATGGACAAACGACTGGACAGACTTATTTCTCACTGC
GGCCCAGTAACAGGCTACATCTTTGCTTTGTTGGCAGTTTTCAACTTCCTCTTCCTCATT
TTCTTGAGATGGATGACTCCAGATTCTATCATTGATGTTGCAATAGATGCCACTGGGCCA
CGGGGTGCCTGGACTAATAACTATTCTCACAGTAAAAGAGGGGGTGAGAATAATGAGATA
TCTGAAACCAGGTAG
Enzyme 32 GenBank Gene ID D11466 Link Image
Enzyme 32 GeneCard ID PIGA Link Image
Enzyme 32 GenAtlas ID PIGA Link Image
Enzyme 32 HGNC ID HGNC:8957 Link Image
Enzyme 32 Chromosome Location X
Enzyme 32 Locus Xp22.1
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 General References
  1. Miyata T, Takeda J, Iida Y, Yamada N, Inoue N, Takahashi M, Maeda K, Kitani T, Kinoshita T: The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis. Science. 1993 Feb 26;259(5099):1318-20. [PubMed Link Image]
  2. Bessler M, Hillmen P, Longo L, Luzzatto L, Mason PJ: Genomic organization of the X-linked gene (PIG-A) that is mutated in paroxysmal nocturnal haemoglobinuria and of a related autosomal pseudogene mapped to 12q21. Hum Mol Genet. 1994 May;3(5):751-7. [PubMed Link Image]
  3. Iida Y, Takeda J, Miyata T, Inoue N, Nishimura J, Kitani T, Maeda K, Kinoshita T: Characterization of genomic PIG-A gene: a gene for glycosylphosphatidylinositol-anchor biosynthesis and paroxysmal nocturnal hemoglobinuria. Blood. 1994 Jun 1;83(11):3126-31. [PubMed Link Image]
  4. Yu J, Nagarajan S, Ueda E, Knez JJ, Petersen RB, Medof ME: Characterization of alternatively spliced PIG-A transcripts in normal and paroxysmal nocturnal hemoglobinuria cells. Braz J Med Biol Res. 1994 Feb;27(2):195-201. [PubMed Link Image]
  5. Takeda J, Miyata T, Kawagoe K, Iida Y, Endo Y, Fujita T, Takahashi M, Kitani T, Kinoshita T: Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell. 1993 May 21;73(4):703-11. [PubMed Link Image]
  6. Bessler M, Mason PJ, Hillmen P, Miyata T, Yamada N, Takeda J, Luzzatto L, Kinoshita T: Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene. EMBO J. 1994 Jan 1;13(1):110-7. [PubMed Link Image]
  7. Ware RE, Rosse WF, Howard TA: Mutations within the Piga gene in patients with paroxysmal nocturnal hemoglobinuria. Blood. 1994 May 1;83(9):2418-22. [PubMed Link Image]
  8. Nafa K, Bessler M, Castro-Malaspina H, Jhanwar S, Luzzatto L: The spectrum of somatic mutations in the PIG-A gene in paroxysmal nocturnal hemoglobinuria includes large deletions and small duplications. Blood Cells Mol Dis. 1998 Sep;24(3):370-84. [PubMed Link Image]
  9. Yoon JH, Cho HI, Park SS, Chang YH, Kim BK: Mutation analysis of the PIG-A gene in Korean patients with paroxysmal nocturnal haemoglobinuria. J Clin Pathol. 2002 Jun;55(6):410-3. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6282
Enzyme 33 Name Polypeptide N-acetylgalactosaminyltransferase 4
Enzyme 33 Synonyms
  1. Protein-UDP acetylgalactosaminyltransferase 4
  2. UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferase 4
  3. Polypeptide GalNAc transferase 4
  4. GalNAc-T4
  5. pp-GaNTase 4
Enzyme 33 Gene Name GALNT4
Enzyme 33 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 4
MAVRWTWAGKSCLLLAFLTVAYIFVELLVSTFHASAGAGRARELGSRRLSGLQKNTEDLS
RPLYKKPPADSRALGEWGKASKLQLNEDELKQQEELIERYAINIYLSDRISLHRHIEDKR
MYECKSQKFNYRTLPTTSVIIAFYNEAWSTLLRTIHSVLETSPAVLLKEIILVDDLSDRV
YLKTQLETYISNLDRVRLIRTNKREGLVRARLIGATFATGDVLTFLDCHCECNSGWLEPL
LERIGRDETAVVCPVIDTIDWNTFEFYMQIGEPMIGGFDWRLTFQWHSVPKQERDRRISR
IDPIRSPTMAGGLFAVSKKYFQYLGTYDTGMEVWGGENLELSFRVWQCGGKLEIHPCSHV
GHVFPKRAPYARPNFLQNTARAAEVWMDEYKEHFYNRNPPARKEAYGDISERKLLRERLR
CKSFDWYLKNVFPNLHVPEDRPGWHGAIRSRGISSECLDYNSPDNNPTGANLSLFGCHGQ
GGNQFFEYTSNKEIRFNSVTELCAEVPEQKNYVGMQNCPKDGFPVPANIIWHFKEDGTIF
HPHSGLCLSAYRTPEGRPDVQMRTCDALDKNQIWSFEK
Enzyme 33 Number of Residues 578
Enzyme 33 Molecular Weight 66608
Enzyme 33 Theoretical pI 7.80
Enzyme 33 GO Classification Not Available
Enzyme 33 General Function Not Available
Enzyme 33 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has a highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG
Enzyme 33 Pathways
Enzyme 33 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • 1-23
Enzyme 33 Transmembrane Regions Not Available
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 1934912 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q8N4A0 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name GALT4_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 Gene Sequence >1737 bp
ATGGCGGTGAGGTGGACTTGGGCAGGCAAGACCTGCCTGCTGCTGGCGTTTTTAACAGTG
GCCTATATCTTCGTGGAGCTCTTGGTCTCTACTTTTCATGCCTCCGCAGGAGCCGGCCGT
GCCAGGGAGCTGGGGTCAAGAAGGCTCTCAGACCTCCAGAAAAATACGGAGGATTTGTCT
CGACCGCTTTATAAGAAGCCCCCTGCAGATTCCCGTGCACTTGGGGAGTGGGGGAAAGCC
AGCAAACTCCAGCTCAACGAGGATGAACTGAAGCAGCAAGAAGAACTCATTGAGAGATAC
GCCATCAATATTTACCTCAGTGACAGGATTTCCCTGCATCGACACATAGAGGATAAAAGA
ATGTATGAGTGTAAGTCCCAGAAGTTCAACTATAGGACACTTCCTACCACCTCTGTTATC
ATTGCTTTCTATAACGAAGCCTGGTCGACTTTGCTCCGTACCATTCACAGTGTTTTAGAA
ACTTCTCCTGCAGTTCTTTTGAAAGAGATCATCTTGGTGGATGACTTGAGTGACAGAGTT
TATTTGAAGACACAACTTGAAACTTACATCAGCAATCTTGATAGAGTACGCTTGATTAGG
ACCAATAAGCGAGAGGGGCTGGTTAGGGCCCGTCTGATTGGGGCCACTTTCGCCACTGGG
GACGTCCTCACTTTCCTGTATTGTCACTGTGAGTGTAATTCCGGTTGGCTGGAACCGCTT
TTGGAAAGGATTGGGAGATATGAAACAGCAGTTGTGTGTCCTGTTATAGACACAATTGAT
TGGAATACTTTTGAATTCTATATGCAGATAGGGGAGCCCATGATTGGTGGGTTTGACTGG
CGTTTAACATTTCAGTGGCATTCTGTCCCCAAACAGGAAAGGGACAGGCGGATATCAAGA
ATTGACCCCATCAGATCACCTACCATGGCTGGAGGACTGTTTGCTGTCAGCAAGAAATAT
TTTCAGTACCTTGGAACGTATGACACAGGAATGGAAGTGTGGGGAGGTGAAAACCTTGAG
CTGTCTTTTAGGGTGTGGCAGTGTGGTGGCAAATTGGAGATCCACCCGTGTTCCCACGTG
GGCCATGTGTTCCCCAAGCGGGCACCATATGCTCGCCCCAATTTCCTACAGAATACTGCT
CGGGCAGCAGAAGTTTGGATGGATGAATACAAAGAGCACTTCTACAATAGAAACCCTCCA
GCAAGAAAAGAAGCTTATGGTGATATTTCTGAAAGAAAATTACTACGAGAGCGGTTGAGA
TGCAAGAGCTTTGACTGGTATTTGAAAAACGTTTTTCCTAATTTACATGTTCCAGAGGAT
AGACCAGGCTGGCATGGGGCTATTCGCAGTAGAGGGATCTCGTCTGAATGTTTAGATTAT
AATTCTCCTGACAACAACCCCACAGGTGCTAACCTTTCACTGTTTGGATGCCATGGTCAA
GGAGGCAATCAATTCTTTGAATATACTTCAAACAAAGAAATAAGGTTTAATTCTGTGACA
GAGTTATGTGCAGAGGTACCTGAGCAAAAAAATTATGTGGGAATGCAAAATTGTCCCAAA
GATGGGTTCCCTGTACCAGCAAACATTATTTGGCATTTTAAAGAAGATGGAACTATTTTT
CACCCACACTCAGGACTGTGTCTTAGTGCTTATCGGACACCGGAGGGCCGACCTGATGTA
CAAATGAGAACTTGTGATGCTCTAGATAAAAATCAAATTTGGAGTTTTGAGAAATAG
Enzyme 33 GenBank Gene ID Y08564 Link Image
Enzyme 33 GeneCard ID GALNT4 Link Image
Enzyme 33 GenAtlas ID GALNT4 Link Image
Enzyme 33 HGNC ID HGNC:4126 Link Image
Enzyme 33 Chromosome Location 12
Enzyme 33 Locus 12q21.3-q22
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 General References
  1. Bennett EP, Hassan H, Mandel U, Mirgorodskaya E, Roepstorff P, Burchell J, Taylor-Papadimitriou J, Hollingsworth MA, Merkx G, van Kessel AG, Eiberg H, Steffensen R, Clausen H: Cloning of a human UDP-N-acetyl-alpha-D-Galactosamine:polypeptide N-acetylgalactosaminyltransferase that complements other GalNAc-transferases in complete O-glycosylation of the MUC1 tandem repeat. J Biol Chem. 1998 Nov 13;273(46):30472-81. [PubMed Link Image]
Enzyme 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 6283
Enzyme 34 Name Polypeptide N-acetylgalactosaminyltransferase 3
Enzyme 34 Synonyms
  1. Protein-UDP acetylgalactosaminyltransferase 3
  2. UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
  3. Polypeptide GalNAc transferase 3
  4. GalNAc-T3
  5. pp-GaNTase 3
Enzyme 34 Gene Name GALNT3
Enzyme 34 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 3
MAHLKRLVKLHIKRHYHKKFWKLGAVIFFFIIVLVLMQREVSVQYSKEESRMERNMKNKN
KMLDLMLEAVNNIKDAMPKMQIGAPVRQNIDAGERPCLQGYYTAAELKPVLDRPPQDSNA
PGASGKAFKTTNLSVEEQKEKERGEAKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKR
CPPLPTTSVIIVFHNEAWSTLLRTVHSVLYSSPAILLKEIILVDDASVDEYLHDKLDEYV
KQFSIVKIVRQRERKGLITARLLGATVATAETLTFLDAHCECFYGWLEPLLARIAENYTA
VVSPDIASIDLNTFEFNKPSPYGSNHNRGNFDWSLSFGWESLPDHEKQRRKDETYPIKTP
TFAGGLFSISKEYFEYIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSK
SPHSFPKGTQVIARNQVRLAEVWMDEYKEIFYRRNTDAAKIVKQKAFGDLSKRFEIKHRL
RCKNFTWYLNNIYPEVYVPDLNPVISGYIKSVGQPLCLDVGENNQGGKPLIMYTCHGLGG
NQYFEYSAQHEIRHNIQKELCLHAAQGLVQLKACTYKGHKTVVTGEQIWEIQKDQLLYNP
FLKMCLSANGEHPSLVSCNPSDPLQKWILSQND
Enzyme 34 Number of Residues 633
Enzyme 34 Molecular Weight 72639
Enzyme 34 Theoretical pI 8.17
Enzyme 34 GO Classification Not Available
Enzyme 34 General Function Cell wall/membrane/envelope biogenesis
Enzyme 34 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably glycosylates fibronectin in vivo. Plays a central role in phosphate homeostasis
Enzyme 34 Pathways
Enzyme 34 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • 1-36
Enzyme 34 Transmembrane Regions Not Available
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein 1617312 Link Image
Enzyme 34 UniProtKB/Swiss-Prot ID Q14435 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name GALT3_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1902 bp
ATGGCTCACCTAAAGCGACTAGTAAAATTACACATTAAAAGACATTACCATAAAAAGTTC
TGGAAGCTTGGTGCAGTAATTTTTTTCTTTATAATAGTTTTGGTTTTAATGCAAAGAGAA
GTAAGTGTTCAATATTCCAAAGAGGAATCAAGGATGGAAAGGAACATGAAAAACAAAAAC
AAGATGTTGGATTTAATGCTAGAAGCTGTAAACAATATTAAGGATGCCATGCCAAAAATG
CAAATAGGAGCACCTGTCAGGCAAAACATTGATGCTGGTGAGAGACCTTGTTTGCAAGGA
TATTATACAGCAGCAGAATTGAAGCCTGTCCTTGACCGTCCACCTCAGGATTCAAATGCA
CCTGGTGCTTCTGGTAAAGCATTCAAGACAACCAATTTAAGTGTTGAAGAGCAAAAGGAA
AAGGAACGTGGGGAAGCTAAACACTGCTTTAATGCTTTCGCAAGTGACAGGATTTCTTTG
CACCGAGATCTTGGACCAGACACTCGACCTCCTGAATGTATTGAACAAAAATTTAAGCGC
TGCCCTCCCCTGCCCACCACCAGTGTCATAATAGTTTTTCATAATGAAGCGTGGTCCACG
TTGCTTAGAACTGTCCACAGTGTGCTCTATTCTTCACCTGCAATACTGCTGAAGGAAATC
ATTTTGGTGGATGATGCTAGTGTAGATGAGTACTTACATGATAAACTAGATGAATATGTA
AAACAATTTTCTATAGTAAAAATAGTCAGACAAAGAGAAAGAAAAGGTCTGATCACTGCT
CGGTTGCTAGGAGCAACAGTCGCAACAGCTGAAACGCTCACATTTTTAGATGCTCACTGT
GAGTGTTTCTATGGTTGGCTAGAACCTCTGTTGGCCAGAATAGCTGAGAACTACACGGCT
GTCGTAAGTCCAGATATTGCATCCATAGATCTGAACACGTTTGAATTCAACAAACCTTCT
CCTTATGGAAGTAACCATAACCGTGGAAATTTTGACTGGAGTCTTTCATTTGGCTGGGAG
TCGCTTCCTGATCATGAGAAGCAAAGAAGGAAAGATGAAACCTACCCAATTAAAACACCC
ACTTTTGCAGGAGGACTTTTTTCCATATCAAAAGAATATTTTGAGTATATTGGAAGCTAT
GATGAAGAAATGGAAATCTGGGGAGGTGAAAATATAGAAATGTCTTTCAGAGTATGGCAA
TGTGGTGGGCAGTTGGAGATTATGCCTTGCTCTGTTGTTGGACATGTTTTTCGCAGCAAA
AGCCCTCATAGCTTTCCAAAAGGCACTCAGGTGATTGCTAGAAACCAAGTTCGCCTTGCA
GAAGTCTGGATGGATGAATACAAGGAAATATTTTATAGGAGAAATACAGATGCAGCAAAA
ATTGTTAAACAAAAAGCATTTGGTGATCTTTCAAAAAGATTTGAAATAAAACACCGTCTT
CGGTGTAAAAATTTTACATGGTATCTGAACAACATTTATCCAGAGGTGTATGTGCCAGAC
CTTAATCCTGTTATATCTGGATACATTAAAAGCGTTGGTCAGCCTCTATGTCTGGATGTT
GGAGAAAACAATCAAGGAGGCAAACCATTAATTATGTATACATGTCATGGACTTGGGGGA
AACCAGTACTTTGAATACTCTGCTCAACATGAAATTCGGCACAACATCCAGAAGGAATTA
TGTCTTCATGCTGCTCAAGGTCTCGTTCAGCTGAAGGCATGTACCTACAAAGGTCACAAG
ACAGTTGTCACTGGAGAGCAGATATGGGAGATCCAGAAGGATCAACTTCTATACAATCCA
TTCTTAAAAATGTGCCTTTCAGCAAATGGAGAGCATCCAAGTTTAGTGTCATGCAACCCA
TCAGATCCACTCCAAAAATGGATACTTAGCCAAAATGATTAA
Enzyme 34 GenBank Gene ID X92689 Link Image
Enzyme 34 GeneCard ID GALNT3 Link Image
Enzyme 34 GenAtlas ID GALNT3 Link Image
Enzyme 34 HGNC ID HGNC:4125 Link Image
Enzyme 34 Chromosome Location 2
Enzyme 34 Locus 2q24-q31
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Bennett EP, Hassan H, Clausen H: cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3. J Biol Chem. 1996 Jul 19;271(29):17006-12. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 6285
Enzyme 35 Name Polypeptide N-acetylgalactosaminyltransferase-like protein 2
Enzyme 35 Synonyms
  1. Protein-UDP acetylgalactosaminyltransferase-like protein 2
  2. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase- like protein 2
  3. Polypeptide GalNAc transferase-like protein 2
  4. GalNAc-T-like protein 2
  5. pp-GaNTase-like protein 2
Enzyme 35 Gene Name GALNTL2
Enzyme 35 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase-like protein 2
MLLRKRYRHRPCRLQFLLLLLMLGCVLMMVAMLHPPHHTLHQTVTAQASKHSPEARYRLD
FGESQDWVLEAEDEGEEYSPLEGLPPFISLREDQLLVAVALPQARRNQSQGRRGGSYRLI
KQPRRQDKEAPKRDWGADEDGEVSEEEELTPFSLDPRGLQEALSARIPLQRALPEVRHPL
CLQQHPQDSLPTASVILCFHDEAWSTLLRTVHSILDTVPRAFLKEIILVDDLSQQGQLKS
ALSEYVARLEGVKLLRSNKRLGAIRARMLGATRATGDVLVFMDAHCECHPGWLEPLLSRI
AGDRSRVVSPVIDVIDWKTFQYYPSKDLQRGVLDWKLDFHWEPLPEHVRKALQSPISPIR
SPVVPGEVVAMDRHYFQNTGAYDSLMSLRGGENLELSFKAWLCGGSVEILPCSRVGHIYQ
NQDSHSPLDQEATLRNRVRIAETWLGSFKETFYKHSPEAFSLSKAEKPDCMERLQLQRRL
GCRTFHWFLANVYPELYPSEPRPSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSR
QQQYLQHTSRKEIHFGSPQHLCFAVRQEQVILQNCTEEGLAIHQQHWDFQENGMIVHILS
GKCMEAVVQENNKDLYLRPCDGKARQQWRFDQINAVDER
Enzyme 35 Number of Residues 639
Enzyme 35 Molecular Weight 73064
Enzyme 35 Theoretical pI 6.90
Enzyme 35 GO Classification Not Available
Enzyme 35 General Function Not Available
Enzyme 35 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, it is able to transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues incorporation with other GALNT proteins. Prefers Muc1a as substrate
Enzyme 35 Pathways
Enzyme 35 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • 1-28
Enzyme 35 Transmembrane Regions Not Available
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 16756125 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID Q8N3T1 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name GLTL2_HUMAN Link Image
Enzyme 35 PDB ID Not Available
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1920 bp
ATGCTCCTAAGGAAGCGATACAGGCACAGACCATGCAGACTCCAGTTCCTCCTGCTGCTC
CTGATGCTGGGATGCGTCCTGATGATGGTGGCGATGTTGCACCCTCCCCACCACACCCTG
CACCAGACTGTCACAGCCCAAGCCAGCAAGCACAGCCCTGAAGCCAGGTACCGCCTGGAC
TTTGGGGAATCCCAGGATTGGGTACTGGAAGCTGAGGATGAGGGTGAAGAGTACAGCCCT
CTGGAGGGCCTGCCACCCTTTATCTCACTGCGGGAGGATCAGCTGCTGGTGGCCGTGGCC
TTACCCCAGGCCAGAAGGAACCAGAGCCAGGGCAGGAGAGGTGGGAGCTACCGCCTCATC
AAGCAGCCAAGGAGGCAGGATAAGGAAGCCCCAAAGAGGGACTGGGGGGCTGATGAGGAC
GGGGAGGTGTCTGAAGAAGAGGAGTTGACCCCGTTCAGCCTGGACCCACGTGGCCTCCAG
GAGGCACTCAGTGCCCGCATCCCCCTCCAGAGGGCTCTGCCCGAGGTGCGGCACCCACTG
TGTCTGCAGCAGCACCCTCAGGACAGCCTGCCCACAGCCAGCGTCATCCTCTGTTTCCAT
GATGAGGCCTGGTCCACTCTCCTGCGGACTGTACACAGCATCCTCGACACAGTGCCCAGG
GCCTTCCTGAAGGAGATCATCCTCGTGGACGACCTCAGCCAGCAAGGACAACTCAAGTCT
GCTCTCAGCGAATATGTGGCCAGGCTGGAGGGGGTGAAGTTACTCAGGAGCAACAAGAGG
CTGGGTGCCATCAGGGCCCGGATGCTGGGGGCCACCAGAGCCACCGGGGATGTGCTCGTC
TTCATGGATGCCCACTGCGAGTGCCACCCAGGCTGGCTGGAGCCCCTCCTCAGCAGAATA
GCTGGTGACAGGAGCCGAGTGGTATCTCCGGTGATAGATGTGATTGACTGGAAGACTTTC
CAGTATTACCCCTCAAAGGACCTGCAGCGTGGGGTGTTGGACTGGAAGCTGGATTTCCAC
TGGGAACCTTTGCCAGAGCATGTGAGGAAGGCCCTCCAGTCCCCCATAAGCCCCATCAGG
AGCCCTGTGGTGCCCGGAGAGGTGGTGGCCATGGACAGACATTACTTCCAAAACACTGGA
GCGTATGACTCTCTTATGTCGCTGCGAGGTGGTGAAAACCTCGAACTGTCTTTCAAGGCC
TGGCTCTGTGGTGGCTCTGTTGAAATCCTTCCCTGCTCTCGGGTAGGACACATCTACCAA
AATCAGGATTCCCATTCCCCCCTCGACCAGGAGGCCACCCTGAGGAACAGGGTTCGCATT
GCTGAGACCTGGCTGGGGTCATTCAAAGAAACCTTCTACAAGCATAGCCCAGAGGCCTTC
TCCTTGAGCAAGGCTGAGAAGCCAGACTGCATGGAACGCTTGCAGCTGCAAAGGAGACTG
GGTTGTCGGACATTCCACTGGTTTCTGGCTAATGTCTACCCTGAGCTGTACCCATCTGAA
CCCAGGCCCAGTTTCTCTGGAAAGCTCCACAACACTGGACTTGGGCTCTGTGCAGACTGC
CAGGCAGAAGGGGACATCCTGGGCTGTCCCATGGTGTTGGCTCCTTGCAGTGACAGCCGG
CAGCAACAGTACCTGCAGCACACCAGCAGGAAGGAGATTCACTTTGGCAGCCCACAGCAC
CTGTGCTTTGCTGTCAGGCAGGAGCAGGTGATTCTTCAGAACTGCACGGAGGAAGGCCTG
GCCATCCACCAGCAGCACTGGGACTTCCAGGAGAATGGGATGATTGTCCACATTCTTTCT
GGGAAATGCATGGAAGCTGTGGTGCAAGAAAACAATAAAGATTTGTACCTGCGTCCGTGT
GATGGAAAAGCCCGCCAGCAGTGGCGTTTTGACCAGATCAATGCTGTGGATGAACGATGA
Enzyme 35 GenBank Gene ID AY035399 Link Image
Enzyme 35 GeneCard ID GALNTL2 Link Image
Enzyme 35 GenAtlas ID GALNTL2 Link Image
Enzyme 35 HGNC ID HGNC:21531 Link Image
Enzyme 35 Chromosome Location 3
Enzyme 35 Locus 3p24.3
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 General References
  1. Kumar S, Connor JR, Dodds RA, Halsey W, Van Horn M, Mao J, Sathe G, Mui P, Agarwal P, Badger AM, Lee JC, Gowen M, Lark MW: Identification and initial characterization of 5000 expressed sequenced tags (ESTs) each from adult human normal and osteoarthritic cartilage cDNA libraries. Osteoarthritis Cartilage. 2001 Oct;9(7):641-53. [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 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 6287
Enzyme 36 Name Polypeptide N-acetylgalactosaminyltransferase 10
Enzyme 36 Synonyms
  1. Protein-UDP acetylgalactosaminyltransferase 10
  2. UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
  3. Polypeptide GalNAc transferase 10
  4. GalNAc-T10
  5. pp-GaNTase 10
Enzyme 36 Gene Name GALNT10
Enzyme 36 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 10
MRRKEKRLLQAVALVLAALVLLPNVGLWALYRERQPDGTPGGSGAAVAPAAGQGSHSRQK
KTFFLGDGQKLKDWHDKEAIRRDAQRVGNGEQGRPYPMTDAERVDQAYRENGFNIYVSDK
ISLNRSLPDIRHPNCNSKRYLETLPNTSIIIPFHNEGWSSLLRTVHSVLNRSPPELVAEI
VLVDDFSDREHLKKPLEDYMALFPSVRILRTKKREGLIRTRMLGASVATGDVITFLDSHC
EANVNWLPPLLDRIARNRKTIVCPMIDVIDHDDFRYETQAGDAMRGAFDWEMYYKRIPIP
PELQKADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGRM
EDIPCSRVGHIYRKYVPYKVPAGVSLARNLKRVAEVWMDEYAEYIYQRRPEYRHLSAGDV
AVQKKLRSSLNCKSFKWFMTKIAWDLPKFYPPVEPPAAAWGEIRNVGTGLCADTKHGALG
SPLRLEGCVRGRGEAAWNNMQVFTFTWREDIRPGDPQHTKKFCFDAISHTSPVTLYDCHS
MKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRIFMNTCNPSSLTQQWLFEHTNSTVLEKF
NRN
Enzyme 36 Number of Residues 603
Enzyme 36 Molecular Weight 68992
Enzyme 36 Theoretical pI 8.74
Enzyme 36 GO Classification Not Available
Enzyme 36 General Function Not Available
Enzyme 36 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward Muc5Ac and EA2 peptide substrates
Enzyme 36 Pathways
Enzyme 36 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • 1-29
Enzyme 36 Transmembrane Regions Not Available
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 28268676 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q86SR1 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name GLT10_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >1812 bp
ATGAGGCGGAAGGAGAAGCGGCTCCTGCAGGCGGTGGCGCTGGTGCTGGCGGCCCTGGTC
CTCCTGCCCAACGTGGGGCTTTGGGCGCTGTACCGCGAGCGGCAGCCCGACGGCACCCCT
GGGGGATCGGGGGCGGCGGTGGCGCCGGCGGCGGGACAGGGCTCACACAGTCGACAAAAG
AAAACGTTTTTCTTGGGAGATGGGCAGAAGCTGAAGGACTGGCATGACAAGGAGGCCATC
CGGAGGGACGCTCAGCGCGTAGGAAATGGAGAACAAGGAAGACCTTACCCCATGACCGAT
GCTGAGAGAGTGGATCAGGCATACCGAGAAAATGGATTTAACATCTACGTCAGTGATAAA
ATCTCCTTGAATCGCTCTCTCCCAGATATCCGGCACCCAAACTGCAACAGCAAGCGCTAC
CTGGAGACACTTCCCAACACAAGCATCATCATCCCCTTCCACAACGAGGGCTGGTCCTCC
CTCCTCCGCACCGTCCACAGTGTGCTCAATCGCTCGCCTCCAGAGCTGGTCGCCGAGATT
GTACTGGTCGACGACTTCAGTGATCGAGAGCACCTGAAGAAGCCTCTTGAAGACTACATG
GCCCTTTTCCCCAGTGTGAGGATTCTTCGAACCAAGAAACGGGAAGGGCTGATAAGGACC
CGAATGCTGGGGGCCTCAGTGGCAACTGGGGATGTCATCACATTCTTGGATTCACACTGT
GAAGCCAATGTCAACTGGCTTCCCCCCTTGCTTGACCGCATTGCTCGGAACCGCAAGACC
ATTGTGTGCCCGATGATTGATGTAATTGACCATGACGACTTTCGGTACGAGACACAGGCA
GGGGATGCCATGCGGGGAGCCTTTGACTGGGAGATGTACTACAAGCGGATCCCGATCCCT
CCAGAACTGCAGAAAGCTGACCCCAGCGACCCATTTGAGTCTCCCGTGATGGCCGGTGGA
CTGTTCGCCGTGGATCGGAAGTGGTTCTGGGAACTCGGCGGGTATGACCCAGGCTTGGAG
ATCTGGGGAGGGGAGCAGTATGAAATCTCCTTCAAGGTGTGGATGTGTGGGGGCCGCATG
GAGGACATCCCCTGCTCCAGGGTGGGCCATATCTACAGGAAGTATGTGCCCTACAAGGTC
CCGGCCGGAGTCAGCCTGGCCCGGAACCTTAAGCGGGTGGCCGAAGTGTGGATGGATGAG
TACGCAGAGTACATTTACCAGCGCCGGCCTGAATACCGCCACCTCTCCGCTGGGGATGTC
GCAGTCCAGAAAAAGCTCCGCAGCTCCCTTAACTGCAAGAGTTTCAAGTGGTTTATGACG
AAGATAGCCTGGGACCTGCCCAAATTCTACCCACCCGTGGAGCCCCCGGCTGCAGCTTGG
GGGGAGATCCGAAATGTGGGCACAGGGCTGTGTGCAGACACAAAGCACGGGGCCTTGGGC
TCCCCACTAAGGCTAGAGGGCTGCGTCCGAGGCCGTGGGGAGGCTGCCTGGAACAACATG
CAGGTATTCACCTTCACCTGGAGAGAGGACATCCGGCCTGGAGACCCCCAGTACACCAAG
AAGTTCTGCTTTGATGCCATTTCCCACACCAGCCCTGTCACGCTGTACGACTGCCACAGC
ATGAAGGGCAACCAGCTGTGGAAATACCGCAAAGACAAGACCCTGTACCACCCTGTCAGT
GGCAGCTGCATGGACTGCAGTGAAAGTGACCATAGGATCTTCATGAACACCTGCAACCCA
TCCTCTCTCACCCAGCAATGGCTGTTTGAACACACCAACTCAACAGTCTTGGAAAAATTC
AATAGGAACTGA
Enzyme 36 GenBank Gene ID AB078145 Link Image
Enzyme 36 GeneCard ID GALNT10 Link Image
Enzyme 36 GenAtlas ID GALNT10 Link Image
Enzyme 36 HGNC ID HGNC:19873 Link Image
Enzyme 36 Chromosome Location 5
Enzyme 36 Locus 5q33.2
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 General References
  1. Cheng L, Tachibana K, Zhang Y, Guo J, Kahori Tachibana K, Kameyama A, Wang H, Hiruma T, Iwasaki H, Togayachi A, Kudo T, Narimatsu H: Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T10. FEBS Lett. 2002 Nov 6;531(2):115-21. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 6290
Enzyme 37 Name Putative polypeptide N-acetylgalactosaminyltransferase-like protein 4
Enzyme 37 Synonyms
  1. Protein-UDP acetylgalactosaminyltransferase-like protein 4
  2. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase- like protein 4
  3. Polypeptide GalNAc transferase-like protein 4
  4. GalNAc-T-like protein 4
  5. pp-GaNTase-like protein 4
Enzyme 37 Gene Name GALNTL4
Enzyme 37 Protein Sequence >Putative polypeptide N-acetylgalactosaminyltransferase-like protein 4
MVCTRKTKTLVSTCVILSGMTNIICLLYVGWVTNYIASVYVRGQEPAPDKKLEEDKGDTL
KIIERLDHLENVIKQHIQEAPAKPEEAEAEPFTDSSLFAHWGQELSPEGRRVALKQFQYY
GYNAYLSDRLPLDRPLPDLRPSGCRNLSFPDSLPEVSIVFIFVNEALSVLLRSIHSAMER
TPPHLLKEIILVDDNSSNEELKEKLTEYVDKVNSQKPGFIKVVRHSKQEGLIRSRVSGWR
AATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFEIEEYPLAAQGF
DWELWCRYLNPPKAWWKLENSTAPIRSPALIGCFIVDRQYFQEIGLLDEGMEVYGGENVE
LGIRVWQCGGSVEVLPCSRIAHIERAHKPYTEDLTAHVRRNALRVAEVWMDEFKSHVYMA
WNIPQEDSGIDIGDITARKALRKQLQCKTFRWYLVSVYPEMRMYSDIIAYGVLQNSLKTD
LCLDQGPDTENVPIMYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRCLVDVNSRPRL
IECSYAKAKRMKLHWQFSQGGPIQNRKSKRCLELQENSDLEFGFQLVLQKCSGQHWSITN
VLRSLAS
Enzyme 37 Number of Residues 607
Enzyme 37 Molecular Weight 69561
Enzyme 37 Theoretical pI 6.46
Enzyme 37 GO Classification Not Available
Enzyme 37 General Function Not Available
Enzyme 37 Specific Function May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor
Enzyme 37 Pathways
Enzyme 37 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • 1-37
Enzyme 37 Transmembrane Regions Not Available
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 4406698 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q6P9A2 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name GLTL4_HUMAN Link Image
Enzyme 37 PDB ID Not Available
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >441 bp
CACGGCGGCTACACCGGCAGCGGACCGGGCTTTGGAGAACCTCGGGACTCAGGTGCTGAG
GTGCCCAGCGGCTCCGGACGTGCTACGGGGTGCGAGCGCGGGGGAGTTCGGGGCGCACGA
CAAGGAAGGGCCCCCGGGAGCTCTATATGGAGGAAGGAGCCCAGAATGGTGTGCACCAGG
AAGACCAAAACTTTGGTGTCCACTTGCGTGATCCTGAGCGGCATGACTAACATCATCTGC
CTGCTCTACGTGGGCTGGGTCACCAACTACATCGCCAGCGTGTATGTGCGGGGGCAGGAG
CCGGCGCCCGACAAGAAGCTGGAGGAAGACAAAGGGGACACTCTGAAGATTATTGAGCGG
CTGGACCACCTGGAGAATGTCATCAAGCAGCACATTCAAGGCTATAGGAGAAATTTCTCC
CTTCTGAATGTGTCCAACTAA
Enzyme 37 GenBank Gene ID AF131852 Link Image
Enzyme 37 GeneCard ID GALNTL4 Link Image
Enzyme 37 GenAtlas ID GALNTL4 Link Image
Enzyme 37 HGNC ID HGNC:30488 Link Image
Enzyme 37 Chromosome Location 11
Enzyme 37 Locus 11p15.3
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 General References Not Available
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 6292
Enzyme 38 Name Polypeptide N-acetylgalactosaminyltransferase 6
Enzyme 38 Synonyms
  1. Protein-UDP acetylgalactosaminyltransferase 6
  2. UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferase 6
  3. Polypeptide GalNAc transferase 6
  4. GalNAc-T6
  5. pp-GaNTase 6
Enzyme 38 Gene Name GALNT6
Enzyme 38 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 6
MRLLRRRHMPLRLAMVGCAFVLFLFLLHRDVSSREEATEKPWLKSLVSRKDHVLDLMLEA
MNNLRDSMPKLQIRAPEAQQTLFSINQSCLPGFYTPAELKPFWERPPQDPNAPGADGKAF
QKSKWTPLETQEKEEGYKKHCFNAFASDRISLQRSLGPDTRPPECVDQKFRRCPPLATTS
VIIVFHNEAWSTLLRTVYSVLHTTPAILLKEIILVDDASTEEHLKEKLEQYVKQLQVVRV
VRQEERKGLITARLLGASVAQAEVLTFLDAHCECFHGWLEPLLARIAEDKTVVVSPDIVT
IDLNTFEFAKPVQRGRVHSRGNFDWSLTFGWETLPPHEKQRRKDETYPIKSPTFAGGLFS
ISKSYFEHIGTYDNQMEIWGGENVEMSFRVWQCGGQLEIIPCSVVGHVFRTKSPHTFPKG
TSVIARNQVRLAEVWMDSYKKIFYRRNLQAAKMAQEKSFGDISERLQLREQLHCHNFSWY
LHNVYPEMFVPDLTPTFYGAIKNLGTNQCLDVGENNRGGKPLIMYSCHGLGGNQYFEYTT
QRDLRHNIAKQLCLHVSKGALGLGSCHFTGKNSQVPKDEEWELAQDQLIRNSGSGTCLTS
QDKKPAMAPCNPSDPHQLWLFV
Enzyme 38 Number of Residues 622
Enzyme 38 Molecular Weight 71159
Enzyme 38 Theoretical pI 8.25
Enzyme 38 GO Classification Not Available
Enzyme 38 General Function Cell wall/membrane/envelope biogenesis
Enzyme 38 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. May participate in synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin peptides
Enzyme 38 Pathways
Enzyme 38 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • 1-33
Enzyme 38 Transmembrane Regions Not Available
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 5834600 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID Q8NCL4 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name GALT6_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 Gene Sequence >1869 bp
ATGAGGCTCCTCCGCAGACGCCACATGCCCCTGCGCCTGGCCATGGTGGGCTGCGCCTTT
GTGCTCTTCCTCTTCCTCCTGCATAGGGATGTGAGCAGCAGAGAGGAGGCCACAGAGAAG
CCGTGGCTGAAGTCCCTGGTGAGCCGGAAGGATCACGTCCTGGACCTCATGCTGGAGGCC
ATGAACAACCTTAGAGATTCAATGCCCAAGCTCCAAATCAGGGCTCCAGAAGCCCAGCAG
ACTCTGTTCTCCATAAACCAGTCCTGCCTCCCTGGGTTCTATACCCCAGCTGAACTGAAG
CCCTTCTGGGAACGGCCACCACAGGACCCCAATGCCCCTGGGGCAGATGGAAAAGCATTT
CAGAAGAGCAAGTGGACCCCCCTGGAGACCCAGGAAAAGGAAGAAGGCTATAAGAAGCAC
TGTTTCAATGCCTTTGCCAGCGACCGGATCTCCCTGCAGAGGTCCCTGGGGCCAGACACC
CGACCACCTGAGTGTGTGGACCAGAAGTTCCGGCGCTGCCCCCCACTGGCCACCACCAGC
GTGATCATTGTGTTCCACAACGAAGCCTGGTCCACACTGCTGCGAACAGTGTACAGCGTC
CTACACACCACCCCTGCCATCTTGCTCAAGGAGATCATACTGGTGGATGATGCCAGCACA
GAGGAGCACCTAAAGGAGAAGCTGGAGCAGTACGTGAAGCAGCTGCAGGTGGTGAGGGTG
GTGCGGCAGGAGGAGCGGAAGGGGTTGATCACCGCCCGGCTGCTGGGGGCCAGCGTGGCA
CAGGCGGAGGTGCTCACGTTCCTGGATGCCCACTGTGAGTGCTTCCACGGCTGGCTGGAG
CCCCTCCTGGCTCGAATCGCTGAGGACAAGACAGTGGTGGTGAGCCCAGACATCGTCACC
ATCGACCTTAATACTTTTGAGTTCGCCAAGCCCGTCCAGAGGGGCAGAGTCCATAGCCGA
GGCAACTTTGACTGGAGCCTGACCTTCGGCTGGGAAACACTTCCTCCACATGAGAAGCAG
AGGCGCAAGGATGAAACATACCCCATCAAATCCCCGACGTTTGCTGGTGGCCTCTTCTCC
ATCCCCAAGTCCTACTTTGAGCACATCGGTACCTATGATAATCAGATGGAGATCTGGGGA
GGGGAGAACGTGGAAATGTCCTTCCGGGTGTGGCAGTGTGGGGGCCAGCTGGAGATCATC
CCCTGCTCTGTCGTAGGCCATGTGTTCCGGACCAAGAGCCCCCACACCTTCCCCAAGGGC
ACTAGTGTCATTGCTCGCAATCAAGTGCGCCTGGCAGAGGTCTGGATGGACAGCTACAAG
AAGATTTTCTATAGGAGAAATCTGCAGGCAGCAAAGATGGCCCAAGAGAAATCCTTCGGT
GACATTTCGGAACGACTGCAGCTGAGGGAACAACTGCACTGTCACAACTTTTCCTGGTAC
CTGCACAATGTCTACCCAGAGATGTTTGTTCCTGACCTGACGCCCACCTTCTATGGTGCC
ATCAAGAACCTCGGCACCAACCAATGCCTGGATGTGGGTGAGAACAACCGCGGGGGGAAG
CCCCTCATCATGTACTCCTGCCACGGCCTTGGCGGCAACCAGTACTTTGAGTACACAACT
CAGAGGGACCTTCGCCACAACATCGCAAAGCAGCTGTGTCTACATGTCAGCAAGGGTGCT
CTGGGCCTTGGGAGCTGTCACTTCACTGGCAAGAATAGCCAGGTCCCCAAGGACGAGGAA
TGGGAATTGGCCCAGGATCAGCTCATCAGGAACTCAGGATCTGGTACCTGCCTGACATCC
CAGGACAAAAAGCCAGCCATGGCCCCCTGCAATCCCAGTGACCCCCATCAGTTGTGGCTC
TTTGTCTAG
Enzyme 38 GenBank Gene ID Y08565 Link Image
Enzyme 38 GeneCard ID GALNT6 Link Image
Enzyme 38 GenAtlas ID GALNT6 Link Image
Enzyme 38 HGNC ID HGNC:4128 Link Image
Enzyme 38 Chromosome Location 12
Enzyme 38 Locus 12q13
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 General References
  1. Bennett EP, Hassan H, Mandel U, Hollingsworth MA, Akisawa N, Ikematsu Y, Merkx G, van Kessel AG, Olofsson S, Clausen H: Cloning and characterization of a close homologue of human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy. J Biol Chem. 1999 Sep 3;274(36):25362-70. [PubMed Link Image]
Enzyme 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 6293
Enzyme 39 Name Polypeptide N-acetylgalactosaminyltransferase 14
Enzyme 39 Synonyms
  1. Protein-UDP acetylgalactosaminyltransferase 14
  2. UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferase 14
  3. Polypeptide GalNAc transferase 14
  4. GalNAc-T14
  5. pp-GaNTase 14
Enzyme 39 Gene Name GALNT14
Enzyme 39 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 14
MRRLTRRLVLPVFGVLWITVLLFFWVTKRKLEVPTGPEVQTPKPSDADWDDLWDQFDERR
YLNAKKWRVGDDPYKLYAFNQRESERISSNRAIPDTRHLRCTLLVYCTDLPPTSIIITFH
NEARSTLLRTIRSVLNRTPTHLIREIILVDDFSNDPDDCKQLIKLPKVKCLRNNERQGLV
RSRIRGADIAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIE
SASELRGGFDWSLHFQWEQLSPEQKARRLDPTEPIRTPIIAGGLFVIDKAWFDYLGKYDM
DMDIWGGENFEISFRVWMCGGSLEIVPCSRVGHVFRKKHPYVFPDGNANTYIKNTKRTAE
VWMDEYKQYYYAARPFALERPFGNVESRLDLRKNLRCQSFKWYLENIYPELSIPKESSIQ
KGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKGEDAKSQVWAFTYTQQILQEELCLSVI
TLFPGAPVVLVLCKNGDDRQQWTKTGSHIEHIASHLCLDTDMFGDGTENGKEIVVNPCES
SLMSQHWDMVSS
Enzyme 39 Number of Residues 552
Enzyme 39 Molecular Weight 64321
Enzyme 39 Theoretical pI 7.78
Enzyme 39 GO Classification Not Available
Enzyme 39 General Function Not Available
Enzyme 39 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney
Enzyme 39 Pathways
Enzyme 39 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • 1-31
Enzyme 39 Transmembrane Regions Not Available
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 28268674 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q96FL9 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name GLT14_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >1659 bp
ATGCGGCGCCTGACTCGTCGGCTGGTTCTGCCAGTCTTCGGGGTGCTCTGGATCACGGTG
CTGCTGTTCTTCTGGGTAACCAAGAGGAAGTTGGAGGTGCCGACGGGACCTGAAGTGCAG
ACCCCTAAGCCTTCGGACGCTGACTGGGACGACCTGTGGGACCAGTTTGATGAGCGGCGG
TATCTGAATGCCAAAAAGTGGCGCGTTGGTGACGACCCCTATAAGCTGTATGCTTTCAAC
CAGCGGGAGAGTGAGCGGATCTCCAGCAATCGGGCCATCCCGGACACTCGCCATCTGAGA
TGCACACTGCTGGTGTATTGCACGGACCTTCCACCCACTAGCATCATCATCACCTTCCAC
AACGAGGCCCGCTCCACGCTGCTCAGGACCATCCGCAGTGTATTAAACCGCACCCCTACG
CATCTGATCCGGGAAATCATATTAGTGGATGACTTCAGCAATGATCCTGATGACTGTAAA
CAGCTCATCAAGTTGCCCAAGGTGAAATGCTTGCGCAATAATGAACGGCAAGGTCTGGTC
CGGTCCCGGATTCGGGGCGCTGACATCGCCCAGGGCACCACTCTGACTTTCCTCGACAGC
CACTGTGAGGTGAACAGGGACTGGCTCCAGCCTCTGTTGCACAGGGTCAAAGAGGACTAC
ACGCGGGTGGTGTGCCCTGTGATCGATATCATTAACCTGGACACCTTCACCTACATCGAG
TCTGCCTCGGAGCTCAGAGGGGGGTTTGACTGGAGCCTCCACTTCCAGTGGGAGCAGCTC
TCCCCAGAGCAGAAGGCTCGGCGCCTGGACCCCACGGAGCCCATCAGGACTCCTATCATA
GCTGGAGGGCTCTTCGTGATCGACAAAGCTTGGTTTGATTACCTGGGGAAATATGATATG
GACATGGACATCTGGGGTGGGGAGAACTTTGAAATCTCCTTCCGAGTGTGGATGTGCGGG
GGCAGCCTAGAGATCGTCCCCTGCAGCCGAGTGGGGCACGTCTTCCGGAAGAAGCACCCC
TACGTTTTCCCTGATGGAAATGCCAACACGTATATAAAGAACACCAAGCGGACAGCTGAA
GTGTGGATGGATGAATACAAGCAATACTATTACGCTGCCCGGCCATTCGCCCTGGAGAGG
CCCTTCGGGAATGTTGAGAGCAGATTGGACCTGAGGAAGAATCTGCGCTGCCAGAGCTTC
AAGTGGTACCTGGAGAATATCTACCCTGAACTCAGCATCCCCAAGGAGTCCTCCATCCAG
AAGGGCAATATCCGACAGAGACAGAAGTGCCTGGAATCTCAAAGGCAGAACAACCAAGAA
ACCCCAAACCTAAAGTTGAGCCCCTGTGCCAAGGTCAAAGGCGAAGATGCAAAGTCCCAG
GTATGGGCCTTCACATACACCCAGCAGATCCTCCAGGAGGAGCTGTGCCTGTCAGTCATC
ACCTTGTTCCCTGGCGCCCCAGTGGTTCTTGTCCTTTGCAAGAATGGAGATGACCGACAG
CAATGGACCAAAACTGGTTCCCACATCGAGCACATAGCATCCCACCTCTGCCTCGATACA
GATATGTTCGGTGATGGCACCGAGAACGGCAAGGAAATCGTCGTCAACCCATGTGAGTCC
TCACTCATGAGCCAGCACTGGGACATGGTGAGCTCTTGA
Enzyme 39 GenBank Gene ID AB078144 Link Image
Enzyme 39 GeneCard ID GALNT14 Link Image
Enzyme 39 GenAtlas ID GALNT14 Link Image
Enzyme 39 HGNC ID HGNC:22946 Link Image
Enzyme 39 Chromosome Location 2
Enzyme 39 Locus 2p23.1
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Wang H, Tachibana K, Zhang Y, Iwasaki H, Kameyama A, Cheng L, Guo J, Hiruma T, Togayachi A, Kudo T, Kikuchi N, Narimatsu H: Cloning and characterization of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T14. Biochem Biophys Res Commun. 2003 Jan 17;300(3):738-44. [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 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 6294
Enzyme 40 Name Polypeptide N-acetylgalactosaminyltransferase 2
Enzyme 40 Synonyms
  1. Protein-UDP acetylgalactosaminyltransferase 2
  2. UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferase 2
  3. Polypeptide GalNAc transferase 2
  4. GalNAc-T2
  5. pp-GaNTase 2[Contains: Polypeptide N-acetylgalactosaminyltransferase 2 soluble form]
Enzyme 40 Gene Name GALNT2
Enzyme 40 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 2
MRRRSRMLLCFAFLWVLGIAYYMYSGGGSALAGGAGGGAGRKEDWNEIDPIKKKDLHHSN
GEEKAQSMETLPPGKVRWPDFNQEAYVGGTMVRSGQDPYARNKFNQVESDKLRMDRAIPD
TRHDQCQRKQWRVDLPATSVVITFHNEARSALLRTVVSVLKKSPPHLIKEIILVDDYSND
PEDGALLGKIEKVRVLRNDRREGLMRSRVRGADAAQAKVLTFLDSHCECNEHWLEPLLER
VAEDRTRVVSPIIDVINMDNFQYVGASADLKGGFDWNLVFKWDYMTPEQRRSRQGNPVAP
IKTPMIAGGLFVMDKFYFEELGKYDMMMDVWGGENLEISFRVWQCGGSLEIIPCSRVGHV
FRKQHPYTFPGGSGTVFARNTRRAAEVWMDEYKNFYYAAVPSARNVPYGNIQSRLELRKK
LSCKPFKWYLENVYPELRVPDHQDIAFGALQQGTNCLDTLGHFADGVVGVYECHNAGGNQ
EWALTKEKSVKHMDLCLTVVDRAPGSLIKLQGCRENDSRQKWEQIEGNSKLRHVGSNLCL
DSRTAKSGGLSVEVCGPALSQQWKFTLNLQQ
Enzyme 40 Number of Residues 571
Enzyme 40 Molecular Weight 64733
Enzyme 40 Theoretical pI 8.46
Enzyme 40 GO Classification Not Available
Enzyme 40 General Function Not Available
Enzyme 40 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region
Enzyme 40 Pathways
Enzyme 40 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • 1-20
Enzyme 40 Transmembrane Regions Not Available
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 971461 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q10471 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name GALT2_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1716 bp
ATGCGGCGGCGCTCGCGGATGCTGCTCTGCTTCGCCTTCCTGTGGGTGCTGGGCATCGCC
TACTACATGTACTCGGGGGGCGGCTCTGCGCTGGCCGGGGGCGCGGGCGGCGGCGCCGGC
AGGAAGGAGGACTGGAATGAAATTGACCCCATTAAAAAGAAAGACCTTCATCACAGCAAT
GGAGAAGAGAAAGCACAAAGCATGGAGACCCTCCCTCCAGGGAAAGTACGGTGGCCAGAC
TTTAACCAGGAAGCTTATGTTGGAGGGACGATGGTCCGCTCCGGGCAGGACCCTTACGCC
CGCAACAAGTTCAACCAGGTGGAGAGTGATAAGCTTCGAATGGACAGAGCCATCCCTGAC
ACCCGGCATGACCAGTGTCAGCGGAAGCAGTGGCGGGTGGATCTGCCGGCCACCAGCGTG
GTGATCACGTTTCACAATGAAGCCAGGTCGGCCCTACTCAGGACCGTGGTCAGCGTGCTT
AAGAAAAGCCCGCCCCATCTCATAAAAGAAATCATCTTGGTGGATGACTACAGCAATGAT
CCTGAGGACGGGGCTCTCTTGGGGAAAATTGAGAAAGTGCGAGTTCTTAGAAATGATCGA
CGAGAAGGCCTCATGCGCTCACGGGTTCGGGGGGCCGATGCTGCCCAAGCCAAGGTCCTG
ACCTTCCTGGACAGTCACTGCGAGTGTAATGAGCACTGGCTGGAGCCCCTCCTGGAAAGG
GTGGCGGAGGACAGGACTCGGGTTGTGTCACCCATCATCGATGTCATTAATATGGACAAC
TTTCAGTATGTGGGGGCATCTGCTGACTTGAAGGGCGGTTTTGATTGGAACTTGGTATTC
AAGTGGGATTACATGACGCCTGAGCAGAGAAGGTCCCGGCAGGGGAACCCAGTCGCCCCT
ATAAAAACCCCCATGATTGCTGGTGGGCTGTTTGTGATGGATAAGTTCTATTTTGAAGAA
CTGGGGAAGTACGACATGATGATGGATGTGTGGGGAGGAGAGAACCTAGAGATCTCGTTC
CGCGTGTGGCAGTGTGGTGGCAGCCTGGAGATCATCCCGTGCAGCCGTGTGGGACACGTG
TTCCGGAAGCAGCACCCCTACACGTTCCCGGGTGGCAGTGGCACTGTCTTTGCCCGAAAC
ACCCGCCGGGCAGCAGAGGTCTGGATGGATGAATACAAAAATTTCTATTATGCAGCAGTG
CCTTCTGCTAGAAACGTTCCTTATGGAAATATTCAGAGCAGATTGGAGCTTAGGAAGAAA
CTCAGCTGCAAGCCTTTCAAATGGTACCTTGAAAATGTCTATCCAGAGTTAAGGGTTCCA
GACCATCAGGATATAGCTTTTGGGGCCTTGCAGCAGGGAACTAACTGCCTCGACACTTTG
GGACACTTTGCTGATGGTGTGGTTGGAGTTTATGAATGTCACAATGCTGGGGGAAACCAG
GAATGGGCCTTGACGAAGGAGAAGTCGGTGAAGCACATGGATTTGTGCCTTACTGTGGTG
GACCGGGCACCGGGCTCTCTTATAAAGCTGCAGGGCTGCCGAGAAAATGACAGCAGACAG
AAATGGGAACAGATCGAGGGCAACTCCAAGCTGAGGCACGTGGGCAGCAACCTGTGCCTG
GACAGTCGCACGGCCAAGAGCGGGGGCCTAAGCGTGGAGGTGTGTGGCCCGGCCCTTTCG
CAGCAGTGGAAGTTCACGCTCAACCTGCAGCAGTAG
Enzyme 40 GenBank Gene ID X85019 Link Image
Enzyme 40 GeneCard ID GALNT2 Link Image
Enzyme 40 GenAtlas ID GALNT2 Link Image
Enzyme 40 HGNC ID HGNC:4124 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 1q41-q42
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 General References
  1. White T, Bennett EP, Takio K, Sorensen T, Bonding N, Clausen H: Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem. 1995 Oct 13;270(41):24156-65. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 6295
Enzyme 41 Name Polypeptide N-acetylgalactosaminyltransferase 12
Enzyme 41 Synonyms
  1. Protein-UDP acetylgalactosaminyltransferase 12
  2. UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferase 12
  3. Polypeptide GalNAc transferase 12
  4. GalNAc-T12
  5. pp-GaNTase 12
Enzyme 41 Gene Name GALNT12
Enzyme 41 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 12
MWGRTARRRCPRELRRGREALLVLLALLALAGLGSVLRAQRGAGAGAAEPGPPRTPRPGR
REPVMPRPPVPANALGARGEAVRLQLQGEELRLQEESVRLHQINIYLSDRISLHRRLPER
WNPLCKEKKYDYDNLPRTSVIIAFYNEAWSTLLRTVYSVLETSPDILLEEVILVDDYSDR
EHLKERLANELSGLPKVRLIRANKREGLVRARLLGASAARGDVLTFLDCHCECHEGWLEP
LLQRIHEEESAVVCPVIDVIDWNTFEYLGNSGEPQIGGFDWRLVFTWHTVPERERIRMQS
PVDVIRSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSH
VGHVFPKQAPYSRNKALANSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKL
QCKDFKWFLETVYPELHVPEDRPGFFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCH
GMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCEETAPENQKFILQEDGSLF
HEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKERML
Enzyme 41 Number of Residues 581
Enzyme 41 Molecular Weight 66939
Enzyme 41 Theoretical pI 6.78
Enzyme 41 GO Classification Not Available
Enzyme 41 General Function Not Available
Enzyme 41 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with Muc2 and Muc7. Displays enzymatic activity toward the Gal-NAc- Muc5AC glycopeptide, but no detectable activity to mono-GalNAc- glycosylated Muc1a, Muc2, Muc7 and EA2. May play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs
Enzyme 41 Pathways
Enzyme 41 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • 1-34
Enzyme 41 Transmembrane Regions Not Available
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 22122074 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID Q8IXK2 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name GLT12_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 Gene Sequence >1746 bp
ATGTGGGGGCGCACGGCGCGGCGGCGCTGCCCGCGGGAACTGCGGCGCGGCCGGGAGGCG
CTGTTGGTGCTCCTGGCGCTACTGGCGTTGGCCGGGCTGGGCTCGGTGCTGCGGGCGCAG
CGTGGGGCCGGGGCCGGGGCTGCCGAGCCGGGACCCCCGCGCACCCCGCGCCCCGGGCGG
CGCGAGCCGGTCATGCCGCGGCCGCCGGTGCCGGCGAACGCGCTGGGCGCGCGGGGCGAG
GCGGTGCGGCTGCAGCTGCAGGGCGAGGAGCTGCGGCTGCAGGAGGAGAGCGTGCGGCTG
CACCAGATTAACATCTACCTCAGCGACCGCATCTCACTGCACCGCCGCCTGCCCGTGCGC
TGGAACCCGCTGTGCAAAGAGAAGAAATATGATTATGATAATTTGCCCAGGACATCTGTT
ATCATAGCATTTTATAATGAAGCCTGGTCAACTCTCCTTCGGACAGTTTACAGTGTCCTT
GAGACATCCCCGGATATCCTGCTAGAAGAAGTGATCCTTGTAGATGACTACAGTGATAGA
GAGCACCTGAAGGAGCGCTTGGCCAATGAGCTTTCGGGACTGCCCAAGGTGCGCCTGATC
CGCGCCAACAAGAGAGAGGGCCTGGTGCGAGCCCGGCTGCTGGGGGCGTCTGCGGCGAGG
GGCGATGTTCTGACCTTCCTGGACTGTCACTGTGAGTGCCACGAAGGGTGGCTGGAGCCG
CTGCTGCAGAGGATCCATGAAGAGGAGTCGGCAGTGGTGTGCCCGGTGATTGATGTGATC
GACTGGAACACCTTCGAATACCTGGGGAACTCCGGGGAGCCCCAGATCGGCGGTTTCGAC
TGGAGGCTGGTGTTCACGTGGCACACAGTTCCTGAGAGGGAGAGGATACGGATGCAATCC
CCCGTCGATGTCATCAGGTCTCCAACAATGGCTGGTGGGCTGTTTGCTGTGAGTAAGAAA
TATTTTGAATATCTGGGGTCTTATGATACAGGAATGGAAGTTTGGGGAGGAGAAAACCTC
GAATTTTCCTTTAGGATCTGGCAGTGTGGTGGGGTTCTGGAAACACACCCATGTTCCCAT
GTTGGCCATGTTTTCCCCAAGCAAGCTCCCTACTCCCGCAACAAGGCTCTGGCCAACAGT
GTTCGTGCAGCTGAAGTATGGATGGATGAATTTAAAGAGCTCTACTACCATCGCAACCCC
CGTGCCCGCTTGGAACCTTTTGGGGATGTGACAGAGAGGAAGCAGCTCCGGGACAAGCTC
CAGTGTAAAGACTTCAAGTGGTTCTTGGAGACTGTGTATCCAGAACTGCATGTGCCTGAG
GACAGGCCTGGCTTCTTCGGGATGCTCCAGAACAAAGGACTAACAGACTACTGCTTTGAC
TATAACCCTCCCGATGAAAACCAGATTGTGGGACACCAGGTCATTCTGTACCTCTGTCAT
GGGATGGGCCAGAATCAGTTTTTCGAGTACACGTCCCAGAAAGAAATACGCTATAACACC
CACCAGCCTGAGGGCTGCATTGCTGTGGAAGCAGGAATGGATACCCTTATCATGCATCTC
TGCGAAGAAACTGCCCCAGAGAATCAGAAGTTCATCTTGCAGGAGGATGGATCTTTATTT
CACGAACAGTCCAAGAAATGTGTCCAGGCTGCGAGGAAGGAGTCGAGTGACAGTTTCGTT
CCACTCTTACGAGACTGCACCAACTCGGATCATCAGAAATGGTTCTTCAAAGAGCGCATG
TTATGA
Enzyme 41 GenBank Gene ID AB078146 Link Image
Enzyme 41 GeneCard ID GALNT12 Link Image
Enzyme 41 GenAtlas ID GALNT12 Link Image
Enzyme 41 HGNC ID HGNC:19877 Link Image
Enzyme 41 Chromosome Location 9
Enzyme 41 Locus 9q22.33
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 General References
  1. Guo JM, Zhang Y, Cheng L, Iwasaki H, Wang H, Kubota T, Tachibana K, Narimatsu H: Molecular cloning and characterization of a novel member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, pp-GalNAc-T12. FEBS Lett. 2002 Jul 31;524(1-3):211-8. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 6296
Enzyme 42 Name Polypeptide N-acetylgalactosaminyltransferase 1
Enzyme 42 Synonyms
  1. Protein-UDP acetylgalactosaminyltransferase 1
  2. UDP- GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
  3. Polypeptide GalNAc transferase 1
  4. GalNAc-T1
  5. pp-GaNTase 1[Contains: Polypeptide N-acetylgalactosaminyltransferase 1 soluble form]
Enzyme 42 Gene Name GALNT1
Enzyme 42 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 1
MRKFAYCKVVLATSLIWVLLDMFLLLYFSECNKCDEKKERGLPAGDVLEPVQKPHEGPGE
MGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALNRSLPDVRLEGCKTKVYPDNLPTTSV
VIVFHNEAWSTLLRTVHSVINRSPRHMIEEIVLVDDASERDFLKRPLESYVKKLKVPVHV
IRMEQRSGLIRARLKGAAVSKGQVITFLDAHCECTVGWLEPLLARIKHDRRTVVCPIIDV
ISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDR
DYFQEIGTYDAGMDIWGGENLEISFRIWQCGGTLEIVTCSHVGHVFRKATPYTFPGGTGQ
IINKNNRRLAEVWMDEFKNFFYIISPGVTKVDYGDISSRVGLRHKLQCKPFSWYLENIYP
DSQIPRHYFSLGEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDD
LCLDVSKLNGPVTMLKCHHLKGNQLWEYDPVKLTLQHVNSNQCLDKATEEDSQVPSIRDC
NGSRSQQWLLRNVTLPEIF
Enzyme 42 Number of Residues 559
Enzyme 42 Molecular Weight 64220
Enzyme 42 Theoretical pI 7.77
Enzyme 42 GO Classification Not Available
Enzyme 42 General Function Not Available
Enzyme 42 Specific Function Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7
Enzyme 42 Pathways
Enzyme 42 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • 1-31
Enzyme 42 Transmembrane Regions Not Available
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 1136285 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q10472 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name GALT1_HUMAN Link Image
Enzyme 42 PDB ID 1XHB Link Image
Enzyme 42 PDB File Show
Enzyme 42 3D Structure
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >1680 bp
ATGAGAAAATTTGCATACTGCAAGGTGGTCCTAGCCACCTCCTTGATTTGGGTACTCTTG
GATATGTTCCTGCTGCTTTACTTCAGTGAATGCAACAAATGTGATGAAAAAAAGGAGAGA
GGACTTCCTGCTGGAGATGTTCTAGAGCCAGTACAAAAGCCTCATGAAGGTCCTGGAGAA
ATGGGGAAACCAGTCGTCATTCCTAAAGAGGATCAAGAAAAGATGAAAGAGATGTTTAAA
ATCAATCAGTTCAATTTAATGGCAAGTGAGATGATTGCACTCAACAGATCTTTACCAGAT
GTTAGGTTAGAAGGGTGTAAAACAAAGGTGTATCCAGATAATCTTCCTACAACAAGTGTG
GTGATTGTTTTCCACAATGAGGCTTGGAGCACACTTCTGCGAACTGTCCATAGTGTCATT
AATCGCTCACCAAGACACATGATAGAAGAAATTGTTCTAGTAGATGATGCCAGTGAAAGA
GACTTTTTGAAAAGGCCTTTAGAGAGTTATGTGAAAAAACTAAAAGTACCAGTTCATGTA
ATTCGAATGGAACAACGTTCTGGATTGATCAGAGCTAGATTAAAAGGAGCTGCTGTGTCT
AAAGGCCAAGTGATCACCTTCCTGGATGCCCATTGTGAGTGTACAGTGGGATGGCTGGAG
CCTCTCTTGGCCAGGATCAAACATGACAGGAGAACAGTGGTGTGTCCCATCATCGATGTG
ATCAGTGATGATACTTTTGAGTACATGGCAGGCTCTGATATGACCTATGGTGGGTTCAAC
TGGAAGCTCAATTTTCGCTGGTATCCTGTTCCCCAAAGAGAAATGGACAGAAGGAAAGGT
GATCGGACTCTTCCTGTCAGGACACCTACCATGGCAGGAGGCCTTTTTTCAATAGACAGA
GATTACTTTCAGGAAATTGGAACATATGATGCTGGAATGGATATTTGGGGAGGAGAAAAC
CTAGAAATTTCCTTTAGGATTTGGCAGTGTGGAGGAACTTTGGAAATTGTTACATGCTCA
CATGTTGGACATGTGTTTCGGAAAGCTACACCTTACACGTTTCCAGGAGGCACAGGGCAG
ATTATCAATAAAAATAACAGACGACTTGCAGAAGTGTGGATGGATGAATTCAAGAATTTC
TTCTATATAATTTCTCCAGGTGTTACAAAGGTAGATTATGGAGATATATCGTCAAGAGTT
GGTCTAAGACACAAACTACAATGCAAACCTTTTTCCTGGTACCTAGAGAATATATATCCT
GATTCTCAAATTCCACGTCACTATTTCTCATTGGGAGAGATACGAAAAGAGGAAACGAAT
CAGTGTCTAGATAACATGGCTAGAAAAGAGAATGAAAAAGTTGGAATTTTTAATTGCCAT
GGTATGGGGGGTAATCAGGTTTTCTCTTATACTGCCAACAAAGAAATTAGAACAGATGAC
CTTTGCTTGGATGTTTCCAAACTTAATGGCCCAGTTACAATGCTCAAATGCCACCACCTA
AAGGGCAACCAACTCTGGGAGTATGACCCAGTGAAATTAACCCTGCAGCATGTGAACAGT
AATCAGTGCCTGGATAAAGCCACAGAAGAGGATAGCCAGGTGCCCAGCATTAGAGACTGC
AATGGAAGTCGGTCCCAGCAGTGGCTTCTTCGAAACGTCACCCTGCCAGAAATATTCTGA
Enzyme 42 GenBank Gene ID U41514 Link Image
Enzyme 42 GeneCard ID GALNT1 Link Image
Enzyme 42 GenAtlas ID GALNT1 Link Image
Enzyme 42 HGNC ID HGNC:4123 Link Image
Enzyme 42 Chromosome Location 18
Enzyme 42 Locus 18q12.1
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. Meurer JA, Naylor JM, Baker CA, Thomsen DR, Homa FL, Elhammer AP: cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase. J Biochem (Tokyo). 1995 Sep;118(3):568-74. [PubMed Link Image]
  2. White T, Bennett EP, Takio K, Sorensen T, Bonding N, Clausen H: Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem. 1995 Oct 13;270(41):24156-65. [PubMed Link Image]
  3. Meurer JA, Drong RF, Homa FL, Slightom JL, Elhammer AP: Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene. Glycobiology. 1996 Mar;6(2):231-41. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 6320
Enzyme 43 Name Beta-1,4-galactosyltransferase 3
Enzyme 43 Synonyms
  1. Beta-1,4-GalTase 3
  2. Beta4Gal-T3
  3. b4Gal-T3
  4. UDP-galactose:beta-N-acetylglucosamine beta- 1,4-galactosyltransferase 3
  5. UDP-Gal:beta-GlcNAc beta-1,4- galactosyltransferase 3[Includes: N-acetyllactosamine synthase
  6. Nal synthetase
  7. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
Enzyme 43 Gene Name B4GALT3
Enzyme 43 Protein Sequence >Beta-1,4-galactosyltransferase 3
MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSH
LPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCE
PRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVR
EALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSAL
TPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEEN
PHRFDLLVRTQNSWTQDGMNSLTYQLLARELGPLYTNITADIGTDPRGPRAPSGPRYPPG
SSQAFRQEMLQRRPPARPGPLSTANHTALRGSH
Enzyme 43 Number of Residues 393
Enzyme 43 Molecular Weight 43929
Enzyme 43 Theoretical pI 9.45
Enzyme 43 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 43 General Function Not Available
Enzyme 43 Specific Function Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids
Enzyme 43 Pathways
Enzyme 43 Reactions
  • UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • 1-36
Enzyme 43 Transmembrane Regions Not Available
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 2982510 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID O60512 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name B4GT3_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 Gene Sequence >1182 bp
ATGTTGCGGAGGCTGCTGGAGCGGCCTTGCACGCTGGCCCTGCTTGTGGGCTCCCAGCTG
GCTGTCATGATGTACCTGTCACTGGGGGGCTTCCGAAGTCTCAGTGCCCTATTTGGCCGA
GATCAGGGACCGACATTTGACTATTCTCACCCTCGTGATGTCTACAGTAACCTCAGTCAC
CTGCCTGGGGCCCCAGGGGGTCCTCCAGCTCCTCAAGGTCTGCCCTACTGTCCAGAACGA
TCTCCTCTCTTAGTGGGTCCTGTGTCGGTGTCCTTTAGCCCAGTGCCATCACTGGCAGAG
ATTGTGGAGCGGAATCCCCGGGTAGAACCAGGGGGCCGGTACCGCCCTGCAGGTTGTGAG
CCCCGCTCCCGAACAGCCATCATTGTGCCTCATCGTGCCCGGGAGCACCACCTGCGCCTG
CTGCTCTACCACCTGCACCCCTTCTTGCAGCGCCAGCAGCTTGCTTATGGCATCTATGTC
ATCCACCAGGCTGGAAATGGAACATTTAACAGGGCAAAACTGTTGAACGTTGGGGTGCGA
GAGGCCCTGCGTGATGAAGAGTGGGACTGCCTGTTCTTGCACGATGTGGACCTCTTGCCA
GAAAATGACCACAATCTGTATGTGTGTGACCCCCGGGGACCCCGCCATGTTGCCGTTGCT
ATGAACAAGTTTGGATACAGCCTCCCGTACCCCCAGTACTTCGGAGGAGTCTCAGCACTT
ACTCCTGACCAGTACCTGAAGATGAATGGCTTCCCCAATGAATACTGGGGCTGGGGTGGT
GAGGATGACGACATTGCTACCAGGGTGCGCCTGGCTGGGATGAAGATCTCTCGGCCCCCC
ACATCTGTAGGACACTATAAGATGGTGAAGCACCGAGGAGATAAGGGCAATGAGGAAAAT
CCCCACAGATTTGACCTCCTGGTCCGTACCCAGAATTCCTGGACGCAAGATGGGATGAAC
TCACTGACATACCAGTTGCTGGCTCGAGAGCTGGGGCCTCTTTATACCAACATCACAGCA
GACATTGGGACTGACCCTCGGGGTCCTCGGGCTCCTTCTGGGCCACGTTACCCACCTGGT
TCCTCCCAAGCCTTCCGTCAAGAGATGCTGCAACGCCGGCCCCCAGCCAGGCCTGGGCCT
CTATCTACTGCCAACCACACAGCCCTCCGAGGTTCACACTGA
Enzyme 43 GenBank Gene ID Y12509 Link Image
Enzyme 43 GeneCard ID B4GALT3 Link Image
Enzyme 43 GenAtlas ID B4GALT3 Link Image
Enzyme 43 HGNC ID HGNC:926 Link Image
Enzyme 43 Chromosome Location 1
Enzyme 43 Locus 1q21-q23
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Almeida R, Amado M, David L, Levery SB, Holmes EH, Merkx G, van Kessel AG, Rygaard E, Hassan H, Bennett E, Clausen H: A family of human beta4-galactosyltransferases. Cloning and expression of two novel UDP-galactose:beta-n-acetylglucosamine beta1, 4-galactosyltransferases, beta4Gal-T2 and beta4Gal-T3. J Biol Chem. 1997 Dec 19;272(51):31979-91. [PubMed Link Image]
  2. Lo NW, Shaper JH, Pevsner J, Shaper NL: The expanding beta 4-galactosyltransferase gene family: messages from the databanks. Glycobiology. 1998 May;8(5):517-26. [PubMed Link Image]
  3. Guo S, Sato T, Shirane K, Furukawa K: Galactosylation of N-linked oligosaccharides by human beta-1,4-galactosyltransferases I, II, III, IV, V, and VI expressed in Sf-9 cells. Glycobiology. 2001 Oct;11(10):813-20. [PubMed Link Image]
  4. Amado M, Almeida R, Schwientek T, Clausen H: Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1999 Dec 6;1473(1):35-53. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 6343
Enzyme 44 Name UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1
Enzyme 44 Synonyms
  1. Beta-3-GalNAc-T1
  2. Beta-1,3-galactosyltransferase 3
  3. Beta-1,3- GalTase 3
  4. Beta3Gal-T3
  5. b3Gal-T3
  6. Galactosylgalactosylglucosylceramide beta-D-acetyl- galactosaminyltransferase
  7. UDP-N- acetylgalactosamine:globotriaosylceramide beta-1,3-N- acetylgalactosaminyltransferase
  8. Globoside synthase
  9. Beta-3-Gx-T3
Enzyme 44 Gene Name B3GALNT1
Enzyme 44 Protein Sequence >UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1
MASALWTVLPSRMSLRSLKWSLLLLSLLSFFVMWYLSLPHYNVIERVNWMYFYEYEPIYR
QDFHFTLREHSNCSHQNPFLVILVTSHPSDVKARQAIRVTWGEKKSWWGYEVLTFFLLGQ
EAEKEDKMLALSLEDEHLLYGDIIRQDFLDTYNNLTLKTIMAFRWVTEFCPNAKYVMKTD
TDVFINTGNLVKYLLNLNHSEKFFTGYPLIDNYSYRGFYQKTHISYQEYPFKVFPPYCSG
LGYIMSRDLVPRIYEMMGHVKPIKFEDVYVGICLNLLKVNIHIPEDTNLFFLYRIHLDVC
QLRRVIAAHGFSSKEIITFWQVMLRNTTCHY
Enzyme 44 Number of Residues 331
Enzyme 44 Molecular Weight 39512
Enzyme 44 Theoretical pI 7.89
Enzyme 44 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 44 General Function Not Available
Enzyme 44 Specific Function Transfers N-acetylgalactosamine on to globotriaosylceramide
Enzyme 44 Pathways
Enzyme 44 Reactions
  • UDP-N-acetyl-D-galactosamine + D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide = UDP + N-acetyl-D-galactosaminyl-1,3-D-galactosyl-1,4-D-galactosyl-1,4-D-glucosylceramide
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • 1-37
Enzyme 44 Transmembrane Regions Not Available
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 3256005 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID O75752 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name B3GL1_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 Gene Sequence >996 bp
ATGGCCTCGGCTCTCTGGACTGTCCTTCCGAGTAGGATGTCACTGAGATCCCTCAAATGG
AGCCTCCTGCTGCTGTCACTCCTGAGTTTCTTTGTGATGTGGTACCTCAGCCTTCCCCAC
TACAATGTGATAGAACGCGTGAACTGGATGTACTTCTATGAGTATGAGCCGATTTACAGA
CAAGACTTTCACTTCACACTTCGAGAGCATTCAAACTGCTCTCATCAAAATCCATTTCTG
GTCATTCTGGTGACCTCCCACCCTTCAGATGTGAAAGCCAGGCAGGCCATTAGAGTTACT
TGGGGTGAAAAAAAGTCTTGGTGGGGATATGAGGTTCTTACATTTTTCTTATTAGGCCAA
GAGGCTGAAAAGGAAGACAAAATGTTGGCATTGTCCTTAGAGGATGAACACCTTCTTTAT
GGTGACATAATCCGACAAGATTTTTTAGACACATATAATAACCTGACCTTGAAAACCATT
ATGGCATTCAGGTGGGTAACTGAGTTTTGCCCCAATGCCAAGTACGTAATGAAGACAGAC
ACTGATGTTTTCATCAATACTGGCAATTTAGTGAAGTATCTTTTAAACCTAAACCACTCA
GAGAAGTTTTTCACAGGTTATCCTCTAATTGATAATTATTCCTATAGAGGATTTTACCAA
AAAACCCATATTTCTTACCAGGAGTATCCTTTCAAGGTGTTCCCTCCATACTGCAGTGGG
TTGGGTTATATAATGTCCAGAGATTTGGTGCCAAGGATCTATGAAATGATGGGTCACGTA
AAACCCATCAAGTTTGAAGATGTTTATGTCGGGATCTGTTTGAATTTATTAAAAGTGAAC
ATTCATATTCCAGAAGACACAAATCTTTTCTTTCTATATAGAATCCATTTGGATGTCTGT
CAACTGAGACGTGTGATTGCAGCCCATGGCTTTTCTTCCAAGGAGATCATCACTTTTTGG
CAGGTCATGCTAAGGAACACCACATGCCATTATTAA
Enzyme 44 GenBank Gene ID Y15062 Link Image
Enzyme 44 GeneCard ID B3GALNT1 Link Image
Enzyme 44 GenAtlas ID B3GALNT1 Link Image
Enzyme 44 HGNC ID HGNC:918 Link Image
Enzyme 44 Chromosome Location 3
Enzyme 44 Locus 3q25
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 General References
  1. Amado M, Almeida R, Carneiro F, Levery SB, Holmes EH, Nomoto M, Hollingsworth MA, Hassan H, Schwientek T, Nielsen PA, Bennett EP, Clausen H: A family of human beta3-galactosyltransferases. Characterization of four members of a UDP-galactose:beta-N-acetyl-glucosamine/beta-nacetyl-galactosamine beta-1,3-galactosyltransferase family. J Biol Chem. 1998 May 22;273(21):12770-8. [PubMed Link Image]
  2. Okajima T, Nakamura Y, Uchikawa M, Haslam DB, Numata SI, Furukawa K, Urano T, Furukawa K: Expression cloning of human globoside synthase cDNAs. Identification of beta 3Gal-T3 as UDP-N-acetylgalactosamine:globotriaosylceramide beta 1,3-N-acetylgalactosaminyltransferase. J Biol Chem. 2000 Dec 22;275(51):40498-503. [PubMed Link Image]
  3. Hellberg A, Poole J, Olsson ML: Molecular basis of the globoside-deficient P(k) blood group phenotype. Identification of four inactivating mutations in the UDP-N-acetylgalactosamine: globotriaosylceramide 3-beta-N-acetylgalactosaminyltransferase gene. J Biol Chem. 2002 Aug 16;277(33):29455-9. Epub 2002 May 21. [PubMed Link Image]
  4. 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 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 6380
Enzyme 45 Name Glycogen [starch] synthase, liver
Enzyme 45 Synonyms Not Available
Enzyme 45 Gene Name GYS2
Enzyme 45 Protein Sequence >Glycogen [starch] synthase, liver
MLRGRSLSVTSLGGLPQWEVEELPVEELLLFEVAWEVTNKVGGIYTVIQTKAKTTADEWG
ENYFLIGPYFEHNMKTQVEQCEPVNDAVRRAVDAMNKHGCQVHFGRWLIEGSPYVVLFDI
GYSAWNLDRWKGDLWEACSVGIPYHDREANDMLIFGSLTAWFLKEVTDHADGKYVVAQFH
EWQAGIGLILSRARKLPIATIFTTHATLLGRYLCAANIDFYNHLDKFNIDKEAGERQIYH
RYCMERASVHCAHVFTTVSEITAIEAEHMLKRKPDVVTPNGLNVKKFSAVHEFQNLHAMY
KARIQDFVRGHFYGHLDFDLEKTLFLFIAGRYEFSNKGADIFLESLSRLNFLLRMHKSDI
TVVVFFIMPAKTNNFNVETLKGQAVRKQLWDVAHSVKEKFGKKLYDALLRGEIPDLNDIL
DRDDLTIMKRAIFSTQRQSLPPVTTHNMIDDSTDPILSTIRRIGLFNNRTDRVKVILHPE
FLSSTSPLLPMDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSVTTNLSGFGCFMQE
HVADPTAYGIYIVDRRFRSPDDSCNQLTKFLYGFCKQSRRQRIIQRNRTERLSDLLDWRY
LGRYYQHARHLTLSRAFPDKFHVELTSPPTTEGFKYPRPSSVPPSPSGSQASSPQSSDVE
DEVEDERYDEEEEAERDRLNIKSPFSLSHVPHGKKKLHGEYKN
Enzyme 45 Number of Residues 703
Enzyme 45 Molecular Weight 80958
Enzyme 45 Theoretical pI 6.82
Enzyme 45 GO Classification
Function
  • UDP-glucosyltransferase activity
  • UDP-glycosyltransferase activity
  • catalytic activity
  • glycogen (starch) synthase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • cellular polysaccharide metabolism
  • glucan metabolism
  • glycogen biosynthesis
  • glycogen metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • polysaccharide metabolism
Component
Enzyme 45 General Function Cell wall/membrane/envelope biogenesis
Enzyme 45 Specific Function Transfers the glycosyl residue from UDP-Glc to the nonreducing end of alpha-1,4-glucan
Enzyme 45 Pathways
Enzyme 45 Reactions
  • UDP-glucose + (1,4-alpha-D-glucosyl)n = UDP + (1,4-alpha-D-glucosyl)n+1
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • None
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 546961 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID P54840 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name GYS2_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >2112 bp
ATGCTTCGAGGCCGATCCCTCTCTGTAACATCCCTGGGTGGGCTTCCCCAGTGGGAAGTC
GAAGAACTTCCTGTGGAGGAGTTACTGCTCTTTGAAGTTGCTTGGGAAGTGACCAATAAA
GTTGGAGGCATCTATACTGTGATTCAGACAAAGGCCAAAACAACAGCAGATGAATGGGGA
GAGAACTATTTTCTGATAGGTCCATATTTTGAGCATAATATGAAGACTCAGGTGGAACAG
TGTGAACCTGTAAATGATGCTGTCAGAAGAGCAGTGGACGCAATGAATAAGCATGGCTGC
CAGGTGCATTTTGGAAGATGGCTGATAGAAGGAAGTCCTTATGTGGTACTTTTTGACATA
GGCTATTCAGCTTGGAATCTGGACAGGTGGAAGGGTGACCTCTGGGAAGCATGCAGTGTC
GGCATTCCTTATCATGACCGAGAAGCCAATGATATGCTGATATTTGGATCTTTAACTGCC
TGGTTCTTAAAAGAGGTGACAGATCATGCAGATGGTAAATATGTCGTTGCCCAATTCCAT
GAATGGCAGGCTGGAATTGGACTGATCCTTTCTCGAGCCAGGAAACTTCCTATTGCCACA
ATATTTACAACCCACGCTACACTACTTGGGAGGTATCTCTGTGCAGCAAATATTGATTTC
TACAACCATCTTGATAAGTTTAACATTGACAAAGAGGCTGGGGAAAGGCAGATTTACCAC
CGGTACTGCATGGAGCGAGCTTCCGTTCATTGCGCTCACGTGTTCACCACGGTTTCTGAA
ATAACAGCAATAGAAGCTGAACATATGCTGAAGAGAAAGCCTGATGTAGTTACTCCAAAC
GGCTTGAATGTTAAGAAATTTTCAGCAGTGCATGAGTTTCAAAATCTACATGCCATGTAC
AAGGCCAGAATCCAAGATTTTGTTCGAGGTCATTTCTATGGTCATCTCGACTTTGATCTT
GAAAAGACTTTGTTCCTTTTCATTGCTGGGAGGTATGAGTTTTCAAACAAAGGAGCTGAC
ATCTTCCTAGAATCCTTATCCAGGCTAAATTTCCTGCTGAGGATGCATAAAAGTGACATC
ACAGTGGTGGTGTTTTTCATTATGCCTGCCAAGACAAATAATTTCAACGTGGAAACCCTG
AAAGGACAAGCAGTGCGAAAACAGCTGTGGGATGTTGCACATTCTGTGAAGGAAAAGTTT
GGAAAAAAACTCTATGATGCATTATTAAGAGGAGAAATTCCTGACCTGAACGATATTTTA
GATCGAGATGATCTAACAATTATGAAAAGAGCCATCTTTTCAACTCAGCGACAGTCATTG
CCCCCAGTGACCACGCACAACATGATTGATGACTCCACCGACCCCATCCTCAGCACCATT
AGACGGATTGGACTTTTCAACAACCGCACAGATAGAGTCAAGGTGATTTTGCACCCAGAG
TTTCTATCCTCCACCAGTCCCTTACTACCCATGGACTATGAAGAGTTTGTTAGAGGTTGT
CATCTTGGAGTATTTCCATCATACTATGAACCCTGGGGTTATACTCCAGCTGAATGCACT
GTGATGGGTATCCCCAGTGTGACCACGAATCTCTCCGGGTTTGGCTGTTTCATGCAGGAG
CACGTGGCTGATCCTACTGCTTACGGTATTTACATCGTTGACAGGCGGTTCCGTTCTCCA
GATGATTCTTGCAATCAGCTGACTAAGTTTCTCTATGGATTTTGCAAACAGTCACGCCGC
CAAAGGATTATCCAGAGGAACAGAACTGAGAGGCTCTCAGATCTTCTGGATTGGAGATAC
TTAGGCAGATATTACCAGCATGCCAGACACCTGACATTAAGCAGAGCTTTTCCAGATAAA
TTCCATGTGGAACTAACATCACCACCAACGACAGAAGGATTTAAATATCCCAGGCCTTCC
TCAGTACCACCTTCTCCTTCAGGGTCTCAGGCCTCCAGTCCTCAGAGCAGTGATGTGGAA
GATGAAGTGGAGGATGAGAGATACGATGAGGAAGAGGAGGCTGAAAGGGATCGGTTAAAT
ATCAAGTCACCATTTTCACTGAGCCACGTTCCTCATGGGAAGAAAAAGCTGCATGGTGAA
TATAAGAACTGA
Enzyme 45 GenBank Gene ID S70004 Link Image
Enzyme 45 GeneCard ID GYS2 Link Image
Enzyme 45 GenAtlas ID GYS2 Link Image
Enzyme 45 HGNC ID HGNC:4707 Link Image
Enzyme 45 Chromosome Location 12
Enzyme 45 Locus 12p12.2
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Nuttall FQ, Gannon MC, Bai G, Lee EY: Primary structure of human liver glycogen synthase deduced by cDNA cloning. Arch Biochem Biophys. 1994 Jun;311(2):443-9. [PubMed Link Image]
  2. Orho M, Bosshard NU, Buist NR, Gitzelmann R, Aynsley-Green A, Blumel P, Gannon MC, Nuttall FQ, Groop LC: Mutations in the liver glycogen synthase gene in children with hypoglycemia due to glycogen storage disease type 0. J Clin Invest. 1998 Aug 1;102(3):507-15. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 6382
Enzyme 46 Name Glycogenin-1
Enzyme 46 Synonyms Not Available
Enzyme 46 Gene Name GYG1
Enzyme 46 Protein Sequence >Glycogenin-1
MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEVIM
VDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDREEL
SAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTDIR
KHLPFIYNLSSISIYSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPNM
THPEFLILWWNIFTTNVLPLLQQFGLVKDTCSYVNVLSDLVYTLAFSCGFCRKEDVSGAI
SHLSLGEIPAMAQPFVSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ
Enzyme 46 Number of Residues 350
Enzyme 46 Molecular Weight 39384
Enzyme 46 Theoretical pI 5.19
Enzyme 46 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 46 General Function Not Available
Enzyme 46 Specific Function Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions
  • UDP-glucose + glycogenin = UDP + glucosylglycogenin
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • None
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 1174167 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID P46976 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name GLYG_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >1002 bp
ATGACAGATCAGGCCTTTGTGACACTAACCACAAACGATGCCTACGCCAAAGGTGCCCTG
GTCCTGGGATCATCTCTGAAACAGCACAGGACCACCAGGAGGCTGGTCGTGCTCGCCACC
CCTCAGGTCTCAGACTCCATGAGAAAAGTTTTAGAGACAGTCTTTGATGAAGTCATCATG
GTAGATGTCTTGGACAGTGGCGATTCTGCTCATCTAACCTTAATGAAGAGGCCAGAGTTG
GGTGTCACGCTGACAAAGCTCCACTGCTGGTCGCTTACACAGTATTCAAAATGTGTATTC
ATGGATGCAGATACTCTGGTCCTAGCAAATATTGATGATCTTTTTGACAGAGAAGAATTG
TCAGCAGCACCAGACCCAGGGTGGCCTGACTGCTTCAATTCCGGAGTCTTCGTTTATCAG
CCTTCAGTTGAAACATACAATCAGCTGTTGCATCTTGCTTCTGAGCAAGGTAGTTTTGAT
GGTGGGGACCAAGGCATACTGAACACATTTTTTAGCAGCTGGGCAACAACAGATATCAGA
AAACACCTGCCGTTTATTTATAACCTAAGCAGCATCTCTATATACTCCTACCTCCCGGCA
TTTAAAGTGTTTGGTGCAAGTGCCAAAGTTGTGCATTTCCTGGGACGAGTCAAACCATGG
AATTATACTTATGATCCCAAAACAAAAAGTGTCAAAAGTGAGGCCCATGATCCCAACATG
ACTCATCCAGAGTTTCTCATCCTGTGGTGGAACATCTTTACCACCAACGTTTTACCTCTG
CTTCAACAATTTGGCCTTGTCAAAGACACCTGCTCATATGTAAATGTGGAAGATGTCTCA
GGAGCCATATCACATCTGTCCCTTGGGGAGATCCCAGCTATGGCACAGCCGTTTGTATCC
TCGGAAGAACGGAAGGAACGATGGGAACAGGGCCAGGCTGATTATATGGGAGCAGATTCC
TTTGACAACATCAAGAGGAAACTTGACACTTACCTCCAGTAG
Enzyme 46 GenBank Gene ID U44131 Link Image
Enzyme 46 GeneCard ID GYG1 Link Image
Enzyme 46 GenAtlas ID GYG1 Link Image
Enzyme 46 HGNC ID HGNC:4699 Link Image
Enzyme 46 Chromosome Location 3
Enzyme 46 Locus 3q24-q25.1
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Barbetti F, Rocchi M, Bossolasco M, Cordera R, Sbraccia P, Finelli P, Consalez GG: The human skeletal muscle glycogenin gene: cDNA, tissue expression and chromosomal localization. Biochem Biophys Res Commun. 1996 Mar 7;220(1):72-7. [PubMed Link Image]
  2. Lomako J, Mazuruk K, Lomako WM, Alonso MD, Whelan WJ, Rodriguez IR: The human intron-containing gene for glycogenin maps to chromosome 3, band q24. Genomics. 1996 May 1;33(3):519-22. [PubMed Link Image]
  3. van Maanen MH, Fournier PA, Palmer TN, Abraham LJ: Characterization of the human glycogenin-1 gene: identification of a muscle-specific regulatory domain. Gene. 1999 Jul 8;234(2):217-26. [PubMed Link Image]
  4. Zhai L, Mu J, Zong H, DePaoli-Roach AA, Roach PJ: Structure and chromosomal localization of the human glycogenin-2 gene GYG2. Gene. 2000 Jan 25;242(1-2):229-35. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 6383
Enzyme 47 Name Glycogen [starch] synthase, muscle
Enzyme 47 Synonyms Not Available
Enzyme 47 Gene Name GYS1
Enzyme 47 Protein Sequence >Glycogen [starch] synthase, muscle
MPLNRTLSMSSLPGLEDWEDEFDLENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGD
NYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVG
ASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFH
EWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYH
RYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQS
KARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQ
TVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKML
DKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPE
FLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEE
HIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKY
LGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYRYPRPASVPPSPSLSRHSSPHQSEDE
EDPRNGPLEEDGERYDEDEEAAKDRRNIRAPEWPRRASCTSSTSGSKRNSVDTATSSSLS
TPSEPLSPTSSLGEERN
Enzyme 47 Number of Residues 737
Enzyme 47 Molecular Weight 83786
Enzyme 47 Theoretical pI 6.10
Enzyme 47 GO Classification
Function
  • UDP-glucosyltransferase activity
  • UDP-glycosyltransferase activity
  • catalytic activity
  • glycogen (starch) synthase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • cellular polysaccharide metabolism
  • glucan metabolism
  • glycogen biosynthesis
  • glycogen metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • polysaccharide metabolism
Component
Enzyme 47 General Function Cell wall/membrane/envelope biogenesis
Enzyme 47 Specific Function Transfers the glycosyl residue from UDP-Glc to the nonreducing end of alpha-1,4-glucan
Enzyme 47 Pathways
Enzyme 47 Reactions
  • UDP-glucose + (1,4-alpha-D-glucosyl)n = UDP + (1,4-alpha-D-glucosyl)n+1
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • None
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 183355 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID P13807 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name GYS1_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >2214 bp
ATGCCTTTAAACCGCACTTTGTCCATGTCCTCACTGCCAGGACTGGAGGACTGGGAGGAT
GAATTCGACCTGGAGAACGCAGTGCTCTTCGAAGTGGCCTGGGAGGTGGCTAACAAGGTG
GGTGGCATCTACACGGTGCTGCAGACGAAGGCGAAGGTGACAGGGGACGAATGGGGCGAC
AACTACTTCCTGGTGGGGCCGTACACGGAGCAGGGCGTCAGGACCCAGGTGGAACTGCTG
GAGGCCCCCACCCCGGCCCTGAAGAGGACACTGGATTCCATGAACAGCAAGGGCTGCAAG
GTGTATTTCGGGCGCTGGCTGATCGAGGGAGGCCCTCTGGTGGTGCTCCTGGACGTGGGT
GCCTCAGCTTGGGCCCTGGAGCGCTGGAAGGGAGAGCTCTGGGATATCTGCAACATCGGA
GTGCCGTGGTACGACCGCGAGGCCAACGACGCTGTCCTCTTTGGCTTTCTGACCACCTGG
TTCCTGGGTGAGTTCCTGGCACAGAGTGAGGAGAAGCCACATGTGGTTGCTCACTTCCAT
GAGTGGTTGGCAGGCGTTGGACTCTGCCTGTGTCGTGCCCGGCGACTGCCTGTAGCAACC
ATCTTCACCACCCATGCCACGCTGCTGGGGCGCTACCTGTGTGCCGGTGCCGTGGACTTC
TACAACAACCTGGAGAACTTCAACGTGGACAAGGAAGCAGGGGAGAGGCAGATCTACCAC
CGATACTGCATGGAAAGGGCGGCAGCCCACTGCGCTCACGTCTTCACTACTGTGTCCCAG
ATCACCGCCATCGAGGCACAGCACTTGCTCAAGAGGAAACCAGATATTGTGACCCCCAAT
GGGCTGAATGTGAAGAAGTTTTCTGCCATGCATGAGTTCCAGAACCTCCATGCTCAGAGC
AAGGCTCGAATCCAGGAGTTTGTGCGGGGCCATTTTTATGGGCATCTGGACTTCAACTTG
GACAAGACCTTATACTTCTTTATCGCCGGCCGCTATGAGTTCTCCAACAAGGGTGCTGAC
GTCTTTCTGGAGGCATTGGCTCGGCTCAACTATCTGCTCAGAGTGAACGGCAGCGAGCAG
ACAGTGGTTGCCTTCTTCATCATGCCAGCGCGGACCAACAATTTCAACGTGGAAACCCTC
AAAGGCCAAGCTGTGCGCAAACAGCTTTGGGACACGGCCAACACGGTGAAGGAAAAGTTC
GGGAGGAAGCTTTATGAATCCTTACTGGTTGGGAGCCTTCCCGACATGAACAAGATGCTG
GATAAGGAAGACTTCACTATGATGAAGAGAGCCATCTTTGCAACGCAGCGGCAGTCTTTC
CCCCCTGTGTGCACCCACAATATGCTGGATGACTCCTCAGACCCCATCCTGACCACCATC
CGCCGAATCGGCCTCTTCAATAGCAGTGCCGACAGGGTGAAGGTGATTTTCCACCCGGAG
TTCCTCTCCTCCACAAGCCCCCTGCTCCCTGTGGACTATGAGGAGTTTGTCCGTGGCTGT
CACCTTGGAGTCTTCCCCTCCTACTATGAGCCTTGGGGCTACACACCGGCTGAGTGCACG
GTTATGGGAATCCCCAGTATCTCCACCAATCTCTCCGGCTTCGGCTGCTTCATGGAGGAA
CACATCGCAGACCCCTCAGCTTACGGTATCTACATTCTTGACCGGCGGTTCCGCAGCCTG
GATGATTCCTGCTCGCAGCTCACCTCCTTCCTCTACAGTTTCTGTCAGCAGAGCCGGCGG
CAGCGTATCATCCAGCGGAACCGCACGGAGCGCCTCTCCGACCTTCTGGACTGGAAATAC
CTAGGCCGGTACTATATGTCTGCGCGCCACATGGCGCTGTCCAAGGCCTTTCCAGAGCAC
TTCACCTACGAGCCCAACGAGGCGGATGCGGCCCAGGGGTACCGCTACCCACGGCCAGCC
TCGGTGCCACCGTCGCCCTCGCTGTCACGACACTCCAGCCCGCACCAGAGTGAGGACGAG
GAGGATCCCCGGAACGGGCCGCTGGAGGAAGACGGCGAGCGCTACGATGAGGACGAGGAG
GCCGCCAAGGACCGGCGCAACATCCGTGCACCAGAGTGGCCGCGCCGAGCGTCCTGCACC
TCCTCCACCAGCGGCCGCAAGCGCAACTCTGTGGACACGGCCACCTCCAGCTCACTCAGC
ACCCCGAGCGAGCCCCTCAGCCCCACCAGCTCCCTGGGCGAGGAGCGTAACTAA
Enzyme 47 GenBank Gene ID J04501 Link Image
Enzyme 47 GeneCard ID GYS1 Link Image
Enzyme 47 GenAtlas ID GYS1 Link Image
Enzyme 47 HGNC ID HGNC:4706 Link Image
Enzyme 47 Chromosome Location 19
Enzyme 47 Locus 19q13.3
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 General References
  1. Browner MF, Nakano K, Bang AG, Fletterick RJ: Human muscle glycogen synthase cDNA sequence: a negatively charged protein with an asymmetric charge distribution. Proc Natl Acad Sci U S A. 1989 Mar;86(5):1443-7. [PubMed Link Image]
  2. Orho M, Nikula-Ijas P, Schalin-Jantti C, Permutt MA, Groop LC: Isolation and characterization of the human muscle glycogen synthase gene. Diabetes. 1995 Sep;44(9):1099-105. [PubMed Link Image]
  3. Su X, Schuler L, Shapiro S: Cloning and characterization of a glycogen synthase cDNA from human endometrium. J Steroid Biochem Mol Biol. 1996 Dec;59(5-6):459-65. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 6384
Enzyme 48 Name Glycogenin-2
Enzyme 48 Synonyms
  1. GN-2
  2. GN2
Enzyme 48 Gene Name GYG2
Enzyme 48 Protein Sequence >Glycogenin-2
MSETEFHHGAQAGLELLRSSNSPTSASQSAGMTVTDQAFVTLATNDIYCQGALVLGQSLR
RHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSADYIHLAFLKRPELGLTLTKL
HCWTLTHYSKCVFLDADTLVLSNVDELFDRGEFSAAPDPGWPDCFNSGVFVFQPSLHTHK
LLLQHAMEHGSFDGADQGLLNSFFRNWSTTDIHKHLPFIYNLSSNTMYTYSPAFKQFGSS
AKVVHFLGSMKPWNYKYNPQSGSVLEQGSASSSQHQAAFLHLWWTVYQNNVLPLYKSVQA
GEARASPGHTLCHSDVGGPCADSASGVGEPCENSTPSAGVPCANSPLGSNQPAQGLPEPT
QIVDETLSLPEGRRSEDMIACPETETPAVITCDPLSQPSPQPADFTETETILQPANKVES
VSSEETFEPSQELPAEALRDPSLQDALEVDLAVSVSQISIEEKVKELSPEEERRKWEEGR
IDYMGKDAFARIQEKLDRFLQ
Enzyme 48 Number of Residues 501
Enzyme 48 Molecular Weight 55184
Enzyme 48 Theoretical pI 4.74
Enzyme 48 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 48 General Function Not Available
Enzyme 48 Specific Function Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase
Enzyme 48 Pathways Not Available
Enzyme 48 Reactions
  • UDP-glucose + glycogenin = UDP + glucosylglycogenin
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • None
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 2618766 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID O15488 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name GLYG2_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 Gene Sequence >1506 bp
ATGTCGGAGACAGAGTTTCACCATGGTGCCCAGGCTGGTCTCGAACTCCTGAGGTCAAGC
AATTCACCCACCTCAGCCTCCCAAAGTGCTGGAATGACAGTGACTGATCAGGCTTTTGTC
ACACTAGCCACCAATGACATCTACTGCCAGGGCGCCCTGGTCCTGGGGCAGTCACTGAGG
AGACACAGGCTGACGAGGAAGCTGGTGGTGTTGATCACTCCTCAGGTGTCCAGCCTGCTC
AGGGTCATCCTCTCGAAGGTGTTCGATGAAGTCATTGAAGTGAATCTAATCGATAGTGCC
GACTACATCCACCTGGCCTTTCTGAAGAGACCTGAGCTCGGGCTCACCCTCACCAAGCTT
CACTGTTGGACTCTCACTCACTACAGCAAGTGTGTCTTCCTGGATGCAGACACTCTGGTG
CTGTCCAATGTCGATGAGCTGTTTGACAGGGGAGAGTTTTCTGCGGCCCCGGACCCCGGA
TGGCCGGATTGCTTCAATAGCGGGGTGTTTGTCTTCCAGCCTTCTCTCCACACGCATAAA
CTCCTGCTACAGCACGCCATGGAACACGGCAGCTTTGACGGGGCAGACCAAGGCTTACTG
AATAGTTTCTTCAGGAACTGGTCGACCACAGACATCCACAAGCACCTGCCGTTCATCTAT
AACTTGAGTAGTAACACGATGTACACTTACAGCCCTGCCTTCAAGCAATTCGGTTCCAGT
GCAAAGGTCGTCCACTTTTTGGGGTCCATGAAACCTTGGAACTACAAGTACAATCCACAG
AGTGGCTCGGTGTTGGAGCAAGGCTCAGTGTCCAGCAGCCAGCACCAGGCGGCATTCCTT
CATCTCTGGTGGACGGTCTACCAGAACAACGTGCTGCCCCTTTATAAAAGCGTCCAAGCG
GGGGAAGCACGCGCGTCTCCTGGTCACACACTTTGCCACAGTGATGTGGGGGGGCCGTGT
GCGGATTCAGCCTCTGGTGTTGGAGAGCCGTGTGAAAATTCAACACCCAGTGCGGGCGTG
CCGTGTGCAAATTCACCACTGGGTTCTAACCAGCCTGCTCAGGGCCTTCCGGAGCCGACC
CAGATAGTGGATGAGACCCTGTCCCTACCTGAAGGACGCCGTTCAGAAGATATGATAGCT
TGTCCTGAAACTGAGACTCCTGCCGTGATAACGTGTGACCCACTGTCCCAGCCTTCCCCT
CAGCCTGCAGACTTCACAGAGACTGAAACCATCTTGCAGCCAGCAAATAAAGTCGAAAGT
GTCTCATCCGAGGAAACCTTCGAACCAAGCCAGGAACTCCCTGCTGAGGCTCTCAGGGAC
CCCAGTCTGCAGGATGCACTGGAGGTCGACCTGGCCGTCTCTGTTTCCCAGATCTCCATC
GAAGAGAAGGTGAAGGAATTGAGCCCCGAGGAAGAGAGGAGGAAGTGGGAGGAAGGCCGT
ATCGACTACATGGGGAAGGACGCGTTTGCTCGCATCCAGGAGAAGCTGGACCGGTTCCTG
CAGTAA
Enzyme 48 GenBank Gene ID U94362 Link Image
Enzyme 48 GeneCard ID GYG2 Link Image
Enzyme 48 GenAtlas ID GYG2 Link Image
Enzyme 48 HGNC ID HGNC:4700 Link Image
Enzyme 48 Chromosome Location X
Enzyme 48 Locus Xp22.3
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 General References
  1. Mu J, Skurat AV, Roach PJ: Glycogenin-2, a novel self-glucosylating protein involved in liver glycogen biosynthesis. J Biol Chem. 1997 Oct 31;272(44):27589-97. [PubMed Link Image]
  2. Zhai L, Mu J, Zong H, DePaoli-Roach AA, Roach PJ: Structure and chromosomal localization of the human glycogenin-2 gene GYG2. Gene. 2000 Jan 25;242(1-2):229-35. [PubMed Link Image]
  3. Mu J, Roach PJ: Characterization of human glycogenin-2, a self-glucosylating initiator of liver glycogen metabolism. J Biol Chem. 1998 Dec 25;273(52):34850-6. [PubMed Link Image]
  4. Harris RA, Yang A, Stein RC, Lucy K, Brusten L, Herath A, Parekh R, Waterfield MD, O'Hare MJ, Neville MA, Page MJ, Zvelebil MJ: Cluster analysis of an extensive human breast cancer cell line protein expression map database. Proteomics. 2002 Feb;2(2):212-23. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 6389
Enzyme 49 Name Histo-blood group ABO system transferase
Enzyme 49 Synonyms
  1. NAGAT[Includes: Glycoprotein-fucosylgalactoside alpha-N- acetylgalactosaminyltransferase
  2. Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
  3. Histo-blood group A transferase
  4. A transferase
  5. Glycoprotein-fucosylgalactoside alpha- galactosyltransferase
  6. Fucosylglycoprotein 3-alpha- galactosyltransferase
  7. Histo-blood group B transferase
  8. B transferase] [Contains: Fucosylglycoprotein alpha-N- acetylgalactosaminyltransferase
  9. Fucosylglycoprotein alpha-N- acetylgalactosaminyltransferase soluble form]
Enzyme 49 Gene Name ABO
Enzyme 49 Protein Sequence >Histo-blood group ABO system transferase
MAEVLRTLAGKPKCHALRPMILFLIMLVLVLFGYGVLSPRSLMPGSLERGFCMAVREPDH
LQRVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTV
FAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQLSVLEVRAYKR
WQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSS
REAFTYERRPQSQAYIPKDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVW
HDESHLNKYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP
Enzyme 49 Number of Residues 354
Enzyme 49 Molecular Weight 40934
Enzyme 49 Theoretical pI 9.24
Enzyme 49 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • cell
  • membrane
Enzyme 49 General Function Not Available
Enzyme 49 Specific Function This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens:A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity
Enzyme 49 Pathways
  • Blood group glycolipid biosynthesis-neolactoseries (map00602 Link Image)
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
Enzyme 49 Reactions
  • UDP-N-acetyl-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)-[alpha-L-fucosyl-(1,2)]-D-galactose
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • 1-35
Enzyme 49 Transmembrane Regions Not Available
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 340078 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID P16442 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name BGAT_HUMAN Link Image
Enzyme 49 PDB ID 1LZI Link Image
Enzyme 49 PDB File Show
Enzyme 49 3D Structure
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >1062 bp
ATGGCCGAGGTGTTGCGGACGCTGGCCGGAAAACCAAAATGCCACGCACTTCGACCTATG
ATCCTTTTCCTAATAATGCTTGTCTTGGTCTTGTTTGGTTACGGGGTCCTAAGCCCCAGA
AGTCTAATGCCAGGAAGCCTGGAACGGGGGTTCTGCATGGCTGTTAGGGAACCTGACCAT
CTGCAGCGCGTCTCGTTGCCAAGGATGGTCTACCCCCAGCCAAAGGTGCTGACACCGTGG
AAGGATGTCCTCGTGGTGACCCCTTGGCTGGCTCCCATTGTCTGGGAGGGCACATTCAAC
ATCGACATCCTCAACGAGCAGTTCAGGCTCCAGAACACCACCATTGGGTTAACTGTGTTT
GCCATCAAGAAATACGTGGCTTTCCTGAAGCTGTTCCTGGAGACGGCGGAGAAGCACTTC
ATGGTGGGCCACCGTGTCCACTACTATGTCTTCACCGACCAGCTGGCCGCGGTGCCCCGC
GTGACGCTGGGGACCGGTCGGCAGCTGTCAGTGCTGGAGGTGCGCGCCTACAAGCGCTGG
CAGGACGTGTCCATGCGCCGCATGGAGATGATCAGTGACTTCTGCGAGCGGCGCTTCCTC
AGCGAGGTGGATTACCTGGTGTGCGTGGACGTGGACATGGAGTTCCGCGACCACGTGGGC
GTGGAGATCCTGACTCCGCTGTTCGGCACCCTGCACCCCGGCTTCTACGGAAGCAGCCGG
GAGGCCTTCACCTACGAGCGCCGGCCCCAGTCCCAGGCCTACATCCCCAAGGACGAGGGC
GATTTCTACTACCTGGGGGGGTTCTTCGGGGGGTCGGTGCAAGAGGTGCAGCGGCTCACC
AGGGCCTGCCACCAGGCCATGATGGTCGACCAGGCCAACGGCATCGAGGCCGTGTGGCAC
GACGAGAGCCACCTGAACAAGTACCTGCTGCGCCACAAACCCACCAAGGTGCTCTCCCCC
GAGTACTTGTGGGACCAGCAGCTGCTGGGCTGGCCCGCCGTCCTGAGGAAGCTGAGGTTC
ACTGCGGTGCCCAAGAACCACCAGGCGGTCCGGAACCCGTGA
Enzyme 49 GenBank Gene ID J05175 Link Image
Enzyme 49 GeneCard ID ABO Link Image
Enzyme 49 GenAtlas ID ABO Link Image
Enzyme 49 HGNC ID HGNC:79 Link Image
Enzyme 49 Chromosome Location 9
Enzyme 49 Locus 9q34.1-q34.2
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 General References
  1. Yamamoto F, Marken J, Tsuji T, White T, Clausen H, Hakomori S: Cloning and characterization of DNA complementary to human UDP-GalNAc: Fuc alpha 1----2Gal alpha 1----3GalNAc transferase (histo-blood group A transferase) mRNA. J Biol Chem. 1990 Jan 15;265(2):1146-51. [PubMed Link Image]
  2. Yamamoto F, Clausen H, White T, Marken J, Hakomori S: Molecular genetic basis of the histo-blood group ABO system. Nature. 1990 May 17;345(6272):229-33. [PubMed Link Image]
  3. Bennett EP, Steffensen R, Clausen H, Weghuis DO, van Kessel AG: Genomic cloning of the human histo-blood group ABO locus. Biochem Biophys Res Commun. 1995 Jan 5;206(1):318-25. [PubMed Link Image]
  4. Bennett EP, Steffensen R, Clausen H, Weghuis DO, Geurts van Kessel A: Genomic cloning of the human histo-blood group ABO locus. Biochem Biophys Res Commun. 1995 Jun 6;211(1):347. [PubMed Link Image]
  5. Olsson ML, Chester MA: Heterogeneity of the blood group Ax allele: genetic recombination of common alleles can result in the Ax phenotype. Transfus Med. 1998 Sep;8(3):231-8. [PubMed Link Image]
  6. Kominato Y, McNeill PD, Yamamoto M, Russell M, Hakomori S, Yamamoto F: Animal histo-blood group ABO genes. Biochem Biophys Res Commun. 1992 Nov 30;189(1):154-64. [PubMed Link Image]
  7. Yamamoto F, Hakomori S: Sugar-nucleotide donor specificity of histo-blood group A and B transferases is based on amino acid substitutions. J Biol Chem. 1990 Nov 5;265(31):19257-62. [PubMed Link Image]
  8. Patenaude SI, Seto NO, Borisova SN, Szpacenko A, Marcus SL, Palcic MM, Evans SV: The structural basis for specificity in human ABO(H) blood group biosynthesis. Nat Struct Biol. 2002 Sep;9(9):685-90. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 6392
Enzyme 50 Name Chondroitin sulfate synthase 3
Enzyme 50 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 50 Gene Name CSS3
Enzyme 50 Protein Sequence >Chondroitin sulfate synthase 3
MAVRSRRPWMSVALGLVLGFTAASWLIAPRVAELSERKRRGSSLCSYYGRSAAGPRAGAQ
QPLPQPQSRPRQEQSPPPARQDLQGPPLPEAAPGITSFRSSPWQQPPPLQQRRRGREPEG
ATGLPGAPAAEGEPEEEDGGAAGQRRDGRPGSSHNGSGDGGAAAPSARPRDFLYVGVMTA
QKYLGSRALAAQRTWARFIPGRVEFFSSQQPPNAGQPPPPLPVIALPGVDDSYPPQKKSF
MMIKYMHDHYLDKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQTGLGNIEELGKL
GLEPGENFCMGGPGMIFSREVLRRMVPHIGECLREMYTTHEDVEVGRCVRRFGGTQCVWS
YEMQQLFHENYEHNRKGYIQDLHNSKIHAAITLHPNKRPAYQYRLHNYMLSRKISELRYR
TIQLHRESALMSKLSNTEVSKEDQQLGVIPSFNHFQPRERNEVIEWEFLTGKLLYSAAEN
QPPRQSLSSILRTALDDTVLQVMEMINENAKSRGRLIDFKEIQYGYRRVNPMHGVEYILD
LLLLYKRHKGRKLTVPVRRHAYLQQLFSKPFFRETEELDVNSLVESINSETQSFSFISNS
LKILSSFQGAKEMGGHNEKKVHILVPLIGRYDIFLRFMENFENMCLIPKQNVKLVIILFS
RDSGQDSSKHIELIKGYQNKYPKAEMTLIPMKGEFSRGLGLEMASAQFDNDTLLLFCDVD
LIFREDFLQRCRDNTIQGQQVYYPIIFSQYDPKVTNGGNPPTDDYFIFSKKTGFWRDYGY
GITCIYKSDLLGAGGFDTSIQGWGLEDVDLYNKVILSGLRPFRSQEVGVVHIFHPVHCDP
NLDPKQYKMCLGSKASTFASTMQLAELWLEKHLGVRYNRTLS
Enzyme 50 Number of Residues 882
Enzyme 50 Molecular Weight 100286
Enzyme 50 Theoretical pI 8.97
Enzyme 50 GO Classification Not Available
Enzyme 50 General Function Not Available
Enzyme 50 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 50 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 50 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 50 Pfam Domain Function
Enzyme 50 Signals
  • 1-23
Enzyme 50 Transmembrane Regions Not Available
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 37573674 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q70JA7 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name CHSS3_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 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 50 GenBank Gene ID AB086062 Link Image
Enzyme 50 GeneCard ID Not Available
Enzyme 50 GenAtlas ID Not Available
Enzyme 50 HGNC ID Not Available
Enzyme 50 Chromosome Location 5
Enzyme 50 Locus 5q23.3
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 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 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 6393
Enzyme 51 Name Chondroitin sulfate synthase 2
Enzyme 51 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 51 Gene Name CSS2
Enzyme 51 Protein Sequence >Chondroitin sulfate synthase 2
MRASLLLSVLRPAGPVAVGISLGFTLSLLSVTWVEEPCGPGPPQPGDSELPPRGNTNAAR
RPNSVQPGAEREKPGAGEGAGENWEPRVLPYHPAQPGQAAKKAVRTRYISTELGIRQRLL
VAVLTSQTTLPTLGVAVNRTLGHRLERVVFLTGARGRRAPPGMAVVTLGEERPIGHLHLA
LRHLLEQHGDDFDWFFLVPDTTYTEAHGLARLTGHLSLASAAHLYLGRPQDFIGGEPTPG
RYCHGGFGVLLSRMLLQQLRPHLEGCRNDIVSARPDEWLGRCILDATGVGCTGDHEGVHY
SHLELSPGEPVQEGDPHFRSALTAHPVRDPVHMYQLHKAFARAELERTYQEIQELQWEIQ
NTSHLAVDGDRAAAWPVGIPAPSRPASRFEVLRWDYFTEQHAFSCADGSPRCPLRGADRA
DVADVLGTALEELNRRYHPALRLQKQQLVNGYRRFDPARGMEYTLDLQLEALTPQGGRRP
LTRRVQLLRPLSRVEILPVPYVTEASRLTVLLPLAAAERDLAPGFLEAFATAALEPGDAA
AALTLLLLYEPRQAQRVAHADVFAPVKAHVAELERRFPGARVPWLSVQTAAPSPLRLMDL
LSKKHPLDTLFLLAGPDTVLTPDFLNRCRMHAISGWQAFFPMHFQAFHPAVAPPQGPGPP
ELGRDTGRFDRQAASEACFYNSDYVAARGRLAAASEQEEELLESLDVYELFLHFSSLHVL
RAVEPALLQRYRAQTCSARLSEDLYHRCLQSVLEGLGSRTQLAMLLFEQEQGNST
Enzyme 51 Number of Residues 775
Enzyme 51 Molecular Weight 85496
Enzyme 51 Theoretical pI 6.99
Enzyme 51 GO Classification Not Available
Enzyme 51 General Function Not Available
Enzyme 51 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 51 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 51 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 51 Pfam Domain Function
Enzyme 51 Signals
  • 1-34
Enzyme 51 Transmembrane Regions Not Available
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 32170677 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID Q8IZ52 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name CHSS2_HUMAN Link Image
Enzyme 51 PDB ID Not Available
Enzyme 51 Cellular Location Not Available
Enzyme 51 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 51 GenBank Gene ID AB095813 Link Image
Enzyme 51 GeneCard ID Not Available
Enzyme 51 GenAtlas ID Not Available
Enzyme 51 HGNC ID Not Available
Enzyme 51 Chromosome Location Not Available
Enzyme 51 Locus Not Available
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 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 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 6394
Enzyme 52 Name Chondroitin sulfate synthase 1
Enzyme 52 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 52 Gene Name CHSY1
Enzyme 52 Protein Sequence >Chondroitin sulfate synthase 1
MAARGRRAWLSVLLGLVLGFVLASRLVLPRASELKRAGPRRRASPEGCRSGQAAASQAGG
ARGDARGAQLWPPGSDPDGGPRDRNFLFVGVMTAQKYLQTRAVAAYRTWSKTIPGKVQFF
SSEGSDTSVPIPVVPLRGVDDSYPPQKKSFMMLKYMHDHYLDKYEWFMRADDDVYIKGDR
LENFLRSLNSSEPLFLGQTGLGTTEEMGKLALEPGENFCMGGPGVIMSREVLRRMVPHIG
KCLREMYTTHEDVEVGRCVRRFAGVQCVWSYEMQQLFYENYEQNKKGYIRDLHNSKIHQA
ITLHPNKNPPYQYRLHSYMLSRKISELRHRTIQLHREIVLMSKYSNTEIHKEDLQLGIPP
SFMRFQPRQREEILEWEFLTGKYLYSAVDGQPPRRGMDSAQREALDDIVMQVMEMINANA
KTRGRIIDFKEIQYGYRRVNPMYGAEYILDLLLLYKKHKGKKMTVPVRRHAYLQQTFSKI
QFVEHEELDAQELAKRINQESGSLSFLSNSLKKLVPFQLPGSKSEHKEPKDKKINILIPL
SGRFDMFVRFMGNFEKTCLIPNQNVKLVVLLFNSDSNPDKAKQVELMRDYRIKYPKADMQ
ILPVSGEFSRALALEVGSSQFNNESLLFFCDVDLVFTTEFLQRCRANTVLGQQIYFPIIF
SQYDPKIVYSGKVPSDNHFAFTQKTGFWRNYGFGITCIYKGDLVRVGGFDVSIQGWGLED
VDLFNKVVQAGLKTFRSQEVGVVHVHHPVFCDPNLDPKQYKMCLGSKASTYGSTQQLAEM
WLEKNDPSYSKSSNNNGSVRTA
Enzyme 52 Number of Residues 802
Enzyme 52 Molecular Weight 91786
Enzyme 52 Theoretical pI 9.63
Enzyme 52 GO Classification Not Available
Enzyme 52 General Function Not Available
Enzyme 52 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 52 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 52 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 52 Pfam Domain Function
Enzyme 52 Signals
  • 1-23
Enzyme 52 Transmembrane Regions Not Available
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 15617453 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID Q86X52 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name CHSS1_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 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 52 GenBank Gene ID AB071402 Link Image
Enzyme 52 GeneCard ID CHSY1 Link Image
Enzyme 52 GenAtlas ID CHSY1 Link Image
Enzyme 52 HGNC ID HGNC:17198 Link Image
Enzyme 52 Chromosome Location 15
Enzyme 52 Locus 15q26.3
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 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 cl