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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 Link Image
SDF File Show Link Image
PDB File Show Link Image
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. Ectonucleoside triphosphate diphosphohydrolase 3
  4. Nucleoside diphosphate kinase, mitochondrial
  5. Ribonucleoside-diphosphate reductase large subunit
  6. Nucleoside diphosphate kinase A
  7. Ribonucleoside-diphosphate reductase subunit M2
  8. Nucleoside diphosphate kinase B
  9. Nucleoside diphosphate kinase 6
  10. Beta-1,4-galactosyltransferase 2
  11. Alpha-lactalbumin
  12. Beta-1,4-galactosyltransferase 1
  13. UDP-glucuronosyltransferase 2B28
  14. UDP-glucuronosyltransferase 2B4
  15. UDP-glucuronosyltransferase 1-4
  16. UDP-glucuronosyltransferase 2B7
  17. UDP-glucuronosyltransferase 2B15
  18. UDP-glucuronosyltransferase 2A1
  19. UDP-glucuronosyltransferase 1-1
  20. UDP-glucuronosyltransferase 1-9
  21. UDP-glucuronosyltransferase 1-3
  22. UDP-glucuronosyltransferase 2B17
  23. UDP-glucuronosyltransferase 1-6
  24. UDP-glucuronosyltransferase 1-5
  25. UDP-glucuronosyltransferase 2B11
  26. GTP:AMP phosphotransferase, mitochondrial
  27. 6-phosphofructokinase type C
  28. 6-phosphofructokinase, liver type
  29. 6-phosphofructokinase, muscle type
  30. Pyruvate kinase isozymes M1/M2
  31. Pyruvate kinase isozymes R/L
  32. Ceramide glucosyltransferase
  33. Beta-1,4 N-acetylgalactosaminyltransferase 1
  34. Lactosylceramide 4-alpha-galactosyltransferase
  35. Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
  36. Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
  37. Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
  38. Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
  39. Dolichyl-phosphate beta-glucosyltransferase
  40. Polypeptide N-acetylgalactosaminyltransferase 4
  41. Polypeptide N-acetylgalactosaminyltransferase 3
  42. Probable polypeptide N-acetylgalactosaminyltransferase 8
  43. Polypeptide N-acetylgalactosaminyltransferase-like protein 2
  44. Polypeptide N-acetylgalactosaminyltransferase 10
  45. Putative polypeptide N-acetylgalactosaminyltransferase-like protein 4
  46. N-acetylgalactosaminyltransferase 7
  47. Polypeptide N-acetylgalactosaminyltransferase 6
  48. Polypeptide N-acetylgalactosaminyltransferase 14
  49. Polypeptide N-acetylgalactosaminyltransferase 2
  50. Polypeptide N-acetylgalactosaminyltransferase 12
  51. Polypeptide N-acetylgalactosaminyltransferase 1
  52. Beta-1,4-galactosyltransferase 3
  53. UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1
  54. Glycogen [starch] synthase, liver
  55. Glycogenin-1
  56. Glycogen [starch] synthase, muscle
  57. Glycogenin-2
  58. Histo-blood group ABO system transferase
  59. 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
  60. Chondroitin sulfate synthase 3
  61. Chondroitin sulfate synthase 2
  62. Chondroitin sulfate synthase 1
  63. Polyribonucleotide nucleotidyltransferase 1, mitochondrial
  64. Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
  65. Exostosin-1
  66. Hyaluronan synthase 1
  67. Exostosin-like 3
  68. Exostosin-2
  69. Exostosin-like 1
  70. N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase
  71. Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
  72. UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
  73. Hyaluronan synthase 3
  74. Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
  75. Hyaluronan synthase 2
  76. Uridine-cytidine kinase 2
  77. N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase, isoform B
  78. Chondroitin sulfate glucuronyltransferase
  79. OTTHUMP00000018263
  80. Polypeptide N-acetylgalactosaminyltransferase 13
  81. ENTPD4 protein
  82. Beta-1,3-N-acetylglucosaminyltransferase bGnT-2
  83. Polypeptide N-acetylgalactosaminyltransferase 9
  84. Exostosin-like 2
  85. Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
  86. Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
  87. UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
  88. UDP-glucuronosyltransferase 2A3
  89. Ribonucleoside-diphosphate reductase subunit M2 B
  90. UMP-CMP kinase 2, mitochondrial
  91. Uridine-cytidine kinase-like 1
  92. Ectonucleoside triphosphate diphosphohydrolase 8
  93. Polypeptide N-acetylgalactosaminyltransferase-like 6
  94. Putative polypeptide N-acetylgalactosaminyltransferase-like protein 5
  95. HCG2039726, isoform CRA_f
  96. HCG2039726, isoform CRA_e
  97. UDP glycosyltransferase 1 family polypeptide A7
  98. cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b)
  99. 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)
  100. Uridine kinase
  101. Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
  102. Ectonucleoside triphosphate diphosphohydrolase 5
  103. cDNA FLJ75238, highly similar to Homo sapiens asparagine-linked glycosylation 14 homolog (yeast) (ALG14), mRNA (Asparagine-linked glycosylation 14 homolog (Yeast), isoform CRA_b)
  104. HCG2018639
  105. Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase, isoform CRA_a
  106. UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 5 (GalNAc-T5)
  107. 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)
  108. Pp-GalNAc-transferase 20
  109. 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)
  110. cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
  111. cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
  112. cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
  113. 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)
  114. cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-)
  115. UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4
  116. Glycosyltransferase 28 domain containing 1, isoform CRA_b
  117. 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)
  118. cDNA, FLJ93340, Homo sapiens exostoses (multiple)-like 2 (EXTL2), mRNA (Exostoses (Multiple)-like 2, isoform CRA_a)
  119. cDNA, FLJ93616, highly similar to Homo sapiens exostoses (multiple) 1 (EXT1), mRNA (Exostoses (Multiple) 1)
  120. UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 8 (GalNAc-T8)
  121. cDNA PSEC0182 fis, clone OVARC1001636, highly similar to N-acetylgalactosaminyltransferase 7 (EC 2.4.1.-)
  122. cDNA FLJ42944 fis, clone BRSTN2004863, highly similar to PolypeptideN-acetylgalactosaminyltransferase 11 (EC 2.4.1.41)
  123. cDNA FLJ46085 fis, clone TESTI2007490, highly similar to 2-hydroxyacylsphingosine1-beta-galactosyltransferase (EC 2.4.1.45)
  124. cDNA FLJ90831 fis, clone Y79AA1001795, highly similar to Beta-1,3-galactosyltransferase 4 (EC 2.4.1.62)
  125. Chondroitin synthase-3 (Chondroitin sulfate glucuronyltransferase, isoform CRA_b)
  126. cDNA, FLJ93377, Homo sapiens alpha 1,4-galactosyltransferase (A4GALT), mRNA (Alpha 1,4-galactosyltransferase) (Globotriaosylceramide synthase)
  127. UDP-N-acetylglucosamine transferase subunit ALG13 homolog
Enzyme 1 [top]
Enzyme 1 ID 5313
Enzyme 1 Name Ectonucleoside triphosphate diphosphohydrolase 1
Enzyme 1 Synonyms
  1. NTPDase 1
  2. Ecto-ATP diphosphohydrolase 1
  3. Ecto-ATPDase 1
  4. Ecto-ATPase 1
  5. Ecto-apyrase
  6. Lymphoid cell activation antigen
  7. 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 57964.1
Enzyme 1 Theoretical pI 6.29
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 1 General Function Involved in hydrolase activity
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 [RN:R00085]
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 45580700 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 NM_001776.5 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 1
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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  6. 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]
  7. 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]
  8. 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]
  9. Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed Link Image]
  10. 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]
  11. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
  12. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed 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 MAPK-activating protein PM09
  4. Putative NF-kappa-B-activating protein 107
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 44839.2
Enzyme 2 Theoretical pI 5.98
Enzyme 2 GO Classification
Function
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • hydrolase activity
  • hydrolase activity, acting on acid anhydrides
  • hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
  • ion binding
  • metal ion binding
  • pyrophosphatase activity
Process
Component
Enzyme 2 General Function Involved in calcium ion binding
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 [RN:R00329]
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 229577440 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 >1206 bp
ATGCCCGTGCAGCTGTCTGAGCACCCGGAATGGAATGAGTCTATGCACTCCCTCCGGATC
AGTGTGGGGGGCCTTCCTGTGCTGGCGTCCATGACCAAGGCCGCGGACCCCCGCTTCCGC
CCCCGCTGGAAGGTGATCCTGACGTTCTTTGTGGGTGCTGCCATCCTCTGGCTGCTCTGC
TCCCACCGCCCGGCCCCCGGCAGGCCCCCCACCCACAATGCACACAACTGGAGGCTCGGC
CAGGCGCCCGCCAACTGGTACAATGACACCTACCCCCTGTCTCCCCCACAAAGGACACCG
GCTGGGATTCGGTATCGAATCGCAGTTATCGCAGACCTGGACACAGAGTCAAGGGCCCAA
GAGGAAAACACCTGGTTCAGTTACCTGAAAAAGGGCTACCTGACCCTGTCAGACAGTGGG
GACAAGGTGGCCGTGGAATGGGACAAAGACCATGGGGTCCTGGAGTCCCACCTGGCGGAG
AAGGGGAGAGGCATGGAGCTATCCGACCTGATTGTTTTCAATGGGAAACTCTACTCCGTG
GATGACCGGACGGGGGTCGTCTACCAGATCGAAGGCAGCAAAGCCGTGCCCTGGGTGATT
CTGTCCGACGGCGACGGCACCGTGGAGAAAGGCTTCAAGGCCGAATGGCTGGCAGTGAAG
GACGAGCGTCTGTACGTGGGCGGCCTGGGCAAGGAGTGGACGACCACTACGGGTGATGTG
GTGAACGAGAACCCGGAGTGGGTGAAGGTGGTGGGCTACAAGGGCAGCGTGGACCACGAG
AACTGGGTGTCCAACTACAACGCCCTGCGGGCTGCTGCCGGCATCCAGCCGCCAGGCTAC
CTCATCCATGAGTCTGCCTGCTGGAGTGACACGCTGCAGCGCTGGTTCTTCCTGCCGCGC
CGCGCCAGCCAGGAGCGCTACAGCGAGAAGGACGACGAGCGCAAGGGCGCCAACCTGCTG
CTGAGCGCCTCCCCTGACTTCGGCGACATCGCTGTGAGCCACGTCGGGGCGGTGGTCCCC
ACTCACGGCTTCTCGTCCTTCAAGTTCATCCCCAACACCGACGACCAGATCATTGTGGCC
CTCAAATCCGAGGAGGACAGCGGCAGAGTCGCCTCCTACATCATGGCCTTCACGCTGGAC
GGGCGCTTCCTGTTGCCGGAGACCAAGATCGGAAGCGTGAAATACGAAGGCATCGAGTTC
ATTTAA
Enzyme 2 GenBank Gene ID NM_001159772.1 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 1
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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Yang M, Kirley TL: Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1): identification of residues essential for enzyme activity and the Ca(2+)-induced conformational change. Biochemistry. 2004 Jul 20;43(28):9185-94. [PubMed Link Image]
  7. Dai J, Liu J, Deng Y, Smith TM, Lu M: Structure and protein design of a human platelet function inhibitor. Cell. 2004 Mar 5;116(5):649-59. [PubMed Link Image]
  8. Huber C, Oules B, Bertoli M, Chami M, Fradin M, Alanay Y, Al-Gazali LI, Ausems MG, Bitoun P, Cavalcanti DP, Krebs A, Le Merrer M, Mortier G, Shafeghati Y, Superti-Furga A, Robertson SP, Le Goff C, Muda AO, Paterlini-Brechot P, Munnich A, Cormier-Daire V: Identification of CANT1 mutations in Desbuquois dysplasia. Am J Hum Genet. 2009 Nov;85(5):706-10. Epub 2009 Oct 22. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 5318
Enzyme 3 Name Ectonucleoside triphosphate diphosphohydrolase 3
Enzyme 3 Synonyms
  1. NTPDase 3
  2. CD39 antigen-like 3
  3. Ecto-ATP diphosphohydrolase 3
  4. Ecto-ATPDase 3
  5. Ecto-ATPase 3
  6. Ecto-apyrase 3
  7. HB6
Enzyme 3 Gene Name ENTPD3
Enzyme 3 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 3
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Enzyme 3 Number of Residues 529
Enzyme 3 Molecular Weight 59104.8
Enzyme 3 Theoretical pI 6.40
Enzyme 3 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 3 General Function Involved in hydrolase activity
Enzyme 3 Specific Function Has a threefold preference for the hydrolysis of ATP over ADP
Enzyme 3 Pathways
Enzyme 3 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 23-43 486-506
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 13817037 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID O75355 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name ENTP3_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1590 bp
ATGTTCACTGTGCTGACCCGCCAACCATGTGAGCAAGCAGGCCTCAAGGCCCTCTACCGA
ACTCCAACCATCATTGCCTTGGTGGTCTTGCTTGTGAGTATTGTGGTACTTGTGAGTATC
ACTGTCATCCAGATCCACAAGCAAGAGGTCCTCCCTCCAGGACTGAAGTATGGTATTGTG
CTGGATGCCGGGTCTTCAAGAACCACAGTCTACGTGTATCAATGGCCAGCAGAAAAAGAG
AATAATACCGGAGTGGTCAGTCAAACCTTCAAATGTAGTGTGAAAGGCTCTGGAATCTCC
AGCTATGGAAATAACCCCCAAGATGTCCCCAGAGCCTTTGAGGAGTGTATGCAAAAAGTC
AAGGGGCAGGTTCCATCCCACCTCCACGGATCCACCCCCATTCACCTGGGAGCCACGGCT
GGGATGCGCTTGCTGAGGTTGCAAAATGAAACAGCAGCTAATGAAGTCCTTGAAAGCATC
CAAAGCTACTTCAAGTCCCAGCCCTTTGACTTTAGGGGTGCTCAAATCATTTCTGGGCAA
GAAGAAGGGGTATATGGATGGATTACAGCCAACTATTTAATGGGAAATTTCCTGGAGAAG
AACCTGTGGCACATGTGGGTGCACCCGCATGGAGTGGAAACCACGGGTGCCCTGGACTTA
GGTGGTGCCTCCACCCAAATATCCTTCGTGGCAGGAGAGAAGATGGATCTGAACACCAGC
GACATCATGCAGGTGTCCCTGTATGGCTACGTATACACGCTCTACACACACAGCTTCCAG
TGCTATGGCCGGAATGAGGCTGAGAAGAAGTTTCTGGCAATGCTCCTGCAGAATTCTCCT
ACCAAAAACCATCTCACCAATCCCTGTTACCCTCGGGATTATAGCATCAGCTTCACCATG
GGCCATGTATTTGATAGCCTGTGCACTGTGGACCAGAGGCCAGAAAGTTATAACCCCAAT
GATGTCATCACTTTTGAAGGAACTGGGGACCCATCTCTGTGTAAGGAGAAGGTGGCTTCC
ATATTTGACTTCAAAGCTTGCCATGATCAAGAAACCTGTTCTTTTGATGGGGTTTATCAG
CCAAAGATTAAAGGGCCATTTGTGGCTTTTGCAGGATTCTACTACACAGCCAGTGCTTTA
AATCTTTCAGGTAGCTTTTCCCTGGACACCTTCAACTCCAGCACCTGGAATTTCTGCTCA
CAGAATTGGAGTCAGCTCCCACTGCTGCTCCCCAAATTTGATGAGGTATATGCCCGCTCT
TACTGCTTCTCAGCCAACTACATCTACCACTTGTTTGTGAACGGTTACAAATTCACAGAG
GAGACTTGGCCCCAAATACACTTTGAAAAAGAAGTGGGGAATAGCAGCATAGCCTGGTCT
CTTGGCTACATGCTCAGCCTGACCAACCAGATCCCAGCTGAAAGCCCTCTGATCCGTCTG
CCCATAGAACCACCTGTCTTTGTGGGCACCCTCGCTTTCTTCACAGCGGCAGCCTTGCTG
TGTCTGGCATTTCTTGCATACCTGTGTTCAGCAACCAGAAGAAAGAGGCACTCCGAGCAT
GCCTTTGACCATGCAGTGGATTCTGACTGA
Enzyme 3 GenBank Gene ID AF034840 Link Image
Enzyme 3 GeneCard ID ENTPD3 Link Image
Enzyme 3 GenAtlas ID ENTPD3 Link Image
Enzyme 3 HGNC ID HGNC:3365 Link Image
Enzyme 3 Chromosome Location 3
Enzyme 3 Locus 3p21.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed Link Image]
  2. Smith TM, Kirley TL: Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases1. Biochim Biophys Acta. 1998 Jul 28;1386(1):65-78. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Smith TM, Lewis Carl SA, Kirley TL: Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase. Biochemistry. 1999 May 4;38(18):5849-57. [PubMed Link Image]
  5. Yang F, Hicks-Berger CA, Smith TM, Kirley TL: Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions. Biochemistry. 2001 Apr 3;40(13):3943-50. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 5338
Enzyme 4 Name Nucleoside diphosphate kinase, mitochondrial
Enzyme 4 Synonyms
  1. NDK
  2. NDP kinase, mitochondrial
  3. Nucleoside diphosphate kinase D
  4. NDPKD
  5. nm23-H4
Enzyme 4 Gene Name NME4
Enzyme 4 Protein Sequence >Nucleoside diphosphate kinase, mitochondrial
MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQR
FERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRAS
RAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQ
HSSIHPA
Enzyme 4 Number of Residues 187
Enzyme 4 Molecular Weight 20658.5
Enzyme 4 Theoretical pI 10.75
Enzyme 4 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 4 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 4 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP
Enzyme 4 Pathways
Enzyme 4 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 14336697 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O00746 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name NDKM_HUMAN Link Image
Enzyme 4 PDB ID 1EHW Link Image
Enzyme 4 PDB File Show
Enzyme 4 3D Structure
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >564 bp
ATGGGCGGCCTCTTCTGGCGCTCCGCGCTGCGGGGGCTGCGCTGCGGCCCGCGGGCCCCG
GGCCCGAGCCTGCTAGTGCGCCACGGCTCGGGAGGGCCCTCCTGGACCCGGGAGCGGACC
CTGGTGGCGGTGAAGCCCGATGGCGTGCAACGGCGGCTCGTTGGGGACGTGATCCAGCGC
TTTGAGAGGCGGGGCTTCACGCTGGTGGGGATGAAGATGCTGCAGGCACCAGAGAGCGTC
CTTGCCGAGCACTACCAGGACCTGCGGAGGAAGCCCTTCTACCCTGCCCTCATCCGCTAC
ATGAGCTCTGGGCCTGTGGTGGCCATGGTCTGGGAAGGGTACAATGTCGTCCGCGCCTCG
AGGGCCATGATTGGACACACCGACTCGGCTGAGGCTGCCCCAGGAACCATAAGGGGTGAC
TTCAGCGTCCACATCAGCAGGAATGTCATCCACGCCAGCGACTCCGTGGAGGGGGCCCAG
CGGGAGATCCAGCTGTGGTTCCAGAGCAGTGAGCTGGTGAGCTGGGCAGACGGGGGCCAG
CACAGCAGCATCCACCCAGCCTGA
Enzyme 4 GenBank Gene ID AE006463 Link Image
Enzyme 4 GeneCard ID NME4 Link Image
Enzyme 4 GenAtlas ID NME4 Link Image
Enzyme 4 HGNC ID HGNC:7852 Link Image
Enzyme 4 Chromosome Location 1
Enzyme 4 Locus 16p13.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 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. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 5340
Enzyme 5 Name Ribonucleoside-diphosphate reductase large subunit
Enzyme 5 Synonyms
  1. Ribonucleoside-diphosphate reductase subunit M1
  2. Ribonucleotide reductase large subunit
Enzyme 5 Gene Name RRM1
Enzyme 5 Protein Sequence >Ribonucleoside-diphosphate reductase large subunit
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS
Enzyme 5 Number of Residues 792
Enzyme 5 Molecular Weight 90069.4
Enzyme 5 Theoretical pI 7.16
Enzyme 5 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH or CH2 groups
  • oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
  • protein binding
  • purine nucleoside binding
  • ribonucleoside-diphosphate reductase activity
Process
  • DNA metabolic process
  • DNA replication
  • cellular macromolecule metabolic process
  • macromolecule metabolic process
  • metabolic process
  • oxidation reduction
Component
  • macromolecular complex
  • protein complex
  • ribonucleoside-diphosphate reductase complex
Enzyme 5 General Function Involved in oxidation reduction
Enzyme 5 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides
Enzyme 5 Pathways
Enzyme 5 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • None
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 36065 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID P23921 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name RIR1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 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 5 GenBank Gene ID X59543 Link Image
Enzyme 5 GeneCard ID RRM1 Link Image
Enzyme 5 GenAtlas ID RRM1 Link Image
Enzyme 5 HGNC ID HGNC:10451 Link Image
Enzyme 5 Chromosome Location 1
Enzyme 5 Locus 11p15.5
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Harrington JA, Spector T: Human ribonucleotide reductase. Activation and inhibition by analogs of ATP. Biochem Pharmacol. 1991 Jul 25;42(4):759-63. [PubMed Link Image]
  7. Xue L, Zhou B, Liu X, Qiu W, Jin Z, Yen Y: Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. Cancer Res. 2003 Mar 1;63(5):980-6. [PubMed Link Image]
  8. Qiu W, Zhou B, Darwish D, Shao J, Yen Y: Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. Biochem Biophys Res Commun. 2006 Feb 10;340(2):428-34. Epub 2005 Dec 15. [PubMed Link Image]
  9. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 5341
Enzyme 6 Name Nucleoside diphosphate kinase A
Enzyme 6 Synonyms
  1. NDK A
  2. NDP kinase A
  3. Granzyme A-activated DNase
  4. GAAD
  5. Metastasis inhibition factor nm23
  6. Tumor metastatic process-associated protein
  7. nm23-H1
Enzyme 6 Gene Name NME1
Enzyme 6 Protein Sequence >Nucleoside diphosphate kinase A
MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPF
FAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVESAEKEIGLWFHPEELVDYTSCAQNWIYE
Enzyme 6 Number of Residues 152
Enzyme 6 Molecular Weight 17148.6
Enzyme 6 Theoretical pI 6.11
Enzyme 6 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 6 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 6 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein- coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination
Enzyme 6 Pathways
Enzyme 6 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 4557797 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID P15531 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name NDKA_HUMAN Link Image
Enzyme 6 PDB ID 1JXV Link Image
Enzyme 6 PDB File Show
Enzyme 6 3D Structure
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >459 bp
ATGGCCAACTGTGAGCGTACCTTCATTGCGATCAAACCAGATGGGGTCCAGCGGGGTCTT
GTGGGAGAGATTATCAAGCGTTTTGAGCAGAAAGGATTCCGCCTTGTTGGTCTGAAATTC
ATGCAAGCTTCCGAAGATCTTCTCAAGGAACACTACGTTGACCTGAAGGACCGTCCATTC
TTTGCCGGCCTGGTGAAATACATGCACTCAGGGCCGGTAGTTGCCATGGTCTGGGAGGGG
CTGAATGTGGTGAAGACGGGCCGAGTCATGCTCGGGGAGACCAACCCTGCAGACTCCAAG
CCTGGGACCATCCGTGGAGACTTCTGCATACAAGTTGGCAGGAACATTATACATGGCAGT
GATTCTGTGGAGAGTGCAGAGAAGGAGATCGGCTTGTGGTTTCACCCTGAGGAACTGGTA
GATTACACGAGCTGTGCTCAGAACTGGATCTATGAATGA
Enzyme 6 GenBank Gene ID NM_000269.2 Link Image
Enzyme 6 GeneCard ID NME1 Link Image
Enzyme 6 GenAtlas ID NME1 Link Image
Enzyme 6 HGNC ID HGNC:7849 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 17q21.3
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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. 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]
  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. 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]
  5. Ni X, Gu S, Dai J, Cheng H, Guo L, Li L, Ji C, Xie Y, Ying K, Mao Y: Isolation and characterization of a novel human NM23-H1B gene, a different transcript of NM23-H1. J Hum Genet. 2003;48(2):96-100. [PubMed Link Image]
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  7. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. 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]
  10. MacDonald NJ, Freije JM, Stracke ML, Manrow RE, Steeg PS: Site-directed mutagenesis of nm23-H1. Mutation of proline 96 or serine 120 abrogates its motility inhibitory activity upon transfection into human breast carcinoma cells. J Biol Chem. 1996 Oct 11;271(41):25107-16. [PubMed Link Image]
  11. 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]
  12. 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]
  13. Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed Link Image]
  14. Meierhofer D, Wang X, Huang L, Kaiser P: Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry. J Proteome Res. 2008 Oct;7(10):4566-76. Epub 2008 Sep 10. [PubMed Link Image]
  15. Garzia L, D'Angelo A, Amoresano A, Knauer SK, Cirulli C, Campanella C, Stauber RH, Steegborn C, Iolascon A, Zollo M: Phosphorylation of nm23-H1 by CKI induces its complex formation with h-prune and promotes cell motility. Oncogene. 2008 Mar 20;27(13):1853-64. Epub 2007 Oct 1. [PubMed Link Image]
  16. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  17. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  18. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  19. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  20. 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]
  21. 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]
  22. 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 5343
Enzyme 7 Name Ribonucleoside-diphosphate reductase subunit M2
Enzyme 7 Synonyms
  1. Ribonucleotide reductase small chain
  2. Ribonucleotide reductase small subunit
Enzyme 7 Gene Name RRM2
Enzyme 7 Protein Sequence >Ribonucleoside-diphosphate reductase subunit M2
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF
Enzyme 7 Number of Residues 389
Enzyme 7 Molecular Weight 44877.2
Enzyme 7 Theoretical pI 5.05
Enzyme 7 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH or CH2 groups
  • oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
  • ribonucleoside-diphosphate reductase activity
  • transition metal ion binding
Process
  • cellular nitrogen compound metabolic process
  • deoxyribonucleoside diphosphate metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside diphosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • oxidation reduction
Component
Enzyme 7 General Function Involved in oxidoreductase activity
Enzyme 7 Specific Function Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling
Enzyme 7 Pathways
Enzyme 7 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294]
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 36155 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID P31350 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name RIR2_HUMAN Link Image
Enzyme 7 PDB ID 1H0N Link Image
Enzyme 7 PDB File Show
Enzyme 7 3D Structure
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID X59618 Link Image
Enzyme 7 GeneCard ID RRM2 Link Image
Enzyme 7 GenAtlas ID RRM2 Link Image
Enzyme 7 HGNC ID HGNC:10452 Link Image
Enzyme 7 Chromosome Location 2
Enzyme 7 Locus 2p25-p24
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  7. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  8. Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed Link Image]
  9. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  12. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  13. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 5344
Enzyme 8 Name Nucleoside diphosphate kinase B
Enzyme 8 Synonyms
  1. NDK B
  2. NDP kinase B
  3. C-myc purine-binding transcription factor PUF
  4. nm23-H2
Enzyme 8 Gene Name NME2
Enzyme 8 Protein Sequence >Nucleoside diphosphate kinase B
MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPF
FPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGS
DSVKSAEKEISLWFKPEELVDYKSCAHDWVYE
Enzyme 8 Number of Residues 152
Enzyme 8 Molecular Weight 17297.9
Enzyme 8 Theoretical pI 8.69
Enzyme 8 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 8 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 8 Specific Function Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752)
Enzyme 8 Pathways
Enzyme 8 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 4467843 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID P22392 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name NDKB_HUMAN Link Image
Enzyme 8 PDB ID 1NSK Link Image
Enzyme 8 PDB File Show
Enzyme 8 3D Structure
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >459 bp
ATGGCCAACCTGGAGCGCACCTTCATCGCCATCAAGCCGGACGGCGTGCAGCGCGGCCTG
GTGGGCGAGATCATCAAGCGCTTCGAGCAGAAGGGATTCCGCCTCGTGGCCATGAAGTTC
CTCCGGGCCTCTGAAGAACACCTGAAGCAGCACTACATTGACCTGAAAGACCGACCATTC
TTCCCTGGGCTGGTGAAGTACATGAACTCAGGGCCGGTTGTGGCCATGGTCTGGGAGGGG
CTGAACGTGGTGAAGACAGGCCGAGTGATGCTTGGGGAGACCAATCCAGCAGATTCAAAG
CCAGGCACCATTCGTGGGGACTTCTGCATTCAGGTTGGCAGGAACATCATTCATGGCAGT
GATTCAGTAAAAAGTGCTGAAAAAGAAATCAGCCTATGGTTTAAGCCTGAAGAACTGGTT
GACTACAAGTCTTGTGCTCATGACTGGGTCTATGAATAA
Enzyme 8 GenBank Gene ID X58965 Link Image
Enzyme 8 GeneCard ID NME2 Link Image
Enzyme 8 GenAtlas ID NME2 Link Image
Enzyme 8 HGNC ID HGNC:7850 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 17q21.3
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References
  1. 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]
  2. 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]
  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. Valentijn LJ, Koster J, Versteeg R: Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV. Genomics. 2006 Apr;87(4):483-9. Epub 2006 Jan 25. [PubMed Link Image]
  5. Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Seifert M, Seib T, Engel M, Dooley S, Welter C: Characterization of the human nm23-H2 promoter region and localization of the microsatellite D17S396. Biochem Biophys Res Commun. 1995 Oct 24;215(3):910-4. [PubMed Link Image]
  8. Iwashita S, Fujii M, Mukai H, Ono Y, Miyamoto M: Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2. Biochem Biophys Res Commun. 2004 Aug 6;320(4):1063-8. [PubMed Link Image]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  10. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  12. 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]
  13. 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 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 5346
Enzyme 9 Name Nucleoside diphosphate kinase 6
Enzyme 9 Synonyms
  1. NDK 6
  2. NDP kinase 6
  3. Inhibitor of p53-induced apoptosis-alpha
  4. IPIA-alpha
  5. nm23-H6
Enzyme 9 Gene Name NME6
Enzyme 9 Protein Sequence >Nucleoside diphosphate kinase 6
MASILRSPQALQLTLALIKPDAVAHPLILEAVHQQILSNKFLIVRMRELLWRKEDCQRFY
REHEGRFFYQRLVEFMASGPIRAYILAHKDAIQLWRTLMGPTRVFRARHVAPDSIRGSFG
LTDTRNTTHGSDSVVSASREIAAFFPDFSEQRWYEEEEPQLRCGPVCYSPEGGVHYVAGT
GGLGPA
Enzyme 9 Number of Residues 186
Enzyme 9 Molecular Weight 21142.0
Enzyme 9 Theoretical pI 8.49
Enzyme 9 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • nucleoside diphosphate kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • CTP biosynthetic process
  • GTP biosynthetic process
  • UTP biosynthetic process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • purine nucleoside triphosphate biosynthetic process
  • purine nucleotide biosynthetic process
  • purine nucleotide metabolic process
  • purine ribonucleoside triphosphate biosynthetic process
  • pyrimidine nucleoside triphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
  • pyrimidine ribonucleoside triphosphate biosynthetic process
Component
Enzyme 9 General Function Involved in nucleoside diphosphate kinase activity
Enzyme 9 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 9 Pathways
Enzyme 9 Reactions
  • ATP + nucleoside diphosphate = ADP + nucleoside triphosphate [RN:R00331]
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 3228530 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID O75414 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name NDK6_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >561 bp
ATGGCCTCAATCTTGCGAAGCCCTCAGGCTCTCCAGCTCACTCTAGCCCTGATCAAGCCT
GACGCAGTCGCCCATCCACTGATTCTGGAGGCTGTTCATCAGCAGATTCTAAGCAACAAG
TTCCTGATTGTACGAATGAGAGAACTACTGTGGAGAAAGGAAGATTGCCAGAGGTTTTAC
CGAGAGCATGAAGGGCGTTTTTTCTATCAGAGGCTGGTGGAGTTCATGGCCAGCGGGCCA
ATCCGAGCCTACATCCTTGCCCACAAGGATGCCATCCAGCTCTGGAGGACGCTCATGGGA
CCCACCAGAGTGTTCCGAGCACGCCATGTGGCCCCAGATTCTATCCGTGGGAGTTTCGGC
CTCACTGACACCCGCAACACCACCCATGGTTCGGACTCTGTGGTTTCAGCCAGCAGAGAG
ATTGCAGCCTTCTTCCCTGACTTCAGTGAACAGCGCTGGTATGAGGAGGAAGAGCCCCAG
TTGCGCTGTGGCCCTGTGTGCTATAGCCCAGAGGGAGGTGTCCACTATGTAGCTGGAACA
GGAGGCCTAGGACCAGCCTGA
Enzyme 9 GenBank Gene ID AF051941 Link Image
Enzyme 9 GeneCard ID NME6 Link Image
Enzyme 9 GenAtlas ID NME6 Link Image
Enzyme 9 HGNC ID HGNC:20567 Link Image
Enzyme 9 Chromosome Location 3
Enzyme 9 Locus 3p21
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 5607
Enzyme 10 Name Beta-1,4-galactosyltransferase 2
Enzyme 10 Synonyms
  1. Beta-1,4-GalTase 2
  2. Beta4Gal-T2
  3. b4Gal-T2
  4. UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 2
  5. UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 2
  6. Lactose synthase A protein
  7. N-acetyllactosamine synthase
  8. Nal synthase
  9. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
  10. Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
Enzyme 10 Gene Name B4GALT2
Enzyme 10 Protein Sequence >Beta-1,4-galactosyltransferase 2
MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSARGPAHALHPAASS
SSSSSNCSRPNATASSSGLPEVPSALPGPTAPTLPPCPDSPPGLVGRLLIEFTSPMPLER
VQRENPGVLMGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPILRRQRLRYGVYV
INQHGEDTFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIA
MDKFGFRLPYAGYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPD
IRIGRYRMIKHDRDKHNEPNPQRFTKIQNTKLTMKRDGIGSVRYQVLEVSRQPLFTNITV
DIGRPPSWPPRG
Enzyme 10 Number of Residues 372
Enzyme 10 Molecular Weight 41971.8
Enzyme 10 Theoretical pI 9.66
Enzyme 10 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 10 General Function Involved in transferase activity, transferring glycosyl groups
Enzyme 10 Specific Function Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Can produce lactose
Enzyme 10 Pathways
Enzyme 10 Reactions
  • UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine [RN:R01205 R06055]
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • 16-36
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 4520136 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID O60909 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name B4GT2_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1119 bp
ATGAGCAGACTGCTGGGGGGGACGCTGGAGCGCGTCTGCAAGGCTGTGCTCCTTCTCTGC
CTGCTGCACTTCCTCGTGGCCGTCATCCTCTACTTTGACGTCTACGCCCAGCACCTGGCC
TTCTTCAGCCGCTTCAGTGCCCGAGGCCCTGCCCATGCCCTCCACCCAGCTGCTAGCAGC
AGCAGCAGCAGCAGCAACTGCTCCCGGCCCAACGCCACCGCCTCTAGCTCCGGGCTCCCT
GAGGTCCCCAGTGCCCTGCCCGGTCCCACGGCTCCCACGCTGCCACCCTGTCCTGACTCG
CCACCTGGTCTTGTGGGCAGACTGCTGATCGAGTTCACCTCACCCATGCCCCTGGAGCGG
GTGCAGAGGGAGAACCCAGGCGTGCTCATGGGCGGCCGATACACACCGCCCGACTGCACC
CCAGCCCAGACGGTGGCGGTCATCATCCCCTTTAGACACCGGGAACACCACCTGCGCTAC
TGGCTCCACTATCTACACCCCATCTTGAGGCGGCAGCGGCTGCGCTACGGCGTCTATGTC
ATCAACCAGCATGGTGAGGACACCTTCAACCGGGCCAAGCTGCTTAACGTGGGCTTCCTA
GAGGCGCTGAAGGAGGATGCCGCCTATGACTGCTTCATCTTCAGCGATGTGGACCTGGTC
CCCATGGATGACCGCAACCTATACCGCTGCGGCGACCAACCCCGCCACTTTGCCATTGCC
ATGGACAAGTTTGGCTTCCGGCTTCCCTATGCTGGCTACTTTGGAGGTGTGTCAGGCCTG
AGTAAGGCTCAGTTTCTGAGAATCAATGGCTTCCCCAATGAGTACTGGGGCTGGGGTGGC
GAGGATGATGACATCTTCAACCGGATCTCCCTGACTGGGATGAAGATCTCACGCCCAGAC
ATCCGAATTGGCCGCTACCGCATGATCAAGCACGACCGCGACAAGCATAACGAACCTAAC
CCTCAGAGGTTTACCAAGATTCAAAACACGAAGCTGACCATGAAGCGGGACGGCATTGGG
TCAGTGCGGTACCAGGTCTTGGAGGTGTCTCGGCAACCACTCTTCACCAATATCACAGTG
GACATTGGGCGGCCTCCGTCGTGGCCCCCTCGGGGCTGA
Enzyme 10 GenBank Gene ID AB024434 Link Image
Enzyme 10 GeneCard ID B4GALT2 Link Image
Enzyme 10 GenAtlas ID B4GALT2 Link Image
Enzyme 10 HGNC ID HGNC:925 Link Image
Enzyme 10 Chromosome Location 1
Enzyme 10 Locus 1p34-p33
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  8. 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 5608
Enzyme 11 Name Alpha-lactalbumin
Enzyme 11 Synonyms
  1. Lactose synthase B protein
  2. Lysozyme-like protein 7
Enzyme 11 Gene Name LALBA
Enzyme 11 Protein Sequence >Alpha-lactalbumin
MRFFVPLFLVGILFPAILAKQFTKCELSQLLKDIDGYGGIALPELICTMFHTSGYDTQAI
VENNESTEYGLFQISNKLWCKSSQVPQSRNICDISCDKFLDDDITDDIMCAKKILDIKGI
DYWLAHKALCTEKLEQWLCEKL
Enzyme 11 Number of Residues 142
Enzyme 11 Molecular Weight 16224.7
Enzyme 11 Theoretical pI 4.60
Enzyme 11 GO Classification
Function
  • UDP-galactosyltransferase activity
  • UDP-glycosyltransferase activity
  • binding
  • calcium ion binding
  • catalytic activity
  • cation binding
  • ion binding
  • lactose synthase activity
  • metal ion binding
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolic process
  • disaccharide metabolic process
  • lactose biosynthetic process
  • lactose metabolic process
  • metabolic process
  • oligosaccharide metabolic process
  • primary metabolic process
Component
Enzyme 11 General Function Involved in lactose synthase activity
Enzyme 11 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 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-19
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 307104 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID P00709 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name LALBA_HUMAN Link Image
Enzyme 11 PDB ID 1HML Link Image
Enzyme 11 PDB File Show
Enzyme 11 3D Structure
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence >429 bp
ATGAGGTTCTTTGTCCCTCTGTTCCTGGTGGGCATCCTGTTCCCTGCCATCCTGGCCAAG
CAATTCACAAAATGTGAGCTGTCCCAGCTGCTGAAAGACATAGATGGTTATGGAGGCATC
GCTTTGCCTGAATTGATCTGTACCATGTTTCACACCAGTGGTTATGACACACAAGCCATA
GTTGAAAACAATGAAAGCACGGAATATGGACTCTTCCAGATCAGTAATAAGCTTTGGTGC
AAGAGCAGCCAGGTCCCTCAGTCAAGGAACATCTGTGACATCTCCTGTGACAAGTTCCTG
GATGATGACATTACTGATGACATAATGTGTGCCAAGAAGATCCTGGATATTAAAGGAATT
GACTACTGGTTGGCCCATAAAGCCCTCTGCACTGAGAAGCTGGAACAGTGGCTTTGTGAG
AAGTTGTGA
Enzyme 11 GenBank Gene ID J00270 Link Image
Enzyme 11 GeneCard ID LALBA Link Image
Enzyme 11 GenAtlas ID LALBA Link Image
Enzyme 11 HGNC ID HGNC:6480 Link Image
Enzyme 11 Chromosome Location 1
Enzyme 11 Locus 12q13
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Findlay JB, Brew K: The complete amino-acid sequence of human -lactalbumin. Eur J Biochem. 1972 May;27(1):65-86. [PubMed Link Image]
  5. Maynard F: Identification of a new molecular form of human alpha-lactalbumin. J Dairy Res. 1992 Aug;59(3):425-9. [PubMed Link Image]
  6. Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. [PubMed Link Image]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. Chowanadisai W, Kelleher SL, Nemeth JF, Yachetti S, Kuhlman CF, Jackson JG, Davis AM, Lien EL, Lonnerdal B: Detection of a single nucleotide polymorphism in the human alpha-lactalbumin gene: implications for human milk proteins. J Nutr Biochem. 2005 May;16(5):272-8. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 5614
Enzyme 12 Name Beta-1,4-galactosyltransferase 1
Enzyme 12 Synonyms
  1. Beta-1,4-GalTase 1
  2. Beta4Gal-T1
  3. b4Gal-T1
  4. UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1
  5. UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1
  6. Lactose synthase A protein
  7. N-acetyllactosamine synthase
  8. Nal synthase
  9. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
  10. Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
  11. Processed beta-1,4-galactosyltransferase 1
Enzyme 12 Gene Name B4GALT1
Enzyme 12 Protein Sequence >Beta-1,4-galactosyltransferase 1
MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPL
QGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVP
HTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAI
IIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYD
YTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTI
NGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIA
HTKETMLSDGLNSLTYQVLDVQRYPLYTQITVDIGTPS
Enzyme 12 Number of Residues 398
Enzyme 12 Molecular Weight 43919.9
Enzyme 12 Theoretical pI 8.77
Enzyme 12 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 12 General Function Involved in transferase activity, transferring glycosyl groups
Enzyme 12 Specific Function The cell surface form functions as a recognition molecule during a variety of cell to cell and cell to matrix interactions, as those occurring during development and egg fertilization, by binding to specific oligosaccharide ligands on opposing cells or in the extracellular matrix
Enzyme 12 Pathways
Enzyme 12 Reactions
  • UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine [RN:R01205 R06055]
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • None
Enzyme 12 Transmembrane Regions
  • 25-44
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 189053491 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID P15291 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name B4GT1_HUMAN Link Image
Enzyme 12 PDB ID 1FR8 Link Image
Enzyme 12 PDB File Show
Enzyme 12 3D Structure
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1197 bp
ATGAGGCTTCGGGAGCCGCTCCTGAGCGGCAGCGCCGCGATGCCAGGCGCGTCCCTACAG
CGGGCCTGCCGCCTGCTCGTGGCCGTCTGCGCTCTGCACCTTGGCGTCACCCTCGTTTAC
TACCTGGCTGGCCGCGACCTGAGCCGCCTGCCCCAACTGGTCGGAGTCTCCACACCGCTG
CAGGGCGGCTCGAACAGTGCCGCCGCCATCGGGCAGTCCTCCGGGGAGCTCCGGACCGGA
GGGGCCCGGCCGCCGCCTCCTCTAGGCGCCTCCTCCCAGCCGCGCCCGGGTGGCGACTCC
AGCCCAGTCGTGGATTCTGGCCCTGGCCCCGCTAGCAACTTGACCTCGGTCCCAGTGCCC
CACACCACCGCACTGTCGCTGCCCGCCTGCCCTGAGGAGTCCCCGCTGCTTGTGGGCCCC
ATGCTGATTGAGTTTAACATGCCTGTGGACCTGGAGCTCGTGGCAAAGCAGAACCCAAAT
GTGAAGATGGGCGGCCGCTATGCCCCCAGGGACTGCGTCTCTCCTCACAAGGTGGCCATC
ATCATTCCATTCCGCAACCGGCAGGAGCACCTCAAGTACTGGCTATATTATTTGCACCCA
GTCCTGCAGCGCCAGCAGCTGGACTATGGCATCTATGTTATCAACCAGGCGGGAGACACT
ATATTCAATCGTGCTAAGCTCCTCAATGTTGGCTTTCAAGAAGCCTTGAAGGACTATGAC
TACACCTGCTTTGTGTTTAGCGACGTGGACCTCATTCCAATGAATGACCATAATGCGTAC
AGGTGTTTTTCACAGCCACGGCACATTTCCGTTGCAATGGATAAGTTTGGATTCAGCCTA
CCTTATGTTCAGTATTTTGGAGGTGTCTCTGCTCTAAGTAAACAACAGTTTCTAACCATC
AATGGATTTCCTAATAATTATTGGGGCTGGGGAGGAGAAGATGATGACATTTTTAACAGA
TTAGTTTTTAGAGGCATGTCTATATCTCGCCCAAATGCTGTGGTCGGGAGGTGTCGCATG
ATCCGCCACTCAAGAGACAAGAAAAATGAACCCAATCCTCAGAGGTTTGACCGAATTGCA
CACACAAAGGAGACAATGCTCTCTGATGGTTTGAACTCACTCACCTACCAGGTGCTGGAT
GTACAGAGATACCCATTGTATACCCAAATCACAGTGGACATCGGGACACCGAGCTAG
Enzyme 12 GenBank Gene ID AK312797 Link Image
Enzyme 12 GeneCard ID B4GALT1 Link Image
Enzyme 12 GenAtlas ID B4GALT1 Link Image
Enzyme 12 HGNC ID HGNC:924 Link Image
Enzyme 12 Chromosome Location 9
Enzyme 12 Locus 9p13
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 General References
  1. Masri KA, Appert HE, Fukuda MN: Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-galactosyltransferase). Biochem Biophys Res Commun. 1988 Dec 15;157(2):657-63. [PubMed Link Image]
  2. Watzele G, Berger EG: Near identity of HeLa cell galactosyltransferase with the human placental enzyme. Nucleic Acids Res. 1990 Dec 11;18(23):7174. [PubMed Link Image]
  3. Mengle-Gaw L, McCoy-Haman MF, Tiemeier DC: Genomic structure and expression of human beta-1,4-galactosyltransferase. Biochem Biophys Res Commun. 1991 May 15;176(3):1269-76. [PubMed Link Image]
  4. Uejima T, Uemura M, Nozawa S, Narimatsu H: Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies. Cancer Res. 1992 Nov 15;52(22):6158-63. [PubMed Link Image]
  5. Kudo T, Narimatsu H: The beta 1,4-galactosyltransferase gene is post-transcriptionally regulated during differentiation of mouse F9 teratocarcinoma cells. Glycobiology. 1995 Jun;5(4):397-403. [PubMed Link Image]
  6. Chatterjee SK, Mukerjee S, Tripathi PK: Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA clones. Int J Biochem Cell Biol. 1995 Mar;27(3):329-36. [PubMed Link Image]
  7. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  8. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  9. Appert HE, Rutherford TJ, Tarr GE, Wiest JS, Thomford NR, McCorquodale DJ: Isolation of a cDNA coding for human galactosyltransferase. Biochem Biophys Res Commun. 1986 Aug 29;139(1):163-8. [PubMed Link Image]
  10. Appert HE, Rutherford TJ, Tarr GE, Thomford NR, McCorquodale DJ: Isolation of galactosyltransferase from human milk and the determination of its N-terminal amino acid sequence. Biochem Biophys Res Commun. 1986 Jul 16;138(1):224-9. [PubMed Link Image]
  11. Aoki D, Appert HE, Johnson D, Wong SS, Fukuda MN: Analysis of the substrate binding sites of human galactosyltransferase by protein engineering. EMBO J. 1990 Oct;9(10):3171-8. [PubMed Link Image]
  12. Lopez LC, Youakim A, Evans SC, Shur BD: Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase. J Biol Chem. 1991 Aug 25;266(24):15984-91. [PubMed Link Image]
  13. Yamaguchi N, Fukuda MN: Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane-spanning domain-dependent homodimerization and association with alpha- and beta-tubulins. J Biol Chem. 1995 May 19;270(20):12170-6. [PubMed Link Image]
  14. 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 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 5687
Enzyme 13 Name UDP-glucuronosyltransferase 2B28
Enzyme 13 Synonyms
  1. UDPGT 2B28
Enzyme 13 Gene Name UGT2B28
Enzyme 13 Protein Sequence >UDP-glucuronosyltransferase 2B28
MALKWTSVLLLIHLGCYFSSGSCGKVLVWTGEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDAFTLKLEVYPTSLTKTEFENIIMQQVKRWSDIQKDSFWLYFSQEQEILWEFH
DIFRNFCKDVVSNKKVMKKLQESRFDIIFADAFFPCGELLAALLNIPFVYSLCFTPGYTI
ERHSGGLIFPPSYIPVVMSKLSDQMTFMERVKNMIYVLYFDFWFQMCDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNIDFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGLPKTRAFITHGGANGIYEAIYHGIPMVGIPLFWDQPDNIAHMKAKGAAVRLDFHTM
SSTDLLNALKTVINDPSYKENVMKLSIIQHDQPVKPLHRAVFWIEFVMCHKGAKHLRVAA
RDLTWFQYHSLDVIGFLLACVATVIFVVTKFCLFCFWKFARKGKKGKRD
Enzyme 13 Number of Residues 529
Enzyme 13 Molecular Weight 60905.8
Enzyme 13 Theoretical pI 8.80
Enzyme 13 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 13 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 13 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 13 Pathways
Enzyme 13 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-24
Enzyme 13 Transmembrane Regions
  • 495-517
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 13603476 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q9BY64 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name UDB28_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 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 13 GenBank Gene ID AF177272 Link Image
Enzyme 13 GeneCard ID UGT2B28 Link Image
Enzyme 13 GenAtlas ID UGT2B28 Link Image
Enzyme 13 HGNC ID HGNC:13479 Link Image
Enzyme 13 Chromosome Location 4
Enzyme 13 Locus 4q13.2
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 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]
  2. Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 5696
Enzyme 14 Name UDP-glucuronosyltransferase 2B4
Enzyme 14 Synonyms
  1. UDPGT 2B4
  2. HLUG25
  3. Hyodeoxycholic acid-specific UDPGT
  4. UDPGTh-1
Enzyme 14 Gene Name UGT2B4
Enzyme 14 Protein Sequence >UDP-glucuronosyltransferase 2B4
MSMKWTSALLLIQLSCYFSSGSCGKVLVWPTEFSHWMNIKTILDELVQRGHEVTVLASSA
SISFDPNSPSTLKFEVYPVSLTKTEFEDIIKQLVKRWAELPKDTFWSYFSQVQEIMWTFN
DILRKFCKDIVSNKKLMKKLQESRFDVVLADAVFPFGELLAELLKIPFVYSLRFSPGYAI
EKHSGGLLFPPSYVPVVMSELSDQMTFIERVKNMIYVLYFEFWFQIFDMKKWDQFYSEVL
GRPTTLSETMAKADIWLIRNYWDFQFPHPLLPNVEFVGGLHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSMVSNTSEERANVIASALAKIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGVPLFADQPDNIAHMKAKGAAVSLDFHTM
SSTDLLNALKTVINDPLYKENAMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVTGFLLACVATVIFIITKCLFCVWKFVRTGKKGKRD
Enzyme 14 Number of Residues 528
Enzyme 14 Molecular Weight 60512.0
Enzyme 14 Theoretical pI 8.75
Enzyme 14 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 14 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 14 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 14 Pathways
Enzyme 14 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-23
Enzyme 14 Transmembrane Regions
  • 493-509
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 37589 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID P06133 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name UD2B4_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 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 14 GenBank Gene ID Y00317 Link Image
Enzyme 14 GeneCard ID UGT2B4 Link Image
Enzyme 14 GenAtlas ID UGT2B4 Link Image
Enzyme 14 HGNC ID HGNC:12553 Link Image
Enzyme 14 Chromosome Location 4
Enzyme 14 Locus 4q13
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 5719
Enzyme 15 Name UDP-glucuronosyltransferase 1-4
Enzyme 15 Synonyms
  1. UDPGT 1-4
  2. UGT1*4
  3. UGT1-04
  4. UGT1.4
  5. Bilirubin-specific UDPGT isozyme 2
  6. hUG-BR2
  7. UDP-glucuronosyltransferase 1-D
  8. UGT-1D
  9. UGT1D
  10. UDP-glucuronosyltransferase 1A4
Enzyme 15 Gene Name UGT1A4
Enzyme 15 Protein Sequence >UDP-glucuronosyltransferase 1-4
MARGLQVPLPRLATGLLLLLSVQPWAESGKVLVVPTDGSPWLSMREALRELHARGHQAVV
LTPEVNMHIKEEKFFTLTAYAVPWTQKEFDRVTLGYTQGFFETEHLLKRYSRSMAIMNNV
SLALHRCCVELLHNEALIRHLNATSFDVVLTDPVNLCGAVLAKYLSIPAVFFWRYIPCDL
DFKGTQCPNPSSYIPKLLTTNSDHMTFLQRVKNMLYPLALSYICHTFSAPYASLASELFQ
REVSVVDLVSYASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 15 Number of Residues 534
Enzyme 15 Molecular Weight 60024.5
Enzyme 15 Theoretical pI 8.68
Enzyme 15 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 15 General Function Involved in transferase activity, transferring hexosyl groups
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 [RN:R01383]
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-28
Enzyme 15 Transmembrane Regions
  • 492-508
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein Not Available
Enzyme 15 UniProtKB/Swiss-Prot ID P22310 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name UD14_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >1605 bp
ATGGCCAGAGGACTCCAGGTTCCCCTGCCGCGGCTGGCCACAGGACTGCTGCTCCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGAAAGGTGTTGGTGGTGCCCACTGATGGCAGCCCC
TGGCTCAGCATGCGGGAGGCCTTGCGGGAGCTCCATGCCAGAGGCCACCAGGCGGTGGTC
CTCACCCCAGAGGTGAATATGCACATCAAAGAAGAGAAATTTTTCACCCTGACAGCCTAT
GCTGTTCCATGGACCCAGAAGGAATTTGATCGCGTTACGCTGGGCTACACTCAAGGGTTC
TTTGAAACAGAACATCTTCTGAAGAGATATTCTAGAAGTATGGCAATTATGAACAATGTA
TCTTTGGCCCTTCATAGGTGTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGAATGCTACTTCCTTTGATGTGGTTTTAACAGACCCCGTTAACCTCTGCGGGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTTTGGAGGTACATTCCATGTGACTTA
GACTTTAAGGGCACACAGTGTCCAAATCCTTCCTCCTATATTCCTAAGTTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACATTTGCCATACTTTTTCTGCCCCTTATGCAAGTCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCTATGCATCCGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGACTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAGGAATTTGAAGCCTACATTAATGCTTCTGGAGAA
CATGGAATTGTGGTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCT
ATGGCAATTGCTGATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGA
ACCCGACCATCGAATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGAT
CTGCTTGGTCACCCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTAT
GAAAGCATATGCAATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGAC
AATGCAAAGCGCATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACT
TCTGAAGATTTAGAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAAC
ATCATGCGCCTCTCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTG
TTCTGGGTGGAGTTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCAC
GACCTCACCTGGTACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTG
CTGACAGTGGCCTTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGG
AAAAAAGGGCGAGTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 15 GenBank Gene ID M57951 Link Image
Enzyme 15 GeneCard ID UGT1A4 Link Image
Enzyme 15 GenAtlas ID UGT1A4 Link Image
Enzyme 15 HGNC ID HGNC:12536 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  6. 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]
  7. 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]
  8. 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]
  9. Menard V, Girard H, Harvey M, Perusse L, Guillemette C: Analysis of inherited genetic variations at the UGT1 locus in the French-Canadian population. Hum Mutat. 2009 Apr;30(4):677-87. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 5721
Enzyme 16 Name UDP-glucuronosyltransferase 2B7
Enzyme 16 Synonyms
  1. UDPGT 2B7
  2. 3,4-catechol estrogen-specific UDPGT
  3. UDP-glucuronosyltransferase 2B9
  4. UDPGT 2B9
  5. UDPGTh-2
Enzyme 16 Gene Name UGT2B7
Enzyme 16 Protein Sequence >UDP-glucuronosyltransferase 2B7
MSVKWTSVILLIQLSFCFSSGNCGKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSA
SILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRWSDLPKDTFWLYFSQVQEIMSIFG
DITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTF
EKHSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSEVL
GRPTTLSETMGKADVWLIRNSWNFQFPHPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSG
ENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFADQPDNIAHMKARGAAVRVDFNTM
SSTDLLNALKRVINDPSYKENVMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLVCVATVIFIVTKCCLFCFWKFARKAKKGKND
Enzyme 16 Number of Residues 529
Enzyme 16 Molecular Weight 60694.1
Enzyme 16 Theoretical pI 8.45
Enzyme 16 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 16 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 16 Specific Function Its unique specificity for 3,4-catechol estrogens and estriol suggests it may play an important role in regulating the level and activity of these potent and active estrogen metabolites
Enzyme 16 Pathways
Enzyme 16 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-23
Enzyme 16 Transmembrane Regions
  • 493-509
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein Not Available
Enzyme 16 UniProtKB/Swiss-Prot ID P16662 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name UD2B7_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 Gene Sequence >1590 bp
ATGTCTGTGAAATGGACTTCAGTAATTTTGCTAATACAACTGAGCTTTTGCTTTAGCTCT
GGGAATTGTGGAAAGGTGCTGGTGTGGGCAGCAGAATACAGCCATTGGATGAATATAAAG
ACAATCCTGGATGAGCTTATTCAGAGAGGTCATGAGGTGACTGTACTGGCATCTTCAGCT
TCCATTCTTTTTGATCCCAACAACTCATCCGCTCTTAAAATTGAAATTTATCCCACATCT
TTAACTAAAACTGAGTTGGAGAATTTCATCATGCAACAGATTAAGAGATGGTCAGACCTT
CCAAAAGATACATTTTGGTTATATTTTTCACAAGTACAGGAAATCATGTCAATATTTGGT
GACATAACTAGAAAGTTCTGTAAAGATGTAGTTTCAAATAAGAAATTTATGAAAAAAGTA
CAAGAGTCAAGATTTGACGTCATTTTTGCAGATGCTATTTTTCCCTGTAGTGAGCTGCTG
GCTGAGCTATTTAACATACCCTTTGTGTACAGTCTCAGCTTCTCTCCTGGCTACACTTTT
GAAAAGCATAGTGGAGGATTTATTTTCCCTCCTTCCTACGTACCTGTTGTTATGTCAGAA
TTAACTGATCAAATGACTTTCATGGAGAGGGTAAAAAATATGATCTATGTGCTTTACTTT
GACTTTTGGTTCGAAATATTTGACATGAAGAAGTGGGATCAGTTTTATAGTGAAGTTCTA
GGAAGACCCACTACGTTATCTGAGACAATGGGGAAAGCTGACGTATGGCTTATTCGAAAC
TCCTGGAATTTTCAGTTTCCTCATCCACTCTTACCAAATGTTGATTTTGTTGGAGGACTC
CACTGCAAACCTGCCAAACCCCTGCCTAAGGAAATGGAAGACTTTGTACAGAGCTCTGGA
GAAAATGGTGTTGTGGTGTTTTCTCTGGGGTCAATGGTCAGTAACATGACAGAAGAAAGG
GCCAACGTAATTGCATCAGCCCTGGCCCAGATCCCACAAAAGGTTCTGTGGAGATTTGAT
GGGAATAAACCAGATACCTTAGGTCTCAATACTCGGCTGTATAAGTGGATACCCCAGAAT
GACCTTCTAGGTCATCCAAAGACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATC
TACGAGGCAATCTACCATGGGATCCCTATGGTGGGGATTCCATTGTTTGCCGATCAACCT
GATAACATTGCTCACATGAAGGCCAGGGGAGCAGCTGTTAGAGTGGACTTCAACACAATG
TCGAGTACAGACTTGCTGAATGCATTGAAGAGAGTAATTAATGATCCTTCATATAAAGAG
AATGTTATGAAATTATCAAGAATTCAACATGATCAACCAGTGAAGCCCCTGGATCGAGCA
GTCTTCTGGATTGAATTTGTCATGCGCCACAAAGGAGCTAAACACCTTCGGGTTGCAGCC
CACGACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGATTGGGTTCCTGCTGGTCTGT
GTGGCAACTGTGATATTTATCGTCACAAAATGTTGTCTGTTTTGTTTCTGGAAGTTTGCT
AGAAAAGCAAAGAAGGGAAAAAATGATTAG
Enzyme 16 GenBank Gene ID J05428 Link Image
Enzyme 16 GeneCard ID UGT2B7 Link Image
Enzyme 16 GenAtlas ID UGT2B7 Link Image
Enzyme 16 HGNC ID HGNC:12554 Link Image
Enzyme 16 Chromosome Location 4
Enzyme 16 Locus 4q13
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. Ritter JK, Sheen YY, Owens IS: Cloning and expression of human liver UDP-glucuronosyltransferase in COS-1 cells. 3,4-catechol estrogens and estriol as primary substrates. J Biol Chem. 1990 May 15;265(14):7900-6. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  6. Bhasker CR, McKinnon W, Stone A, Lo AC, Kubota T, Ishizaki T, Miners JO: Genetic polymorphism of UDP-glucuronosyltransferase 2B7 (UGT2B7) at amino acid 268: ethnic diversity of alleles and potential clinical significance. Pharmacogenetics. 2000 Nov;10(8):679-85. [PubMed Link Image]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 5722
Enzyme 17 Name UDP-glucuronosyltransferase 2B15
Enzyme 17 Synonyms
  1. UDPGT 2B15
  2. HLUG4
  3. UDP-glucuronosyltransferase 2B8
  4. UDPGT 2B8
  5. UDPGTh-3
Enzyme 17 Gene Name UGT2B15
Enzyme 17 Protein Sequence >UDP-glucuronosyltransferase 2B15
MSLKWTSVFLLIQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVTVLTSSA
STLVNASKSSAIKLEVYPTSLTKNDLEDSLLKILDRWIYGVSKNTFWSYFSQLQELCWEY
YDYSNKLCKDAVLNKKLMMKLQESKFDVILADALNPCGELLAELFNIPFLYSLRFSVGYT
FEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIHMLYFDFWFQIYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPVYKENVMKLSRIHHDQPMKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATVIFIITKFCLFCFRKLAKKGKKKKRD
Enzyme 17 Number of Residues 530
Enzyme 17 Molecular Weight 60987.7
Enzyme 17 Theoretical pI 9.04
Enzyme 17 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 17 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 17 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 17 Pathways
Enzyme 17 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • 1-23
Enzyme 17 Transmembrane Regions
  • 495-515
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 116517299 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID P54855 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name UDB15_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence >1593 bp
ATGTCTCTGAAATGGACGTCAGTCTTTCTGCTGATACAGCTCAGTTGTTACTTTAGCTCT
GGAAGCTGTGGAAAGGTGCTAGTGTGGCCCACAGAATACAGCCATTGGATAAATATGAAG
ACAATCCTGGAAGAGCTTGTTCAGAGGGGTCATGAGGTGACTGTGTTGACATCTTCGGCT
TCTACTCTTGTCAATGCCAGTAAATCATCTGCTATTAAATTAGAAGTTTATCCTACATCT
TTAACTAAAAATTATTTGGAAGATTCTCTTCTGAAAATTCTCGATAGATGGATATATGGT
GTTTCAAAAAATACATTTTGGTCATATTTTTCACAATTACAAGAATTGTGTTGGGAATAT
TATGACTACAGTAACAAGCTCTGTAAAGATGCAGTTTTGAATAAGAAACTTATGATGAAA
CTACAAGAGTCAAAGTTTGATGTCATTCTGGCAGATGCCCTTAATCCCTGTGGTGAGCTA
CTGGCTGAACTATTTAACATACCCTTTCTGTACAGTCTTCGATTCTCTGTTGGCTACACA
TTTGAGAAGAATGGTGGAGGATTTCTGTTCCCTCCTTCCTATGTACCTGTTGTTATGTCA
GAATTAAGTGATCAAATGATTTTCATGGAGAGGATAAAAAATATGATACATATGCTTTAT
TTTGACTTTTGGTTTCAAATTTATGATCTGAAGAAGTGGGACCAGTTTTATAGTGAAGTT
CTAGGAAGACCCACTACATTATTTGAGACAATGGGGAAAGCTGAAATGTGGCTCATTCGA
ACCTATTGGGATTTTGAATTTCCTCGCCCATTCTTACCAAATGTTGATTTTGTTGGAGGA
CTTCACTGTAAACCAGCCAAACCCCTGCCTAAGGAAATGGAAGAGTTTGTGCAGAGCTCT
GGAGAAAATGGTATTGTGGTGTTTTCTCTGGGGTCGATGATCAGTAACATGTCAGAAGAA
AGTGCCAACATGATTGCATCAGCCCTTGCCCAGATCCCACAAAAGGTTCTATGGAGATTT
GATGGCAAGAAGCCAAATACTTTAGGTTCCAATACTCGACTGTACAAGTGGTTACCCCAG
AATGACCTTCTTGGTCATCCCAAAACCAAAGCTTTTATAACTCATGGTGGAACCAATGGC
ATCTATGAGGCGATCTACCATGGGATCCCTATGGTGGGCATTCCCTTGTTTGCGGATCAA
CATGATAACATTGCTCACATGAAAGCCAAGGGAGCAGCCCTCAGTGTGGACATCAGGACC
ATGTCAAGTAGAGATTTGCTCAATGCATTGAAGTCAGTCATTAATGACCCTGTCTATAAA
GAGAATGTCATGAAATTATCAAGAATTCATCATGACCAACCAATGAAGCCCCTGGATCGA
GCAGTCTTCTGGATTGAGTTTGTCATGCGCCACAAAGGAGCCAAGCACCTTCGAGTCGCA
GCTCACAACCTCACCTGGATCCAGTACCACTCTTTGGATGTGATAGCATTCCTGCTGGCC
TGCGTGGCAACTGTGATATTTATCATCACAAAATTTTGCCTGTTTTGTTTCCGAAAGCTT
GCCAAAAAAGGAAAGAAGAAGAAAAGAGATTAG
Enzyme 17 GenBank Gene ID NM_001076.2 Link Image
Enzyme 17 GeneCard ID UGT2B15 Link Image
Enzyme 17 GenAtlas ID UGT2B15 Link Image
Enzyme 17 HGNC ID HGNC:12546 Link Image
Enzyme 17 Chromosome Location 4
Enzyme 17 Locus 4q13
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 General References
  1. Chen F, Ritter JK, Wang MG, McBride OW, Lubet RA, Owens IS: Characterization of a cloned human dihydrotestosterone/androstanediol UDP-glucuronosyltransferase and its comparison to other steroid isoforms. Biochemistry. 1993 Oct 12;32(40):10648-57. [PubMed Link Image]
  2. 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]
  3. 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]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. 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]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  7. Toide K, Umeda S, Yamazaki H, Takahashi Y, Terauchi Y, Fujii T, Kamataki T: A major genotype in UDP-glucuronosyltransferase 2B15. Drug Metab Pharmacokinet. 2002;17(2):164-6. [PubMed Link Image]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 5724
Enzyme 18 Name UDP-glucuronosyltransferase 2A1
Enzyme 18 Synonyms
  1. UDPGT 2A1
Enzyme 18 Gene Name UGT2A1
Enzyme 18 Protein Sequence >UDP-glucuronosyltransferase 2A1
MLNNLLLFSLQISLIGTTLGGNVLIWPMEGSHWLNVKIIIDELIKKEHNVTVLVASGALF
ITPTSNPSLTFEIYRVPFGKERIEGVIKDFVLTWLENRPSPSTIWRFYQEMAKVIKDFHM
VSQEICDGVLKNQQLMAKLKKSKFEVLVSDPVFPCGDIVALKLGIPFMYSLRFSPASTVE
KHCGKVPYPPSYVPAVLSELTDQMSFTDRIRNFISYHLQDYMFETLWKSWDSYYSKALGR
PTTLCETMGKAEIWLIRTYWDFEFPRPYLPNFEFVGGLHCKPAKPLPKEMEEFIQSSGKN
GVVVFSLGSMVKNLTEEKANLIASALAQIPQKVLWRYKGKKPATLGNNTQLFDWIPQNDL
LGHPKTKAFITHGGTNGIYEAIYHGVPMVGVPMFADQPDNIAHMKAKGAAVEVNLNTMTS
VDLLSALRTVINEPSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHD
LTWFQYHSLDVIGFLLVCVTTAIFLVIQCCLFSCQKFGKIGKKKKRE
Enzyme 18 Number of Residues 527
Enzyme 18 Molecular Weight 59925.7
Enzyme 18 Theoretical pI 9.29
Enzyme 18 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 18 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 18 Specific Function UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds. Active on odorants and seems to be involved in olfaction; it could help clear lipophilic odorant molecules from the sensory epithelium
Enzyme 18 Pathways
Enzyme 18 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • 1-20
Enzyme 18 Transmembrane Regions
  • 491-507
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 110611919 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9Y4X1 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name UD2A1_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence >1584 bp
ATGTTAAACAACCTTCTGCTGTTCTCCCTTCAGATAAGTCTCATAGGAACCACTCTTGGT
GGGAATGTTTTGATTTGGCCAATGGAAGGTAGTCATTGGCTAAATGTTAAGATAATTATA
GATGAGCTCATTAAAAAGGAGCATAATGTGACTGTCCTAGTTGCCTCTGGTGCACTTTTC
ATCACACCAACCTCTAACCCATCTCTGACATTTGAAATATATAGGGTGCCCTTTGGCAAA
GAAAGAATAGAAGGAGTAATTAAGGACTTCGTTTTGACATGGCTGGAAAATAGACCATCT
CCTTCAACCATTTGGAGATTCTATCAGGAGATGGCCAAAGTAATCAAGGACTTCCACATG
GTGTCTCAGGAGATCTGTGATGGCGTTCTTAAAAACCAACAGCTGATGGCAAAGCTAAAG
AAAAGCAAGTTTGAAGTCCTGGTGTCTGATCCAGTATTTCCTTGTGGCGATATAGTAGCT
TTAAAACTTGGAATTCCATTTATGTACTCCTTGAGGTTTTCTCCAGCCTCAACAGTGGAA
AAGCACTGTGGGAAGGTACCATACCCTCCTTCCTATGTTCCTGCTGTTTTATCAGAACTC
ACCGACCAAATGTCTTTCACTGACAGAATAAGAAATTTCATCTCCTACCACCTACAGGAC
TACATGTTTGAAACTCTTTGGAAATCATGGGATTCATACTATAGTAAAGCTTTAGGAAGA
CCCACTACGTTATGTGAGACTATGGGGAAAGCTGAAATTTGGTTAATCCGAACATATTGG
GATTTTGAATTTCCTCGTCCATACTTACCTAATTTTGAGTTTGTTGGAGGATTGCACTGC
AAACCTGCCAAACCTTTACCTAAGGAAATGGAAGAATTTATCCAGAGCTCAGGTAAAAAT
GGTGTTGTGGTGTTTTCTCTGGGATCAATGGTCAAAAACCTTACAGAAGAAAAGGCCAAT
CTTATTGCCTCAGCCCTTGCCCAGATTCCACAGAAGGTTTTATGGAGATACAAAGGAAAG
AAACCAGCCACATTAGGAAACAATACTCAGCTCTTTGATTGGATACCCCAGAATGATCTT
CTTGGACATCCCAAAACCAAAGCTTTTATCACTCATGGTGGAACTAATGGGATCTACGAA
GCTATTTACCACGGAGTCCCTATGGTGGGAGTTCCCATGTTTGCTGATCAGCCTGATAAC
ATTGCTCACATGAAGGCCAAAGGAGCAGCTGTGGAAGTGAACCTAAACACAATGACAAGT
GTGGATTTGCTTAGCGCTTTGAGAACAGTCATTAATGAACCTTCTTATAAAGAGAATGCT
ATGAGGTTATCAAGAATTCACCATGATCAACCTGTAAAGCCCCTGGATCGAGCAGTCTTC
TGGATCGAGTTTGTCATGCGCCACAAAGGAGCCAAGCACCTTCGGGTTGCAGCCCATGAC
CTCACCTGGTTCCAGTACCACTCTTTGGATGTAATTGGGTTCTTGCTGGTCTGTGTGACA
ACGGCTATATTTTTGGTCATACAATGTTGTTTGTTTTCCTGTCAAAAATTTGGTAAGATA
GGAAAGAAGAAAAAAAGAGAATAG
Enzyme 18 GenBank Gene ID NM_006798.2 Link Image
Enzyme 18 GeneCard ID UGT2A1 Link Image
Enzyme 18 GenAtlas ID UGT2A1 Link Image
Enzyme 18 HGNC ID HGNC:12542 Link Image
Enzyme 18 Chromosome Location 4
Enzyme 18 Locus 4q13
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 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]
  2. Sneitz N, Court MH, Zhang X, Laajanen K, Yee KK, Dalton P, Ding X, Finel M: Human UDP-glucuronosyltransferase UGT2A2: cDNA construction, expression, and functional characterization in comparison with UGT2A1 and UGT2A3. Pharmacogenet Genomics. 2009 Oct 24. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 5725
Enzyme 19 Name UDP-glucuronosyltransferase 1-1
Enzyme 19 Synonyms
  1. UDPGT 1-1
  2. UGT1*1
  3. UGT1-01
  4. UGT1.1
  5. Bilirubin-specific UDPGT isozyme 1
  6. hUG-BR1
  7. UDP-glucuronosyltransferase 1-A
  8. UGT-1A
  9. UGT1A
  10. UDP-glucuronosyltransferase 1A1
Enzyme 19 Gene Name UGT1A1
Enzyme 19 Protein Sequence >UDP-glucuronosyltransferase 1-1
MAVESQGGRPLVLGLLLCVLGPVVSHAGKILLIPVDGSHWLSMLGAIQQLQQRGHEIVVL
APDASLYIRDGAFYTLKTYPVPFQREDVKESFVSLGHNVFENDSFLQRVIKTYKKIKKDS
AMLLSGCSHLLHNKELMASLAESSFDVMLTDPFLPCSPIVAQYLSLPTVFFLHALPCSLE
FEATQCPNPFSYVPRPLSSHSDHMTFLQRVKNMLIAFSQNFLCDVVYSPYATLASEFLQR
EVTVQDLLSSASVWLFRSDFVKDYPRPIMPNMVFVGGINCLHQNPLSQEFEAYINASGEH
GIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDL
LGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTS
EDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHD
LTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 19 Number of Residues 533
Enzyme 19 Molecular Weight 59590.9
Enzyme 19 Theoretical pI 8.09
Enzyme 19 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 19 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 19 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 19 Pathways
Enzyme 19 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • 1-25
Enzyme 19 Transmembrane Regions
  • 491-507
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein Not Available
Enzyme 19 UniProtKB/Swiss-Prot ID P22309 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name UD11_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 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 19 GenBank Gene ID M57899 Link Image
Enzyme 19 GeneCard ID UGT1A1 Link Image
Enzyme 19 GenAtlas ID UGT1A1 Link Image
Enzyme 19 HGNC ID HGNC:12530 Link Image
Enzyme 19 Chromosome Location 2
Enzyme 19 Locus 2q37
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 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. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Meunier L, Usherwood YK, Chung KT, Hendershot LM: A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell. 2002 Dec;13(12):4456-69. [PubMed Link Image]
  6. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. Erps LT, Ritter JK, Hersh JH, Blossom D, Martin NC, Owens IS: Identification of two single base substitutions in the UGT1 gene locus which abolish bilirubin uridine diphosphate glucuronosyltransferase activity in vitro. J Clin Invest. 1994 Feb;93(2):564-70. [PubMed Link Image]
  13. 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]
  14. 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]
  15. Seppen J, Steenken E, Lindhout D, Bosma PJ, Elferink RP: A mutation which disrupts the hydrophobic core of the signal peptide of bilirubin UDP-glucuronosyltransferase, an endoplasmic reticulum membrane protein, causes Crigler-Najjar type II. FEBS Lett. 1996 Jul 29;390(3):294-8. [PubMed Link Image]
  16. Ciotti M, Chen F, Rubaltelli FF, Owens IS: Coding defect and a TATA box mutation at the bilirubin UDP-glucuronosyltransferase gene cause Crigler-Najjar type I disease. Biochim Biophys Acta. 1998 Jul 1;1407(1):40-50. [PubMed Link Image]
  17. 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]
  18. 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]
  19. Kadakol A, Ghosh SS, Sappal BS, Sharma G, Chowdhury JR, Chowdhury NR: Genetic lesions of bilirubin uridine-diphosphoglucuronate glucuronosyltransferase (UGT1A1) causing Crigler-Najjar and Gilbert syndromes: correlation of genotype to phenotype. Hum Mutat. 2000 Oct;16(4):297-306. [PubMed Link Image]
  20. Maruo Y, Nishizawa K, Sato H, Sawa H, Shimada M: Prolonged unconjugated hyperbilirubinemia associated with breast milk and mutations of the bilirubin uridine diphosphate- glucuronosyltransferase gene. Pediatrics. 2000 Nov;106(5):E59. [PubMed Link Image]
  21. Kadakol A, Sappal BS, Ghosh SS, Lowenheim M, Chowdhury A, Chowdhury S, Santra A, Arias IM, Chowdhury JR, Chowdhury NR: Interaction of coding region mutations and the Gilbert-type promoter abnormality of the UGT1A1 gene causes moderate degrees of unconjugated hyperbilirubinaemia and may lead to neonatal kernicterus. J Med Genet. 2001 Apr;38(4):244-9. [PubMed Link Image]
  22. Labrune P, Myara A, Chalas J, Le Bihan B, Capel L, Francoual J: Association of a homozygous (TA)8 promoter polymorphism and a N400D mutation of UGT1A1 in a child with Crigler-Najjar type II syndrome. Hum Mutat. 2002 Nov;20(5):399-401. [PubMed Link Image]
  23. Sutomo R, Laosombat V, Sadewa AH, Yokoyama N, Nakamura H, Matsuo M, Nishio H: Novel missense mutation of the UGT1A1 gene in Thai siblings with Gilbert's syndrome. Pediatr Int. 2002 Aug;44(4):427-32. [PubMed Link Image]
  24. Ohnishi A, Emi Y: Rapid proteasomal degradation of translocation-deficient UDP-glucuronosyltransferase 1A1 proteins in patients with Crigler-Najjar type II. Biochem Biophys Res Commun. 2003 Oct 24;310(3):735-41. [PubMed Link Image]
  25. Servedio V, d'Apolito M, Maiorano N, Minuti B, Torricelli F, Ronchi F, Zancan L, Perrotta S, Vajro P, Boschetto L, Iolascon A: Spectrum of UGT1A1 mutations in Crigler-Najjar (CN) syndrome patients: identification of twelve novel alleles and genotype-phenotype correlation. Hum Mutat. 2005 Mar;25(3):325. [PubMed Link Image]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 5726
Enzyme 20 Name UDP-glucuronosyltransferase 1-9
Enzyme 20 Synonyms
  1. UDPGT 1-9
  2. UGT1*9
  3. UGT1-09
  4. UGT1.9
  5. UDP-glucuronosyltransferase 1-I
  6. UGT-1I
  7. UGT1I
  8. UDP-glucuronosyltransferase 1A9
  9. lugP4
Enzyme 20 Gene Name UGT1A9
Enzyme 20 Protein Sequence >UDP-glucuronosyltransferase 1-9
MACTGWTSPLPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMRSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDLDREFKAFAHAQWKAQVRSIYSLLMGSYNDIFDLF
FSNCRSLFKDKKLVEYLKESSFDAVFLDPFDNCGLIVAKYFSLPSVVFARGILCHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLLCHRFFKNALEIASEILQTPVT
EYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 20 Number of Residues 530
Enzyme 20 Molecular Weight 59940.5
Enzyme 20 Theoretical pI 7.96
Enzyme 20 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 20 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 20 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 20 Pathways
Enzyme 20 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • 1-25
Enzyme 20 Transmembrane Regions
  • 488-504
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 3025896 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID O60656 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name UD19_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >1593 bp
ATGGCTTGCACAGGGTGGACCAGCCCCCTTCCTCTATGTGTGTGTCTGCTGCTGACCTGT
GGCTTTGCCGAGGCAGGGAAGCTACTGGTAGTGCCCATGGATGGGAGCCACTGGTTCACC
ATGAGGTCGGTGGTGGAGAAACTCATTCTCAGGGGGCATGAGGTGGTTGTAGTCATGCCA
GAGGTGAGTTGGCAACTGGGAAGATCACTGAATTGCACAGTGAAGACTTATTCAACTTCA
TATACCCTGGAGGATCTGGACCGGGAGTTCAAGGCTTTTGCCCATGCTCAATGGAAAGCA
CAAGTACGAAGTATATATTCTCTATTAATGGGTTCATACAATGACATTTTTGACTTATTT
TTTTCAAATTGCAGGAGTTTGTTTAAAGACAAAAAATTAGTAGAATACTTAAAGGAGAGT
TCTTTTGATGCAGTGTTTCTCGATCCTTTTGATAACTGTGGCTTAATTGTTGCCAAATAT
TTCTCCCTCCCCTCCGTGGTCTTCGCCAGGGGAATACTTTGCCACTATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAGAATTCTCTTAGGGTTCTCAGATGCC
ATGACTTTCAAGGAGAGAGTACGGAACCACATCATGCACTTGGAGGAACATTTATTATGC
CACCGTTTTTTCAAAAATGCCCTAGAAATAGCCTCTGAAATTCTCCAAACACCTGTTACG
GAGTATGATCTCTACAGCCACACATCAATTTGGTTGTTGCGAACGGACTTTGTTTTGGAC
TATCCCAAACCCGTGATGCCCAACATGATCTTCATTGGTGGTATCAACTGCCATCAGGGA
AAGCCGTTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATCG
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAAGATTTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACAGTGGCC
TTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 20 GenBank Gene ID AF056188 Link Image
Enzyme 20 GeneCard ID UGT1A9 Link Image
Enzyme 20 GenAtlas ID UGT1A9 Link Image
Enzyme 20 HGNC ID HGNC:12541 Link Image
Enzyme 20 Chromosome Location 2
Enzyme 20 Locus 2q37
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 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]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed Link Image]
  5. Menard V, Girard H, Harvey M, Perusse L, Guillemette C: Analysis of inherited genetic variations at the UGT1 locus in the French-Canadian population. Hum Mutat. 2009 Apr;30(4):677-87. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 5728
Enzyme 21 Name UDP-glucuronosyltransferase 1-3
Enzyme 21 Synonyms
  1. UDPGT 1-3
  2. UGT1*3
  3. UGT1-03
  4. UGT1.3
  5. UDP-glucuronosyltransferase 1-C
  6. UGT-1C
  7. UGT1C
  8. UDP-glucuronosyltransferase 1A3
Enzyme 21 Gene Name UGT1A3
Enzyme 21 Protein Sequence >UDP-glucuronosyltransferase 1-3
MATGLQVPLPWLATGLLLLLSVQPWAESGKVLVVPIDGSHWLSMREVLRELHARGHQAVV
LTPEVNMHIKEENFFTLTTYAISWTQDEFDRHVLGHTQLYFETEHFLKKFFRSMAMLNNM
SLVYHRSCVELLHNEALIRHLNATSFDVVLTDPVNLCAAVLAKYLSIPTVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFMQRVKNMLYPLALSYICHAFSAPYASLASELFQ
REVSVVDILSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANRKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 21 Number of Residues 534
Enzyme 21 Molecular Weight 60337.8
Enzyme 21 Theoretical pI 8.28
Enzyme 21 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 21 General Function Involved in transferase activity, transferring hexosyl groups
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 [RN:R01383]
Enzyme 21 Pfam Domain Function
Enzyme 21 Signals
  • 1-28
Enzyme 21 Transmembrane Regions
  • 492-508
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 11118746 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID P35503 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name UD13_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >1605 bp
ATGGCCACAGGACTCCAGGTTCCCCTGCCGCAGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGGAAGGTGCTGGTGGTGCCCACTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGCCTTGCGGGACCTCCATGCGAGAGGCCACCAGGTGGTGGTC
CTCACCCTGGAGGTGAATATGTACATCAAAGAAGAGAACTTTTTCACCCTGACAACGTAT
GCCATTTCATGGACCCAGGACGAATTTGATCGCCTTTTGCTGGGTCACACTCAATCGTTC
TTTGAAACAGAACATCTTCTGATGAAATTTTCTAGAAGAATGGCAATTATGAACAATATG
TCTTTGATCATACATAGGTCTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGCATGCTACTTCCTTTGATGTGGTTCTAACAGACCCCTTTCACCTCTGCGCGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTCTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACCTTTGCCATGCTGTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGATTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAGGAATTTGAAGCCTACATTAATGCTTCTGGAGAA
CATGGAATTGTGGTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCT
ATGGCAATTGCTGATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGA
ACCCGACCATCGAATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGAT
CTGCTTGGTCACCCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTAT
GAAAGCATATGCAATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGAC
AATGCAAAGCGCATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACT
TCTGAAGATTTAGAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAAC
ATCATGCGCCTCTCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTG
TTCTGGGTGGAGTTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCAC
GACCTCACCTGGTACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTG
CTGACAGTGGCCTTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGG
AAAAAAGGGCGAGTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 21 GenBank Gene ID AF297093 Link Image
Enzyme 21 GeneCard ID UGT1A3 Link Image
Enzyme 21 GenAtlas ID UGT1A3 Link Image
Enzyme 21 HGNC ID HGNC:12535 Link Image
Enzyme 21 Chromosome Location 2
Enzyme 21 Locus 2q37
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 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]
  3. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
  4. Menard V, Girard H, Harvey M, Perusse L, Guillemette C: Analysis of inherited genetic variations at the UGT1 locus in the French-Canadian population. Hum Mutat. 2009 Apr;30(4):677-87. [PubMed Link Image]
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 5731
Enzyme 22 Name UDP-glucuronosyltransferase 2B17
Enzyme 22 Synonyms
  1. UDPGT 2B17
  2. C19-steroid-specific UDP-glucuronosyltransferase
  3. C19-steroid-specific UDPGT
Enzyme 22 Gene Name UGT2B17
Enzyme 22 Protein Sequence >UDP-glucuronosyltransferase 2B17
MSLKWMSVFLLMQLSCYFSSGSCGKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSA
SILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEY
SDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYT
VEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEV
LGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSS
GENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQ
NDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRT
MSSRDLLNALKSVINDPIYKENIMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVA
AHNLTWIQYHSLDVIAFLLACVATMIFMITKCCLFCFRKLAKTGKKKKRD
Enzyme 22 Number of Residues 530
Enzyme 22 Molecular Weight 61094.9
Enzyme 22 Theoretical pI 8.73
Enzyme 22 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 22 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 22 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-3-alpha,17-beta-diol (3-alpha-diol) > testosterone > androsterone (ADT)
Enzyme 22 Pathways
Enzyme 22 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 22 Pfam Domain Function
Enzyme 22 Signals
  • 1-23
Enzyme 22 Transmembrane Regions
  • 495-515
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein Not Available
Enzyme 22 UniProtKB/Swiss-Prot ID O75795 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name UDB17_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 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 22 GenBank Gene ID U59209 Link Image
Enzyme 22 GeneCard ID UGT2B17 Link Image
Enzyme 22 GenAtlas ID UGT2B17 Link Image
Enzyme 22 HGNC ID HGNC:12547 Link Image
Enzyme 22 Chromosome Location 4
Enzyme 22 Locus 4q13
Enzyme 22 SNPs SNPJam Report Link Image
Enzyme 22 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]
  3. Yang TL, Chen XD, Guo Y, Lei SF, Wang JT, Zhou Q, Pan F, Chen Y, Zhang ZX, Dong SS, Xu XH, Yan H, Liu X, Qiu C, Zhu XZ, Chen T, Li M, Zhang H, Zhang L, Drees BM, Hamilton JJ, Papasian CJ, Recker RR, Song XP, Cheng J, Deng HW: Genome-wide copy-number-variation study identified a susceptibility gene, UGT2B17, for osteoporosis. Am J Hum Genet. 2008 Dec;83(6):663-74. Epub 2008 Nov 6. [PubMed Link Image]
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 5732
Enzyme 23 Name UDP-glucuronosyltransferase 1-6
Enzyme 23 Synonyms
  1. UDPGT 1-6
  2. UGT1*6
  3. UGT1-06
  4. UGT1.6
  5. Phenol-metabolizing UDP-glucuronosyltransferase
  6. UDP-glucuronosyltransferase 1-F
  7. UGT-1F
  8. UGT1F
  9. UDP-glucuronosyltransferase 1A6
Enzyme 23 Gene Name UGT1A6
Enzyme 23 Protein Sequence >UDP-glucuronosyltransferase 1-6
MACLLRSFQRISAGVFFLALWGMVVGDKLLVVPQDGSHWLSMKDIVEVLSDRGHEIVVVV
PEVNLLLKESKYYTRKIYPVPYDQEELKNRYQSFGNNHFAERSFLTAPQTEYRNNMIVIG
LYFINCQSLLQDRDTLNFFKESKFDALFTDPALPCGVILAEYLGLPSVYLFRGFPCSLEH
TFSRSPDPVSYIPRCYTKFSDHMTFSQRVANFLVNLLEPYLFYCLFSKYEELASAVLKRD
VDIITLYQKVSVWLLRYDFVLEYPRPVMPNMVFIGGINCKKRKDLSQEFEAYINASGEHG
IVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLL
GHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSE
DLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDL
TWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 23 Number of Residues 532
Enzyme 23 Molecular Weight 60750.2
Enzyme 23 Theoretical pI 8.55
Enzyme 23 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 23 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 23 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 23 Pathways
Enzyme 23 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • 1-26
Enzyme 23 Transmembrane Regions
  • 490-506
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 45827765 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID P19224 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name UD16_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 Gene Sequence >1599 bp
ATGGCCTGCCTCCTTCGCTCATTTCAGAGAATTTCTGCAGGGGTTTTCTTCTTAGCACTT
TGGGGCATGGTTGTAGGTGACAAGCTGCTGGTGGTCCCTCAGGACGGAAGCCACTGGCTT
AGTATGAAGGATATAGTTGAGGTTCTCAGTGACCGGGGTCATGAGATTGTAGTGGTGGTG
CCTGAAGTTAATTTGCTTTTGAAAGAATCCAAATACTACACAAGAAAAATCTATCCAGTG
CCGTATGACCAAGAAGAGCTGAAGAACCGTTACCAATCATTTGGAAACAATCACTTTGCT
GAGCGATCATTCCTAACTGCTCCTCAGACAGAGTACAGGAATAACATGATTGTTATTGGC
CTGTACTTCATCAACTGCCAGAGCCTCCTGCAGGACAGGGACACCCTGAACTTCTTTAAG
GAGAGCAAGTTTGATGCTCTTTTCACAGACCCAGCCTTACCCTGTGGGGTGATCCTGGCT
GAGTATTTGGGCCTACCATCTGTGTACCTCTTCAGGGGTTTTCCGTGTTCCCTGGAGCAT
ACATTCAGCAGAAGCCCAGACCCTGTGTCCTACATTCCCAGGTGCTACACAAAGTTTTCA
GACCACATGACTTTTTCCCAACGAGTGGCCAACTTCCTTGTTAATTTGTTGGAGCCCTAT
CTATTTTATTGTCTGTTTTCAAAGTATGAAGAACTCGCATCAGCTGTCCTCAAGAGAGAT
GTGGATATAATCACCTTATATCAGAAGGTCTCTGTTTGGCTGTTAAGATATGACTTTGTG
CTTGAATATCCTAGGCCGGTCATGCCCAACATGGTCTTCATTGGAGGTATCAACTGTAAG
AAGAGGAAAGACTTGTCTCAGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGA
ATTGTGGTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCA
ATTGCTGATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGA
CCATCGAATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTT
GGTCACCCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGC
ATATGCAATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCA
AAGCGCATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAA
GATTTAGAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATG
CGCCTCTCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGG
GTGGAGTTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTC
ACCTGGTACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACA
GTGGCCTTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAA
GGGCGAGTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 23 GenBank Gene ID NM_001072.3 Link Image
Enzyme 23 GeneCard ID UGT1A6 Link Image
Enzyme 23 GenAtlas ID UGT1A6 Link Image
Enzyme 23 HGNC ID HGNC:12538 Link Image
Enzyme 23 Chromosome Location 2
Enzyme 23 Locus 2q37
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 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]
  6. Nagar S, Zalatoris JJ, Blanchard RL: Human UGT1A6 pharmacogenetics: identification of a novel SNP, characterization of allele frequencies and functional analysis of recombinant allozymes in human liver tissue and in cultured cells. Pharmacogenetics. 2004 Aug;14(8):487-99. [PubMed Link Image]
  7. Menard V, Girard H, Harvey M, Perusse L, Guillemette C: Analysis of inherited genetic variations at the UGT1 locus in the French-Canadian population. Hum Mutat. 2009 Apr;30(4):677-87. [PubMed Link Image]
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 5733
Enzyme 24 Name UDP-glucuronosyltransferase 1-5
Enzyme 24 Synonyms
  1. UDPGT 1-5
  2. UGT1*5
  3. UGT1-05
  4. UGT1.5
  5. UDP-glucuronosyltransferase 1-E
  6. UGT-1E
  7. UGT1E
  8. UDP-glucuronosyltransferase 1A5
Enzyme 24 Gene Name UGT1A5
Enzyme 24 Protein Sequence >UDP-glucuronosyltransferase 1-5
MATGLQVPLPQLATGLLLLLSVQPWAESGKVLVVPTDGSHWLSMREALRDLHARGHQVVV
LTLEVNMYIKEENFFTLTTYAISWTQDEFDRLLLGHTQSFFETEHLLMKFSRRMAIMNNM
SLIIHRSCVELLHNEALIRHLHATSFDVVLTDPFHLCAAVLAKYLSIPAVFFLRNIPCDL
DFKGTQCPNPSSYIPRLLTTNSDHMTFLQRVKNMLYPLALSYLCHAVSAPYASLASELFQ
REVSVVDLVSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANGKPLSQEFEAYINASGE
HGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQND
LLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMT
SEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAH
DLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 24 Number of Residues 534
Enzyme 24 Molecular Weight 60070.6
Enzyme 24 Theoretical pI 8.14
Enzyme 24 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 24 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 24 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 24 Pathways
Enzyme 24 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • 1-28
Enzyme 24 Transmembrane Regions
  • 492-508
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein 11118746 Link Image
Enzyme 24 UniProtKB/Swiss-Prot ID P35504 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name UD15_HUMAN Link Image
Enzyme 24 PDB ID Not Available
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence >1605 bp
ATGGCCACAGGACTCCAGGTTCCCCTGCCGCAGCTGGCCACAGGACTGCTGCTTCTCCTC
AGTGTCCAGCCCTGGGCTGAGAGTGGGAAGGTGCTGGTGGTGCCCACTGATGGCAGCCAC
TGGCTCAGCATGCGGGAGGCCTTGCGGGACCTCCATGCGAGAGGCCACCAGGTGGTGGTC
CTCACCCTGGAGGTGAATATGTACATCAAAGAAGAGAACTTTTTCACCCTGACAACGTAT
GCCATTTCATGGACCCAGGACGAATTTGATCGCCTTTTGCTGGGTCACACTCAATCGTTC
TTTGAAACAGAACATCTTCTGATGAAATTTTCTAGAAGAATGGCAATTATGAACAATATG
TCTTTGATCATACATAGGTCTTGTGTGGAGCTACTGCATAATGAGGCCCTGATCAGGCAC
CTGCATGCTACTTCCTTTGATGTGGTTCTAACAGACCCCTTTCACCTCTGCGCGGCGGTG
CTGGCTAAGTACCTGTCGATTCCTGCTGTGTTTTTCTTGAGGAACATTCCATGTGATTTA
GACTTTAAGGGCACACAGTGTCCAAACCCTTCCTCCTATATTCCTAGATTACTAACGACC
AATTCAGACCACATGACATTCCTGCAAAGGGTCAAGAACATGCTCTACCCTCTGGCCCTG
TCCTACCTTTGCCATGCTGTTTCTGCTCCTTATGCAAGCCTTGCCTCTGAGCTTTTTCAG
AGAGAGGTGTCAGTGGTGGATCTTGTCAGCCATGCATCTGTGTGGCTGTTCCGAGGGGAC
TTTGTGATGGATTACCCCAGGCCGATCATGCCCAACATGGTCTTCATTGGGGGCATCAAC
TGTGCCAACGGGAAGCCACTATCTCAGGAATTTGAAGCCTACATTAATGCTTCTGGAGAA
CATGGAATTGTGGTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCT
ATGGCAATTGCTGATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGA
ACCCGACCATCGAATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGAT
CTGCTTGGTCACCCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTAT
GAAAGCATATGCAATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGAC
AATGCAAAGCGCATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACT
TCTGAAGATTTAGAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAAC
ATCATGCGCCTCTCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTG
TTCTGGGTGGAGTTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCAC
GACCTCACCTGGTACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTG
CTGACAGTGGCCTTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGG
AAAAAAGGGCGAGTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 24 GenBank Gene ID AF297093 Link Image
Enzyme 24 GeneCard ID UGT1A5 Link Image
Enzyme 24 GenAtlas ID UGT1A5 Link Image
Enzyme 24 HGNC ID HGNC:12537 Link Image
Enzyme 24 Chromosome Location 2
Enzyme 24 Locus 2q37
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 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 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 5734
Enzyme 25 Name UDP-glucuronosyltransferase 2B11
Enzyme 25 Synonyms
  1. UDPGT 2B11
Enzyme 25 Gene Name UGT2B11
Enzyme 25 Protein Sequence >UDP-glucuronosyltransferase 2B11
MTLKWTSVLLLIHLSCYFSSGSCGKVLVWAAEYSHWMNMKTILKELVQRGHEVTVLASSA
SILFDPNDASTLKFEVYPTSLTKTEFENIIMQQVKRWSDIRKDSFWLYFSQEQEILWELY
DIFRNFCKDVVSNKKVMKKLQESRFDIVFADAVFPCGELLAALLNIRFVYSLRFTPGYTI
ERHSGGLIFPPSYIPIVMSKLSDQMTFMERVKNMIYVLYFDFWFQMSDMKKWDQFYSEVL
GRPTTLFETMGKADIWLMRNSWSFQFPHPFLPNVDFVGGFHCKPAKPLPKEMEEFVQSSG
ENGVVVFSLGSVISNMTAERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRLDFNTM
SSTDLLNALKTVINDPLYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMPHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLACVATVIFIITKFCLFCFWKFARKGKKGKRD
Enzyme 25 Number of Residues 529
Enzyme 25 Molecular Weight 61037.8
Enzyme 25 Theoretical pI 9.29
Enzyme 25 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 25 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 25 Specific Function UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 25 Pathways
Enzyme 25 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • 1-21
Enzyme 25 Transmembrane Regions
  • 493-513
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein 3360273 Link Image
Enzyme 25 UniProtKB/Swiss-Prot ID O75310 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name UDB11_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 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 25 GenBank Gene ID AF016492 Link Image
Enzyme 25 GeneCard ID UGT2B11 Link Image
Enzyme 25 GenAtlas ID UGT2B11 Link Image
Enzyme 25 HGNC ID HGNC:12545 Link Image
Enzyme 25 Chromosome Location 4
Enzyme 25 Locus 4q13.2
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 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]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 5845
Enzyme 26 Name GTP:AMP phosphotransferase, mitochondrial
Enzyme 26 Synonyms
  1. Adenylate kinase 3
  2. AK 3
  3. Adenylate kinase 3 alpha-like 1
Enzyme 26 Gene Name AK3
Enzyme 26 Protein Sequence >GTP:AMP phosphotransferase, mitochondrial
MGASARLLRAVIMGAPGSGKGTVSSRITTHFELKHLSSGDLLRDNMLRGTEIGVLAKAFI
DQGKLIPDDVMTRLALHELKNLTQYSWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEV
IKQRLTARWIHPASGRVYNIEFNPPKTVGIDDLTGEPLIQREDDKPETVIKRLKAYEDQT
KPVLEYYQKKGVLETFSGTETNKIWPYVYAFLQTKVPQRSQKASVTP
Enzyme 26 Number of Residues 227
Enzyme 26 Molecular Weight 25565.2
Enzyme 26 Theoretical pI 9.64
Enzyme 26 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • adenylate kinase activity
  • binding
  • catalytic activity
  • kinase activity
  • nucleobase, nucleoside, nucleotide kinase activity
  • nucleoside binding
  • nucleotide kinase activity
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular nitrogen compound metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
Component
Enzyme 26 General Function Involved in ATP binding
Enzyme 26 Specific Function NTP + AMP = NDP + ADP
Enzyme 26 Pathways
Enzyme 26 Reactions
  • nucleoside triphosphate + AMP = nucleoside diphosphate + ADP [RN:R00333]
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein 6518533 Link Image
Enzyme 26 UniProtKB/Swiss-Prot ID Q9UIJ7 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name KAD3_HUMAN Link Image
Enzyme 26 PDB ID 2AK3 Link Image
Enzyme 26 PDB File Show
Enzyme 26 3D Structure
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence >684 bp
ATGGGGGCGTCGGGGCGGCTGCTGCGAGCGGTGATCATGGGGGCCCCGGGCTCGGGCAAG
GGCACCGTGTCGTCCCGCATCACTACACACTTCGAGCTGAAGCACCTCTCCCGCGGGGAC
CTGCTCCGGGACAACATGCTGCGGGGCACAGAAATTGGCGTGTTAGCCCAGGCTTTCATT
GACCAAGGGAAACTCATCCCAGATTATGTCACGACTCGGCTGGCCCTTCATGAGCTGAAA
AACCTCACCCAGTATAGCTGGCTGTTGGATGGTTTTCCAAGGACACTTCCACAGGCAGAA
GCCCTAGATAGAGCTTATCAGATCGACACAGTGATTAACCTGAATGTGCCCTTTGAGGTC
ATTAAACAACGCCTTACTGCTCGCTGGATTCATCCCGCCAGTGGCCGAGTCTATAACATT
GAATTCAACCCTCCCAAAACTGTGGGCATTGATGACCTGACTGGGGAGCCTCTCATTCAG
CGTGAGGATGATAAACCAGAGACGGTTATCAAGAGACTAAAGGCTTATGAAGACCAAACA
AAGCCAGTCCTGGAATATTACCAGAAAAAAGGGGTGTTGGAAACATTCTCCGGAACAGAA
ACCAACAAGATTTGGCCCTATGTATATGCTTTCCTACAAACTAAAGTTCCACAAAGAAGC
CAGAAAGCTTCAGTTACTCCATGA
Enzyme 26 GenBank Gene ID AB021870 Link Image
Enzyme 26 GeneCard ID AK3 Link Image
Enzyme 26 GenAtlas ID AK3 Link Image
Enzyme 26 HGNC ID HGNC:17376 Link Image
Enzyme 26 Chromosome Location 9
Enzyme 26 Locus 9p24.1
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 6009
Enzyme 27 Name 6-phosphofructokinase type C
Enzyme 27 Synonyms
  1. 6-phosphofructokinase, platelet type
  2. Phosphofructo-1-kinase isozyme C
  3. PFK-C
  4. Phosphofructokinase 1
  5. Phosphohexokinase
Enzyme 27 Gene Name PFKP
Enzyme 27 Protein Sequence >6-phosphofructokinase type C
MDADDSRAPKGSLRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFI
YEGYQGMVDGGSNIAEADWESVSSILQVGGTIIGSARCQAFRTREGRLKAACNLLQRGIT
NLCVIGGDGSLTGANLFRKEWSGLLEELARNGQIDKEAVQKYAYLNVVGMVGSIDNDFCG
TDMTIGTDSALHRIIEVVDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLP
ESPPEEGWEEQMCVKLSENRARKKRLNIIIVAEGAIDTQNKPITSEKIKELVVTQLGYDT
RVTILGHVQRGGTPSAFDRILASRMGVEAVIALLEATPDTPACVVSLNGNHAVRLPLMEC
VQMTQDVQKAMDERRFQDAVRLRGRSFAGNLNTYKRLAIKLPDDQIPKTNCNVAVINVGA
PAAGMNAAVRSAVRVGIADGHRMLAIYDGFDGFAKGQIKEIGWTDVGGWTGQGGSILGTK
RVLPGKYLEEIATQMRTHSINALLIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVS
NNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGA
DAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGKG
VFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMEWITAKLKEARGRGKKFTTDDSICVL
GISKRNVIFQPVAELKKQTDFEHRIPKEQWWLKLRPLMKILAKYKASYDVSDSGQLEHVQ
PWSV
Enzyme 27 Number of Residues 784
Enzyme 27 Molecular Weight 85595.4
Enzyme 27 Theoretical pI 7.60
Enzyme 27 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 metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
  • 6-phosphofructokinase complex
  • cell part
  • cytoplasm
  • intracellular part
  • macromolecular complex
  • protein complex
Enzyme 27 General Function Involved in 6-phosphofructokinase activity
Enzyme 27 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 27 Pathways
Enzyme 27 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID Q01813 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name K6PP_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 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 27 GenBank Gene ID D25328 Link Image
Enzyme 27 GeneCard ID PFKP Link Image
Enzyme 27 GenAtlas ID PFKP Link Image
Enzyme 27 HGNC ID HGNC:8878 Link Image
Enzyme 27 Chromosome Location 1
Enzyme 27 Locus 10p15.3-p15.2
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed Link Image]
  7. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  8. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  9. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  10. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  11. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  12. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  13. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 6033
Enzyme 28 Name 6-phosphofructokinase, liver type
Enzyme 28 Synonyms
  1. Phosphofructo-1-kinase isozyme B
  2. PFK-B
  3. Phosphofructokinase 1
  4. Phosphohexokinase
Enzyme 28 Gene Name PFKL
Enzyme 28 Protein Sequence >6-phosphofructokinase, liver type
MAAVDLEKLRASGAGKAIGVLTSGGDAQGMNAAVRAVTRMGIYVGAKVFLIYEGYEGLVE
GGENIKQANWLSVSNIIQLGGTIIGSARCKAFTTREGRRAAAYNLVQHGITNLCVIGGDG
SLTGANIFRSEWGSLLEELVAEGKISETTARTYSHLNIAGLVGSIDNDFCGTDMTIGTDS
ALHRIMEVIDAITTTAQSHQRTFVLEVMGRHCGYLALVSALASGADWLFIPEAPPEDGWE
NFMCERLGETRSRGSRLNIIIIAEGAIDRNGKPISSSYVKDLVVQRLGFDTRVTVLGHVQ
RGGTPSAFDRILSSKMGMEAVMALLEATPDTPACVVTLSGNQSVRLPLMECVQMTKEVQK
AMDDKRFDEATQLRGGSFENNWNIYKLLAHQKPPKEKSNFSLAILNVGAPAAGMNAAVRS
AVRTGISHGHTVYVVHDGFEGLAKGQVQEVGWHDVAGWLGRGGSMLGTKRTLPKGQLESI
VENIRIYGIHALLVVGGFEAYEGVLQLVEARGRYEELCIVMCVIPATISNNVPGTDFSLG
SDTAVNAAMESCDRIKQSASGTKRRVFIVETMGGYCGYLATVTGIAVGADAAYVFEDPFN
IHDLKVNVEHMTEKMKTDIQRGLVLRNEKCHDYYTTEFLYNLYSSEGKGVFDCRTNVLGH
LQQGGAPTPFDRNYGTKLGVKAMLWLSEKLREVYRKGRVFANAPDSACVIGLKKKAVAFS
PVTELKKDTDFEHRMPREQWWLSLRLMLKMLAQYRISMAAYVSGELEHVTRRTLSMDKGF
Enzyme 28 Number of Residues 780
Enzyme 28 Molecular Weight 85017.8
Enzyme 28 Theoretical pI 7.54
Enzyme 28 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 metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
  • 6-phosphofructokinase complex
  • cell part
  • cytoplasm
  • intracellular part
  • macromolecular complex
  • protein complex
Enzyme 28 General Function Involved in 6-phosphofructokinase activity
Enzyme 28 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 28 Pathways
Enzyme 28 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein 35431 Link Image
Enzyme 28 UniProtKB/Swiss-Prot ID P17858 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name K6PL_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 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 28 GenBank Gene ID X15573 Link Image
Enzyme 28 GeneCard ID PFKL Link Image
Enzyme 28 GenAtlas ID PFKL Link Image
Enzyme 28 HGNC ID HGNC:8876 Link Image
Enzyme 28 Chromosome Location 2
Enzyme 28 Locus 21q22.3
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
Enzyme 28 Metabolite References Not Available
Enzyme 29 [top]
Enzyme 29 ID 6037
Enzyme 29 Name 6-phosphofructokinase, muscle type
Enzyme 29 Synonyms
  1. Phosphofructo-1-kinase isozyme A
  2. PFK-A
  3. Phosphofructokinase-M
  4. Phosphofructokinase 1
  5. Phosphohexokinase
Enzyme 29 Gene Name PFKM
Enzyme 29 Protein Sequence >6-phosphofructokinase, muscle type
MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVD
GGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDG
SLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDS
ALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWE
EHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQ
RGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTK
AMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVR
STVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQ
ISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSV
GADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPF
TIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLG
HMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVF
QPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV
Enzyme 29 Number of Residues 780
Enzyme 29 Molecular Weight 85181.9
Enzyme 29 Theoretical pI 8.07
Enzyme 29 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 metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
  • 6-phosphofructokinase complex
  • cell part
  • cytoplasm
  • intracellular part
  • macromolecular complex
  • protein complex
Enzyme 29 General Function Involved in 6-phosphofructokinase activity
Enzyme 29 Specific Function ATP + D-fructose 6-phosphate = ADP + D- fructose 1,6-bisphosphate
Enzyme 29 Pathways
Enzyme 29 Reactions
  • ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate [RN:R00756]
Enzyme 29 Pfam Domain Function
Enzyme 29 Signals
  • None
Enzyme 29 Transmembrane Regions
  • None
Enzyme 29 Essentiality Not Available
Enzyme 29 GenBank ID Protein 189855 Link Image
Enzyme 29 UniProtKB/Swiss-Prot ID P08237 Link Image
Enzyme 29 UniProtKB/Swiss-Prot Entry Name K6PF_HUMAN Link Image
Enzyme 29 PDB ID Not Available
Enzyme 29 Cellular Location Not Available
Enzyme 29 Gene Sequence >2343 bp
ATGACCCATGAAGAGCACCATGCAGCCAAAACCCTGGGGATTGGCAAAGCCATTGCTGTC
TTAACCTCTGGTGGAGATGCCCAAGGTATGAATGCTGCTGTCAGGGCTGTGGTTCGAGTT
GGTATCTTCACCGGTGCCCGTGTCTTCTTTGTCCATGAGGGTTATCAAGGCCTGGTGGAT
GGTGGAGATCACATCAAGGAAGCCACCTGGGAGAGCGTTTCGATGATGCTTCAGCTGGGA
GGCACGGTGATTGGAAGTGCCCGGTGCAAGGACTTTCGGGAACGAGAAGGACGACTCCGA
GCTGCCTACAACCTGGTGAAGCGTGGGATCACCAATCTCTGTGTCATTGGGGGTGATGGC
AGCCTCACTGGGGCTGACACCTTCCGTTCTGAGTGGAGTGACTTGTTGAGTGACCTCCAG
AAAGCAGGTAAGATCACAGATGAGGAGGCTACGAAGTCCAGCTACCTGAACATTGTGGGC
CTGGTTGGGTCAATTGACAATGACTTCTGTGGCACCGATATGACCATTGGCACTGACTCT
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 29 GenBank Gene ID M26066 Link Image
Enzyme 29 GeneCard ID PFKM Link Image
Enzyme 29 GenAtlas ID PFKM Link Image
Enzyme 29 HGNC ID HGNC:8877 Link Image
Enzyme 29 Chromosome Location 1
Enzyme 29 Locus 12q13.3
Enzyme 29 SNPs SNPJam Report Link Image
Enzyme 29 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. 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]
  7. Raben N, Sherman JB: Mutations in muscle phosphofructokinase gene. Hum Mutat. 1995;6(1):1-6. [PubMed Link Image]
  8. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  9. 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]
  10. 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]
  11. 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 29 Metabolite References Not Available
Enzyme 30 [top]
Enzyme 30 ID 6039
Enzyme 30 Name Pyruvate kinase isozymes M1/M2
Enzyme 30 Synonyms
  1. Cytosolic thyroid hormone-binding protein
  2. CTHBP
  3. Opa-interacting protein 3
  4. OIP-3
  5. Pyruvate kinase 2/3
  6. Pyruvate kinase muscle isozyme
  7. Thyroid hormone-binding protein 1
  8. THBP1
  9. Tumor M2-PK
  10. p58
Enzyme 30 Gene Name PKM2
Enzyme 30 Protein Sequence >Pyruvate kinase isozymes M1/M2
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVET
LKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIR
TGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGL
ISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMV
FASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIE
IPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIM
LSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEAS
FKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQE
AWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
Enzyme 30 Number of Residues 531
Enzyme 30 Molecular Weight 57936.4
Enzyme 30 Theoretical pI 7.94
Enzyme 30 GO Classification
Function
  • alkali metal ion binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • magnesium ion binding
  • metal ion binding
  • potassium ion binding
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 30 General Function Involved in magnesium ion binding
Enzyme 30 Specific Function Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival
Enzyme 30 Pathways
Enzyme 30 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate [RN:R00200]
Enzyme 30 Pfam Domain Function
Enzyme 30 Signals
  • None
Enzyme 30 Transmembrane Regions
  • None
Enzyme 30 Essentiality Not Available
Enzyme 30 GenBank ID Protein 33286418 Link Image
Enzyme 30 UniProtKB/Swiss-Prot ID P14618 Link Image
Enzyme 30 UniProtKB/Swiss-Prot Entry Name KPYM_HUMAN Link Image
Enzyme 30 PDB ID 1F3X Link Image
Enzyme 30 PDB File Show
Enzyme 30 3D Structure
Enzyme 30 Cellular Location Not Available
Enzyme 30 Gene Sequence >1596 bp
ATGTCGAAGCCCCATAGTGAAGCCGGGACTGCCTTCATTCAGACCCAGCAGCTGCACGCA
GCCATGGCTGACACATTCCTGGAGCACATGTGCCGCCTGGACATTGATTCACCACCCATC
ACAGCCCGGAACACTGGCATCATCTGTACCATTGGCCCAGCTTCCCGATCAGTGGAGACG
TTGAAGGAGATGATTAAGTCTGGAATGAATGTGGCTCGTCTGAACTTCTCTCATGGAACT
CATGAGTACCATGCGGAGACCATCAAGAATGTGCGCACAGCCACGGAAAGCTTTGCTTCT
GACCCCATCCTCTACCGGCCCGTTGCTGTGGCTCTAGACACTAAAGGACCTGAGATCCGA
ACTGGGCTCATCAAGGGCAGCGGCACTGCAGAGGTGGAGCTGAAGAAGGGAGCCACTCTC
AAAATCACGCTGGATAACGCCTACATGGAAAAGTGTGACGAGAACATCCTGTGGCTGGAC
TACAAGAACATCTGCAAGGTGGTGGAAGTGGGCAGCAAGATCTACGTGGATGATGGGCTT
ATTTCTCTCCAGGTGAAGCAGAAAGGTGCCGACTTCCTGGTGACGGAGGTGGAAAATGGT
GGCTCCTTGGGCAGCAAGAAGGGTGTGAACCTTCCTGGGGCTGCTGTGGACTTGCCTGCT
GTGTCGGAGAAGGACATCCAGGATCTGAAGTTTGGGGTCGAGCAGGATGTTGATATGGTG
TTTGCGTCATTCATCCGCAAGGCATCTGATGTCCATGAAGTTAGGAAGGTCCTGGGAGAG
AAGGGAAAGAACATCAAGATTATCAGCAAAATCGAGAATCATGAGGGGGTTCGGAGGTTT
GATGAAATCCTGGAGGCCAGTGATGGGATCATGGTGGCTCGTGGTGATCTAGGCATTGAG
ATTCCTGCAGAGAAGGTCTTCCTTGCTCAGAAGATGATGATTGGACGGTGCAACCGAGCT
GGGAAGCCTGTCATCTGTGCTACTCAGATGCTGGAGAGCATGATCAAGAAGCCCCGCCCC
ACTCGGGCTGAAGGCAGTGATGTGGCCAATGCAGTCCTGGATGGAGCCGACTGCATCATG
CTGTCTGGAGAAACAGCCAAAGGGGACTATCCTCTGGAGGCTGTGCGCATGCAGCACCTG
ATTGCCCGTGAGGCAGAGGCTGCCATCTACCACTTGCAATTATTTGAGGAACTCCGCCGC
CTGGCGCCCATTACCAGCGACCCCACAGAAGCCACCGCCGTGGGTGCCGTGGAGGCCTCC
TTCAAGTGCTGCAGTGGGGCCATAATCGTCCTCACCAAGTCTGGCAGGTCTGCTCACCAG
GTGGCCAGATACCGCCCACGTGCCCCCATCATTGCTGTGACCCGGAATCCCCAGACAGCT
CGTCAGGCCCACCTGTACCGTGGCATCTTCCCTGTGCTGTGCAAGGACCCAGTCCAGGAG
GCCTGGGCTGAGGACGTGGACCTCCGGGTGAACTTTGCCATGAATGTTGGCAAGGCCCGA
GGCTTCTTCAAGAAGGGAGATGTGGTCATTGTGCTGACCGGATGGCGCCCTGGCTCCGGC
TTCACCAACACCATGCGTGTTGTTCCTGTGCCGTGA
Enzyme 30 GenBank Gene ID NM_002654.3 Link Image
Enzyme 30 GeneCard ID PKM2 Link Image
Enzyme 30 GenAtlas ID PKM2 Link Image
Enzyme 30 HGNC ID HGNC:9021 Link Image
Enzyme 30 Chromosome Location 1
Enzyme 30 Locus 15q22
Enzyme 30 SNPs SNPJam Report Link Image
Enzyme 30 General References
  1. Tani K, Yoshida MC, Satoh H, Mitamura K, Noguchi T, Tanaka T, Fujii H, Miwa S: Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment and expression in hepatoma. Gene. 1988 Dec 20;73(2):509-16. [PubMed Link Image]
  2. Kato H, Fukuda T, Parkison C, McPhie P, Cheng SY: Cytosolic thyroid hormone-binding protein is a monomer of pyruvate kinase. Proc Natl Acad Sci U S A. 1989 Oct;86(20):7861-5. [PubMed Link Image]
  3. Takenaka M, Noguchi T, Sadahiro S, Hirai H, Yamada K, Matsuda T, Imai E, Tanaka T: Isolation and characterization of the human pyruvate kinase M gene. Eur J Biochem. 1991 May 23;198(1):101-6. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Ashizawa K, McPhie P, Lin KH, Cheng SY: An in vitro novel mechanism of regulating the activity of pyruvate kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate. Biochemistry. 1991 Jul 23;30(29):7105-11. [PubMed Link Image]
  8. 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]
  9. Williams JM, Chen GC, Zhu L, Rest RF: Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth. Mol Microbiol. 1998 Jan;27(1):171-86. [PubMed Link Image]
  10. Garcia-Gonzalo FR, Cruz C, Munoz P, Mazurek S, Eigenbrodt E, Ventura F, Bartrons R, Rosa JL: Interaction between HERC1 and M2-type pyruvate kinase. FEBS Lett. 2003 Mar 27;539(1-3):78-84. [PubMed Link Image]
  11. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed Link Image]
  12. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  13. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  14. Stetak A, Veress R, Ovadi J, Csermely P, Keri G, Ullrich A: Nuclear translocation of the tumor marker pyruvate kinase M2 induces programmed cell death. Cancer Res. 2007 Feb 15;67(4):1602-8. [PubMed Link Image]
  15. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed Link Image]
  16. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  17. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed Link Image]
  18. Shimada N, Shinagawa T, Ishii S: Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML tumor suppressor protein. Genes Cells. 2008 Mar;13(3):245-54. [PubMed Link Image]
  19. Lee J, Kim HK, Han YM, Kim J: Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with Oct-4 in regulating transcription. Int J Biochem Cell Biol. 2008;40(5):1043-54. Epub 2007 Nov 29. [PubMed Link Image]
  20. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed Link Image]
  21. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  22. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  23. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  24. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed Link Image]
  25. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
  26. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  27. Dombrauckas JD, Santarsiero BD, Mesecar AD: Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis. Biochemistry. 2005 Jul 12;44(27):9417-29. [PubMed Link Image]
Enzyme 30 Metabolite References Not Available
Enzyme 31 [top]
Enzyme 31 ID 6041
Enzyme 31 Name Pyruvate kinase isozymes R/L
Enzyme 31 Synonyms
  1. Pyruvate kinase 1
  2. R-type/L-type pyruvate kinase
  3. Red cell/liver pyruvate kinase
Enzyme 31 Gene Name PKLR
Enzyme 31 Protein Sequence >Pyruvate kinase isozymes R/L
MSIQENISSLQLRSWVSKSQRDLAKSILIGAPGGPAGYLRRASVAQLTQELGTAFFQQQQ
LPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFS
HGSHEYHAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEVELVKG
SQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQKIGPEGLVTQV
ENGGVLGSRKGVNLPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRAA
LGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC
NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVKM
QHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS
AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIESG
KLRGFLRVGDLVIVVTGWRPGSGYTNIMRVLSIS
Enzyme 31 Number of Residues 574
Enzyme 31 Molecular Weight 61829.6
Enzyme 31 Theoretical pI 7.83
Enzyme 31 GO Classification
Function
  • alkali metal ion binding
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • kinase activity
  • magnesium ion binding
  • metal ion binding
  • potassium ion binding
  • pyruvate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolic process
  • glucose catabolic process
  • glucose metabolic process
  • glycolysis
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 31 General Function Involved in magnesium ion binding
Enzyme 31 Specific Function Plays a key role in glycolysis
Enzyme 31 Pathways
Enzyme 31 Reactions
  • ATP + pyruvate = ADP + phosphoenolpyruvate [RN:R00200]
Enzyme 31 Pfam Domain Function
Enzyme 31 Signals
  • None
Enzyme 31 Transmembrane Regions
  • None
Enzyme 31 Essentiality Not Available
Enzyme 31 GenBank ID Protein Not Available
Enzyme 31 UniProtKB/Swiss-Prot ID P30613 Link Image
Enzyme 31 UniProtKB/Swiss-Prot Entry Name KPYR_HUMAN Link Image
Enzyme 31 PDB ID 1LIU Link Image
Enzyme 31 PDB File Show
Enzyme 31 3D Structure
Enzyme 31 Cellular Location Not Available
Enzyme 31 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 31 GenBank Gene ID AB015983 Link Image
Enzyme 31 GeneCard ID PKLR Link Image
Enzyme 31 GenAtlas ID PKLR Link Image
Enzyme 31 HGNC ID HGNC:9020 Link Image
Enzyme 31 Chromosome Location 1
Enzyme 31 Locus 1q21
Enzyme 31 SNPs SNPJam Report Link Image
Enzyme 31 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. 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]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
  7. Beutler E, Baronciani L: Mutations in pyruvate kinase. Hum Mutat. 1996;7(1):1-6. [PubMed Link Image]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
  13. Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A: Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia. J Biol Chem. 2002 Jun 28;277(26):23807-14. Epub 2002 Apr 17. [PubMed Link Image]
  14. 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]
  15. 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]
  16. 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]
  17. 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]
  18. 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]
  19. 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]
  20. 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]
  21. 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]
  22. 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]
  23. 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]
  24. 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]
  25. 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]
  26. van Wijk R, Huizinga EG, van Wesel AC, van Oirschot BA, Hadders MA, van Solinge WW: Fifteen novel mutations in PKLR associated with pyruvate kinase (PK) deficiency: structural implications of amino acid substitutions in PK. Hum Mutat. 2009 Mar;30(3):446-53. [PubMed Link Image]
Enzyme 31 Metabolite References Not Available
Enzyme 32 [top]
Enzyme 32 ID 6126
Enzyme 32 Name Ceramide glucosyltransferase
Enzyme 32 Synonyms
  1. GLCT-1
  2. Glucosylceramide synthase
  3. GCS
  4. UDP-glucose ceramide glucosyltransferase
  5. UDP-glucose:N-acylsphingosine D-glucosyltransferase
Enzyme 32 Gene Name UGCG
Enzyme 32 Protein Sequence >Ceramide glucosyltransferase
MALLDLALEGMAVFGFVLFLVLWLMHFMAIIYTRLHLNKKATDKQPYSKLPGVSLLKPLK
GVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVG
INPKINNLMPGYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTEKVGLVHGLPYVADRQGF
AATLEQVYFGTSHPRYYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMA
KAIADRGWRFAMSTQVAMQNSGSYSISQFQSRMIRWTKLRINMLPATIICEPISECFVAS
LIIGWAAHHVFRWDIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVAWFIRESMT
IYIFLSALWDPTISWRTGRYRLRCGGTAEEILDV
Enzyme 32 Number of Residues 394
Enzyme 32 Molecular Weight 44853.3
Enzyme 32 Theoretical pI 7.86
Enzyme 32 GO Classification Not Available
Enzyme 32 General Function Cell wall/membrane/envelope biogenesis
Enzyme 32 Specific Function Catalyzes the first glycosylation step in glycosphingolipid biosynthesis, the transfer of glucose to ceramide. May also serve as a "flippase"
Enzyme 32 Pathways
Enzyme 32 Reactions
  • UDP-glucose + an N-acylsphingosine = UDP + a D-glucosyl-N-acylsphingosine [RN:R01497 R06275]
Enzyme 32 Pfam Domain Function
Enzyme 32 Signals
  • None
Enzyme 32 Transmembrane Regions
  • 11-31 286-306 314-334 349-369
Enzyme 32 Essentiality Not Available
Enzyme 32 GenBank ID Protein Not Available
Enzyme 32 UniProtKB/Swiss-Prot ID Q16739 Link Image
Enzyme 32 UniProtKB/Swiss-Prot Entry Name CEGT_HUMAN Link Image
Enzyme 32 PDB ID Not Available
Enzyme 32 Cellular Location Not Available
Enzyme 32 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 32 GenBank Gene ID D50840 Link Image
Enzyme 32 GeneCard ID UGCG Link Image
Enzyme 32 GenAtlas ID UGCG Link Image
Enzyme 32 HGNC ID HGNC:12524 Link Image
Enzyme 32 Chromosome Location 9
Enzyme 32 Locus 9q31
Enzyme 32 SNPs SNPJam Report Link Image
Enzyme 32 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]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 32 Metabolite References Not Available
Enzyme 33 [top]
Enzyme 33 ID 6155
Enzyme 33 Name Beta-1,4 N-acetylgalactosaminyltransferase 1
Enzyme 33 Synonyms
  1. (N-acetylneuraminyl)-galactosylglucosylceramide
  2. GM2/GD2 synthase
  3. GalNAc-T
Enzyme 33 Gene Name B4GALNT1
Enzyme 33 Protein Sequence >Beta-1,4 N-acetylgalactosaminyltransferase 1
MWLGRRALCALVLLLACASLGLLYASTRDAPGLRLPLAPWAPPQSPRRPELPDLAPEPRY
AHIPVRIKEQVVGLLAWNNCSCESSGGGLPLPFQKQVRAIDLTKAFDPAELRAASATREQ
EFQAFLSRSQSPADQLLIAPANSPLQYPLQGVEVQPLRSILVPGLSLQAASGQEVYQVNL
TASLGTWDVAGEVTGVTLTGEGQADLTLVSPGLDQLNRQLQLVTYSSRSYQTNTADTVRF
STEGHEAAFTIRIRHPPNPRLYPPGSLPQGAQYNISALVTIATKTFLRYDRLRALITSIR
RFYPTVTVVIADDSDKPERVSGPYVEHYLMPFGKGWFAGRNLAVSQVTTKYVLWVDDDFV
FTARTRLERLVDVLERTPLDLVGGAVREISGFATTYRQLLSVEPGAPGLGNCLRQRRGFH
HELVGFPGCVVTDGVVNFFLARTDKVREVGFDPRLSRVAHLEFFLDGLGSLRVGSCSDVV
VDHASKLKLPWTSRDAGAETYARYRYPGSLDESQMAKHRLLFFKHRLQCMTSQ
Enzyme 33 Number of Residues 533
Enzyme 33 Molecular Weight 58881.8
Enzyme 33 Theoretical pI 8.82
Enzyme 33 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • cellular lipid metabolic process
  • lipid glycosylation
  • lipid metabolic process
  • lipid modification
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 33 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 33 Specific Function Involved in the biosynthesis of gangliosides GM2, GD2 and GA2
Enzyme 33 Pathways
Enzyme 33 Reactions
  • UDP-N-acetyl-D-galactosamine + 1-O-[O-(N-acetyl-alpha-neuraminosyl)-(2->3)-O-beta-D- galactopyranosyl-(1->4)-beta-D-glucopyranosyl]-ceramide = UDP + 1-O-[O-2-(acetylamino)-2-deoxy-beta-D-galactopyranosyl-(1->4)-O-[N- acetyl-alpha-neuraminosyl-(2->3)]-O-beta-D-galactopyranosyl-(1->4)- beta-D-glucopyranosyl]-ceramide [RN:R04584 R05939]
Enzyme 33 Pfam Domain Function
Enzyme 33 Signals
  • None
Enzyme 33 Transmembrane Regions
  • 8-25
Enzyme 33 Essentiality Not Available
Enzyme 33 GenBank ID Protein 431033 Link Image
Enzyme 33 UniProtKB/Swiss-Prot ID Q00973 Link Image
Enzyme 33 UniProtKB/Swiss-Prot Entry Name B4GN1_HUMAN Link Image
Enzyme 33 PDB ID Not Available
Enzyme 33 Cellular Location Not Available
Enzyme 33 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 33 GenBank Gene ID M83651 Link Image
Enzyme 33 GeneCard ID B4GALNT1 Link Image
Enzyme 33 GenAtlas ID B4GALNT1 Link Image
Enzyme 33 HGNC ID HGNC:4117 Link Image
Enzyme 33 Chromosome Location 1
Enzyme 33 Locus 12q13.3
Enzyme 33 SNPs SNPJam Report Link Image
Enzyme 33 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 33 Metabolite References Not Available
Enzyme 34 [top]
Enzyme 34 ID 6156
Enzyme 34 Name Lactosylceramide 4-alpha-galactosyltransferase
Enzyme 34 Synonyms
  1. Alpha-1,4-N-acetylglucosaminyltransferase
  2. Alpha-1,4-galactosyltransferase
  3. Alpha4Gal-T1
  4. CD77 synthase
  5. Globotriaosylceramide synthase
  6. Gb3 synthase
  7. P1/Pk synthase
  8. UDP-galactose:beta-D-galactosyl-beta1-R 4-alpha-D-galactosyltransferase
Enzyme 34 Gene Name A4GALT
Enzyme 34 Protein Sequence >Lactosylceramide 4-alpha-galactosyltransferase
MSKPPDLLLRLLRGAPRQRVCTLFIIGFKFTFFVSIMIYWHVVGEPKEKGQLYNLPAEIP
CPTLTPPTPPSHGPTPGNIFFLETSDRTNPNFLFMCSVESAARTHPESHVLVLMKGLPGG
NASLPRHLGISLLSCFPNVQMLPLDLRELFRDTPLADWYAAVQGRWEPYLLPVLSDASRI
ALMWKFGGIYLDTDFIVLKNLRNLTNVLGTQSRYVLNGAFLAFERRHEFMALCMRDFVDH
YNGWIWGHQGPQLLTRVFKKWCSIRSLAESRACRGVTTLPPEAFYPIPWQDWKKYFEDIN
PEELPRLLSATYAVHVWNKKSQGTRFEATSRALLAQLHARYCPTTHEAMKMYL
Enzyme 34 Number of Residues 353
Enzyme 34 Molecular Weight 40498.8
Enzyme 34 Theoretical pI 9.18
Enzyme 34 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • Golgi apparatus part
  • Golgi stack
  • cell part
  • cytoplasmic part
  • intracellular part
Enzyme 34 General Function Involved in galactosyltransferase activity
Enzyme 34 Specific Function Necessary for the biosynthesis of the Pk antigen of blood histogroup P. Catalyzes the transfer of galactose to lactosylceramide and galactosylceramide. Necessary for the synthesis of the receptor for bacterial verotoxins
Enzyme 34 Pathways
Enzyme 34 Reactions
  • UDP-galactose + beta-D-galactosyl-(1->4)-D-glucosyl-(11)-ceramide = UDP + alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-D-glucosyl-(11)- ceramide [RN:R03486 R05960]
Enzyme 34 Pfam Domain Function
Enzyme 34 Signals
  • None
Enzyme 34 Transmembrane Regions
  • 23-43
Enzyme 34 Essentiality Not Available
Enzyme 34 GenBank ID Protein Not Available
Enzyme 34 UniProtKB/Swiss-Prot ID Q9NPC4 Link Image
Enzyme 34 UniProtKB/Swiss-Prot Entry Name A4GAT_HUMAN Link Image
Enzyme 34 PDB ID Not Available
Enzyme 34 Cellular Location Not Available
Enzyme 34 Gene Sequence >1062 bp
ATGTCCAAGCCCCCCGACCTCCTGCTGCGGCTGCTCCGGGGCGCCCCAAGGCAGCGGGTC
TGCACCCTGTTCATCATCGGCTTCAAGTTCACGTTTTTCGTCTCCATCATGATCTACTGG
CACGTTGTGGGAGAGCCCAAGGAGAAAGGGCAGCTCTATAACCTGCCAGCAGAGATCCCC
TGCCCCACCTTGACACCCCCCACCCCACCCTCCCACGGCCCCACTCCAGGCAACATCTTC
TTCCTGGAGACTTCAGACCGGACCAACCCCAACTTCCTGTTCATGTGCTCGGTGGAGTCG
GCCGCCAGAACTCACCCCGAATCCCACGTGCTGGTCCTGATGAAAGGGCTTCCGGGTGGC
AACGCCTCTCTGCCCCGGCACCTGGGCATCTCACTTCTGAGCTGCTTCCCGAATGTCCAG
ATGCTCCCGCTGGACCTGCGGGAGCTGTTCCGGGACACACCCCTGGCCGACTGGTACGCG
GCCGTGCAGGGGCGCTGGGAGCCCTACCTGCTGCCCGTGCTCTCCGACGCCTCCAGGATC
GCACTCATGTGGAAGTTCGGCGGCATCTACCTGGACACGGACTTCATTGTTCTCAAGAAC
CTGCGGAACCTGACCAACGTGCTGGGCACCCAGTCCCGCTACGTCCTCAACGGCGCGTTC
CTGGCCTTCGAGCGCCGGCACGAGTTCATGGCGCTGTGCATGCGGGACTTCGTGGACCAC
TACAACGGCTGGATCTGGGGTCACCAGGGCCCGCAGCTGCTCACGCGGGTCTTCAAGAAG
TGGTGTTCCATCCGCAGCCTGGCCGAGAGCCGCGCCTGCCGCGGCGTCACCACCCTGCCC
CCTGAGGCCTTCTACCCCATCCCCTGGCAGGACTGGAAGAAGTACTTTGAGGACATCAAC
CCGGAGGAGCTGCCGCGGCTGCTCAGTGCCACCTATGCTGTCCACGTGTGGAACAAGAAG
AGCCAGGGCACGCGGTTCGAGGCCACGTCCAGGGCACTGCTGGCCCAGCTGCATGCCCGC
TACTGCCCCACGACGCACGAGGCCATGAAAATGTACTTGTGA
Enzyme 34 GenBank Gene ID AB037883 Link Image
Enzyme 34 GeneCard ID A4GALT Link Image
Enzyme 34 GenAtlas ID A4GALT Link Image
Enzyme 34 HGNC ID HGNC:18149 Link Image
Enzyme 34 Chromosome Location 2
Enzyme 34 Locus 22q13.2
Enzyme 34 SNPs SNPJam Report Link Image
Enzyme 34 General References
  1. Kojima Y, Fukumoto S, Furukawa K, Okajima T, Wiels J, Yokoyama K, Suzuki Y, Urano T, Ohta M, Furukawa K: Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase that initiates the synthesis of globo series glycosphingolipids. J Biol Chem. 2000 May 19;275(20):15152-6. [PubMed Link Image]
  2. Steffensen R, Carlier K, Wiels J, Levery SB, Stroud M, Cedergren B, Nilsson Sojka B, Bennett EP, Jersild C, Clausen H: Cloning and expression of the histo-blood group Pk UDP-galactose: Ga1beta-4G1cbeta1-cer alpha1, 4-galactosyltransferase. Molecular genetic basis of the p phenotype. J Biol Chem. 2000 Jun 2;275(22):16723-9. [PubMed Link Image]
  3. Kitano T, Liu YH, Ueda S, Saitou N: Human-specific amino acid changes found in 103 protein-coding genes. Mol Biol Evol. 2004 May;21(5):936-44. Epub 2004 Mar 10. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. Furukawa K, Iwamura K, Uchikawa M, Sojka BN, Wiels J, Okajima T, Urano T, Furukawa K: Molecular basis for the p phenotype. Identification of distinct and multiple mutations in the alpha 1,4-galactosyltransferase gene in Swedish and Japanese individuals. J Biol Chem. 2000 Dec 1;275(48):37752-6. [PubMed Link Image]
  8. Koda Y, Soejima M, Sato H, Maeda Y, Kimura H: Three-base deletion and one-base insertion of the alpha(1,4)galactosyltransferase gene responsible for the P phenotype. Transfusion. 2002 Jan;42(1):48-51. [PubMed Link Image]
Enzyme 34 Metabolite References Not Available
Enzyme 35 [top]
Enzyme 35 ID 6221
Enzyme 35 Name Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
Enzyme 35 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 35 Gene Name B3GAT3
Enzyme 35 Protein Sequence >Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
MKLKLKNVFLAYFLVSIAGLLYALVQLGQPCDCLPPLRAAAEQLRQKDLRISQLQAELRR
PPPAPAQPPEPEALPTIYVVTPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAEGPTPL
VSGLLAASGLLFTHLVVLTPKAQRLREGEPGWVHPRGVEQRNKALDWLRGRGGAVGGEKD
PPPPGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDGRVVGFH
TAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTAPRGHLESSLLSHLVDPKDLEPRAAN
CTRVLVWHTRTEKPKMKQEEQLQRQGRGSDPAIEV
Enzyme 35 Number of Residues 335
Enzyme 35 Molecular Weight 37121.5
Enzyme 35 Theoretical pI 8.47
Enzyme 35 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 part
  • membrane
Enzyme 35 General Function Involved in galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
Enzyme 35 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-1,3-Gal-beta-1,4-Xyl 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-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc
Enzyme 35 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 35 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 [RN:R04607 R05928]
Enzyme 35 Pfam Domain Function
Enzyme 35 Signals
  • None
Enzyme 35 Transmembrane Regions
  • 8-28
Enzyme 35 Essentiality Not Available
Enzyme 35 GenBank ID Protein 3892640 Link Image
Enzyme 35 UniProtKB/Swiss-Prot ID O94766 Link Image
Enzyme 35 UniProtKB/Swiss-Prot Entry Name B3GA3_HUMAN Link Image
Enzyme 35 PDB ID 1KWS Link Image
Enzyme 35 PDB File Show
Enzyme 35 3D Structure
Enzyme 35 Cellular Location Not Available
Enzyme 35 Gene Sequence >1008 bp
ATGAAGCTGAAGCTGAAGAACGTGTTTCTCGCCTACTTCCTGGTGTCGATCGCCGGCCTC
CTCTACGCGCTGGTACAGCTCGGCCAGCCATGTGACTGCCTTCCTCCCCTGCGGGCAGCA
GCCGAGCAGCTACGGCAGAAGGATCTGAGGATTTCCCAGCTGCAAGCGGAACTCCGACGG
CCACCCCCTGCCCCTGCCCAGCCCCCTGAACCCGAGGCCCTGCCTACTATCTATGTTGTT
ACCCCCACCTATGCCAGGCTGGTACAGAAGGCAGAGCTGGTACGACTGTCCCAGACACTG
AGCCTGGTGCCCCGGCTGCATTGGCTGCTGGTGGAGGATGCTGAGGGTCCCACCCCGCTG
GTCTCAGGGCTGCTGGCTGCCTCTGGCCTCCTCTTCACACACCTGGTGGTCCTCACGCCC
AAAGCCCAGCGGCTTCGGGAGGGCGAGCCTGGCTGGGTTCATCCCCGTGGTGTCGAGCAG
CGGAACAAGGCCCTGGACTGGCTCCGGGGCAGAGGGGGTGCTGTGGGTGGGGAGAAGGAC
CCACCACCACCAGGGACCCAAGGAGTCGTTTACTTTGCTGACGATGACAACACCTACAGC
CGGGAGCTGTCTGAGGAGATGCGCTGGACCCGTGGTGTCTCAGTGTGGCCTGTGGGGCTG
GTGGGCGGCCTGCGATTCGAGGGCCCTCAGGTACAGGACGGCCGGGTAGTGGGCTTCCAC
ACAGCATGGGAGCCCAGCAGGCCCTTCCCTGTGGATATGGCTGGATTTGCCGTGGCCCTG
CCCTTGCTGTTAGATAAGCCCAATGCCCAATTTGATTCCACCGCTCCCCGGGGCCACCTG
GAGAGCAGTCTTCTGAGCCACCTTGTGGATCCCAAGGACCTGGAGCCACGGGCTGCCAAC
TGCACTCGGGTACTGGTGTGGCATACTCGGACAGAGAAGCCCAAGATGAAGCAGGAGGAG
CAGCTGCAGCGGCAGGGCCGGGGCTCAGACCCAGCAATTGAGGTGTGA
Enzyme 35 GenBank Gene ID AB009598 Link Image
Enzyme 35 GeneCard ID B3GAT3 Link Image
Enzyme 35 GenAtlas ID B3GAT3 Link Image
Enzyme 35 HGNC ID HGNC:923 Link Image
Enzyme 35 Chromosome Location 1
Enzyme 35 Locus 11q12.3
Enzyme 35 SNPs SNPJam Report Link Image
Enzyme 35 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. 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]
  6. 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 35 Metabolite References Not Available
Enzyme 36 [top]
Enzyme 36 ID 6222
Enzyme 36 Name Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
Enzyme 36 Synonyms
  1. Beta-1,3-glucuronyltransferase 2
  2. GlcAT-D
  3. UDP-glucuronosyltransferase S
  4. GlcAT-S
  5. Glucuronosyltransferase S
Enzyme 36 Gene Name B3GAT2
Enzyme 36 Protein Sequence >Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
MKSALFTRFFILLPWILIVIIMLDVDTRRPVPPLTPRPYFSPYAVGRGGARLPLRRGGPA
HGTQKRNQSRPQPQPEPQLPTIYAITPTYSRPVQKAELTRLANTFRQVAQLHWILVEDAA
ARSELVSRFLARAGLPSTHLHVPTPRRYKRPGLPRATEQRNAGLAWLRQRHQHQRAQPGV
LFFADDDNTYSLELFQEMRTTRKVSVWPVGLVGGRRYERPLVENGKVVGWYTGWRADRPF
AIDMAGFAVSLQVILSNPKAVFKRRGSQPGMQESDFLKQITTVEELEPKANNCTKVLVWH
TRTEKVNLANEPKYHLDTVKIEV
Enzyme 36 Number of Residues 323
Enzyme 36 Molecular Weight 36918.4
Enzyme 36 Theoretical pI 11.20
Enzyme 36 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 part
  • membrane
Enzyme 36 General Function Involved in galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
Enzyme 36 Specific Function Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on both glycolipids and glycoproteins
Enzyme 36 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 36 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 [RN:R04607 R05928]
Enzyme 36 Pfam Domain Function
Enzyme 36 Signals
  • None
Enzyme 36 Transmembrane Regions
  • 3-23
Enzyme 36 Essentiality Not Available
Enzyme 36 GenBank ID Protein 18152775 Link Image
Enzyme 36 UniProtKB/Swiss-Prot ID Q9NPZ5 Link Image
Enzyme 36 UniProtKB/Swiss-Prot Entry Name B3GA2_HUMAN Link Image
Enzyme 36 PDB ID Not Available
Enzyme 36 Cellular Location Not Available
Enzyme 36 Gene Sequence >972 bp
ATGAAGTCCGCGCTTTTCACCCGCTTCTTTATCCTCCTGCCCTGGATCCTAATTGTCATC
ATCATGCTCGACGTGGACACGCGCAGGCCAGTGCCCCCGCTCACCCCGCGCCCCTACTTC
TCTCCCTACGCGGTGGGCCGCGGGGGCGCCCGACTCCCGCTCCGCAGGGGCGGCCCGGCT
CACGGGACCCAAAAGCGCAACCAGTCTCGGCCGCAGCCACAGCCGGAGCCGCAGCTGCCC
ACCATCTATGCCATCACGCCCACCTACAGCCGCCCGGTGCAGAAAGCGGAGCTGACCCGC
CTGGCCAACACGTTCCGCCAGGTGGCGCAGCTGCACTGGATCCTGGTGGAGGACGCGGCG
GCGCGCAGCGAGCTGGTGAGCCGCTTCCTGGCGCGGGCCGGGCTGCCCAGCACTCACCTG
CACGTGCCCACGCCGCGGCGCTACAAGCGGCCCGGGCTGCCGCGCGCCACTGAGCAGCGC
AACGCGGGCCTCGCCTGGCTGCGCCAGAGGCACCAGCACCAGCGCGCGCAGCCCGGCGTG
CTCTTCTTCGCTGACGACGACAACACCTATAGTCTGGAGCTCTTCCAGGAGATGCGAACC
ACCCGCAAGGTCTCCGTCTGGCCTGTGGGCCTGGTTGGTGGGCGGCGCTACGAACGTCCG
CTGGTGGAAAACGGCAAAGTTGTTGGCTGGTACACCGGCTGGAGAGCAGACAGGCCTTTT
GCCATCGACATGGCAGGATTTGCTGTAAGTCTTCAAGTCATTTTGTCCAATCCAAAAGCT
GTATTTAAGCGTCGTGGATCCCAGCCAGGGATGCAAGAATCTGACTTTCTCAAACAGATA
ACAACAGTCGAAGAACTGGAACCGAAAGCAAATAACTGCACTAAGGTTCTCGTGTGGCAC
ACTCGGACAGAGAAGGTTAATCTAGCCAACGAGCCAAAGTACCACCTGGACACAGTGAAA
ATTGAGGTATAA
Enzyme 36 GenBank Gene ID NM_080742.2 Link Image
Enzyme 36 GeneCard ID B3GAT2 Link Image
Enzyme 36 GenAtlas ID B3GAT2 Link Image
Enzyme 36 HGNC ID HGNC:922 Link Image
Enzyme 36 Chromosome Location 6
Enzyme 36 Locus 6q13
Enzyme 36 SNPs SNPJam Report Link Image
Enzyme 36 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]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 36 Metabolite References Not Available
Enzyme 37 [top]
Enzyme 37 ID 6223
Enzyme 37 Name Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
Enzyme 37 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 37 Gene Name B3GAT1
Enzyme 37 Protein Sequence >Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
MPKRRDILAIVLIVLPWTLLITVWHQSTLAPLLAVHKDEGSDPRRETPPGADPREYCTSD
RDIVEVVRTEYVYTRPPPWSDTLPTIHVVTPTYSRPVQKAELTRMANTLLHVPNLHWLVV
EDAPRRTPLTARLLRDTGLNYTHLHVETPRNYKLRGDARDPRIPRGTMQRNLALRWLRET
FPRNSSQPGVVYFADDDNTYSLELFEEMRSTRRVSVWPVAFVGGLRYEAPRVNGAGKVVG
WKTVFDPHRPFAIDMAGFAVNLRLILQRSQAYFKLRGVKGGYQESSLLRELVTLNDLEPK
AANCTKILVWHTRTEKPVLVNEGKKGFTDPSVEI
Enzyme 37 Number of Residues 334
Enzyme 37 Molecular Weight 38255.7
Enzyme 37 Theoretical pI 10.03
Enzyme 37 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 part
  • membrane
Enzyme 37 General Function Involved in galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
Enzyme 37 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 37 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 37 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 [RN:R04607 R05928]
Enzyme 37 Pfam Domain Function
Enzyme 37 Signals
  • None
Enzyme 37 Transmembrane Regions
  • 7-27
Enzyme 37 Essentiality Not Available
Enzyme 37 GenBank ID Protein 8051678 Link Image
Enzyme 37 UniProtKB/Swiss-Prot ID Q9P2W7 Link Image
Enzyme 37 UniProtKB/Swiss-Prot Entry Name B3GA1_HUMAN Link Image
Enzyme 37 PDB ID 1V84 Link Image
Enzyme 37 PDB File Show
Enzyme 37 3D Structure
Enzyme 37 Cellular Location Not Available
Enzyme 37 Gene Sequence >1005 bp
ATGCCGAAGAGACGGGACATCCTAGCGATCGTCCTCATCGTGCTGCCCTGGACTCTGCTC
ATCACTGTCTGGCACCAGAGCACCCTCGCACCCCTGCTCGCGGTACATAAGGATGAGGGC
AGTGACCCCCGACGCGAAACGCCGCCCGGCGCCGACCCCAGGGAGTACTGCACGTCTGAC
CGCGACATCGTGGAGGTGGTGCGCACCGAGTACGTGTACACGCGGCCCCCGCCATGGTCC
GACACGCTGCCCACCATCCACGTGGTGACGCCCACCTACAGCCGCCCGGTGCAGAAGGCC
GAGCTGACGCGCATGGCCAACACGCTGCTGCACGTGCCCAACCTCCACTGGCTGGTGGTG
GAGGATGCGCCGCGCCGGACGCCGCTGACCGCGCGCCTGCTGCGCGACACCGGCCTCAAC
TACACGCACCTGCACGTGGAGACGCCCCGCAACTACAAGCTGCGCGGAGACGCCCGCGAC
CCACGCATCCCGCGGGGCACCATGCAGCGCAACCTGGCCCTGCGCTGGCTGCGCGAGACC
TTCCCGCGCAACTCCAGCCAGCCTGGCGTGGTCTACTTCGCCGACGACGACAACACCTAC
AGCCTGGAGCTCTTCGAAGAGATGCGCAGCACCAGGAGGGTGTCCGTGTGGCCCGTCGCC
TTCGTGGGTGGCCTGCGGTACGAGGCCCCACGGGTGAACGGGGCAGGGAAGGTGGTCCGC
TGGAAGACGGTGTTTGACCCCCACCGGCCATTTGCAATAGACATGGCTGGATTTGCCGTC
AACCTGCGGCTCATTCTGCAGCGAAGCCAGGCCTACTTCAAGCTGCGAGGTGTGAAGGGA
GGCTACCAGGAAAGCAGCCTCCTTCGAGAACTTGTCACCCTCAACGACCTGGAGCCCAAG
GCAGCCAACTGCACCAAGATCCTGGTGTGGCACACACGGACAGAGAAGCCAGTGCTGGTG
AATGAGGGCAAGAAGGGCTTCACTGACCCCTCGGTGGAGATCTGA
Enzyme 37 GenBank Gene ID AB029396 Link Image
Enzyme 37 GeneCard ID B3GAT1 Link Image
Enzyme 37 GenAtlas ID B3GAT1 Link Image
Enzyme 37 HGNC ID HGNC:921 Link Image
Enzyme 37 Chromosome Location 1
Enzyme 37 Locus 11q25
Enzyme 37 SNPs SNPJam Report Link Image
Enzyme 37 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]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Kakuda S, Shiba T, Ishiguro M, Tagawa H, Oka S, Kajihara Y, Kawasaki T, Wakatsuki S, Kato R: Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1. J Biol Chem. 2004 May 21;279(21):22693-703. Epub 2004 Mar 1. [PubMed Link Image]
Enzyme 37 Metabolite References Not Available
Enzyme 38 [top]
Enzyme 38 ID 6229
Enzyme 38 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
Enzyme 38 Synonyms
  1. GlcNAc-PI synthesis protein
  2. Phosphatidylinositol-glycan biosynthesis class A protein
  3. PIG-A
Enzyme 38 Gene Name PIGA
Enzyme 38 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCL
IERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRE
RVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNH
IICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGI
DLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLV
QGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLE
KAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHC
GPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEI
SETR
Enzyme 38 Number of Residues 484
Enzyme 38 Molecular Weight 54126.1
Enzyme 38 Theoretical pI 8.41
Enzyme 38 GO Classification
Function
Process
  • GPI anchor biosynthetic process
  • biosynthetic process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid lipidation
  • protein modification process
Component
Enzyme 38 General Function Involved in biosynthetic process
Enzyme 38 Specific Function Necessary for the synthesis of N-acetylglucosaminyl- phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis
Enzyme 38 Pathways Not Available
Enzyme 38 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [RN:R02654 R05916]
Enzyme 38 Pfam Domain Function
Enzyme 38 Signals
  • None
Enzyme 38 Transmembrane Regions
  • 422-442
Enzyme 38 Essentiality Not Available
Enzyme 38 GenBank ID Protein 23398601 Link Image
Enzyme 38 UniProtKB/Swiss-Prot ID P37287 Link Image
Enzyme 38 UniProtKB/Swiss-Prot Entry Name PIGA_HUMAN Link Image
Enzyme 38 PDB ID Not Available
Enzyme 38 Cellular Location Not Available
Enzyme 38 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 38 GenBank Gene ID BC038236 Link Image
Enzyme 38 GeneCard ID PIGA Link Image
Enzyme 38 GenAtlas ID PIGA Link Image
Enzyme 38 HGNC ID HGNC:8957 Link Image
Enzyme 38 Chromosome Location Not Available
Enzyme 38 Locus Not Available
Enzyme 38 SNPs SNPJam Report Link Image
Enzyme 38 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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]
  7. Murakami Y, Siripanyaphinyo U, Hong Y, Tashima Y, Maeda Y, Kinoshita T: The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component. Mol Biol Cell. 2005 Nov;16(11):5236-46. Epub 2005 Sep 14. [PubMed Link Image]
  8. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  9. 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]
  10. 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]
  11. 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]
  12. 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 38 Metabolite References Not Available
Enzyme 39 [top]
Enzyme 39 ID 6269
Enzyme 39 Name Dolichyl-phosphate beta-glucosyltransferase
Enzyme 39 Synonyms
  1. DolP-glucosyltransferase
  2. Asparagine-linked glycosylation protein 5 homolog
Enzyme 39 Gene Name ALG5
Enzyme 39 Protein Sequence >Dolichyl-phosphate beta-glucosyltransferase
MAPLLLQLAVLGAALAAAALVLISIVAFTTATKMPALHRHEEEKFFLNAKGQKETLPSIW
DSPTKQLSVVVPSYNEEKRLPVMMDEALSYLEKRQKRDPAFTYEVIVVDDGSKDQTSKVA
FKYCQKYGSDKVRVITLVKNRGKGGAIRMGIFSSRGEKILMADADGATKFPDVEKLEKGL
NDLQPWPNQMAIACGSRAHLEKESIAQRSYFRTLLMYGFHFLVWFLCVKGIRDTQCGFKL
FTREAASRTFSSLHVERWAFDVELLYIAQFFKIPIAEIAVNWTEIEGSKLVPFWSWLQMG
KDLLFIRLRYLTGAWRLEQTRKMN
Enzyme 39 Number of Residues 324
Enzyme 39 Molecular Weight 36945.8
Enzyme 39 Theoretical pI 9.79
Enzyme 39 GO Classification Not Available
Enzyme 39 General Function Cell wall/membrane/envelope biogenesis
Enzyme 39 Specific Function UDP-glucose + dolichyl phosphate = UDP + dolichyl beta-D-glucosyl phosphate
Enzyme 39 Pathways
Enzyme 39 Reactions
  • UDP-glucose + dolichyl phosphate = UDP + dolichyl beta-D-glucosyl phosphate [RN:R01005]
Enzyme 39 Pfam Domain Function
Enzyme 39 Signals
  • None
Enzyme 39 Transmembrane Regions
  • 8-28
Enzyme 39 Essentiality Not Available
Enzyme 39 GenBank ID Protein 5281121 Link Image
Enzyme 39 UniProtKB/Swiss-Prot ID Q9Y673 Link Image
Enzyme 39 UniProtKB/Swiss-Prot Entry Name ALG5_HUMAN Link Image
Enzyme 39 PDB ID Not Available
Enzyme 39 Cellular Location Not Available
Enzyme 39 Gene Sequence >975 bp
ATGGCTCCGCTTCTGTTGCAGCTGGCGGTGCTCGGCGCGGCGCTGGCGGCCGCAGCCCTC
GTACTGATTTCCATCGTTGCATTTACAACTGCTACAAAAATGCCAGCACTCCATCGACAT
GAAGAAGAGAAATTCTTCTTAAATGCCAAAGGCCAGAAAGAAACTTTACCCAGCATATGG
GACTCACCTACCAAACAACTTTCTGTCGTTGTGCCTTCATACAATGAAGAAAAACGGTTG
CCTGTGATGATGGATGAAGCTCTGAGCTATCTAGAGAAGAGACAGAAACGAGATCCTGCG
TTCACTTATGAAGTGATAGTAGTTGATGATGGCAGTAAAGATCAGACCTCAAAGGTAGCT
TTTAAATATTGCCAGAAATATGGAAGTGACAAAGTACGTGTGATAACCCTGGTGAAGAAT
CGTGGAAAAGGTGGAGCGATTAGAATGGGTATATTCAGTTCTCGAGGAGAAAAGATCCTT
ATGGCAGATGCTGATGGAGCCACAAAGTTTCCAGATGTTGAGAAATTAGAAAAGGGGCTA
AATGATCTACAGCCTTGGCCTAATCAAATGGCTATAGCATGTGGATCTCGAGCTCATTTA
GAAAAAGAATCAATTGCTCAGCGTTCTTACTTCCGTACTCTTCTCATGTATGGGTTCCAC
TTTCTGGTGTGGTTCCTTTGTGTCAAAGGAATCAGGGACACACAGTGTGGGTTCAAATTA
TTTACTCGAGAAGCAGCTTCACGGACGTTTTCATCTCTACACGTTGAACGATGGGCATTT
GATGTAGAACTACTGTACATAGCACAGTTCTTTAAAATTCCAATAGCAGAAATTGCTGTC
AACTGGACAGAAATTGAAGGTTCTAAATTAGTTCCATTCTGGAGCTGGCTACAAATGGGT
AAAGACCTACTTTTTATACGACTTCGATATTTGACTGGTGCCTGGAGGCTTGAGCAAACT
CGGAAAATGAATTAG
Enzyme 39 GenBank Gene ID AF102850 Link Image
Enzyme 39 GeneCard ID ALG5 Link Image
Enzyme 39 GenAtlas ID ALG5 Link Image
Enzyme 39 HGNC ID HGNC:20266 Link Image
Enzyme 39 Chromosome Location 1
Enzyme 39 Locus 13q13.3
Enzyme 39 SNPs SNPJam Report Link Image
Enzyme 39 General References
  1. Imbach T, Burda P, Kuhnert P, Wevers RA, Aebi M, Berger EG, Hennet T: A mutation in the human ortholog of the Saccharomyces cerevisiae ALG6 gene causes carbohydrate-deficient glycoprotein syndrome type-Ic. Proc Natl Acad Sci U S A. 1999 Jun 8;96(12):6982-7. [PubMed Link Image]
  2. Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed Link Image]
  3. Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 39 Metabolite References Not Available
Enzyme 40 [top]
Enzyme 40 ID 6282
Enzyme 40 Name Polypeptide N-acetylgalactosaminyltransferase 4
Enzyme 40 Synonyms
  1. Polypeptide GalNAc transferase 4
  2. GalNAc-T4
  3. pp-GaNTase 4
  4. Protein-UDP acetylgalactosaminyltransferase 4
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4
Enzyme 40 Gene Name GALNT4
Enzyme 40 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 4
MAVRWTWAGKSCLLLAFLTVAYIFVELLVSTFHASAGAGRARELGSRRLSGLQKNTEDLS
RPLYKKPPADSRALGEWGKASKLQLNEDELKQQEELIERYAINIYLSDRISLHRHIEDKR
MYECKSQKFNYRTLPTTSVIIAFYNEAWSTLLRTIHSVLETSPAVLLKEIILVDDLSDRV
YLKTQLETYISNLDRVRLIRTNKREGLVRARLIGATFATGDVLTFLDCHCECNSGWLEPL
LERIGRDETAVVCPVIDTIDWNTFEFYMQIGEPMIGGFDWRLTFQWHSVPKQERDRRISR
IDPIRSPTMAGGLFAVSKKYFQYLGTYDTGMEVWGGENLELSFRVWQCGGKLEIHPCSHV
GHVFPKRAPYARPNFLQNTARAAEVWMDEYKEHFYNRNPPARKEAYGDISERKLLRERLR
CKSFDWYLKNVFPNLHVPEDRPGWHGAIRSRGISSECLDYNSPDNNPTGANLSLFGCHGQ
GGNQFFEYTSNKEIRFNSVTELCAEVPEQKNYVGMQNCPKDGFPVPANIIWHFKEDGTIF
HPHSGLCLSAYRTPEGRPDVQMRTCDALDKNQIWSFEK
Enzyme 40 Number of Residues 578
Enzyme 40 Molecular Weight 66607.2
Enzyme 40 Theoretical pI 7.80
Enzyme 40 GO Classification Not Available
Enzyme 40 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
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 highest activity toward Muc7, EA2 and Muc2, with a lowest activity than GALNT2. Glycosylates 'Thr-57' of SELPLG
Enzyme 40 Pathways
Enzyme 40 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 40 Pfam Domain Function
Enzyme 40 Signals
  • None
Enzyme 40 Transmembrane Regions
  • 13-35
Enzyme 40 Essentiality Not Available
Enzyme 40 GenBank ID Protein 22137798 Link Image
Enzyme 40 UniProtKB/Swiss-Prot ID Q8N4A0 Link Image
Enzyme 40 UniProtKB/Swiss-Prot Entry Name GALT4_HUMAN Link Image
Enzyme 40 PDB ID Not Available
Enzyme 40 Cellular Location Not Available
Enzyme 40 Gene Sequence >1737 bp
ATGGCGGTGAGGTGGACTTGGGCAGGCAAGAGCTGCCTGCTGCTGGCGTTTTTAACAGTG
GCCTATATCTTCGTGGAGCTCTTGGTCTCTACTTTTCATGCCTCCGCAGGAGCCGGCCGT
GCCAGGGAGCTGGGGTCAAGAAGGCTCTCAGGCCTCCAGAAAAATACGGAGGATTTGTCT
CGACCGCTTTATAAGAAGCCCCCTGCAGATTCCCGTGCACTTGGGGAGTGGGGGAAAGCC
AGCAAACTCCAGCTCAACGAGGATGAACTGAAGCAGCAAGAAGAACTCATTGAGAGATAC
GCCATCAATATTTACCTCAGTGACAGGATTTCCCTGCATCGACACATAGAGGATAAAAGA
ATGTATGAGTGTAAGTCCCAGAAGTTCAACTATAGGACACTTCCTACCACCTCTGTTATC
ATTGCTTTCTATAACGAAGCCTGGTCGACTTTGCTCCGTACCATTCACAGTGTTTTAGAA
ACTTCTCCTGCAGTTCTTTTGAAAGAGATCATCTTGGTGGATGACTTGAGTGACAGAGTT
TATTTGAAGACACAACTTGAAACTTACATCAGCAATCTTGATAGAGTACGCTTGATTAGG
ACCAATAAGCGAGAGGGGCTGGTTAGGGCCCGTCTGATTGGGGCCACTTTCGCCACTGGG
GACGTCCTCACTTTCCTGGATTGTCACTGTGAGTGTAATTCCGGTTGGCTGGAACCGCTT
TTGGAAAGGATTGGGAGAGATGAAACAGCAGTTGTGTGTCCTGTTATAGACACAATTGAT
TGGAATACTTTTGAATTCTATATGCAGATAGGGGAGCCCATGATTGGTGGGTTTGACTGG
CGTTTAACATTTCAGTGGCATTCTGTCCCCAAACAGGAAAGGGACAGGCGGATATCAAGA
ATTGACCCCATCAGATCACCTACCATGGCTGGAGGACTGTTTGCTGTCAGCAAGAAATAT
TTTCAGTACCTTGGAACGTATGACACAGGAATGGAAGTGTGGGGAGGTGAAAACCTTGAG
CTGTCTTTTAGGGTGTGGCAGTGTGGTGGCAAATTGGAGATCCACCCGTGTTCCCACGTG
GGCCATGTGTTCCCCAAGCGGGCACCATATGCTCGCCCCAATTTCCTACAGAATACTGCT
CGGGCAGCAGAAGTTTGGATGGATGAATACAAAGAGCACTTCTACAATAGAAACCCTCCA
GCAAGAAAAGAAGCTTATGGTGATATTTCTGAAAGAAAATTACTACGAGAGCGGTTGAGA
TGCAAGAGCTTTGACTGGTATTTGAAAAACGTTTTTCCTAATTTACATGTTCCAGAGGAT
AGACCAGGCTGGCATGGGGCTATTCGCAGTAGAGGGATCTCGTCTGAATGTTTAGATTAT
AATTCTCCTGACAACAACCCCACAGGTGCTAACCTTTCACTGTTTGGATGCCATGGTCAA
GGAGGCAATCAATTCTTTGAATATACTTCAAACAAAGAAATAAGGTTTAATTCTGTGACA
GAGTTATGTGCAGAGGTACCTGAGCAAAAAAATTATGTGGGAATGCAAAATTGTCCCAAA
GATGGGTTCCCTGTACCAGCAAACATTATTTGGCATTTTAAAGAAGATGGAACTATTTTT
CACCCACACTCAGGACTGTGTCTTAGTGCTTATCGGACACCGGAGGGCCGACCTGATGTA
CAAATGAGAACTTGTGATGCTCTAGATAAAAATCAAATTTGGAGTTTTGAGAAATAG
Enzyme 40 GenBank Gene ID BC036390 Link Image
Enzyme 40 GeneCard ID GALNT4 Link Image
Enzyme 40 GenAtlas ID GALNT4 Link Image
Enzyme 40 HGNC ID HGNC:4126 Link Image
Enzyme 40 Chromosome Location 1
Enzyme 40 Locus 12q21.33
Enzyme 40 SNPs SNPJam Report Link Image
Enzyme 40 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]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Hassan H, Reis CA, Bennett EP, Mirgorodskaya E, Roepstorff P, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H: The lectin domain of UDP-N-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase-T4 directs its glycopeptide specificities. J Biol Chem. 2000 Dec 8;275(49):38197-205. [PubMed Link Image]
Enzyme 40 Metabolite References Not Available
Enzyme 41 [top]
Enzyme 41 ID 6283
Enzyme 41 Name Polypeptide N-acetylgalactosaminyltransferase 3
Enzyme 41 Synonyms
  1. Polypeptide GalNAc transferase 3
  2. GalNAc-T3
  3. pp-GaNTase 3
  4. Protein-UDP acetylgalactosaminyltransferase 3
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
Enzyme 41 Gene Name GALNT3
Enzyme 41 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 3
MAHLKRLVKLHIKRHYHKKFWKLGAVIFFFIIVLVLMQREVSVQYSKEESRMERNMKNKN
KMLDLMLEAVNNIKDAMPKMQIGAPVRQNIDAGERPCLQGYYTAAELKPVLDRPPQDSNA
PGASGKAFKTTNLSVEEQKEKERGEAKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKR
CPPLPTTSVIIVFHNEAWSTLLRTVHSVLYSSPAILLKEIILVDDASVDEYLHDKLDEYV
KQFSIVKIVRQRERKGLITARLLGATVATAETLTFLDAHCECFYGWLEPLLARIAENYTA
VVSPDIASIDLNTFEFNKPSPYGSNHNRGNFDWSLSFGWESLPDHEKQRRKDETYPIKTP
TFAGGLFSISKEYFEYIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSK
SPHSFPKGTQVIARNQVRLAEVWMDEYKEIFYRRNTDAAKIVKQKAFGDLSKRFEIKHRL
QCKNFTWYLNNIYPEVYVPDLNPVISGYIKSVGQPLCLDVGENNQGGKPLIMYTCHGLGG
NQYFEYSAQHEIRHNIQKELCLHAAQGLVQLKACTYKGHKTVVTGEQIWEIQKDQLLYNP
FLKMCLSANGEHPSLVSCNPSDPLQKWILSQND
Enzyme 41 Number of Residues 633
Enzyme 41 Molecular Weight 72609.8
Enzyme 41 Theoretical pI 8.06
Enzyme 41 GO Classification Not Available
Enzyme 41 General Function Cell wall/membrane/envelope biogenesis
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 HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably glycosylates fibronectin in vivo. Glycosylates FGF23. Plays a central role in phosphate homeostasis
Enzyme 41 Pathways
Enzyme 41 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 41 Pfam Domain Function
Enzyme 41 Signals
  • None
Enzyme 41 Transmembrane Regions
  • 20-37
Enzyme 41 Essentiality Not Available
Enzyme 41 GenBank ID Protein 62822129 Link Image
Enzyme 41 UniProtKB/Swiss-Prot ID Q14435 Link Image
Enzyme 41 UniProtKB/Swiss-Prot Entry Name GALT3_HUMAN Link Image
Enzyme 41 PDB ID Not Available
Enzyme 41 Cellular Location Not Available
Enzyme 41 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
ATTGTTAAACAAAAAGCATTTGGTGATCTTTCAAAAAGATTTGAAATAAAACACCGCCTT
CAGTGTAAAAATTTTACATGGTATCTGAACAACATTTATCCAGAGGTGTATGTGCCAGAC
CTTAATCCTGTTATATCTGGATACATTAAAAGCGTTGGTCAGCCTCTATGTCTGGATGTT
GGAGAAAACAATCAAGGAGGCAAACCATTAATTATGTATACATGTCATGGACTTGGGGGA
AACCAGTACTTTGAATACTCTGCTCAACATGAAATTCGGCACAACATCCAGAAGGAATTA
TGTCTTCATGCTGCTCAAGGTCTCGTTCAGCTGAAGGCATGTACCTACAAAGGTCACAAG
ACAGTTGTCACTGGAGAGCAGATATGGGAGATCCAGAAGGATCAACTTCTATACAATCCA
TTCTTAAAAATGTGCCTTTCAGCAAATGGAGAGCATCCAAGTTTAGTGTCATGCAACCCA
TCAGATCCACTCCAAAAATGGATACTTAGCCAAAATGATTAA
Enzyme 41 GenBank Gene ID AC009495 Link Image
Enzyme 41 GeneCard ID GALNT3 Link Image
Enzyme 41 GenAtlas ID GALNT3 Link Image
Enzyme 41 HGNC ID HGNC:4125 Link Image
Enzyme 41 Chromosome Location 2
Enzyme 41 Locus 2q24-q31
Enzyme 41 SNPs SNPJam Report Link Image
Enzyme 41 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]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Wandall HH, Hassan H, Mirgorodskaya E, Kristensen AK, Roepstorff P, Bennett EP, Nielsen PA, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H: Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. J Biol Chem. 1997 Sep 19;272(38):23503-14. [PubMed Link Image]
  5. Rottger S, White J, Wandall HH, Olivo JC, Stark A, Bennett EP, Whitehouse C, Berger EG, Clausen H, Nilsson T: Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. J Cell Sci. 1998 Jan;111 ( Pt 1):45-60. [PubMed Link Image]
  6. Onitsuka K, Shibao K, Nakayama Y, Minagawa N, Hirata K, Izumi H, Matsuo K, Nagata N, Kitazato K, Kohno K, Itoh H: Prognostic significance of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-3 (GalNAc-T3) expression in patients with gastric carcinoma. Cancer Sci. 2003 Jan;94(1):32-6. [PubMed Link Image]
  7. Topaz O, Shurman DL, Bergman R, Indelman M, Ratajczak P, Mizrachi M, Khamaysi Z, Behar D, Petronius D, Friedman V, Zelikovic I, Raimer S, Metzker A, Richard G, Sprecher E: Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis. Nat Genet. 2004 Jun;36(6):579-81. Epub 2004 May 9. [PubMed Link Image]
  8. Frishberg Y, Topaz O, Bergman R, Behar D, Fisher D, Gordon D, Richard G, Sprecher E: Identification of a recurrent mutation in GALNT3 demonstrates that hyperostosis-hyperphosphatemia syndrome and familial tumoral calcinosis are allelic disorders. J Mol Med. 2005 Jan;83(1):33-8. Epub 2004 Dec 15. [PubMed Link Image]
  9. Kato K, Jeanneau C, Tarp MA, Benet-Pages A, Lorenz-Depiereux B, Bennett EP, Mandel U, Strom TM, Clausen H: Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation. J Biol Chem. 2006 Jul 7;281(27):18370-7. Epub 2006 Apr 25. [PubMed Link Image]
Enzyme 41 Metabolite References Not Available
Enzyme 42 [top]
Enzyme 42 ID 6284
Enzyme 42 Name Probable polypeptide N-acetylgalactosaminyltransferase 8
Enzyme 42 Synonyms
  1. Polypeptide GalNAc transferase 8
  2. GalNAc-T8
  3. pp-GaNTase 8
  4. Protein-UDP acetylgalactosaminyltransferase 8
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 8
Enzyme 42 Gene Name GALNT8
Enzyme 42 Protein Sequence >Probable polypeptide N-acetylgalactosaminyltransferase 8
MMFWRKLPKALFIGLTLAIAVNLLLVFSSKGTLQNLFTGGLHRELPLHLNKRYGAVIKRL
SHLEVELQDLKESMKLALRQQENVNSTLKRAKDEVRPLLKAMETKVNETKKHKTQMKLFP
HSQLFRQWGEDLSEAQQKAAQDLFRKFGYNAYLSNQLPLNRTIPDTRDYRCLRKTYPSQL
PSLSVILIFVNEALSIIQRAITSIINRTPSRLLKEIILVDDFSSNGELKVHLDEKIKLYN
QKYPGLLKIIRHPERKGLAQARNTGWEAATADVVAILDAHIEVNVGWAEPILARIQEDRT
VIVSPVFDNIRFDTFKLDKYELAVDGFNWELWCRYDALPQAWIDLHDVTAPVKSPSIMGI
LAANRHFLGEIGSLDGGMLIYGGENVELSLRVWQCGGKVEILPCSRIAHLERHHKPYALD
LTAALKRNALRVAEIWMDEHKHMVYLAWNIPLQNSGIDFGDVSSRMALREKLKCKTFDWY
LKNVYPLLKPLHTIVGYGRMKNLLDENVCLDQGPVPGNTPIMYYCHEFSSQNVYYHLTGE
LYVGQLIAEASASDRCLTDPGKAEKPTLEPCSKAAKNRLHIYWDFKPGGAVINRDTKRCL
EMKKDLLGSHVLVLQTCSTQVWEIQHTVRDWGQTNSQ
Enzyme 42 Number of Residues 637
Enzyme 42 Molecular Weight 72850.8
Enzyme 42 Theoretical pI 9.16
Enzyme 42 GO Classification Not Available
Enzyme 42 General Function Cell wall/membrane/envelope biogenesis
Enzyme 42 Specific Function Probably 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
Enzyme 42 Pathways
Enzyme 42 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 42 Pfam Domain Function
Enzyme 42 Signals
  • None
Enzyme 42 Transmembrane Regions
  • 7-29
Enzyme 42 Essentiality Not Available
Enzyme 42 GenBank ID Protein 7657926 Link Image
Enzyme 42 UniProtKB/Swiss-Prot ID Q9NY28 Link Image
Enzyme 42 UniProtKB/Swiss-Prot Entry Name GALT8_HUMAN Link Image
Enzyme 42 PDB ID Not Available
Enzyme 42 Cellular Location Not Available
Enzyme 42 Gene Sequence >1914 bp
ATGATGTTTTGGAGGAAACTCCCCAAAGCCCTCTTCATTGGGCTGACTCTGGCCATTGCT
GTCAATCTCCTTCTGGTATTTTCTAGCAAGGGGACTTTACAAAACCTGTTTACGGGTGGT
CTCCACAGGGAGCTTCCTTTACATCTGAATAAACGCTACGGGGCAGTGATAAAGAGACTC
TCCCACTTGGAGGTGGAATTGCAGGATCTGAAAGAAAGTATGAAATTAGCTCTGAGGCAA
CAAGAAAATGTGAACAGCACACTGAAGAGGGCGAAAGATGAAGTACGCCCTCTTCTAAAG
GCAATGGAAACCAAGGTGAATGAGACAAAGAAGCACAAAACCCAAATGAAACTCTTCCCA
CACTCACAGCTTTTCAGGCAATGGGGCGAGGATCTTTCTGAGGCCCAGCAGAAGGCGGCC
CAGGACCTCTTCCGGAAGTTTGGTTACAACGCGTACCTCAGCAACCAGCTGCCTCTCAAT
CGCACCATCCCCGACACGCGAGACTACAGATGTCTTCGGAAGACATATCCTTCCCAACTC
CCATCCCTCAGTGTCATTCTCATATTCGTGAATGAAGCTCTGTCCATTATACAACGGGCC
ATCACCAGTATCATCAACCGGACGCCCTCTCGATTGTTGAAGGAAATCATCTTGGTGGAT
GATTTCAGCTCAAATGGAGAACTAAAGGTACACTTGGATGAGAAGATTAAGCTTTACAAC
CAGAAGTATCCAGGACTACTGAAAATAATACGGCATCCTGAAAGGAAAGGTCTTGCTCAA
GCCCGCAACACTGGCTGGGAAGCTGCCACAGCAGACGTGGTCGCCATCTTGGATGCTCAC
ATTGAAGTCAATGTTGGGTGGGCAGAGCCAATCTTGGCTCGGATTCAGGAGGACCGCACT
GTGATTGTGTCTCCTGTGTTTGACAACATTCGTTTTGACACCTTCAAACTGGATAAGTAT
GAACTGGCAGTTGATGGGTTTAACTGGGAACTCTGGTGCCGCTACGATGCACTGCCACAA
GCCTGGATTGATCTGCATGATGTCACTGCCCCAGTGAAGAGTCCTTCAATCATGGGCATC
CTGGCTGCTAACAGGCACTTCCTGGGAGAGATCGGGTCTCTGGATGGTGGAATGCTCATC
TATGGAGGAGAGAACGTGGAGCTTAGCCTGAGGGTGTGGCAGTGTGGAGGGAAGGTCGAG
ATTTTGCCCTGTTCCCGGATTGCCCACCTAGAGAGACACCACAAGCCCTACGCCTTGGAT
CTCACCGCTGCCTTGAAGCGCAATGCTCTGCGAGTGGCCGAAATCTGGATGGATGAGCAC
AAACACATGGTCTACTTGGCCTGGAACATACCTCTCCAGAACTCTGGAATAGATTTTGGA
GACGTTTCTTCCAGAATGGCACTCCGGGAAAAACTGAAATGTAAAACTTTTGACTGGTAC
CTGAAAAATGTTTATCCACTCTTGAAGCCACTCCACACCATCGTGGGCTATGGAAGAATG
AAAAACCTATTGGATGAAAATGTCTGCTTGGATCAGGGACCCGTTCCAGGCAACACCCCC
ATCATGTATTACTGCCATGAATTCAGCTCACAGAATGTCTACTATCACCTAACTGGGGAG
CTCTATGTGGGACAACTGATTGCAGAGGCCAGTGCTAGTGATCGCTGCCTGACAGACCCT
GGCAAGGCGGAGAAGCCCACCTTAGAACCATGCTCCAAGGCAGCTAAGAATAGACTGCAT
ATATATTGGGATTTTAAACCGGGAGGAGCTGTCATAAACAGAGATACCAAGCGGTGTCTG
GAGATGAAGAAGGATCTTTTGGGTAGCCACGTGCTTGTGCTCCAGACCTGTAGCACGCAA
GTGTGGGAAATCCAGCACACTGTCAGAGACTGGGGTCAGACCAACAGCCAGTGA
Enzyme 42 GenBank Gene ID AJ271385 Link Image
Enzyme 42 GeneCard ID GALNT8 Link Image
Enzyme 42 GenAtlas ID GALNT8 Link Image
Enzyme 42 HGNC ID HGNC:4130 Link Image
Enzyme 42 Chromosome Location 1
Enzyme 42 Locus 12p13.3
Enzyme 42 SNPs SNPJam Report Link Image
Enzyme 42 General References
  1. White KE, Lorenz B, Evans WE, Meitinger T, Strom TM, Econs MJ: Molecular cloning of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T8, and analysis as a candidate autosomal dominant hypophosphatemic rickets (ADHR) gene. Gene. 2000 Apr 4;246(1-2):347-56. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 42 Metabolite References Not Available
Enzyme 43 [top]
Enzyme 43 ID 6285
Enzyme 43 Name Polypeptide N-acetylgalactosaminyltransferase-like protein 2
Enzyme 43 Synonyms
  1. Polypeptide GalNAc transferase-like protein 2
  2. GalNAc-T-like protein 2
  3. pp-GaNTase-like protein 2
  4. Protein-UDP acetylgalactosaminyltransferase-like protein 2
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2
Enzyme 43 Gene Name GALNTL2
Enzyme 43 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase-like protein 2
MLLRKRYRHRPCRLQFLLLLLMLGCVLMMVAMLHPPHHTLHQTVTAQASKHSPEARYRLD
FGESQDWVLEAEDEGEEYSPLEGLPPFISLREDQLLVAVALPQARRNQSQGRRGGSYRLI
KQPRRQDKEAPKRDWGADEDGEVSEEEELTPFSLDPRGLQEALSARIPLQRALPEVRHPL
CLQQHPQDSLPTASVILCFHDEAWSTLLRTVHSILDTVPRAFLKEIILVDDLSQQGQLKS
ALSEYVARLEGVKLLRSNKRLGAIRARMLGATRATGDVLVFMDAHCECHPGWLEPLLSRI
AGDRSRVVSPVIDVIDWKTFQYYPSKDLQRGVLDWKLDFHWEPLPEHVRKALQSPISPIR
SPVVPGEVVAMDRHYFQNTGAYDSLMSLRGGENLELSFKAWLCGGSVEILPCSRVGHIYQ
NQDSHSPLDQEATLRNRVRIAETWLGSFKETFYKHSPEAFSLSKAEKPDCMERLQLQRRL
GCRTFHWFLANVYPELYPSEPRPSFSGKLHNTGLGLCADCQAEGDILGCPMVLAPCSDSR
QQQYLQHTSRKEIHFGSPQHLCFAVRQEQVILQNCTEEGLAIHQQHWDFQENGMIVHILS
GKCMEAVVQENNKDLYLRPCDGKARQQWRFDQINAVDER
Enzyme 43 Number of Residues 639
Enzyme 43 Molecular Weight 73062.8
Enzyme 43 Theoretical pI 6.90
Enzyme 43 GO Classification Not Available
Enzyme 43 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 43 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 in cooperation with other GALNT proteins. Prefers Muc1a as substrate
Enzyme 43 Pathways
Enzyme 43 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 43 Pfam Domain Function
Enzyme 43 Signals
  • None
Enzyme 43 Transmembrane Regions
  • 12-34
Enzyme 43 Essentiality Not Available
Enzyme 43 GenBank ID Protein 190014583 Link Image
Enzyme 43 UniProtKB/Swiss-Prot ID Q8N3T1 Link Image
Enzyme 43 UniProtKB/Swiss-Prot Entry Name GLTL2_HUMAN Link Image
Enzyme 43 PDB ID Not Available
Enzyme 43 Cellular Location Not Available
Enzyme 43 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 43 GenBank Gene ID NM_054110.4 Link Image
Enzyme 43 GeneCard ID GALNTL2 Link Image
Enzyme 43 GenAtlas ID GALNTL2 Link Image
Enzyme 43 HGNC ID HGNC:21531 Link Image
Enzyme 43 Chromosome Location 3
Enzyme 43 Locus 3p25.1
Enzyme 43 SNPs SNPJam Report Link Image
Enzyme 43 General References
  1. Cheng L, Tachibana K, Iwasaki H, Kameyama A, Zhang Y, Kubota T, Hiruma T, Tachibana K, Kudo T, Guo JM, Narimatsu H: Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T15. FEBS Lett. 2004 May 21;566(1-3):17-24. [PubMed Link Image]
  2. 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]
  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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed Link Image]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 43 Metabolite References Not Available
Enzyme 44 [top]
Enzyme 44 ID 6287
Enzyme 44 Name Polypeptide N-acetylgalactosaminyltransferase 10
Enzyme 44 Synonyms
  1. Polypeptide GalNAc transferase 10
  2. GalNAc-T10
  3. pp-GaNTase 10
  4. Protein-UDP acetylgalactosaminyltransferase 10
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
Enzyme 44 Gene Name GALNT10
Enzyme 44 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 10
MRRKEKRLLQAVALVLAALVLLPNVGLWALYRERQPDGTPGGSGAAVAPAAGQGSHSRQK
KTFFLGDGQKLKDWHDKEAIRRDAQRVGNGEQGRPYPMTDAERVDQAYRENGFNIYVSDK
ISLNRSLPDIRHPNCNSKRYLETLPNTSIIIPFHNEGWSSLLRTVHSVLNRSPPELVAEI
VLVDDFSDREHLKKPLEDYMALFPSVRILRTKKREGLIRTRMLGASVATGDVITFLDSHC
EANVNWLPPLLDRIARNRKTIVCPMIDVIDHDDFRYETQAGDAMRGAFDWEMYYKRIPIP
PELQKADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGRM
EDIPCSRVGHIYRKYVPYKVPAGVSLARNLKRVAEVWMDEYAEYIYQRRPEYRHLSAGDV
AVQKKLRSSLNCKSFKWFMTKIAWDLPKFYPPVEPPAAAWGEIRNVGTGLCADTKHGALG
SPLRLEGCVRGRGEAAWNNMQVFTFTWREDIRPGDPQHTKKFCFDAISHTSPVTLYDCHS
MKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRIFMNTCNPSSLTQQWLFEHTNSTVLEKF
NRN
Enzyme 44 Number of Residues 603
Enzyme 44 Molecular Weight 68991.2
Enzyme 44 Theoretical pI 8.74
Enzyme 44 GO Classification Not Available
Enzyme 44 General Function Involved in metal ion binding
Enzyme 44 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 44 Pathways
Enzyme 44 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 44 Pfam Domain Function
Enzyme 44 Signals
  • None
Enzyme 44 Transmembrane Regions
  • 12-31
Enzyme 44 Essentiality Not Available
Enzyme 44 GenBank ID Protein 28268676 Link Image
Enzyme 44 UniProtKB/Swiss-Prot ID Q86SR1 Link Image
Enzyme 44 UniProtKB/Swiss-Prot Entry Name GLT10_HUMAN Link Image
Enzyme 44 PDB ID Not Available
Enzyme 44 Cellular Location Not Available
Enzyme 44 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 44 GenBank Gene ID AB078145 Link Image
Enzyme 44 GeneCard ID GALNT10 Link Image
Enzyme 44 GenAtlas ID GALNT10 Link Image
Enzyme 44 HGNC ID HGNC:19873 Link Image
Enzyme 44 Chromosome Location 5
Enzyme 44 Locus 5q33.2
Enzyme 44 SNPs SNPJam Report Link Image
Enzyme 44 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]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Kubota T, Shiba T, Sugioka S, Furukawa S, Sawaki H, Kato R, Wakatsuki S, Narimatsu H: Structural basis of carbohydrate transfer activity by human UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferase (pp-GalNAc-T10). J Mol Biol. 2006 Jun 9;359(3):708-27. Epub 2006 Apr 19. [PubMed Link Image]
Enzyme 44 Metabolite References Not Available
Enzyme 45 [top]
Enzyme 45 ID 6290
Enzyme 45 Name Putative polypeptide N-acetylgalactosaminyltransferase-like protein 4
Enzyme 45 Synonyms
  1. Polypeptide GalNAc transferase-like protein 4
  2. GalNAc-T-like protein 4
  3. pp-GaNTase-like protein 4
  4. Protein-UDP acetylgalactosaminyltransferase-like protein 4
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4
Enzyme 45 Gene Name GALNTL4
Enzyme 45 Protein Sequence >Putative polypeptide N-acetylgalactosaminyltransferase-like protein 4
MVCTRKTKTLVSTCVILSGMTNIICLLYVGWVTNYIASVYVRGQEPAPDKKLEEDKGDTL
KIIERLDHLENVIKQHIQEAPAKPEEAEAEPFTDSSLFAHWGQELSPEGRRVALKQFQYY
GYNAYLSDRLPLDRPLPDLRPSGCRNLSFPDSLPEVSIVFIFVNEALSVLLRSIHSAMER
TPPHLLKEIILVDDNSSNEELKEKLTEYVDKVNSQKPGFIKVVRHSKQEGLIRSRVSGWR
AATAPVVALFDAHVEFNVGWAEPVLTRIKENRKRIISPSFDNIKYDNFEIEEYPLAAQGF
DWELWCRYLNPPKAWWKLENSTAPIRSPALIGCFIVDRQYFQEIGLLDEGMEVYGGENVE
LGIRVWQCGGSVEVLPCSRIAHIERAHKPYTEDLTAHVRRNALRVAEVWMDEFKSHVYMA
WNIPQEDSGIDIGDITARKALRKQLQCKTFRWYLVSVYPEMRMYSDIIAYGVLQNSLKTD
LCLDQGPDTENVPIMYICHGMTPQNVYYTSSQQIHVGILSPTVDDDDNRCLVDVNSRPRL
IECSYAKAKRMKLHWQFSQGGPIQNRKSKRCLELQENSDLEFGFQLVLQKCSGQHWSITN
VLRSLAS
Enzyme 45 Number of Residues 607
Enzyme 45 Molecular Weight 69560.0
Enzyme 45 Theoretical pI 6.46
Enzyme 45 GO Classification Not Available
Enzyme 45 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 45 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 45 Pathways
Enzyme 45 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 45 Pfam Domain Function
Enzyme 45 Signals
  • None
Enzyme 45 Transmembrane Regions
  • 13-35
Enzyme 45 Essentiality Not Available
Enzyme 45 GenBank ID Protein 222446618 Link Image
Enzyme 45 UniProtKB/Swiss-Prot ID Q6P9A2 Link Image
Enzyme 45 UniProtKB/Swiss-Prot Entry Name GLTL4_HUMAN Link Image
Enzyme 45 PDB ID Not Available
Enzyme 45 Cellular Location Not Available
Enzyme 45 Gene Sequence >1824 bp
ATGGTGTGCACCAGGAAGACCAAAACTTTGGTGTCCACTTGCGTGATCCTGAGCGGCATG
ACTAACATCATCTGCCTGCTCTACGTGGGCTGGGTCACCAACTACATCGCCAGCGTGTAT
GTGCGGGGGCAGGAGCCGGCGCCCGACAAGAAGCTGGAGGAAGACAAAGGGGACACTCTG
AAGATTATTGAGCGGCTGGACCACCTGGAGAATGTCATCAAGCAGCACATTCAAGAGGCT
CCTGCCAAGCCTGAGGAGGCAGAGGCCGAGCCCTTCACAGACTCCTCTCTGTTTGCACAC
TGGGGCCAGGAGCTCAGCCCCGAAGGCCGGCGCGTGGCCCTGAAGCAATTCCAGTACTAC
GGCTACAACGCCTACCTCAGCGACCGCCTGCCCCTGGACCGGCCCCTGCCTGACCTCAGA
CCCAGTGGGTGCCGTAACCTCTCATTTCCTGACAGCCTGCCAGAGGTGAGCATCGTGTTC
ATCTTCGTCAATGAAGCGCTTTCAGTGCTGCTGCGCTCCATCCACTCGGCCATGGAACGC
ACGCCCCCACATCTGCTCAAGGAGATCATTCTGGTGGATGACAACAGCAGTAACGAGGAA
CTGAAGGAGAAGCTGACCGAATATGTGGACAAGGTGAACAGCCAGAAGCCAGGCTTCATC
AAAGTCGTGCGTCACAGCAAGCAGGAAGGCCTCATCCGCTCCAGGGTCAGTGGCTGGAGG
GCGGCCACTGCCCCTGTGGTGGCACTCTTTGATGCCCACGTGGAGTTCAATGTGGGCTGG
GCTGAACCTGTACTCACCCGCATCAAGGAGAACCGGAAGCGGATCATCTCGCCATCCTTT
GATAACATCAAATATGACAACTTTGAGATAGAAGAGTACCCGCTGGCTGCCCAGGGCTTT
GACTGGGAGCTGTGGTGCCGCTACCTAAATCCCCCCAAGGCCTGGTGGAAGCTGGAGAAC
TCCACAGCGCCAATCAGGAGCCCTGCCCTCATTGGCTGCTTCATTGTGGACCGGCAGTAC
TTCCAGGAGATCGGCCTGCTGGACGAAGGCATGGAAGTCTACGGGGGCGAGAATGTGGAG
CTTGGGATCAGGGTGTGGCAGTGTGGCGGGAGTGTGGAGGTCCTGCCCTGCTCACGGATT
GCCCACATTGAGCGAGCCCACAAGCCCTACACAGAGGACCTCACCGCCCATGTCCGCAGG
AACGCTCTCAGGGTGGCTGAAGTCTGGATGGATGAATTTAAAAGCCACGTCTACATGGCA
TGGAACATACCGCAGGAGGACTCAGGAATTGACATTGGGGACATCACTGCAAGGAAGGCT
CTCAGGAAACAGCTGCAGTGCAAGACCTTCCGGTGGTACCTGGTCAGCGTGTACCCAGAG
ATGAGGATGTACTCCGACATCATTGCCTATGGAGTGCTGCAGAATTCTCTGAAGACTGAT
TTGTGTCTTGACCAGGGGCCAGATACAGAGAATGTCCCCATCATGTACATCTGCCATGGG
ATGACGCCTCAGAACGTGTACTACACGAGCAGTCAGCAGATCCATGTGGGCATTCTGAGC
CCCACCGTGGATGATGATGACAACCGATGCCTGGTGGACGTCAACAGCCGGCCCCGGCTC
ATCGAATGCAGCTACGCCAAAGCCAAGAGGATGAAGCTTCACTGGCAGTTCTCTCAGGGA
GGACCCATCCAGAACCGCAAGTCTAAGCGCTGTCTGGAGCTGCAGGAGAATAGCGACCTG
GAGTTCGGCTTCCAGCTGGTGTTGCAGAAGTGCTCGGGCCAGCACTGGAGCATCACCAAC
GTCCTGAGGAGCCTCGCGTCCTGA
Enzyme 45 GenBank Gene ID NM_198516.2 Link Image
Enzyme 45 GeneCard ID GALNTL4 Link Image
Enzyme 45 GenAtlas ID GALNTL4 Link Image
Enzyme 45 HGNC ID HGNC:30488 Link Image
Enzyme 45 Chromosome Location 1
Enzyme 45 Locus 11p15.3
Enzyme 45 SNPs SNPJam Report Link Image
Enzyme 45 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 45 Metabolite References Not Available
Enzyme 46 [top]
Enzyme 46 ID 6291
Enzyme 46 Name N-acetylgalactosaminyltransferase 7
Enzyme 46 Synonyms
  1. Polypeptide GalNAc transferase 7
  2. GalNAc-T7
  3. pp-GaNTase 7
  4. Protein-UDP acetylgalactosaminyltransferase 7
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7
Enzyme 46 Gene Name GALNT7
Enzyme 46 Protein Sequence >N-acetylgalactosaminyltransferase 7
MRLKIGFILRSLLVVGSFLGLVVLWSSLTPRPDDPSPLSRMREDRDVNDPMPNRGGNGLA
PGEDRFKPVVPWPHVEGVEVDLESIRRINKAKNEQEHHAGGDSQKDIMQRQYLTFKPQTF
TYHDPVLRPGILGNFEPKEPEPPGVVGGPGEKAKPLVLGPEFKQAIQASIKEFGFNMVAS
DMISLDRSVNDLRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVIKRTPRKYLA
EIVLIDDFSNKEHLKEKLDEYIKLWNGLVKVFRNERREGLIQARSIGAQKAKLGQVLIYL
DAHCEVAVNWYAPLVAPISKDRTICTVPLIDVINGNTYEIIPQGGGDEDGYARGAWDWSM
LWKRVPLTPQEKRLRKTKTEPYRSPAMAGGLFAIEREFFFELGLYDPGLQIWGGENFEIS
YKIWQCGGKLLFVPCSRVGHIYRLEGWQGNPPPIYVGSSPTLKNYVRVVEVWWDEYKDYF
YASRPESQALPYGDISELKKFREDHNCKSFKWFMEEIAYDITSHYPLPPKNVDWGEIRGF
ETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHC
NLNEFKEWQYFKNLHRFTHIPSGKCLDRSEVLHQVFISNCDSSKTTQKWEMNNIHSV
Enzyme 46 Number of Residues 657
Enzyme 46 Molecular Weight 75388.6
Enzyme 46 Theoretical pI 7.12
Enzyme 46 GO Classification Not Available
Enzyme 46 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 46 Specific Function Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified
Enzyme 46 Pathways Not Available
Enzyme 46 Reactions Not Available
Enzyme 46 Pfam Domain Function
Enzyme 46 Signals
  • None
Enzyme 46 Transmembrane Regions
  • 7-29
Enzyme 46 Essentiality Not Available
Enzyme 46 GenBank ID Protein 6318186 Link Image
Enzyme 46 UniProtKB/Swiss-Prot ID Q86SF2 Link Image
Enzyme 46 UniProtKB/Swiss-Prot Entry Name GALT7_HUMAN Link Image
Enzyme 46 PDB ID Not Available
Enzyme 46 Cellular Location Not Available
Enzyme 46 Gene Sequence >1974 bp
ATGAGGCTGAAGATTGGGTTCATCTTACGCAGTTTGCTGGTGGTGGGAAGCTTCCTGGGG
CTAGTGGTCCTCTGGTCTTCCCTGACCCCGCGGCCGGACGACCCAAGCCCGCTGAGCAGG
ATGAGGGAAGACAGAGATGTCAATGACCCCATGCCCAACCGAGGCGGCAATGGACTAGCT
CCTGGGGAGGACAGATTCAAACCTGTGGTACCATGGCCTCATGTTGAAGGAGTAGAAGTG
GACTTAGAGTCTATTAGAAGAATAAACAAGGCCAAAAATGAACAAGAGCACCATGCTGGA
GGAGATTCCCAGAAAGATATCATGCAGAGGCAGTATCTCACATTTAAGCCTCAGACATTC
ACCTACCATGATCCTGTGCTTCGCCCAGGGATCCTCGGTAACTTTGAACCCAAAGAACCT
GAGCCTCCTGGAGTGGTTGGTGGCCCTGGAGAGAAAGCCAAGCCATTGGTTTTGGGACCA
GAATTCAAACAAGCAATTCAAGCCAGCATTAAAGAGTTTGGATTTAACATGGTGGCAAGT
GACATGATCTCACTGGACCGCAACGTCAATGACTTACGCCAAGAAGAATGCAAGTATTGG
CATTATGATGAAAACTTGCTCACTTCGAGCGTTGTCATTGTCTTCCATAATGAAGGATGG
TCAACCCTCATGAGAACAGTCCACAGTGTAATTAAAAGGACTCCAAGGAAATATTTAGCA
GAAATTGTGTTAATTGACGATTTCAGTAATAAAGAACACTTAAAAGAAAAACTGGATGAA
TATATTAAGCTGTGGAATGGCCTAGTGAAGGTATTTCGAAATGAAAGAAGGGAAGGTTTA
ATTCAAGCACGAAGTATTGGTGCTCAGAAGGCTAAACTTGGACAGGTTTTGATATACCTT
GATGCCCACTGTGAAGTGGCAGTTAACTGGTATGCACCACTTGTAGCTCCCATATCTAAG
GACAGAACCATTTGCACTGTGCCGCTTATAGATGTCATAAATGGCAACACATATGAAATT
ATACCCCAAGGGGGTGGTGATGAAGATGGGTATGCCCGAGGAGCATGGGATTGGAGTATG
CTCTGGAAACGGGTGCCTCTGACCCCTCAAGAGAAGAGACTGAGAAAAACAAAAACTGAA
CCGTATCGGTCCCCAGCCATGGCTGGGGGATTATGTGCCATTGAACGAGAGTTCTTCTTT
GAATTGGGTCTCTATGATCCAAGTCTCCAGATTTGGGGTGGTGAAAACTTTGAGATCTCA
TACAAGATATGGCAGTGTGGTGGCAAATTATTATTTGTTCCTTGTTCTCGTGTTGGACAT
ATCTACCGTCTTGAGGGCTGGCAAGGAAATCCTCCGCCCATTTATGTTGGGTCTTCTCCA
ACTCTGAAGAATTATGTTAGAGTTGTGGAGGTTTGGTGGGATGAATATAAAGACTACTTC
TATGCTAGTCGTCCTGAATCGCAGGCATTACCATATGGGGATATATCGGAGCTGAAAAAA
TTTCGAGAAGATCACAACTGCCAAAGTTTTAAGTGGTTCATGGAAGAAATAGCTTATGAT
ATCACCTCACACTACCCTTTGCCACCCAAAAATGTTGACTGGGGAGAAATCAGAGGCTTC
GAAACTGCTTACTGCATTGATAGCATGGGAAAAACAAATGGAGGCTTTGTTGAACTAGGA
CCCTGCCACAGGATGGGAGGGAATCAGCTTTTCAGAATCAATGAAGCAAATCAACTCATG
CAGTATGACCAGTGTTTGACAAAGGGAGCTGATGGATCAAAAGTTATGATTACACACTGT
AATCTAAATGAATTTAAGGAATGGCAGTACTTCAAGAACCTGCACAGATTTACTCATATT
CCTTCAGGAAAGTGTTTAGATCGCTCAGAGGTCCTGCATCAAGTATTCATCTCCAATTGT
GACTCCAGTAAAACGACTCAAAAATGGGAAATGAATAACATCCATAGTGTTTAG
Enzyme 46 GenBank Gene ID AJ002744 Link Image
Enzyme 46 GeneCard ID GALNT7 Link Image
Enzyme 46 GenAtlas ID GALNT7 Link Image
Enzyme 46 HGNC ID HGNC:4129 Link Image
Enzyme 46 Chromosome Location 4
Enzyme 46 Locus 4q31.1
Enzyme 46 SNPs SNPJam Report Link Image
Enzyme 46 General References
  1. Bennett EP, Hassan H, Hollingsworth MA, Clausen H: A novel human UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates. FEBS Lett. 1999 Oct 29;460(2):226-30. [PubMed Link Image]
  2. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 46 Metabolite References Not Available
Enzyme 47 [top]
Enzyme 47 ID 6292
Enzyme 47 Name Polypeptide N-acetylgalactosaminyltransferase 6
Enzyme 47 Synonyms
  1. Polypeptide GalNAc transferase 6
  2. GalNAc-T6
  3. pp-GaNTase 6
  4. Protein-UDP acetylgalactosaminyltransferase 6
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6
Enzyme 47 Gene Name GALNT6
Enzyme 47 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 6
MRLLRRRHMPLRLAMVGCAFVLFLFLLHRDVSSREEATEKPWLKSLVSRKDHVLDLMLEA
MNNLRDSMPKLQIRAPEAQQTLFSINQSCLPGFYTPAELKPFWERPPQDPNAPGADGKAF
QKSKWTPLETQEKEEGYKKHCFNAFASDRISLQRSLGPDTRPPECVDQKFRRCPPLATTS
VIIVFHNEAWSTLLRTVYSVLHTTPAILLKEIILVDDASTEEHLKEKLEQYVKQLQVVRV
VRQEERKGLITARLLGASVAQAEVLTFLDAHCECFHGWLEPLLARIAEDKTVVVSPDIVT
IDLNTFEFAKPVQRGRVHSRGNFDWSLTFGWETLPPHEKQRRKDETYPIKSPTFAGGLFS
ISKSYFEHIGTYDNQMEIWGGENVEMSFRVWQCGGQLEIIPCSVVGHVFRTKSPHTFPKG
TSVIARNQVRLAEVWMDSYKKIFYRRNLQAAKMAQEKSFGDISERLQLREQLHCHNFSWY
LHNVYPEMFVPDLTPTFYGAIKNLGTNQCLDVGENNRGGKPLIMYSCHGLGGNQYFEYTT
QRDLRHNIAKQLCLHVSKGALGLGSCHFTGKNSQVPKDEEWELAQDQLIRNSGSGTCLTS
QDKKPAMAPCNPSDPHQLWLFV
Enzyme 47 Number of Residues 622
Enzyme 47 Molecular Weight 71158.1
Enzyme 47 Theoretical pI 8.25
Enzyme 47 GO Classification Not Available
Enzyme 47 General Function Cell wall/membrane/envelope biogenesis
Enzyme 47 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 47 Pathways
Enzyme 47 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 47 Pfam Domain Function
Enzyme 47 Signals
  • None
Enzyme 47 Transmembrane Regions
  • 9-28
Enzyme 47 Essentiality Not Available
Enzyme 47 GenBank ID Protein 115298684 Link Image
Enzyme 47 UniProtKB/Swiss-Prot ID Q8NCL4 Link Image
Enzyme 47 UniProtKB/Swiss-Prot Entry Name GALT6_HUMAN Link Image
Enzyme 47 PDB ID Not Available
Enzyme 47 Cellular Location Not Available
Enzyme 47 Gene Sequence >1869 bp
ATGAGGCTCCTCCGCAGACGCCACATGCCCCTGCGCCTGGCCATGGTGGGCTGCGCCTTT
GTGCTCTTCCTCTTCCTCCTGCATAGGGATGTGAGCAGCAGAGAGGAGGCCACAGAGAAG
CCGTGGCTGAAGTCCCTGGTGAGCCGGAAGGATCACGTCCTGGACCTCATGCTGGAGGCC
ATGAACAACCTTAGAGATTCAATGCCCAAGCTCCAAATCAGGGCTCCAGAAGCCCAGCAG
ACTCTGTTCTCCATAAACCAGTCCTGCCTCCCTGGGTTCTATACCCCAGCTGAACTGAAG
CCCTTCTGGGAACGGCCACCACAGGACCCCAATGCCCCTGGGGCAGATGGAAAAGCATTT
CAGAAGAGCAAGTGGACCCCCCTGGAGACCCAGGAAAAGGAAGAAGGCTATAAGAAGCAC
TGTTTCAATGCCTTTGCCAGCGACCGGATCTCCCTGCAGAGGTCCCTGGGGCCAGACACC
CGACCACCTGAGTGTGTGGACCAGAAGTTCCGGCGCTGCCCCCCACTGGCCACCACCAGC
GTGATCATTGTGTTCCACAACGAAGCCTGGTCCACACTGCTGCGAACAGTGTACAGCGTC
CTACACACCACCCCTGCCATCTTGCTCAAGGAGATCATACTGGTGGATGATGCCAGCACA
GAGGAGCACCTAAAGGAGAAGCTGGAGCAGTACGTGAAGCAGCTGCAGGTGGTGAGGGTG
GTGCGGCAGGAGGAGCGGAAGGGGCTGATCACCGCCCGGCTGCTGGGGGCCAGCGTGGCA
CAGGCGGAGGTGCTCACGTTCCTGGATGCCCACTGTGAGTGCTTCCACGGCTGGCTGGAG
CCCCTCCTGGCTCGAATCGCTGAGGACAAGACAGTGGTGGTGAGCCCAGACATCGTCACC
ATCGACCTTAATACTTTTGAGTTCGCCAAGCCCGTCCAGAGGGGCAGAGTCCATAGCCGA
GGCAACTTTGACTGGAGCCTGACCTTCGGCTGGGAAACACTTCCTCCACATGAGAAGCAG
AGGCGCAAGGATGAAACCTACCCCATCAAATCCCCGACGTTTGCTGGTGGCCTCTTCTCC
ATCTCCAAGTCCTACTTTGAGCACATCGGTACCTATGATAATCAGATGGAGATCTGGGGA
GGGGAGAACGTGGAAATGTCCTTCCGGGTGTGGCAGTGTGGGGGCCAGCTGGAGATCATC
CCCTGCTCTGTCGTAGGCCATGTGTTCCGGACCAAGAGCCCCCACACCTTCCCCAAGGGC
ACTAGTGTCATTGCTCGCAATCAAGTGCGCCTGGCAGAGGTCTGGATGGACAGCTACAAG
AAGATTTTCTATAGGAGAAATCTGCAGGCAGCAAAGATGGCCCAAGAGAAATCCTTCGGT
GACATTTCGGAACGACTGCAGCTGAGGGAACAACTGCACTGTCACAACTTTTCCTGGTAC
CTGCACAATGTCTACCCAGAGATGTTTGTTCCTGACCTGACGCCCACCTTCTATGGTGCC
ATCAAGAACCTCGGCACCAACCAATGCCTGGATGTGGGTGAGAACAACCGCGGGGGGAAG
CCCCTCATCATGTACTCCTGCCACGGCCTTGGCGGCAACCAGTACTTTGAGTACACAACT
CAGAGGGACCTTCGCCACAACATCGCAAAGCAGCTGTGTCTACATGTCAGCAAGGGTGCT
CTGGGCCTTGGGAGCTGTCACTTCACTGGCAAGAATAGCCAGGTCCCCAAGGACGAGGAA
TGGGAATTGGCCCAGGATCAGCTCATCAGGAACTCAGGATCTGGTACCTGCCTGACATCC
CAGGACAAAAAGCCAGCCATGGCCCCCTGCAATCCCAGTGACCCCCATCAGTTGTGGCTC
TTTGTCTAG
Enzyme 47 GenBank Gene ID NM_007210.3 Link Image
Enzyme 47 GeneCard ID GALNT6 Link Image
Enzyme 47 GenAtlas ID GALNT6 Link Image
Enzyme 47 HGNC ID HGNC:4128 Link Image
Enzyme 47 Chromosome Location 1
Enzyme 47 Locus 12q13
Enzyme 47 SNPs SNPJam Report Link Image
Enzyme 47 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]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 47 Metabolite References Not Available
Enzyme 48 [top]
Enzyme 48 ID 6293
Enzyme 48 Name Polypeptide N-acetylgalactosaminyltransferase 14
Enzyme 48 Synonyms
  1. Polypeptide GalNAc transferase 14
  2. GalNAc-T14
  3. pp-GaNTase 14
  4. Protein-UDP acetylgalactosaminyltransferase 14
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14
Enzyme 48 Gene Name GALNT14
Enzyme 48 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 14
MRRLTRRLVLPVFGVLWITVLLFFWVTKRKLEVPTGPEVQTPKPSDADWDDLWDQFDERR
YLNAKKWRVGDDPYKLYAFNQRESERISSNRAIPDTRHLRCTLLVYCTDLPPTSIIITFH
NEARSTLLRTIRSVLNRTPTHLIREIILVDDFSNDPDDCKQLIKLPKVKCLRNNERQGLV
RSRIRGADIAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIE
SASELRGGFDWSLHFQWEQLSPEQKARRLDPTEPIRTPIIAGGLFVIDKAWFDYLGKYDM
DMDIWGGENFEISFRVWMCGGSLEIVPCSRVGHVFRKKHPYVFPDGNANTYIKNTKRTAE
VWMDEYKQYYYAARPFALERPFGNVESRLDLRKNLRCQSFKWYLENIYPELSIPKESSIQ
KGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKGEDAKSQVWAFTYTQQILQEELCLSVI
TLFPGAPVVLVLCKNGDDRQQWTKTGSHIEHIASHLCLDTDMFGDGTENGKEIVVNPCES
SLMSQHWDMVSS
Enzyme 48 Number of Residues 552
Enzyme 48 Molecular Weight 64320.0
Enzyme 48 Theoretical pI 7.78
Enzyme 48 GO Classification Not Available
Enzyme 48 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 48 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 48 Pathways
Enzyme 48 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 48 Pfam Domain Function
Enzyme 48 Signals
  • None
Enzyme 48 Transmembrane Regions
  • 7-26
Enzyme 48 Essentiality Not Available
Enzyme 48 GenBank ID Protein 28268674 Link Image
Enzyme 48 UniProtKB/Swiss-Prot ID Q96FL9 Link Image
Enzyme 48 UniProtKB/Swiss-Prot Entry Name GLT14_HUMAN Link Image
Enzyme 48 PDB ID Not Available
Enzyme 48 Cellular Location Not Available
Enzyme 48 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 48 GenBank Gene ID AB078144 Link Image
Enzyme 48 GeneCard ID GALNT14 Link Image
Enzyme 48 GenAtlas ID GALNT14 Link Image
Enzyme 48 HGNC ID HGNC:22946 Link Image
Enzyme 48 Chromosome Location 2
Enzyme 48 Locus 2p23.1
Enzyme 48 SNPs SNPJam Report Link Image
Enzyme 48 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]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 48 Metabolite References Not Available
Enzyme 49 [top]
Enzyme 49 ID 6294
Enzyme 49 Name Polypeptide N-acetylgalactosaminyltransferase 2
Enzyme 49 Synonyms
  1. Polypeptide GalNAc transferase 2
  2. GalNAc-T2
  3. pp-GaNTase 2
  4. Protein-UDP acetylgalactosaminyltransferase 2
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2
  6. Polypeptide N-acetylgalactosaminyltransferase 2 soluble form
Enzyme 49 Gene Name GALNT2
Enzyme 49 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 2
MRRRSRMLLCFAFLWVLGIAYYMYSGGGSALAGGAGGGAGRKEDWNEIDPIKKKDLHHSN
GEEKAQSMETLPPGKVRWPDFNQEAYVGGTMVRSGQDPYARNKFNQVESDKLRMDRAIPD
TRHDQCQRKQWRVDLPATSVVITFHNEARSALLRTVVSVLKKSPPHLIKEIILVDDYSND
PEDGALLGKIEKVRVLRNDRREGLMRSRVRGADAAQAKVLTFLDSHCECNEHWLEPLLER
VAEDRTRVVSPIIDVINMDNFQYVGASADLKGGFDWNLVFKWDYMTPEQRRSRQGNPVAP
IKTPMIAGGLFVMDKFYFEELGKYDMMMDVWGGENLEISFRVWQCGGSLEIIPCSRVGHV
FRKQHPYTFPGGSGTVFARNTRRAAEVWMDEYKNFYYAAVPSARNVPYGNIQSRLELRKK
LSCKPFKWYLENVYPELRVPDHQDIAFGALQQGTNCLDTLGHFADGVVGVYECHNAGGNQ
EWALTKEKSVKHMDLCLTVVDRAPGSLIKLQGCRENDSRQKWEQIEGNSKLRHVGSNLCL
DSRTAKSGGLSVEVCGPALSQQWKFTLNLQQ
Enzyme 49 Number of Residues 571
Enzyme 49 Molecular Weight 64732.3
Enzyme 49 Theoretical pI 8.46
Enzyme 49 GO Classification Not Available
Enzyme 49 General Function Involved in manganese ion binding
Enzyme 49 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 49 Pathways
Enzyme 49 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 49 Pfam Domain Function
Enzyme 49 Signals
  • None
Enzyme 49 Transmembrane Regions
  • 7-24
Enzyme 49 Essentiality Not Available
Enzyme 49 GenBank ID Protein 158261119 Link Image
Enzyme 49 UniProtKB/Swiss-Prot ID Q10471 Link Image
Enzyme 49 UniProtKB/Swiss-Prot Entry Name GALT2_HUMAN Link Image
Enzyme 49 PDB ID Not Available
Enzyme 49 Cellular Location Not Available
Enzyme 49 Gene Sequence >1716 bp
ATGCGGCGGCGCTCGCGGATGCTGCTCTGCTTCGCCTTCCTGTGGGTGCTGGGCATCGCC
TACTACATGTACTCGGGGGGCGGCTCTGCGCTGGCCGGGGGCGCGGGCGGCGGCGCCGGC
AGGAAGGAGGACTGGAATGAAATTGACCCCATTAAAAAGAAAGACCTTCATCACAGCAAT
GGAGAAGAGAAAGCACAAAGCATGGAGACCCTCCCTCCAGGGAAAGTACGGTGGCCAGAC
TTTAACCAGGAAGCTTATGTTGGAGGGACGATGGTCCGCTCCGGGCAGGACCCTTACGCC
CGCAACAAGTTCAACCAGGTGGAGAGTGATAAGCTTCGAATGGACAGAGCCATCCCTGAC
ACCCGGCATGACCAGTGTCAGCGGAAGCAGTGGCGGGTGGATCTGCCGGCCACCAGCGTG
GTGATCACGTTTCACAATGAAGCCAGGTCGGCCCTACTCAGGACCGTGGTCAGCGTGCTT
AAGAAAAGCCCGCCCCATCTCATAAAAGAAATCATCTTGGTGGATGACTACAGCAATGAT
CCTGAGGACGGGGCTCTCTTGGGGAAAATTGAGAAAGTGCGAGTTCTTAGAAATGATCGA
CGAGAAGGCCTCATGCGCTCACGGGTTCGGGGGGCCGATGCTGCCCAAGCCAAGGTCCTG
ACCTTCCTGGACAGTCACTGCGAGTGTAATGAGCACTGGCTGGAGCCCCTCCTGGAAAGG
GTGGCGGAGGACAGGACTCGGGTTGTGTCACCCATCATCGATGTCATTAATATGGACAAC
TTTCAGTATGTGGGGGCATCTGCTGACTTGAAGGGCGGTTTTGACTGGAACTTGGTATTC
AAGTGGGATTACATGACGCCTGAGCAGAGAAGGTCCCGGCAGGGGAACCCAGTCGCCCCT
ATAAAAACCCCCATGATTGCTGGTGGGCTGTTTGTGATGGATAAGTTCTATTTTGAAGAA
CTGGGGAAGTACGACATGATGATGGATGTGTGGGGAGGAGAGAACCTAGAGATCTCGTTC
CGCGTGTGGCAGTGTGGTGGCAGCCTGGAGATCATCCCGTGCAGCCGTGTGGGACACGTG
TTCCGGAAGCAGCACCCCTACACGTTCCCGGGTGGCAGTGGCACTGTCTTTGCCCGAAAC
ACCCGCCGGGCAGCAGAGGTCTGGATGGATGAATACAAAAATTTCTATTATGCAGCAGTG
CCTTCTGCTAGAAACGTTCCTTATGGAAATATTCAGAGCAGATTGGAGCTTAGGAAGAAA
CTCAGCTGCAAGCCTTTCAAATGGTACCTTGAAAATGTCTATCCAGAGTTAAGGGTTCCA
GACCATCAGGATATAGCTTTTGGGGCCTTGCAGCAGGGAACTAACTGCCTCGACACTTTG
GGACACTTTGCTGATGGTGTGGTTGGAGTTTATGAATGTCACAATGCTGGGGGAAACCAG
GAATGGGCCTTGACGAAGGAGAAGTCGGTGAAGCACATGGATTTGTGCCTTACTGTGGTG
GACCGGGCACCGGGCTCTCTTATAAAGCTGCAGGGCTGCCGAGAAAATGACAGCAGACAG
AAATGGGAACAGATCGAGGGCAACTCCAAGCTGAGGCACGTGGGCAGCAACCTGTGCCTG
GACAGTCGCACGGCCAAGAGCGGGGGCCTAAGCGTGGAGATGTGTGGCCCGGCCCTTTCG
CAGCAGTGGAAGTTCACGCTCAACCTGCAGCAGTAG
Enzyme 49 GenBank Gene ID AK290048 Link Image
Enzyme 49 GeneCard ID GALNT2 Link Image
Enzyme 49 GenAtlas ID GALNT2 Link Image
Enzyme 49 HGNC ID HGNC:4124 Link Image
Enzyme 49 Chromosome Location 1
Enzyme 49 Locus 1q41-q42
Enzyme 49 SNPs SNPJam Report Link Image
Enzyme 49 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]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Wandall HH, Hassan H, Mirgorodskaya E, Kristensen AK, Roepstorff P, Bennett EP, Nielsen PA, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H: Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. J Biol Chem. 1997 Sep 19;272(38):23503-14. [PubMed Link Image]
  6. Rottger S, White J, Wandall HH, Olivo JC, Stark A, Bennett EP, Whitehouse C, Berger EG, Clausen H, Nilsson T: Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. J Cell Sci. 1998 Jan;111 ( Pt 1):45-60. [PubMed Link Image]
  7. Iwasaki H, Zhang Y, Tachibana K, Gotoh M, Kikuchi N, Kwon YD, Togayachi A, Kudo T, Kubota T, Narimatsu H: Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2. J Biol Chem. 2003 Feb 21;278(8):5613-21. Epub 2002 Nov 15. [PubMed Link Image]
Enzyme 49 Metabolite References Not Available
Enzyme 50 [top]
Enzyme 50 ID 6295
Enzyme 50 Name Polypeptide N-acetylgalactosaminyltransferase 12
Enzyme 50 Synonyms
  1. Polypeptide GalNAc transferase 12
  2. GalNAc-T12
  3. pp-GaNTase 12
  4. Protein-UDP acetylgalactosaminyltransferase 12
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12
Enzyme 50 Gene Name GALNT12
Enzyme 50 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 12
MWGRTARRRCPRELRRGREALLVLLALLALAGLGSVLRAQRGAGAGAAEPGPPRTPRPGR
REPVMPRPPVPANALGARGEAVRLQLQGEELRLQEESVRLHQINIYLSDRISLHRRLPER
WNPLCKEKKYDYDNLPRTSVIIAFYNEAWSTLLRTVYSVLETSPDILLEEVILVDDYSDR
EHLKERLANELSGLPKVRLIRANKREGLVRARLLGASAARGDVLTFLDCHCECHEGWLEP
LLQRIHEEESAVVCPVIDVIDWNTFEYLGNSGEPQIGGFDWRLVFTWHTVPERERIRMQS
PVDVIRSPTMAGGLFAVSKKYFEYLGSYDTGMEVWGGENLEFSFRIWQCGGVLETHPCSH
VGHVFPKQAPYSRNKALANSVRAAEVWMDEFKELYYHRNPRARLEPFGDVTERKQLRDKL
QCKDFKWFLETVYPELHVPEDRPGFFGMLQNKGLTDYCFDYNPPDENQIVGHQVILYLCH
GMGQNQFFEYTSQKEIRYNTHQPEGCIAVEAGMDTLIMHLCEETAPENQKFILQEDGSLF
HEQSKKCVQAARKESSDSFVPLLRDCTNSDHQKWFFKERML
Enzyme 50 Number of Residues 581
Enzyme 50 Molecular Weight 66937.8
Enzyme 50 Theoretical pI 6.78
Enzyme 50 GO Classification Not Available
Enzyme 50 General Function Involved in polypeptide N-acetylgalactosaminyltransfera
Enzyme 50 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 50 Pathways
Enzyme 50 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 50 Pfam Domain Function
Enzyme 50 Signals
  • None
Enzyme 50 Transmembrane Regions
  • 20-37
Enzyme 50 Essentiality Not Available
Enzyme 50 GenBank ID Protein 22122074 Link Image
Enzyme 50 UniProtKB/Swiss-Prot ID Q8IXK2 Link Image
Enzyme 50 UniProtKB/Swiss-Prot Entry Name GLT12_HUMAN Link Image
Enzyme 50 PDB ID Not Available
Enzyme 50 Cellular Location Not Available
Enzyme 50 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 50 GenBank Gene ID AB078146 Link Image
Enzyme 50 GeneCard ID GALNT12 Link Image
Enzyme 50 GenAtlas ID GALNT12 Link Image
Enzyme 50 HGNC ID HGNC:19877 Link Image
Enzyme 50 Chromosome Location 9
Enzyme 50 Locus 9q22.33
Enzyme 50 SNPs SNPJam Report Link Image
Enzyme 50 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]
  2. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 50 Metabolite References Not Available
Enzyme 51 [top]
Enzyme 51 ID 6296
Enzyme 51 Name Polypeptide N-acetylgalactosaminyltransferase 1
Enzyme 51 Synonyms
  1. Polypeptide GalNAc transferase 1
  2. GalNAc-T1
  3. pp-GaNTase 1
  4. Protein-UDP acetylgalactosaminyltransferase 1
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
  6. Polypeptide N-acetylgalactosaminyltransferase 1 soluble form
Enzyme 51 Gene Name GALNT1
Enzyme 51 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 1
MRKFAYCKVVLATSLIWVLLDMFLLLYFSECNKCDEKKERGLPAGDVLEPVQKPHEGPGE
MGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALNRSLPDVRLEGCKTKVYPDNLPTTSV
VIVFHNEAWSTLLRTVHSVINRSPRHMIEEIVLVDDASERDFLKRPLESYVKKLKVPVHV
IRMEQRSGLIRARLKGAAVSKGQVITFLDAHCECTVGWLEPLLARIKHDRRTVVCPIIDV
ISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDR
DYFQEIGTYDAGMDIWGGENLEISFRIWQCGGTLEIVTCSHVGHVFRKATPYTFPGGTGQ
IINKNNRRLAEVWMDEFKNFFYIISPGVTKVDYGDISSRVGLRHKLQCKPFSWYLENIYP
DSQIPRHYFSLGEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDD
LCLDVSKLNGPVTMLKCHHLKGNQLWEYDPVKLTLQHVNSNQCLDKATEEDSQVPSIRDC
NGSRSQQWLLRNVTLPEIF
Enzyme 51 Number of Residues 559
Enzyme 51 Molecular Weight 64218.5
Enzyme 51 Theoretical pI 7.77
Enzyme 51 GO Classification Not Available
Enzyme 51 General Function Involved in manganese ion binding
Enzyme 51 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 51 Pathways
Enzyme 51 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 51 Pfam Domain Function
Enzyme 51 Signals
  • None
Enzyme 51 Transmembrane Regions
  • 9-28
Enzyme 51 Essentiality Not Available
Enzyme 51 GenBank ID Protein 13124891 Link Image
Enzyme 51 UniProtKB/Swiss-Prot ID Q10472 Link Image
Enzyme 51 UniProtKB/Swiss-Prot Entry Name GALT1_HUMAN Link Image
Enzyme 51 PDB ID 1XHB Link Image
Enzyme 51 PDB File Show
Enzyme 51 3D Structure
Enzyme 51 Cellular Location Not Available
Enzyme 51 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
GATTCTCAAATTCCACGTCACTATTTCTCATTGGGAGAGATACGAAATGTGGAAACGAAT
CAGTGTCTAGATAACATGGCTAGAAAAGAGAATGAAAAAGTTGGAATTTTTAATTGCCAT
GGTATGGGGGGTAATCAGGTTTTCTCTTATACTGCCAACAAAGAAATTAGAACAGATGAC
CTTTGCTTGGATGTTTCCAAACTTAATGGCCCAGTTACAATGCTCAAATGCCACCACCTA
AAAGGCAACCAACTCTGGGAGTATGACCCAGTGAAATTAACCCTGCAGCATGTGAACAGT
AATCAGTGCCTGGATAAAGCCACAGAAGAGGATAGCCAGGTGCCCAGCATTAGAGACTGC
AATGGAAGTCGGTCCCAGCAGTGGCTTCTTCGAAACGTCACCCTGCCAGAAATATTCTGA
Enzyme 51 GenBank Gene ID NM_020474.3 Link Image
Enzyme 51 GeneCard ID GALNT1 Link Image
Enzyme 51 GenAtlas ID GALNT1 Link Image
Enzyme 51 HGNC ID HGNC:4123 Link Image
Enzyme 51 Chromosome Location 1
Enzyme 51 Locus 18q12.1
Enzyme 51 SNPs SNPJam Report Link Image
Enzyme 51 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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. 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]
  5. Wandall HH, Hassan H, Mirgorodskaya E, Kristensen AK, Roepstorff P, Bennett EP, Nielsen PA, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H: Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. J Biol Chem. 1997 Sep 19;272(38):23503-14. [PubMed Link Image]
  6. Rottger S, White J, Wandall HH, Olivo JC, Stark A, Bennett EP, Whitehouse C, Berger EG, Clausen H, Nilsson T: Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. J Cell Sci. 1998 Jan;111 ( Pt 1):45-60. [PubMed Link Image]
Enzyme 51 Metabolite References Not Available
Enzyme 52 [top]
Enzyme 52 ID 6320
Enzyme 52 Name Beta-1,4-galactosyltransferase 3
Enzyme 52 Synonyms
  1. Beta-1,4-GalTase 3
  2. Beta4Gal-T3
  3. b4Gal-T3
  4. UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 3
  5. UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 3
  6. N-acetyllactosamine synthase
  7. Nal synthase
  8. Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase
  9. Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase
Enzyme 52 Gene Name B4GALT3
Enzyme 52 Protein Sequence >Beta-1,4-galactosyltransferase 3
MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDQGPTFDYSHPRDVYSNLSH
LPGAPGGPPAPQGLPYCPERSPLLVGPVSVSFSPVPSLAEIVERNPRVEPGGRYRPAGCE
PRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVR
EALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSAL
TPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEEN
PHRFDLLVRTQNSWTQDGMNSLTYQLLARELGPLYTNITADIGTDPRGPRAPSGPRYPPG
SSQAFRQEMLQRRPPARPGPLSTANHTALRGSH
Enzyme 52 Number of Residues 393
Enzyme 52 Molecular Weight 43927.6
Enzyme 52 Theoretical pI 9.45
Enzyme 52 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 52 General Function Involved in transferase activity, transferring glycosyl groups
Enzyme 52 Specific Function Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids
Enzyme 52 Pathways
Enzyme 52 Reactions
  • UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine [RN:R01205 R06055]
Enzyme 52 Pfam Domain Function
Enzyme 52 Signals
  • None
Enzyme 52 Transmembrane Regions
  • 11-31
Enzyme 52 Essentiality Not Available
Enzyme 52 GenBank ID Protein 2982510 Link Image
Enzyme 52 UniProtKB/Swiss-Prot ID O60512 Link Image
Enzyme 52 UniProtKB/Swiss-Prot Entry Name B4GT3_HUMAN Link Image
Enzyme 52 PDB ID Not Available
Enzyme 52 Cellular Location Not Available
Enzyme 52 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 52 GenBank Gene ID Y12509 Link Image
Enzyme 52 GeneCard ID B4GALT3 Link Image
Enzyme 52 GenAtlas ID B4GALT3 Link Image
Enzyme 52 HGNC ID HGNC:926 Link Image
Enzyme 52 Chromosome Location 1
Enzyme 52 Locus 1q21-q23
Enzyme 52 SNPs SNPJam Report Link Image
Enzyme 52 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. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  7. 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 52 Metabolite References Not Available
Enzyme 53 [top]
Enzyme 53 ID 6343
Enzyme 53 Name UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1
Enzyme 53 Synonyms
  1. Beta-1,3-GalNAc-T1
  2. Beta-1,3-galactosyltransferase 3
  3. Beta-1,3-GalTase 3
  4. Beta3Gal-T3
  5. Beta3GalT3
  6. b3Gal-T3
  7. Beta-3-Gx-T3
  8. Galactosylgalactosylglucosylceramide beta-D-acetyl-galactosaminyltransferase
  9. Globoside synthase
  10. UDP-N-acetylgalactosamine:globotriaosylceramide beta-1,3-N-acetylgalactosaminyltransferase
Enzyme 53 Gene Name B3GALNT1
Enzyme 53 Protein Sequence >UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 1
MASALWTVLPSRMSLRSLKWSLLLLSLLSFFVMWYLSLPHYNVIERVNWMYFYEYEPIYR
QDFHFTLREHSNCSHQNPFLVILVTSHPSDVKARQAIRVTWGEKKSWWGYEVLTFFLLGQ
EAEKEDKMLALSLEDEHLLYGDIIRQDFLDTYNNLTLKTIMAFRWVTEFCPNAKYVMKTD
TDVFINTGNLVKYLLNLNHSEKFFTGYPLIDNYSYRGFYQKTHISYQEYPFKVFPPYCSG
LGYIMSRDLVPRIYEMMGHVKPIKFEDVYVGICLNLLKVNIHIPEDTNLFFLYRIHLDVC
QLRRVIAAHGFSSKEIITFWQVMLRNTTCHY
Enzyme 53 Number of Residues 331
Enzyme 53 Molecular Weight 39511.6
Enzyme 53 Theoretical pI 7.89
Enzyme 53 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 53 General Function Involved in galactosyltransferase activity
Enzyme 53 Specific Function Transfers N-acetylgalactosamine onto globotriaosylceramide
Enzyme 53 Pathways
Enzyme 53 Reactions
  • UDP-N-acetyl-D-galactosamine + alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosyl- (11)-ceramide = UDP + N-acetyl-beta-D-galactosaminyl-(1->3)-alpha-D-galactosyl-(1->4)- beta-D-galactosyl-(1->4)-beta-D-glucosyl-(11)-ceramide [RN:R05631 R05962]
Enzyme 53 Pfam Domain Function
Enzyme 53 Signals
  • None
Enzyme 53 Transmembrane Regions
  • 21-43
Enzyme 53 Essentiality Not Available
Enzyme 53 GenBank ID Protein 3256005 Link Image
Enzyme 53 UniProtKB/Swiss-Prot ID O75752 Link Image
Enzyme 53 UniProtKB/Swiss-Prot Entry Name B3GL1_HUMAN Link Image
Enzyme 53 PDB ID Not Available
Enzyme 53 Cellular Location Not Available
Enzyme 53 Gene Sequence >996 bp
ATGGCCTCGGCTCTCTGGACTGTCCTTCCGAGTAGGATGTCACTGAGATCCCTCAAATGG
AGCCTCCTGCTGCTGTCACTCCTGAGTTTCTTTGTGATGTGGTACCTCAGCCTTCCCCAC
TACAATGTGATAGAACGCGTGAACTGGATGTACTTCTATGAGTATGAGCCGATTTACAGA
CAAGACTTTCACTTCACACTTCGAGAGCATTCAAACTGCTCTCATCAAAATCCATTTCTG
GTCATTCTGGTGACCTCCCACCCTTCAGATGTGAAAGCCAGGCAGGCCATTAGAGTTACT
TGGGGTGAAAAAAAGTCTTGGTGGGGATATGAGGTTCTTACATTTTTCTTATTAGGCCAA
GAGGCTGAAAAGGAAGACAAAATGTTGGCATTGTCCTTAGAGGATGAACACCTTCTTTAT
GGTGACATAATCCGACAAGATTTTTTAGACACATATAATAACCTGACCTTGAAAACCATT
ATGGCATTCAGGTGGGTAACTGAGTTTTGCCCCAATGCCAAGTACGTAATGAAGACAGAC
ACTGATGTTTTCATCAATACTGGCAATTTAGTGAAGTATCTTTTAAACCTAAACCACTCA
GAGAAGTTTTTCACAGGTTATCCTCTAATTGATAATTATTCCTATAGAGGATTTTACCAA
AAAACCCATATTTCTTACCAGGAGTATCCTTTCAAGGTGTTCCCTCCATACTGCAGTGGG
TTGGGTTATATAATGTCCAGAGATTTGGTGCCAAGGATCTATGAAATGATGGGTCACGTA
AAACCCATCAAGTTTGAAGATGTTTATGTCGGGATCTGTTTGAATTTATTAAAAGTGAAC
ATTCATATTCCAGAAGACACAAATCTTTTCTTTCTATATAGAATCCATTTGGATGTCTGT
CAACTGAGACGTGTGATTGCAGCCCATGGCTTTTCTTCCAAGGAGATCATCACTTTTTGG
CAGGTCATGCTAAGGAACACCACATGCCATTATTAA
Enzyme 53 GenBank Gene ID Y15062 Link Image
Enzyme 53 GeneCard ID B3GALNT1 Link Image
Enzyme 53 GenAtlas ID B3GALNT1 Link Image
Enzyme 53 HGNC ID HGNC:918 Link Image
Enzyme 53 Chromosome Location 3
Enzyme 53 Locus 3q25
Enzyme 53 SNPs SNPJam Report Link Image
Enzyme 53 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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed Link Image]
Enzyme 53 Metabolite References Not Available
Enzyme 54 [top]
Enzyme 54 ID 6380
Enzyme 54 Name Glycogen [starch] synthase, liver
Enzyme 54 Synonyms Not Available
Enzyme 54 Gene Name GYS2
Enzyme 54 Protein Sequence >Glycogen [starch] synthase, liver
MLRGRSLSVTSLGGLPQWEVEELPVEELLLFEVAWEVTNKVGGIYTVIQTKAKTTADEWG
ENYFLIGPYFEHNMKTQVEQCEPVNDAVRRAVDAMNKHGCQVHFGRWLIEGSPYVVLFDI
GYSAWNLDRWKGDLWEACSVGIPYHDREANDMLIFGSLTAWFLKEVTDHADGKYVVAQFH
EWQAGIGLILSRARKLPIATIFTTHATLLGRYLCAANIDFYNHLDKFNIDKEAGERQIYH
RYCMERASVHCAHVFTTVSEITAIEAEHMLKRKPDVVTPNGLNVKKFSAVHEFQNLHAMY
KARIQDFVRGHFYGHLDFDLEKTLFLFIAGRYEFSNKGADIFLESLSRLNFLLRMHKSDI
TVMVFFIMPAKTNNFNVETLKGQAVRKQLWDVAHSVKEKFGKKLYDALLRGEIPDLNDIL
DRDDLTIMKRAIFSTQRQSLPPVTTHNMIDDSTDPILSTIRRIGLFNNRTDRVKVILHPE
FLSSTSPLLPMDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSVTTNLSGFGCFMQE
HVADPTAYGIYIVDRRFRSPDDSCNQLTKFLYGFCKQSRRQRIIQRNRTERLSDLLDWRY
LGRYYQHARHLTLSRAFPDKFHVELTSPPTTEGFKYPRPSSVPPSPSGSQASSPQSSDVE
DEVEDERYDEEEEAERDRLNIKSPFSLSHVPHGKKKLHGEYKN
Enzyme 54 Number of Residues 703
Enzyme 54 Molecular Weight 80988.4
Enzyme 54 Theoretical pI 6.82
Enzyme 54 GO Classification
Function
  • UDP-glucosyltransferase activity
  • UDP-glycosyltransferase activity
  • catalytic activity
  • glycogen (starch) synthase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • alcohol metabolic process
  • glucose metabolic process
  • glycogen biosynthetic process
  • glycogen metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 54 General Function Involved in glycogen (starch) synthase activity
Enzyme 54 Specific Function Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan
Enzyme 54 Pathways
Enzyme 54 Reactions
  • UDP-glucose + [(1->4)-alpha-D-glucosyl]n = UDP + [(1->4)-alpha-D-glucosyl]n+1 [RN:R00292 R06051]
Enzyme 54 Pfam Domain Function
Enzyme 54 Signals
  • None
Enzyme 54 Transmembrane Regions
  • None
Enzyme 54 Essentiality Not Available
Enzyme 54 GenBank ID Protein 119372286 Link Image
Enzyme 54 UniProtKB/Swiss-Prot ID P54840 Link Image
Enzyme 54 UniProtKB/Swiss-Prot Entry Name GYS2_HUMAN Link Image
Enzyme 54 PDB ID Not Available
Enzyme 54 Cellular Location Not Available
Enzyme 54 Gene Sequence >2112 bp
ATGCTTCGAGGCCGATCCCTCTCTGTAACATCCCTGGGTGGGCTTCCCCAGTGGGAAGTC
GAAGAACTTCCTGTGGAGGAGTTACTGCTCTTTGAAGTTGCTTGGGAAGTGACCAATAAA
GTTGGAGGCATCTATACTGTGATTCAGACAAAGGCCAAAACAACAGCAGATGAATGGGGA
GAGAACTATTTTCTGATAGGTCCATATTTTGAGCATAATATGAAGACTCAGGTGGAACAG
TGTGAACCTGTAAATGATGCTGTCAGAAGAGCAGTGGACGCAATGAATAAGCATGGCTGC
CAGGTGCATTTTGGAAGATGGCTGATAGAAGGAAGTCCTTATGTGGTACTTTTTGACATA
GGCTATTCAGCTTGGAATCTGGACAGGTGGAAGGGTGACCTCTGGGAAGCATGCAGTGTC
GGCATTCCTTATCATGACCGAGAAGCCAATGATATGCTGATATTTGGATCTTTAACTGCC
TGGTTCTTAAAAGAGGTGACAGATCATGCAGATGGTAAATATGTCGTTGCCCAATTCCAT
GAATGGCAGGCTGGAATTGGACTGATCCTTTCTCGAGCCAGGAAACTTCCTATTGCCACA
ATATTTACAACCCACGCTACACTACTTGGGAGGTATCTCTGTGCAGCAAATATTGATTTC
TACAACCATCTTGATAAGTTTAACATTGACAAAGAGGCTGGGGAAAGGCAGATTTACCAC
CGGTACTGCATGGAGCGAGCTTCCGTTCATTGCGCTCACGTGTTCACCACGGTTTCTGAA
ATAACAGCAATAGAAGCTGAACATATGCTGAAGAGAAAGCCTGATGTAGTTACTCCAAAC
GGCTTGAATGTTAAGAAATTTTCAGCAGTGCATGAGTTTCAAAATCTACATGCCATGTAC
AAGGCCAGAATCCAAGATTTTGTTCGAGGTCATTTCTATGGTCATCTCGACTTTGATCTT
GAAAAGACTTTGTTCCTTTTCATTGCTGGGAGGTATGAGTTTTCAAACAAAGGAGCTGAC
ATCTTCCTAGAATCCTTATCCAGGCTAAATTTCCTGCTGAGGATGCATAAAAGTGACATC
ACAGTGATGGTGTTTTTCATTATGCCTGCCAAGACAAATAATTTCAACGTGGAAACCCTG
AAAGGACAAGCAGTGCGAAAACAGCTGTGGGATGTTGCACATTCTGTGAAGGAAAAGTTT
GGAAAAAAACTCTATGATGCATTATTAAGAGGAGAAATTCCTGACCTGAACGATATTTTA
GATCGAGATGATCTAACAATTATGAAAAGAGCCATCTTTTCAACTCAGCGACAGTCATTG
CCCCCAGTGACCACGCACAACATGATTGATGACTCCACCGACCCCATCCTCAGCACCATT
AGACGGATTGGACTTTTCAACAACCGCACAGATAGAGTCAAGGTGATTTTGCACCCAGAG
TTTCTATCCTCCACCAGTCCCTTACTACCCATGGACTATGAAGAGTTTGTTAGAGGTTGT
CATCTTGGAGTATTTCCATCATACTATGAACCCTGGGGTTATACTCCAGCTGAATGCACT
GTGATGGGTATCCCCAGTGTGACCACGAATCTCTCCGGGTTTGGCTGTTTCATGCAGGAG
CACGTGGCTGATCCTACTGCTTACGGTATTTACATCGTTGACAGGCGGTTCCGTTCTCCA
GATGATTCTTGCAATCAGCTGACTAAGTTTCTCTATGGATTTTGCAAACAGTCACGCCGC
CAAAGGATTATCCAGAGGAACAGAACTGAGAGGCTCTCAGATCTTCTGGATTGGAGATAC
TTAGGCAGATATTACCAGCATGCCAGACACCTGACATTAAGCAGAGCTTTTCCAGATAAA
TTCCATGTGGAACTAACATCACCACCAACGACAGAAGGATTTAAATATCCCAGGCCTTCC
TCAGTACCACCTTCTCCTTCAGGGTCTCAGGCCTCCAGTCCTCAGAGCAGTGATGTGGAA
GATGAAGTGGAGGATGAGAGATACGATGAGGAAGAGGAGGCTGAAAGGGATCGGTTAAAT
ATCAAGTCACCATTTTCACTGAGCCACGTTCCTCATGGGAAGAAAAAGCTGCATGGTGAA
TATAAGAACTGA
Enzyme 54 GenBank Gene ID NM_021957.3 Link Image
Enzyme 54 GeneCard ID GYS2 Link Image
Enzyme 54 GenAtlas ID GYS2 Link Image
Enzyme 54 HGNC ID HGNC:4707 Link Image
Enzyme 54 Chromosome Location 1
Enzyme 54 Locus 12p12.2
Enzyme 54 SNPs SNPJam Report Link Image
Enzyme 54 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]
  3. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 54 Metabolite References Not Available
Enzyme 55 [top]
Enzyme 55 ID 6382
Enzyme 55 Name Glycogenin-1
Enzyme 55 Synonyms
  1. GN-1
  2. GN1
Enzyme 55 Gene Name GYG1
Enzyme 55 Protein Sequence >Glycogenin-1
MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTTRRLVVLATPQVSDSMRKVLETVFDEVIM
VDVLDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFDREEL
SAAPDPGWPDCFNSGVFVYQPSVETYNQLLHLASEQGSFDGGDQGILNTFFSSWATTDIR
KHLPFIYNLSSISIYSYLPAFKVFGASAKVVHFLGRVKPWNYTYDPKTKSVKSEAHDPNM
THPEFLILWWNIFTTNVLPLLQQFGLVKDTCSYVNVLSDLVYTLAFSCGFCRKEDVSGAI
SHLSLGEIPAMAQPFVSSEERKERWEQGQADYMGADSFDNIKRKLDTYLQ
Enzyme 55 Number of Residues 350
Enzyme 55 Molecular Weight 39383.4
Enzyme 55 Theoretical pI 5.19
Enzyme 55 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
Component
Enzyme 55 General Function Involved in transferase activity, transferring glycosyl groups
Enzyme 55 Specific Function Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase
Enzyme 55 Pathways Not Available
Enzyme 55 Reactions
  • UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin [RN:R03681]
Enzyme 55 Pfam Domain Function
Enzyme 55 Signals
  • None
Enzyme 55 Transmembrane Regions
  • None
Enzyme 55 Essentiality Not Available
Enzyme 55 GenBank ID Protein 20127457 Link Image
Enzyme 55 UniProtKB/Swiss-Prot ID P46976 Link Image
Enzyme 55 UniProtKB/Swiss-Prot Entry Name GLYG_HUMAN Link Image
Enzyme 55 PDB ID Not Available
Enzyme 55 Cellular Location Not Available
Enzyme 55 Gene Sequence >1053 bp
ATGACAGATCAGGCCTTTGTGACACTAACCACAAACGATGCCTACGCCAAAGGTGCCCTG
GTCCTGGGATCATCTCTGAAACAGCACAGGACCACCAGGAGGCTGGTCGTGCTCGCCACC
CCTCAGGTCTCAGACTCCATGAGAAAAGTTTTAGAGACAGTCTTTGATGAAGTCATCATG
GTAGATGTCTTGGACAGTGGCGATTCTGCTCATCTAACCTTAATGAAGAGGCCAGAGTTG
GGTGTCACGCTGACAAAGCTCCACTGCTGGTCGCTTACACAGTATTCAAAATGTGTATTC
ATGGATGCAGATACTCTGGTCCTAGCAAATATTGATGATCTTTTTGACAGAGAAGAATTG
TCAGCAGCACCAGACCCAGGGTGGCCTGACTGCTTCAATTCCGGAGTCTTCGTTTATCAG
CCTTCAGTTGAAACATACAATCAGCTGTTGCATCTTGCTTCTGAGCAAGGTAGTTTTGAT
GGTGGGGACCAAGGCATACTGAACACATTTTTTAGCAGCTGGGCAACAACAGATATCAGA
AAACACCTGCCGTTTATTTATAACCTAAGCAGCATCTCTATATACTCCTACCTCCCGGCA
TTTAAAGTGTTTGGTGCAAGTGCCAAAGTTGTGCATTTCCTGGGACGAGTCAAACCATGG
AATTATACTTATGATCCCAAAACAAAAAGTGTCAAAAGTGAGGCCCATGATCCCAACATG
ACTCATCCAGAGTTTCTCATCCTGTGGTGGAACATCTTTACCACCAACGTTTTACCTCTG
CTTCAACAATTTGGCCTTGTCAAAGACACCTGCTCATATGTAAATGTGCTTTCAGACTTG
GTCTATACACTGGCTTTCTCTTGTGGCTTCTGTAGAAAGGAAGATGTCTCAGGAGCCATA
TCACATCTGTCCCTTGGGGAGATCCCAGCTATGGCACAGCCGTTTGTATCCTCGGAAGAA
CGGAAGGAACGATGGGAACAGGGCCAGGCTGATTATATGGGAGCAGATTCCTTTGACAAC
ATCAAGAGGAAACTTGACACTTACCTCCAGTAG
Enzyme 55 GenBank Gene ID NM_004130.3 Link Image
Enzyme 55 GeneCard ID GYG1 Link Image
Enzyme 55 GenAtlas ID GYG1 Link Image
Enzyme 55 HGNC ID HGNC:4699 Link Image
Enzyme 55 Chromosome Location 3
Enzyme 55 Locus 3q24-q25.1
Enzyme 55 SNPs SNPJam Report Link Image
Enzyme 55 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]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 55 Metabolite References Not Available
Enzyme 56 [top]
Enzyme 56 ID 6383
Enzyme 56 Name Glycogen [starch] synthase, muscle
Enzyme 56 Synonyms Not Available
Enzyme 56 Gene Name GYS1
Enzyme 56 Protein Sequence >Glycogen [starch] synthase, muscle
MPLNRTLSMSSLPGLEDWEDEFDLENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGD
NYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVG
ASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFH
EWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYH
RYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQS
KARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQ
TVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKML
DKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPE
FLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEE
HIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKY
LGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYRYPRPASVPPSPSLSRHSSPHQSEDE
EDPRNGPLEEDGERYDEDEEAAKDRRNIRAPEWPRRASCTSSTSGSKRNSVDTATSSSLS
TPSEPLSPTSSLGEERN
Enzyme 56 Number of Residues 737
Enzyme 56 Molecular Weight 83784.8
Enzyme 56 Theoretical pI 6.10
Enzyme 56 GO Classification
Function
  • UDP-glucosyltransferase activity
  • UDP-glycosyltransferase activity
  • catalytic activity
  • glycogen (starch) synthase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • alcohol metabolic process
  • glucose metabolic process
  • glycogen biosynthetic process
  • glycogen metabolic process
  • hexose metabolic process
  • metabolic process
  • monosaccharide metabolic process
  • small molecule metabolic process
Component
Enzyme 56 General Function Involved in glycogen (starch) synthase activity
Enzyme 56 Specific Function Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan
Enzyme 56 Pathways
Enzyme 56 Reactions
  • UDP-glucose + [(1->4)-alpha-D-glucosyl]n = UDP + [(1->4)-alpha-D-glucosyl]n+1 [RN:R00292 R06051]
Enzyme 56 Pfam Domain Function
Enzyme 56 Signals
  • None
Enzyme 56 Transmembrane Regions
  • None
Enzyme 56 Essentiality Not Available
Enzyme 56 GenBank ID Protein 12803569 Link Image
Enzyme 56 UniProtKB/Swiss-Prot ID P13807 Link Image
Enzyme 56 UniProtKB/Swiss-Prot Entry Name GYS1_HUMAN Link Image
Enzyme 56 PDB ID Not Available
Enzyme 56 Cellular Location Not Available
Enzyme 56 Gene Sequence >2214 bp
ATGCCTTTAAACCGCACTTTGTCCATGTCCTCACTGCCAGGACTGGAGGACTGGGAGGAT
GAATTCGACCTGGAGAACGCAGTGCTCTTCGAAGTGGCCTGGGAGGTGGCTAACAAGGTG
GGTGGCATCTACACGGTGCTGCAGACGAAGGCGAAGGTGACAGGGGACGAATGGGGCGAC
AACTACTTCCTGGTGGGGCCGTACACGGAGCAGGGCGTGAGGACCCAGGTGGAACTGCTG
GAGGCCCCCACCCCGGCCCTGAAGAGGACACTGGATTCCATGAACAGCAAGGGCTGCAAG
GTGTATTTCGGGCGCTGGCTGATCGAGGGAGGCCCTCTGGTGGTGCTCCTGGACGTGGGT
GCCTCAGCTTGGGCCCTGGAGCGCTGGAAGGGAGAGCTCTGGGATACCTGCAACATCGGA
GTGCCGTGGTACGACCGCGAGGCCAACGACGCTGTCCTCTTTGGCTTTCTGACCACCTGG
TTCCTGGGTGAGTTCCTGGCACAGAGTGAGGAGAAGCCACATGTGGTTGCTCACTTCCAT
GAGTGGTTGGCAGGCGTTGGACTCTGCCTGTGTCGTGCCCGGCGACTGCCTGTAGCAACC
ATCTTCACCACCCATGCCACGCTGCTGGGGCGCTACCTGTGTGCCGGTGCCGTGGACTTC
TACAACAACCTGGAGAACTTCAACGTGGACAAGGAAGCAGGGGAGAGGCAGATCTACCAC
CGATACTGCATGGAAAGGGCGGCAGCCCACTGCGCTCACGTCTTCACTACTGTGTCCCAG
ATCACCGCCATCGAGGCACAGCACTTGCTCAAGAGGAAACCAGATATTGTGACCCCCAAT
GGGCTGAATGTGAAGAAGTTTTCTGCCATGCATGAGTTCCAGAACCTCCATGCTCAGAGC
AAGGCTCGAATCCAGGAGTTTGTGCGGGGCCATTTTTATGGGCATCTGGACTTCAACTTG
GACAAGACCTTATACTTCTTTATCGCCGGCCGCTATGAGTTCTCCAACAAGGGTGCTGAC
GTCTTCCTGGAGGCATTGGCTCGGCTCAACTATCTGCTCAGAGTGAACGGCAGCGAGCAG
ACAGTGGTTGCCTTCTTCATCATGCCAGCGCGGACCAACAATTTCAACGTGGAAACCCTC
AAAGGCCAAGCTGTGCGCAAACAGCTTTGGGACACGGCCAACACGGTGAAGGAAAAGTTC
GGGAGGAAGCTTTATGAATCCTTACTGGTTGGGAGCCTTCCCGACATGAACAAGATGCTG
GATAAGGAAGACTTCACTATGATGAAGAGAGCCATCTTTGCAACGCAGCGGCAGTCTTTC
CCCCCTGTGTGCACCCACAATATGCTGGATGACTCCTCAGACCCCATCCTGACCACCATC
CGCCGAATCGGCCTCTTCAATAGCAGTGCCGACAGGGTGAAGGTGATTTTCCACCCGGAG
TTCCTCTCCTCCACAAGCCCCCTGCTCCCTGTGGACTATGAGGAGTTTGTCCGTGGCTGT
CACCTTGGAGTCTTCCCCTCCTACTATGAGCCTTGGGGCTACACACCGGCTGAGTGCACG
GTTATGGGAATCCCCAGTATCTCCACCAATCTCTCCGGCTTCGGCTGCTTCATGGAGGAA
CACATCGCAGACCCCTCAGCTTACGGTATCTACATTCTTGACCGGCGGTTCCGCAGCCTG
GATGATTCCTGCTCGCAGCTCACCTCCTTCCTCTACAGTTTCTGTCAGCAGAGCCGGCGG
CAGCGTATCATCCAGCGGAACCGCACGGAGCGCCTCTCCGACCTTCTGGACTGGAAATAC
CTAGGCCGGTACTATATGTCTGCGCGCCACATGGCGCTGTCCAAGGCCTTTCCAGAGCAC
TTCACCTACGAGCCCAACGAGGCGGATGCGGCCCAGGGGTACCGCTACCCACGGCCAGCC
TCGGTGCCACCGTCGCCCTCGCTGTCACGACACTCCAGCCCGCACCAGAGTGAGGACGAG
GAGGATCCCCGGAACGGGCCGCTGGAGGAAGACGGCGAGCGCTACGATGAGGACGAGGAG
GCCGCCAAGGACCGGCGCAACATCCGTGCACCAGAGTGGCCGCGCCGAGCGTCCTGCACC
TCCTCCACCAGCGGCAGCAAGCGCAACTCTGTGGACACGGCCACCTCCAGCTCACTCAGC
ACCCCGAGCGAGCCCCTCAGCCCCACCAGCTCCCTGGGCGAGGAGCGTAACTAA
Enzyme 56 GenBank Gene ID BC002617 Link Image
Enzyme 56 GeneCard ID GYS1 Link Image
Enzyme 56 GenAtlas ID GYS1 Link Image
Enzyme 56 HGNC ID HGNC:4706 Link Image
Enzyme 56 Chromosome Location 1
Enzyme 56 Locus 19q13.3
Enzyme 56 SNPs SNPJam Report Link Image
Enzyme 56 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Kollberg G, Tulinius M, Gilljam T, Ostman-Smith I, Forsander G, Jotorp P, Oldfors A, Holme E: Cardiomyopathy and exercise intolerance in muscle glycogen storage disease 0. N Engl J Med. 2007 Oct 11;357(15):1507-14. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  8. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  9. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 56 Metabolite References Not Available
Enzyme 57 [top]
Enzyme 57 ID 6384
Enzyme 57 Name Glycogenin-2
Enzyme 57 Synonyms
  1. GN-2
  2. GN2
Enzyme 57 Gene Name GYG2
Enzyme 57 Protein Sequence >Glycogenin-2
MSETEFHHGAQAGLELLRSSNSPTSASQSAGMTVTDQAFVTLATNDIYCQGALVLGQSLR
RHRLTRKLVVLITPQVSSLLRVILSKVFDEVIEVNLIDSADYIHLAFLKRPELGLTLTKL
HCWTLTHYSKCVFLDADTLVLSNVDELFDRGEFSAAPDPGWPDCFNSGVFVFQPSLHTHK
LLLQHAMEHGSFDGADQGLLNSFFRNWSTTDIHKHLPFIYNLSSNTMYTYSPAFKQFGSS
AKVVHFLGSMKPWNYKYNPQSGSVLEQGSASSSQHQAAFLHLWWTVYQNNVLPLYKSVQA
GEARASPGHTLCHSDVGGPCADSASGVGEPCENSTPSAGVPCANSPLGSNQPAQGLPEPT
QIVDETLSLPEGRRSEDMIACPETETPAVITCDPLSQPSPQPADFTETETILQPANKVES
VSSEETFEPSQELPAEALRDPSLQDALEVDLAVSVSQISIEEKVKELSPEEERRKWEEGR
IDYMGKDAFARIQEKLDRFLQ
Enzyme 57 Number of Residues 501
Enzyme 57 Molecular Weight 55183.3
Enzyme 57 Theoretical pI 4.74
Enzyme 57 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
Component
Enzyme 57 General Function Involved in transferase activity, transferring glycosyl groups
Enzyme 57 Specific Function Self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase
Enzyme 57 Pathways Not Available
Enzyme 57 Reactions
  • UDP-alpha-D-glucose + glycogenin = UDP + alpha-D-glucosylglycogenin [RN:R03681]
Enzyme 57 Pfam Domain Function
Enzyme 57 Signals
  • None
Enzyme 57 Transmembrane Regions
  • None
Enzyme 57 Essentiality Not Available
Enzyme 57 GenBank ID Protein 119964690 Link Image
Enzyme 57 UniProtKB/Swiss-Prot ID O15488 Link Image
Enzyme 57 UniProtKB/Swiss-Prot Entry Name GLYG2_HUMAN Link Image
Enzyme 57 PDB ID Not Available
Enzyme 57 Cellular Location Not Available
Enzyme 57 Gene Sequence >1506 bp
ATGTCGGAGACAGAGTTTCACCATGGTGCCCAGGCTGGTCTCGAACTCCTGAGGTCAAGC
AATTCACCCACCTCAGCCTCCCAAAGTGCTGGAATGACAGTGACTGATCAGGCTTTTGTC
ACACTAGCCACCAATGACATCTACTGCCAGGGCGCCCTGGTCCTGGGGCAGTCACTGAGG
AGACACAGGCTGACGAGGAAGCTGGTGGTGTTGATCACTCCTCAGGTGTCCAGCCTGCTC
AGGGTCATCCTCTCGAAGGTGTTCGATGAAGTCATTGAAGTGAATCTAATCGATAGTGCC
GACTACATCCACCTGGCCTTTCTGAAGAGACCTGAGCTCGGGCTCACCCTCACCAAGCTT
CACTGTTGGACTCTCACTCACTACAGCAAGTGTGTCTTCCTGGATGCAGACACTCTGGTG
CTGTCCAATGTCGATGAGCTGTTTGACAGGGGAGAGTTTTCTGCGGCCCCGGACCCCGGA
TGGCCGGATTGCTTCAATAGCGGGGTGTTTGTCTTCCAGCCTTCTCTCCACACGCATAAA
CTCCTGCTACAGCACGCCATGGAACACGGCAGCTTTGACGGGGCAGACCAAGGCTTACTG
AATAGTTTCTTCAGGAACTGGTCGACCACAGACATCCACAAGCACCTGCCGTTCATCTAT
AACTTGAGTAGTAACACGATGTACACTTACAGCCCTGCCTTCAAGCAATTCGGTTCCAGT
GCAAAGGTCGTCCACTTTTTGGGGTCCATGAAACCTTGGAACTACAAGTACAATCCACAG
AGTGGCTCGGTGTTGGAGCAAGGCTCAGCGTCCAGCAGCCAGCACCAGGCGGCATTCCTT
CATCTCTGGTGGACGGTCTACCAGAACAACGTGCTGCCCCTTTATAAAAGCGTCCAAGCG
GGGGAAGCACGCGCGTCTCCTGGTCACACACTTTGCCACAGTGATGTGGGGGGGCCGTGT
GCGGATTCAGCCTCTGGTGTTGGAGAGCCGTGTGAAAATTCAACACCCAGTGCGGGCGTG
CCGTGTGCAAATTCACCACTGGGTTCTAACCAGCCTGCTCAGGGCCTTCCGGAGCCGACC
CAGATAGTGGATGAGACCCTGTCCCTACCTGAAGGACGCCGTTCAGAAGATATGATAGCT
TGTCCTGAAACTGAGACTCCTGCCGTGATAACGTGTGACCCACTGTCCCAGCCTTCCCCT
CAGCCTGCAGACTTCACAGAGACTGAAACCATCTTGCAGCCAGCAAATAAAGTCGAAAGT
GTCTCATCCGAGGAAACCTTCGAACCAAGCCAGGAACTCCCTGCTGAGGCTCTCAGGGAC
CCCAGTCTGCAGGATGCACTGGAGGTCGACCTGGCCGTCTCTGTTTCCCAGATCTCCATC
GAAGAGAAGGTGAAGGAATTGAGCCCCGAGGAAGAGAGGAGGAAGTGGGAGGAAGGCCGT
ATCGACTACATGGGGAAGGACGCGTTTGCTCGCATCCAGGAGAAGCTGGACCGGTTCCTG
CAGTAA
Enzyme 57 GenBank Gene ID NM_003918.2 Link Image
Enzyme 57 GeneCard ID GYG2 Link Image
Enzyme 57 GenAtlas ID GYG2 Link Image
Enzyme 57 HGNC ID HGNC:4700 Link Image
Enzyme 57 Chromosome Location Not Available
Enzyme 57 Locus Not Available
Enzyme 57 SNPs SNPJam Report Link Image
Enzyme 57 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. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. 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 57 Metabolite References Not Available
Enzyme 58 [top]
Enzyme 58 ID 6389
Enzyme 58 Name Histo-blood group ABO system transferase
Enzyme 58 Synonyms
  1. Fucosylglycoprotein 3-alpha-galactosyltransferase
  2. Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
  3. Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase
  4. Glycoprotein-fucosylgalactoside alpha-galactosyltransferase
  5. Histo-blood group A transferase
  6. A transferase
  7. Histo-blood group B transferase
  8. B transferase
  9. NAGAT
  10. Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form
Enzyme 58 Gene Name ABO
Enzyme 58 Protein Sequence >Histo-blood group ABO system transferase
MAEVLRTLAGKPKCHALRPMILFLIMLVLVLFGYGVLSPRSLMPGSLERGFCMAVREPDH
LQRVSLPRMVYPQPKVLTPCRKDVLVVTPWLAPIVWEGTFNIDILNEQFRLQNTTIGLTV
FAIKKYVAFLKLFLETAEKHFMVGHRVHYYVFTDQPAAVPRVTLGTGRQLSVLEVRAYKR
WQDVSMRRMEMISDFCERRFLSEVDYLVCVDVDMEFRDHVGVEILTPLFGTLHPGFYGSS
REAFTYERRPQSQAYIPKDEGDFYYLGGFFGGSVQEVQRLTRACHQAMMVDQANGIEAVW
HDESHLNKYLLRHKPTKVLSPEYLWDQQLLGWPAVLRKLRFTAVPKNHQAVRNP
Enzyme 58 Number of Residues 354
Enzyme 58 Molecular Weight 40933.6
Enzyme 58 Theoretical pI 9.24
Enzyme 58 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • membrane
Enzyme 58 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 58 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 58 Pathways
  • Blood group glycolipid biosynthesis-neolactoseries (map00602 Link Image)
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
Enzyme 58 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 [RN:R04423]
Enzyme 58 Pfam Domain Function
Enzyme 58 Signals
  • None
Enzyme 58 Transmembrane Regions
  • 33-53
Enzyme 58 Essentiality Not Available
Enzyme 58 GenBank ID Protein 58331216 Link Image
Enzyme 58 UniProtKB/Swiss-Prot ID P16442 Link Image
Enzyme 58 UniProtKB/Swiss-Prot Entry Name BGAT_HUMAN Link Image
Enzyme 58 PDB ID 1LZI Link Image
Enzyme 58 PDB File Show
Enzyme 58 3D Structure
Enzyme 58 Cellular Location Not Available
Enzyme 58 Gene Sequence >1065 bp
ATGGCCGAGGTGTTGCGGACGCTGGCCGGAAAACCAAAATGCCACGCACTTCGACCTATG
ATCCTTTTCCTAATAATGCTTGTCTTGGTCTTGTTTGGTTACGGGGTCCTAAGCCCCAGA
AGTCTAATGCCAGGAAGCCTGGAACGGGGGTTCTGCATGGCTGTTAGGGAACCTGACCAT
CTGCAGCGCGTCTCGTTGCCAAGGATGGTCTACCCCCAGCCAAAGGTGCTGACACCGTGT
AGGAAGGATGTCCTCGTGGTGACCCCTTGGCTGGCTCCCATTGTCTGGGAGGGCACATTC
AACATCGACATCCTCAACGAGCAGTTCAGGCTCCAGAACACCACCATTGGGTTAACTGTG
TTTGCCATCAAGAAATACGTGGCTTTCCTGAAGCTGTTCCTGGAGACGGCGGAGAAGCAC
TTCATGGTGGGCCACCGTGTCCACTACTATGTCTTCACCGACCAGCCGGCCGCGGTGCCC
CGCGTGACGCTGGGGACCGGTCGGCAGCTGTCAGTGCTGGAGGTGCGCGCCTACAAGCGC
TGGCAGGACGTGTCCATGCGCCGCATGGAGATGATCAGTGACTTCTGCGAGCGGCGCTTC
CTCAGCGAGGTGGATTACCTGGTGTGCGTGGACGTGGACATGGAGTTCCGCGACCACGTG
GGCGTGGAGATCCTGACTCCGCTGTTCGGCACCCTGCACCCCGGCTTCTACGGAAGCAGC
CGGGAGGCCTTCACCTACGAGCGCCGGCCCCAGTCCCAGGCCTACATCCCCAAGGACGAG
GGCGATTTCTACTACCTGGGGGGGTTCTTCGGGGGGTCGGTGCAAGAGGTGCAGCGGCTC
ACCAGGGCCTGCCACCAGGCCATGATGGTCGACCAGGCCAACGGCATCGAGGCCGTGTGG
CACGACGAGAGCCACCTGAACAAGTACCTGCTGCGCCACAAACCCACCAAGGTGCTCTCC
CCCGAGTACTTGTGGGACCAGCAGCTGCTGGGCTGGCCCGCCGTCCTGAGGAAGCTGAGG
TTCACTGCGGTGCCCAAGAACCACCAGGCGGTCCGGAACCCGTGA
Enzyme 58 GenBank Gene ID NM_020469.2 Link Image
Enzyme 58 GeneCard ID ABO Link Image
Enzyme 58 GenAtlas ID ABO Link Image
Enzyme 58 HGNC ID HGNC:79 Link Image
Enzyme 58 Chromosome Location 9
Enzyme 58 Locus 9q34.2
Enzyme 58 SNPs SNPJam Report Link Image
Enzyme 58 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. Seltsam A, Das Gupta C, Bade-Doeding C, Blasczyk R: A weak blood group A phenotype caused by a translation-initiator mutation in the ABO gene. Transfusion. 2006 Mar;46(3):434-40. [PubMed Link Image]
  6. Seltsam A, Wagner FF, Gruger D, Gupta CD, Bade-Doeding C, Blasczyk R: Weak blood group B phenotypes may be caused by variations in the CCAAT-binding factor/NF-Y enhancer region of the ABO gene. Transfusion. 2007 Dec;47(12):2330-5. Epub 2007 Aug 30. [PubMed Link Image]
  7. Seltsam A, Gruger D, Just B, Figueiredo C, Gupta CD, Deluca DS, Blasczyk R: Aberrant intracellular trafficking of a variant B glycosyltransferase. Transfusion. 2008 Sep;48(9):1898-905. Epub 2008 May 29. [PubMed Link Image]
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  9. Seltsam A, Hallensleben M, Kollmann A, Blasczyk R: The nature of diversity and diversification at the ABO locus. Blood. 2003 Oct 15;102(8):3035-42. Epub 2003 Jun 26. [PubMed Link Image]
  10. Ogasawara K, Yabe R, Uchikawa M, Saitou N, Bannai M, Nakata K, Takenaka M, Fujisawa K, Ishikawa Y, Juji T, Tokunaga K: Molecular genetic analysis of variant phenotypes of the ABO blood group system. Blood. 1996 Oct 1;88(7):2732-7. [PubMed Link Image]
  11. 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]
  12. Roubinet F, Despiau S, Calafell F, Jin F, Bertranpetit J, Saitou N, Blancher A: Evolution of the O alleles of the human ABO blood group gene. Transfusion. 2004 May;44(5):707-15. [PubMed Link Image]
  13. 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]
  14. 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]
  15. 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]
  16. Marcus SL, Polakowski R, Seto NO, Leinala E, Borisova S, Blancher A, Roubinet F, Evans SV, Palcic MM: A single point mutation reverses the donor specificity of human blood group B-synthesizing galactosyltransferase. J Biol Chem. 2003 Apr 4;278(14):12403-5. Epub 2003 Jan 15. [PubMed Link Image]
  17. Nguyen HP, Seto NO, Cai Y, Leinala EK, Borisova SN, Palcic MM, Evans SV: The influence of an intramolecular hydrogen bond in differential recognition of inhibitory acceptor analogs by human ABO(H) blood group A and B glycosyltransferases. J Biol Chem. 2003 Dec 5;278(49):49191-5. Epub 2003 Sep 11. [PubMed Link Image]
  18. Lee HJ, Barry CH, Borisova SN, Seto NO, Zheng RB, Blancher A, Evans SV, Palcic MM: Structural basis for the inactivity of human blood group O2 glycosyltransferase. J Biol Chem. 2005 Jan 7;280(1):525-9. Epub 2004 Oct 8. [PubMed Link Image]
  19. Letts JA, Rose NL, Fang YR, Barry CH, Borisova SN, Seto NO, Palcic MM, Evans SV: Differential recognition of the type I and II H antigen acceptors by the human ABO(H) blood group A and B glycosyltransferases. J Biol Chem. 2006 Feb 10;281(6):3625-32. Epub 2005 Dec 2. [PubMed Link Image]
  20. Persson M, Letts JA, Hosseini-Maaf B, Borisova SN, Palcic MM, Evans SV, Olsson ML: Structural effects of naturally occurring human blood group B galactosyltransferase mutations adjacent to the DXD motif. J Biol Chem. 2007 Mar 30;282(13):9564-70. Epub 2007 Jan 26. [PubMed Link Image]
Enzyme 58 Metabolite References Not Available
Enzyme 59 [top]
Enzyme 59 ID 6390
Enzyme 59 Name 2-hydroxyacylsphingosine 1-beta-galactosyltransferase
Enzyme 59 Synonyms
  1. Ceramide UDP-galactosyltransferase
  2. Cerebroside synthase
  3. UDP-galactose-ceramide galactosyltransferase
Enzyme 59 Gene Name UGT8
Enzyme 59 Protein Sequence >2-hydroxyacylsphingosine 1-beta-galactosyltransferase
MKSYTPYFILLWSAVGIAKAAKIIIVPPIMFESHMYIFKTLASALHERGHHTVFLLSEGR
DIAPSNHYSLQRYPGIFNSTTSDAFLQSKMRNIFSGRLTAIELFDILDHYTKNCDLMVGN
HALIQGLKKEKFDLLLVDPNDMCGFVIAHLLGVKYAVFSTGLWYPAEVGAPAPLAYVPEF
NSLLTDRMNLLQRMKNTGVYLISRLGVSFLVLPKYERIMQKYNLLPEKSMYDLVHGSSLW
MLCTDVALEFPRPTLPNVVYVGGILTKPASPLPEDLQRWVNGANEHGFVLVSFGAGVKYL
SEDIANKLAGALGRLPQKVIWRFSGPKPKNLGNNTKLIEWLPQNDLLGHSKIKAFLSHGG
LNSIFETIYHGVPVVGIPLFGDHYDTMTRVQAKGMGILLEWKTVTEKELYEALVKVINNP
SYRQRAQKLSEIHKDQPGHPVNRTIYWIDYIIRHNGAHHLRAAVHQISFCQYFLLDIAFV
LLLGAALLYFLLSWVTKFIYRKIKSLWSRNKHSTVNGHYHNGILNGKYKRNGHIKHEKKV
K
Enzyme 59 Number of Residues 541
Enzyme 59 Molecular Weight 61437.3
Enzyme 59 Theoretical pI 9.97
Enzyme 59 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 59 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 59 Specific Function Catalyzes the transfer of galactose to ceramide, a key enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system
Enzyme 59 Pathways Not Available
Enzyme 59 Reactions
  • UDP-galactose + 2-(2-hydroxyacyl)sphingosine = UDP + 1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine [RN:R04322]
Enzyme 59 Pfam Domain Function
Enzyme 59 Signals
  • 1-20
Enzyme 59 Transmembrane Regions
  • 472-492
Enzyme 59 Essentiality Not Available
Enzyme 59 GenBank ID Protein 189491660 Link Image
Enzyme 59 UniProtKB/Swiss-Prot ID Q16880 Link Image
Enzyme 59 UniProtKB/Swiss-Prot Entry Name CGT_HUMAN Link Image
Enzyme 59 PDB ID Not Available
Enzyme 59 Cellular Location Not Available
Enzyme 59 Gene Sequence >1626 bp
ATGAAGTCTTACACTCCATATTTCATTCTCCTGTGGAGTGCTGTTGGGATAGCGAAGGCT
GCCAAAATCATCATCGTGCCGCCAATTATGTTTGAAAGCCATATGTACATTTTCAAGACG
CTAGCCTCAGCCTTGCACGAGAGAGGCCACCATACAGTGTTCCTCCTCTCTGAAGGCAGA
GACATCGCCCCATCTAATCATTACAGCCTCCAGCGCTACCCAGGGATCTTTAACAGTACC
ACCTCAGATGCTTTCCTACAGTCCAAGATGCGGAATATTTTCTCTGGGAGATTGACAGCA
ATCGAACTGTTTGACATACTGGATCACTATACTAAGAACTGTGACCTGATGGTTGGCAAC
CATGCCCTGATCCAGGGTCTGAAGAAAGAAAAATTTGACCTGCTGCTGGTGGACCCTAAT
GATATGTGTGGATTTGTGATAGCTCATCTTTTAGGGGTTAAATATGCTGTATTTTCAACT
GGCCTTTGGTATCCTGCTGAAGTGGGTGCTCCTGCTCCATTAGCATACGTCCCAGAGTTT
AACTCACTCCTCACAGACCGCATGAACTTGCTGCAAAGGATGAAAAATACCGGTGTTTAC
CTCATTTCCAGATTAGGGGTCAGCTTTCTGGTTCTTCCCAAATATGAAAGGATAATGCAG
AAGTACAACCTGCTGCCGGAGAAGTCCATGTATGATTTGGTTCATGGGTCCAGCCTGTGG
ATGCTGTGTACTGACGTAGCACTGGAATTCCCAAGACCCACTCTGCCTAATGTTGTTTAT
GTAGGAGGAATCCTAACCAAACCAGCCAGCCCACTACCAGAAGATCTCCAAAGATGGGTA
AATGGTGCTAATGAACATGGCTTTGTCTTGGTGTCTTTTGGAGCTGGTGTCAAGTATCTG
TCAGAAGACATTGCTAACAAACTGGCAGGAGCTCTGGGGAGATTGCCTCAAAAAGTGATT
TGGAGGTTTTCTGGACCCAAACCAAAGAATCTAGGAAACAACACTAAACTCATAGAATGG
TTACCACAAAATGACCTGCTTGGGCATTCAAAGATTAAAGCCTTCCTGAGCCATGGTGGT
TTGAACAGTATTTTTGAAACTATGTATCATGGTGTGCCTGTAGTGGGAATTCCACTCTTT
GGAGACCATTATGATACTATGACCAGAGTACAGGCAAAAGGCATGGGGATATTGCTAGAA
TGGAAGACAGTTACTGAAAAAGAGCTCTATGAAGCACTAGTGAAGGTTATCAATAATCCC
AGCTACCGTCAGAGGGCTCAGAAGCTTTCGGAAATTCACAAGGATCAACCTGGTCACCCT
GTCAATCGAACTATCTATTGGATAGATTATATTATTCGTCACAATGGAGCCCATCACCTA
CGTGCCGCTGTCCATCAGATCTCCTTTTGTCAGTATTTTTTACTGGATATTGCCTTTGTG
CTTTTGCTTGGTGCTGCCTTGTTATACTTTCTCTTGTCTTGGGTGACAAAATTTATCTAC
AGAAAAATCAAAAGTCTGTGGTCTAGAAATAAGCATAGCACAGTTAATGGACATTACCAC
AATGGAATCCTCAATGGCAAGTACAAAAGAAATGGCCATATTAAACATGAAAAGAAAGTG
AAATGA
Enzyme 59 GenBank Gene ID NM_001128174.1 Link Image
Enzyme 59 GeneCard ID UGT8 Link Image
Enzyme 59 GenAtlas ID UGT8 Link Image
Enzyme 59 HGNC ID HGNC:12555 Link Image
Enzyme 59 Chromosome Location 4
Enzyme 59 Locus 4q26
Enzyme 59 SNPs SNPJam Report Link Image
Enzyme 59 General References
  1. Bosio A, Binczek E, Le Beau MM, Fernald AA, Stoffel W: The human gene CGT encoding the UDP-galactose ceramide galactosyl transferase (cerebroside synthase): cloning, characterization, and assignment to human chromosome 4, band q26. Genomics. 1996 May 15;34(1):69-75. [PubMed Link Image]
  2. Kapitonov D, Yu RK: Cloning, characterization, and expression of human ceramide galactosyltransferase cDNA. Biochem Biophys Res Commun. 1997 Mar 17;232(2):449-53. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 59 Metabolite References Not Available
Enzyme 60 [top]
Enzyme 60 ID 6392
Enzyme 60 Name Chondroitin sulfate synthase 3
Enzyme 60 Synonyms
  1. Carbohydrate synthase 2
  2. Chondroitin glucuronyltransferase 3
  3. Chondroitin synthase 2
  4. ChSy-2
  5. Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II
  6. N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 3
  7. N-acetylgalactosaminyltransferase 3
Enzyme 60 Gene Name CHSY3
Enzyme 60 Protein Sequence >Chondroitin sulfate synthase 3
MAVRSRRPWMSVALGLVLGFTAASWLIAPRVAELSERKRRGSSLCSYYGRSAAGPRAGAQ
QPLPQPQSRPRQEQSPPPARQDLQGPPLPEAAPGITSFRSSPWQQPPPLQQRRRGREPEG
ATGLPGAPAAEGEPEEEDGGAAGQRRDGRPGSSHNGSGDGGAAAPSARPRDFLYVGVMTA
QKYLGSRALAAQRTWARFIPGRVEFFSSQQPPNAGQPPPPLPVIALPGVDDSYPPQKKSF
MMIKYMHDHYLDKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQTGLGNIEELGKL
GLEPGENFCMGGPGMIFSREVLRRMVPHIGECLREMYTTHEDVEVGRCVRRFGGTQCVWS
YEMQQLFHENYEHNRKGYIQDLHNSKIHAAITLHPNKRPAYQYRLHNYMLSRKISELRYR
TIQLHRESALMSKLSNTEVSKEDQQLGVIPSFNHFQPRERNEVIEWEFLTGKLLYSAAEN
QPPRQSLSSILRTALDDTVLQVMEMINENAKSRGRLIDFKEIQYGYRRVNPMHGVEYILD
LLLLYKRHKGRKLTVPVRRHAYLQQLFSKPFFRETEELDVNSLVESINSETQSFSFISNS
LKILSSFQGAKEMGGHNEKKVHILVPLIGRYDIFLRFMENFENMCLIPKQNVKLVIILFS
RDSGQDSSKHIELIKGYQNKYPKAEMTLIPMKGEFSRGLGLEMASAQFDNDTLLLFCDVD
LIFREDFLQRCRDNTIQGQQVYYPIIFSQYDPKVTNGGNPPTDDYFIFSKKTGFWRDYGY
GITCIYKSDLLGAGGFDTSIQGWGLEDVDLYNKVILSGLRPFRSQEVGVVHIFHPVHCDP
NLDPKQYKMCLGSKASTFASTMQLAELWLEKHLGVRYNRTLS
Enzyme 60 Number of Residues 882
Enzyme 60 Molecular Weight 100283.5
Enzyme 60 Theoretical pI 8.97
Enzyme 60 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • Golgi cisterna membrane
  • Golgi membrane
  • cell part
  • membrane
  • organelle membrane
Enzyme 60 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 60 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 60 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 60 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 [RN:R07336]
Enzyme 60 Pfam Domain Function
Enzyme 60 Signals
  • None
Enzyme 60 Transmembrane Regions
  • 8-28
Enzyme 60 Essentiality Not Available
Enzyme 60 GenBank ID Protein 37573674 Link Image
Enzyme 60 UniProtKB/Swiss-Prot ID Q70JA7 Link Image
Enzyme 60 UniProtKB/Swiss-Prot Entry Name CHSS3_HUMAN Link Image
Enzyme 60 PDB ID Not Available
Enzyme 60 Cellular Location Not Available
Enzyme 60 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 60 GenBank Gene ID AB086062 Link Image
Enzyme 60 GeneCard ID CHSY3 Link Image
Enzyme 60 GenAtlas ID CHSY3 Link Image
Enzyme 60 HGNC ID HGNC:24293 Link Image
Enzyme 60 Chromosome Location 5
Enzyme 60 Locus 5q23.3
Enzyme 60 SNPs SNPJam Report Link Image
Enzyme 60 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]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed Link Image]
Enzyme 60 Metabolite References Not Available
Enzyme 61 [top]
Enzyme 61 ID 6393
Enzyme 61 Name Chondroitin sulfate synthase 2
Enzyme 61 Synonyms
  1. Chondroitin glucuronyltransferase 2
  2. Chondroitin-polymerizing factor
  3. ChPF
  4. Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II
  5. N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase II
  6. N-acetylgalactosaminyltransferase 2
Enzyme 61 Gene Name CHPF
Enzyme 61 Protein Sequence >Chondroitin sulfate synthase 2
MRASLLLSVLRPAGPVAVGISLGFTLSLLSVTWVEEPCGPGPPQPGDSELPPRGNTNAAR
RPNSVQPGAEREKPGAGEGAGENWEPRVLPYHPAQPGQAAKKAVRTRYISTELGIRQRLL
VAVLTSQTTLPTLGVAVNRTLGHRLERVVFLTGARGRRAPPGMAVVTLGEERPIGHLHLA
LRHLLEQHGDDFDWFFLVPDTTYTEAHGLARLTGHLSLASAAHLYLGRPQDFIGGEPTPG
RYCHGGFGVLLSRMLLQQLRPHLEGCRNDIVSARPDEWLGRCILDATGVGCTGDHEGVHY
SHLELSPGEPVQEGDPHFRSALTAHPVRDPVHMYQLHKAFARAELERTYQEIQELQWEIQ
NTSHLAVDGDRAAAWPVGIPAPSRPASRFEVLRWDYFTEQHAFSCADGSPRCPLRGADRA
DVADVLGTALEELNRRYHPALRLQKQQLVNGYRRFDPARGMEYTLDLQLEALTPQGGRRP
LTRRVQLLRPLSRVEILPVPYVTEASRLTVLLPLAAAERDLAPGFLEAFATAALEPGDAA
AALTLLLLYEPRQAQRVAHADVFAPVKAHVAELERRFPGARVPWLSVQTAAPSPLRLMDL
LSKKHPLDTLFLLAGPDTVLTPDFLNRCRMHAISGWQAFFPMHFQAFHPAVAPPQGPGPP
ELGRDTGRFDRQAASEACFYNSDYVAARGRLAAASEQEEELLESLDVYELFLHFSSLHVL
RAVEPALLQRYRAQTCSARLSEDLYHRCLQSVLEGLGSRTQLAMLLFEQEQGNST
Enzyme 61 Number of Residues 775
Enzyme 61 Molecular Weight 85494.5
Enzyme 61 Theoretical pI 6.99
Enzyme 61 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • Golgi cisterna membrane
  • Golgi membrane
  • cell part
  • membrane
  • organelle membrane
Enzyme 61 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 61 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 61 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 61 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 [RN:R07336]
Enzyme 61 Pfam Domain Function
Enzyme 61 Signals
  • None
Enzyme 61 Transmembrane Regions
  • 16-34
Enzyme 61 Essentiality Not Available
Enzyme 61 GenBank ID Protein 33456982 Link Image
Enzyme 61 UniProtKB/Swiss-Prot ID Q8IZ52 Link Image
Enzyme 61 UniProtKB/Swiss-Prot Entry Name CHSS2_HUMAN Link Image
Enzyme 61 PDB ID Not Available
Enzyme 61 Cellular Location Not Available
Enzyme 61 Gene Sequence >2328 bp
ATGCGGGCATCGCTGCTGCTGTCGGTGCTGCGGCCCGCAGGGCCCGTGGCCGTGGGCATC
TCCCTGGGCTTCACCCTGAGCCTGCTCAGCGTCACCTGGGTGGAGGAGCCGTGCGGCCCA
GGCCCGCCCCAACCTGGAGACTCTGAGCTGCCGCCGCGCGGCAACACCAACGCGGCGCGC
CGGCCCAACTCGGTGCAGCCCGGAGCGGAGCGCGAGAAGCCCGGGGCCGGCGAAGGCGCC
GGGGAGAATTGGGAGCCGCGCGTCTTGCCCTACCACCCTGCACAGCCCGGCCAGGCCGCC
AAAAAGGCCGTCAGGACCCGCTACATCAGCACGGAGCTGGGCATCAGGCAGAGGCTGCTG
GTGGCGGTGCTGACCTCTCAGACCACGCTGCCCACGCTGGGCGTGGCCGTGAACCGCACG
CTGGGGCACCGGCTGGAGCGTGTGGTGTTCCTGACGGGCGCACGGGGCCGCCGGGCCCCA
CCTGGCATGGCAGTGGTGACGCTAGGCGAGGAGCGACCCATTGGACACCTGCACCTGGCG
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 61 GenBank Gene ID AB086063 Link Image
Enzyme 61 GeneCard ID CHPF Link Image
Enzyme 61 GenAtlas ID CHPF Link Image
Enzyme 61 HGNC ID HGNC:24291 Link Image
Enzyme 61 Chromosome Location 2
Enzyme 61 Locus 2q35
Enzyme 61 SNPs SNPJam Report Link Image
Enzyme 61 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. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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]
  7. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  8. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
Enzyme 61 Metabolite References Not Available
Enzyme 62 [top]
Enzyme 62 ID 6394
Enzyme 62 Name Chondroitin sulfate synthase 1
Enzyme 62 Synonyms
  1. Chondroitin glucuronyltransferase 1
  2. Chondroitin synthase 1
  3. ChSy-1
  4. Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase 1
  5. N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 1
  6. N-acetylgalactosaminyltransferase 1
Enzyme 62 Gene Name CHSY1
Enzyme 62 Protein Sequence >Chondroitin sulfate synthase 1
MAARGRRAWLSVLLGLVLGFVLASRLVLPRASELKRAGPRRRASPEGCRSGQAAASQAGG
ARGDARGAQLWPPGSDPDGGPRDRNFLFVGVMTAQKYLQTRAVAAYRTWSKTIPGKVQFF
SSEGSDTSVPIPVVPLRGVDDSYPPQKKSFMMLKYMHDHYLDKYEWFMRADDDVYIKGDR
LENFLRSLNSSEPLFLGQTGLGTTEEMGKLALEPGENFCMGGPGVIMSREVLRRMVPHIG
KCLREMYTTHEDVEVGRCVRRFAGVQCVWSYEMQQLFYENYEQNKKGYIRDLHNSKIHQA
ITLHPNKNPPYQYRLHSYMLSRKISELRHRTIQLHREIVLMSKYSNTEIHKEDLQLGIPP
SFMRFQPRQREEILEWEFLTGKYLYSAVDGQPPRRGMDSAQREALDDIVMQVMEMINANA
KTRGRIIDFKEIQYGYRRVNPMYGAEYILDLLLLYKKHKGKKMTVPVRRHAYLQQTFSKI
QFVEHEELDAQELAKRINQESGSLSFLSNSLKKLVPFQLPGSKSEHKEPKDKKINILIPL
SGRFDMFVRFMGNFEKTCLIPNQNVKLVVLLFNSDSNPDKAKQVELMRDYRIKYPKADMQ
ILPVSGEFSRALALEVGSSQFNNESLLFFCDVDLVFTTEFLQRCRANTVLGQQIYFPIIF
SQYDPKIVYSGKVPSDNHFAFTQKTGFWRNYGFGITCIYKGDLVRVGGFDVSIQGWGLED
VDLFNKVVQAGLKTFRSQEVGVVHVHHPVFCDPNLDPKQYKMCLGSKASTYGSTQQLAEM
WLEKNDPSYSKSSNNNGSVRTA
Enzyme 62 Number of Residues 802
Enzyme 62 Molecular Weight 91783.8
Enzyme 62 Theoretical pI 9.63
Enzyme 62 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • Golgi cisterna membrane
  • Golgi membrane
  • cell part
  • membrane
  • organelle membrane
Enzyme 62 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 62 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 62 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 62 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 [RN:R07336]
Enzyme 62 Pfam Domain Function
Enzyme 62 Signals
  • None
Enzyme 62 Transmembrane Regions
  • 8-28
Enzyme 62 Essentiality Not Available
Enzyme 62 GenBank ID Protein 31542309 Link Image
Enzyme 62 UniProtKB/Swiss-Prot ID Q86X52 Link Image
Enzyme 62 UniProtKB/Swiss-Prot Entry Name CHSS1_HUMAN Link Image
Enzyme 62 PDB ID Not Available
Enzyme 62 Cellular Location Not Available
Enzyme 62 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
GCCAAACAAGTTGAACTGATGAGAGATTACCGCATTAAGTACCCTAAAGCCGACATGCAG
ATTTTGCCTGTGTCTGGAGAGTTTTCAAGAGCCCTGGCCCTGGAAGTAGGATCCTCCCAG
TTTAACAATGAATCTTTGCTCTTCTTCTGCGACGTCGACCTCGTGTTTACTACAGAATTC
CTTCAGCGATGTCGAGCAAATACAGTTCTGGGCCAACAAATATATTTTCCAATCATCTTC
AGCCAGTATGACCCAAAGATTGTTTATAGTGGGAAAGTTCCCAGTGACAACCATTTTGCC
TTTACTCAGAAAACTGGCTTCTGGAGAAACTATGGGTTTGGCATCACGTGTATTTATAAG
GGAGATCTTGTCCGAGTGGGTGGCTTTGATGTTTCCATCCAAGGCTGGGGGCTGGAGGAT
GTGGACCTTTTCAACAAGGTTGTCCAGGCAGGTTTGAAGACGTTTAGGAGCCAGGAAGTA
GGAGTAGTCCACGTCCACCATCCTGTCTTTTGTGATCCCAATCTTGACCCCAAACAGTAC
AAAATGTGCTTGGGGTCCAAAGCATCGACCTATGGGTCCACCCAGCAGCTGGCTGAGATG
TGGCTGGAAAAAAATGATCCAAGTTACAGTAAAAGCAGCAATAATAATGGCTCAGTGAGG
ACAGCCTAA
Enzyme 62 GenBank Gene ID NM_014918.4 Link Image
Enzyme 62 GeneCard ID CHSY1 Link Image
Enzyme 62 GenAtlas ID CHSY1 Link Image
Enzyme 62 HGNC ID HGNC:17198 Link Image
Enzyme 62 Chromosome Location 1
Enzyme 62 Locus 15q26.3
Enzyme 62 SNPs SNPJam Report Link Image
Enzyme 62 General References
  1. Kitagawa H, Uyama T, Sugahara K: Molecular cloning and expression of a human chondroitin synthase. J Biol Chem. 2001 Oct 19;276(42):38721-6. Epub 2001 Aug 20. [PubMed Link Image]
  2. 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]
  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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. 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]
  6. 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 62 Metabolite References Not Available
Enzyme 63 [top]
Enzyme 63 ID 6586
Enzyme 63 Name Polyribonucleotide nucleotidyltransferase 1, mitochondrial
Enzyme 63 Synonyms
  1. 3'-5' RNA exonuclease OLD35
  2. PNPase old-35
  3. Polynucleotide phosphorylase 1
  4. PNPase 1
  5. Polynucleotide phosphorylase-like protein
Enzyme 63 Gene Name PNPT1
Enzyme 63 Protein Sequence >Polyribonucleotide nucleotidyltransferase 1, mitochondrial
MAACRYCCSCLRLRPLSDGPFLLPRRDRALTQLQVRALWSSAGSRAVAVDLGNRKLEISS
GKLARFADGSAVVQSGDTAVMVTAVSKTKPSPSQFMPLVVDYRQKAAAAGRIPTNYLRRE
IGTSDKEILTSRIIDRSIRPLFPAGYFYDTQVLCNLLAVDGVNEPDVLAINGASVALSLS
DIPWNGPVGAVRIGIIDGEYVVNPTRKEMSSSTLNLVVAGAPKSQIVMLEASAENILQQD
FCHAIKVGVKYTQQIIQGIQQLVKETGVTKRTPQKLFTPSPEIVKYTHKLAMERLYAVFT
DYEHDKVSRDEAVNKIRLDTEEQLKEKFPEADPYEIIESFNVVAKEVFRSIVLNEYKRCD
GRDLTSLRNVSCEVDMFKTLHGSALFQRGQTQVLCTVTFDSLESGIKSDQVITAINGIKD
KNFMLHYEFPPYATNEIGKVTGLNRRELGHGALAEKALYPVIPRDFPFTIRVTSEVLESN
GSSSMASACGGSLALMDSGVPISSAVAGVAIGLVTKTDPEKGEIEDYRLLTDILGIEDYN
GDMDFKIAGTNKGITALQADIKLPGIPIKIVMEAIQQASVAKKEILQIMNKTISKPRASR
KENGPVVETVQVPLSKRAKFVGPGGYNLKKLQAETGVTISQVDEETFSVFAPTPSAMHEA
RDFITEICKDDQEQQLEFGAVYTATITEIRDTGVMVKLYPNMTAVLLHNTQLDQRKIKHP
TALGLEVGQEIQVKYFGRDPADGRMRLSRKVLQSPATTVVRTLNDRSSIVMGEPISQSSS
NSQ
Enzyme 63 Number of Residues 783
Enzyme 63 Molecular Weight 85949.8
Enzyme 63 Theoretical pI 7.86
Enzyme 63 GO Classification
Function
  • 3'-5' exonuclease activity
  • 3'-5'-exoribonuclease activity
  • RNA binding
  • binding
  • catalytic activity
  • exonuclease activity
  • hydrolase activity
  • hydrolase activity, acting on ester bonds
  • nuclease activity
  • nucleic acid binding
  • nucleotidyltransferase activity
  • polyribonucleotide nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • RNA catabolic process
  • RNA metabolic process
  • RNA processing
  • cellular macromolecule metabolic process
  • mRNA catabolic process
  • macromolecule metabolic process
  • metabolic process
Component
  • intracellular membrane-bounded organelle
  • membrane-bounded organelle
  • mitochondrion
  • organelle
Enzyme 63 General Function Involved in 3'-5'-exoribonuclease activity
Enzyme 63 Specific Function Involved in mRNA degradation. Hydrolyzes single-stranded polyribonucleotides processively in the 3'- to 5'-direction
Enzyme 63 Pathways
Enzyme 63 Reactions
  • RNAn+1 + phosphate = RNAn + a nucleoside diphosphate [RN:R07282]
Enzyme 63 Pfam Domain Function
Enzyme 63 Signals
  • None
Enzyme 63 Transmembrane Regions
  • None
Enzyme 63 Essentiality Not Available
Enzyme 63 GenBank ID Protein 62988884 Link Image
Enzyme 63 UniProtKB/Swiss-Prot ID Q8TCS8 Link Image
Enzyme 63 UniProtKB/Swiss-Prot Entry Name PNPT1_HUMAN Link Image
Enzyme 63 PDB ID Not Available
Enzyme 63 Cellular Location Not Available
Enzyme 63 Gene Sequence >2352 bp
ATGGCGGCCTGCAGGTACTGCTGCTCGTGCCTCCGGCTCCGGCCCCTGAGCGATGGTCCT
TTCCTTCTGCCACGGCGGGATCGGGCACTCACCCAGTTGCAAGTGCGAGCACTATGGAGT
AGCGCAGGGTCTCGAGCTGTGGCCGTGGACTTAGGCAACAGGAAATTAGAAATATCTTCT
GGAAAGCTGGCCAGATTTGCAGATGGCTCTGCTGTAGTACAGTCAGGTGACACTGCAGTA
ATGGTCACAGCGGTCAGTAAAACAAAACCTTCCCCTTCCCAGTTTATGCCTTTGGTGGTT
GACTACAGACAAAAAGCTGCTGCAGCAGGTAGAATTCCCACAAACTATCTGAGAAGAGAG
ATTGGTACTTCTGATAAAGAAATTCTAACAAGTCGAATAATAGATCGTTCAATTAGACCG
CTCTTTCCAGCTGGCTACTTCTATGATACACAGGTTCTGTGTAATCTGTTAGCAGTAGAT
GGTGTAAATGAGCCTGATGTCCTAGCAATTAATGGCGCTTCCGTAGCCCTCTCATTATCA
GATATTCCTTGGAATGGACCTGTTGGGGCAGTACGAATAGGAATAATTGATGGAGAATAT
GTTGTTAACCCAACAAGAAAAGAAATGTCTTCTAGTACTTTAAATTTAGTGGTTGCTGGA
GCACCTAAAAGTCAGATTGTCATGTTGGAAGCCTCTGCAGAGAACATTTTACAGCAGGAC
TTTTGCCATGCTATCAAAGTGGGAGTGAAATATACCCAACAAATAATTCAGGGCATTCAG
CAGTTGGTAAAAGAAACTGGTGTTACCAAGAGGACACCTCAGAAGTTATTTACCCCTTCG
CCAGAGATTGTGAAATATACTCATAAACTTGCTATGGAGAGACTCTATGCAGTTTTTACA
GATTACGAGCATGACAAAGTTTCCAGAGATGAAGCTGTTAACAAAATAAGATTAGATACG
GAGGAACAACTAAAAGAAAAATTTCCAGAAGCCGATCCATATGAAATAATAGAATCCTTC
AATGTTGTTGCAAAGGAAGTTTTTAGAAGTATTGTTTTGAATGAATACAAAAGGTGCGAT
GGTCGGGATTTGACTTCACTTAGGAATGTAAGTTGTGAGGTAGATATGTTTAAAACCCTT
CATGGATCAGCATTATTTCAAAGAGGACAAACACAGGTGCTTTGTACCGTTACATTTGAT
TCATTAGAATCTGGTATTAAGTCAGATCAAGTTATAACAGCTATAAATGGGATAAAAGAT
AAAAATTTCATGCTGCACTACGAGTTTCCTCCTTATGCAACTAATGAAATTGGCAAAGTC
ACTGGTTTAAATAGAAGAGAACTTGGGCATGGTGCTCTTGCTGAGAAAGCTTTGTATCCT
GTTATTCCCCGAGATTTTCCTTTCACCATAAGAGTTACATCTGAAGTCCTAGAGTCAAAT
GGGTCATCTTCTATGGCATCTGCATGTGGCGGAAGTTTAGCATTAATGGATTCAGGGGTT
CCAATTTCATCTGCTGTTGCAGGCGTAGCAATAGGATTGGTCACCAAAACCGATCCTGAG
AAGGGTGAAATAGAAGATTATCGTTTGCTGACAGATATTTTGGGAATTGAAGATTACAAT
GGTGACATGGACTTCAAAATAGCTGGCACTAATAAAGGAATAACTGCATTACAGGCTGAT
ATTAAATTACCTGGAATACCAATAAAAATTGTGATGGAGGCTATTCAACAAGCTTCAGTG
GCAAAAAAGGAGATATTACAGATCATGAACAAAACTATTTCAAAACCTCGAGCATCTAGA
AAAGAAAATGGACCTGTTGTAGAAACTGTTCAGGTTCCATTATCAAAACGAGCAAAATTT
GTTGGACCTGGTGGCTATAACTTAAAAAAACTTCAGGCTGAAACAGGTGTAACTATTAGT
CAGGTGGATGAAGAAACGTTTTCTGTATTTGCACCAACACCCAGTGCTATGCATGAGGCA
AGAGACTTCATTACTGAAATCTGCAAGGATGATCAGGAGCAGCAATTAGAATTTGGAGCA
GTATATACCGCCACAATAACTGAAATCAGAGATACTGGTGTAATGGTAAAATTATATCCA
AATATGACTGCGGTACTGCTTCATAACACACAACTTGATCAACGAAAGATTAAACATCCT
ACTGCCCTAGGATTAGAAGTTGGCCAAGAAATTCAGGTGAAATACTTTGGACGTGACCCA
GCCGATGGAAGAATGAGGCTTTCTCGAAAAGTGCTTCAGTCGCCAGCTACAACCGTGGTC
AGAACTTTGAATGACAGAAGTAGTATTGTAATGGGAGAACCTATTTCACAGTCATCATCT
AATTCTCAGTGA
Enzyme 63 GenBank Gene ID AC015982 Link Image
Enzyme 63 GeneCard ID PNPT1 Link Image
Enzyme 63 GenAtlas ID PNPT1 Link Image
Enzyme 63 HGNC ID HGNC:23166 Link Image
Enzyme 63 Chromosome Location 2
Enzyme 63 Locus 2p15
Enzyme 63 SNPs SNPJam Report Link Image
Enzyme 63 General References
  1. Raijmakers R, Egberts WV, van Venrooij WJ, Pruijn GJ: Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring. J Mol Biol. 2002 Nov 1;323(4):653-63. [PubMed Link Image]
  2. Leszczyniecka M, Kang DC, Sarkar D, Su ZZ, Holmes M, Valerie K, Fisher PB: Identification and cloning of human polynucleotide phosphorylase, hPNPase old-35, in the context of terminal differentiation and cellular senescence. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16636-41. Epub 2002 Dec 9. [PubMed Link Image]
  3. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  6. Piwowarski J, Grzechnik P, Dziembowski A, Dmochowska A, Minczuk M, Stepien PP: Human polynucleotide phosphorylase, hPNPase, is localized in mitochondria. J Mol Biol. 2003 Jun 20;329(5):853-7. [PubMed Link Image]
  7. French SW, Dawson DW, Chen HW, Rainey RN, Sievers SA, Balatoni CE, Wong L, Troke JJ, Nguyen MT, Koehler CM, Teitell MA: The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity. Cancer Lett. 2007 Apr 18;248(2):198-210. Epub 2006 Aug 28. [PubMed Link Image]
  8. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed Link Image]
  9. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed Link Image]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  11. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed Link Image]
Enzyme 63 Metabolite References Not Available
Enzyme 64 [top]
Enzyme 64 ID 6932
Enzyme 64 Name Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
Enzyme 64 Synonyms
  1. Beta-1,2-N-acetylglucosaminyltransferase II
  2. GlcNAc-T II
  3. GNT-II
  4. Mannoside acetylglucosaminyltransferase 2
  5. N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II
Enzyme 64 Gene Name MGAT2
Enzyme 64 Protein Sequence >Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
MRFRIYKRKVLILTLVVAACGFVLWSSNGRQRKNEALAPPLLDAEPARGAGGRGGDHPSV
AVGIRRVSNVSAASLVPAVPQPEADNLTLRYRSLVYQLNFDQTLRNVDKAGTWAPRELVL
VVQVHNRPEYLRLLLDSLRKAQGIDNVLVIFSHDFWSTEINQLIAGVNFCPVLQVFFPFS
IQLYPNEFPGSDPRDCPRDLPKNAALKLGCINAEYPDSFGHYREAKFSQTKHHWWWKLHF
VWERVKILRDYAGLILFLEEDHYLAPDFYHVFKKMWKLKQQECPECDVLSLGTYSASRSF
YGMADKVDVKTWKSTEHNMGLALTRNAYQKLIECTDTFCTYDDYNWDWTLQYLTVSCLPK
FWKVLVPQIPRIFHAGDCGMHHKKTCRPSTQSAQIESLLNNNKQYMFPETLTISEKFTVV
AISPPRKNGGWGDIRDHELCKSYRRLQ
Enzyme 64 Number of Residues 447
Enzyme 64 Molecular Weight 51549.8
Enzyme 64 Theoretical pI 8.94
Enzyme 64 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • oligosaccharide biosynthetic process
  • oligosaccharide metabolic process
  • primary metabolic process
Component
  • Golgi apparatus part
  • Golgi stack
  • cell part
  • cytoplasmic part
  • integral to membrane
  • intracellular part
  • intrinsic to membrane
  • membrane part
Enzyme 64 General Function Involved in alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity
Enzyme 64 Specific Function Catalyzes an essential step in the conversion of oligo- mannose to complex N-glycans
Enzyme 64 Pathways
Enzyme 64 Reactions
  • UDP-N-acetyl-D-glucosamine + 6-(alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D- mannosyl-R [RN:R07258]
Enzyme 64 Pfam Domain Function
Enzyme 64 Signals
  • None
Enzyme 64 Transmembrane Regions
  • 10-29
Enzyme 64 Essentiality Not Available
Enzyme 64 GenBank ID Protein 193786354 Link Image
Enzyme 64 UniProtKB/Swiss-Prot ID Q10469 Link Image
Enzyme 64 UniProtKB/Swiss-Prot Entry Name MGAT2_HUMAN Link Image
Enzyme 64 PDB ID Not Available
Enzyme 64 Cellular Location Not Available
Enzyme 64 Gene Sequence >1344 bp
ATGAGGTTCCGCATCTACAAACGGAAGGTGCTAATCCTGACGCTCGTGGTGGCCGCCTGC
GGCTTCGTCCTCTGGAGCAGCAATGGGCGACAAAGGAAGAACGAGGCCCTCGCCCCACCG
TTGCTGGACGCCGAACCCGCGCGGGGTGCCGGCGGCCGCGGTGGGGACCACCCCTCTGTG
GCTGTGGGCATCCGCAGGGTCTCCAACGTGTCGGCGGCTTCCCTGGTCCCGGCGGTCCCC
CAGCCCGAGGCGGACAACCTGACGCTGCGGTACCGGTCCCTGGTGTACCAGCTGAACTTT
GATCAGACCCTGAGGAATGTAGATAAGGCTGGCACCTGGGCCCCCCGGGAGCTGGTGCTG
GTGGTCCAGGTGCATAACCGGCCCGAATACCTCAGACTGCTGCTGGACTCACTTCGAAAA
GCCCAGGGAATTGACAACGTCCTCGTCATCTTTAGCCATGACTTCTGGTCGACCGAGATC
AATCAGCTGATCGCCGGGGTGAATTTCTGTCCGGTTCTGCAGGTGTTCTTTCCTTTCAGC
ATTCAGTTGTACCCTAACGAGTTTCCAGGTAGTGACCCTAGAGATTGTCCCAGAGACCTG
CCGAAGAATGCCGCTTTGAAATTGGGGTGCATCAATGCTGAGTATCCCGACTCCTTCGGC
CATTATAGAGAGGCCAAATTCTCCCAGACCAAACATCACTGGTGGTGGAAGCTGCATTTT
GTGTGGGAAAGAGTGAAAATTCTTCGAGATTATGCTGGCCTTATACTTTTCCTAGAAGAG
GATCACTACTTAGCCCCAGACTTTTACCATGTCTTCAAAAAGATGTGGAAACTGAAGCAG
CAAGAGTGCCCTGAATGTGATGTTCTCTCCCTGGGGACCTATAGTGCCAGTCGCAGTTTC
TATGGCATGGCTGACAAGGTAGATGTGAAAACTTGGAAATCCACAGAGCACAATATGGGT
CTAGCCTTGACCCGGAATGCCTATCAGAAGCTGATCGAGTGCACAGACACTTTCTGTACT
TATGATGATTATAACTGGGACTGGACTCTTCAATACTTGACTGTATCTTGTCTTCCAAAA
TTCTGGAAAGTGCTGGTTCCTCAAATTCCTAGGATCTTTCATGCTGGAGACTGTGGTATG
CATCACAAGAAAACCTGTAGACCATCCACTCAGAGTGCCCAAATTGAGTCACTCTTAAAT
AATAACAAACAATACATGTTTCCAGAAACTCTAACTATCAGTGAAAAGTTTACTGTGGTA
GCCATTTCCCCACCTAGAAAAAATGGAGGGTGGGGAGATATTAGGGACCATGAACTCTGT
AAAAGTTATAGAAGACTGCAGTGA
Enzyme 64 GenBank Gene ID AK056167 Link Image
Enzyme 64 GeneCard ID MGAT2 Link Image
Enzyme 64 GenAtlas ID MGAT2 Link Image
Enzyme 64 HGNC ID HGNC:7045 Link Image
Enzyme 64 Chromosome Location 1
Enzyme 64 Locus 14q21
Enzyme 64 SNPs SNPJam Report Link Image
Enzyme 64 General References
  1. Tan J, D'Agostaro AF, Bendiak B, Reck F, Sarkar M, Squire JA, Leong P, Schachter H: The human UDP-N-acetylglucosamine: alpha-6-D-mannoside-beta-1,2- N-acetylglucosaminyltransferase II gene (MGAT2). Cloning of genomic DNA, localization to chromosome 14q21, expression in insect cells and purification of the recombinant protein. Eur J Biochem. 1995 Jul 15;231(2):317-28. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Tan J, Dunn J, Jaeken J, Schachter H: Mutations in the MGAT2 gene controlling complex N-glycan synthesis cause carbohydrate-deficient glycoprotein syndrome type II, an autosomal recessive disease with defective brain development. Am J Hum Genet. 1996 Oct;59(4):810-7. [PubMed Link Image]
  5. Cormier-Daire V, Amiel J, Vuillaumier-Barrot S, Tan J, Durand G, Munnich A, Le Merrer M, Seta N: Congenital disorders of glycosylation IIa cause growth retardation, mental retardation, and facial dysmorphism. J Med Genet. 2000 Nov;37(11):875-7. [PubMed Link Image]
Enzyme 64 Metabolite References Not Available
Enzyme 65 [top]
Enzyme 65 ID 7037
Enzyme 65 Name Exostosin-1
Enzyme 65 Synonyms
  1. Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
  2. Multiple exostoses protein 1
  3. Putative tumor suppressor protein EXT1
Enzyme 65 Gene Name EXT1
Enzyme 65 Protein Sequence >Exostosin-1
MQAKKRYFILLSAGSCLALLFYFGGLQFRASRSHSRREEHSGRNGLHHPSPDHFWPRFPD
ALRPFVPWDQLENEDSSVHISPRQKRDANSSIYKGKKCRMESCFDFTLCKKNGFKVYVYP
QQKGEKIAESYQNILAAIEGSRFYTSDPSQACLFVLSLDTLDRDQLSPQYVHNLRSKVQS
LHLWNNGRNHLIFNLYSGTWPDYTEDVGFDIGQAMLAKASISTENFRPNFDVSIPLFSKD
HPRTGGERGFLKFNTIPPLRKYMLVFKGKRYLTGIGSDTRNALYHVHNGEDVVLLTTCKH
GKDWQKHKDSRCDRDNTEYEKYDYREMLHNATFCLVPRGRRLGSFRFLEALQAACVPVML
SNGWELPFSEVINWNQAAVIGDERLLLQIPSTIRSIHQDKILALRQQTQFLWEAYFSSVE
KIVLTTLEIIQDRIFKHISRNSLIWNKHPGGLFVLPQYSSYLGDFPYYYANLGLKPPSKF
TAVIHAVTPLVSQSQPVLKLLVAAAKSQYCAQIIVLWNCDKPLPAKHRWPATAVPVVVIE
GESKVMSSRFLPYDNIITDAVLSLDEDTVLSTTEVDFAFTVWQSFPERIVGYPARSHFWD
NSKERWGYTSKWTNDYSMVLTGAAIYHKYYHYLYSHYLPASLKNMVDQLANCEDILMNFL
VSAVTKLPPIKVTQKKQYKETMMGQTSRASRWADPDHFAQRQSCMNTFASWFGYMPLIHS
QMRLDPVLFKDQVSILRKKYRDIERL
Enzyme 65 Number of Residues 746
Enzyme 65 Molecular Weight 86254.0
Enzyme 65 Theoretical pI 9.34
Enzyme 65 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
  • membrane part
Enzyme 65 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 65 Specific Function Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor
Enzyme 65 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 65 Reactions
  • UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl- proteoglycan = UDP + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)- beta-D-glucuronosyl-proteoglycan [RN:R07335]
Enzyme 65 Pfam Domain Function
Enzyme 65 Signals
  • None
Enzyme 65 Transmembrane Regions
  • 8-28
Enzyme 65 Essentiality Not Available
Enzyme 65 GenBank ID Protein 1168162 Link Image
Enzyme 65 UniProtKB/Swiss-Prot ID Q16394 Link Image
Enzyme 65 UniProtKB/Swiss-Prot Entry Name EXT1_HUMAN Link Image
Enzyme 65 PDB ID Not Available
Enzyme 65 Cellular Location Not Available
Enzyme 65 Gene Sequence >2241 bp
ATGCAGGCCAAAAAACGCTATTTCATCCTGCTCTCAGCTGGCTCTTGTCTCGCCCTTTTG
TTTTATTTCGGAGGCTTGCAGTTTAGGGCATCGAGGAGCCACAGCCGGAGAGAAGAACAC
AGCGGTAGGAATGGCTTGCACCACCCCAGTCCGGATCATTTCTGGCCCCGCTTCCCGGAG
CCTCTGCGCCCCTTCGTTCCTTGGGATCAATTGGAAAACGAGGATTCCAGCGTGCACATT
TCCCCCCGGCAGAAGCGAGATGCCAACTCCAGCATCTACAAAGGCAAGAAGTGCCGCATG
GAGTCCTGCTTCGATTTCACCCTTTGCAAGAAAAACGGCTTCAAAGTCTACGTATACCCA
CAGCAAAAAGGGGAGAAAATCGCCGAAAGTTACCAAAACATTCTAGCGGCCATCGAGGGC
TCCAGGTTCTACACCTCGGACCCCAGCCAGGCGTGCCTCTTTGTCCTGAGTCTGGATACT
TTAGACAGAGACCAGTTGTCACCTCAGTATGTGCACAATTTGAGATCCAAAGTGCAGAGT
CTCCACTTGTGGAACAATGGTAGGAATCATTTAATTTTTAATTTATATTCCGGCACTTGG
CCTGACTACACCGAGGACGTGGGGTTTGACATCGGCCAGGCGATGCTGGCCAAAGCCAGC
ATCAGTACTGAAAACTTCCGACCCAACTTTGATGTTTCTATTCCCCTCTTTTCTAAGGAT
CATCCCAGGACAGGAGGGGAGAGGGGGTTTTTGAAGTTCAACACCATCCCTCCTCTCAGG
AAGTACATGCTGGTATTCAAGGGGAAGAGGTACCTGACAGGGATAGGATCAGACACCAGG
AATGCCTTATATCACGTCCATAACGGGGAGGACGTTGTGCTCCTCACCACCTGCAAGCAT
GGCAAAGACTGGCAAAAGCACAAGGATTCTCGCTGTGACAGAGACAACACCGAGTATGAG
AAGTATGATTATCGGGAAATGCTGCACAATGCCACTTTCTGTCTGGTTCCTCGTGGTCGC
AGGCTTGGGTCCTTCAGATTCCTGGAGGCTTTGCAGGCTGCCTGCGTCCCTGTGATGCTC
AGCAATGGATGGGAGTTGCCATTCTCTGAAGTGATTAATTGGAACCAAGCTGCCGTCATA
GGCGATGAGAGATTGTTATTACAGATTCCTTCTACAATCAGGTCTATTCATCAGGATAAA
ATCCTAGCACTTAGACAGCAGACACAATTCTTGTGGGAGGCTTATTTTTCTTCAGTTGAG
AAGATTGTATTAACTACACTAGAGATTATTCAGGACAGAATATTCAAGCACATATCACGT
AACAGTTTAATATGGAACAAACATCCTGGAGGATTGTTCGTACTACCACAGTATTCATCT
TATCTGGGAGATTTTCCTTACTACTATGCTAATTTAGGTTTAAAGCCCCCCTCCAAATTC
ACTGCAGTCATCCATGCGGTGACCCCCCTGGTCTCTCAGTCCCAGCCAGTGTTGAAGCTT
CTCGTGGCTGCAGCCAAGTCCCAGTACTGTGCCCAGATCATAGTTCTATGGAATTGTGAC
AAGCCCCTACCAGCCAAACACCGCTGGCCTGCCACTGCTGTGCCTGTCGTCGTCATTGAA
GGAGAGAGCAAGGTTATGAGCAGCCGTTTTCTGCCCTACGACAACATCATCACAGACGCC
GTGCTCAGCCTTGACGAGGACACGGTGCTTTCAACAACAGAGGTGGATTTCGCCTTCACA
GTGTGGCAGAGCTTCCCTGAGAGGATTGTGGGGTACCCCGCGCGCAGCCACTTCTGGGAT
AACTCTAAGGAGCGGTGGGGATACACATCAAAGTGGACGAACGACTACTCCATGGTGTTG
ACAGGAGCTGCTATTTACCACAAATATTATCACTACCTATACTCCCATTACCTGCCAGCC
AGCCTGAAGAACATGGTGGACCAATTGGCCAATTGTGAGGACATTCTCATGAACTTCCTG
GTGTCTGCTGTGACAAAATTGCCTCCAATCAAAGTGACCCAGAAGAAGCAGTATAAGGAG
ACAATGATGGGACAGACTTCTCGGGCTTCCCGTTGGGCTGACCCTGACCACTTTGCCCAG
CGACAGAGCTGCATGAATACGTTTGCCAGCTGGTTTGGCTACATGCCGCTGATCCACTCT
CAGATGAGGCTCGACCCCGTCCTCTTTAAAGACCAGGTCTCTATTTTGAGGAAGAAATAC
CGAGACATTGAGCGACTTTGA
Enzyme 65 GenBank Gene ID S79639 Link Image
Enzyme 65 GeneCard ID EXT1 Link Image
Enzyme 65 GenAtlas ID EXT1 Link Image
Enzyme 65 HGNC ID HGNC:3512 Link Image
Enzyme 65 Chromosome Location 8
Enzyme 65 Locus 8q24.11
Enzyme 65 SNPs SNPJam Report Link Image
Enzyme 65 General References
  1. Ahn J, Ludecke HJ, Lindow S, Horton WA, Lee B, Wagner MJ, Horsthemke B, Wells DE: Cloning of the putative tumour suppressor gene for hereditary multiple exostoses (EXT1). Nat Genet. 1995 Oct;11(2):137-43. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ludecke HJ, Ahn J, Lin X, Hill A, Wagner MJ, Schomburg L, Horsthemke B, Wells DE: Genomic organization and promoter structure of the human EXT1 gene. Genomics. 1997 Mar 1;40(2):351-4. [PubMed Link Image]
  5. Kobayashi S, Morimoto K, Shimizu T, Takahashi M, Kurosawa H, Shirasawa T: Association of EXT1 and EXT2, hereditary multiple exostoses gene products, in Golgi apparatus. Biochem Biophys Res Commun. 2000 Feb 24;268(3):860-7. [PubMed Link Image]
  6. Duncan G, McCormick C, Tufaro F: The link between heparan sulfate and hereditary bone disease: finding a function for the EXT family of putative tumor suppressor proteins. J Clin Invest. 2001 Aug;108(4):511-6. [PubMed Link Image]
  7. Wuyts W, Van Hul W: Molecular basis of multiple exostoses: mutations in the EXT1 and EXT2 genes. Hum Mutat. 2000;15(3):220-7. [PubMed Link Image]
  8. Hecht JT, Hogue D, Wang Y, Blanton SH, Wagner M, Strong LC, Raskind W, Hansen MF, Wells D: Hereditary multiple exostoses (EXT): mutational studies of familial EXT1 cases and EXT-associated malignancies. Am J Hum Genet. 1997 Jan;60(1):80-6. [PubMed Link Image]
  9. Philippe C, Porter DE, Emerton ME, Wells DE, Simpson AH, Monaco AP: Mutation screening of the EXT1 and EXT2 genes in patients with hereditary multiple exostoses. Am J Hum Genet. 1997 Sep;61(3):520-8. [PubMed Link Image]
  10. Wuyts W, Van Hul W, De Boulle K, Hendrickx J, Bakker E, Vanhoenacker F, Mollica F, Ludecke HJ, Sayli BS, Pazzaglia UE, Mortier G, Hamel B, Conrad EU, Matsushita M, Raskind WH, Willems PJ: Mutations in the EXT1 and EXT2 genes in hereditary multiple exostoses. Am J Hum Genet. 1998 Feb;62(2):346-54. [PubMed Link Image]
  11. Raskind WH, Conrad EU 3rd, Matsushita M, Wijsman EM, Wells DE, Chapman N, Sandell LJ, Wagner M, Houck J: Evaluation of locus heterogeneity and EXT1 mutations in 34 families with hereditary multiple exostoses. Hum Mutat. 1998;11(3):231-9. [PubMed Link Image]
  12. Bovee JV, Cleton-Jansen AM, Wuyts W, Caethoven G, Taminiau AH, Bakker E, Van Hul W, Cornelisse CJ, Hogendoorn PC: EXT-mutation analysis and loss of heterozygosity in sporadic and hereditary osteochondromas and secondary chondrosarcomas. Am J Hum Genet. 1999 Sep;65(3):689-98. [PubMed Link Image]
  13. Xu L, Xia J, Jiang H, Zhou J, Li H, Wang D, Pan Q, Long Z, Fan C, Deng HX: Mutation analysis of hereditary multiple exostoses in the Chinese. Hum Genet. 1999 Jul-Aug;105(1-2):45-50. [PubMed Link Image]
  14. Bernard MA, Hall CE, Hogue DA, Cole WG, Scott A, Snuggs MB, Clines GA, Ludecke HJ, Lovett M, Van Winkle WB, Hecht JT: Diminished levels of the putative tumor suppressor proteins EXT1 and EXT2 in exostosis chondrocytes. Cell Motil Cytoskeleton. 2001 Feb;48(2):149-62. [PubMed Link Image]
  15. Cheung PK, McCormick C, Crawford BE, Esko JD, Tufaro F, Duncan G: Etiological point mutations in the hereditary multiple exostoses gene EXT1: a functional analysis of heparan sulfate polymerase activity. Am J Hum Genet. 2001 Jul;69(1):55-66. Epub 2001 Jun 5. [PubMed Link Image]
Enzyme 65 Metabolite References Not Available
Enzyme 66 [top]
Enzyme 66 ID 7038
Enzyme 66 Name Hyaluronan synthase 1
Enzyme 66 Synonyms
  1. Hyaluronate synthase 1
  2. Hyaluronic acid synthase 1
  3. HA synthase 1
  4. HuHAS1
Enzyme 66 Gene Name HAS1
Enzyme 66 Protein Sequence >Hyaluronan synthase 1
MRQQDAPKPTPAACRCSGLARRVLTIAFALLILGLMTWAYAAGVPLASDRYGLLAFGLYG
AFLSAHLVAQSLFAYLEHRRVAAAARGPLDAATARSVALTISAYQEDPAYLRQCLASARA
LLYPRARLRVLMVVDGNRAEDLYMVDMFREVFADEDPATYVWDGNYHQPWEPAAAGAVGA
GAYREVEAEDPGRLAVEALVRTRRCVCVAQRWGGKREVMYTAFKALGDSVDYVQVCDSDT
RLDPMALLELVRVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFH
CVSCISGPLGLYRNNLLQQFLEAWYNQKFLGTHCTFGDDRHLTNRMLSMGYATKYTSRSR
CYSETPSSFLRWLSQQTRWSKSYFREWLYNALWWHRHHAWMTYEAVVSGLFPFFVAATVL
RLFYAGRPWALLWVLLCVQGVALAKAAFAAWLRGCLRMVLLSLYAPLYMCGLLPAKFLAL
VTMNQSGWGTSGRRKLAANYVPLLPLALWALLLLGGLVRSVAHEARADWSGPSRAAEAYH
LAAGAGAYVGYWVAMLTLYWVGVRRLCRRRTGGYRVQV
Enzyme 66 Number of Residues 578
Enzyme 66 Molecular Weight 64831.4
Enzyme 66 Theoretical pI 9.34
Enzyme 66 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
Enzyme 66 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 66 Specific Function Plays a role in hyaluronan/hyaluronic acid (HA) synthesis. Also able to catalyze the synthesis of chito- oligosaccharide depending on the substrate
Enzyme 66 Pathways Not Available
Enzyme 66 Reactions
  • (1) UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)- [nascent hyaluronan] = UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N- acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan] [RN:R05327 R06068]
  • (2) UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)- [nascent hyaluronan] = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta- D-glucuronosyl-(1->3)-[nascent hyaluronan]
Enzyme 66 Pfam Domain Function
Enzyme 66 Signals
  • None
Enzyme 66 Transmembrane Regions
  • 26-46 53-73 400-420 431-451 458-478 498-518 541-561
Enzyme 66 Essentiality Not Available
Enzyme 66 GenBank ID Protein 9454519 Link Image
Enzyme 66 UniProtKB/Swiss-Prot ID Q92839 Link Image
Enzyme 66 UniProtKB/Swiss-Prot Entry Name HAS1_HUMAN Link Image
Enzyme 66 PDB ID Not Available
Enzyme 66 Cellular Location Not Available
Enzyme 66 Gene Sequence >1737 bp
ATGAGACAGCAGGACGCGCCCAAGCCCACTCCTGCAGCCTGCCGCTGCTCCGGCCTGGCC
CGGAGGGTGCTGACCATCGCCTTCGCCCTGCTCATCCTGGGCCTCATGACCTGGGCCTAC
GCCGCCGGGGTGCCGCTGGCCTCCGATCGCTACGGCCTCCTGGCCTTCGGCCTCTACGGG
GCCTTCCTTTCAGCGCACCTGGTGGCGCAGAGCCTCTTCGCGTACCTGGAGCACCGGCGG
GTGGCGGCGGCGGCGCGGGGGCCGCTGGATGCAGCCACCGCGCGCAGTGTGGCGCTGACC
ATCTCCGCCTACCAGGAGGACCCCGCGTACCTGCGCCAGTGCCTGGCGTCCGCCCGCGCC
CTGCTGTACCCGCGCGCGCGGCTGCGCGTCCTCATGGTGGTGGATGGCAACCGCGCCGAG
GACCTCTACATGGTCGACATGTTCCGCGAGGTCTTCGCTGACGAGGACCCCGCCACGTAC
GTGTGGGACGGCAACTACCACCAGCCCTGGGAACCCGCGGCGGCGGGCGCGGTGGGCGCC
GGAGCCTATCGGGAGGTGGAGGCGGAGGATCCTGGGCGGCTGGCAGTGGAGGCGCTGGTG
AGGACTCGCAGGTGCGTGTGCGTGGCGCAGCGCTGGGGCGGCAAGCGCGAGGTCATGTAC
ACAGCCTTCAAGGCGCTCGGAGATTCGGTGGACTACGTGCAGGTCTGTGACTCGGACACA
AGGTTGGACCCCATGGCACTGCTGGAGCTCGTGCGGGTACTGGACGAGGACCCCCGGGTA
GGGGCTGTTGGTGGGGACGTGCGGATCCTTAACCCTCTGGACTCCTGGGTCAGCTTCCTA
AGCAGCCTGCGATACTGGGTAGCCTTCAATGTGGAGCGGGCTTGTCAGAGCTACTTCCAC
TGTGTATCCTGCATCAGCGGTCCTCTAGGCCTATATAGGAATAACCTCTTGCAGCAGTTT
CTTGAGGCCTGGTACAACCAGAAGTTCCTGGGTACCCACTGTACTTTTGGGGATGACCGG
CACCTCACCAACCGCATGCTCAGCATGGGTTATGCTACCAAGTACACCTCCAGGTCCCGC
TGCTACTCAGAGACGCCCTCGTCCTTCCTGCGGTGGCTGAGCCAGCAGACACGCTGGTCC
AAGTCGTACTTCCGTGAGTGGCTGTACAACGCGCTCTGGTGGCACCGGCACCATGCGTGG
ATGACCTACGAGGCGGTGGTCTCCGGCCTGTTCCCCTTCTTCGTGGCGGCCACTGTGCTG
CGTCTGTTCTACGCGGGCCGCCCTTGGGCGCTGCTGTGGGTGCTGCTGTGCGTGCAGGGC
GTGGCACTGGCCAAGGCGGCCTTCGCGGCCTGGCTGCGGGGCTGCCTGCGCATGGTGCTT
CTGTCGCTCTACGCGCCCCTCTACATGTGTGGCCTCCTGCCTGCCAAGTTCCTGGCGCTA
GTCACCATGAACCAGAGTGGCTGGGGCACCTCGGGCCGGCGGAAGCTGGCCGCTAACTAC
GTCCCTCTGCTGCCCCTGGCGCTCTGGGCGCTGCTGCTGCTTGGGGGCCTGGTCCGCAGC
GTAGCACACGAGGCCAGGGCCGACTGGAGCGGCCCTTCCCGCGCAGCCGAGGCCTACCAC
TTGGCCGCGGGGGCCGGCGCCTACGTGGGCTACTGGGTGGCCATGTTGACGCTGTACTGG
GTGGGCGTGCGGAGGCTTTGCCGGCGGCGGACCGGGGGCTACCGCGTCCAGGTGTGA
Enzyme 66 GenBank Gene ID AC018755 Link Image
Enzyme 66 GeneCard ID HAS1 Link Image
Enzyme 66 GenAtlas ID HAS1 Link Image
Enzyme 66 HGNC ID HGNC:4818 Link Image
Enzyme 66 Chromosome Location 1
Enzyme 66 Locus 19q13.4
Enzyme 66 SNPs SNPJam Report Link Image
Enzyme 66 General References
  1. Itano N, Kimata K: Molecular cloning of human hyaluronan synthase. Biochem Biophys Res Commun. 1996 May 24;222(3):816-20. [PubMed Link Image]
  2. Shyjan AM, Heldin P, Butcher EC, Yoshino T, Briskin MJ: Functional cloning of the cDNA for a human hyaluronan synthase. J Biol Chem. 1996 Sep 20;271(38):23395-9. [PubMed Link Image]
  3. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed Link Image]
  4. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed Link Image]
Enzyme 66 Metabolite References Not Available
Enzyme 67 [top]
Enzyme 67 ID 7039
Enzyme 67 Name Exostosin-like 3
Enzyme 67 Synonyms
  1. EXT-related protein 1
  2. Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
  3. Hereditary multiple exostoses gene isolog
  4. Multiple exostosis-like protein 3
  5. Putative tumor suppressor protein EXTL3
Enzyme 67 Gene Name EXTL3
Enzyme 67 Protein Sequence >Exostosin-like 3
MTGYTMLRNGGAGNGGQTCMLRWSNRIRLTWLSFTLFVILVFFPLIAHYYLTTLDEADEA
GKRIFGPRVGNELCEVKHVLDLCRIRESVSEELLQLEAKRQELNSEIAKLNLKIEACKKS
IENAKQDLLQLKNVISQTEHSYKELMAQNQPKLSLPIRLLPEKDDAGLPPPKATRGCRLH
NCFDYSRCPLTSGFPVYVYDSDQFVFGSYLDPLVKQAFQATARANVYVTENADIACLYVI
LVGEMQEPVVLRPAELEKQLYSLPHWRTDGHNHVIINLSRKSDTQNLLYNVSTGRAMVAQ
STFYTVQYRPGFDLVVSPLVHAMSEPNFMEIPPQVPVKRKYLFTFQGEKIESLRSSLQEA
RSFEEEMEGDPPADYDDRIIATLKAVQDSKLDQVLVEFTCKNQPKPSLPTEWALCGERED
RLELLKLSTFALIITPGDPRLVISSGCATRLFEALEVGAVPVVLGEQVQLPYQDMLQWNE
AALVVPKPRVTEVHFLLRSLSDSDLLAMRRQGRFLWETYFSTADSIFNTVLAMIRTRIQI
PAAPIREEAAAEIPHRSGKAAGTDPNMADNGDLDLGPVETEPPYASPRYLRNFTLTVTDF
YRSWNCAPGPFHLFPHTPFDPVLPSEAKFLGSGTGFRPIGGGAGGSGKEFQAALGGNVPR
EQFTVVMLTYEREEVLMNSLERLNGLPYLNKVVVVWNSPKLPSEDLLWPDIGVPIMVVRT
EKNSLNNRFLPWNEIETEAILSIDDDAHLRHDEIMFGFRVWREARDRIVGFPGRYHAWDI
PHQSWLYNSNYSCELSMVLTGAAFFHKYYAYLYSYVMPQAIRDMVDEYINCEDIAMNFLV
SHITRKPPIKVTSRWTFRCPGCPQALSHDDSHFHERHKCINFFVKVYGYMPLLYTQFRVD
SVLFKTRLPHDKTKCFKFI
Enzyme 67 Number of Residues 919
Enzyme 67 Molecular Weight 104748.2
Enzyme 67 Theoretical pI 6.48
Enzyme 67 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
  • membrane part
Enzyme 67 General Function Involved in glucuronyl-galactosyl-proteoglycan 4-alpha-
Enzyme 67 Specific Function Probable glycosyltransferase
Enzyme 67 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 67 Reactions
  • UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D- galactosyl-(1->4)-beta-D-xylosyl-proteoglycan = UDP + alpha-N-acetyl-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)- beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl- proteoglycan [RN:R05930]
Enzyme 67 Pfam Domain Function
Enzyme 67 Signals
  • None
Enzyme 67 Transmembrane Regions
  • 31-51
Enzyme 67 Essentiality Not Available
Enzyme 67 GenBank ID Protein 2723391 Link Image
Enzyme 67 UniProtKB/Swiss-Prot ID O43909 Link Image
Enzyme 67 UniProtKB/Swiss-Prot Entry Name EXTL3_HUMAN Link Image
Enzyme 67 PDB ID Not Available
Enzyme 67 Cellular Location Not Available
Enzyme 67 Gene Sequence >2760 bp
ATGACAGGCTATACCATGCTGCGGAATGGGGGCGCGGGGAACGGAGGTCAGACCTGCATG
CTGCGCTGGTCCAACCGCATCCGCCTCACGTGGCTCAGCTTCACGCTCTTTGTCATCCTG
GTCTTCTTCCCGCTCATCGCCCACTATTACCTCACCACTCTGGATGAGGCTGATGAGGCA
GGCAAGCGGATTTTTGGTCCCCGGGTGGGGAACGAGCTGTGCGAGGTGAAGCACGTGCTG
GATCTGTGCCGCATCCGGGAGTCGGTGAGTGAAGAGCTCCTGCAGCTGGAGGCCAAGCGC
CAAGAGCTGAACAGCGAGATCGCCAAGCTGAATCTGAAGATCGAAGCCTGTAAGAAGAGC
ATTGAGAACGCCAAGCAGGACCTGCTCCAGCTCAAGAATGTCATCAGCCAGACCGAGCAT
TCCTACAAGGAGCTCATGGCCCAGAACCAGCCCAAGCTGTCCCTGCCCATCCGACTGCTC
CCAGAGAAGGACGATGCCGGCCTCCCTCCCCCGAAGGCCACTCGGGGCTGCCGGCTACAC
AACTGCTTTGATTATTCTCGTTGCCCTCTCACCTCTGGCTTCCCGGTCTACGTCTATGAC
AGTGACCAGTTTGTCTTTGGCAGCTACCTGGATCCCTTGGTCAAGCAGGCTTTTCAGGCG
ACAGCACGAGCTAACGTTTATGTTACAGAAAATGCAGACATCGCCTGCCTTTACGTGATA
CTAGTGGGAGAGATGCAGGAGCCCGTGGTGCTGCGGCCTGCTGAGCTGGAGAAGCAGTTG
TATTCCCTGCCACACTGGCGGACGGATGGACACAACCATGTCATCATCAATCTGTCACGT
AAGTCAGATACACAGAACCTTCTCTATAACGTCAGTACTGGCCGTGCCATGGTGGCCCAG
TCCACCTTCTACACTGTCCAGTACAGACCTGGCTTTGACTTGGTCGTATCACCGCTGGTC
CATGCCATGTCTGAGCCCAACTTCATGGAAATCCCACCACAGGTGCCGGTGAAGCGGAAA
TATCTCTTCACCTTCCAGGGCGAGAAGATTGAGTCTCTGAGGTCTAGCCTTCAGGAGGCC
CGCTCCTTCGAAGAGGAAATGGAGGGCGACCCTCCCGCCGACTACGATGACCGGATCATT
GCCACCCTGAAGGCGGTGCAGGACAGCAAGCTGGATCAGGTCCTGGTGGAATTCACCTGC
AAAAACCAGCCCAAACCCAGCCTGCCGACTGAGTGGGCACTGTGTGGAGAGCGGGAGGAC
CGCTTGGAATTGCTGAAGCTCTCCACCTTCGCCCTCATCATTACCCCCGGGGACCCTCGC
TTGGTTATTTCCTCTGGGTGTGCAACACGGCTCTTCGAAGCCCTGGAAGTCGGTGCCGTC
CCGGTGGTGCTGGGGGAGCAGGTCCAGCTTCCCTACCAGGACATGCTGCAGTGGAACGAG
GCGGCCCTGGTGGTGCCAAAGCCTCGTGTTACCGAGGTTCATTTCCTGCTCAGAAGCCTC
TCCGATAGTGACCTCCTGGCTATGAGGCGGCAAGGCCGCTTTCTCTGGGAGACTTACTTC
TCCACTGCTGACAGTATTTTTAATACCGTGCTGGCTATGATTAGGACTCGCATCCAGATC
CCAGCCGCTCCCATCCGGGAAGAGGCGGCAGCTGAGATCCCCCACCGTTCAGGCAAGGCG
GCTGGAACTGACCCCAACATGGCTGACAACGGGGACCTGGACCTGGGGCCAGTGGAGACG
GAGCCGCCCTACGCCTCACCCAGATACCTCCGCAATTTCACTCTGACTGTCACTGACTTT
TACCGCAGCTGGAACTGTGCTCCAGGGCCTTTCCATCTTTTCCCCCACACTCCCTTTGAC
CCTGTGTTGCCCTCAGAGGCCAAATTCTTGGGCTCAGGGACTGGCTTTCGGCCTATTGGT
GGTGGAGCTGGGGGTTCTGGCAAGGAATTTCAGGCAGCGCTTGGAGGCAATGTTCCCCGA
GAGCAGTTCACGGTGGTGATGTTGACTTATGAGCGGGAGGAAGTGCTTATGAACTCTTTA
GAGAGGCTGAATGGCCTCCCTTACCTGAACAAGGTCGTGGTGGTGTGGAATTCTCCCAAG
CTGCCATCAGAGGACCTTCTGTGGCCTGACATTGGCGTTCCCATCATGGTGGTCCGTACT
GAGAAGAACAGTTTGAACAACCGATTCTTACCCTGGAATGAAATTGAGACAGAGGCCATC
CTGTCCATTGATGACGATGCTCACCTCCGCCATGACGAAATCATGTTTGGGTTCCGGGTG
TGGAGAGAAGCTCGGGACCGCATCGTGGGCTTCCCTGGCCGTTACCACGCATGGGACATC
CCCCATCAGTCCTGGCTCTACAACTCCAACTACTCCTGTGAGCTGTCCATGGTGCTGACA
GGTGCTGCCTTCTTTCACAAGTATTATGCCTACCTGTATTCTTATGTGATGCCCCAGGCC
ATCCGGGACATGGTGGATGAATACATCAACTGTGAGGACATTGCCATGAACTTCCTTGTC
TCCCACATCACTCGGAAGCCCCCCATCAAGGTGACCTCACGGTGGACATTCCGATGCCCA
GGATGCCCTCAGGCCCTGTCTCATGATGACTCCCACTTCCACGAGCGGCACAAGTGCATC
AACTTCTTCGTGAAGGTGTACGGCTACATGCCCCTCCTGTACACGCAGTTCAGGGTGGAT
TCTGTGCTCTTCAAGACACGCCTGCCCCATGACAAGACCAAGTGCTTCAAGTTCATCTAG
Enzyme 67 GenBank Gene ID AB007042 Link Image
Enzyme 67 GeneCard ID EXTL3 Link Image
Enzyme 67 GenAtlas ID Not Available
Enzyme 67 HGNC ID Not Available
Enzyme 67 Chromosome Location 8
Enzyme 67 Locus 8p21
Enzyme 67 SNPs SNPJam Report Link Image
Enzyme 67 General References
  1. Van Hul W, Wuyts W, Hendrickx J, Speleman F, Wauters J, De Boulle K, Van Roy N, Bossuyt P, Willems PJ: Identification of a third EXT-like gene (EXTL3) belonging to the EXT gene family. Genomics. 1998 Jan 15;47(2):230-7. [PubMed Link Image]
  2. Saito T, Seki N, Yamauchi M, Tsuji S, Hayashi A, Kozuma S, Hori T: Structure, chromosomal location, and expression profile of EXTR1 and EXTR2, new members of the multiple exostoses gene family. Biochem Biophys Res Commun. 1998 Feb 4;243(1):61-6. [PubMed Link Image]
  3. Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. McCormick C, Duncan G, Goutsos KT, Tufaro F: The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate. Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):668-73. [PubMed Link Image]
Enzyme 67 Metabolite References Not Available
Enzyme 68 [top]
Enzyme 68 ID 7040
Enzyme 68 Name Exostosin-2
Enzyme 68 Synonyms
  1. Glucuronosyl-N-acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
  2. Multiple exostoses protein 2
  3. Putative tumor suppressor protein EXT2
Enzyme 68 Gene Name EXT2
Enzyme 68 Protein Sequence >Exostosin-2
MCASVKYNIRGPALIPRMKTKHRIYYITLFSIVLLGLIATGMFQFWPHSIESSNDWNVEK
RSIRDVPVVRLPADSPIPERGDLSCRMHTCFDVYRCGFNPKNKIKVYIYALKKYVDDFGV
SVSNTISREYNELLMAISDSDYYTDDINRACLFVPSIDVLNQNTLRIKETAQAMAQLSRW
DRGTNHLLFNMLPGGPPDYNTALDVPRDRALLAGGGFSTWTYRQGYDVSIPVYSPLSAEV
DLPEKGPGPRQYFLLSSQVGLHPEYREDLEALQVKHGESVLVLDKCTNLSEGVLSVRKRC
HKHQVFDYPQVLQEATFCVVLRGARLGQAVLSDVLQAGCVPVVIADSYILPFSEVLDWKR
ASVVVPEEKMSDVYSILQSIPQRQIEEMQRQARWFWEAYFQSIKAIALATLQIINDRIYP
YAAISYEEWNDPPAVKWGSVSNPLFLPLIPPQSQGFTAIVLTYDRVESLFRVITEVSKVP
SLSKLLVVWNNQNKNPPEDSLWPKIRVPLKVVRTAENKLSNRFFPYDEIETEAVLAIDDD
IIMLTSDELQFGYEVWREFPDRLVGYPGRLHLWDHEMNKWKYESEWTNEVSMVLTGAAFY
HKYFNYLYTYKMPGDIKNWVDAHMNCEDIAMNFLVANVTGKAVIKVTPRKKFKCPECTAI
DGLSLDQTHMVERSECINKFASVFGTMPLKVVEHRADPVLYKDDFPEKLKSFPNIGSL
Enzyme 68 Number of Residues 718
Enzyme 68 Molecular Weight 82253.8
Enzyme 68 Theoretical pI 6.51
Enzyme 68 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
  • membrane part
Enzyme 68 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 68 Specific Function Glycosyltransferase required for the biosynthesis of heparan-sulfate. The EXT1/EXT2 complex possesses substantially higher glycosyltransferase activity than EXT1 or EXT2 alone. Appears to be a tumor suppressor
Enzyme 68 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 68 Reactions
  • UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl- proteoglycan = UDP + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)- beta-D-glucuronosyl-proteoglycan [RN:R07335]
Enzyme 68 Pfam Domain Function
Enzyme 68 Signals
  • None
Enzyme 68 Transmembrane Regions
  • 26-46
Enzyme 68 Essentiality Not Available
Enzyme 68 GenBank ID Protein 189065454 Link Image
Enzyme 68 UniProtKB/Swiss-Prot ID Q93063 Link Image
Enzyme 68 UniProtKB/Swiss-Prot Entry Name EXT2_HUMAN Link Image
Enzyme 68 PDB ID Not Available
Enzyme 68 Cellular Location Not Available
Enzyme 68 Gene Sequence >2157 bp
ATGTGTGCGTCGGTCAAGTATAATATCCGGGGTCCTGCCCTCATCCCAAGAATGAAGACC
AAGCACCGAATCTACTATATCACCCTCTTCTCCATTGTCCTCCTGGGCCTCATTGCCACT
GGCATGTTTCAGTTTTGGCCCCATTCTATCGAGTCCTCAAATGACTGGAATGTAGAGAAG
CGCAGCATCCGTGATGTGCCGGTTGTTAGGCTGCCAGCCGACAGTCCCATCCCAGAGCGG
GGGGATCTCAGTTGCAGAATGCACACGTGTTTTGATGTCTATCGCTGTGGCTTCAACCCA
AAGAACAAAATCAAGGTGTATATCTATGCTCTGAAAAAGTACGTGGATGACTTTGGCGTC
TCTGTCAGCAACACCATCTCCCGGGAGTATAATGAACTGCTCATGGCCATCTCAGACAGT
GACTACTACACTGATGACATCAACCGGGCCTGTCTGTTTGTTCCCTCCATCGATGTGCTT
AACCAGAACACACTGCGCATCAAGGAGACAGCACAAGCGATGGCCCAGCTCTCTAGGTGG
GATCGAGGTACGAATCACCTGTTGTTCAACATGTTGCCTGGAGGTCCCCCAGATTATAAC
ACAGCCCTGGATGTCCCCAGAGACAGGGCCCTGTTGGCTGGTGGCGGCTTTTCTACGTGG
ACTTACCGGCAAGGCTACGATGTCAGCATTCCTGTCTATAGTCCACTGTCAGCTGAGGTG
GATCTTCCAGAGAAAGGACCAGGTCCACGGCAATACTTCCTCCTGTCATCTCAGGTGGGT
CTCCATCCTGAGTACAGAGAGGACCTAGAAGCCCTCCAGGTCAAACATGGAGAGTCAGTG
TTAGTACTCGATAAATGCACCAACCTCTCAGAGGGTGTCCTTTCTGTCCGTAAGCGCTGC
CACAAGCACCAGGTCTTCGATTACCCACAGGTGCTACAGGAGGCTACTTTCTGTGTGGTT
CTTCGTGGAGCTCGGCTGGGCCAGGCAGTATTGAGCGATGTGTTACAAGCTGGCTGTGTC
CCGGTTGTCATTGCAGACTCCTATATTTTGCCTTTCTCTGAAGTTCTTGACTGGAAGAGA
GCATCTGTGGTTGTACCAGAAGAAAAGATGTCAGATGTGTACAGTATTTTGCAGAGCATC
CCCCAAAGACAGATTGAAGAAATGCAGAGACAGGCCCGGTGGTTCTGGGAAGCGTACTTC
CAGTCAATTAAAGCCATTGCCCTGGCCACCCTGCAGATTATCAATGACCGGATCTATCCA
TATGCTGCCATCTCCTATGAAGAATGGAATGACCCTCCTGCTGTGAAGTGGGGCAGCGTG
AGCAATCCACTCTTCCTCCCGCTGATCCCACCACAGTCTCAAGGGTTCACCGCCATAGTC
CTCACCTACGACCGAGTAGAGAGCCTCTTCCGGGTCATCACTGAAGTGTCCAAGGTGCCC
AGTCTATCCAAACTACTTGTCGTCTGGAATAATCAGAATAAAAACCCTCCAGAAGATTCT
CTCTGGCCCAAAATCCGGGTTCCATTAAAAGTTGTGAGGACTGCTGAAAACAAGTTAAGT
AACCGTTTCTTCCCTTATGATGAAATCGAGACAGAAGCTGTTCTGGCCATTGATGATGAT
ATCATTATGCTGACCTCTGACGAGCTGCAATTTGGTTATGAGGTCTGGCGGGAATTTCCT
GACCGGTTGGTGGGTTACCCGGGTCGTCTGCATCTCTGGGACCATGAGATGAATAAGTGG
AAGTATGAGTCTGAGTGGACGAATGAAGTGTCCATGGTGCTCACTGGGGCAGCTTTTTAT
CACAAGTATTTTAATTACCTGTATACCTACAAAATGCCTGGGGATATCAAGAACTGGGTA
GATGCTCATATGAACTGTGAAGATATTGCCATGAACTTCCTGGTGGCCAACGTCACGGGA
AAAGCAGTTATCAAGGTAACCCCACGAAAGAAATTCAAGTGTCCTGAGTGCACAGCCATA
GATGGGCTTTCACTAGACCAAACACACATGGTGGAGAGGTCAGAGTGCATCAACAAGTTT
GCTTCAGTCTTCGGGACCATGCCTCTCAAGGTGGTGGAACACCGAGCTGACCCTGTCCTG
TACAAAGATGACTTTCCTGAGAAGCTGAAGAGCTTCCCCAACATTGGCAGCTTATGA
Enzyme 68 GenBank Gene ID AK312375 Link Image
Enzyme 68 GeneCard ID EXT2 Link Image
Enzyme 68 GenAtlas ID EXT2 Link Image
Enzyme 68 HGNC ID HGNC:3513 Link Image
Enzyme 68 Chromosome Location 1
Enzyme 68 Locus 11p12-p11
Enzyme 68 SNPs SNPJam Report Link Image
Enzyme 68 General References
  1. Stickens D, Clines G, Burbee D, Ramos P, Thomas S, Hogue D, Hecht JT, Lovett M, Evans GA: The EXT2 multiple exostoses gene defines a family of putative tumour suppressor genes. Nat Genet. 1996 Sep;14(1):25-32. [PubMed Link Image]
  2. Wuyts W, Van Hul W, Wauters J, Nemtsova M, Reyniers E, Van Hul EV, De Boulle K, de Vries BB, Hendrickx J, Herrygers I, Bossuyt P, Balemans W, Fransen E, Vits L, Coucke P, Nowak NJ, Shows TB, Mallet L, van den Ouweland AM, McGaughran J, Halley DJ, Willems PJ: Positional cloning of a gene involved in hereditary multiple exostoses. Hum Mol Genet. 1996 Oct;5(10):1547-57. [PubMed Link Image]
  3. Clines GA, Ashley JA, Shah S, Lovett M: The structure of the human multiple exostoses 2 gene and characterization of homologs in mouse and Caenorhabditis elegans. Genome Res. 1997 Apr;7(4):359-67. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Kobayashi S, Morimoto K, Shimizu T, Takahashi M, Kurosawa H, Shirasawa T: Association of EXT1 and EXT2, hereditary multiple exostoses gene products, in Golgi apparatus. Biochem Biophys Res Commun. 2000 Feb 24;268(3):860-7. [PubMed Link Image]
  7. Simmons AD, Musy MM, Lopes CS, Hwang LY, Yang YP, Lovett M: A direct interaction between EXT proteins and glycosyltransferases is defective in hereditary multiple exostoses. Hum Mol Genet. 1999 Nov;8(12):2155-64. [PubMed Link Image]
  8. Wuyts W, Van Hul W: Molecular basis of multiple exostoses: mutations in the EXT1 and EXT2 genes. Hum Mutat. 2000;15(3):220-7. [PubMed Link Image]
  9. Philippe C, Porter DE, Emerton ME, Wells DE, Simpson AH, Monaco AP: Mutation screening of the EXT1 and EXT2 genes in patients with hereditary multiple exostoses. Am J Hum Genet. 1997 Sep;61(3):520-8. [PubMed Link Image]
  10. Xu L, Xia J, Jiang H, Zhou J, Li H, Wang D, Pan Q, Long Z, Fan C, Deng HX: Mutation analysis of hereditary multiple exostoses in the Chinese. Hum Genet. 1999 Jul-Aug;105(1-2):45-50. [PubMed Link Image]
  11. Park KJ, Shin KH, Ku JL, Cho TJ, Lee SH, Choi IH, Phillipe C, Monaco AP, Porter DE, Park JG: Germline mutations in the EXT1 and EXT2 genes in Korean patients with hereditary multiple exostoses. J Hum Genet. 1999;44(4):230-4. [PubMed Link Image]
  12. Shi YR, Wu JY, Tsai FJ, Lee CC, Tsai CH: An R223P mutation in EXT2 gene causes hereditary multiple exostoses. Hum Mutat. 2000 Apr;15(4):390-1. [PubMed Link Image]
  13. Seki H, Kubota T, Ikegawa S, Haga N, Fujioka F, Ohzeki S, Wakui K, Yoshikawa H, Takaoka K, Fukushima Y: Mutation frequencies of EXT1 and EXT2 in 43 Japanese families with hereditary multiple exostoses. Am J Med Genet. 2001 Feb 15;99(1):59-62. [PubMed Link Image]
  14. Bernard MA, Hall CE, Hogue DA, Cole WG, Scott A, Snuggs MB, Clines GA, Ludecke HJ, Lovett M, Van Winkle WB, Hecht JT: Diminished levels of the putative tumor suppressor proteins EXT1 and EXT2 in exostosis chondrocytes. Cell Motil Cytoskeleton. 2001 Feb;48(2):149-62. [PubMed Link Image]
  15. Gigante M, Matera MG, Seripa D, Izzo AM, Venanzi R, Giannotti A, Digilio MC, Gravina C, Lazzari M, Monteleone G, Monteleone M, Dallapiccola B, Fazio VM: Ext-mutation analysis in Italian sporadic and hereditary osteochondromas. Int J Cancer. 2001 Nov 20;95(6):378-83. [PubMed Link Image]
  16. Francannet C, Cohen-Tanugi A, Le Merrer M, Munnich A, Bonaventure J, Legeai-Mallet L: Genotype-phenotype correlation in hereditary multiple exostoses. J Med Genet. 2001 Jul;38(7):430-4. [PubMed Link Image]
Enzyme 68 Metabolite References Not Available
Enzyme 69 [top]
Enzyme 69 ID 7041
Enzyme 69 Name Exostosin-like 1
Enzyme 69 Synonyms
  1. Exostosin-L
  2. Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
  3. Multiple exostosis-like protein
Enzyme 69 Gene Name EXTL1
Enzyme 69 Protein Sequence >Exostosin-like 1
MQSWRRRKSLWLALSASWLLLVLLGGFSLLRLALPPRPRPGASQGWPRWLDAELLQSFSQ
PGELPEDAVSPPQAPHGGSCNWESCFDTSKCRGDGLKVFVYPAVGTISETHRRILASIEG
SRFYTFSPAGACLLLLLSLDAQTGECSSMPLQWNRGRNHLVLRLHPAPCPRTFQLGQAMV
AEASPTVDSFRPGFDVALPFLPEAHPLRGGAPGQLRQHSPQPGVALLALEEERGGWRTAD
TGSSACPWDGRCEQDPGPGQTQRQETLPNATFCLISGHRPEAASRFLQALQAGCIPVLLS
PRWELPFSEVIDWTKAAIVADERLPLQVLAALQEMSPARVLALRQQTQFLWDAYFSSVEK
VIHTTLEVIQDRIFGTSAHPSLLWNSPPGALLALSTFSTSPQDFPFYYLQQGSRPEGRFS
ALIWVGPPGQPPLKLIQAVAGSQHCAQILVLWSNERPLPSRWPETAVPLTVIDGHRKVSD
RFYPYSTIRTDAILSLDARSSLSTSEVDFAFLVWQSFPERMVGFLTSSHFWDEAHGGWGY
TAERTNEFSMVLTTAAFYHRYYHTLFTHSLPKALRTLADEAPTCVDVLMNFIVAAVTKLP
PIKVPYGKQRQEAAPLAPGGPGPRPKPPAPAPDCINQIAAAFGHMPLLSSRLRLDPVLFK
DPVSVQRKKYRSLEKP
Enzyme 69 Number of Residues 676
Enzyme 69 Molecular Weight 74695.8
Enzyme 69 Theoretical pI 8.26
Enzyme 69 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
  • membrane part
Enzyme 69 General Function Involved in glucuronosyl-N-acetylglucosaminyl-proteogly
Enzyme 69 Specific Function Probable glycosyltransferase
Enzyme 69 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 69 Reactions
  • UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl- proteoglycan = UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->4)-N- acetyl-alpha-D-glucosaminyl-proteoglycan [RN:R07334]
Enzyme 69 Pfam Domain Function
Enzyme 69 Signals
  • None
Enzyme 69 Transmembrane Regions
  • 10-30
Enzyme 69 Essentiality Not Available
Enzyme 69 GenBank ID Protein 4106426 Link Image
Enzyme 69 UniProtKB/Swiss-Prot ID Q92935 Link Image
Enzyme 69 UniProtKB/Swiss-Prot Entry Name EXTL1_HUMAN Link Image
Enzyme 69 PDB ID Not Available
Enzyme 69 Cellular Location Not Available
Enzyme 69 Gene Sequence >2031 bp
ATGCAGTCGTGGAGGAGAAGAAAGTCCCTGTGGCTGGCACTGTCAGCCTCCTGGCTCCTG
CTTGTCCTGCTGGGAGGCTTCTCCCTTCTCCGCCTGGCGTTGCCTCCCAGACCTCGGCCC
GGGGCTTCCCAAGGCTGGCCCCGCTGGCTGGATGCAGAGCTCCTGCAGAGCTTCTCCCAG
CCTGGAGAGCTCCCAGAAGATGCCGTTTCACCTCCTCAAGCCCCTCATGGTGGCAGCTGC
AACTGGGAATCTTGCTTTGATACCTCAAAGTGCAGGGGCGATGGCCTTAAGGTATTCGTG
TACCCAGCGGTTGGAACCATCTCTGAGACTCATCGCAGGATCCTGGCTTCCATTGAGGGC
TCTCGCTTCTACACATTCAGCCCTGCTGGGGCCTGCCTCCTCCTCCTCCTCAGCCTGGAC
GCCCAGACTGGAGAGTGCAGCTCAATGCCTCTGCAATGGAACAGGGGCAGGAACCATCTG
GTCCTCCGTCTCCACCCGGCTCCCTGCCCCAGGACCTTCCAGCTGGGACAGGCTATGGTG
GCTGAGGCCAGCCCCACGGTGGACTCCTTCCGGCCCGGCTTTGATGTGGCCCTCCCTTTT
CTCCCTGAAGCCCACCCGTTGCGAGGTGGGGCTCCTGGCCAGCTGCGGCAACACAGCCCC
CAGCCCGGGGTAGCCCTGCTAGCCCTGGAAGAGGAGAGGGGTGGGTGGCGCACAGCAGAC
ACTGGCTCCTCTGCCTGCCCCTGGGATGGGCGCTGTGAGCAAGACCCTGGACCTGGGCAG
ACCCAGCGCCAGGAGACGCTGCCCAATGCCACCTTCTGCCTCATCTCTGGCCACCGTCCC
GAGGCTGCCTCGCGCTTCCTCCAAGCCCTGCAGGCCGGCTGCATCCCAGTGCTTCTCAGC
CCCCGCTGGGAGCTGCCCTTCTCCGAGGTCATCGACTGGACCAAGGCAGCCATCGTAGCT
GATGAGAGGCTCCCACTTCAGGTCCTGGCTGCCCTCCAGGAGATGTCCCCTGCACGGGTC
CTCGCCCTGCGTCAGCAGACCCAGTTTCTATGGGATGCCTACTTCTCCTCAGTGGAGAAG
GTCATCCATACCACTCTGGAGGTTATTCAGGACCGGATTTTTGGAACATCAGCTAACCCC
TCACTGCTGTGGAACAGCCCCCCAGGGGCACTCCTGGCCCTGTCTACTTTTTCCACAAGC
CCCCAGGACTTCCCCTTCTACTACCTGCAACAGGGCTCCCGCCCTGAGGGCAGATTCAGC
GCCCTGATCTGGGTGGGGCCCCCAGGCCAGCCCCCTCTGAAGCTCATCCAGGCGGTGGCA
GGCTCCCAGCACTGTGCCCAGATCTTGGTTCTCTGGAGCAATGAGAGGCCACTCCCATCC
AGGTGGCCGGAGACAGCTGTGCCCTTGACAGTCATTGATGGGCACAGGAAGGTTAGTGAT
CGCTTCTACCCATATAGCACCATCAGAACAGATGCCATCCTCAGCCTCGATGCCCGCAGC
AGTCTTTCCACAAGTGAGGTGGACTTTGCCTTTCTGGTGTGGCAGAGCTTCCCAGAGCGG
ATGGTGGGCTTCCTGACGTCGAGCCATTTCTGGGACGAGGCCCATGGTGGCTGGGGCTAC
ACTGCTGAGAGGACCAACGAATTCTCCATGGTTCTCACCACAGCCGCCTTCTACCATAGG
TATTACCACACTCTCTTCACCCACTCCCTGCCCAAGGCTCTGAGGACCCTGGCAGATGAG
GCACCCACCTGTGTGGACGTCCTGATGAATTTCATAGTAGCAGCAGTCACCAAGCTGCCC
CCTATCAAGGTGCCCTATGGCAAGCAGCGCCAGGAGGCTGCTCCACTGGCGCCTGGGGGC
CCGGGGCCCAGGCCAAAGCCGCCTGCCCCAGCCCCCGACTGCATCAACCAGATAGCGGCA
GCGTTCGGCCACATGCCCTTGCTGTCCTCTCGTCTGCGTCTGGACCCGGTGCTGTTTAAG
GACCCGGTGTCCGTGCAGCGCAAGAAGTACCGCAGCCTGGAGAAGCCCTAG
Enzyme 69 GenBank Gene ID AF083633 Link Image
Enzyme 69 GeneCard ID EXTL1 Link Image
Enzyme 69 GenAtlas ID Not Available
Enzyme 69 HGNC ID Not Available
Enzyme 69 Chromosome Location 1
Enzyme 69 Locus 1p36.1
Enzyme 69 SNPs SNPJam Report Link Image
Enzyme 69 General References
  1. Wise CA, Clines GA, Massa H, Trask BJ, Lovett M: Identification and localization of the gene for EXTL, a third member of the multiple exostoses gene family. Genome Res. 1997 Jan;7(1):10-6. [PubMed Link Image]
  2. Xu L, Xia J, Jiang H, Zhou J, Li H, Wang D, Pan Q, Long Z, Fan C, Deng HX: Mutation analysis of hereditary multiple exostoses in the Chinese. Hum Genet. 1999 Jul-Aug;105(1-2):45-50. [PubMed Link Image]
  3. Wuyts W, Spieker N, Van Roy N, De Boulle K, De Paepe A, Willems PJ, Van Hul W, Versteeg R, Speleman F: Refined physical mapping and genomic structure of the EXTL1 gene. Cytogenet Cell Genet. 1999;86(3-4):267-70. [PubMed Link Image]
  4. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 69 Metabolite References Not Available
Enzyme 70 [top]
Enzyme 70 ID 7042
Enzyme 70 Name N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase
Enzyme 70 Synonyms
  1. I-beta-1,3-N-acetylglucosaminyltransferase
  2. iGnT
  3. Poly-N-acetyllactosamine extension enzyme
  4. UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1
Enzyme 70 Gene Name B3GNT1
Enzyme 70 Protein Sequence >N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase
MQMSYAIRCAFYQLLLAALMLVAMLQLLYLSLLSGLHGQEEQDQYFEFFPPSPRSVDQVK
AQLRTALASGGVLDASGDYRVYRGLLKTTMDPNDVILATHASVDNLLHLSGLLERWEGPL
SVSVFAATKEEAQLATVLAYALSSHCPDMRARVAMHLVCPSRYEAAVPDPREPGEFALLR
SCQEVFDKLARVAQPGINYALGTNVSYPNNLLRNLAREGANYALVIDVDMVPSEGLWRGL
REMLDQSNQWGGTALVVPAFEIRRARRMPMNKNELVQLYQVGEVRPFYYGLCTPCQAPTN
YSRWVNLPEESLLRPAYVVPWQDPWEPFYVAGGKVPTFDERFRQYGFNRISQACELHVAG
FDFEVLNEGFLVHKGFKEALKFHPQKEAENQHNKILYRQFKQELKAKYPNSPRRC
Enzyme 70 Number of Residues 415
Enzyme 70 Molecular Weight 47118.7
Enzyme 70 Theoretical pI 7.22
Enzyme 70 GO Classification Not Available
Enzyme 70 General Function Involved in N-acetyllactosaminide beta-1,3-N-acetylgluc
Enzyme 70 Specific Function Can initiate the synthesis or the elongation of the linear poly-N-acetyllactosaminoglycans
Enzyme 70 Pathways
  • Blood group glycolipid biosynthesis-neolactoseries (map00602 Link Image)
  • Keratan sulfate biosynthesis (map00533 Link Image)
Enzyme 70 Reactions
  • UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N- acetyl-D-glucosaminyl-R [RN:R02789]
Enzyme 70 Pfam Domain Function Not Available
Enzyme 70 Signals
  • None
Enzyme 70 Transmembrane Regions
  • 9-36
Enzyme 70 Essentiality Not Available
Enzyme 70 GenBank ID Protein 2745741 Link Image
Enzyme 70 UniProtKB/Swiss-Prot ID O43505 Link Image
Enzyme 70 UniProtKB/Swiss-Prot Entry Name B3GN1_HUMAN Link Image
Enzyme 70 PDB ID Not Available
Enzyme 70 Cellular Location Not Available
Enzyme 70 Gene Sequence >1248 bp
ATGCAGATGTCCTACGCCATCCGGTGCGCCTTCTACCAGCTGCTGCTGGCCGCGCTCATG
CTGGTGGCGATGCTGCAGCTGCTCTACCTGTCGCTGCTGTCCGGACTGCACGGGCAGGAG
GAGCAAGACCAATATTTTGAGTTCTTTCCCCCGTCCCCACGGTCCGTGGACCAGGTCAAG
GCGCAGCTCCGCACCGCGCTGGCCTCTGGAGGCGTCCTGGACGCTAGCGGCGATTACCGC
GTCTACAGGGGCCTGCTGAAGACCACCATGGACCCCAACGATGTGATCCTGGCCACGCAC
GCCAGCGTGGACAACCTGCTGCACCTGTCGGGTCTGCTGGAGCGCTGGGAGGGCCCGCTG
TCCGTGTCGGTGTTCGCGGCCACCAAGGAGGAGGCGCAGCTGGCCACGGTGCTGGCCTAC
GCGCTGAGCAGCCACTGCCCCGACATGCGCGCCAGGGTCGCCATGCACCTCGTGTGCCCC
TCGCGTTACGAGGCAGCCGTGCCCGACCCCCGGGAGCCGGGGGAGTTTGCCCTGCTGCGG
TCCTGCCAGGAGGTCTTTGACAAGCTAGCCAGGGTGGCCCAGCCCGGGATTAATTATGCG
CTGGGCACCAATGTCTCCTACCCCAATAACCTGCTGAGGAATCTGGCTCGTGAGGGGGCC
AACTATGCCCTGGTGATCGATGTGGACATGGTGCCCAGCGAGGGGCTGTGGAGAGGCCTG
CGGGAAATGCTGGATCAGAGCAACCAGTGGGGAGGCACCGCGCTGGTGGTGCCTGCCTTC
GAAATCCGAAGAGCCCGCCGCATGCCCATGAACAAAAACGAGCTGGTGCAGCTCTACCAG
GTTGGCGAGGTGCGGCCCTTCTATTATGGGTTGTGCACCCCCTGCCAGGCACCCACCAAC
TATTCCCGCTGGGTCAACCTGCCGGAAGAGAGCTTGCTGCGGCCCGCCTACGTGGTACCT
TGGCAGGACCCCTGGGAGCCATTCTACGTGGCAGGAGGCAAGGTGCCCACCTTCGACGAG
CGCTTTCGGCAGTACGGCTTCAACCGAATCAGCCAGGCCTGCGAGCTGCATGTGGCGGGG
TTTGATTTTGAGGTCCTGAACGAAGGTTTCTTGGTTCATAAGGGCTTCAAAGAAGCGTTG
AAGTTCCATCCCCAAAAGGAGGCTGAAAATCAGCACAATAAGATCCTATATCGCCAGTTC
AAACAGGAGTTGAAGGCCAAGTACCCCAACTCTCCCCGACGCTGCTGA
Enzyme 70 GenBank Gene ID AF029893 Link Image
Enzyme 70 GeneCard ID B3GNT1 Link Image
Enzyme 70 GenAtlas ID B3GNT1 Link Image
Enzyme 70 HGNC ID HGNC:15685 Link Image
Enzyme 70 Chromosome Location 1
Enzyme 70 Locus 11q13.2
Enzyme 70 SNPs SNPJam Report Link Image
Enzyme 70 General References
  1. Sasaki K, Kurata-Miura K, Ujita M, Angata K, Nakagawa S, Sekine S, Nishi T, Fukuda M: Expression cloning of cDNA encoding a human beta-1,3-N-acetylglucosaminyltransferase that is essential for poly-N-acetyllactosamine synthesis. Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14294-9. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 70 Metabolite References Not Available
Enzyme 71 [top]
Enzyme 71 ID 7043
Enzyme 71 Name Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
Enzyme 71 Synonyms
  1. Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase
  2. GlcNAc-T V
  3. GNT-V
  4. Mannoside acetylglucosaminyltransferase 5
  5. N-acetylglucosaminyl-transferase V
Enzyme 71 Gene Name MGAT5
Enzyme 71 Protein Sequence >Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A
MALFTPWKLSSQKLGFFLVTFGFIWGMMLLHFTIQQRTQPESSSMLREQILDLSKRYIKA
LAEENRNVVDGPYAGVMTAYDLKKTLAVLLDNILQRIGKLESKVDNLVVNGTGTNSTNST
TAVPSLVALEKINVADIINGAQEKCVLPPMDGYPHCEGKIKWMKDMWRSDPCYADYGVDG
STCSFFIYLSEVENWCPHLPWRAKNPYEEADHNSLAEIRTDFNILYSMMKKHEEFRWMRL
RIRRMADAWIQAIKSLAEKQNLEKRKRKKVLVHLGLLTKESGFKIAETAFSGGPLGELVQ
WSDLITSLYLLGHDIRISASLAELKEIMKKVVGNRSGCPTVGDRIVELIYIDIVGLAQFK
KTLGPSWVHYQCMLRVLDSFGTEPEFNHANYAQSKGHKTPWGKWNLNPQQFYTMFPHTPD
NSFLGFVVEQHLNSSDIHHINEIKRQNQSLVYGKVDSFWKNKKIYLDIIHTYMEVHATVY
GSSTKNIPSYVKNHGILSGRDLQFLLRETKLFVGLGFPYEGPAPLEAIANGCAFLNPKFN
PPKSSKNTDFFIGKPTLRELTSQHPYAEVFIGRPHVWTVDLNNQEEVEDAVKAILNQKIE
PYMPYEFTCEGMLQRINAFIEKQDFCHGQVMWPPLSALQVKLAEPGQSCKQVCQESQLIC
EPSFFQHLNKDKDMLKYKVTCQSSELAKDILVPSFDPKNKHCVFQGDLLLFSCAGAHPRH
QRVCPCRDFIKGQVALCKDCL
Enzyme 71 Number of Residues 741
Enzyme 71 Molecular Weight 84542.0
Enzyme 71 Theoretical pI 8.21
Enzyme 71 GO Classification Not Available
Enzyme 71 General Function Involved in alpha-1,6-mannosyl-glycoprotein 6-beta-N-ac
Enzyme 71 Specific Function Catalyzes the addition of N-acetylglucosamine in beta 1- 6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides
Enzyme 71 Pathways
Enzyme 71 Reactions
  • UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D- mannosyl-R = UDP + 6-(2,6-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D- mannosyl-R [RN:R04665]
Enzyme 71 Pfam Domain Function Not Available
Enzyme 71 Signals
  • None
Enzyme 71 Transmembrane Regions
  • 14-30
Enzyme 71 Essentiality Not Available
Enzyme 71 GenBank ID Protein 4545222 Link Image
Enzyme 71 UniProtKB/Swiss-Prot ID Q09328 Link Image
Enzyme 71 UniProtKB/Swiss-Prot Entry Name MGT5A_HUMAN Link Image
Enzyme 71 PDB ID Not Available
Enzyme 71 Cellular Location Not Available
Enzyme 71 Gene Sequence >2226 bp
ATGGCTCTCTTCACTCCGTGGAAGTTGTCCTCTCAGAAGCTGGGCTTTTTCCTGGTGACT
TTTGGCTTCATTTGGGGTATGATGCTTCTGCACTTTACCATCCAGCAGCGAACTCAGCCT
GAAAGCAGCTCCATGCTGCGCGAGCAGATCCTGGACCTCAGCAAAAGGTACATCAAGGCA
CTGGCAGAAGAAAACAGGAATGTGGTGGATGGGCCATACGCTGGAGTCATGACAGCTTAT
GATCTGAAGAAAACCCTTGCTGTGTTATTAGATAACATTTTGCAGCGCATTGGCAAGTTG
GAGTCGAAGGTGGACAATCTTGTTGTCAATGGCACCGGAACAAACTCAACCAACTCCACT
ACAGCTGTTCCCAGCTTGGTTGCACTTGAGAAAATTAATGTGGCAGATATCATTAACGGA
GCTCAAGAAAAATGTGTATTGCCTCCTATGGACGGCTACCCTCACTGTGAGGGAAAGATC
AAGTGGATGAAAGACATGTGGCGTTCAGATCCCTGCTACGCAGACTATGGAGTGGATGGA
TCCACCTGCTCTTTTTTTATTTACCTCAGTGAGGTTGAAAATTGGTGTCCTCATTTACCT
TGGAGAGCAAAAAATCCCTACGAAGAAGCTGATCATAATTCATTGGCGGAAATTCGTACA
GATTTTAATATTCTCTACAGTATGATGAAAAAGCATGAAGAATTCCGGTGGATGAGACTA
CGGATCCGGCGAATGGCTGACGCATGGATCCAAGCAATCAAGTCCCTGGCAGAAAAGCAG
AACCTTGAAAAGAGAAAGCGGAAGAAAGTCCTCGTTCACCTGGGACTCCTGACCAAGGAA
TCTGGATTTAAGATTGCAGAGACAGCTTTCAGTGGTGGCCCTCTTGGTGAATTAGTTCAA
TGGAGTGATTTAATTACATCTCTGTACTTACTGGGCCATGACATTAGGATTTCAGCTTCA
CTGGCTGAGCTCAAGGAAATCATGAAGAAGGTTGTAGGAAACCGATCTGGCTGCCCAACT
GTAGGAGACAGAATTGTTGAGCTCATTTACATTGATATTGTAGGACTTGCTCAATTCAAG
AAAACTCTTGGACCATCCTGGGTTCATTACCAGTGCATGCTCCGAGTGCTGGATTCCTTT
GGAACAGAACCTGAGTTCAATCACGCAAATTATGCCCAATCGAAAGGCCACAAGACCCCT
TGGGGAAAATGGAATCTGAACCCTCAGCAGTTTTATACCATGTTCCCTCATACCCCAGAC
AACAGCTTTCTGGGGTTTGTGGTTGAGCAGCACCTGAACTCCAGTGATATCCACCACATT
AATGAAATCAAAAGGCAGAACCAGTCCCTTGTGTATGGCAAAGTGGATAGCTTCTGGAAG
AATAAGAAGATCTACTTGGACATTATTCACACATACATGGAAGTGCATGCAACTGTTTAT
GGCTCCAGCACAAAGAATATTCCCAGTTACGTGAAAAACCATGGTATCCTCAGTGGACGG
GACCTGCAGTTCCTTCTTCGAGAAACCAAGTTGTTTGTTGGACTTGGGTTCCCTTACGAG
GGCCCAGCTCCCCTGGAAGCTATCGCAAATGGATGTGCTTTTCTGAATCCCAAGTTCAAC
CCACCCAAAAGCAGCAAAAACACAGACTTCTTCATTGGCAAGCCAACACTGAGAGAGCTC
ACATCCCAGCATCCTTACGCTGAAGTTTTCATCGGGCGGCCACATGTGTGGACTGTTGAC
CTCAACAATCAGGAGGAAGTAGAGGATGCAGTGAAAGCCATCTTAAACCAGAAGATTGAG
CCATACATGCCATATGAATTTACGTGCGAGGGGATGCTACAGAGAATCAATGCTTTCATT
GAAAAACAGGACTTCTGCCATGGGCAAGTGATGTGGCCACCCCTCAGCGCCCTACAGGTC
AAGCTTGCTGAGCCCGGGCAGTCCTGCAAGCAGGTGTGCCAGGAGAGCCAGCTCATCTGC
GAGCCTTCTTTCTTCCAGCACCTCAACAAGGACAAGGACATGCTGAAGTACAAGGTGACC
TGCCAAAGCTCAGAGCTGGCCAAGGACATCCTGGTGCCCTCCTTTGACCCTAAGAATAAG
CACTGTGTGTTTCAAGGTGACCTCCTGCTCTTCAGCTGTGCAGGCGCCCACCCCAGGCAC
CAGAGGGTCTGCCCCTGCCGGGACTTCATCAAGGGCCAGGTGGCTCTCTGCAAAGACTGC
CTATAG
Enzyme 71 GenBank Gene ID AF113921 Link Image
Enzyme 71 GeneCard ID MGAT5 Link Image
Enzyme 71 GenAtlas ID Not Available
Enzyme 71 HGNC ID Not Available
Enzyme 71 Chromosome Location 2
Enzyme 71 Locus 2q21
Enzyme 71 SNPs SNPJam Report Link Image
Enzyme 71 General References
  1. Saito H, Nishikawa A, Gu J, Ihara Y, Soejima H, Wada Y, Sekiya C, Niikawa N, Taniguchi N: cDNA cloning and chromosomal mapping of human N-acetylglucosaminyltransferase V+. Biochem Biophys Res Commun. 1994 Jan 14;198(1):318-27. [PubMed Link Image]
  2. Park C, Jin UH, Lee YC, Cho TJ, Kim CH: Characterization of UDP-N-acetylglucosamine:alpha-6-d-mannoside beta-1,6-N-acetylglucosaminyltransferase V from a human hepatoma cell line Hep3B. Arch Biochem Biophys. 1999 Jul 15;367(2):281-8. [PubMed Link Image]
Enzyme 71 Metabolite References Not Available
Enzyme 72 [top]
Enzyme 72 ID 7045
Enzyme 72 Name UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
Enzyme 72 Synonyms
  1. O-GlcNAc transferase subunit p110
  2. O-linked N-acetylglucosamine transferase 110 kDa subunit
Enzyme 72 Gene Name OGT
Enzyme 72 Protein Sequence >UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
MASSVGNVADSTEPTKRMLSFQGLAELAHREYQAGDFEAAERHCMQLWRQEPDNTGVLLL
LSSIHFQCRRLDRSAHFSTLAIKQNPLLAEAYSNLGNVYKERGQLQEAIEHYRHALRLKP
DFIDGYINLAAALVAAGDMEGAVQAYVSALQYNPDLYCVRSDLGNLLKALGRLEEAKACY
LKAIETQPNFAVAWSNLGCVFNAQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARI
FDRAVAAYLRALSLSPNHAVVHGNLACVYYEQGLIDLAIDTYRRAIELQPHFPDAYCNLA
NALKEKGSVAEAEDCYNTALRLCPTHADSLNNLANIKREQGNIEEAVRLYRKALEVFPEF
AAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQCYTR
AIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVCDWT
DYDERMKKLVSIVADQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINVLHK
PPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDDGTN
FRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAPIQA
MWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKKKAV
IDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVIPMN
TIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGLPED
AIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQNRI
IFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAASQL
TCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELERLY
LQMWEHYAAGNKPDHMIKPVEVTESA
Enzyme 72 Number of Residues 1046
Enzyme 72 Molecular Weight 116923.5
Enzyme 72 Theoretical pI 6.68
Enzyme 72 GO Classification
Function
  • binding
Process
Component
Enzyme 72 General Function Involved in binding
Enzyme 72 Specific Function Addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Mediates the O-glycosylation of MLL5
Enzyme 72 Pathways Not Available
Enzyme 72 Reactions Not Available
Enzyme 72 Pfam Domain Function
Enzyme 72 Signals
  • None
Enzyme 72 Transmembrane Regions
  • None
Enzyme 72 Essentiality Not Available
Enzyme 72 GenBank ID Protein 18250915 Link Image
Enzyme 72 UniProtKB/Swiss-Prot ID O15294 Link Image
Enzyme 72 UniProtKB/Swiss-Prot Entry Name OGT1_HUMAN Link Image
Enzyme 72 PDB ID 1W3B Link Image
Enzyme 72 PDB File Show
Enzyme 72 3D Structure
Enzyme 72 Cellular Location Not Available
Enzyme 72 Gene Sequence >3141 bp
ATGGCGTCTTCCGTGGGCAACGTGGCCGACAGCACAGAACCAACGAAACGTATGCTTTCC
TTCCAAGGGTTAGCTGAGTTGGCACATCGAGAATATCAGGCAGGAGATTTTGAGGCAGCT
GAGAGACACTGCATGCAGCTCTGGAGACAAGAGCCAGACAATACTGGTGTGCTTTTATTA
CTTTCATCTATACACTTCCAGTGTCGAAGGCTGGACAGATCTGCTCACTTTAGCACTCTG
GCAATTAAACAGAACCCCCTTCTGGCAGAAGCTTATTCGAATTTGGGGAATGTGTACAAG
GAAAGAGGGCAGTTGCAGGAGGCAATTGAGCATTATCGACATGCATTGCGTCTCAAACCT
GATTTCATCGATGGTTATATTAACCTGGCAGCCGCCTTGGTAGCAGCGGGTGACATGGAA
GGGGCAGTACAAGCTTACGTCTCTGCTCTTCAGTACAATCCTGATTTGTACTGTGTTCGC
AGTGACCTGGGGAACCTGCTCAAAGCCCTGGGTCGCTTGGAAGAAGCCAAGGCATGTTAT
TTGAAAGCAATTGAGACGCAACCGAACTTTGCAGTAGCTTGGAGTAATCTTGGCTGTGTT
TTCAATGCACAAGGGGAAATTTGGCTTGCAATTCATCACTTTGAAAAGGCTGTCACCCTT
GACCCAAACTTTCTGGATGCTTATATCAATTTAGGAAATGTCTTGAAAGAGGCACGCATT
TTTGACAGAGCTGTGGCAGCTTATCTTCGTGCCCTAAGTTTGAGTCCAAATCACGCAGTG
GTGCACGGCAACCTGGCTTGTGTATACTATGAGCAAGGCCTGATAGATCTGGCAATAGAC
ACCTACAGGCGGGCTATCGAACTACAACCACATTTCCCTGATGCTTACTGCAACCTAGCC
AATGCTCTCAAAGAGAAGGGCAGTGTTGCTGAAGCAGAAGATTGTTATAATACAGCTCTC
CGTCTGTGTCCCACCCATGCAGACTCTCTGAATAACCTAGCCAATATCAAACGAGAACAG
GGAAACATTGAAGAGGCAGTTCGCTTGTATCGTAAAGCATTAGAAGTCTTCCCAGAGTTT
GCTGCTGCCCATTCAAATTTAGCAAGTGTACTGCAGCAGCAGGGAAAACTGCAGGAAGCT
CTGATGCATTATAAGGAGGCTATTCGAATCAGTCCTACCTTTGCTGATGCCTACTCTAAT
ATGGGAAACACTCTAAAGGAGATGCAGGATGTTCAGGGAGCCTTGCAGTGTTATACGCGT
GCCATCCAAATTAATCCTGCATTTGCAGATGCACATAGCAATCTGGCTTCCATTCATAAG
GATTCAGGGAATATTCCAGAAGCCATAGCTTCTTACCGCACGGCTCTGAAACTTAAGCCT
GATTTTCCTGATGCTTATTGTAACTTGGCTCATTGCCTGCAGATTGTCTGTGATTGGACA
GACTATGATGAGCGAATGAAGAAGTTGGTCAGTATTGTGGCTGACCAGTTAGAGAAGAAT
AGGTTGCCTTCTGTGCATCCTCATCATAGTATGCTATATCCTCTTTCTCATGGCTTCAGG
AAGGCTATTGCTGAGAGGCACGGCAACCTGTGCTTAGATAAGATTAATGTTCTTCATAAA
CCACCATATGAACATCCAAAAGACTTGAAGCTCAGTGATGGTCGGCTGCGTGTAGGATAT
GTGAGTTCCGACTTTGGGAATCATCCTACTTCTCACCTTATGCAGTCTATTCCAGGCATG
CACAATCCTGATAAATTTGAGGTGTTCTGTTATGCCCTGAGCCCAGACGATGGCACAAAC
TTCCGAGTGAAGGTGATGGCAGAAGCCAATCATTTCATTGATCTTTCTCAGATTCCATGC
AATGGAAAAGCAGCTGATCGCATCCATCAGGATGGAATTCATATCCTTGTAAATATGAAT
GGCTATACTAAGGGCGCTCGAAATGAGCTTTTTGCTCTCAGGCCAGCTCCTATTCAGGCA
ATGTGGCTGGGATACCCTGGGACGAGTGGTGCGCTTTTCATGGATTATATTATCACTGAT
CAGGAAACTTCGCCAGCTGAAGTTGCTGAGCAGTATTCCGAGAAATTGGCTTATATGCCC
CACACTTTTTTTATTGGTGATCATGCTAATATGTTCCCTCACCTGAAGAAAAAAGCAGTC
ATCGATTTTAAGTCCAATGGGCACATTTATGACAATCGGATAGTTCTGAATGGCATCGAC
CTCAAAGCATTTCTTGATAGTCTACCAGATGTGAAAATTGTCAAGATGAAGTGTCCTGAT
GGAGGAGACAATGCAGATAGCAGTAACACAGCTCTTAATATGCCTGTTATTCCTATGAAT
ACTATTGCAGAAGCAGTTATTGAAATGATTAACCGAGGACAGATTCAAATAACAATTAAT
GGATTCAGTATTAGCAATGGACTGGCAACTACTCAGATCAACAATAAGGCTGCAACTGGA
GAGGAGGTTCCCCGTACCATTATTGTAACCACCCGTTCTCAGTACGGGTTACCAGAAGAT
GCCATCGTATACTGTAACTTTAATCAGTTGTATAAAATTGACCCTTCTACTTTGCAGATG
TGGGCAAACATTCTGAAGCGTGTTCCCAATAGTGTACTCTGGCTGTTGCGTTTTCCAGCA
GTAGGAGAACCTAATATTCAACAGTATGCACAAAACATGGGCCTGCCCCAGAACCGTATC
ATTTTTTCACCTGTTGCTCCTAAAGAGGAACACGTCAGGAGAGGCCAGCTGGCTGATGTC
TGCTTGGACACTCCACTCTGTAATGGGCACACCACAGGGATGGATGTCCTCTGGGCAGGG
ACCCCCATGGTGACTATGCCAGGAGAGACTCTTGCTTCTCGAGTTGCAGCATCCCAGCTC
ACTTGCTTAGGTTGTCTTGAGCTTATTGCTAAAAACAGACAAGAATATGAAGACATAGCT
GTGAAGCTGGGAACTGATCTAGAATACCTGAAGAAAGTTCGTGGCAAAGTCTGGAAGCAA
AGAATATCTAGCCCTCTGTTCAACACCAAACAATACACAATGGAACTAGAGCGGCTCTAT
CTACAGATGTGGGAGCATTATGCAGCTGGCAACAAACCTGACCACATGATTAAGCCTGTT
GAAGTCACTGAGTCAGCATAA
Enzyme 72 GenBank Gene ID AJ315767 Link Image
Enzyme 72 GeneCard ID OGT Link Image
Enzyme 72 GenAtlas ID OGT Link Image
Enzyme 72 HGNC ID HGNC:8127 Link Image
Enzyme 72 Chromosome Location Not Available
Enzyme 72 Locus Not Available
Enzyme 72 SNPs SNPJam Report Link Image
Enzyme 72 General References
  1. Lubas WA, Frank DW, Krause M, Hanover JA: O-Linked GlcNAc transferase is a conserved nucleocytoplasmic protein containing tetratricopeptide repeats. J Biol Chem. 1997 Apr 4;272(14):9316-24. [PubMed Link Image]
  2. Nolte D, Muller U: Human O-GlcNAc transferase (OGT): genomic structure, analysis of splice variants, fine mapping in Xq13.1. Mamm Genome. 2002 Jan;13(1):62-4. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W: Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1. Genes Dev. 2003 Apr 1;17(7):896-911. [PubMed Link Image]
  6. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  8. Fujiki R, Chikanishi T, Hashiba W, Ito H, Takada I, Roeder RG, Kitagawa H, Kato S: GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis. Nature. 2009 May 21;459(7245):455-9. Epub 2009 Apr 19. [PubMed Link Image]
Enzyme 72 Metabolite References Not Available
Enzyme 73 [top]
Enzyme 73 ID 7046
Enzyme 73 Name Hyaluronan synthase 3
Enzyme 73 Synonyms
  1. Hyaluronate synthase 3
  2. Hyaluronic acid synthase 3
  3. HA synthase 3
Enzyme 73 Gene Name HAS3
Enzyme 73 Protein Sequence >Hyaluronan synthase 3
MPVQLTTALRVVGTSLFALAVLGGILAAYVTGYQFIHTEKHYLSFGLYGAILGLHLLIQS
LFAFLEHRRMRRAGQALKLPSPRRGSVALCIAAYQEDPDYLRKCLRSAQRISFPDLKVVM
VVDGNRQEDAYMLDIFHEVLGGTEQAGFFVWRSNFHEAGEGETEASLQEGMDRVRDVVRA
STFSCIMQKWGGKREVMYTAFKALGDSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGG
VGGDVQILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLE
DWYHQKFLGSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKS
YFREWLYNSLWFHKHHLWMTYESVVTGFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVG
IIKATYACFLRGNAEMIFMSLYSLLYMSSLLPAKIFAIATINKSGWGTSGRKTIVVNFIG
LIPVSIWVAVLLGGLAYTAYCQDLFSETELAFLVSGAILYGCYWVALLMLYLAIIARRCG
KKPEQYSLAFAEV
Enzyme 73 Number of Residues 553
Enzyme 73 Molecular Weight 62997.7
Enzyme 73 Theoretical pI 8.58
Enzyme 73 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
Enzyme 73 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 73 Specific Function Plays a role in hyaluronan/hyaluronic acid (HA) synthesis
Enzyme 73 Pathways Not Available
Enzyme 73 Reactions
  • (1) UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)- [nascent hyaluronan] = UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N- acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan] [RN:R05327 R06068]
  • (2) UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)- [nascent hyaluronan] = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta- D-glucuronosyl-(1->3)-[nascent hyaluronan]
Enzyme 73 Pfam Domain Function
Enzyme 73 Signals
  • None
Enzyme 73 Transmembrane Regions
  • 16-36 45-65 378-398 409-429 441-461 474-494 516-536
Enzyme 73 Essentiality Not Available
Enzyme 73 GenBank ID Protein 7110558 Link Image
Enzyme 73 UniProtKB/Swiss-Prot ID O00219 Link Image
Enzyme 73 UniProtKB/Swiss-Prot Entry Name HAS3_HUMAN Link Image
Enzyme 73 PDB ID Not Available
Enzyme 73 Cellular Location Not Available
Enzyme 73 Gene Sequence >1662 bp
ATGCCGGTGCAGCTGACGACAGCCCTGCGTGTGGTGGGCACCAGCCTGTTTGCCCTGGCA
GTGCTGGGTGGCATCCTGGCAGCCTATGTGACGGGCTACCAGTTCATCCACACGGAAAAG
CACTACCTGTCCTTCGGCCTGTACGGCGCCATCCTGGGCCTGCACCTGCTCATTCAGAGC
CTTTTTGCCTTCCTGGAGCACCGGCGCATGCGACGTGCCGGCCAGGCCCTGAAGCTGCCC
TCCCCGCGGCGGGGCTCGGTGGCACTGTGCATTGCCGCATACCAGGAGGACCCTGACTAC
TTGCGCAAGTGCCTGCGCTCGGCCCAGCGCATCTCCTTCCCTGACCTCAAGGTGGTCATG
GTGGTGGATGGCAACCGCCAGGAGGACGCCTACATGCTGGACATCTTCCACGAGGTGCTG
GGCGGCACCGAGCAGGCCGGCTTCTTTGTGTGGCGCAGCAACTTCCATGAGGCAGGCGAG
GGTGAGACGGAGGCCAGCCTGCAGGAGGGCATGGACCGTGTGCGGGATGTGGTGCGGGCC
AGCACCTTCTCGTGCATCATGCAGAAGTGGGGAGGCAAGCGCGAGGTCATGTACACGGCC
TTCAAGGCCCTCGGCGATTCGGTGGACTACATCCAGGTGTGCGACTCTGACACTGTGCTG
GATCCAGCCTGCACCATCGAGATGCTTCGAGTCCTGGAGGAGGATCCCCAAGTAGGGGGA
GTCGGGGGAGATGTCCAGATCCTCAACAAGTACGACTCATGGATTTCCTTCCTGAGCAGC
GTGCGGTACTGGATGGCCTTCAACGTGGAGCGGGCCTGCCAGTCCTACTTTGGCTGTGTG
CAGTGTATTAGTGGGCCCTTGGGCATGTACCGCAACAGCCTCCTCCAGCAGTTCCTGGAG
GACTGGTACCATCAGAAGTTCCTAGGCAGCAAGTGCAGCTTCGGGGATGACCGGCACCTC
ACCAACCGAGTCCTGAGCCTTGGCTACCGAACTAAGTATACCGCGCGCTCCAAGTGCCTC
ACAGAGACCCCCACTAAGTACCTCCGGTGGCTCAACCAGCAAACCCGCTGGAGCAAGTCT
TACTTCCGGGAGTGGCTCTACAACTCTCTGTGGTTCCATAAGCACCACCTCTGGATGACC
TACGAGTCAGTGGTCACGGGTTTCTTCCCCTTCTTCCTCATTGCCACGGTTATACAGCTT
TTCTACCGGGGCCGCATCTGGAACATTCTCCTCTTCCTGCTGACGGTGCAGCTGGTGGGC
ATTATCAAGGCCACCTACGCCTGCTTCCTTCGGGGCAATGCAGAGATGATCTTCATGTCC
CTCTACTCCCTCCTCTATATGTCCAGCCTTCTGCCGGCCAAGATCTTTGCCATTGCTACC
ATCAACAAATCTGGCTGGGGCACCTCTGGCCGAAAAACCATTGTGGTGAACTTCATTGGC
CTCATTCCTGTGTCCATCTGGGTGGCAGTTCTCCTGGAGGGGCTGGCCTACACAGCTTAT
TGCCAGGACCTGTTCAGTGAGACAGAGCTAGCCTTCCTTGTCTCTGGGGCTATACTGTAT
GGCTGCTACTGGGTGGCCCTCCTCATGCTATATCTGGCCATCATCGCCCGGCGATGTGGG
AAGAAGCCGGAGCAGTACAGCTTGGCTTTTGCTGAGGTGTGA
Enzyme 73 GenBank Gene ID AF232772 Link Image
Enzyme 73 GeneCard ID HAS3 Link Image
Enzyme 73 GenAtlas ID HAS3 Link Image
Enzyme 73 HGNC ID HGNC:4820 Link Image
Enzyme 73 Chromosome Location 1
Enzyme 73 Locus 16q22.1
Enzyme 73 SNPs SNPJam Report Link Image
Enzyme 73 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Spicer AP, Olson JS, McDonald JA: Molecular cloning and characterization of a cDNA encoding the third putative mammalian hyaluronan synthase. J Biol Chem. 1997 Apr 4;272(14):8957-61. [PubMed Link Image]
Enzyme 73 Metabolite References Not Available
Enzyme 74 [top]
Enzyme 74 ID 7047
Enzyme 74 Name Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
Enzyme 74 Synonyms
  1. N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase III
  2. GNT-III
  3. GlcNAc-T III
  4. N-acetylglucosaminyltransferase III
Enzyme 74 Gene Name MGAT3
Enzyme 74 Protein Sequence >Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
MKMRRYKLFLMFCMAGLCLISFLHFFKTLSYVTFPRELASLSPNLVSSFFWNNAPVTPQA
SPEPGGPDLLRTPLYSHSPLLQPLPPSKAAEELHRVDLVLPEDTTEYFVRTKAGGVCFKP
GTKMLERPPPGRPEEKPEGANGSSARRPPRYLLSARERTGGRGARRKWVECVCLPGWHGP
SCGVPTVVQYSNLPTKERLVPREVPRRVINAINVNHEFDLLDVRFHELGDVVDAFVVCES
NFTAYGEPRPLKFREMLTNGTFEYIRHKVLYVFLDHFPPGGRQDGWIADDYLRTFLTQDG
VSRLRNLRPDDVFIIDDADEIPARDGVLFLKLYDGWTEPFAFHMRKSLYGFFWKQPGTLE
VVSGCTVDMLQAVYGLDGIRLRRRQYYTMPNFRQYENRTGHILVQWSLGSPLHFAGWHCS
WCFTPEGIYFKLVSAQNGDFPRWGDYEDKRDLNYIRGLIRTGGWFDGTQQEYPPADPSEH
MYAPKYLLKNYDRFHYLLDNPYQEPRSTAAGGWRHRGPEGRPPARGKLDEAEV
Enzyme 74 Number of Residues 533
Enzyme 74 Molecular Weight 61312.5
Enzyme 74 Theoretical pI 8.37
Enzyme 74 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • beta-1,4-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid N-linked glycosylation
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 74 General Function Involved in beta-1,4-mannosylglycoprotein 4-beta-N-acet
Enzyme 74 Specific Function It is involved in the regulation of the biosynthesis and biological function of glycoprotein oligosaccharides. Catalyzes the addition of N-acetylglucosamine in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-linked sugar chains. It is one of the most important enzymes involved in the regulation of the biosynthesis of glycoprotein oligosaccharides
Enzyme 74 Pathways
Enzyme 74 Reactions
  • UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R = UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R [RN:R07259]
Enzyme 74 Pfam Domain Function
Enzyme 74 Signals
  • None
Enzyme 74 Transmembrane Regions
  • 8-23
Enzyme 74 Essentiality Not Available
Enzyme 74 GenBank ID Protein 56202888 Link Image
Enzyme 74 UniProtKB/Swiss-Prot ID Q09327 Link Image
Enzyme 74 UniProtKB/Swiss-Prot Entry Name MGAT3_HUMAN Link Image
Enzyme 74 PDB ID Not Available
Enzyme 74 Cellular Location Not Available
Enzyme 74 Gene Sequence >1602 bp
ATGAAGATGAGACGCTACAAGCTCTTTCTCATGTTCTGTATGGCCGGCCTGTGCCTCATC
TCCTTCCTGCACTTCTTCAAGACCCTGTCCTATGTCACCTTCCCCCGAGAACTGGCCTCC
CTCAGCCCTAACCTGGTGTCCAGCTTTTTCTGGAACAATGCCCCGGTCACGCCCCAGGCC
AGCCCCGAGCCAGGAGGCCCTGACCTGCTGCGTACCCCACTCTACTCCCACTCGCCCCTG
CTGCAGCCGCTGCCGCCCAGCAAGGCGGCCGAGGAGCTCCACCGGGTGGACTTGGTGCTG
CCCGAGGACACCACCGAGTATTTCGTGCGCACCAAGGCCGGCGGCGTCTGCTTCAAACCC
GGCACCAAGATGCTGGAGAGGCCGCCCCCGGGACGGCCGGAGGAGAAGCCTGAGGGGGCC
AACGGCTCCTCGGCCCGGCGGCCACCCCGGTACCTCCTGAGCGCCCGGGAGCGCACGGGG
GGCCGAGGCGCCCGGCGCAAGTGGGTGGAGTGCGTGTGCCTGCCCGGCTGGCACGGACCC
AGCTGCGGCGTGCCCACTGTGGTGCAGTACTCCAACCTGCCCACCAAGGAGCGGCTGGTG
CCCAGGGAGGTGCCGCGCCGCGTCATCAACGCCATCAACGTCAACCACGAGTTCGACCTG
CTGGACGTGCGCTTCCACGAGCTGGGCGACGTGGTGGACGCCTTTGTGGTGTGCGAGTCC
AACTTCACGGCTTATGGGGAGCCGCGGCCGCTCAAGTTCCGGGAGATGCTGACCAATGGC
ACCTTCGAGTACATCCGCCACAAGGTGCTCTATGTCTTCCTGGACCACTTCCCGCCCGGC
GGCCGGCAGGACGGCTGGATCGCCGACGACTACCTGCGCACCTTCCTCACCCAGGACGGC
GTCTCGCGGCTGCGCAACCTGCGGCCCGACGACGTCTTCATCATTGACGATGCGGACGAG
ATCCCGGCCCGTGACGGCGTCCTTTTCCTCAAGCTCTACGATGGCTGGACCGAGCCCTTC
GCCTTCCACATGCGCAAGTCGCTCTACGGCTTCTTCTGGAAGCAGCCGGGCACCCTGGAG
GTGGTGTCAGGCTGCACGGTGGACATGCTGCAGGCAGTGTATGGGCTGGACGGCATCCGC
CTGCGCCGCCGCCAGTACTACACCATGCCCAACTTCAGACAGTATGAGAACCGCACCGGC
CACATCCTGGTGCAGTGGTCGCTGGGCAGCCCCCTGCACTTCGCCGGCTGGCACTGCTCC
TGGTGCTTCACGCCCGAGGGCATCTACTTCAAGCTCGTGTCCGCCCAGAATGGCGACTTC
CCACGCTGGGGTGACTACGAGGACAAGCGGGACCTGAACTACATCCGCGGCCTGATCCGC
ACCGGGGGCTGGTTCGACGGCACGCAGCAGGAGTACCCGCCTGCAGACCCCAGCGAGCAC
ATGTATGCGCCCAAGTACCTGCTGAAGAACTACGACCGGTTCCACTACCTGCTGGACAAC
CCCTACCAGGAGCCCAGGAGCACGGCGGCGGGCGGGTGGCGCCACAGGGGTCCCGAGGGA
AGGCCGCCCGCCCGGGGCAAACTGGACGAGGCGGAAGTCTAG
Enzyme 74 GenBank Gene ID AL022312 Link Image
Enzyme 74 GeneCard ID MGAT3 Link Image
Enzyme 74 GenAtlas ID Not Available
Enzyme 74 HGNC ID Not Available
Enzyme 74 Chromosome Location 2
Enzyme 74 Locus 22q13.1
Enzyme 74 SNPs SNPJam Report Link Image
Enzyme 74 General References
  1. Ihara Y, Nishikawa A, Tohma T, Soejima H, Niikawa N, Taniguchi N: cDNA cloning, expression, and chromosomal localization of human N-acetylglucosaminyltransferase III (GnT-III). J Biochem (Tokyo). 1993 Jun;113(6):692-8. [PubMed Link Image]
  2. Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed Link Image]
  3. Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 74 Metabolite References Not Available
Enzyme 75 [top]
Enzyme 75 ID 7269
Enzyme 75 Name Hyaluronan synthase 2
Enzyme 75 Synonyms
  1. Hyaluronate synthase 2
  2. Hyaluronic acid synthase 2
  3. HA synthase 2
Enzyme 75 Gene Name HAS2
Enzyme 75 Protein Sequence >Hyaluronan synthase 2
MHCERFLCILRIIGTTLFGVSLLLGITAAYIVGYQFIQTDNYYFSFGLYGAFLASHLIIQ
SLFAFLEHRKMKKSLETPIKLNKTVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKVVMVI
DGNSEDDLYMMDIFSEVMGRDKSATYIWKNNFHEKGPGETDESHKESSQHVTQLVLSNKS
ICIMQKWGGKREVMYTAFRALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGG
DVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWY
NQEFMGNQCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFR
EWLYNAMWFHKHHLWMTYEAIITGFFPFFLIATVIQLFYRGKIWNILLFLLTVQLVGLIK
SSFASCLRGNIVMVFMSLYSVLYMSSLLPAKMFAIATINKAGWGTSGRKTIVVNFIGLIP
VSVWFTILLGGVIFTIYKESKRPFSESKQTVLIVGTLLYACYWVMLLTLYVVLINKCGRR
KKGQQYDMVLDV
Enzyme 75 Number of Residues 552
Enzyme 75 Molecular Weight 63565.8
Enzyme 75 Theoretical pI 8.74
Enzyme 75 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
Enzyme 75 General Function Cell wall/membrane/envelope biogenesis
Enzyme 75 Specific Function Plays a role in hyaluronan/hyaluronic acid (HA) synthesis
Enzyme 75 Pathways Not Available
Enzyme 75 Reactions
  • (1) UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)- [nascent hyaluronan] = UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N- acetyl-beta-D-glucosaminyl-(1->4)-[nascent hyaluronan] [RN:R05327 R06068]
  • (2) UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)- [nascent hyaluronan] = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta- D-glucuronosyl-(1->3)-[nascent hyaluronan]
Enzyme 75 Pfam Domain Function
Enzyme 75 Signals
  • None
Enzyme 75 Transmembrane Regions
  • 12-32 46-66 375-395 403-423 430-450 476-496 511-531
Enzyme 75 Essentiality Not Available
Enzyme 75 GenBank ID Protein 46854837 Link Image
Enzyme 75 UniProtKB/Swiss-Prot ID Q92819 Link Image
Enzyme 75 UniProtKB/Swiss-Prot Entry Name HAS2_HUMAN Link Image
Enzyme 75 PDB ID Not Available
Enzyme 75 Cellular Location Not Available
Enzyme 75 Gene Sequence >1659 bp
ATGCATTGTGAGAGGTTTCTATGTATCCTGAGAATAATTGGAACCACACTCTTTGGAGTC
TCTCTCCTCCTTGGAATCACAGCTGCTTATATTGTTGGCTACCAGTTTATCCAAACGGAT
AATTACTATTTCTCTTTTGGACTGTATGGTGCCTTTTTGGCATCACACCTCATCATCCAA
AGCCTGTTTGCCTTTTTGGAGCACCGAAAAATGAAAAAATCCCTAGAAACCCCCATAAAG
TTGAACAAAACAGTTGCCCTTTGCATCGCTGCCTATCAAGAAGATCCAGACTACTTAAGG
AAATGTTTGCAATCTGTGAAAAGGCTAACCTACCCTGGGATTAAAGTTGTCATGGTCATA
GATGGGAACTCAGAAGATGACCTTTACATGATGGACATCTTCAGTGAAGTCATGGGCAGA
GACAAATCAGCCACTTATATCTGGAAGAACAACTTCCACGAAAAGGGTCCCGGTGAGACA
GATGAGTCACATAAAGAAAGCTCGCAACACGTAACGCAATTGGTCTTGTCCAACAAAAGT
ATCTGCATCATGCAAAAATGGGGTGGAAAAAGAGAAGTCATGTACACAGCCTTCAGAGCA
CTGGGACGAAGTGTGGATTATGTACAGGTTTGTGATTCAGACACTATGCTTGACCCAGCC
TCATCTGTGGAGATGGTAAAAGTTTTAGAAGAAGATCCCATGGTTGGAGGTGTTGGGGGA
GATGTCCAGATTTTAAACAAGTACGATTCCTGGATCTCATTCCTCAGCAGTGTAAGATAT
TGGATGGCTTTTAATATAGAAAGGGCCTGTCAGTCTTATTTTGGGTGTGTTCAGTGCATT
AGTGGACCTCTGGGAATGTACAGAAACTCCTTGTTGCATGAGTTTGTGGAAGATTGGTAC
AATCAAGAATTTATGGGCAACCAATGTAGCTTTGGTGATGACAGGCATCTCACGAACCGG
GTGCTGAGCCTGGGCTATGCAACAAAATACACAGCTCGATCTAAGTGCCTTACTGAAACA
CCTATAGAATATCTCAGATGGCTAAACCAGCAGACCCGTTGGAGCAAGTCCTACTTCCGA
GAATGGCTGTACAATGCAATGTGGTTTCACAAACATCACTTGTGGATGACCTACGAAGCG
ATTATCACTGGATTCTTTCCTTTCTTTCTCATTGCCACAGTAATCCAGCTCTTCTACCGG
GGTAAAATTTGGAACATTCTCCTCTTCTTGTTAACTGTCCAGCTAGTAGGTCTCATAAAA
TCATCTTTTGCCAGCTGCCTTAGAGGAAATATCGTCATGGTCTTCATGTCTCTCTACTCA
GTGTTATACATGTCGAGTTTACTTCCCGCCAAGATGTTTGCAATTGCAACAATAAACAAA
GCTGGGTGGGGCACATCAGGAAGGAAAACCATTGTTGTTAATTTCATAGGACTCATTCCA
GTATCAGTTTGGTTTACAATCCTCCTGGGTGGTGTGATTTTCACCATTTATAAGGAGTCT
AAAAGGCCATTTTCAGAATCCAAACAGACAGTTCTAATTGTTGGAACGTTGCTCTATGCA
TGCTATTGGGTCATGCTTTTGACGCTGTATGTAGTTCTCATCAATAAGTGTGGCAGGCGG
AAGAAGGGACAACAATATGACATGGTGCTTGATGTATGA
Enzyme 75 GenBank Gene ID BC069353 Link Image
Enzyme 75 GeneCard ID HAS2 Link Image
Enzyme 75 GenAtlas ID Not Available
Enzyme 75 HGNC ID Not Available
Enzyme 75 Chromosome Location 8
Enzyme 75 Locus 8q24.12
Enzyme 75 SNPs SNPJam Report Link Image
Enzyme 75 General References
  1. Watanabe K, Yamaguchi Y: Molecular identification of a putative human hyaluronan synthase. J Biol Chem. 1996 Sep 20;271(38):22945-8. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Morerio C, Rapella A, Rosanda C, Tassano E, Gambini C, Romagnoli G, Panarello C: PLAG1-HAS2 fusion in lipoblastoma with masked 8q intrachromosomal rearrangement. Cancer Genet Cytogenet. 2005 Jan 15;156(2):183-4. [PubMed Link Image]
Enzyme 75 Metabolite References Not Available
Enzyme 76 [top]
Enzyme 76 ID 8075
Enzyme 76 Name Uridine-cytidine kinase 2
Enzyme 76 Synonyms
  1. UCK 2
  2. Cytidine monophosphokinase 2
  3. Testis-specific protein TSA903
  4. Uridine monophosphokinase 2
Enzyme 76 Gene Name UCK2
Enzyme 76 Protein Sequence >Uridine-cytidine kinase 2
MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILS
QDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRK
EETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQ
ILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNG
CLNGYTPSRKRQASESSSRPH
Enzyme 76 Number of Residues 261
Enzyme 76 Molecular Weight 29298.9
Enzyme 76 Theoretical pI 6.68
Enzyme 76 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
Component
Enzyme 76 General Function Involved in ATP binding
Enzyme 76 Specific Function Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4- thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)- benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5- methylcytidine, and N(4)-anisoylcytidine
Enzyme 76 Pathways
Enzyme 76 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964]
Enzyme 76 Pfam Domain Function
Enzyme 76 Signals
  • None
Enzyme 76 Transmembrane Regions
  • None
Enzyme 76 Essentiality Not Available
Enzyme 76 GenBank ID Protein 18699734 Link Image
Enzyme 76 UniProtKB/Swiss-Prot ID Q9BZX2 Link Image
Enzyme 76 UniProtKB/Swiss-Prot Entry Name UCK2_HUMAN Link Image
Enzyme 76 PDB ID 1XRJ Link Image
Enzyme 76 PDB File Show
Enzyme 76 3D Structure
Enzyme 76 Cellular Location Not Available
Enzyme 76 Gene Sequence >786 bp
ATGGCCGGGGACAGCGAGCAGACCCTGCAGAACCACCAGCAGCCCAACGGCGGCGAGCCC
TTCCTTATAGGCGTCAGCGGGGGAACAGCTAGCGGCAAGTCTTCCGTGTGTGCTAAGATC
GTGCAGCTCCTGGGGCAGAATGAGGTGGACTATCGCCAGAAGCAGGTGGTCATCCTGAGC
CAGGATAGCTTCTACCGTGTCCTTACCTCGGAGCAGAAGGCCAAAGCCCTGAAGGGCCAG
TTCAACTTTGACCACCCGGATGCCTTTGACAATGAACTCATTCTCAAAACACTCAAAGAA
ATCACTGAAGGGAAAACAGTCCAGATCCCCGTGTATGACTTTGTCTCCCATTCCCGGAAG
GAGGAGACAGTTACTGTCTATCCCGCAGACGTGGTGCTCTTTGAAGGGATCCTGGCCTTC
TACTCCCAGGAGGTACGAGACCTGTTCCAGATGAAGCTTTTTGTGGATACAGATGCGGAC
ACCCGGCTCTCACGCAGAGTATTAAGGGACATCAGCGAGAGAGGCAGGGATCTTGAGCAG
ATTTTATCTCAGTACATTACGTTCGTCAAGCCTGCCTTTGAGGAATTCTGCTTGCCAACA
AAGAAGTATGCTGATGTGATCATCCCTAGAGGTGCAGATAATCTGGTGGCCATCAACCTC
ATCGTGCAGCACATCCAGGACATCCTGAATGGAGGGCCCTCCAAACGGCAGACCAATGGC
TGTCTCAACGGCTACACCCCTTCACGCAAGAGGCAGGCATCGGAGTCCAGCAGCAGGCCG
CATTGA
Enzyme 76 GenBank Gene ID NM_012474.3 Link Image
Enzyme 76 GeneCard ID UCK2 Link Image
Enzyme 76 GenAtlas ID UCK2 Link Image
Enzyme 76 HGNC ID HGNC:12562 Link Image
Enzyme 76 Chromosome Location 1
Enzyme 76 Locus 1q23
Enzyme 76 SNPs SNPJam Report Link Image
Enzyme 76 General References
  1. Ozaki K, Kuroki T, Hayashi S, Nakamura Y: Isolation of three testis-specific genes (TSA303, TSA806, TSA903) by a differential mRNA display method. Genomics. 1996 Sep 1;36(2):316-9. [PubMed Link Image]
  2. Van Rompay AR, Norda A, Linden K, Johansson M, Karlsson A: Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases. Mol Pharmacol. 2001 May;59(5):1181-6. [PubMed Link Image]
  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Koizumi K, Shimamoto Y, Azuma A, Wataya Y, Matsuda A, Sasaki T, Fukushima M: Cloning and expression of uridine/cytidine kinase cDNA from human fibrosarcoma cells. Int J Mol Med. 2001 Sep;8(3):273-8. [PubMed Link Image]
  6. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed Link Image]
  8. Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F: Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase. Structure. 2004 May;12(5):751-64. [PubMed Link Image]
  9. Appleby TC, Larson G, Cheney IW, Walker H, Wu JZ, Zhong W, Hong Z, Yao N: Structure of human uridine-cytidine kinase 2 determined by SIRAS using a rotating-anode X-ray generator and a single samarium derivative. Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):278-84. Epub 2005 Feb 24. [PubMed Link Image]
Enzyme 76 Metabolite References Not Available
Enzyme 77 [top]
Enzyme 77 ID 8392
Enzyme 77 Name N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase, isoform B
Enzyme 77 Synonyms
  1. N-acetylglucosaminyltransferase
  2. I-branching enzyme
  3. IGNT
Enzyme 77 Gene Name GCNT2
Enzyme 77 Protein Sequence >N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase, isoform B
MPLSMRYLFIISVSSVIIFIVFSVFNFGGDPSFQRLNISDPLRLTQVCTSFINGKTRFLW
KNKLMIHEKSSCKEYLTQSHYITAPLSKEEADFPLAYIMVIHHHFDTFARLFRAIYMPQN
IYCVHVDEKATTEFKDAVEQLLSCFPNAFLASKMEPVVYGGISRLQADLNCIRDLSAFEV
SWKYVINTCGQDFPLKTNKEIVQYLKGFKGKNITPGVLPPAHAIGRTKYVHQEHLGKELS
YVIRTTALKPPPPHNLTIYFGSAYVALSREFANFVLHDPRAVDLLQWSKDTFSPDEHFWV
TLNRIPGVPGSMPNASWTGNLRAIKWSDMEDRHGGCHGHYVHGICIYGNGDLKWLVNSPS
LFANKFELNTYPLTVECLELRHRERTLNQSETAIQPSWYF
Enzyme 77 Number of Residues 400
Enzyme 77 Molecular Weight 45854.4
Enzyme 77 Theoretical pI 8.32
Enzyme 77 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
Component
  • cell part
  • membrane
Enzyme 77 General Function Involved in acetylglucosaminyltransferase activity
Enzyme 77 Specific Function Branching enzyme that converts linear into branched poly-N-acetyllactosaminoglycans. Introduces the blood group I antigen during embryonic development. It is closely associated with the development and maturation of erythroid cells. The expression of the blood group I antigen in erythrocytes is determined by isoform C
Enzyme 77 Pathways
  • Blood group glycolipid biosynthesis-neolactoseries (map00602 Link Image)
Enzyme 77 Reactions
  • UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-(1->6)-beta-D-galactosyl-(1->4)-N- acetyl-D-glucosaminyl-R [RN:R02790]
Enzyme 77 Pfam Domain Function
Enzyme 77 Signals
  • None
Enzyme 77 Transmembrane Regions
  • 7-25
Enzyme 77 Essentiality Not Available
Enzyme 77 GenBank ID Protein 21667009 Link Image
Enzyme 77 UniProtKB/Swiss-Prot ID Q06430 Link Image
Enzyme 77 UniProtKB/Swiss-Prot Entry Name GNT2B_HUMAN Link Image
Enzyme 77 PDB ID Not Available
Enzyme 77 Cellular Location Not Available
Enzyme 77 Gene Sequence >1203 bp
ATGCCTTTATCAATGCGTTACCTCTTCATAATTTCTGTCTCTAGTGTAATTATTTTTATC
GTCTTCTCTGTGTTCAATTTTGGGGGAGATCCAAGCTTCCAAAGGCTAAATATCTCAGAC
CCTTTGAGGCTGACTCAAGTTTGCACATCTTTTATCAATGGAAAAACACGTTTCCTGTGG
AAAAACAAACTAATGATCCATGAGAAGTCTTCTTGCAAGGAATACTTGACCCAGAGCCAC
TACATCACAGCCCCTTTATCTAAGGAAGAAGCTGACTTTCCCTTGGCATATATAATGGTC
ATCCATCATCACTTTGACACCTTTGCAAGGCTCTTCAGGGCTATTTACATGCCCCAAAAT
ATCTACTGTGTTCATGTGGATGAAAAAGCAACAACTGAATTTAAAGATGCGGTAGAGCAA
CTATTAAGCTGCTTCCCAAACGCTTTTCTGGCTTCCAAGATGGAACCCGTTGTCTATGGA
GGGATCTCCAGGCTCCAGGCTGACCTGAACTGCATCAGAGATCTTTCTGCCTTCGAGGTC
TCATGGAAGTACGTTATCAACACCTGTGGGCAAGACTTCCCCCTGAAAACCAACAAGGAA
ATAGTTCAGTATCTGAAAGGATTTAAAGGTAAAAATATCACCCCAGGGGTGCTGCCCCCA
GCTCATGCAATTGGACGGACTAAATATGTCCACCAAGAGCACCTGGGCAAAGAGCTTTCC
TATGTGATAAGAACAACAGCGTTGAAACCGCCTCCCCCCCATAATCTCACAATTTACTTT
GGCTCTGCCTATGTGGCTCTATCAAGAGAGTTTGCCAACTTTGTTCTGCATGACCCACGG
GCTGTTGATTTGCTCCAGTGGTCCAAGGACACTTTCAGTCCTGATGAGCATTTCTGGGTG
ACACTCAATAGGATTCCAGGTGTTCCTGGCTCTATGCCAAATGCATCCTGGACTGGAAAC
CTCAGAGCTATAAAGTGGAGTGACATGGAAGACAGACACGGAGGCTGCCACGGCCACTAT
GTACATGGTATTTGTATCTATGGAAACGGAGACTTAAAGTGGCTGGTTAATTCACCAAGC
CTGTTTGCTAACAAGTTTGAGCTTAATACCTACCCCCTTACTGTGGAATGCCTAGAACTG
AGGCATCGCGAAAGAACCCTCAATCAGAGTGAAACTGCGATACAACCCAGCTGGTATTTT
TGA
Enzyme 77 GenBank Gene ID AF458025 Link Image
Enzyme 77 GeneCard ID GCNT2 Link Image
Enzyme 77 GenAtlas ID GCNT2 Link Image
Enzyme 77 HGNC ID HGNC:4204 Link Image
Enzyme 77 Chromosome Location 6
Enzyme 77 Locus 6p24.2
Enzyme 77 SNPs SNPJam Report Link Image
Enzyme 77 General References
  1. Bierhuizen MF, Mattei MG, Fukuda M: Expression of the developmental I antigen by a cloned human cDNA encoding a member of a beta-1,6-N-acetylglucosaminyltransferase gene family. Genes Dev. 1993 Mar;7(3):468-78. [PubMed Link Image]
  2. Bierhuizen MF, Maemura K, Kudo S, Fukuda M: Genomic organization of core 2 and I branching beta-1,6-N-acetylglucosaminyltransferases. Implication for evolution of the beta-1,6-N-acetylglucosaminyltransferase gene family. Glycobiology. 1995 Jun;5(4):417-25. [PubMed Link Image]
  3. Yu LC, Twu YC, Chou ML, Reid ME, Gray AR, Moulds JM, Chang CY, Lin M: The molecular genetics of the human I locus and molecular background explain the partial association of the adult i phenotype with congenital cataracts. Blood. 2003 Mar 15;101(6):2081-8. Epub 2002 Nov 7. [PubMed Link Image]
  4. Zhang T, Haws P, Wu Q: Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation. Genome Res. 2004 Jan;14(1):79-89. Epub 2003 Dec 12. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  6. 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]
  7. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  8. Sasaki K, Kurata-Miura K, Ujita M, Angata K, Nakagawa S, Sekine S, Nishi T, Fukuda M: Expression cloning of cDNA encoding a human beta-1,3-N-acetylglucosaminyltransferase that is essential for poly-N-acetyllactosamine synthesis. Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14294-9. [PubMed Link Image]
Enzyme 77 Metabolite References Not Available
Enzyme 78 [top]
Enzyme 78 ID 8476
Enzyme 78 Name Chondroitin sulfate glucuronyltransferase
Enzyme 78 Synonyms
  1. CSGlcA-T
  2. Chondroitin glucuronyltransferase
  3. Chondroitin polymerizing factor 2
  4. ChPF-2
  5. Chondroitin synthase 3
  6. ChSy-3
  7. N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase
Enzyme 78 Gene Name CHPF2
Enzyme 78 Protein Sequence >Chondroitin sulfate glucuronyltransferase
MRLSSLLALLRPALPLILGLSLGCSLSLLRVSWIQGEGEDPCVEAVGERGGPQNPDSRAR
LDQSDEDFKPRIVPYYRDPNKPYKKVLRTRYIQTELGSRERLLVAVLTSRATLSTLAVAV
NRTVAHHFPRLLYFTGQRGARAPAGMQVVSHGDERPAWLMSETLRHLHTHFGADYDWFFI
MQDDTYVQAPRLAALAGHLSINQDLYLGRAEEFIGAGEQARYCHGGFGYLLSRSLLLRLR
PHLDGCRGDILSARPDEWLGRCLIDSLGVGCVSQHQGQQYRSFELAKNRDPEKEGSSAFL
SAFAVHPVSEGTLMYRLHKRFSALELERAYSEIEQLQAQIRNLTVLTPEGEAGLSWPVGL
PAPFTPHSRFEVLGWDYFTEQHTFSCADGAPKCPLQGASRADVGDALETALEQLNRRYQP
RLRFQKQRLLNGYRRFDPARGMEYTLDLLLECVTQRGHRRALARRVSLLRPLSRVEILPM
PYVTEATRVQLVLPLLVAEAAAAPAFLEAFAANVLEPREHALLTLLLVYGPREGGRGAPD
PFLGVKAAAAELERRYPGTRLAWLAVRAEAPSQVRLMDVVSKKHPVDTLFFLTTVWTRPG
PEVLNRCRMNAISGWQAFFPVHFQEFNPALSPQRSPPGPPGAGPDPPSPPGADPSRGAPI
GGRFDRQASAEGCFYNADYLAARARLAGELAGQEEEEALEGLEVMDVFLRFSGLHLFRAV
EPGLVQKFSLRDCSPRLSEELYHRCRLSNLEGLGGRAQLAMALFEQEQANST
Enzyme 78 Number of Residues 772
Enzyme 78 Molecular Weight 85947.2
Enzyme 78 Theoretical pI 7.88
Enzyme 78 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • Golgi cisterna membrane
  • Golgi membrane
  • cell part
  • membrane
  • organelle membrane
Enzyme 78 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 78 Specific Function Transfers glucuronic acid (GlcUA) from UDP-GlcUA to N- acetylgalactosamine residues on the non-reducing end of the elongating chondroitin polymer. Has no N- acetylgalactosaminyltransferase activity
Enzyme 78 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 78 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 [RN:R07336]
Enzyme 78 Pfam Domain Function
Enzyme 78 Signals
  • None
Enzyme 78 Transmembrane Regions
  • 7-29
Enzyme 78 Essentiality Not Available
Enzyme 78 GenBank ID Protein Not Available
Enzyme 78 UniProtKB/Swiss-Prot ID Q9P2E5 Link Image
Enzyme 78 UniProtKB/Swiss-Prot Entry Name CHPF2_HUMAN Link Image
Enzyme 78 PDB ID Not Available
Enzyme 78 Cellular Location Not Available
Enzyme 78 Gene Sequence >2319 bp
ATGCGACTGAGCTCCCTGTTGGCTCTGCTGCGGCCAGCGCTTCCCCTCATCTTAGGGCTG
TCTCTGGGGTGCAGCCTGAGCCTCCTGCGGGTTTCCTGGATCCAGGGGGAGGGAGAAGAT
CCCTGTGTCGAGGCTGTAGGGGAGCGAGGAGGGCCACAGAATCCAGATTCCAGAGCTCGG
CTAGACCAAAGTGATGAAGACTTCAAACCCCGGATTGTCCCCTACTACAGGGACCCCAAC
AAGCCCTACAAGAAGGTGCTCAGGACTCGGTACATCCAGACAGAGCTGGGCTCCCGTGAG
CGGTTGCTGGTGGCTGTCCTGACCTCCCGAGCTACACTGTCCACTTTGGCCGTGGCTGTG
AACCGTACGGTGGCCCATCACTTCCCTCGGTTACTCTACTTCACTGGGCAGCGGGGGGCC
CGGGCTCCAGCAGGGATGCAGGTGGTGTCTCATGGGGATGAGCGGCCCGCCTGGCTCATG
TCAGAGACCCTGCGCCACCTTCACACACACTTTGGGGCCGACTACGACTGGTTCTTCATC
ATGCAGGATGACACATATGTGCAGGCCCCCCGCCTGGCAGCCCTTGCTGGCCACCTCAGC
ATCAACCAAGACCTGTACTTAGGCCGGGCAGAGGAGTTCATTGGCGCAGGCGAGCAGGCC
CGGTACTGTCATGGGGGCTTTGGCTACCTGTTGTCACGGAGTCTCCTGCTTCGTCTGCGG
CCACATCTGGATGGCTGCCGAGGAGACATTCTCAGTGCCCGTCCTGACGAGTGGCTTGGA
CGCTGCCTCATTGACTCTCTGGGCGTCGGCTGTGTCTCACAGCACCAGGGGCAGCAGTAT
CGCTCATTTGAACTGGCCAAAAATAGGGACCCTGAGAAGGAAGGGAGCTCGGCTTTCCTG
AGTGCCTTCGCCGTGCACCCTGTCTCCGAAGGTACCCTCATGTACCGGCTCCACAAACGC
TTCAGCGCTCTGGAGTTGGAGCGGGCTTACAGTGAAATAGAACAACTGCAGGCTCAGATC
CGGAACCTGACCGTGCTGACCCCCGAAGGGGAGGCAGGGCTGAGCTGGCCCGTTGGGCTC
CCTGCTCCTTTCACACCACACTCTCGCTTTGAGGTGCTGGGCTGGGACTACTTCACAGAG
CAGCACACCTTCTCCTGTGCAGATGGGGCTCCCAAGTGCCCACTACAGGGGGCTAGCAGG
GCGGACGTGGGTGATGCGTTGGAGACTGCCCTGGAGCAGCTCAATCGGCGCTATCAGCCC
CGCCTGCGCTTCCAGAAGCAGCGACTGCTCAACGGCTATCGGCGCTTCGACCCAGCACGG
GGCATGGAGTACACCCTGGACCTGCTGTTGGAATGTGTGACACAGCGTGGGCACCGGCGG
GCCCTGGCTCGCAGGGTCAGCCTGCTGCGGCCACTGAGCCGGGTGGAAATCCTACCTATG
CCCTATGTCACTGAGGCCACCCGAGTGCAGCTGGTGCTGCCACTCCTGGTGGCTGAAGCT
GCTGCAGCCCCGGCTTTCCTCGAGGCCTTTGCAGCCAATGTCCTGGAGCCACGAGAACAT
GCATTGCTCACCCTGTTGCTGGTCTACGGGCCACGAGAAGGTGGCCGTGGAGCTCCAGAC
CCATTTCTTGGGGTGAAGGCTGCAGCAGCGGAGTTAGAGCGACGGTACCCTGGGACGAGG
CTGGCCTGGCTCGCTGTGCGAGCAGAGGCCCCTTCCCAGGTGCGACTCATGGACGTGGTC
TCGAAGAAGCACCCTGTGGACACTCTCTTCTTCCTTACCACCGTGTGGACAAGGCCTGGG
CCCGAAGTCCTCAACCGCTGTCGCATGAATGCCATCTCTGGCTGGCAGGCCTTCTTTCCA
GTCCATTTCCAGGAGTTCAATCCTGCCCTGTCACCACAGAGATCACCCCCAGGGCCCCCG
GGGGCTGGCCCTGACCCCCCCTCCCCTCCTGGTGCTGACCCCTCCCGGGGGGCTCCTATA
GGGGGGAGATTTGACCGGCAGGCTTCTGCGGAGGGCTGCTTCTACAACGCTGACTACCTG
GCGGCCCGAGCCCGGCTGGCAGGTGAACTGGCAGGCCAGGAAGAGGAGGAAGCCCTGGAG
GGGCTGGAGGTGATGGATGTTTTCCTCCGGTTCTCAGGGCTCCACCTCTTTCGGGCCGTA
GAGCCAGGGCTGGTGCAGAAGTTCTCCCTGCGAGACTGCAGCCCACGGCTCAGTGAAGAA
CTCTACCACCGCTGCCGCCTCAGCAACCTGGAGGGGCTAGGGGGCCGTGCCCAGCTGGCT
ATGGCTCTCTTTGAGCAGGAGCAGGCCAATAGCACTTAG
Enzyme 78 GenBank Gene ID AB095812 Link Image
Enzyme 78 GeneCard ID CHPF2 Link Image
Enzyme 78 GenAtlas ID CHPF2 Link Image
Enzyme 78 HGNC ID HGNC:29270 Link Image
Enzyme 78 Chromosome Location 7
Enzyme 78 Locus 7q36.1
Enzyme 78 SNPs SNPJam Report Link Image
Enzyme 78 General References
  1. Izumikawa T, Koike T, Shiozawa S, Sugahara K, Tamura J, Kitagawa H: Identification of chondroitin sulfate glucuronyltransferase as chondroitin synthase-3 involved in chondroitin polymerization: chondroitin polymerization is achieved by multiple enzyme complexes consisting of chondroitin synthase family members. J Biol Chem. 2008 Apr 25;283(17):11396-406. Epub 2008 Mar 3. [PubMed Link Image]
  2. Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Gotoh M, Yada T, Sato T, Akashima T, Iwasaki H, Mochizuki H, Inaba N, Togayachi A, Kudo T, Watanabe H, Kimata K, Narimatsu H: Molecular cloning and characterization of a novel chondroitin sulfate glucuronyltransferase that transfers glucuronic acid to N-acetylgalactosamine. J Biol Chem. 2002 Oct 11;277(41):38179-88. Epub 2002 Jul 26. [PubMed Link Image]
Enzyme 78 Metabolite References Not Available
Enzyme 79 [top]
Enzyme 79 ID 8484
Enzyme 79 Name OTTHUMP00000018263
Enzyme 79 Synonyms Not Available
Enzyme 79 Gene Name RP11-421P11.2
Enzyme 79 Protein Sequence >OTTHUMP00000018263
MAPLLLQLAVLGAALAAAALVLISIVAFTTATKMPALHRHEEEKFFLNAKGQKETLPSIW
DSPTKQLSVVVPSYNEEKRLPVMMDEALSYLEKRQKRDPAFTYEVIVVDDGSKDQTSKVA
FKYCQKYGSDKVRVITLVKNRGKGGAIRMGIFSSRGEKILMADADGATKFPDVEKLEKGL
NDLQPWPNQMAIACGSRAHLEKESIAQRSYFRTLLMYGFHFLVWFLCVKGIRDTQCGFKL
FTREAASRTFSSLHVERWAFDVELLYIAQFFKIPIAEIAVNWTEIEGSKLVPFWSWLQMG
KDLLFIRLRYLTGAWRLEQTRKMN
Enzyme 79 Number of Residues 324
Enzyme 79 Molecular Weight 36947
Enzyme 79 Theoretical pI 9.79
Enzyme 79 GO Classification Not Available
Enzyme 79 General Function Cell wall/membrane/envelope biogenesis
Enzyme 79 Specific Function Not Available
Enzyme 79 Pathways Not Available
Enzyme 79 Reactions Not Available
Enzyme 79 Pfam Domain Function
Enzyme 79 Signals
  • 1-31
Enzyme 79 Transmembrane Regions
  • 4-26
Enzyme 79 Essentiality Not Available
Enzyme 79 GenBank ID Protein Not Available
Enzyme 79 UniProtKB/Swiss-Prot ID Q5TBA6 Link Image
Enzyme 79 UniProtKB/Swiss-Prot Entry Name Q5TBA6_HUMAN Link Image
Enzyme 79 PDB ID Not Available
Enzyme 79 Cellular Location Not Available
Enzyme 79 Gene Sequence Not Available
Enzyme 79 GenBank Gene ID AL138706 Link Image
Enzyme 79 GeneCard ID ALG5 Link Image
Enzyme 79 GenAtlas ID ALG5 Link Image
Enzyme 79 HGNC ID HGNC:20266 Link Image
Enzyme 79 Chromosome Location Not Available
Enzyme 79 Locus Not Available
Enzyme 79 SNPs SNPJam Report Link Image
Enzyme 79 General References Not Available
Enzyme 79 Metabolite References Not Available
Enzyme 80 [top]
Enzyme 80 ID 8534
Enzyme 80 Name Polypeptide N-acetylgalactosaminyltransferase 13
Enzyme 80 Synonyms
  1. SubName: UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13 (GalNAc-T13)
  2. SubName: UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 13 (GalNAc-T13), isoform CRA_a
Enzyme 80 Gene Name GALNT13
Enzyme 80 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 13
MRRFVYCKVVLATSLMWVLVDVFLLLYFSECNKCDDKKERSLLPALRAVISRNQEGPGEM
GKAVLIPKDDQEKMKELFKINQFNLMASDLIALNRSLPDVRLEGCKTKVYPDELPNTSVV
IVFHNEAWSTLLRTVYSVINRSPHYLLSEVILVDDASERDFLKLTLENYVKNLEVPVKII
RMEERSGLIRARLRGAAASKGQVITFLDAHCECTLGWLEPLLARIKEDRKTVVCPIIDVI
SDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDRN
YFEEIGTYDAGMDIWGGENLEMSFRIWQCGGSLEIVTCSHVGHVFRKATPYTFPGGTGHV
INKNNRRLAEVWMDEFKDFFYIISPGVVKVDYGDVSVRKTLRENLKCKPFSWYLENIYPD
SQIPRRYYSLGEIRNVETNQCLDNMGRKENEKVGIFNCHGMGGNQVFSYTADKEIRTDDL
CLDVSRLNGPVIMLKCHHMRGNQLWEYDAERLTLRHVNSNQCLDEPSEEDKMVPTMQDCS
GSRSQQWLLRNMTLGT
Enzyme 80 Number of Residues 556
Enzyme 80 Molecular Weight 64050.1
Enzyme 80 Theoretical pI 6.82
Enzyme 80 GO Classification Not Available
Enzyme 80 General Function Involved in sugar binding
Enzyme 80 Specific Function Not Available
Enzyme 80 Pathways Not Available
Enzyme 80 Reactions Not Available
Enzyme 80 Pfam Domain Function
Enzyme 80 Signals
  • None
Enzyme 80 Transmembrane Regions
  • None
Enzyme 80 Essentiality Not Available
Enzyme 80 GenBank ID Protein 51490969 Link Image
Enzyme 80 UniProtKB/Swiss-Prot ID Q68VI8 Link Image
Enzyme 80 UniProtKB/Swiss-Prot Entry Name Q68VI8_HUMAN Link Image
Enzyme 80 PDB ID Not Available
Enzyme 80 Cellular Location Not Available
Enzyme 80 Gene Sequence >1671 bp
ATGAGGAGATTTGTCTACTGCAAGGTGGTTCTAGCCACTTCGCTGATGTGGGTTCTTGTT
GATGTCTTCTTACTGCTGTACTTCAGTGAATGTAACAAATGTGATGACAAGAAGGAGAGA
TCTCTGCTGCCTGCATTGAGGGCTGTTATTTCAAGAAACCAAGAAGGGCCAGGAGAAATG
GGAAAAGCTGTGTTGATTCCTAAAGATGACCAGGAGAAAATGAAAGAGCTGTTTAAAATC
AATCAGTTTAACCTTATGGCCAGTGATTTGATTGCCCTTAATAGAAGTCTGCCAGATGTA
AGATTAGAAGGATGTAAGACAAAAGTCTACCCTGATGAACTTCCAAACACAAGTGTAGTC
ATTGTGTTTCATAATGAAGCTTGGAGCACTCTCCTTAGAACTGTTTACAGTGTGATAAAT
CGTTCCCCACACTATCTACTCTCAGAGGTCATCTTGGTAGATGATGCCAGTGAAAGAGAT
TTTCTCAAGTTGACATTAGAGAATTACGTGAAAAATTTAGAAGTGCCAGTAAAAATTATT
AGGATGGAAGAACGCTCTGGGTTAATACGTGCCCGTCTTCGAGGAGCAGCTGCTTCAAAA
GGGCAGGTCATAACTTTTCTTGATGCACACTGTGAATGCACGTTAGGATGGCTGGAGCCT
TTGCTGGCAAGAATAAAGGAAGACAGGAAAACGGTTGTCTGCCCTATCATTGATGTGATT
AGTGATGATACTTTTGAATATATGGCTGGGTCAGACATGACTTATGGGGGTTTTAACTGG
AAACTGAATTTCCGCTGGTATCCTGTTCCCCAAAGAGAAATGGACAGGAGGAAAGGAGAC
AGAACATTACCTGTCAGGACCCCTACTATGGCTGGTGGCCTATTTTCTATTGACAGAAAC
TACTTTGAAGAGATAGGAACTTACGATGCAGGAATGGATATCTGGGGTGGAGAGAATCTT
GAAATGTCTTTTAGGATTTGGCAATGTGGAGGCTCCTTGGAGATTGTTACTTGCTCCCAT
GTTGGTCATGTTTTTCGGAAGGCAACTCCATACACTTTTCCTGGTGGCACTGGTCATGTC
ATCAACAAGAACAACAGGAGACTGGCAGAAGTTTGGATGGATGAATTTAAAGATTTCTTC
TACATCATATCCCCAGGTGTTGTCAAAGTGGATTATGGAGATGTGTCAGTCAGAAAAACA
CTAAGAGAAAATCTGAAGTGTAAGCCCTTTTCTTGGTACCTAGAAAACATCTATCCGGAC
TCCCAGATCCCAAGACGTTATTACTCACTTGGTGAGATAAGAAATGTTGAAACCAATCAG
TGTTTAGACAACATGGGCCGCAAGGAAAATGAAAAAGTGGGTATATTCAACTGTCATGGT
ATGGGAGGAAATCAGGTATTTTCTTACACTGCTGACAAAGAAATCCGAACCGATGACTTG
TGCTTGGATGTTTCTAGACTCAATGGACCTGTAATCATGTTAAAATGCCACCATATGAGA
GGAAATCAGTTATGGGAATATGATGCTGAGAGACTCACGTTGCGACATGTTAACAGTAAC
CAATGTCTCGATGAACCTTCTGAAGAAGACAAAATGGTGCCTACAATGCAGGACTGTAGT
GGAAGCAGATCCCAACAGTGGCTGCTAAGGAACATGACCTTGGGCACATGA
Enzyme 80 GenBank Gene ID AJ505991 Link Image
Enzyme 80 GeneCard ID GALNT13 Link Image
Enzyme 80 GenAtlas ID GALNT13 Link Image
Enzyme 80 HGNC ID HGNC:23242 Link Image
Enzyme 80 Chromosome Location 2
Enzyme 80 Locus 2q24.1
Enzyme 80 SNPs SNPJam Report Link Image
Enzyme 80 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 80 Metabolite References Not Available
Enzyme 81 [top]
Enzyme 81 ID 8772
Enzyme 81 Name ENTPD4 protein
Enzyme 81 Synonyms Not Available
Enzyme 81 Gene Name ENTPD4
Enzyme 81 Protein Sequence >ENTPD4 protein
MGRIGISCLFPASWHFSISPVGCPRILNTNLRQIMVISVLAAAVSLLYFSVVIIRNKYGR
LTRDKKFQRYLARVTDIEATDTNNPNVNYGIVVDCGSSGSRVFVYCWPRHNGNPHDLLDI
RQMRDKNRKPVVMKIKPGISEFATSPEKVSDYISPLLNFAAEHVPRAKHKETPLYILCTA
GMRILPESQQKAILEDLLTDIPVHFDFLFSDSHAEVISGKQEGVYAWIGINFVLGRFEHI
EDDDEAVVEVNIPGSESSEAIVRKRTAGILDMGGVSTQIAYEVPKTEEVAKNLLAEFNLG
CDVHQTEHVYRVYVATFLGFGGNAARQRYEDRIFANTIQKNRLLGKQTGLTPDMPYLDPC
LPLDIKDEIQQNGQTIYLRGTGDFDLCRETIQPFMNKTNETQTSLNGVYQPPIHFQNSEF
YGFSEFYYCTEDVLRMGGDYNAAKFTKAAKDYCATKWSILRERFDRGLYASHADLHRLKY
QCFKSAWMFEVFHRGFSFPVNYKSLKTALQVYDKEVQWTLGAILYRTRFLPLRKIGMLII
PCSGGCPKLCCAVWQPPPYGATKHLQCAAWN
Enzyme 81 Number of Residues 571
Enzyme 81 Molecular Weight 64852.9
Enzyme 81 Theoretical pI 8.13
Enzyme 81 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 81 General Function Involved in hydrolase activity
Enzyme 81 Specific Function Not Available
Enzyme 81 Pathways Not Available
Enzyme 81 Reactions Not Available
Enzyme 81 Pfam Domain Function
Enzyme 81 Signals
  • None
Enzyme 81 Transmembrane Regions
  • None
Enzyme 81 Essentiality Not Available
Enzyme 81 GenBank ID Protein 21759777 Link Image
Enzyme 81 UniProtKB/Swiss-Prot ID Q8NE73 Link Image
Enzyme 81 UniProtKB/Swiss-Prot Entry Name Q8NE73_HUMAN Link Image
Enzyme 81 PDB ID Not Available
Enzyme 81 Cellular Location Not Available
Enzyme 81 Gene Sequence >1716 bp
ATGGGGAGGATTGGCATCTCCTGTCTTTTTCCTGCTTCTTGGCATTTTAGCATATCTCCA
GTAGGGTGTCCTCGAATTCTGAATACCAATTTACGCCAAATTATGGTCATTAGTGTCCTG
GCTGCTGCTGTTTCACTTTTATATTTTTCTGTTGTCATAATCCGAAATAAGTATGGGCGA
CTAACCAGAGACAAGAAATTTCAAAGGTACCTGGCACGAGTTACCGACATTGAAGCTACA
GACACCAATAACCCCAATGTGAACTATGGGATCGTGGTGGACTGTGGTAGCAGTGGGTCT
CGAGTATTTGTTTACTGCTGGCCAAGGCATAATGGCAATCCACATGATCTGTTGGATATC
AGGCAAATGAGGGATAAAAACCGAAAGCCAGTGGTCATGAAGATAAAACCGGGCATTTCA
GAATTTGCTACCTCTCCAGAGAAAGTCAGTGATTACATTTCTCCACTTTTGAACTTTGCT
GCAGAGCATGTGCCACGGGCAAAACACAAAGAGACACCTCTCTACATTCTCTGCACGGCT
GGAATGAGAATCCTCCCCGAAAGCCAGCAGAAAGCTATTCTGGAAGACCTTCTGACCGAT
ATCCCCGTGCACTTTGACTTTCTGTTTTCTGACTCTCATGCAGAAGTAATTTCTGGGAAA
CAAGAAGGTGTGTATGCTTGGATTGGCATTAATTTTGTCCTTGGACGATTTGAGCATATT
GAAGATGATGATGAGGCCGTTGTGGAAGTTAACATTCCTGGAAGTGAAAGCAGCGAAGCC
ATTGTCCGTAAAAGGACAGCGGGCATTCTCGACATGGGCGGCGTGTCGACTCAGATAGCG
TACGAAGTCCCCAAAACTGAAGAAGTAGCTAAAAACTTGTTAGCTGAATTTAACTTGGGA
TGTGATGTTCACCAAACTGAGCATGTGTATCGAGTCTATGTGGCCACGTTTCTTGGGTTT
GGTGGCAATGCTGCTCGACAGAGATACGAAGACAGAATATTTGCCAACACCATTCAAAAG
AACAGGCTCCTGGGTAAACAGACTGGTCTGACTCCTGATATGCCGTACTTGGACCCCTGC
CTACCCCTAGACATTAAAGATGAAATCCAGCAAAATGGACAAACCATATACCTACGAGGG
ACTGGAGACTTTGACCTGTGTCGAGAGACTATCCAGCCTTTCATGAATAAAACAAACGAG
ACCCAGACTTCCCTCAATGGGGTCTACCAGCCCCCAATTCACTTCCAGAACAGTGAATTC
TATGGCTTCTCCGAATTCTACTACTGCACCGAGGATGTGTTACGAATGGGGGGAGACTAC
AATGCTGCTAAATTTACTAAAGCTGCAAAGGATTATTGTGCAACAAAGTGGTCCATTTTG
CGGGAACGCTTTGACCGAGGACTGTACGCCTCTCATGCTGACCTCCACAGGCTTAAGTAT
CAGTGCTTCAAATCGGCCTGGATGTTTGAGGTGTTTCATAGGGGCTTTTCGTTTCCTGTC
AACTATAAAAGCTTAAAGACTGCCTTGCAAGTTTACGACAAGGAGGTTCAGTGGACCCTT
GGAGCCATCCTCTACAGGACCCGCTTTCTACCATTAAGGAAAATAGGGATGCTGATAATA
CCTTGCTCAGGGGGTTGTCCAAAGCTGTGTTGTGCAGTATGGCAGCCACCACCATATGGG
GCCACCAAACACTTGCAATGTGCTGCTTGGAATTGA
Enzyme 81 GenBank Gene ID BC034477 Link Image
Enzyme 81 GeneCard ID ENTPD4 Link Image
Enzyme 81 GenAtlas ID ENTPD4 Link Image
Enzyme 81 HGNC ID HGNC:14573 Link Image
Enzyme 81 Chromosome Location 8
Enzyme 81 Locus 8p21.3
Enzyme 81 SNPs SNPJam Report Link Image
Enzyme 81 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 81 Metabolite References Not Available
Enzyme 82 [top]
Enzyme 82 ID 8792
Enzyme 82 Name Beta-1,3-N-acetylglucosaminyltransferase bGnT-2
Enzyme 82 Synonyms
  1. SubName: Putative uncharacterized protein B3GNT1
  2. SubName: UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1, isoform CRA_a
Enzyme 82 Gene Name bGnT-2
Enzyme 82 Protein Sequence >Beta-1,3-N-acetylglucosaminyltransferase bGnT-2
MSVGRRRIKLLGILMMANVFIYFIMEVSKSSSQEKNGKGEVIIPKEKFWKISTPPEAYWN
REQEKLNRQYNPILSMLTNQTGEAGRLSNISHLNYCEPDLRVTSVVTGFNNLPDRFKDFL
LYLRCRNYSLLIDQPDKCAKKPFLLLAIKSLTPHFARRQAIRESWGQESNAGNQTVVRVF
LLGQTPPEDNHPDLSDMLKFESEKHQDILMWNYRDTFFNLSLKEVLFLRWVSTSCPDTEF
VFKGDDDVFVNTHHILNYLNSLSKTKAKDLFIGDVIHNAGPHRDKKLKYYIPEVVYSGLY
PPYAGGGGFLYSGHLALRLYHITDQVHLYPIDDVYTGMCLQKLGLVPEKHKGFRTFDIEE
KNKNNICSYVDLMLVHSRKPQEMIDIWSQLQSAHLKC
Enzyme 82 Number of Residues 397
Enzyme 82 Molecular Weight 46021.6
Enzyme 82 Theoretical pI 8.75
Enzyme 82 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 82 General Function Involved in galactosyltransferase activity
Enzyme 82 Specific Function Not Available
Enzyme 82 Pathways Not Available
Enzyme 82 Reactions Not Available
Enzyme 82 Pfam Domain Function
Enzyme 82 Signals
  • None
Enzyme 82 Transmembrane Regions
  • None
Enzyme 82 Essentiality Not Available
Enzyme 82 GenBank ID Protein 12619294 Link Image
Enzyme 82 UniProtKB/Swiss-Prot ID Q54AC1 Link Image
Enzyme 82 UniProtKB/Swiss-Prot Entry Name Q54AC1_HUMAN Link Image
Enzyme 82 PDB ID Not Available
Enzyme 82 Cellular Location Not Available
Enzyme 82 Gene Sequence >1194 bp
ATGAGTGTTGGACGTCGAAGAATAAAGTTGTTGGGTATCCTGATGATGGCAAATGTCTTC
ATTTATTTTATTATGGAAGTCTCCAAAAGCAGTAGCCAAGAAAAAAATGGAAAAGGGGAA
GTAATAATACCCAAAGAGAAGTTCTGGAAGATATCTACCCCTCCCGAGGCATACTGGAAC
CGAGAGCAAGAGAAGCTGAACCGGCAGTACAACCCCATCCTGAGCATGCTGACCAACCAG
ACGGGGGAGGCGGGCAGGCTCTCCAATATAAGCCATCTGAACTACTGCGAACCTGACCTG
AGGGTCACGTCGGTGGTTACGGGTTTTAACAACTTGCCGGACAGATTTAAAGACTTTCTG
CTGTATTTGAGATGCCGCAATTATTCACTGCTTATAGATCAGCCGGATAAGTGTGCAAAG
AAACCTTTCTTGTTGCTGGCGATTAAGTCCCTCACTCCACATTTTGCCAGAAGGCAAGCA
ATCCGGGAATCCTGGGGCCAAGAAAGCAACGCAGGGAACCAAACGGTGGTGCGAGTCTTC
CTGCTGGGCCAGACACCCCCAGAGGACAACCACCCCGACCTTTCAGATATGCTGAAATTT
GAGAGTGAGAAGCACCAAGACATTCTTATGTGGAACTACAGAGACACTTTCTTCAACTTG
TCTCTGAAGGAAGTGCTGTTTCTCAGGTGGGTAAGTACTTCCTGCCCAGACACTGAGTTT
GTTTTCAAGGGCGATGACGATGTTTTTGTGAACACCCATCACATCCTGAATTACTTGAAT
AGTTTATCCAAGACCAAAGCCAAAGATCTCTTCATAGGTGATGTGATCCACAATGCTGGA
CCTCATCGGGATAAGAAGCTGAAGTACTACATCCCAGAAGTTGTTTACTCTGGCCTCTAC
CCACCCTATGCAGGGGGAGGGGGGTTCCTCTACTCCGGCCACCTGGCCCTGAGGCTGTAC
CATATCACTGACCAGGTCCATCTCTACCCCATTGATGACGTTTATACTGGAATGTGCCTT
CAGAAACTCGGCCTCGTTCCAGAGAAACACAAAGGCTTCAGGACATTTGATATCGAGGAG
AAAAACAAAAATAACATCTGCTCCTATGTAGATCTGATGTTAGTACATAGTAGAAAACCT
CAAGAGATGATTGATATTTGGTCTCAGTTGCAGAGTGCTCATTTAAAATGCTAA
Enzyme 82 GenBank Gene ID AB049584 Link Image
Enzyme 82 GeneCard ID bGnT-2 Link Image
Enzyme 82 GenAtlas ID bGnT-2 Link Image
Enzyme 82 HGNC ID HGNC:15685 Link Image
Enzyme 82 Chromosome Location Not Available
Enzyme 82 Locus Not Available
Enzyme 82 SNPs SNPJam Report Link Image
Enzyme 82 General References
  1. Shiraishi N, Natsume A, Togayachi A, Endo T, Akashima T, Yamada Y, Imai N, Nakagawa S, Koizumi S, Sekine S, Narimatsu H, Sasaki K: Identification and characterization of three novel beta 1,3-N-acetylglucosaminyltransferases structurally related to the beta 1,3-galactosyltransferase family. J Biol Chem. 2001 Feb 2;276(5):3498-507. Epub 2000 Oct 19. [PubMed Link Image]
  2. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 82 Metabolite References Not Available
Enzyme 83 [top]
Enzyme 83 ID 10883
Enzyme 83 Name Polypeptide N-acetylgalactosaminyltransferase 9
Enzyme 83 Synonyms
  1. Polypeptide GalNAc transferase 9
  2. GalNAc-T9
  3. pp-GaNTase 9
  4. Protein-UDP acetylgalactosaminyltransferase 9
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9
Enzyme 83 Gene Name GALNT9
Enzyme 83 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase 9
MAVARKIRTLLTVNILVFVGIVLFSVYCRLQGRSQELVRIVSGDRRVRSRHAKVGTLGDR
EAILQRLDHLEEVVYNQLNGLAKPIGLVEGPGGLGQGGLAATLRDDGQEAEGKYEEYGYN
AQLSDRISLDRSIPDYRPRKCRQMSYAQDLPQVSVVFIFVNEALSVILRSVHSVVNHTPS
QLLKEVILVDDNSDNVELKFNLDQYVNKRYPGLVKIVRNSRREGLIRARLQGWKAATAPV
VGFFDAHVEFNTGWAEPALSRIREDRRRIVLPAIDNIKYSTFEVQQYANAAHGYNWGLRC
MYIIPPQDWLDRGDESAPIRTPAMIGCSFVVDREYFGDIGLLDPGMEVYGGENVELGMRV
WQCGGSMEVLPCSRVAHIERTRKPYNNDIDYYAKRNALRAAEVWMDDFKSHVYMAWNIPM
SNPGVDFGDVSERLALRQRLKCRSFKWYLENVYPEMRVYNNTLTYGEVRNSKASAYCLDQ
GAEDGDRAILYPCHGMSSQLVRYSADGLLQLGPLGSTAFLPDSKCLVDDGTGRMPTLKKC
EDVARPTQRLWDFTQSGPIVSRATGRCLEVEMSKDANFGLRLVVQRCSGQKWMIRNWIKH
ARH
Enzyme 83 Number of Residues 603
Enzyme 83 Molecular Weight 68358.6
Enzyme 83 Theoretical pI 8.54
Enzyme 83 GO Classification
Function
  • binding
  • protein binding
Process
Component
Enzyme 83 General Function Involved in protein binding
Enzyme 83 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. Does not glycosylate apomucin or SDC3
Enzyme 83 Pathways
Enzyme 83 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 83 Pfam Domain Function
Enzyme 83 Signals
  • None
Enzyme 83 Transmembrane Regions
  • 7-29
Enzyme 83 Essentiality Not Available
Enzyme 83 GenBank ID Protein 10336504 Link Image
Enzyme 83 UniProtKB/Swiss-Prot ID Q9HCQ5 Link Image
Enzyme 83 UniProtKB/Swiss-Prot Entry Name GALT9_HUMAN Link Image
Enzyme 83 PDB ID Not Available
Enzyme 83 Cellular Location Not Available
Enzyme 83 Gene Sequence >1812 bp
ATGGCGGTGGCCAGGAAGATCCGAACTTTGCTGACGGTGAACATCCTGGTGTTCGTGGGC
ATCGTCCTGTTCTCCGTGTACTGCCGCCTGCAGGGCCGCTCCCAGGAGCTCGTGCGCATC
GTGAGCGGCGACCGCCGGGTGCGCAGCCGACACGCCAAGGTGGGCACGCTGGGGGACCGT
GAGGCCATCCTGCAGCGCCTGGACCACCTGGAGGAGGTGGTCTACAACCAGCTCAACGGC
CTTGCCAAGCCCATCGGCCTGGTGGAGGGGCCAGGAGGTCTGGGCCAGGGTGGCTTGGCG
GCCACCCTGCGTGATGACGGCCAGGAGGCGGAAGGCAAGTATGAGGAGTACGGCTACAAC
GCTCAGCTCAGCGACCGCATCTCCCTCGATCGGAGCATCCCCGACTACCGGCCCAGAAAG
TGCAGACAGATGAGCTACGCCCAGGACCTGCCCCAGGTCTCCGTGGTCTTCATCTTCGTC
AATGAGGCGCTGTCGGTCATCCTGCGCTCCGTGCACAGCGTGGTCAACCACACGCCCTCC
CAGCTCCTCAAGGAGGTCATCCTGGTGGACGACAACAGTGACAACGTGGAACTCAAGTTC
AATCTGGACCAGTACGTCAACAAGCGGTACCCAGGCCTCGTGAAGATTGTCCGCAACAGC
CGGCGGGAAGGACTGATCCGCGCGCGGCTGCAGGGCTGGAAGGCGGCCACCGCCCCAGTC
GTCGGCTTCTTTGATGCCCACGTCGAGTTCAACACGGGTTGGGCCGAGCCCGCACTGTCG
CGGATCCGAGAGGACCGGCGTCGCATCGTGCTGCCAGCCATCGACAACATCAAGTACAGC
ACGTTTGAGGTGCAGCAGTATGCGAACGCCGCCCATGGCTACAACTGGGGCCTCCGGTGC
ATGTACATCATCCCCCCGCAGGACTGGCTGGACCGCGGCGACGAGTCAGCACCCATCAGG
ACCCCAGCCATGATCGGCTGCTCCTTCGTAGTGGACCGCGAGTACTTCGGAGACATTGGG
CTGCTGGACCCCGGCATGGAGGTGTATGGCGGCGAGAACGTAGAACTGGGCATGAGGGTG
TGGCAGTGTGGCGGCAGCATGGAGGTGCTGCCCTGCTCCCGCGTGGCCCACATCGAGCGC
ACCAGGAAGCCCTACAACAACGACATTGACTACTACGCCAAGCGCAACGCCCTGCGCGCC
GCCGAGGTGTGGATGGATGACTTCAAGTCCCACGTGTACATGGCCTGGAACATCCCCATG
TCGAACCCAGGGGTGGACTTCGGGGACGTGTCTGAGAGGCTGGCCCTGCGTCAGAGGCTG
AAGTGTCGCAGCTTCAAGTGGTACCTGGAGAACGTGTACCCGGAGATGAGGGTCTACAAC
AACACCCTCACGTACGGAGAGGTGAGAAACAGCAAAGCCAGTGCCTACTGTCTGGACCAG
GGAGCGGAGGACGGCGACCGGGCGATCCTCTACCCCTGCCACGGGATGTCCTCCCAGCTG
GTGCGGTACAGCGCTGACGGCCTGCTGCAGCTGGGGCCTCTGGGCTCCACAGCCTTCTTG
CCTGACTCCAAGTGTCTGGTGGATGACGGCACGGGCCGCATGCCCACCCTGAAGAGGTGT
GAGGATGTGGCGCGGCCAACACAGCGGCTGTGGGACTTCACCCAGAGTGGCCCCATTGTG
AGCCGGGCCACGGGCCGCTGCCTGGAGGTGGAGATGTCCAAAGATGCCAACTTTGGGCTC
CGGCTGGTGGTACAGAGGTGCTCGGGGCAGAAGTGGATGATCAGAAACTGGATCAAACAC
GCACGGCACTGA
Enzyme 83 GenBank Gene ID AB040672 Link Image
Enzyme 83 GeneCard ID GALNT9 Link Image
Enzyme 83 GenAtlas ID GALNT9 Link Image
Enzyme 83 HGNC ID HGNC:4131 Link Image
Enzyme 83 Chromosome Location 1
Enzyme 83 Locus 12q24.33
Enzyme 83 SNPs SNPJam Report Link Image
Enzyme 83 General References
  1. Toba S, Tenno M, Konishi M, Mikami T, Itoh N, Kurosaka A: Brain-specific expression of a novel human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T9). Biochim Biophys Acta. 2000 Sep 7;1493(1-2):264-8. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  3. Zhang Y, Iwasaki H, Wang H, Kudo T, Kalka TB, Hennet T, Kubota T, Cheng L, Inaba N, Gotoh M, Togayachi A, Guo J, Hisatomi H, Nakajima K, Nishihara S, Nakamura M, Marth JD, Narimatsu H: Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen. J Biol Chem. 2003 Jan 3;278(1):573-84. Epub 2002 Oct 28. [PubMed Link Image]
Enzyme 83 Metabolite References Not Available
Enzyme 84 [top]
Enzyme 84 ID 11852
Enzyme 84 Name Exostosin-like 2
Enzyme 84 Synonyms
  1. Alpha-1,4-N-acetylhexosaminyltransferase EXTL2
  2. Alpha-GalNAcT EXTL2
  3. EXT-related protein 2
  4. Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase
  5. Processed exostosin-like 2
Enzyme 84 Gene Name EXTL2
Enzyme 84 Protein Sequence >Exostosin-like 2
MRCCHICKLPGRVMGIRVLRLSLVVILVLLLVAGALTALLPSVKEDKMLMLRREIKSQGK
STMDSFTLIMQTYNRTDLLLKLLNHYQAVPNLHKVIVVWNNIGEKAPDELWNSLGPHPIP
VIFKQQTANRMRNRLQVFPELETNAVLMVDDDTLISTPDLVFAFSVWQQFPDQIVGFVPR
KHVSTSSGIYSYGSFEMQAPGSGNGDQYSMVLIGASFFNSKYLELFQRQPAAVHALIDDT
QNCDDIAMNFIIAKHIGKTSGIFVKPVNMDNLEKETNSGYSGMWHRAEHALQRSYCINKL
VNIYDSMPLRYSNIMISQFGFPYANYKRKI
Enzyme 84 Number of Residues 330
Enzyme 84 Molecular Weight 37465.4
Enzyme 84 Theoretical pI 9.24
Enzyme 84 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • cell part
  • intrinsic to endoplasmic reticulum membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 84 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 84 Specific Function Glycosyltransferase required for the biosynthesis of heparan-sulfate and responsible for the alternating addition of beta-1-4-linked glucuronic acid (GlcA) and alpha-1-4-linked N- acetylglucosamine (GlcNAc) units to nascent heparan sulfate chains
Enzyme 84 Pathways
Enzyme 84 Reactions
  • UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D- galactosyl-(1->4)-beta-D-xylosyl-proteoglycan = UDP + alpha-N-acetyl-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)- beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl- proteoglycan [RN:R05930]
Enzyme 84 Pfam Domain Function
Enzyme 84 Signals
  • None
Enzyme 84 Transmembrane Regions
  • 23-43
Enzyme 84 Essentiality Not Available
Enzyme 84 GenBank ID Protein 2895062 Link Image
Enzyme 84 UniProtKB/Swiss-Prot ID Q9UBQ6 Link Image
Enzyme 84 UniProtKB/Swiss-Prot Entry Name EXTL2_HUMAN Link Image
Enzyme 84 PDB ID Not Available
Enzyme 84 Cellular Location Not Available
Enzyme 84 Gene Sequence >993 bp
ATGAGGTGTTGCCACATCTGCAAACTTCCTGGGAGAGTAATGGGGATTCGAGTGCTTCGA
TTATCTTTGGTGGTCATCCTCGTATTATTACTGGTAGCTGGTGCTTTGACTGCCTTACTT
CCCAGTGTTAAAGAAGACAAGATGCTCATGTTGCGTAGGGAAATAAAATCCCAGGGCAAG
TCCACCATGGACTCCTTTACTCTCATAATGCAGACGTACAACAGAACAGATCTCTTATTG
AAACTTTTAAATCATTATCAGGCTGTACCAAATCTGCACAAAGTGATTGTGGTATGGAAC
AATATTGGAGAGAAGGCACCAGATGAATTATGGAATTCTCTAGGGCCCCACCCTATCCCT
GTGATCTTCAAACAACAGACAGCAAACAGGATGAGAAATCGACTCCAGGTCTTTCCTGAA
CTGGAAACCAATGCAGTGTTGATGGTAGATGATGACACACTCATCAGCACCCCAGACCTT
GTTTTTGCTTTCTCAGTTTGGCAGCAATTTCCTGATCAAATTGTAGGATTTGTTCCTAGA
AAGCACGTCTCTACTTCATCAGGTATCTACAGTTATGGAAGTTTTGAAATGCAAGCACCA
GGGTCTGGAAATGGTGACCAGTACTCTATGGTGCTGATTGGAGCCTCATTCTTCAATAGC
AAATATCTTGAATTATTTCAGAGGCAACCTGCAGCTGTCCATGCTTTGATAGATGATACT
CAAAACTGTGATGATATTGCCATGAATTTTATCATTGCCAAGCATATTGGCAAGACTTCA
GGGATATTTGTGAAGCCTGTAAACATGGACAATTTGGAAAAAGAAACCAACAGTGGCTAT
TCTGGAATGTGGCATCGAGCTGAGCACGCTCTGCAGAGGTCTTATTGTATAAATAAGCTT
GTTAATATCTATGATAGCATGCCCTTAAGATACTCCAACATTATGATTTCCCAGTTTGGT
TTTCCATATGCCAACTACAAAAGAAAAATATAA
Enzyme 84 GenBank Gene ID AF000416 Link Image
Enzyme 84 GeneCard ID EXTL2 Link Image
Enzyme 84 GenAtlas ID EXTL2 Link Image
Enzyme 84 HGNC ID HGNC:3516 Link Image
Enzyme 84 Chromosome Location 1
Enzyme 84 Locus 1p21
Enzyme 84 SNPs SNPJam Report Link Image
Enzyme 84 General References
  1. Wuyts W, Van Hul W, Hendrickx J, Speleman F, Wauters J, De Boulle K, Van Roy N, Van Agtmael T, Bossuyt P, Willems PJ: Identification and characterization of a novel member of the EXT gene family, EXTL2. Eur J Hum Genet. 1997 Nov-Dec;5(6):382-9. [PubMed Link Image]
  2. Saito T, Seki N, Yamauchi M, Tsuji S, Hayashi A, Kozuma S, Hori T: Structure, chromosomal location, and expression profile of EXTR1 and EXTR2, new members of the multiple exostoses gene family. Biochem Biophys Res Commun. 1998 Feb 4;243(1):61-6. [PubMed Link Image]
  3. McCormick C, Duncan G, Goutsos KT, Tufaro F: The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate. Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):668-73. [PubMed Link Image]
  4. Kitagawa H, Shimakawa H, Sugahara K: The tumor suppressor EXT-like gene EXTL2 encodes an alpha1, 4-N-acetylhexosaminyltransferase that transfers N-acetylgalactosamine and N-acetylglucosamine to the common glycosaminoglycan-protein linkage region. The key enzyme for the chain initiation of heparan sulfate. J Biol Chem. 1999 May 14;274(20):13933-7. [PubMed Link Image]
  5. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 84 Metabolite References Not Available
Enzyme 85 [top]
Enzyme 85 ID 11945
Enzyme 85 Name Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
Enzyme 85 Synonyms
  1. N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVa
  2. GlcNAc-T IVa
  3. GnT-IVa
  4. N-acetylglucosaminyltransferase IVa
  5. UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVa
  6. Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form
Enzyme 85 Gene Name MGAT4A
Enzyme 85 Protein Sequence >Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
MRLRNGTVATALAFITSFLTLSWYTTWQNGKEKLIAYQREFLALKERLRIAEHRISQRSS
ELNTIVQQFKRVGAETNGSKDALNKFSDNTLKLLKELTSKKSLQVPSIYYHLPHLLKNEG
SLQPAVQIGNGRTGVSIVMGIPTVKREVKSYLIETLHSLIDNLYPEEKLDCVIVVFIGET
DIDYVHGVVANLEKEFSKEISSGLVEVISPPESYYPDLTNLKETFGDSKERVRWRTKQNL
DYCFLMMYAQEKGIYYIQLEDDIIVKQNYFNTIKNFALQLSSEEWMILEFSQLGFIGKMF
QAPDLTLIVEFIFMFYKEKPIDWLLDHILWVKVCNPEKDAKHCDRQKANLRIRFRPSLFQ
HVGLHSSLSGKIQKLTDKDYMKPLLLKIHVNPPAEVSTSLKVYQGHTLEKTYMGEDFFWA
ITPIAGDYILFKFDKPVNVESYLFHSGNQEHPGDILLNTTVEVLPFKSEGLEISKETKDK
RLEDGYFRIGKFENGVAEGMVDPSLNPISAFRLSVIQNSAVWAILNEIHIKKATN
Enzyme 85 Number of Residues 535
Enzyme 85 Molecular Weight 61543.4
Enzyme 85 Theoretical pI 7.44
Enzyme 85 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • membrane
Enzyme 85 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 85 Specific Function Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N- linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells
Enzyme 85 Pathways
Enzyme 85 Reactions
  • UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D- mannosyl-R = UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D- mannosyl-R [RN:R04662]
Enzyme 85 Pfam Domain Function
Enzyme 85 Signals
  • None
Enzyme 85 Transmembrane Regions
  • 5-27
Enzyme 85 Essentiality Not Available
Enzyme 85 GenBank ID Protein Not Available
Enzyme 85 UniProtKB/Swiss-Prot ID Q9UM21 Link Image
Enzyme 85 UniProtKB/Swiss-Prot Entry Name MGT4A_HUMAN Link Image
Enzyme 85 PDB ID Not Available
Enzyme 85 Cellular Location Not Available
Enzyme 85 Gene Sequence >1608 bp
ATGAGGCTCCGCAATGGAACTGTAGCCACTGCTTTAGCATTTATCACTTCCTTCCTTACT
TTGTCTTGGTATACTACATGGCAAAATGGGAAAGAAAAACTGATTGCTTATCAACGAGAA
TTCCTTGCTTTGAAAGAACGTCTTCGAATAGCTGAACACAGAATCTCACAGCGCTCTTCT
GAATTAAATACGATTGTGCAACAGTTCAAGCGTGTAGGAGCAGAAACAAATGGAAGTAAG
GATGCGTTGAATAAGTTTTCAGATAATACCCTAAAGCTGTTAAAGGAGTTAACAAGCAAA
AAATCTCTTCAAGTGCCAAGTATTTATTATCATTTGCCTCATTTATTGAAAAATGAAGGA
AGTCTTCAACCTGCTGTACAGATTGGCAACGGAAGAACAGGAGTTTCAATAGTCATGGGC
ATTCCCACAGTGAAGAGAGAAGTTAAATCTTACCTCATAGAAACTCTTCATTCCCTTATT
GATAACCTGTATCCTGAAGAGAAGTTGGACTGTGTTATAGTAGTCTTCATAGGAGAGACA
GATATTGATTATGTACATGGTGTTGTAGCCAACCTGGAGAAAGAATTTTCTAAAGAAATC
AGTTCTGGCTTGGTGGAAGTCATATCACCCCCTGAAAGCTATTATCCTGACTTGACAAAC
CTAAAGGAGACATTTGGAGACTCCAAAGAAAGAGTAAGATGGAGAACAAAGCAAAACCTA
GATTACTGTTTTCTAATGATGTATGCTCAAGAAAAGGGCATATATTACATTCAGCTTGAA
GATGATATTATTGTCAAACAAAATTATTTTAATACCATAAAAAATTTTGCACTTCAACTT
TCTTCTGAGGAATGGATGATTCTAGAGTTTTCCCAGCTGGGCTTCATTGGTAAAATGTTT
CAAGCGCCGGATCTTACTCTGATTGTAGAATTCATATTCATGTTTTACAAGGAGAAACCC
ATTGATTGGCTCCTGGACCATATTCTCTGGGTGAAAGTCTGCAACCCTGAAAAAGATGCA
AAACATTGTGATAGACAGAAAGCAAATCTGCGAATTCGCTTCAGACCTTCCCTTTTCCAA
CATGTTGGTCTGCACTCATCACTATCAGGAAAAATCCAAAAACTCACGGATAAAGATTAT
ATGAAACCATTACTTCTTAAAATCCATGTAAACCCACCTGCGGAGGTATCTACTTCCTTG
AAGGTCTACCAAGGGCATACGCTGGAGAAAACTTACATGGGAGAGGATTTCTTCTGGGCT
ATCACACCGATAGCTGGAGACTACATCTTGTTTAAATTTGATAAACCAGTCAATGTAGAA
AGTTATTTGTTCCATAGCGGCAACCAAGAACATCCTGGAGATATTCTGCTAAACACAACT
GTGGAAGTTTTGCCTTTTAAGAGTGAAGGTTTGGAAATAAGCAAAGAAACCAAAGACAAA
CGATTAGAAGATGGCTATTTCAGAATAGGAAAATTTGAGAATGGTGTTGCAGAAGGAATG
GTGGATCCAAGTCTCAATCCCATTTCAGCCTTTCGACTTTCAGTTATTCAGAATTCTGCT
GTTTGGGCCATTCTTAATGAGATTCATATTAAAAAAGCCACCAACTGA
Enzyme 85 GenBank Gene ID AB000616 Link Image
Enzyme 85 GeneCard ID MGAT4A Link Image
Enzyme 85 GenAtlas ID MGAT4A Link Image
Enzyme 85 HGNC ID HGNC:7047 Link Image
Enzyme 85 Chromosome Location 2
Enzyme 85 Locus 2q12
Enzyme 85 SNPs SNPJam Report Link Image
Enzyme 85 General References
  1. Yoshida A, Minowa MT, Takamatsu S, Hara T, Oguri S, Ikenaga H, Takeuchi M: Tissue specific expression and chromosomal mapping of a human UDP-N-acetylglucosamine: alpha1,3-d-mannoside beta1, 4-N-acetylglucosaminyltransferase. Glycobiology. 1999 Mar;9(3):303-10. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Takamatsu S, Oguri S, Minowa MT, Yoshida A, Nakamura K, Takeuchi M, Kobata A: Unusually high expression of N-acetylglucosaminyltransferase-IVa in human choriocarcinoma cell lines: a possible enzymatic basis of the formation of abnormal biantennary sugar chain. Cancer Res. 1999 Aug 15;59(16):3949-53. [PubMed Link Image]
  5. Ide Y, Miyoshi E, Nakagawa T, Gu J, Tanemura M, Nishida T, Ito T, Yamamoto H, Kozutsumi Y, Taniguchi N: Aberrant expression of N-acetylglucosaminyltransferase-IVa and IVb (GnT-IVa and b) in pancreatic cancer. Biochem Biophys Res Commun. 2006 Mar 10;341(2):478-82. Epub 2006 Jan 11. [PubMed Link Image]
  6. Oguri S, Yoshida A, Minowa MT, Takeuchi M: Kinetic properties and substrate specificities of two recombinant human N-acetylglucosaminyltransferase-IV isozymes. Glycoconj J. 2006 Nov;23(7-8):473-80. [PubMed Link Image]
Enzyme 85 Metabolite References Not Available
Enzyme 86 [top]
Enzyme 86 ID 11946
Enzyme 86 Name Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
Enzyme 86 Synonyms
  1. N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVb
  2. GlcNAc-T IVb
  3. GnT-IVb
  4. N-acetylglucosaminyltransferase IVb
  5. UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVb
Enzyme 86 Gene Name MGAT4B
Enzyme 86 Protein Sequence >Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
MRLRNGTFLTLLLFCLCAFLSLSWYAALSGQKGDVVDVYQREFLALRDRLHAAEQESLKR
SKELNLVLDEIKRAVSERQALRDGDGNRTWGRLTEDPRLKPWNGSHRHVLHLPTVFHHLP
HLLAKESSLQPAVRVGQGRTGVSVVMGIPSVRREVHSYLTDTLHSLISELSPQEKEDSVI
VVLIAETDSQYTSAVTENIKALFPTEIHSGLLEVISPSPHFYPDFSRLRESFGDPKERVR
WRTKQNLDYCFLMMYAQSKGIYYVQLEDDIVAKPNYLSTMKNFALQQPSEDWMILEFSQL
GFIGKMFKSLDLSLIVEFILMFYRDKPIDWLLDHILWVKVCNPEKDAKHCDRQKANLRIR
FKPSLFQHVGTHSSLAGKIQKLKDKDFGKQALRKEHVNPPAEVSTSLKTYQHFTLEKAYL
REDFFWAFTPAAGDFIRFRFFQPLRLERFFFRSGNIEHPEDKLFNTSVEVLPFDNPQSDK
EALQEGRTATLRYPRSPDGYLQIGSFYKGVAEGEVDPAFGPLEALRLSIQTDSPVWVILS
EIFLKKAD
Enzyme 86 Number of Residues 548
Enzyme 86 Molecular Weight 63197.8
Enzyme 86 Theoretical pI 7.99
Enzyme 86 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
  • cell part
  • membrane
Enzyme 86 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 86 Specific Function Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N- linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains. Has lower affinities for donors or acceptors than MGAT4A, suggesting that, under physiological conditions, it is not the main contributor in N- glycan biosynthesis
Enzyme 86 Pathways
Enzyme 86 Reactions
  • UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D- mannosyl-R = UDP + 3-(2,4-bis[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D- mannosyl-R [RN:R04662]
Enzyme 86 Pfam Domain Function
Enzyme 86 Signals
  • None
Enzyme 86 Transmembrane Regions
  • 8-28
Enzyme 86 Essentiality Not Available
Enzyme 86 GenBank ID Protein 5748487 Link Image
Enzyme 86 UniProtKB/Swiss-Prot ID Q9UQ53 Link Image
Enzyme 86 UniProtKB/Swiss-Prot Entry Name MGT4B_HUMAN Link Image
Enzyme 86 PDB ID Not Available
Enzyme 86 Cellular Location Not Available
Enzyme 86 Gene Sequence >1647 bp
ATGAGGCTCCGCAATGGCACCTTCCTGACGCTGCTGCTCTTCTGCCTGTGCGCCTTCCTC
TCGCTGTCCTGGTACGCGGCACTCAGCGGCCAGAAAGGCGACGTTGTGGACGTTTACCAG
CGGGAGTTCCTGGCGCTGCGCGATCGGTTGCACGCAGCTGAGCAGGAGAGCCTCAAGCGC
TCCAAGGAGCTCAACCTGGTGCTGGACGAGATCAAGAGGGCCGTGTCAGAAAGGCAGGCG
CTGCGAGACGGAGACGGCAATCGCACCTGGGGCCGCCTAACAGAGGACCCCCGATTGAAG
CCGTGGAACGGCTCACACCGGCACGTGCTGCACCTGCCCACCGTCTTCCATCACCTGCCA
CACCTGCTGGCCAAGGAGAGCAGTCTGCAGCCCGCGGTGCGCGTGGGCCAGGGCCGCACC
GGAGTGTCGGTGGTGATGGGCATCCCGAGCGTGCGGCGCGAGGTGCACTCGTACCTGACT
GACACTCTGCACTCGCTCATCTCCGAGCTGAGCCCGCAGGAGAAGGAGGACTCGGTCATC
GTGGTGCTGATCGCCGAGACTGACTCACAGTACACTTCGGCAGTGACAGAGAACATCAAG
GCCTTGTTCCCCACGGAGATCCATTCTGGGCTCCTGGAGGTCATCTCACCCTCCCCCCAC
TTCTACCCTGACTTCTCCCGCCTCCGAGAGTCCTTTGGGGACCCCAAGGAGAGAGTCAGG
TGGAGGACCAAACAGAACCTCGATTACTGCTTCCTCATGATGTACGCGCAGTCCAAAGGC
ATCTACTACGTGCAGCTGGAGGATGACATCGTGGCCAAGCCCAACTACCTGAGCACCATG
AAGAACTTTGCACTGCAGCAGCCTTCAGAGGACTGGATGATCCTGGAGTTCTCCCAGCTG
GGCTTCATTGGTAAGATGTTCAAGTCGCTGGACCTGAGCCTGATTGTAGAGTTCATTCTC
ATGTTCTACCGGGACAAGCCCATCGACTGGCTCCTGGACCATATTCTGTGGGTGAAAGTC
TGCAACCCCGAGAAGGATGCGAAGCACTGTGACCGGCAGAAAGCCAACCTGCGGATCCGC
TTCAAACCGTCCCTCTTCCAGCACGTGGGCACTCACTCCTCGCTGGCTGGCAAGATCCAG
AAACTGAAGGACAAAGACTTTGGAAAGCAGGCGCTGCGGAAGGAGCATGTGAACCCGCCA
GCAGAGGTGAGCACGAGCCTGAAGACATACCAGCACTTCACCCTGGAGAAAGCCTACCTG
CGCGAGGACTTCTTCTGGGCCTTCACCCCTGCCGCGGGGGACTTCATCCGCTTCCGCTTC
TTCCAACCTCTAAGACTGGAGCGGTTCTTCTTCCGCAGTGGGAACATCGAGCACCCGGAG
GACAAGCTCTTCAACACGTCTGTGGAGGTGCTGCCCTTCGACAACCCTCAGTCAGACAAG
GAGGCCCTGCAGGAGGGCCGCACCGCCACCCTCCGGTACCCTCGGAGCCCCGACGGCTAC
CTCCAGATCGGCTCCTTCTACAAGGGAGTGGCAGAGGGAGAGGTGGACCCAGCCTTCGGC
CCTCTGGAAGCACTGCGCCTCTCGATCCAGACGGACTCCCCTGTGTGGGTGATTCTGAGC
GAGATCTTCCTGAAAAAGGCCGACTAA
Enzyme 86 GenBank Gene ID AB000624 Link Image
Enzyme 86 GeneCard ID MGAT4B Link Image
Enzyme 86 GenAtlas ID MGAT4B Link Image
Enzyme 86 HGNC ID HGNC:7048 Link Image
Enzyme 86 Chromosome Location 5
Enzyme 86 Locus 5q35
Enzyme 86 SNPs SNPJam Report Link Image
Enzyme 86 General References
  1. Yoshida A, Minowa MT, Takamatsu S, Hara T, Ikenaga H, Takeuchi M: A novel second isoenzyme of the human UDP-N-acetylglucosamine:alpha1,3-D-mannoside beta1,4-N-acetylglucosaminyltransferase family: cDNA cloning, expression, and chromosomal assignment. Glycoconj J. 1998 Dec;15(12):1115-23. [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. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  5. Ide Y, Miyoshi E, Nakagawa T, Gu J, Tanemura M, Nishida T, Ito T, Yamamoto H, Kozutsumi Y, Taniguchi N: Aberrant expression of N-acetylglucosaminyltransferase-IVa and IVb (GnT-IVa and b) in pancreatic cancer. Biochem Biophys Res Commun. 2006 Mar 10;341(2):478-82. Epub 2006 Jan 11. [PubMed Link Image]
  6. Oguri S, Yoshida A, Minowa MT, Takeuchi M: Kinetic properties and substrate specificities of two recombinant human N-acetylglucosaminyltransferase-IV isozymes. Glycoconj J. 2006 Nov;23(7-8):473-80. [PubMed Link Image]
Enzyme 86 Metabolite References Not Available
Enzyme 87 [top]
Enzyme 87 ID 11996
Enzyme 87 Name UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
Enzyme 87 Synonyms
  1. BGnT-5
  2. Beta-1,3-Gn-T5
  3. Beta-1,3-N-acetylglucosaminyltransferase 5
  4. Beta3Gn-T5
  5. Lactotriaosylceramide synthase
  6. Lc(3)Cer synthase
  7. Lc3 synthase
Enzyme 87 Gene Name B3GNT5
Enzyme 87 Protein Sequence >UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
MRMLVSGRRVKKWQLIIQLFATCFLASLMFFWEPIDNHIVSHMKSYSYRYLINSYDFVND
TLSLKHTSAGPRYQYLINHKEKCQAQDVLLLLFVKTAPENYDRRSGIRRTWGNENYVRSQ
LNANIKTLFALGTPNPLEGEELQRKLAWEDQRYNDIIQQDFVDSFYNLTLKLLMQFSWAN
TYCPHAKFLMTADDDIFIHMPNLIEYLQSLEQIGVQDFWIGRVHRGAPPIRDKSSKYYVS
YEMYQWPAYPDYTAGAAYVISGDVAAKVYEASQTLNSSLYIDDVFMGLCANKIGIVPQDH
VFFSGEGKTPYHPCIYEKMMTSHGHLEDLQDLWKNATDPKVKTISKGFFGQIYCRLMKII
LLCKISYVDTYPCRAAFI
Enzyme 87 Number of Residues 378
Enzyme 87 Molecular Weight 44052.3
Enzyme 87 Theoretical pI 8.00
Enzyme 87 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 87 General Function Involved in galactosyltransferase activity
Enzyme 87 Specific Function Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids, notably by participating in biosynthesis of HNK-1 and Lewis X carbohydrate structures. Has strong activity toward lactosylceramide (LacCer) and neolactotetraosylceramide (nLc(4)Cer; paragloboside), resulting in the synthesis of Lc(3)Cer and neolactopentaosylceramide (nLc(5)Cer), respectively. Probably plays a central role in regulating neolacto-series glycolipid synthesis during embryonic development
Enzyme 87 Pathways Not Available
Enzyme 87 Reactions Not Available
Enzyme 87 Pfam Domain Function
Enzyme 87 Signals
  • None
Enzyme 87 Transmembrane Regions
  • 15-35
Enzyme 87 Essentiality Not Available
Enzyme 87 GenBank ID Protein 13568434 Link Image
Enzyme 87 UniProtKB/Swiss-Prot ID Q9BYG0 Link Image
Enzyme 87 UniProtKB/Swiss-Prot Entry Name B3GN5_HUMAN Link Image
Enzyme 87 PDB ID Not Available
Enzyme 87 Cellular Location Not Available
Enzyme 87 Gene Sequence >1137 bp
ATGAGAATGTTGGTTAGTGGCAGAAGAGTCAAAAAATGGCAGTTAATTATTCAGTTATTT
GCTACTTGTTTTTTAGCGAGCCTCATGTTTTTTTGGGAACCAATCGATAATCACATTGTG
AGCCATATGAAGTCATATTCTTACAGATACCTCATAAATAGCTATGACTTTGTGAATGAT
ACCCTGTCTCTTAAGCACACCTCAGCGGGGCCTCGCTACCAATACTTGATTAACCACAAG
GAAAAGTGTCAAGCTCAAGACGTCCTCCTTTTACTGTTTGTAAAAACTGCTCCTGAAAAC
TATGATCGACGTTCCGGAATTAGAAGGACGTGGGGCAATGAAAATTATGTTCGGTCTCAG
CTGAATGCCAACATCAAAACTCTGTTTGCCTTAGGAACTCCTAATCCACTGGAGGGAGAA
GAACTACAAAGAAAACTGGCTTGGGAAGATCAAAGGTACAATGATATAATTCAGCAAGAC
TTTGTTGATTCTTTCTACAATCTTACTCTGAAATTACTTATGCAGTTCAGTTGGGCAAAT
ACCTATTGTCCACATGCCAAATTTCTTATGACTGCTGATGATGACATATTTATTCACATG
CCAAATCTGATTGAGTACCTTCAAAGTTTAGAACAAATTGGTGTTCAAGACTTTTGGATT
GGTCGTGTTCATCGTGGTGCCCCTCCCATTAGAGATAAAAGCAGCAAATACTACGTGTCC
TATGAAATGTACCAGTGGCCAGCTTACCCTGACTACACAGCCGGAGCTGCCTATGTAATC
TCCGGTGATGTAGCTGCCAAAGTCTATGAGGCATCACAGACACTAAATTCAAGTCTTTAC
ATAGACGATGTGTTCATGGGCCTCTGTGCCAATAAAATAGGGATAGTACCGCAGGACCAT
GTGTTTTTTTCTGGAGAGGGTAAAACTCCTTATCATCCCTGCATCTATGAAAAAATGATG
ACATCTCATGGACACTTAGAAGATCTCCAGGACCTTTGGAAGAATGCTACAGATCCTAAA
GTAAAAACCATTTCCAAAGGTTTTTTTGGTCAAATATACTGCAGATTAATGAAGATAATT
CTCCTTTGTAAAATTAGCTATGTGGACACATACCCTTGTAGGGCTGCGTTTATCTAA
Enzyme 87 GenBank Gene ID AB045278 Link Image
Enzyme 87 GeneCard ID B3GNT5 Link Image
Enzyme 87 GenAtlas ID B3GNT5 Link Image
Enzyme 87 HGNC ID HGNC:15684 Link Image
Enzyme 87 Chromosome Location 3
Enzyme 87 Locus 3q28
Enzyme 87 SNPs SNPJam Report Link Image
Enzyme 87 General References
  1. Togayachi A, Akashima T, Ookubo R, Kudo T, Nishihara S, Iwasaki H, Natsume A, Mio H, Inokuchi J, Irimura T, Sasaki K, Narimatsu H: Molecular cloning and characterization of UDP-GlcNAc:lactosylceramide beta 1,3-N-acetylglucosaminyltransferase (beta 3Gn-T5), an essential enzyme for the expression of HNK-1 and Lewis X epitopes on glycolipids. J Biol Chem. 2001 Jun 22;276(25):22032-40. Epub 2001 Mar 30. [PubMed Link Image]
  2. Henion TR, Zhou D, Wolfer DP, Jungalwala FB, Hennet T: Cloning of a mouse beta 1,3 N-acetylglucosaminyltransferase GlcNAc(beta 1,3)Gal(beta 1,4)Glc-ceramide synthase gene encoding the key regulator of lacto-series glycolipid biosynthesis. J Biol Chem. 2001 Aug 10;276(32):30261-9. Epub 2001 May 30. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 87 Metabolite References Not Available
Enzyme 88 [top]
Enzyme 88 ID 12970
Enzyme 88 Name UDP-glucuronosyltransferase 2A3
Enzyme 88 Synonyms
  1. UDPGT 2A3
Enzyme 88 Gene Name UGT2A3
Enzyme 88 Protein Sequence >UDP-glucuronosyltransferase 2A3
MRSDKSALVFLLLQLFCVGCGFCGKVLVWPCDMSHWLNVKVILEELIVRGHEVTVLTHSK
PSLIDYRKPSALKFEVVHMPQDRTEENEIFVDLALNVLPGLSTWQSVIKLNDFFVEIRGT
LKMMCESFIYNQTLMKKLQETNYDVMLIDPVIPCGDLMAELLAVPFVLTLRISVGGNMER
SCGKLPAPLSYVPVPMTGLTDRMTFLERVKNSMLSVLFHFWIQDYDYHFWEEFYSKALGR
PTTLCETVGKAEIWLIRTYWDFEFPQPYQPNFEFVGGLHCKPAKALPKEMENFVQSSGED
GIVVFSLGSLFQNVTEEKANIIASALAQIPQKVLWRYKGKKPSTLGANTRLYDWIPQNDL
LGHPKTKAFITHGGMNGIYEAIYHGVPMVGVPIFGDQLDNIAHMKAKGAAVEINFKTMTS
EDLLRALRTVITDSSYKENAMRLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRSAAHD
LTWFQHYSIDVIGFLLACVATAIFLFTKCFLFSCQKFNKTRKIEKRE
Enzyme 88 Number of Residues 527
Enzyme 88 Molecular Weight 60253.9
Enzyme 88 Theoretical pI 8.04
Enzyme 88 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 88 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 88 Specific Function UDP-glucuronosyltransferases catalyze phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase water solubility and enhance excretion. They are of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds
Enzyme 88 Pathways
Enzyme 88 Reactions
  • UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside [RN:R01383]
Enzyme 88 Pfam Domain Function
Enzyme 88 Signals
  • 1-23
Enzyme 88 Transmembrane Regions
  • 492-512
Enzyme 88 Essentiality Not Available
Enzyme 88 GenBank ID Protein 193211427 Link Image
Enzyme 88 UniProtKB/Swiss-Prot ID Q6UWM9 Link Image
Enzyme 88 UniProtKB/Swiss-Prot Entry Name UD2A3_HUMAN Link Image
Enzyme 88 PDB ID Not Available
Enzyme 88 Cellular Location Not Available
Enzyme 88 Gene Sequence >1584 bp
ATGAGGTCTGACAAGTCAGCTTTGGTATTTCTGCTCCTGCAGCTCTTCTGTGTTGGCTGT
GGATTCTGTGGGAAAGTCCTGGTGTGGCCCTGTGACATGAGCCATTGGCTTAATGTCAAG
GTCATTCTAGAAGAGCTCATAGTGAGAGGCCATGAGGTAACAGTATTGACTCACTCAAAG
CCTTCGTTAATTGACTACAGGAAGCCTTCTGCATTGAAATTTGAGGTGGTCCATATGCCA
CAGGACAGAACAGAAGAAAATGAAATATTTGTTGACCTAGCTCTGAATGTCTTGCCAGGC
TTATCAACCTGGCAATCAGTTATAAAATTAAATGATTTTTTTGTTGAAATAAGAGGAACT
TTAAAAATGATGTGTGAGAGCTTTATCTACAATCAGACGCTTATGAAGAAGCTACAGGAA
ACCAACTACGATGTAATGCTTATAGACCCTGTGATTCCCTGTGGAGACCTGATGGCTGAG
TTGCTTGCAGTCCCTTTTGTGCTCACACTTAGAATTTCTGTAGGAGGCAATATGGAGCGA
AGCTGTGGGAAACTTCCAGCTCCACTTTCCTATGTACCTGTGCCTATGACAGGACTAACA
GACAGAATGACCTTTCTGGAAAGAGTAAAAAATTCAATGCTTTCAGTTTTGTTCCACTTC
TGGATTCAGGATTACGACTATCATTTTTGGGAAGAGTTTTATAGTAAGGCATTAGGAAGG
CCCACTACATTATGTGAGACTGTGGGAAAAGCTGAGATATGGCTAATACGAACATATTGG
GATTTTGAATTTCCTCAACCATACCAACCTAACTTTGAGTTTGTTGGAGGATTGCACTGT
AAACCTGCCAAAGCTTTGCCTAAGGAAATGGAAAATTTTGTCCAGAGTTCAGGGGAAGAT
GGTATTGTGGTGTTTTCTCTGGGGTCACTGTTTCAAAATGTTACAGAAGAAAAGGCTAAT
ATCATTGCTTCAGCCCTTGCCCAGATCCCACAGAAGGTGTTATGGAGGTACAAAGGAAAA
AAACCATCCACATTAGGAGCCAATACTCGGCTGTATGATTGGATACCCCAGAATGATCTT
CTTGGTCATCCCAAAACCAAAGCTTTTATCACTCATGGTGGAATGAATGGGATCTATGAA
GCTATTTACCATGGGGTCCCTATGGTGGGAGTTCCCATATTTGGTGATCAGCTTGATAAC
ATAGCTCACATGAAGGCCAAAGGAGCAGCTGTAGAAATAAACTTCAAAACTATGACAAGC
GAAGATTTACTGAGGGCTTTGAGAACAGTCATTACCGATTCCTCTTATAAAGAGAATGCT
ATGAGATTATCAAGAATTCACCATGATCAACCTGTAAAGCCCCTAGATCGAGCAGTCTTC
TGGATCGAGTTTGTCATGCGCCACAAAGGAGCCAAGCACCTGCGATCAGCTGCCCATGAC
CTCACCTGGTTCCAGCACTACTCTATAGATGTGATTGGGTTCCTGCTGGCCTGTGTGGCA
ACTGCTATATTCTTGTTCACAAAATGTTTTTTATTTTCCTGTCAAAAATTTAATAAAACT
AGAAAGATAGAAAAGAGGGAATAG
Enzyme 88 GenBank Gene ID NM_024743.3 Link Image
Enzyme 88 GeneCard ID UGT2A3 Link Image
Enzyme 88 GenAtlas ID UGT2A3 Link Image
Enzyme 88 HGNC ID HGNC:28528 Link Image
Enzyme 88 Chromosome Location 4
Enzyme 88 Locus 4q13.2
Enzyme 88 SNPs SNPJam Report Link Image
Enzyme 88 General References
  1. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 88 Metabolite References Not Available
Enzyme 89 [top]
Enzyme 89 ID 13094
Enzyme 89 Name Ribonucleoside-diphosphate reductase subunit M2 B
Enzyme 89 Synonyms
  1. TP53-inducible ribonucleotide reductase M2 B
  2. p53-inducible ribonucleotide reductase small subunit 2-like protein
  3. p53R2
Enzyme 89 Gene Name RRM2B
Enzyme 89 Protein Sequence >Ribonucleoside-diphosphate reductase subunit M2 B
MGDPERPEAAGLDQDERSSSDTNESEIKSNEEPLLRKSSRRFVIFPIQYPDIWKMYKQAQ
ASFWTAEEVDLSKDLPHWNKLKADEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEA
RCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRK
STFGERVVAFAAVEGVFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQ
YLVNKPSEERVREIIVDAVKIEQEFLTEALPVGLIGMNCILMKQYIEFVADRLLVELGFS
KVFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDADF
Enzyme 89 Number of Residues 351
Enzyme 89 Molecular Weight 40736.1
Enzyme 89 Theoretical pI 4.61
Enzyme 89 GO Classification
Function
  • binding
  • catalytic activity
  • cation binding
  • ion binding
  • metal ion binding
  • oxidoreductase activity
  • oxidoreductase activity, acting on CH or CH2 groups
  • oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
  • ribonucleoside-diphosphate reductase activity
  • transition metal ion binding
Process
  • cellular nitrogen compound metabolic process
  • deoxyribonucleoside diphosphate metabolic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside diphosphate metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • oxidation reduction
Component
Enzyme 89 General Function Involved in oxidoreductase activity
Enzyme 89 Specific Function Plays a pivotal role in cell survival by repairing damaged DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free radical center required for catalysis. Forms an active ribonucleotide reductase (RNR) complex with RRM1 which is expressed both in resting and proliferating cells in response to DNA damage
Enzyme 89 Pathways
Enzyme 89 Reactions
  • 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294]
Enzyme 89 Pfam Domain Function
Enzyme 89 Signals
  • None
Enzyme 89 Transmembrane Regions
  • None
Enzyme 89 Essentiality Not Available
Enzyme 89 GenBank ID Protein Not Available
Enzyme 89 UniProtKB/Swiss-Prot ID Q7LG56 Link Image
Enzyme 89 UniProtKB/Swiss-Prot Entry Name RIR2B_HUMAN Link Image
Enzyme 89 PDB ID Not Available
Enzyme 89 Cellular Location Not Available
Enzyme 89 Gene Sequence >1056 bp
ATGGGCGACCCGGAAAGGCCGGAAGCGGCCGGGCTGGATCAGGATGAGAGATCATCTTCA
GACACCAACGAAAGTGAAATAAAGTCAAATGAAGAGCCACTCCTAAGAAAGAGTTCTCGC
CGGTTTGTCATCTTTCCAATCCAGTACCCTGATATTTGGAAAATGTATAAACAGGCACAG
GCTTCCTTCTGGACAGCAGAAGAGGTCGACTTATCAAAGGATCTCCCTCACTGGAACAAG
CTTAAAGCAGATGAGAAGTACTTCATCTCTCACATCTTAGCCTTTTTTGCAGCCAGTGAT
GGAATTGTAAATGAAAATTTGGTGGAGCGCTTTAGTCAGGAGGTGCAGGTTCCAGAGGCT
CGCTGTTTCTATGGCTTTCAAATTCTCATCGAGAATGTTCACTCAGAGATGTACAGTTTG
CTGATAGACACTTACATCAGAGATCCCAAGAAAAGGGAATTTTTATTTAATGCAATTGAA
ACCATGCCCTATGTTAAGAAAAAAGCAGATTGGGCCTTGCGATGGATAGCAGATAGAAAA
TCTACTTTTGGGGAAAGAGTGGTGGCCTTTGCTGCTGTAGAAGGAGTTTTCTTCTCAGGA
TCTTTTGCTGCTATATTCTGGCTAAAGAAGAGAGGTCTTATGCCAGGACTCACTTTTTCC
AATGAACTCATCAGCAGAGATGAAGGACTTCACTGTGACTTTGCTTGCCTGATGTTCCAA
TACTTAGTAAATAAGCCTTCAGAAGAAAGGGTCAGGGAGATCATTGTTGATGCTGTCAAA
ATTGAGCAGGAGTTTTTAACAGAAGCCTTGCCAGTTGGCCTCATTGGAATGAATTGCATT
TTGATGAAACAGTACATTGAGTTTGTAGCTGACAGATTACTTGTGGAACTTGGATTCTCA
AAGGTTTTTCAGGCAGAAAATCCTTTTGATTTTATGGAAAACATTTCTTTAGAAGGAAAA
ACAAATTTCTTTGAGAAACGAGTTTCAGAGTATCAGCGTTTTGCAGTTATGGCAGAAACC
ACAGATAACGTCTTCACCTTGGATGCAGATTTTTAA
Enzyme 89 GenBank Gene ID AB036063 Link Image
Enzyme 89 GeneCard ID RRM2B Link Image
Enzyme 89 GenAtlas ID RRM2B Link Image
Enzyme 89 HGNC ID HGNC:17296 Link Image
Enzyme 89 Chromosome Location 8
Enzyme 89 Locus 8q23.1
Enzyme 89 SNPs SNPJam Report Link Image
Enzyme 89 General References
  1. Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, Takei Y, Nakamura Y: A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage. Nature. 2000 Mar 2;404(6773):42-9. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Guittet O, Hakansson P, Voevodskaya N, Fridd S, Graslund A, Arakawa H, Nakamura Y, Thelander L: Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells. J Biol Chem. 2001 Nov 2;276(44):40647-51. Epub 2001 Aug 21. [PubMed Link Image]
  6. Yamaguchi T, Matsuda K, Sagiya Y, Iwadate M, Fujino MA, Nakamura Y, Arakawa H: p53R2-dependent pathway for DNA synthesis in a p53-regulated cell cycle checkpoint. Cancer Res. 2001 Nov 15;61(22):8256-62. [PubMed Link Image]
  7. Xue L, Zhou B, Liu X, Qiu W, Jin Z, Yen Y: Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. Cancer Res. 2003 Mar 1;63(5):980-6. [PubMed Link Image]
  8. Zhou B, Liu X, Mo X, Xue L, Darwish D, Qiu W, Shih J, Hwu EB, Luh F, Yen Y: The human ribonucleotide reductase subunit hRRM2 complements p53R2 in response to UV-induced DNA repair in cells with mutant p53. Cancer Res. 2003 Oct 15;63(20):6583-94. [PubMed Link Image]
  9. Qiu W, Zhou B, Darwish D, Shao J, Yen Y: Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. Biochem Biophys Res Commun. 2006 Feb 10;340(2):428-34. Epub 2005 Dec 15. [PubMed Link Image]
  10. Tyynismaa H, Ylikallio E, Patel M, Molnar MJ, Haller RG, Suomalainen A: A heterozygous truncating mutation in RRM2B causes autosomal-dominant progressive external ophthalmoplegia with multiple mtDNA deletions. Am J Hum Genet. 2009 Aug;85(2):290-5. Epub 2009 Aug 6. [PubMed Link Image]
  11. Smith P, Zhou B, Ho N, Yuan YC, Su L, Tsai SC, Yen Y: 2.6 A X-ray crystal structure of human p53R2, a p53-inducible ribonucleotide reductase . Biochemistry. 2009 Nov 24;48(46):11134-41. [PubMed Link Image]
  12. Bourdon A, Minai L, Serre V, Jais JP, Sarzi E, Aubert S, Chretien D, de Lonlay P, Paquis-Flucklinger V, Arakawa H, Nakamura Y, Munnich A, Rotig A: Mutation of RRM2B, encoding p53-controlled ribonucleotide reductase (p53R2), causes severe mitochondrial DNA depletion. Nat Genet. 2007 Jun;39(6):776-80. Epub 2007 May 7. [PubMed Link Image]
  13. Bornstein B, Area E, Flanigan KM, Ganesh J, Jayakar P, Swoboda KJ, Coku J, Naini A, Shanske S, Tanji K, Hirano M, DiMauro S: Mitochondrial DNA depletion syndrome due to mutations in the RRM2B gene. Neuromuscul Disord. 2008 Jun;18(6):453-9. Epub 2008 May 27. [PubMed Link Image]
Enzyme 89 Metabolite References Not Available
Enzyme 90 [top]
Enzyme 90 ID 13097
Enzyme 90 Name UMP-CMP kinase 2, mitochondrial
Enzyme 90 Synonyms Not Available
Enzyme 90 Gene Name CMPK2
Enzyme 90 Protein Sequence >UMP-CMP kinase 2, mitochondrial
MAFARRLLRGPLSGPLLGRRGVCAGAMAPPRRFVLELPDCTLAHFALGADAPGDADAPDP
RLAALLGPPERSYSLCVPVTPDAGCGARVRAARLHQRLLHQLRRGPFQRCQLLRLLCYCP
GGQAGGAQQGFLLRDPLDDPDTRQALLELLGACQEAPRPHLGEFEADPRGQLWQRLWEVQ
DGRRLQVGCAQVVPVPEPPLHPVVPDLPSSVVFPDREAARAVLEECTSFIPEARAVLDLV
DQCPKQIQKGKFQVVAIEGLDATGKTTVTQSVADSLKAVLLKSPPSCIGQWRKIFDDEPT
IIRRAFYSLGNYIVASEIAKESAKSPVIVDRYWHSTATYAIATEVSGGLQHLPPAHHPVY
QWPEDLLKPDLILLLTVSPEERLQRLQGRGMEKTREEAELEANSVFRQKVEMSYQRMENP
GCHVVDASPSREKVLQTVLSLIQNSFSEP
Enzyme 90 Number of Residues 449
Enzyme 90 Molecular Weight 49447.3
Enzyme 90 Theoretical pI 7.00
Enzyme 90 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • nucleoside binding
  • phosphotransferase activity, phosphate group as acceptor
  • purine nucleoside binding
  • thymidylate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular nitrogen compound metabolic process
  • dTDP biosynthetic process
  • metabolic process
  • nitrogen compound metabolic process
  • nucleobase, nucleoside and nucleotide metabolic process
  • nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
  • nucleoside phosphate metabolic process
  • nucleotide metabolic process
  • pyrimidine deoxyribonucleoside diphosphate biosynthetic process
  • pyrimidine nucleoside diphosphate biosynthetic process
  • pyrimidine nucleotide biosynthetic process
  • pyrimidine nucleotide metabolic process
Component
Enzyme 90 General Function Involved in thymidylate kinase activity
Enzyme 90 Specific Function May participate in dUTP and dCTP synthesis in mitochondria. Is able to phosphorylate dUMP, dCMP, CMP, UMP and monophosphates of the pyrimidine nucleoside analogs ddC, dFdC, araC, BVDU and FdUrd with ATP as phosphate donor. Efficacy is highest for dUMP followed by dCMP; CMP and UMP are poor substrates. May be involved in mtDNA depletion caused by long term treatment with ddC or other pyrimidine analogs
Enzyme 90 Pathways Not Available
Enzyme 90 Reactions
  • ATP + (d)CMP = ADP + (d)CDP [RN:R00512 R01665]
Enzyme 90 Pfam Domain Function
Enzyme 90 Signals
  • None
Enzyme 90 Transmembrane Regions
  • None
Enzyme 90 Essentiality Not Available
Enzyme 90 GenBank ID Protein 117606370 Link Image
Enzyme 90 UniProtKB/Swiss-Prot ID Q5EBM0 Link Image
Enzyme 90 UniProtKB/Swiss-Prot Entry Name CMPK2_HUMAN Link Image
Enzyme 90 PDB ID Not Available
Enzyme 90 Cellular Location Not Available
Enzyme 90 Gene Sequence >1350 bp
ATGGCCTTCGCCCGCCGGCTCCTGCGCGGGCCACTGTCGGGGCCGCTGCTCGGGCGGCGC
GGGGTCTGCGCTGGGGCCATGGCTCCGCCGCGCCGCTTCGTCCTGGAGCTTCCCGACTGC
ACCCTGGCTCACTTCGCCCTAGGCGCCGACGCCCCCGGCGACGCAGACGCCCCCGACCCC
CGCCTGGCGGCGCTGCTGGGGCCCCCGGAGCGCAGCTACTCGCTGTGCGTGCCCGTGACC
CCGGACGCCGGCTGCGGGGCCCGGGTCCGGGCGGCGCGGCTGCACCAGCGCCTGCTGCAC
CAGCTGCGCCGCGGCCCCTTCCAGCGGTGCCAGCTGCTCAGGCTGCTCTGCTACTGCCCG
GGCGGCCAGGCCGGCGGCGCACAGCAAGGCTTCCTGCTGCGCGACCCCCTGGATGACCCT
GACACCCGGCAAGCGCTGCTCGAGCTGCTGGGCGCCTGTCAGGAGGCACCACGCCCGCAC
TTGGGCGAGTTCGAGGCCGACCCGCGCGGCCAGCTGTGGCAGCGCCTCTGGGAGGTGCAA
GACGGCAGGCGGCTGCAGGTGGGCTGCGCACAGGTCGTGCCCGTCCCGGAGCCCCCGCTG
CACCCGGTGGTGCCAGACTTGCCCAGTTCCGTGGTCTTCCCGGACCGGGAAGCCGCCCGG
GCCGTTTTGGAGGAGTGTACCTCCTTTATTCCTGAAGCCCGGGCAGTGCTTGACCTGGTC
GACCAGTGCCCAAAACAGATCCAGAAAGGAAAGTTCCAGGTTGTTGCCATCGAAGGACTG
GATGCCACGGGTAAAACCACGGTGACCCAGTCAGTGGCAGATTCACTTAAGGCTGTCCTC
TTAAAGTCACCACCCTCTTGCATTGGCCAGTGGAGGAAGATCTTTGATGATGAACCAACT
ATCATTAGAAGAGCTTTTTACTCTTTGGGCAATTATATTGTGGCCTCCGAAATAGCTAAA
GAATCTGCCAAATCTCCTGTGATTGTAGACAGGTACTGGCACAGCACGGCCACCTATGCC
ATAGCCACTGAGGTGAGTGGGGGTCTCCAGCACCTGCCCCCAGCCCATCACCCTGTGTAC
CAGTGGCCAGAGGACCTGCTCAAACCTGACCTTATCCTGCTGCTCACTGTGAGTCCTGAG
GAGAGGTTGCAGAGGCTGCAGGGCCGGGGCATGGAGAAGACCAGGGAAGAAGCAGAACTT
GAGGCCAACAGTGTGTTTCGTCAAAAGGTAGAAATGTCCTACCAGCGGATGGAGAATCCT
GGCTGCCATGTGGTTGATGCCAGCCCCTCCAGAGAAAAGGTCCTGCAGACGGTATTAAGC
CTAATCCAGAATAGTTTTAGTGAACCGTAG
Enzyme 90 GenBank Gene ID NM_207315.2 Link Image
Enzyme 90 GeneCard ID CMPK2 Link Image
Enzyme 90 GenAtlas ID CMPK2 Link Image
Enzyme 90 HGNC ID HGNC:27015 Link Image
Enzyme 90 Chromosome Location 2
Enzyme 90 Locus 2p25.2
Enzyme 90 SNPs SNPJam Report Link Image
Enzyme 90 General References
  1. Xu Y, Johansson M, Karlsson A: Human UMP-CMP kinase 2, a novel nucleoside monophosphate kinase localized in mitochondria. J Biol Chem. 2008 Jan 18;283(3):1563-71. Epub 2007 Nov 13. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 90 Metabolite References Not Available
Enzyme 91 [top]
Enzyme 91 ID 13098
Enzyme 91 Name Uridine-cytidine kinase-like 1
Enzyme 91 Synonyms Not Available
Enzyme 91 Gene Name UCKL1
Enzyme 91 Protein Sequence >Uridine-cytidine kinase-like 1
MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKR
TTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIE
ALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKV
PIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRR
DISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQL
EERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRL
LIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIG
TILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIF
LLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSD
EEEVAYTG
Enzyme 91 Number of Residues 548
Enzyme 91 Molecular Weight 61140.4
Enzyme 91 Theoretical pI 7.40
Enzyme 91 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
Component
Enzyme 91 General Function Involved in ATP binding
Enzyme 91 Specific Function May contribute to UTP accumulation needed for blast transformation and proliferation
Enzyme 91 Pathways
Enzyme 91 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964]
Enzyme 91 Pfam Domain Function
Enzyme 91 Signals
  • None
Enzyme 91 Transmembrane Regions
  • None
Enzyme 91 Essentiality Not Available
Enzyme 91 GenBank ID Protein 57863312 Link Image
Enzyme 91 UniProtKB/Swiss-Prot ID Q9NWZ5 Link Image
Enzyme 91 UniProtKB/Swiss-Prot Entry Name UCKL1_HUMAN Link Image
Enzyme 91 PDB ID Not Available
Enzyme 91 Cellular Location Not Available
Enzyme 91 Gene Sequence >1647 bp
ATGGCTGCGCCCCCGGCCCGCGCGGACGCTGATCCTTCGCCCACGTCGCCACCTACGGCC
CGAGACACACCAGGCCGGCAGGCTGAGAAAAGCGAGACCGCGTGCGAGGACCGCAGCAAT
GCAGAGTCCCTGGACAGGCTCCTGCCACCTGTGGGCACTGGGCGCTCTCCCCGGAAGCGG
ACCACCAGCCAGTGCAAGTCAGAGCCTCCCCTGCTGCGTACAAGCAAGCGTACCATCTAC
ACCGCCGGGCGGCCGCCCTGGTACAATGAACACGGCACGCAATCCAAAGAGGCCTTCGCC
ATCGGCTTGGGAGGCGGCAGTGCCTCTGGGAAGACCACTGTGGCCAGAATGATCATCGAG
GCCCTGGATGTGCCCTGGGTGGTCTTGCTGTCCATGGACTCCTTCTACAAGGTGCTGACT
GAGCAGCAGCAGGAACAGGCCGCACACAACAACTTCAACTTCGACCACCCAGATGCCTTT
GACTTCGACCTCATCATTTCCACCCTCAAGAAGCTGAAGCAGGGGAAGAGTGTCAAGGTG
CCCATTTATGACTTCACCACGCACAGCCGGAAGAAGGACTGGAAAACACTGTATGGTGCA
AACGTCATCATCTTTGAGGGCATCATGGCCTTTGCTGACAAGACACTGTTGGAGCTCCTG
GACATGAAGATCTTTGTGGACACAGACTCCGACATCCGCCTGGTACGGCGGCTGCGCCGG
GACATCAGTGAGCGCGGCCGGGACATCGAGGGTGTCATCAAGCAGTACAACAAGTTTGTC
AAGCCCTCCTTCGACCAGTACATCCAGCCCACCATGCGCCTGGCAGACATCGTGGTCCCC
AGAGGGAGCGGCAACACGGTGGCCATCGACCTGATTGTGCAGCACGTGCACAGCCAGCTG
GAGGAGCGTGAACTCAGCGTCAGGGCTGCGCTGGCCTCGGCACACCAGTGCCACCCGCTG
CCCCGGACGCTGAGCGTCCTGAAGAGCACGCCGCAGGTACGGGGCATGCACACCATCATC
AGGGACAAGGAGACCAGTCGCGACGAGTTCATCTTCTACTCCAAGAGACTGATGCGGCTG
CTCATCGAGCACGCGCTCTCCTTCCTGCCCTTTCAGGACTGCGTCGTACAGACCCCGCAG
GGGCAGGACTATGCGGGCAAGTGCTATGCGGGGAAGCAGATCACCGGTGTGTCCATTCTG
CGCGCCGGTGAAACCATGGAGCCCGCGCTGCGCGCTGTGTGCAAAGACGTGCGCATCGGC
ACCATCCTCATCCAGACCAACCAGCTTACCGGGGAGCCCGAGCTCCACTACCTGAGGCTG
CCCAAGGACATCAGCGATGACCACGTGATCCTCATGGACTGCACCGTGTCCACGGGCGCG
GCGGCCATGATGGCAGTGCGCGTGCTCCTGGACCACGACGTGCCTGAGGACAAGATCTTT
TTGCTGTCGCTGCTCATGGCAGAGATGGGCGTGCACTCAGTGGCCTATGCATTTCCGCGA
GTGAGAATCATCACCACGGCGGTGGACAAGCGGGTCAATGACCTTTTCCGCATCATCCCA
GGCATTGGGAACTTTGGCGACCGCTACTTTGGGACAGACGCGGTCCCCGATGGCAGTGAC
GAGGAGGAAGTGGCCTACACGGGTTAG
Enzyme 91 GenBank Gene ID NM_017859.3 Link Image
Enzyme 91 GeneCard ID UCKL1 Link Image
Enzyme 91 GenAtlas ID UCKL1 Link Image
Enzyme 91 HGNC ID HGNC:15938 Link Image
Enzyme 91 Chromosome Location 2
Enzyme 91 Locus 20q13.33
Enzyme 91 SNPs SNPJam Report Link Image
Enzyme 91 General References
  1. Kashuba E, Kashuba V, Sandalova T, Klein G, Szekely L: Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase. BMC Cell Biol. 2002 Aug 29;3:23. Epub 2002 Aug 29. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  5. Fortier JM, Kornbluth J: NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase. J Immunol. 2006 Jun 1;176(11):6454-63. [PubMed Link Image]
  6. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed Link Image]
  7. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed Link Image]
  8. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed Link Image]
Enzyme 91 Metabolite References Not Available
Enzyme 92 [top]
Enzyme 92 ID 13379
Enzyme 92 Name Ectonucleoside triphosphate diphosphohydrolase 8
Enzyme 92 Synonyms
  1. E-NTPDase 8
  2. NTPDase 8
  3. NTPDase8
Enzyme 92 Gene Name ENTPD8
Enzyme 92 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 8
MGLSRKEQVFLALLGASGVSGLTALILLLVEATSVLLPTDIKFGIVFDAGSSHTSLFLYQ
WLANKENGTGVVSQALACQVEGPGISSYTSNAAQAGESLQGCLEEALVLIPEAQHRKTPT
FLGATAGMRLLSRKNSSQARDIFAAVTQVLGRSPVDFWGAELLAGQAEGAFGWITVNYGL
GTLVKYSFTGEWIQPPEEMLVGALDMGGASTQITFVPGGPILDKSTQADFRLYGSDYSVY
THSYLCFGRDQMLSRLLVGLVQSRPAALLRHPCYLSGYQTTLALGPLYESPCVHATPPLS
LPQNLTVEGTGNPGACVSAIRELFNFSSCQGQEDCAFDGVYQPPLRGQFYAFSNFYYTFH
FLNLTSRQPLSTVNATIWEFCQRPWKLVEASYPGQDRWLRDYCASGLYILTLLHEGYGFS
EETWPSLEFRKQAGGVDIGWTLGYMLNLTGMIPADAPAQWRAESYGVWVAKVVFMVLALV
AVVGAALVQLFWLQD
Enzyme 92 Number of Residues 495
Enzyme 92 Molecular Weight 53903.1
Enzyme 92 Theoretical pI 4.96
Enzyme 92 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 92 General Function Involved in hydrolase activity
Enzyme 92 Specific Function Canalicular ectonucleoside NTPDase responsible for the main hepatic NTPDase activity. Ectonucleoside NTPDases catalyze the hydrolyzis of gamma- and beta-phosphate residues of nucleotides, playing a central role in concentration of extracellular nucleotides. Has activity toward ATP, ADP, UTP and UDP, but not toward AMP
Enzyme 92 Pathways
Enzyme 92 Reactions
  • ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
Enzyme 92 Pfam Domain Function
Enzyme 92 Signals
  • None
Enzyme 92 Transmembrane Regions
  • 9-29 472-492
Enzyme 92 Essentiality Not Available
Enzyme 92 GenBank ID Protein 110431368 Link Image
Enzyme 92 UniProtKB/Swiss-Prot ID Q5MY95 Link Image
Enzyme 92 UniProtKB/Swiss-Prot Entry Name ENTP8_HUMAN Link Image
Enzyme 92 PDB ID Not Available
Enzyme 92 Cellular Location Not Available
Enzyme 92 Gene Sequence >1488 bp
ATGGGGCTGTCCCGGAAGGAGCAGGTCTTCTTGGCCCTGCTGGGGGCCTCGGGGGTCTCA
GGCCTCACGGCACTCATTCTCCTCCTGGTGGAGGCCACCAGCGTGCTCCTGCCCACAGAC
ATCAAGTTTGGGATCGTGTTTGATGCGGGCTCCTCCCACACGTCCCTCTTCCTGTATCAG
TGGCTGGCGAACAAGGAGAATGGCACGGGTGTGGTCAGCCAGGCCCTGGCCTGCCAGGTG
GAAGGGCCTGGAATCTCCTCCTACACTTCTAATGCTGCACAGGCTGGTGAGAGCCTGCAG
GGCTGCTTGGAGGAGGCGCTGGTGCTGATCCCAGAGGCCCAGCATCGGAAAACACCCACG
TTCCTGGGGGCCACGGCTGGCATGAGGTTGCTCAGCCGGAAGAACAGCTCTCAGGCCAGG
GACATCTTTGCAGCAGTCACCCAGGTCCTGGGCCGGTCTCCCGTGGACTTTTGGGGTGCC
GAGCTCCTGGCCGGGCAGGCCGAAGGTGCCTTTGGTTGGATCACTGTCAACTACGGCTTG
GGGACGCTGGTCAAGTACTCCTTCACTGGAGAATGGATCCAGCCTCCGGAGGAGATGCTG
GTGGGTGCCCTGGACATGGGAGGGGCCTCCACCCAGATCACGTTCGTGCCTGGGGGCCCC
ATCTTGGACAAGAGCACCCAGGCCGATTTTCGCCTCTACGGCTCCGACTACAGCGTCTAC
ACTCACAGCTACCTGTGCTTTGGACGGGACCAGATGCTGAGCAGGCTCCTCGTGGGGCTG
GTACAGAGCCGCCCGGCTGCCCTGCTCCGTCACCCGTGCTACCTCAGCGGCTACCAGACC
ACACTGGCCCTGGGCCCGCTGTATGAGTCACCCTGTGTCCACGCCACGCCCCCGCTGAGC
CTCCCCCAGAACCTCACAGTTGAAGGGACAGGCAACCCTGGAGCCTGCGTCTCAGCCATC
CGGGAACTTTTCAACTTCTCCAGCTGCCAGGGCCAGGAGGACTGCGCCTTTGACGGGGTC
TACCAGCCCCCGCTGCGGGGCCAGTTCTATGCCTTCTCCAACTTCTACTACACCTTCCAC
TTCCTGAACCTCACCTCCAGGCAGCCCCTGAGCACGGTCAACGCCACCATCTGGGAGTTT
TGCCAGAGGCCCTGGAAACTGGTGGAGGCCAGCTACCCTGGGCAGGACCGCTGGCTGCGG
GACTACTGTGCCTCAGGCCTGTACATCCTCACCCTCCTGCACGAGGGCTACGGGTTCAGC
GAGGAGACCTGGCCCAGCCTCGAGTTCCGAAAGCAGGCGGGCGGTGTGGACATTGGCTGG
ACACTGGGCTACATGCTGAACCTGACCGGGATGATCCCGGCCGATGCGCCGGCTCAGTGG
CGGGCAGAGAGCTACGGCGTCTGGGTGGCCAAAGTGGTGTTCATGGTGCTGGCCCTGGTG
GCGGTGGTGGGGGCTGCCTTGGTCCAGCTCTTCTGGTTGCAGGACTAG
Enzyme 92 GenBank Gene ID NM_001033113.1 Link Image
Enzyme 92 GeneCard ID ENTPD8 Link Image
Enzyme 92 GenAtlas ID ENTPD8 Link Image
Enzyme 92 HGNC ID HGNC:24860 Link Image
Enzyme 92 Chromosome Location 9
Enzyme 92 Locus 9q34.3
Enzyme 92 SNPs SNPJam Report Link Image
Enzyme 92 General References
  1. Knowles AF, Li C: Molecular cloning and characterization of expressed human ecto-nucleoside triphosphate diphosphohydrolase 8 (E-NTPDase 8) and its soluble extracellular domain. Biochemistry. 2006 Jun 13;45(23):7323-33. [PubMed Link Image]
  2. Fausther M, Lecka J, Kukulski F, Levesque SA, Pelletier J, Zimmermann H, Dranoff JA, Sevigny J: Cloning, purification, and identification of the liver canalicular ecto-ATPase as NTPDase8. Am J Physiol Gastrointest Liver Physiol. 2007 Mar;292(3):G785-95. Epub 2006 Nov 9. [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. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. Levesque SA, Lavoie EG, Lecka J, Bigonnesse F, Sevigny J: Specificity of the ecto-ATPase inhibitor ARL 67156 on human and mouse ectonucleotidases. Br J Pharmacol. 2007 Sep;152(1):141-50. Epub 2007 Jul 2. [PubMed Link Image]
Enzyme 92 Metabolite References Not Available
Enzyme 93 [top]
Enzyme 93 ID 13420
Enzyme 93 Name Polypeptide N-acetylgalactosaminyltransferase-like 6
Enzyme 93 Synonyms
  1. Polypeptide GalNAc transferase 17
  2. GalNAc-T17
  3. pp-GaNTase 17
  4. Protein-UDP acetylgalactosaminyltransferase 17
  5. Putative polypeptide N-acetylgalactosaminyltransferase 17
  6. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17
Enzyme 93 Gene Name GALNTL6
Enzyme 93 Protein Sequence >Polypeptide N-acetylgalactosaminyltransferase-like 6
MKRKQKRFLQMTLLFTVALIFLPNVGLWSLYKDKHLVKSAEPGEQQTFPLGLGDGQFYSW
TDGLRRKDWHDYESIQKEAMRSGKGEHGKPYPLTEEDHDDSAYRENGFNIFVSNNIALER
SLPDIRHANCKHKMYLERLPNTSIIIPFHNEGWTSLLRTIHSIINRTPGSLIAEIILVDD
FSEREHLKDKLEEYMARFSKVRIVRTKKREGLIRTRLLGASMARGEVLTFLDSHCEVNVN
WLPPLLNQIALNHKTIVCPMIDVIDHNHFGYEAQAGDAMRGAFDWEMYYKRIPIPPELQR
ADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGEMFDVPC
SRVGHIYRKYVPYKVPSGTSLARNLKRVAETWMDEFAEYIYQRRPEYRHLSTGDISAQKE
LRKQLKCKDFKWFMAAVAWDVPKYYPPVEPPPAAWGEIRNVAANLCVDSKHGATGTELRL
DICVKDGSERTWSHEQLFTFGWREDIRPGEPLHTRKFCFDAISHNSPVTLYDCHGMKGNQ
LWGYRKDRTLFHPVSNSCMDCNPAEKKIFMARCDPLSETQQWIFEHINMTVLEKFNHHAN
S
Enzyme 93 Number of Residues 601
Enzyme 93 Molecular Weight 69787.2
Enzyme 93 Theoretical pI 7.48
Enzyme 93 GO Classification Not Available
Enzyme 93 General Function Involved in metal ion binding
Enzyme 93 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
Enzyme 93 Pathways Not Available
Enzyme 93 Reactions
  • UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide [RN:R02183]
Enzyme 93 Pfam Domain Function
Enzyme 93 Signals
  • None
Enzyme 93 Transmembrane Regions
  • 8-28
Enzyme 93 Essentiality Not Available
Enzyme 93 GenBank ID Protein 194018457 Link Image
Enzyme 93 UniProtKB/Swiss-Prot ID Q49A17 Link Image
Enzyme 93 UniProtKB/Swiss-Prot Entry Name GLTL6_HUMAN Link Image
Enzyme 93 PDB ID Not Available
Enzyme 93 Cellular Location Not Available
Enzyme 93 Gene Sequence >1806 bp
ATGAAGAGGAAACAGAAGAGATTTCTGCAGATGACTTTGTTGTTCACGGTGGCTTTAATT
TTCCTGCCTAACGTTGGTCTCTGGTCTCTGTACAAGGATAAGCACCTGGTGAAGTCAGCG
GAGCCCGGGGAGCAGCAGACATTTCCACTGGGCCTGGGAGATGGGCAATTCTATTCATGG
ACAGATGGTTTGAGAAGAAAGGACTGGCATGACTATGAAAGCATTCAGAAAGAGGCTATG
CGCTCAGGGAAAGGTGAACATGGGAAACCTTACCCCCTTACTGAAGAGGACCATGATGAC
TCAGCTTACAGGGAAAATGGTTTTAATATTTTCGTCAGCAACAATATTGCTCTAGAGAGG
TCTCTGCCAGATATTCGTCATGCTAACTGTAAGCATAAGATGTATCTGGAAAGGCTGCCA
AACACCAGCATCATTATCCCATTTCATAATGAAGGTTGGACTTCACTCCTGCGGACCATA
CACAGTATAATTAACCGAACCCCAGGGAGTCTGATAGCAGAAATCATTCTAGTAGATGAC
TTCAGTGAGAGAGAACACCTGAAGGATAAATTGGAAGAATACATGGCCCGATTTTCCAAA
GTGAGGATTGTTCGCACCAAGAAAAGAGAAGGACTCATCCGGACCCGTCTCCTGGGGGCA
TCTATGGCCAGAGGAGAAGTCCTGACATTCCTGGACTCCCACTGCGAGGTCAATGTGAAC
TGGCTGCCCCCACTCCTCAACCAAATTGCACTAAACCACAAAACCATCGTGTGTCCCATG
ATCGATGTCATTGACCACAATCACTTCGGGTATGAGGCACAAGCTGGGGATGCCATGCGA
GGAGCCTTCGACTGGGAAATGTACTACAAAAGAATCCCCATCCCTCCAGAGCTCCAGAGG
GCAGATCCCAGCGACCCTTTTGAGTCTCCTGTTATGGCTGGAGGTCTCTTTGCTGTGGAT
CGGAAATGGTTTTGGGAATTGGGTGGCTATGATCCAGGTTTAGAAATCTGGGGAGGAGAA
CAGTATGAAATCTCTTTTAAGGTTTGGATGTGTGGAGGAGAAATGTTTGATGTTCCATGT
TCTAGAGTTGGTCATATCTACAGGAAGTACGTTCCATACAAAGTTCCATCTGGGACAAGC
CTGGCAAGAAACCTGAAGCGGGTAGCTGAGACCTGGATGGATGAATTTGCCGAGTACATT
TACCAGCGGCGGCCGGAGTACAGGCATCTCTCCACGGGGGACATCTCTGCCCAGAAGGAG
CTGCGCAAGCAGCTCAAGTGCAAGGACTTCAAATGGTTCATGGCTGCTGTGGCCTGGGAC
GTGCCTAAATACTACCCTCCAGTGGAGCCCCCGCCTGCTGCCTGGGGGGAGATCCGAAAT
GTGGCAGCAAATCTCTGTGTGGACAGCAAGCATGGAGCCACCGGAACAGAGCTGAGGCTG
GACATCTGTGTCAAGGATGGTTCTGAAAGAACATGGTCTCATGAACAGCTTTTTACCTTT
GGATGGAGAGAAGATATTCGACCCGGTGAGCCACTGCATACCCGGAAATTCTGCTTTGAT
GCGATCTCACACAACAGCCCCGTTACACTCTATGACTGTCATGGCATGAAGGGGAACCAG
CTCTGGGGATACCGGAAGGACAGAACATTATTCCATCCTGTGAGCAACAGCTGCATGGAT
TGCAACCCCGCAGAGAAGAAGATTTTCATGGCCAGATGTGACCCTCTCTCTGAGACTCAG
CAGTGGATTTTTGAACACATTAATATGACTGTTTTAGAAAAATTTAACCACCATGCCAAC
TCCTAG
Enzyme 93 GenBank Gene ID NM_001034845.2 Link Image
Enzyme 93 GeneCard ID GALNTL6 Link Image
Enzyme 93 GenAtlas ID GALNTL6 Link Image
Enzyme 93 HGNC ID HGNC:33844 Link Image
Enzyme 93 Chromosome Location 4
Enzyme 93 Locus 4q34.1
Enzyme 93 SNPs SNPJam Report Link Image
Enzyme 93 General References
  1. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 93 Metabolite References Not Available
Enzyme 94 [top]
Enzyme 94 ID 13421
Enzyme 94 Name Putative polypeptide N-acetylgalactosaminyltransferase-like protein 5
Enzyme 94 Synonyms
  1. Polypeptide GalNAc transferase 15
  2. GalNAc-T15
  3. pp-GaNTase 15
  4. Protein-UDP acetylgalactosaminyltransferase 15
  5. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 15
Enzyme 94 Gene Name GALNTL5
Enzyme 94 Protein Sequence >Putative polypeptide N-acetylgalactosaminyltransferase-like protein 5
MRNAIIQGLFYGSLTFGIWTALLFIYLHHNHVSSWQKKSQEPLSAWSPGKKVHQQIIYGS
EQIPKPHVIVKRTDEDKAKSMLGTDFNHTNPELHKELLKYGFNVIISRSLGIEREVPDTR
SKMRLQKHYPARLPTASIVICFYNEECNALFQTMSSVTNLTPHYFLEEIILVDDMSKVDD
LKEKLDYHLETFRGKVKIIRNKKREGLIRARLIGASHASGDVLVFLDSHCEVNRVWLEPL
LHAIAKDPKMVVCPLIDVIDDRTLEYKPSPLVRGTFDWNLQFKWDNVFSYEMDGPEGSTK
PIRSPAMSGGIFAIRRHYFNEIGQYDKDMDFWGRENLELSLRIWMCGGQLFIIPCSRVGH
ISKKQTGKPSTIISAMTHNYLRLVHVWLDEYKEQFFLRKPGLKYVTYGNIRERVELRKRL
GCKSFQWYLDNVFPELEASVNSL
Enzyme 94 Number of Residues 443
Enzyme 94 Molecular Weight 51480.1
Enzyme 94 Theoretical pI 9.16
Enzyme 94 GO Classification Not Available
Enzyme 94 General Function Cell wall/membrane/envelope biogenesis
Enzyme 94 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 94 Pathways Not Available
Enzyme 94 Reactions Not Available
Enzyme 94 Pfam Domain Function
Enzyme 94 Signals
  • None
Enzyme 94 Transmembrane Regions
  • 5-27
Enzyme 94 Essentiality Not Available
Enzyme 94 GenBank ID Protein 281485547 Link Image
Enzyme 94 UniProtKB/Swiss-Prot ID Q7Z4T8 Link Image
Enzyme 94 UniProtKB/Swiss-Prot Entry Name GLTL5_HUMAN Link Image
Enzyme 94 PDB ID Not Available
Enzyme 94 Cellular Location Not Available
Enzyme 94 Gene Sequence >1332 bp
ATGAGAAATGCCATAATTCAAGGTTTATTCTATGGGTCCTTGACATTTGGGATCTGGACA
GCTCTGTTATTCATATATTTGCACCATAATCATGTGAGCAGCTGGCAGAAGAAAAGCCAG
GAGCCTCTGTCAGCTTGGTCCCCTGGAAAAAAAGTGCATCAGCAAATTATCTATGGCTCA
GAGCAAATACCAAAACCTCATGTAATAGTCAAAAGGACTGATGAAGATAAAGCAAAGTCT
ATGTTAGGTACAGATTTTAACCATACAAACCCAGAACTTCATAAAGAACTTTTAAAATAT
GGATTTAATGTGATTATCAGTAGAAGCTTGGGCATCGAAAGAGAAGTGCCAGATACCAGG
AGTAAAATGTGTCTTCAAAAACATTACCCAGCCCGCCTCCCGACTGCCAGCATTGTCATT
TGCTTCTATAATGAAGAATGTAATGCCTTGTTTCAGACCATGTCCAGTGTCACGAACCTC
ACGCCACACTATTTTCTTGAAGAAATTATTTTGGTAGATGACATGAGCAAAGTTGATGAT
TTGAAAGAAAAACTAGACTATCACCTGGAAACTTTTCGGGGAAAGGTTAAAATAATAAGA
AACAAAAAGAGAGAGGGGCTGATTCGAGCAAGGCTGATTGGAGCTTCTCATGCTTCAGGG
GATGTTCTGGTGTTCCTGGACAGCCACTGTGAGGTGAACAGAGTATGGCTGGAGCCCCTG
CTGCATGCCATTGCCAAGGACCCCAAAATGGTGGTGTGCCCCCTGATAGATGTCATTGAT
GATAGAACTCTGGAGTATAAGCCCTCTCCTCTTGTAAGGGGAACTTTTGATTGGAACCTA
CAATTTAAATGGGATAATGTTTTCTCTTATGAGATGGATGGACCAGAAGGATCTACTAAA
CCAATCCGGTCACCTGCAATGTCTGGAGGAATTTTTGCTATACGTCGGCATTATTTTAAT
GAAATTGGACAGTATGACAAGGATATGGATTTTTGGGGAAGAGAAAATTTGGAACTTTCA
CTAAGGATCTGGATGTGTGGAGGCCAACTCTTTATAATCCCCTGCTCTCGAGTAGGACAT
ATCAGTAAGAAACAAACTGGAAAACCTTCTACAATCATCAGTGCTATGACACATAACTAC
CTAAGACTGGTGCACGTTTGGCTGGATGAATATAAGGAGCAGTTTTTTCTTCGAAAGCCT
GGTCTGAAATATGTCACCTACGGAAATATTCGCGAGCGTGTTGAGTTAAGGAAACGACTG
GGTTGCAAGTCATTTCAGTGGTATTTGGATAATGTCTTCCCAGAGTTGGAGGCATCTGTG
AACAGCCTGTGA
Enzyme 94 GenBank Gene ID NM_145292.3 Link Image
Enzyme 94 GeneCard ID GALNTL5 Link Image
Enzyme 94 GenAtlas ID GALNTL5 Link Image
Enzyme 94 HGNC ID HGNC:21725 Link Image
Enzyme 94 Chromosome Location 7
Enzyme 94 Locus 7q36.1
Enzyme 94 SNPs SNPJam Report Link Image
Enzyme 94 General References
  1. Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed Link Image]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 94 Metabolite References Not Available
Enzyme 95 [top]
Enzyme 95 ID 15056
Enzyme 95 Name HCG2039726, isoform CRA_f
Enzyme 95 Synonyms
  1. SubName: UDP glycosyltransferase 1 family polypeptide A10
Enzyme 95 Gene Name UGT1A10
Enzyme 95 Protein Sequence >HCG2039726, isoform CRA_f
MARAGWTSPVPLCVCLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLERSLNCTVKTYSTSYTLEDQNREFMVFAHAQWKAQAQSIFSLLMSSSSGFLDLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDTCGLIVAKYFSLPSVVFTRGIFCHHLEEG
AQCPAPLSYVPNDLLGFSDAMTFKERVWNHIVHLEDHLFCQYLFRNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 95 Number of Residues 530
Enzyme 95 Molecular Weight 59809.1
Enzyme 95 Theoretical pI 7.31
Enzyme 95 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 95 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 95 Specific Function Not Available
Enzyme 95 Pathways Not Available
Enzyme 95 Reactions Not Available
Enzyme 95 Pfam Domain Function
Enzyme 95 Signals
  • None
Enzyme 95 Transmembrane Regions
  • None
Enzyme 95 Essentiality Not Available
Enzyme 95 GenBank ID Protein 40849852 Link Image
Enzyme 95 UniProtKB/Swiss-Prot ID Q5DT02 Link Image
Enzyme 95 UniProtKB/Swiss-Prot Entry Name Q5DT02_HUMAN Link Image
Enzyme 95 PDB ID Not Available
Enzyme 95 Cellular Location Not Available
Enzyme 95 Gene Sequence >1593 bp
ATGGCTCGCGCAGGGTGGACCAGCCCCGTTCCTTTATGTGTGTGTCTACTGCTGACCTGT
GGCTTTGCCGAGGCAGGGAAGCTGCTGGTAGTGCCCATGGATGGGAGTCACTGGTTCACC
ATGCAGTCGGTGGTGGAGAAACTTATCCTCAGGGGGCATGAGGTGGTTGTAGTCATGCCA
GAGGTGAGTTGGCAACTGGAAAGATCACTGAATTGCACAGTGAAGACTTACTCAACCTCG
TACACTCTGGAAGATCAGAACCGGGAATTCATGGTTTTCGCCCATGCTCAATGGAAAGCA
CAGGCACAAAGTATATTTTCTCTATTAATGAGTTCATCCAGTGGTTTTCTTGACTTATTT
TTTTCGCATTGCAGGAGTTTGTTTAATGACCGAAAATTAGTAGAATACTTAAAGGAGAGT
TCTTTTGATGCAGTGTTTCTGGATCCTTTTGATACCTGTGGCTTAATTGTTGCTAAATAT
TTCTCCCTCCCCTCTGTGGTCTTCACCAGGGGAATATTTTGCCACCATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAATGATCTCTTAGGGTTCTCAGATGCC
ATGACTTTCAAGGAGAGAGTATGGAACCACATCGTGCACTTGGAGGACCATTTATTTTGC
CAGTATCTTTTTAGAAATGCCCTAGAAATAGCCTCTGAAATTCTCCAAACCCCTGTCACG
GCATATGATCTCTACAGTCACACATCAATTTGGTTGTTGCGAACGGACTTTGTTTTGGAC
TATCCCAAACCCGTGATGCCCAACATGATCTTCATTGGTGGTATCAACTGTCATCAGGGA
AAGCCATTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATCG
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAAGATTTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACAGTGGCC
TTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 95 GenBank Gene ID AY435137 Link Image
Enzyme 95 GeneCard ID UGT1A10 Link Image
Enzyme 95 GenAtlas ID UGT1A10 Link Image
Enzyme 95 HGNC ID HGNC:12531 Link Image
Enzyme 95 Chromosome Location 2
Enzyme 95 Locus 2q37
Enzyme 95 SNPs SNPJam Report Link Image
Enzyme 95 General References
  1. Zhang T, Haws P, Wu Q: Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation. Genome Res. 2004 Jan;14(1):79-89. Epub 2003 Dec 12. [PubMed Link Image]
Enzyme 95 Metabolite References Not Available
Enzyme 96 [top]
Enzyme 96 ID 15057
Enzyme 96 Name HCG2039726, isoform CRA_e
Enzyme 96 Synonyms
  1. SubName: UDP glycosyltransferase 1 family polypeptide A8
Enzyme 96 Gene Name UGT1A8
Enzyme 96 Protein Sequence >HCG2039726, isoform CRA_e
MARTGWTSPIPLCVSLLLTCGFAEAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGKSLNCTVKTYSTSYTLEDLDREFMDFADAQWKAQVRSLFSLFLSSSNGFFNLF
FSHCRSLFNDRKLVEYLKESSFDAVFLDPFDACGLIVAKYFSLPSVVFARGIACHYLEEG
AQCPAPLSYVPRILLGFSDAMTFKERVRNHIMHLEEHLFCQYFSKNALEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLDYPKPVMPNMIFIGGINCHQGKPLPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 96 Number of Residues 530
Enzyme 96 Molecular Weight 59741.0
Enzyme 96 Theoretical pI 7.73
Enzyme 96 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 96 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 96 Specific Function Not Available
Enzyme 96 Pathways Not Available
Enzyme 96 Reactions Not Available
Enzyme 96 Pfam Domain Function
Enzyme 96 Signals
  • None
Enzyme 96 Transmembrane Regions
  • None
Enzyme 96 Essentiality Not Available
Enzyme 96 GenBank ID Protein 40849864 Link Image
Enzyme 96 UniProtKB/Swiss-Prot ID Q5DSZ6 Link Image
Enzyme 96 UniProtKB/Swiss-Prot Entry Name Q5DSZ6_HUMAN Link Image
Enzyme 96 PDB ID Not Available
Enzyme 96 Cellular Location Not Available
Enzyme 96 Gene Sequence >1593 bp
ATGGCTCGCACAGGGTGGACCAGCCCCATTCCCCTATGTGTTTCTCTGCTGCTGACCTGT
GGCTTTGCTGAGGCAGGGAAGCTGCTGGTAGTGCCCATGGATGGGAGTCACTGGTTCACC
ATGCAGTCGGTGGTGGAGAAACTTATCCTCAGGGGGCATGAGGTGGTTGTAGTCATGCCA
GAGGTGAGTTGGCAACTGGGAAAATCACTGAATTGCACAGTGAAGACTTACTCAACCTCA
TACACTCTGGAGGATCTGGACCGGGAATTCATGGATTTCGCCGATGCTCAATGGAAAGCA
CAAGTACGAAGTTTGTTTTCTCTATTTCTGAGTTCATCCAATGGTTTTTTTAACTTATTT
TTTTCGCATTGCAGGAGTTTGTTTAATGACCGAAAATTAGTAGAATACTTAAAGGAGAGT
TCTTTTGATGCGGTGTTTCTTGATCCTTTTGATGCCTGTGGCTTAATTGTTGCCAAATAT
TTCTCCCTCCCCTCTGTGGTCTTCGCCAGGGGAATAGCTTGCCACTATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAGAATTCTCTTAGGGTTCTCAGATGCC
ATGACTTTCAAGGAGAGAGTACGGAACCACATCATGCACTTGGAGGAACATTTATTTTGC
CAGTATTTTTCCAAAAATGCCCTAGAAATAGCCTCTGAAATTCTCCAAACACCTGTCACA
GCATATGATCTCTACAGCCACACATCAATTTGGTTGTTGCGAACAGACTTTGTTTTGGAC
TATCCCAAACCCGTGATGCCCAATATGATCTTCATTGGTGGTATCAACTGCCATCAGGGA
AAGCCATTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATCG
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAAGATTTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACAGTGGCC
TTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 96 GenBank Gene ID AY435143 Link Image
Enzyme 96 GeneCard ID UGT1A8 Link Image
Enzyme 96 GenAtlas ID UGT1A8 Link Image
Enzyme 96 HGNC ID HGNC:12540 Link Image
Enzyme 96 Chromosome Location 2
Enzyme 96 Locus 2q37
Enzyme 96 SNPs SNPJam Report Link Image
Enzyme 96 General References
  1. Zhang T, Haws P, Wu Q: Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation. Genome Res. 2004 Jan;14(1):79-89. Epub 2003 Dec 12. [PubMed Link Image]
Enzyme 96 Metabolite References Not Available
Enzyme 97 [top]
Enzyme 97 ID 15058
Enzyme 97 Name UDP glycosyltransferase 1 family polypeptide A7
Enzyme 97 Synonyms Not Available
Enzyme 97 Gene Name UGT1A7
Enzyme 97 Protein Sequence >UDP glycosyltransferase 1 family polypeptide A7
MARAGWTGLLPLYVCLLLTCGFAKAGKLLVVPMDGSHWFTMQSVVEKLILRGHEVVVVMP
EVSWQLGRSLNCTVKTYSTSYTLEDQDREFMVFADARWTAPLRSAFSLLTSSSNGIFDLF
FSNCRSLFNDRKLVEYLKESCFDAVFLDPFDACGLIVAKYFSLPSVVFARGIFCHYLEEG
AQCPAPLSYVPRLLLGFSDAMTFKERVWNHIMHLEEHLFCPYFFKNVLEIASEILQTPVT
AYDLYSHTSIWLLRTDFVLEYPKPVMPNMIFIGGINCHQGKPVPMEFEAYINASGEHGIV
VFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGH
PMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDL
ENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTW
YQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Enzyme 97 Number of Residues 530
Enzyme 97 Molecular Weight 59818.3
Enzyme 97 Theoretical pI 7.85
Enzyme 97 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolic process
Component
Enzyme 97 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 97 Specific Function Not Available
Enzyme 97 Pathways Not Available
Enzyme 97 Reactions Not Available
Enzyme 97 Pfam Domain Function
Enzyme 97 Signals
  • None
Enzyme 97 Transmembrane Regions
  • None
Enzyme 97 Essentiality Not Available
Enzyme 97 GenBank ID Protein 40849862 Link Image
Enzyme 97 UniProtKB/Swiss-Prot ID Q5DSZ7 Link Image
Enzyme 97 UniProtKB/Swiss-Prot Entry Name Q5DSZ7_HUMAN Link Image
Enzyme 97 PDB ID Not Available
Enzyme 97 Cellular Location Not Available
Enzyme 97 Gene Sequence >1593 bp
ATGGCTCGTGCAGGGTGGACTGGCCTCCTTCCCCTATATGTGTGTCTACTGCTGACCTGT
GGCTTTGCCAAGGCAGGGAAGCTGCTGGTAGTGCCCATGGATGGGAGCCACTGGTTCACC
ATGCAGTCGGTGGTGGAGAAACTCATCCTCAGGGGGCATGAGGTGGTCGTAGTCATGCCA
GAGGTGAGTTGGCAACTGGGAAGATCACTGAATTGCACAGTGAAGACTTACTCAACCTCA
TACACTCTGGAGGATCAGGACCGGGAGTTCATGGTTTTTGCCGATGCTCGCTGGACGGCA
CCATTGCGAAGTGCATTTTCTCTATTAACAAGTTCATCCAATGGTATTTTTGACTTATTT
TTTTCAAATTGCAGGAGTTTGTTTAATGACCGAAAATTAGTAGAATACTTAAAGGAGAGT
TGTTTTGATGCAGTGTTTCTCGATCCTTTTGATGCCTGTGGCTTAATTGTTGCCAAATAT
TTCTCCCTCCCCTCTGTGGTCTTCGCCAGGGGAATATTTTGCCACTATCTTGAAGAAGGT
GCACAGTGCCCTGCTCCTCTTTCCTATGTCCCCAGACTTCTCTTAGGGTTCTCAGACGCC
ATGACTTTCAAGGAGAGAGTATGGAACCACATCATGCACTTGGAGGAACATTTATTTTGC
CCCTATTTTTTCAAAAATGTCTTAGAAATAGCCTCTGAAATTCTCCAAACCCCTGTCACG
GCATATGATCTCTACAGCCACACATCAATTTGGTTGTTGCGAACTGACTTTGTTTTGGAG
TATCCCAAACCCGTGATGCCCAATATGATCTTCATTGGTGGTATCAACTGTCATCAGGGA
AAGCCAGTGCCTATGGAATTTGAAGCCTACATTAATGCTTCTGGAGAACATGGAATTGTG
GTTTTCTCTTTGGGATCAATGGTCTCAGAAATTCCAGAGAAGAAAGCTATGGCAATTGCT
GATGCTTTGGGCAAAATCCCTCAGACAGTCCTGTGGCGGTACACTGGAACCCGACCATCG
AATCTTGCGAACAACACGATACTTGTTAAGTGGCTACCCCAAAACGATCTGCTTGGTCAC
CCGATGACCCGTGCCTTTATCACCCATGCTGGTTCCCATGGTGTTTATGAAAGCATATGC
AATGGCGTTCCCATGGTGATGATGCCCTTGTTTGGTGATCAGATGGACAATGCAAAGCGC
ATGGAGACTAAGGGAGCTGGAGTGACCCTGAATGTTCTGGAAATGACTTCTGAAGATTTA
GAAAATGCTCTAAAAGCAGTCATCAATGACAAAAGTTACAAGGAGAACATCATGCGCCTC
TCCAGCCTTCACAAGGACCGCCCGGTGGAGCCGCTGGACCTGGCCGTGTTCTGGGTGGAG
TTTGTGATGAGGCACAAGGGCGCGCCACACCTGCGCCCCGCAGCCCACGACCTCACCTGG
TACCAGTACCATTCCTTGGACGTGATTGGTTTCCTCTTGGCCGTCGTGCTGACAGTGGCC
TTCATCACCTTTAAATGTTGTGCTTATGGCTACCGGAAATGCTTGGGGAAAAAAGGGCGA
GTTAAGAAAGCCCACAAATCCAAGACCCATTGA
Enzyme 97 GenBank Gene ID AY435142 Link Image
Enzyme 97 GeneCard ID UGT1A7 Link Image
Enzyme 97 GenAtlas ID UGT1A7 Link Image
Enzyme 97 HGNC ID HGNC:12539 Link Image
Enzyme 97 Chromosome Location 2
Enzyme 97 Locus 2q37
Enzyme 97 SNPs SNPJam Report Link Image
Enzyme 97 General References
  1. Zhang T, Haws P, Wu Q: Multiple variable first exons: a mechanism for cell- and tissue-specific gene regulation. Genome Res. 2004 Jan;14(1):79-89. Epub 2003 Dec 12. [PubMed Link Image]
Enzyme 97 Metabolite References Not Available
Enzyme 98 [top]
Enzyme 98 ID 15059
Enzyme 98 Name cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b)
Enzyme 98 Synonyms Not Available
Enzyme 98 Gene Name UGT2B10
Enzyme 98 Protein Sequence >cDNA FLJ76966, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B10 (UGT2B10), mRNA (UDP glucuronosyltransferase 2 family, polypeptide B10, isoform CRA_b)
MALKWTTVLLIQLSFYFSSGSCGKVLVWAAEYSLWMNMKTILKELVQRGHEVTVLASSAS
ILFDPNDSSTLKLEVYPTSLTKTEFENIIMQLVKRLSEIQKDTFWLPFSQEQEILWAIND
IIRNFCKDVVSNKKLMKKLQESRFDIVFADAYLPCGELLAELFNIPFVYSHSFSPGYSFE
RHSGGFIFPPSYVPVVMSKLSDQMTFMERVKNMLYVLYFDFWFQIFNMKKWDQFYSEVLG
RPTTLSETMRKADIWLMRNSWNFKFPHPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGE
NGVVVFSLGSMVSNMTEERANVIATALAKIPQKVLWRFDGNKPDALGLNTRLYKWIPQND
LLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFFDQPDNIAHMKAKGAAVRVDFNTMS
STDLLNALKTVINDPSYKENIMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAH
NLTWFQYHSLDVIGFLLACVATVLFIITKCCLFCFWKFARKGKKGKRD
Enzyme 98 Number of Residues 528
Enzyme 98 Molecular Weight 60775
Enzyme 98 Theoretical pI 9.40
Enzyme 98 GO Classification Not Available
Enzyme 98 General Function Carbohydrate transport and metabolism
Enzyme 98 Specific Function Not Available
Enzyme 98 Pathways Not Available
Enzyme 98 Reactions Not Available
Enzyme 98 Pfam Domain Function Not Available
Enzyme 98 Signals
  • None
Enzyme 98 Transmembrane Regions
  • None
Enzyme 98 Essentiality Not Available
Enzyme 98 GenBank ID Protein 158258913 Link Image
Enzyme 98 UniProtKB/Swiss-Prot ID A8K9M3 Link Image
Enzyme 98 UniProtKB/Swiss-Prot Entry Name A8K9M3_HUMAN Link Image
Enzyme 98 PDB ID Not Available
Enzyme 98 Cellular Location Not Available
Enzyme 98 Gene Sequence >1587 bp
ATGGCTCTGAAATGGACTACAGTTCTGCTGATACAACTCAGTTTTTACTTTAGCTCTGGG
AGTTGTGGAAAGGTGCTGGTATGGGCCGCAGAATACAGCCTTTGGATGAATATGAAGACA
ATCCTGAAAGAACTTGTTCAGAGAGGTCATGAGGTGACTGTACTGGCATCTTCAGCTTCC
ATTCTTTTTGATCCCAACGACTCATCCACTCTTAAACTTGAAGTTTATCCTACATCTTTA
ACTAAAACTGAATTTGAGAATATCATCATGCAATTGGTTAAGAGATTGTCAGAAATTCAA
AAAGATACATTTTGGTTACCTTTTTCACAAGAACAAGAAATCCTGTGGGCAATTAATGAC
ATAATTAGAAACTTCTGTAAAGATGTAGTTTCAAATAAGAAACTTATGAAAAAACTACAA
GAGTCAAGATTTGACATCGTTTTTGCAGATGCTTATTTACCCTGTGGTGAGCTGCTGGCT
GAGCTATTTAACATACCCTTTGTGTACAGTCACAGCTTCAGTCCTGGCTACTCATTTGAA
AGGCACAGTGGAGGATTTATTTTCCCTCCTTCCTACGTACCTGTTGTTATGTCAAAATTA
AGTGATCAAATGACTTTCATGGAGAGGGTAAAAAATATGCTCTATGTGCTTTATTTTGAC
TTTTGGTTCCAAATATTTAATATGAAGAAGTGGGATCAGTTTTACAGTGAAGTTTTAGGA
AGACCCACTACATTATCTGAGACAATGAGGAAAGCTGACATATGGCTTATGCGAAACTCC
TGGAATTTTAAATTTCCTCATCCATTCTTACCAAATGTTGATTTTGTTGGAGGACTCCAC
TGCAAACCTGCCAAACCCCTACCTAAGGAAATGGAGGAGTTTGTACAGAGCTCTGGAGAA
AATGGTGTTGTGGTGTTTTCTCTGGGGTCAATGGTCAGTAACATGACAGAAGAAAGGGCC
AACGTAATTGCAACAGCCCTTGCCAAGATCCCACAAAAGGTTCTTTGGAGATTTGATGGG
AATAAACCAGATGCCTTAGGTCTCAATACTCGACTGTACAAGTGGATACCCCAGAATGAC
CTTCTAGGTCATCCAAAAACCAGAGCTTTTATAACTCATGGTGGAGCCAATGGCATCTAT
GAGGCAATCTACCATGGGATCCCTATGGTGGGCATTCCATTGTTTTTTGATCAACCTGAT
AATATTGCTCACATGAAGGCCAAGGGAGCAGCTGTTAGAGTGGACTTCAACACAATGTCG
AGTACAGACCTGCTGAATGCACTGAAGACAGTAATTAATGATCCTTCATATAAAGAGAAT
ATTATGAAATTATCAAGAATTCAACATGATCAACCAGTGAAGCCCCTGGATCGAGCAGTC
TTCTGGATTGAATTTGTCATGCGCCACAAAGGAGCCAAACATCTTCGAGTTGCAGCCCAC
AACCTCACCTGGTTCCAGTACCACTCTTTGGATGTGATTGGGTTCCTGCTGGCTTGTGTG
GCAACCGTGCTATTTATCATCACAAAGTGTTGTCTGTTTTGTTTCTGGAAGTTTGCTAGA
AAAGGAAAGAAGGGAAAAAGGGATTAG
Enzyme 98 GenBank Gene ID AK292738 Link Image
Enzyme 98 GeneCard ID A8K9M3 Link Image
Enzyme 98 GenAtlas ID Not Available
Enzyme 98 HGNC ID Not Available
Enzyme 98 Chromosome Location Not Available
Enzyme 98 Locus Not Available
Enzyme 98 SNPs SNPJam Report Link Image
Enzyme 98 General References Not Available
Enzyme 98 Metabolite References Not Available
Enzyme 99 [top]
Enzyme 99 ID 15191
Enzyme 99 Name 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)
Enzyme 99 Synonyms Not Available
Enzyme 99 Gene Name NME7
Enzyme 99 Protein Sequence >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)
MNHSERFVFIAEWYDPNASLLRRYELLFYPGDGSVEMHDVKNHRTFLKRTKYDNLHLEDL
FIGNKVNVFSRQLVLIDYGDQYTARQLGSRKEKTLALIKPDAISKAGEIIEIINKAGFTI
TKLKMMMLSRKEALDFHVDHQSRPFFNELIQFITTGPIIAMEILRDDAICEWKRLLGPAN
SGVARTDASESIRALFGTDGIRNAAHGPDSFASAAREMELFFPSSGGCGPANTAKFTNCT
CCIVKPHAVSEGLLGKILMAIRDAGFEISAMQMFNMDRVNVEEFYEVYKGVVTEYHDMVT
EMYSGPCVAMEIQQNNATKTFREFCGPADPEIARHLRPGTLRAIFGKTKIQNAVHCTDLP
EDGLLEVQYFFKILDN
Enzyme 99 Number of Residues 376
Enzyme 99 Molecular Weight 42492
Enzyme 99 Theoretical pI 6.44
Enzyme 99 GO Classification Not Available
Enzyme 99 General Function Nucleotide transport and metabolism
Enzyme 99 Specific Function Not Available
Enzyme 99 Pathways Not Available
Enzyme 99 Reactions Not Available
Enzyme 99 Pfam Domain Function Not Available
Enzyme 99 Signals
  • None
Enzyme 99 Transmembrane Regions
  • None
Enzyme 99 Essentiality Not Available
Enzyme 99 GenBank ID Protein 158254838 Link Image
Enzyme 99 UniProtKB/Swiss-Prot ID A8K3T6 Link Image
Enzyme 99 UniProtKB/Swiss-Prot Entry Name A8K3T6_HUMAN Link Image
Enzyme 99 PDB ID Not Available
Enzyme 99 Cellular Location Not Available
Enzyme 99 Gene Sequence >1131 bp
ATGAATCATAGTGAAAGATTTGTTTTCATTGCAGAGTGGTATGATCCAAATGCTTCACTT
CTTCGACGTTATGAGCTTTTATTTTACCCAGGGGATGGATCTGTTGAAATGCATGATGTA
AAGAATCATCGCACCTTTTTAAAGCGGACCAAATATGATAACCTGCACTTGGAAGATTTA
TTTATAGGCAACAAAGTGAATGTCTTTTCTCGACAACTGGTATTAATTGACTATGGGGAT
CAATATACAGCTCGCCAGCTGGGCAGTAGGAAAGAAAAAACGCTAGCCCTAATTAAACCA
GATGCAATATCAAAGGCTGGAGAAATAATTGAAATAATAAACAAAGCTGGATTTACTATA
ACCAAACTCAAAATGATGATGCTTTCAAGGAAAGAAGCATTGGATTTTCATGTAGATCAC
CAGTCAAGACCCTTTTTCAATGAGCTGATCCAGTTTATTACAACTGGTCCTATTATTGCC
ATGGAGATTTTAAGAGATGATGCTATATGTGAATGGAAAAGACTGCTGGGACCTGCAAAC
TCTGGAGTGGCACGCACAGATGCTTCTGAAAGCATTAGAGCCCTCTTTGGAACAGATGGC
ATAAGAAATGCAGCGCATGGCCCTGATTCTTTTGCTTCTGCGGCCAGAGAAATGGAGTTG
TTTTTTCCTTCAAGTGGAGGTTGTGGGCCGGCAAACACTGCTAAATTTACTAATTGTACC
TGTTGCATTGTTAAACCCCATGCTGTCAGTGAAGGACTGTTGGGAAAGATCCTGATGGCT
ATCCGAGATGCAGGTTTTGAAATCTCAGCTATGCAGATGTTCAATATGGATCGGGTTAAT
GTTGAGGAATTCTATGAAGTTTATAAAGGAGTAGTGACCGAATATCATGACATGGTGACA
GAAATGTATTCTGGCCCTTGTGTAGCAATGGAGATTCAACAGAATAATGCTACAAAGACA
TTTCGAGAATTTTGTGGACCTGCTGATCCTGAAATTGCCCGGCATTTACGCCCTGGAACT
CTCAGAGCAATCTTTGGTAAAACTAAGATCCAGAATGCTGTTCACTGTACTGATCTGCCA
GAGGATGGCCTATTAGAGGTTCAATACTTCTTCAAGATCTTGGATAATTAG
Enzyme 99 GenBank Gene ID AK290701 Link Image
Enzyme 99 GeneCard ID A8K3T6 Link Image
Enzyme 99 GenAtlas ID Not Available
Enzyme 99 HGNC ID Not Available
Enzyme 99 Chromosome Location Not Available
Enzyme 99 Locus Not Available
Enzyme 99 SNPs SNPJam Report Link Image
Enzyme 99 General References Not Available
Enzyme 99 Metabolite References Not Available
Enzyme 100 [top]
Enzyme 100 ID 15200
Enzyme 100 Name Uridine kinase
Enzyme 100 Synonyms Not Available
Enzyme 100 Gene Name UCK1
Enzyme 100 Protein Sequence >Uridine kinase
MASAGGEDCESPAPEADRPHQRPFLIGVSGGTASGKSTVCEKIMELLGQNEVEQRQRKVV
ILSQDRFYKVLTAEQKAKALKGQYNFDHPDAFDNDLMHRTLKNIVEGKTVEVPTYDFVTH
SRLPETTVVYPADVVLFEGILVFYSQEIRDMFHLRLFVDTDSDVRLSRRDKEVCRCDHPA
RSGQYGCHQPDRAAHPGHSEW
Enzyme 100 Number of Residues 201
Enzyme 100 Molecular Weight 22760.4
Enzyme 100 Theoretical pI 6.23
Enzyme 100 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolic process
Component
Enzyme 100 General Function Involved in ATP binding
Enzyme 100 Specific Function ATP + cytidine = ADP + CMP
Enzyme 100 Pathways Not Available
Enzyme 100 Reactions
  • ATP + uridine = ADP + UMP [RN:R00964]
Enzyme 100 Pfam Domain Function
Enzyme 100 Signals
  • None
Enzyme 100 Transmembrane Regions
  • None
Enzyme 100 Essentiality Not Available
Enzyme 100 GenBank ID Protein 57162374 Link Image
Enzyme 100 UniProtKB/Swiss-Prot ID Q5JT13 Link Image
Enzyme 100 UniProtKB/Swiss-Prot Entry Name Q5JT13_HUMAN Link Image
Enzyme 100 PDB ID Not Available
Enzyme 100 Cellular Location Not Available
Enzyme 100 Gene Sequence >606 bp
ATGGCTTCGGCGGGAGGCGAAGACTGCGAGAGCCCCGCGCCGGAGGCCGACCGTCCGCAC
CAGCGGCCCTTCCTGATAGGGGTGAGCGGCGGCACTGCCAGCGGGAAGTCGACCGTGTGT
GAGAAGATCATGGAGTTGCTGGGACAGAACGAGGTGGAACAGCGGCAGCGGAAGGTGGTC
ATCCTGAGCCAGGACAGGTTCTACAAGGTCCTGACGGCAGAGCAGAAGGCCAAGGCCTTG
AAAGGACAGTACAATTTTGACCATCCAGATGCCTTTGATAATGATTTGATGCACAGGACT
CTGAAGAACATCGTGGAGGGCAAAACGGTGGAGGTGCCGACCTATGATTTTGTGACACAC
TCAAGGTTACCAGAGACCACGGTGGTCTACCCTGCGGACGTGGTTCTGTTTGAGGGCATC
TTGGTGTTCTACAGCCAGGAGATCCGGGACATGTTCCACCTGCGCCTCTTCGTGGACACC
GACTCCGACGTCAGGCTGTCTCGAAGAGACAAAGAAGTATGCCGATGTGATCATCCCGCG
AGGAGTGGACAATATGGTTGCCATCAACCTGATCGTGCAGCACATCCAGGACATTCTGAA
TGGTGA
Enzyme 100 GenBank Gene ID AL358781 Link Image
Enzyme 100 GeneCard ID UCK1 Link Image
Enzyme 100 GenAtlas ID UCK1 Link Image
Enzyme 100 HGNC ID HGNC:14859 Link Image
Enzyme 100 Chromosome Location 9
Enzyme 100 Locus 9q34.13
Enzyme 100 SNPs SNPJam Report Link Image
Enzyme 100 General References Not Available
Enzyme 100 Metabolite References Not Available
Enzyme 101 [top]
Enzyme 101 ID 15232
Enzyme 101 Name Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
Enzyme 101 Synonyms Not Available
Enzyme 101 Gene Name DKFZp761J1915
Enzyme 101 Protein Sequence >Putative uncharacterized protein DKFZp761J1915 (Ectonucleoside triphosphate diphosphohydrolase 6 (Putative function), isoform CRA_a)
MQPQHGPWQTRMRKISNHGSLRVAKVAYPLGLCVGVFIYVAYIKWHRATATQAFFSITRA
APGARWGQQAHSPLGTAADGHEVFYGIMFDAGSTGTRVHVFQFTRPPRETPTLTHETFKA
LKPGLSAYADDVEKSAQGIRELLDVAKQDIPFDFWKATPLVLKATAGLRLLPGEKAQKLL
QKVKEVFKASPFLVGDDCVSIMNGTDEGVSAWITINFLTGSLKTPGGSSVGMLDLGGGST
QIAFLPRVEGTLQASPPGYLTALRMFNRTYKLYSYSYLGLGLMSARLAILGGVEGQPAKD
GKELVSPCLSPSFKGEWEHAEVTYRVSGQKAAASLHELCAARVSEVLQNRVHRTEEVKHV
DFYAFSYYYDLAAGVGLIDAEKGGSLVVGDFEIAAKYVCRTLETQPQSSPFSCMDLTYVS
LLLQEFGFPRSKVLKLTRKIDNVETSWALGAIFHYIDSLNRQKSPAS
Enzyme 101 Number of Residues 467
Enzyme 101 Molecular Weight 51160
Enzyme 101 Theoretical pI 9.14
Enzyme 101 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 101 General Function Not Available
Enzyme 101 Specific Function Not Available
Enzyme 101 Pathways Not Available
Enzyme 101 Reactions Not Available
Enzyme 101 Pfam Domain Function
Enzyme 101 Signals
  • None
Enzyme 101 Transmembrane Regions
  • None
Enzyme 101 Essentiality Not Available
Enzyme 101 GenBank ID Protein 50949564 Link Image
Enzyme 101 UniProtKB/Swiss-Prot ID Q8N3H3 Link Image
Enzyme 101 UniProtKB/Swiss-Prot Entry Name Q8N3H3_HUMAN Link Image
Enzyme 101 PDB ID Not Available
Enzyme 101 Cellular Location Not Available
Enzyme 101 Gene Sequence >1404 bp
ATGCAGCCGCAGCACGGTCCTTGGCAAACAAGGATGAGAAAAATATCCAACCACGGGAGC
CTGCGGGTGGCGAAGGTGGCATACCCCCTGGGGCTGTGTGTGGGCGTGTTCATCTATGTT
GCCTACATCAAGTGGCACCGGGCCACCGCCACCCAGGCCTTCTTCAGCATCACCAGGGCA
GCCCCGGGGGCCCGGTGGGGTCAGCAGGCCCACAGCCCCCTGGGGACAGCTGCAGACGGG
CACGAGGTCTTCTACGGGATCATGTTTGATGCAGGAAGCACTGGCACCCGAGTACACGTC
TTCCAGTTCACCCGGCCCCCCAGAGAAACTCCCACGTTAACCCACGAAACCTTCAAAGCA
CTGAAGCCAGGTCTTTCTGCCTATGCTGATGATGTTGAAAAGAGCGCTCAGGGAATCCGG
GAACTACTGGATGTTGCTAAACAGGACATTCCGTTCGACTTCTGGAAGGCCACCCCTCTG
GTCCTCAAGGCCACAGCTGGCTTACGCCTGTTACCTGGAGAAAAGGCCCAGAAGTTACTG
CAGAAGGTGAAAGAAGTATTTAAAGCATCGCCTTTCCTTGTAGGGGATGACTGTGTTTCC
ATCATGAACGGAACAGATGAAGGCGTTTCGGCGTGGATCACCATCAACTTCCTGACAGGC
AGCTTGAAAACTCCAGGAGGGAGCAGCGTGGGCATGCTGGACTTGGGCGGAGGATCCACT
CAGATCGCCTTCCTGCCACGCGTGGAGGGCACCCTGCAGGCCTCCCCACCCGGCTACCTG
ACGGCACTGCGGATGTTTAACAGGACCTACAAGCTCTATTCCTACAGCTACCTCGGGCTC
GGGCTGATGTCGGCACGCCTGGCGATCCTGGGCGGCGTGGAGGGGCAGCCTGCTAAGGAT
GGAAAGGAGTTGGTCAGCCCTTGCTTGTCTCCCAGTTTCAAAGGAGAGTGGGAACACGCA
GAAGTCACGTACAGGGTTTCAGGGCAGAAAGCAGCGGCAAGCCTGCACGAGCTGTGTGCT
GCCAGAGTGTCAGAGGTCCTTCAAAACAGAGTGCACAGGACGGAGGAAGTGAAGCATGTG
GACTTCTATGCTTTCTCCTACTATTACGACCTTGCAGCTGGTGTGGGCCTCATAGATGCG
GAGAAGGGAGGCAGCCTGGTGGTGGGGGACTTCGAGATCGCAGCCAAGTACGTGTGTCGG
ACCCTGGAGACACAGCCGCAGAGCAGCCCCTTCTCATGCATGGACCTCACCTACGTCAGC
CTGCTACTCCAGGAGTTCGGCTTTCCCAGGAGCAAAGTGCTGAAGCTCACTCGGAAAATT
GACAATGTTGAGACCAGCTGGGCTCTGGGGGCCATTTTTCATTACATCGACTCCCTGAAC
AGACAGAAGAGTCCAGCCTCATAG
Enzyme 101 GenBank Gene ID AL834158 Link Image
Enzyme 101 GeneCard ID Q8N3H3 Link Image
Enzyme 101 GenAtlas ID DKFZp761J1915 Link Image
Enzyme 101 HGNC ID HGNC:3368 Link Image
Enzyme 101 Chromosome Location Not Available
Enzyme 101 Locus Not Available
Enzyme 101 SNPs SNPJam Report Link Image
Enzyme 101 General References Not Available
Enzyme 101 Metabolite References Not Available
Enzyme 102 [top]
Enzyme 102 ID 15233
Enzyme 102 Name Ectonucleoside triphosphate diphosphohydrolase 5
Enzyme 102 Synonyms
  1. SubName: Ectonucleoside triphosphate diphosphohydrolase 5, isoform CRA_d
Enzyme 102 Gene Name ENTPD5
Enzyme 102 Protein Sequence >Ectonucleoside triphosphate diphosphohydrolase 5
MATSWGTVFFMLVVSCVCSAVSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGT
RIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHW
KKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTV
NFLTGQLHGHRQETVGTLDLGGASTQITFLPQFEKTLEQTPRGYLTSFEMFNSTYKLYTH
SYLGFGLKAARLATLGALETEGTDGHTFRSACLPRWLEAEWIFGGVKYQYGGNQEGEVGF
EPCYAEVLRVVRGKLHQPEEVQRGSFYAFSYYYDRAVDTDMIDYEKGGILKVEDFERKAR
EVCDNLENFTSGSPFLCMDLSYITALLKDGFGFADSTVLQLTKKVNNIETGWALGATFHL
LQSLGISH
Enzyme 102 Number of Residues 428
Enzyme 102 Molecular Weight 47517.0
Enzyme 102 Theoretical pI 6.29
Enzyme 102 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 102 General Function Involved in hydrolase activity
Enzyme 102 Specific Function Not Available
Enzyme 102 Pathways Not Available
Enzyme 102 Reactions Not Available
Enzyme 102 Pfam Domain Function
Enzyme 102 Signals
  • None
Enzyme 102 Transmembrane Regions
  • None
Enzyme 102 Essentiality Not Available
Enzyme 102 GenBank ID Protein 120660392 Link Image
Enzyme 102 UniProtKB/Swiss-Prot ID A1L4C5 Link Image
Enzyme 102 UniProtKB/Swiss-Prot Entry Name A1L4C5_HUMAN Link Image
Enzyme 102 PDB ID Not Available
Enzyme 102 Cellular Location Not Available
Enzyme 102 Gene Sequence >1287 bp
ATGGCCACTTCTTGGGGCACAGTCTTTTTCATGCTGGTGGTATCCTGTGTTTGCAGCGCT
GTCTCCCACAGGAACCAGCAGACTTGGTTTGAGGGTATCTTCCTGTCTTCCATGTGCCCC
ATCAATGTCAGCGCCAGCACCTTGTATGGAATTATGTTTGATGCAGGGAGCACTGGAACT
CGAATTCATGTTTACACCTTTGTGCAGAAAATGCCAGGACAGCTTCCAATTCTAGAAGGG
GAAGTTTTTGATTCTGTGAAGCCAGGACTTTCTGCTTTTGTAGATCAACCTAAGCAGGGT
GCTGAGACCGTTCAAGGGCTCTTAGAGGTGGCCAAAGACTCAATCCCCCGAAGTCACTGG
AAAAAGACCCCAGTGGTCCTAAAGGCAACAGCAGGACTACGCTTACTGCCAGAACACAAA
GCCAAGGCTCTGCTCTTTGAGGTAAAGGAGATCTTCAGGAAGTCACCTTTCCTGGTACCA
AAGGGCAGTGTTAGCATCATGGATGGATCCGACGAAGGCATATTAGCTTGGGTTACTGTG
AATTTTCTGACAGGTCAGCTGCATGGCCACAGACAGGAGACTGTGGGGACCTTGGACCTA
GGGGGAGCCTCCACCCAAATCACGTTCCTGCCCCAGTTTGAGAAAACTCTGGAACAAACT
CCTAGGGGCTACCTCACTTCCTTTGAGATGTTTAACAGCACTTATAAGCTCTATACACAT
AGTTACCTGGGATTTGGATTGAAAGCTGCAAGACTAGCAACCCTGGGAGCCCTGGAGACA
GAAGGGACTGATGGGCACACTTTCCGGAGTGCCTGTTTACCGAGATGGTTGGAAGCAGAG
TGGATCTTTGGGGGTGTGAAATACCAGTATGGTGGCAACCAAGAAGGGGAGGTGGGCTTT
GAGCCCTGCTATGCCGAAGTGCTGAGGGTGGTACGAGGAAAACTTCACCAGCCAGAGGAG
GTCCAGAGAGGTTCCTTCTATGCTTTCTCTTACTATTATGACCGAGCTGTTGACACAGAC
ATGATTGATTATGAAAAGGGGGGTATTTTAAAAGTTGAAGATTTTGAAAGAAAAGCCAGG
GAAGTGTGTGATAACTTGGAAAACTTCACCTCAGGCAGTCCTTTCCTGTGCATGGATCTC
AGCTACATCACAGCCCTGTTAAAGGATGGCTTTGGCTTTGCAGACAGCACAGTCTTACAG
CTCACAAAGAAAGTGAACAACATAGAGACGGGCTGGGCCTTGGGGGCCACCTTTCACCTG
TTGCAGTCTCTGGGCATCTCCCATTGA
Enzyme 102 GenBank Gene ID BC130485 Link Image
Enzyme 102 GeneCard ID ENTPD5 Link Image
Enzyme 102 GenAtlas ID ENTPD5 Link Image
Enzyme 102 HGNC ID HGNC:3367 Link Image
Enzyme 102 Chromosome Location 1
Enzyme 102 Locus 14q24
Enzyme 102 SNPs SNPJam Report Link Image
Enzyme 102 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 102 Metabolite References Not Available
Enzyme 103 [top]
Enzyme 103 ID 15261
Enzyme 103 Name cDNA FLJ75238, highly similar to Homo sapiens asparagine-linked glycosylation 14 homolog (yeast) (ALG14), mRNA (Asparagine-linked glycosylation 14 homolog (Yeast), isoform CRA_b)
Enzyme 103 Synonyms Not Available
Enzyme 103 Gene Name ALG14
Enzyme 103 Protein Sequence >cDNA FLJ75238, highly similar to Homo sapiens asparagine-linked glycosylation 14 homolog (yeast) (ALG14), mRNA (Asparagine-linked glycosylation 14 homolog (Yeast), isoform CRA_b)
MVCVLVLAAAAGAVAVFLILRIWVVLRSMDVTPRESLSILVVAGSGGHTTEILRLLGSLS
NAYSPRHYVIADTDEMSANKINSFELDRADRDPSNMYTKYYIHRIPRSREVQQSWPSTVF
TTLHSMWLSFPLIHRVKPDLVLCNGPGTCVPICVSALLLGILGIKKVIIVYVESICRVET
LSMSGKILFHLSDYFIVQWPALKEKYPKSVYLGRIV
Enzyme 103 Number of Residues 216
Enzyme 103 Molecular Weight 24151
Enzyme 103 Theoretical pI 9.16
Enzyme 103 GO Classification Not Available
Enzyme 103 General Function Not Available
Enzyme 103 Specific Function Not Available
Enzyme 103 Pathways Not Available
Enzyme 103 Reactions Not Available
Enzyme 103 Pfam Domain Function Not Available
Enzyme 103 Signals
  • None
Enzyme 103 Transmembrane Regions
  • None
Enzyme 103 Essentiality Not Available
Enzyme 103 GenBank ID Protein 158259813 Link Image
Enzyme 103 UniProtKB/Swiss-Prot ID A8K030 Link Image
Enzyme 103 UniProtKB/Swiss-Prot Entry Name A8K030_HUMAN Link Image
Enzyme 103 PDB ID Not Available
Enzyme 103 Cellular Location Not Available
Enzyme 103 Gene Sequence >651 bp
ATGGTGTGCGTTCTCGTTCTAGCTGCGGCCGCAGGAGCTGTGGCGGTTTTCCTAATCCTG
CGAATATGGGTAGTGCTTCGTTCCATGGACGTTACGCCCCGGGAGTCTCTCAGTATCTTG
GTAGTGGCTGGGTCCGGTGGGCATACCACTGAGATCCTGAGGCTGCTTGGGAGCTTGTCC
AATGCCTACTCACCTAGACATTATGTCATTGCTGACACTGATGAAATGAGTGCCAATAAA
ATAAATTCTTTTGAACTAGATCGAGCTGATAGAGACCCTAGTAACATGTATACCAAATAC
TACATTCACCGAATTCCAAGAAGCCGGGAGGTTCAGCAGTCCTGGCCCTCCACCGTTTTC
ACCACCTTGCACTCCATGTGGCTCTCCTTTCCCCTAATTCACAGGGTGAAGCCAGATTTG
GTGTTGTGTAACGGACCAGGAACATGTGTTCCTATCTGTGTATCTGCCCTTCTCCTTGGG
ATACTAGGAATAAAGAAAGTGATCATTGTCTACGTTGAAAGCATCTGCCGTGTAGAAACG
TTATCCATGTCCGGAAAGATTCTGTTTCATCTCTCAGATTACTTCATTGTTCAGTGGCCG
GCTCTGAAAGAAAAGTATCCCAAATCGGTGTACCTTGGGCGAATTGTTTGA
Enzyme 103 GenBank Gene ID AK289395 Link Image
Enzyme 103 GeneCard ID A8K030 Link Image
Enzyme 103 GenAtlas ID Not Available
Enzyme 103 HGNC ID Not Available
Enzyme 103 Chromosome Location Not Available
Enzyme 103 Locus Not Available
Enzyme 103 SNPs SNPJam Report Link Image
Enzyme 103 General References Not Available
Enzyme 103 Metabolite References Not Available
Enzyme 104 [top]
Enzyme 104 ID 15262
Enzyme 104 Name HCG2018639
Enzyme 104 Synonyms
  1. SubName: cDNA FLJ78031, highly similar to Homo sapiens beta3GnT6 beta-1,3-N- acetylglucosaminyltransferase 6
  2. SubName: cDNA, FLJ94270, Homo sapiens beta-1,3-N-acetylglucosaminyltransferase protein(IMAGE:4907098), mRNA
Enzyme 104 Gene Name Not Available
Enzyme 104 Protein Sequence >HCG2018639
MAFPCRRSLTAKTLACLLVGVSFLALQQWFLQAPRSPREERSPQEETPEGPTDAPAADEP
PSELVPGPPCVANASANATADFEQLPARIQDFLRYRHCRHFPLLWDAPAKCAGGRGVFLL
LAVKSAPEHYERRELIRRTWGQERSYGGRPVRRLFLLGTPGPEDEARAERLAELVALEAR
EHGDVLQWAFADTFLNLTLKHLHLLDWLAARCPHARFLLSGDDDVFVHTANVVRFLQAQP
PGRHLFSGQLMEGSVPIRDSWSKYFVPPQLFPGSAYPVYCSGGGFLLSGPTARALRAAAR
HTPLFPIDDAYMGMCLERAGLAPSGHEGIRPFGVQLPGAQQSSFDPCMYRELLLVHRFAP
YEMLLMWKALHSPALSCDRGHRVS
Enzyme 104 Number of Residues 384
Enzyme 104 Molecular Weight 42747.6
Enzyme 104 Theoretical pI 7.76
Enzyme 104 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 104 General Function Involved in galactosyltransferase activity
Enzyme 104 Specific Function Not Available
Enzyme 104 Pathways Not Available
Enzyme 104 Reactions Not Available
Enzyme 104 Pfam Domain Function
Enzyme 104 Signals
  • None
Enzyme 104 Transmembrane Regions
  • None
Enzyme 104 Essentiality Not Available
Enzyme 104 GenBank ID Protein 158259007 Link Image
Enzyme 104 UniProtKB/Swiss-Prot ID A8K9Q8 Link Image
Enzyme 104 UniProtKB/Swiss-Prot Entry Name A8K9Q8_HUMAN Link Image
Enzyme 104 PDB ID Not Available
Enzyme 104 Cellular Location Not Available
Enzyme 104 Gene Sequence >1155 bp
ATGGCTTTTCCCTGCCGCAGGTCCCTGACTGCCAAGACTCTGGCCTGCCTCCTGGTGGGC
GTGAGTTTCTTAGCACTGCAGCAGTGGTTCCTCCAGGCGCCAAGGTCCCCGCGGGAGGAG
AGGTCCCCGCAGGAGGAGACGCCAGAGGGTCCCACCGACGCTCCCGCGGCTGACGAGCCG
CCCTCGGAGCTCGTCCCCGGGCCCCCGTGCGTGGCGAACGCCTCGGCGAACGCCACGGCC
GACTTCGAGCAGCTGCCCGCGCGCATCCAGGACTTCCTGCGGTACCGCCACTGCCGCCAC
TTCCCGCTGCTTTGGGACGCACCGGCCAAGTGCGCCGGCGGCCGAGGCGTGTTCCTGCTC
CTGGCGGTGAAGTCGGCGCCTGAGCACTACGAGCGACGCGAGCTCATCCGGCGCACGTGG
GGGCAAGAGCGCAGCTACGGCGGGCGGCCAGTGCGCCGCCTCTTTCTATTGGGCACCCCG
GGCCCCGAGGACGAGGCGCGCGCGGAGCGGCTGGCGGAGCTGGTGGCGCTGGAGGCGCGC
GAGCACGGCGACGTGCTGCAGTGGGCCTTCGCGGACACCTTCCTCAACCTCACGCTCAAG
CACCTGCACTTGCTCGACTGGCTGGCTGCACGCTGCCCGCACGCGCGCTTTCTGCTCAGC
GGCGACGACGACGTGTTCGTGCACACCGCCAACGTAGTCCGCTTCCTGCAGGCGCAGCCA
CCCGGCCGCCACCTGTTCTCCGGCCAGCTCATGGAGGGCTCCGTGCCCATCCGCGACAGC
TGGAGCAAGTACTTCGTGCCGCCGCAGCTCTTCCCCGGGTCCGCTTACCCGGTGTACTGC
AGCGGCGGCGGCTTCCTCCTGTCCGGCCCCACGGCCCGGGCCCTGCGCGCGGCCGCCCGC
CACACCCCGCTCTTCCCCATCGACGACGCCTACATGGGCATGTGTCTGGAGCGCGCCGGC
CTGGCGCCCAGCGGCCACGAGGGCATCCGGCCCTTCGGCGTGCAGCTGCCTGGCGCACAG
CAGTCCTCCTTCGACCCCTGCATGTACCGCGAGTTGCTGCTAGTGCACCGCTTCGCGCCC
TACGAGATGCTGCTCATGTGGAAGGCGCTGCACAGCCCCGCGCTCAGCTGTGACCGGGGA
CACCGGGTCTCCTGA
Enzyme 104 GenBank Gene ID AK292773 Link Image
Enzyme 104 GeneCard ID Not Available
Enzyme 104 GenAtlas ID hCG_2018639 Link Image
Enzyme 104 HGNC ID HGNC:24141 Link Image
Enzyme 104 Chromosome Location Not Available
Enzyme 104 Locus Not Available
Enzyme 104 SNPs Not Available
Enzyme 104 General References Not Available
Enzyme 104 Metabolite References Not Available
Enzyme 105 [top]
Enzyme 105 ID 15263
Enzyme 105 Name Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase, isoform CRA_a
Enzyme 105 Synonyms
  1. SubName: UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Enzyme 105 Gene Name GNE
Enzyme 105 Protein Sequence >Glucosamine (UDP-N-acetyl)-2-epimerase/N-acetylmannosamine kinase, isoform CRA_a
METYGYLQRESCFQGPHELYFKNLSKRNKQIMEKNGNNRKLRVCVATCNRADYSKLAPIM
FGIKTEPEFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVG
LALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHA
ITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDV
KSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKG
IEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGE
NVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCF
PPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLI
LQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHSTKLIQEWNSVDLRTPLSDTLH
LPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH
LVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQ
AAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALS
SVQDVDVVVSDLVDPALLGAASMVLDYTTRRIY
Enzyme 105 Number of Residues 753
Enzyme 105 Molecular Weight 83065.2
Enzyme 105 Theoretical pI 6.93
Enzyme 105 GO Classification
Function
  • ATP binding
  • UDP-N-acetylglucosamine 2-epimerase activity
  • adenyl nucleotide binding
  • adenyl ribonucleotide binding
  • binding
  • catalytic activity
  • isomerase activity
  • nucleoside binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleoside binding
  • racemase and epimerase activity
  • racemase and epimerase activity, acting on carbohydrates and derivatives
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • N-acetylglucosamine metabolic process
  • UDP-N-acetylglucosamine metabolic process
  • alcohol metabolic process
  • amino sugar metabolic process
  • carbohydrate metabolic process
  • glucosamine metabolic process
  • lipid biosynthetic process
  • lipid metabolic process
  • lipopolysaccharide biosynthetic process
  • metabolic process
  • monosaccharide metabolic process
  • primary metabolic process
  • small molecule metabolic process
Component
Enzyme 105 General Function Involved in ATP binding
Enzyme 105 Specific Function Not Available
Enzyme 105 Pathways Not Available
Enzyme 105 Reactions
  • UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine [RN:R00420]
Enzyme 105 Pfam Domain Function
Enzyme 105 Signals
  • None
Enzyme 105 Transmembrane Regions
  • None
Enzyme 105 Essentiality Not Available
Enzyme 105 GenBank ID Protein 150368575 Link Image
Enzyme 105 UniProtKB/Swiss-Prot ID A6PZH2 Link Image
Enzyme 105 UniProtKB/Swiss-Prot Entry Name A6PZH2_HUMAN Link Image
Enzyme 105 PDB ID Not Available
Enzyme 105 Cellular Location Not Available
Enzyme 105 Gene Sequence >2262 bp
ATGGAAACCTATGGTTATCTGCAGAGGGAGTCATGCTTTCAAGGACCTCATGAACTCTAT
TTTAAGAACCTCTCAAAACGAAACAAGCAAATCATGGAGAAGAATGGAAATAACCGAAAG
CTGCGGGTTTGTGTTGCTACTTGTAACCGTGCAGATTATTCTAAACTTGCCCCGATCATG
TTTGGCATTAAAACCGAACCTGAGTTCTTTGAACTTGATGTTGTGGTACTTGGCTCTCAC
CTGATAGATGACTATGGAAATACATATCGAATGATTGAACAAGATGACTTTGACATTAAC
ACCAGGCTACACACAATTGTGAGGGGAGAAGATGAGGCAGCCATGGTGGAGTCAGTAGGC
CTGGCCCTAGTGAAGCTGCCAGATGTCCTTAATCGCCTGAAGCCTGATATCATGATTGTT
CATGGAGACAGGTTTGATGCCCTGGCTCTGGCCACATCTGCTGCCTTGATGAACATCCGA
ATCCTTCACATTGAAGGTGGGGAAGTCAGTGGGACCATTGATGACTCTATCAGACATGCC
ATAACAAAACTGGCTCATTATCATGTGTGCTGCACCCGCAGTGCAGAGCAGCACCTGATA
TCCATGTGTGAGGACCATGATCGCATCCTTTTGGCAGGCTGCCCTTCCTATGACAAACTT
CTCTCAGCCAAGAACAAAGACTACATGAGCATCATTCGCATGTGGCTAGGTGATGATGTA
AAATCTAAAGATTACATTGTTGCACTACAGCACCCTGTGACCACTGACATTAAGCATTCC
ATAAAAATGTTTGAATTAACATTGGATGCACTTATCTCATTTAACAAGCGGACCCTAGTC
CTGTTTCCAAATATTGACGCAGGGAGCAAAGAGATGGTTCGAGTGATGCGGAAGAAGGGC
ATTGAGCATCATCCCAACTTTCGTGCAGTTAAACACGTCCCATTTGACCAGTTTATACAG
TTGGTTGCCCATGCTGGCTGTATGATTGGGAACAGCAGCTGTGGGGTTCGAGAAGTTGGA
GCTTTTGGAACACCTGTGATCAACCTGGGAACACGTCAGATTGGAAGAGAAACAGGGGAG
AATGTTCTTCATGTCCGGGATGCTGACACCCAAGACAAAATATTGCAAGCACTGCACCTT
CAGTTTGGTAAACAGTACCCTTGTTCAAAGATATATGGGGATGGAAATGCTGTTCCAAGG
ATTTTGAAGTTTCTCAAATCTATCGATCTTCAAGAGCCACTGCAAAAGAAATTCTGCTTT
CCTCCTGTGAAGGAGAATATCTCTCAAGATATTGACCATATTCTTGAAACTCTAAGTGCC
TTGGCCGTTGATCTTGGCGGGACGAACCTCCGAGTTGCAATAGTCAGCATGAAGGGTGAA
ATAGTTAAGAAGTATACTCAGTTCAATCCTAAAACCTATGAAGAGAGGATTAATTTAATC
CTACAGATGTGTGTGGAAGCTGCAGCAGAAGCTGTAAAACTGAACTGCAGAATTTTGGGA
GTAGGCATTTCCACAGGTGGCCGTGTAAATCCTCGGGAAGGAATTGTGCTGCATTCAACC
AAACTGATCCAAGAGTGGAACTCTGTGGACCTTAGGACCCCCCTTTCTGACACTTTGCAT
CTCCCTGTGTGGGTAGACAATGATGGCAACTGTGCTGCCCTGGCGGAAAGGAAATTTGGC
CAAGGAAAGGGACTGGAAAACTTTGTTACACTTATCACAGGCACAGGAATCGGTGGTGGA
ATTATCCATCAGCATGAATTGATCCACGGAAGCTCCTTCTGTGCTGCAGAACTGGGCCAC
CTTGTTGTGTCTCTGGATGGGCCTGATTGTTCCTGTGGAAGCCATGGGTGCATTGAAGCA
TACGCCTCTGGAATGGCCTTGCAGAGGGAGGCAAAAAAGCTCCATGATGAGGACCTGCTC
TTGGTGGAAGGGATGTCAGTGCCAAAAGATGAGGCTGTGGGTGCGCTCCATCTCATCCAA
GCTGCGAAACTTGGCAATGCGAAGGCCCAGAGCATCCTAAGAACAGCTGGAACAGCTTTG
GGTCTTGGGGTTGTGAACATCCTCCATACCATGAATCCCTCCCTTGTGATCCTCTCCGGA
GTCCTGGCCAGTCACTATATCCACATTGTCAAAGACGTCATTCGCCAGCAGGCCTTGTCC
TCCGTGCAGGACGTGGATGTGGTGGTTTCGGATTTGGTTGACCCCGCCCTGCTGGGTGCT
GCCAGCATGGTTCTGGACTACACAACACGCAGGATCTACTAG
Enzyme 105 GenBank Gene ID AM697708 Link Image
Enzyme 105 GeneCard ID GNE Link Image
Enzyme 105 GenAtlas ID GNE Link Image
Enzyme 105 HGNC ID HGNC:23657 Link Image
Enzyme 105 Chromosome Location 9
Enzyme 105 Locus 9p13.3
Enzyme 105 SNPs SNPJam Report Link Image
Enzyme 105 General References
  1. Reinke SO, Hinderlich S: Prediction of three different isoforms of the human UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase. FEBS Lett. 2007 Jul 10;581(17):3327-31. Epub 2007 Jun 21. [PubMed Link Image]
  2. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 105 Metabolite References Not Available
Enzyme 106 [top]
Enzyme 106 ID 15264
Enzyme 106 Name UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 5 (GalNAc-T5)
Enzyme 106 Synonyms
  1. SubName: cDNA FLJ75131, highly similar to Homo sapiens UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 5 (GalNAc-T5) (GALNT5), mRNA
Enzyme 106 Gene Name GALNT5
Enzyme 106 Protein Sequence >UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 5 (GalNAc-T5)
MNRIRKFFRGSGRVLAFIFVASVIWLLFDMAALRLSFSEINTRVIKEDIVRRERIGFRVQ
PDQGKIFYSSIKEMKPPLRGHGKGAWGKENVRKTEESVLKVEVDLDQTQRERKMQNALGR
GKVVPLWHPAHLQTLPVTPNKQKTDGRGTKPEASSHQGTPKQTTAQGAPKTSFIAAKGTQ
VVKISVHMGRVSLKQEPRKSHSPSSDTSKLAAERDLNVTISLSTDRPKQRSQAVANERAH
PASTAVPKSGEAMALNKTKTQSKEVNANKHKANTSLPFPKFTVNSNRLRKQSINETPLGS
LSKDDGARGAHGKKLNFSESHLVIITKEEEQKADPKEVSNSKTKTIFPKVLGKSQSKHIS
RNRSEMSSSSLAPHRVPLSQTNHALTGGLEPAKINITAKAPSTEYNQSHIKALLPEDSGT
HQVLRIDVTLSPRDPKAPGQFGRPVVVPHGKEKEAERRWKEGNFNVYLSDLIPVDRAIED
TRPAGCAEQLVHNNLPTTSVIMCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTK
DYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHVECNVGWLEP
LLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDVIAKNRIK
ETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSR
VGHIFRNDNPYSFPKDRMKTVERNLVRVAEVWLDEYKELFYGHGDHLIDQGLDVGNLTQQ
RELRKKLKCKSFKWYLENVFPDLRAPIVRASGVLINVALGKCISIENTTVILEDCDGSKE
LQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHKSTSVFHPELVNHIVF
ENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYYEA
Enzyme 106 Number of Residues 940
Enzyme 106 Molecular Weight 106265.3
Enzyme 106 Theoretical pI 10.07
Enzyme 106 GO Classification Not Available
Enzyme 106 General Function Involved in sugar binding
Enzyme 106 Specific Function Not Available
Enzyme 106 Pathways Not Available
Enzyme 106 Reactions Not Available
Enzyme 106 Pfam Domain Function
Enzyme 106 Signals
  • None
Enzyme 106 Transmembrane Regions
  • None
Enzyme 106 Essentiality Not Available
Enzyme 106 GenBank ID Protein 158257740 Link Image
Enzyme 106 UniProtKB/Swiss-Prot ID A5PKZ1 Link Image
Enzyme 106 UniProtKB/Swiss-Prot Entry Name A5PKZ1_HUMAN Link Image
Enzyme 106 PDB ID Not Available
Enzyme 106 Cellular Location Not Available
Enzyme 106 Gene Sequence >2823 bp
ATGAACAGGATCCGAAAGTTTTTCCGAGGAAGTGGGCGAGTCTTGGCATTTATCTTTGTA
GCTTCTGTCATCTGGCTCCTCTTTGACATGGCAGCTCTCCGCCTCTCATTCAGTGAGATC
AACACTCGGGTCATCAAGGAAGACATTGTGAGGAGGGAGCGGATAGGATTCAGAGTTCAG
CCAGACCAAGGAAAAATTTTTTACAGCAGCATAAAAGAGATGAAACCTCCCCTAAGGGGA
CATGGGAAAGGGGCATGGGGCAAAGAGAATGTTAGAAAAACTGAGGAGAGTGTGCTCAAG
GTTGAGGTGGACTTGGACCAAACCCAGAGGGAAAGAAAAATGCAGAATGCCCTGGGAAGG
GGCAAGGTTGTGCCGTTGTGGCATCCTGCACATCTGCAGACCCTCCCTGTGACTCCTAAC
AAGCAGAAGACAGACGGGAGAGGCACCAAACCTGAAGCCTCCTCTCACCAGGGGACACCA
AAGCAAACGACAGCTCAGGGGGCTCCAAAGACCTCATTCATAGCAGCAAAAGGAACTCAG
GTAGTCAAAATATCAGTACACATGGGACGTGTCAGTTTAAAACAGGAGCCCCGGAAGAGT
CATAGTCCCAGCAGTGACACATCAAAACTAGCAGCTGAAAGGGACTTGAATGTGACCATC
AGTCTTAGTACTGATAGACCAAAGCAGCGATCACAGGCAGTAGCAAACGAGAGGGCACAC
CCTGCCAGCACAGCAGTGCCGAAGTCTGGGGAAGCCATGGCCTTAAACAAAACTAAGACT
CAGAGCAAAGAAGTCAATGCAAATAAACACAAAGCCAATACGAGTCTTCCTTTTCCTAAG
TTCACTGTCAATTCAAATCGCTTAAGGAAGCAATCTATTAATGAGACACCTTTGGGAAGT
TTGTCAAAGGATGATGGAGCTAGAGGGGCTCATGGGAAGAAACTCAATTTCTCTGAAAGC
CATCTTGTGATTATAACCAAAGAGGAAGAGCAAAAGGCAGACCCCAAAGAGGTCTCTAAT
TCTAAAACCAAAACAATATTTCCTAAAGTATTGGGTAAAAGCCAAAGTAAACACATTTCC
AGGAATAGAAGTGAGATGTCTTCCTCTTCACTTGCTCCACATAGAGTGCCACTGTCCCAA
ACTAACCATGCTTTAACTGGAGGGCTAGAGCCAGCAAAAATCAACATAACTGCCAAAGCC
CCCTCTACAGAATACAACCAGAGTCATATAAAAGCCCTTTTACCTGAAGACAGTGGAACG
CACCAGGTGTTAAGAATTGATGTGACACTTTCTCCAAGGGACCCCAAAGCTCCAGGGCAG
TTTGGGCGTCCTGTAGTTGTCCCCCATGGAAAGGAGAAGGAGGCAGAAAGAAGATGGAAA
GAAGGAAACTTCAATGTCTACCTTAGCGATTTGATCCCAGTGGATAGAGCCATTGAAGAC
ACCAGACCTGCTGGATGTGCAGAGCAGCTAGTTCACAATAACCTCCCAACCACCAGTGTC
ATCATGTGCTTTGTGGATGAAGTGTGGTCCACTCTCCTGAGATCTGTTCACAGTGTCATC
AATCGCTCTCCTCCACACCTCATCAAGGAGATTCTGCTGGTAGATGACTTCAGCACCAAA
GACTATCTAAAAGATAATTTGGATAAATACATGTCCCAGTTTCCAAAAGTTCGGATTCTT
CGCCTCAAAGAGAGACATGGCTTAATAAGGGCCAGGCTGGCAGGAGCACAGAATGCAACA
GGTGATGTGTTGACATTTTTAGATTCTCATGTGGAATGTAACGTTGGTTGGTTGGAACCT
CTTCTGGAAAGAGTTTATTTAAGTAGAAAGAAAGTGGCCTGTCCAGTAATCGAAGTCATC
AATGATAAGGATATGAGTTACATGACAGTGGATAACTTTCAAAGAGGCATCTTTGTGTGG
CCCATGAACTTTGGTTGGAGAACAATTCCTCCAGATGTCATTGCAAAAAACAGAATTAAA
GAAACTGATACAATAAGGTGCCCTGTCATGGCTGGTGGATTGTTTTCTATTGACAAAAGT
TACTTTTTTGAACTTGGAACATACGACCCTGGCCTTGATGTTTGGGGTGGGGAAAATATG
GAGCTCTCATTCAAGGTGTGGATGTGTGGTGGTGAAATTGAGATCATTCCCTGCTCCCGA
GTGGGCCATATATTCAGAAATGACAATCCATATTCCTTCCCCAAAGACCGGATGAAGACA
GTGGAGCGGAACTTGGTGCGGGTTGCCGAGGTCTGGCTGGATGAGTATAAGGAGCTGTTC
TATGGCCATGGAGACCACCTCATCGACCAAGGGCTAGATGTTGGCAACCTCACCCAGCAA
AGGGAGCTGCGAAAGAAACTGAAGTGCAAAAGTTTCAAATGGTACTTGGAGAATGTCTTT
CCTGACTTAAGGGCTCCCATTGTGAGAGCTAGTGGTGTGCTTATTAATGTGGCTTTGGGT
AAATGCATTTCCATTGAAAACACTACAGTCATTCTGGAAGACTGCGATGGGAGCAAAGAG
CTTCAACAATTTAATTACACCTGGTTAAGGCTTATTAAATGTGGAGAATGGTGTATAGCC
CCCATCCCTGATAAAGGAGCCGTAAGGCTGCACCCTTGTGATAACAGAAACAAAGGGCTA
AAATGGCTGCATAAATCAACATCAGTCTTTCATCCAGAACTGGTGAATCACATTGTTTTT
GAAAACAATCAGCAATTATTATGCTTGGAAGGAAATTTTTCTCAAAAGATCCTGAAAGTA
GCTGCCTGTGACCCAGTGAAGCCATATCAAAAGTGGAAATTTGAAAAATATTATGAAGCC
TGA
Enzyme 106 GenBank Gene ID AK292154 Link Image
Enzyme 106 GeneCard ID GALNT5 Link Image
Enzyme 106 GenAtlas ID GALNT5 Link Image
Enzyme 106 HGNC ID HGNC:4127 Link Image
Enzyme 106 Chromosome Location 2
Enzyme 106 Locus 2q24.1
Enzyme 106 SNPs SNPJam Report Link Image
Enzyme 106 General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  2. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 106 Metabolite References Not Available
Enzyme 107 [top]
Enzyme 107 ID 15265
Enzyme 107 Name 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)
Enzyme 107 Synonyms Not Available
Enzyme 107 Gene Name GALNTL1
Enzyme 107 Protein Sequence >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)
MRKIRANAIAILTVAWILGTFYYLWQDNRAHAASSGGRGAQRAGRRSEQLREDRTIPLIV
TGTPSKGFDEKAYLSAKQLKAGEDPYRQHAFNQLESDKLSPDRPIRDTRHYSCPSVSYSS
DLPATSVIITFHNEARSTLLRTVKSVLNRTPANLIQEIILVDDFSSDPEDCLLLTRIPKV
KCLRNDRREGLIRSRVRGADMAAATVLTFLDSHCEVNTEWLPPMLQRVKEDHTRVVSPII
DVISLDNFAYLAASADLRGGFDWSLHFKWEQIPLEQKMTRTDPTRPIRTPVIAGGIFVID
KSWFNHLGKYDAQMDIWGGENFELSFRVWMCGGSLEIVPCSRVGHVFRKRHPYNFPEGNA
LTYIRNTKRTAEVWMDEYKQYYYEARPSAIGKAFGSVATRIEQRKKMNCKSFRWYLENVY
PELTVPVKEALPGIIKQGVNCLESQGQNTAGDFLLGMGICRGSAKNPQPAQAWLFSDHLI
QQQGKCLAATSTLMSSPGSPVILQMCNPREGKQKWRRKGSFIQHSVSGLCLETKPAQLVT
SKCQADAQAQQWQLLPHT
Enzyme 107 Number of Residues 558
Enzyme 107 Molecular Weight 63107
Enzyme 107 Theoretical pI 9.47
Enzyme 107 GO Classification Not Available
Enzyme 107 General Function Not Available
Enzyme 107 Specific Function Not Available
Enzyme 107 Pathways Not Available
Enzyme 107 Reactions Not Available
Enzyme 107 Pfam Domain Function
Enzyme 107 Signals
  • None
Enzyme 107 Transmembrane Regions
  • None
Enzyme 107 Essentiality Not Available
Enzyme 107 GenBank ID Protein 68534728 Link Image
Enzyme 107 UniProtKB/Swiss-Prot ID Q4KMG3 Link Image
Enzyme 107 UniProtKB/Swiss-Prot Entry Name Q4KMG3_HUMAN Link Image
Enzyme 107 PDB ID Not Available
Enzyme 107 Cellular Location Not Available
Enzyme 107 Gene Sequence >1677 bp
ATGAGGAAGATCCGCGCCAATGCCATCGCCATCCTGACCGTAGCCTGGATCCTGGGCACT
TTCTACTACTTATGGCAGGACAACCGAGCCCACGCAGCATCCTCCGGCGGCCGGGGCGCG
CAGAGGGCAGGCAGGAGGTCGGAGCAGCTCCGCGAGGACCGCACCATCCCGCTCATTGTG
ACAGGAACTCCCTCGAAAGGCTTTGATGAGAAGGCCTACCTGTCGGCCAAGCAGCTGAAG
GCTGGAGAGGACCCCTACAGACAGCACGCCTTCAACCAGCTGGAGAGTGACAAGCTGAGC
CCAGACCGGCCCATCCGGGACACCCGCCATTACAGCTGCCCATCTGTGTCCTACTCCTCG
GACCTGCCAGCCACCAGCGTCATCATCACCTTCCACAATGAGGCCCGTTCCACCCTGCTG
CGCACAGTGAAGAGTGTCCTGAACCGAACTCCTGCCAACTTGATCCAGGAGATCATTTTA
GTGGATGACTTCAGCTCAGATCCGGAAGACTGTCTACTCCTGACCAGGATCCCCAAGGTC
AAGTGCCTGCGCAATGATCGGCGGGAAGGGCTGATCCGGTCCCGAGTGCGTGGGGCGGAC
ATGGCTGCAGCTACCGTTCTCACCTTTCTGGATAGCCACTGCGAAGTGAACACCGAGTGG
CTGCCGCCCATGCTGCAGCGGGTGAAGGAGGACCACACCCGCGTGGTGAGTCCCATCATT
GATGTCATCAGTCTGGATAATTTTGCCTACCTTGCAGCATCTGCTGACCTTCGTGGAGGG
TTCGACTGGAGCCTGCATTTCAAGTGGGAGCAGATCCCTCTTGAGCAGAAGATGACCCGG
ACAGACCCCACCAGGCCCATAAGGACGCCTGTCATAGCTGGAGGAATCTTCGTGATCGAC
AAGTCCTGGTTTAACCACTTGGGAAAGTATGATGCCCAGATGGACATCTGGGGGGGAGAG
AATTTTGAGCTCTCCTTCAGGGTGTGGATGTGTGGTGGCAGTCTGGAGATCGTCCCCTGC
AGCCGGGTGGGCCATGTCTTCAGGAAACGGCACCCCTACAACTTCCCTGAGGGTAATGCC
CTCACCTACATCAGGAATACTAAGCGCACTGCAGAAGTGTGGATGGATGAATACAAGCAA
TACTACTATGAGGCCCGGCCCTCGGCCATCGGGAAGGCCTTCGGCAGTGTGGCTACGCGG
ATAGAGCAGAGGAAGAAGATGAACTGCAAGTCCTTCCGCTGGTACCTGGAGAACGTCTAC
CCAGAGCTCACGGTCCCCGTGAAGGAAGCACTCCCCGGCATCATTAAGCAGGGGGTGAAC
TGCTTAGAATCTCAGGGCCAGAACACAGCTGGTGACTTCCTGCTTGGAATGGGGATCTGC
AGAGGGTCTGCCAAGAACCCGCAGCCCGCCCAGGCATGGCTGTTCAGTGACCACCTCATC
CAGCAGCAGGGGAAGTGCCTGGCTGCCACCTCCACCTTAATGTCCTCCCCTGGATCCCCA
GTCATACTGCAGATGTGCAACCCTAGAGAAGGCAAGCAGAAATGGAGGAGAAAAGGATCT
TTCATCCAGCATTCAGTCAGTGGCCTCTGCCTGGAGACAAAGCCTGCCCAGCTGGTGACC
AGCAAGTGTCAGGCTGACGCCCAGGCCCAGCAGTGGCAGCTGTTGCCACACACATGA
Enzyme 107 GenBank Gene ID BC098578 Link Image
Enzyme 107 GeneCard ID Q4KMG3 Link Image
Enzyme 107 GenAtlas ID GALNTL1 Link Image
Enzyme 107 HGNC ID HGNC:23233 Link Image
Enzyme 107 Chromosome Location 14
Enzyme 107 Locus 14q24.1
Enzyme 107 SNPs SNPJam Report Link Image
Enzyme 107 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 107 Metabolite References Not Available
Enzyme 108 [top]
Enzyme 108 ID 15266
Enzyme 108 Name Pp-GalNAc-transferase 20
Enzyme 108 Synonyms
  1. SubName: Williams-Beuren syndrome chromosome region 17
  2. SubName: Williams-Beuren syndrome chromosome region 17, isoform CRA_d
  3. SubName: cDNA FLJ76765, highly similar to Homo sapiens Williams-Beuren syndrome chromosome region 17 (WBSCR17), mRNA
Enzyme 108 Gene Name GALNT20
Enzyme 108 Protein Sequence >Pp-GalNAc-transferase 20
MASLRRVKVLLVLNLIAVAGFVLFLAKCRPIAVRSGDAFHEIRPRAEVANLSAHSASPIQ
DAVLKRLSLLEDIVYRQLNGLSKSLGLIEGYGGRGKGGLPATLSPAEEEKAKGPHEKYGY
NSYLSEKISLDRSIPDYRPTKCKELKYSKDLPQISIIFIFVNEALSVILRSVHSAVNHTP
THLLKEIILVDDNSDEEELKVPLEEYVHKRYPGLVKVVRNQKREGLIRARIEGWKVATGQ
VTGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENSAHGYSWELW
CMYISPPKDWWDAGDPSLPIRTPAMIGCSFVVNRKFFGEIGLLDPGMDVYGGENIELGIK
VWLCGGSMEVLPCSRVAHIERKKKPYNSNIGFYTKRNALRVAEVWMDDYKSHVYIAWNLP
LENPGIDIGDVSERRALRKSLKCKNFQWYLDHVYPEMRRYNNTVAYGELRNNKAKDVCLD
QGPLENHTAILYPCHGWGPQLARYTKEGFLHLGALGTTTLLPDTRCLVDNSKSRLPQLLD
CDKVKSSLYKRWNFIQNGAIMNKGTGRCLEVENRGLAGIDLILRSCTGQRWTIKNSIK
Enzyme 108 Number of Residues 598
Enzyme 108 Molecular Weight 67750.5
Enzyme 108 Theoretical pI 9.17
Enzyme 108 GO Classification Not Available
Enzyme 108 General Function Involved in sugar binding
Enzyme 108 Specific Function Not Available
Enzyme 108 Pathways Not Available
Enzyme 108 Reactions Not Available
Enzyme 108 Pfam Domain Function
Enzyme 108 Signals
  • None
Enzyme 108 Transmembrane Regions
  • None
Enzyme 108 Essentiality Not Available
Enzyme 108 GenBank ID Protein 86475573 Link Image
Enzyme 108 UniProtKB/Swiss-Prot ID Q2L4S5 Link Image
Enzyme 108 UniProtKB/Swiss-Prot Entry Name Q2L4S5_HUMAN Link Image
Enzyme 108 PDB ID Not Available
Enzyme 108 Cellular Location Not Available
Enzyme 108 Gene Sequence >1797 bp
ATGGCTTCACTGAGAAGAGTCAAAGTGCTGTTGGTGTTGAACTTGATCGCGGTAGCCGGC
TTCGTGCTCTTCCTGGCCAAGTGCCGGCCCATCGCGGTGCGCAGCGGAGACGCCTTCCAC
GAGATCCGGCCGCGCGCCGAGGTGGCCAACCTCAGCGCGCACAGCGCCAGCCCCATCCAG
GATGCGGTCCTGAAGCGCCTGTCGCTGCTGGAGGACATCGTGTACCGGCAGCTGAATGGC
TTATCCAAATCCCTTGGGCTCATTGAAGGTTATGGTGGGCGGGGTAAAGGGGGCCTTCCG
GCTACTCTTTCCCCGGCTGAAGAAGAAAAGGCTAAGGGACCCCATGAGAAGTATGGCTAC
AATTCATACCTCAGTGAAAAAATTTCACTGGACCGTTCCATTCCGGATTATCGTCCCACC
AAGTGTAAGGAGCTCAAGTACTCCAAGGACCTGCCCCAGATATCCATCATATTCATCTTC
GTGAACGAGGCCCTGTCGGTGATCCTGCGGTCCGTGCACAGTGCCGTCAATCACACGCCC
ACACACCTGCTGAAGGAAATCATTCTGGTGGATGACAACAGCGACGAAGAGGAGCTGAAG
GTCCCCCTAGAGGAGTATGTCCACAAACGCTACCCCGGGCTGGTGAAGGTGGTAAGAAAT
CAGAAGAGGGAAGGCCTGATCCGCGCTCGCATTGAGGGCTGGAAGGTGGCTACCGGGCAG
GTCACTGGCTTCTTTGATGCCCACGTGGAATTCACCGCTGGCTGGGCTGAGCCGGTTCTA
TCCCGCATCCAGGAAAACCGGAAGCGTGTGATCCTCCCCTCCATTGACAACATCAAACAG
GACAACTTTGAGGTGCAGCGGTACGAGAACTCGGCCCACGGGTACAGCTGGGAGCTGTGG
TGCATGTACATCAGCCCCCCAAAAGACTGGTGGGACGCCGGAGACCCTTCTCTCCCCATC
AGGACCCCAGCCATGATAGGCTGCTCGTTCGTGGTCAACAGGAAGTTCTTCGGTGAAATT
GGTCTTCTGGATCCTGGCATGGATGTATACGGAGGAGAAAATATTGAACTGGGAATCAAG
GTATGGCTCTGTGGGGGCAGCATGGAGGTCCTTCCTTGCTCACGGGTGGCCCACATTGAG
CGGAAGAAGAAGCCATATAATAGCAACATTGGCTTCTACACCAAGAGGAATGCTCTTCGC
GTTGCTGAGGTCTGGATGGACGATTACAAGTCTCATGTGTACATAGCGTGGAACCTGCCG
CTGGAGAATCCGGGAATTGACATCGGTGATGTCTCCGAAAGAAGAGCATTAAGGAAAAGT
TTAAAGTGTAAGAATTTCCAGTGGTACCTGGACCATGTTTACCCAGAAATGAGAAGATAC
AATAATACCGTTGCTTACGGGGAGCTTCGCAACAACAAGGCAAAAGACGTCTGCTTGGAC
CAGGGGCCGCTGGAGAACCACACAGCAATATTGTATCCGTGCCATGGCTGGGGACCACAG
CTTGCCCGCTACACCAAGGAAGGCTTCCTGCACTTGGGTGCCCTGGGGACCACCACACTC
CTCCCTGACACCCGCTGCCTGGTGGACAACTCCAAGAGTCGGCTGCCCCAGCTCCTGGAC
TGCGACAAGGTCAAGAGCAGCCTGTACAAGCGCTGGAACTTCATCCAGAATGGAGCCATC
ATGAACAAGGGCACGGGACGCTGCCTGGAGGTGGAGAACCGGGGCCTGGCTGGCATCGAC
CTCATCCTCCGCAGCTGCACAGGTCAGAGGTGGACCATTAAGAACTCCATCAAGTAG
Enzyme 108 GenBank Gene ID AJ626726 Link Image
Enzyme 108 GeneCard ID GALNT20 Link Image
Enzyme 108 GenAtlas ID GALNT20 Link Image
Enzyme 108 HGNC ID HGNC:16347 Link Image
Enzyme 108 Chromosome Location Not Available
Enzyme 108 Locus Not Available
Enzyme 108 SNPs SNPJam Report Link Image
Enzyme 108 General References
  1. Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed Link Image]
Enzyme 108 Metabolite References Not Available
Enzyme 109 [top]
Enzyme 109 ID 15267
Enzyme 109 Name 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)
Enzyme 109 Synonyms Not Available
Enzyme 109 Gene Name GBGT1
Enzyme 109 Protein Sequence >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)
MHRRRLALGLGFCLLAGTSLSVLWVYLENWLPVSYVPYYLPCPEIFNMKLHYKREKPLQP
VVWSQYPQPKLLEHRPTQLLTLTPWLAPIVSEGTFNPELLQHIYQPLNLTIGVTVFAVGK
YTHFIQSFLESAEEFFMRGYRVHYYIFTDNPAAVPGVPLGPHRLLSSIPIQGHSHWEETS
MRRMETISQHIAKRAHREVDYLFCLDVDMVFRNPWGPETLGDLVAAIHPSYYAVPRQQFP
YERRRVSTAFVADSEGDFYYGGAVFGGQVARVYEFTRGCHMAILADKANGIMAAWREESH
LNRHFISNKPSKVLSPEYLWDDRKPQPPSLKLIRFSTLDKDISCLRS
Enzyme 109 Number of Residues 347
Enzyme 109 Molecular Weight 40128
Enzyme 109 Theoretical pI 8.63
Enzyme 109 GO Classification Not Available
Enzyme 109 General Function Not Available
Enzyme 109 Specific Function Not Available
Enzyme 109 Pathways Not Available
Enzyme 109 Reactions Not Available
Enzyme 109 Pfam Domain Function Not Available
Enzyme 109 Signals
  • None
Enzyme 109 Transmembrane Regions
  • None
Enzyme 109 Essentiality Not Available
Enzyme 109 GenBank ID Protein 158256428 Link Image
Enzyme 109 UniProtKB/Swiss-Prot ID A8K633 Link Image
Enzyme 109 UniProtKB/Swiss-Prot Entry Name A8K633_HUMAN Link Image
Enzyme 109 PDB ID Not Available
Enzyme 109 Cellular Location Not Available
Enzyme 109 Gene Sequence >1044 bp
ATGCATCGCCGGAGACTGGCCCTGGGTCTGGGGTTCTGCCTGTTGGCGGGCACAAGCCTC
AGTGTCCTGTGGGTGTATCTTGAGAACTGGCTGCCAGTCTCCTATGTCCCCTATTATCTC
CCCTGCCCAGAGATCTTCAACATGAAGCTGCACTACAAGAGGGAGAAGCCACTCCAGCCC
GTGGTATGGTCACAGTACCCTCAGCCCAAGCTGCTGGAGCACAGGCCCACACAGCTGCTG
ACACTCACACCCTGGTTGGCGCCCATCGTCTCCGAGGGAACCTTCAACCCAGAGCTTCTG
CAGCACATCTACCAGCCACTGAACCTGACCATTGGGGTCACGGTGTTTGCCGTGGGGAAG
TACACTCATTTCATCCAGTCCTTCCTGGAGTCAGCCGAGGAGTTCTTCATGCGTGGGTAC
CGGGTGCACTACTACATCTTCACTGACAACCCTGCAGCCGTTCCCGGGGTCCCGCTGGGT
CCCCACCGGCTTCTCAGCTCCATCCCCATCCAGGGTCACTCCCACTGGGAGGAGACATCC
ATGCGCCGGATGGAGACCATCAGCCAGCACATTGCTAAGAGGGCTCACCGGGAGGTGGAC
TACCTCTTCTGCCTTGATGTGGACATGGTGTTTCGGAACCCGTGGGGCCCTGAGACCTTG
GGAGACCTGGTGGCTGCCATTCACCCAAGCTACTACGCCGTTCCCCGCCAGCAGTTCCCC
TATGAGCGCAGGCGTGTTTCCACTGCCTTTGTGGCAGACAGCGAAGGGGACTTCTATTAT
GGTGGGGCAGTCTTCGGGGGGCAGGTGGCCAGGGTATATGAGTTTACTAGGGGCTGCCAC
ATGGCCATCCTGGCGGACAAGGCCAATGGCATCATGGCTGCCTGGCGGGAGGAAAGCCAC
CTGAACCGTCACTTCATCTCAAACAAGCCGTCCAAGGTGCTGTCCCCCGAGTACCTCTGG
GACGACAGGAAGCCCCAGCCACCCAGCCTGAAGCTGATCCGCTTTTCTACACTGGACAAG
GATATCAGCTGCCTGAGGAGCTGA
Enzyme 109 GenBank Gene ID AK291498 Link Image
Enzyme 109 GeneCard ID A8K633 Link Image
Enzyme 109 GenAtlas ID Not Available
Enzyme 109 HGNC ID Not Available
Enzyme 109 Chromosome Location Not Available
Enzyme 109 Locus Not Available
Enzyme 109 SNPs SNPJam Report Link Image
Enzyme 109 General References Not Available
Enzyme 109 Metabolite References Not Available
Enzyme 110 [top]
Enzyme 110 ID 16420
Enzyme 110 Name cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
Enzyme 110 Synonyms Not Available
Enzyme 110 Gene Name Not Available
Enzyme 110 Protein Sequence >cDNA, FLJ93689, highly similar to Homo sapiens UDP glucuronosyltransferase 2 family, polypeptide B7 (UGT2B7), mRNA
MSVKWTSVILLIQLSFCFSSGNCGKVLVWAAEYSHWMNIKTILDELIQRGHEVTVLASSA
SILFDPNNSSALKIEIYPTSLTKTELENFIMQQIKRWSDLPKDTFWLYFSQVQEIMSIFG
DITRKFCKDVVSNKKFMKKVQESRFDVIFADAIFPCSELLAELFNIPFVYSLSFSPGYTF
EKHSGGFIFPPSYVPVVMSELTDQMTFMERVKNMIYVLYFDFWFEIFDMKKWDQFYSEVL
GRPTTLSETMGKADVWLIRNSWNFQFPYPLLPNVDFVGGLHCKPAKPLPKEMEDFVQSSG
ENGVVVFSLGSMVSNMTEERANVIASALAQIPQKVLWRFDGNKPDTLGLNTRLYKWIPQN
DLLGHPKTRAFITHGGANGIYEAIYHGIPMVGIPLFADQPDNIAHMKARGAAVRVDFNTM
SSTDLLNALKRVINDPSYKENVMKLSRIQHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAA
HDLTWFQYHSLDVIGFLLVCVATVIFIVTKCCLFCFWKFARKAKKGKND
Enzyme 110 Number of Residues 529
Enzyme 110 Molecular Weight 60721
Enzyme 110 Theoretical pI 8.45
Enzyme 110 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 110 General Function Carbohydrate transport and metabolism
Enzyme 110 Specific Function Not Available
Enzyme 110 Pathways Not Available
Enzyme 110 Reactions Not Available
Enzyme 110 Pfam Domain Function
Enzyme 110 Signals
  • None
Enzyme 110 Transmembrane Regions
  • None
Enzyme 110 Essentiality Not Available
Enzyme 110 GenBank ID Protein Not Available
Enzyme 110 UniProtKB/Swiss-Prot ID B2R810 Link Image
Enzyme 110 UniProtKB/Swiss-Prot Entry Name B2R810_HUMAN Link Image
Enzyme 110 PDB ID Not Available
Enzyme 110 Cellular Location Not Available
Enzyme 110 Gene Sequence Not Available
Enzyme 110 GenBank Gene ID AK313190 Link Image
Enzyme 110 GeneCard ID B2R810 Link Image
Enzyme 110 GenAtlas ID Not Available
Enzyme 110 HGNC ID Not Available
Enzyme 110 Chromosome Location Not Available
Enzyme 110 Locus Not Available
Enzyme 110 SNPs Not Available
Enzyme 110 General References Not Available
Enzyme 110 Metabolite References Not Available
Enzyme 111 [top]
Enzyme 111 ID 16437
Enzyme 111 Name cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
Enzyme 111 Synonyms Not Available
Enzyme 111 Gene Name ENTPD3
Enzyme 111 Protein Sequence >cDNA, FLJ93839, highly similar to Homo sapiens ectonucleoside triphosphate diphosphohydrolase 3 (ENTPD3), mRNA (Ectonucleoside triphosphate diphosphohydrolase 3, isoform CRA_b)
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
Enzyme 111 Number of Residues 529
Enzyme 111 Molecular Weight 59106
Enzyme 111 Theoretical pI 6.40
Enzyme 111 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
Component
Enzyme 111 General Function Not Available
Enzyme 111 Specific Function Not Available
Enzyme 111 Pathways Not Available
Enzyme 111 Reactions Not Available
Enzyme 111 Pfam Domain Function
Enzyme 111 Signals
  • None
Enzyme 111 Transmembrane Regions
  • None
Enzyme 111 Essentiality Not Available
Enzyme 111 GenBank ID Protein Not Available
Enzyme 111 UniProtKB/Swiss-Prot ID B2R8D0 Link Image
Enzyme 111 UniProtKB/Swiss-Prot Entry Name B2R8D0_HUMAN Link Image
Enzyme 111 PDB ID Not Available
Enzyme 111 Cellular Location Not Available
Enzyme 111 Gene Sequence Not Available
Enzyme 111 GenBank Gene ID AK313322 Link Image
Enzyme 111 GeneCard ID B2R8D0 Link Image
Enzyme 111 GenAtlas ID Not Available
Enzyme 111 HGNC ID Not Available
Enzyme 111 Chromosome Location Not Available
Enzyme 111 Locus Not Available
Enzyme 111 SNPs SNPJam Report Link Image
Enzyme 111 General References Not Available
Enzyme 111 Metabolite References Not Available
Enzyme 112 [top]
Enzyme 112 ID 16476
Enzyme 112 Name cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
Enzyme 112 Synonyms Not Available
Enzyme 112 Gene Name PKM2
Enzyme 112 Protein Sequence >cDNA, FLJ92548, highly similar to Homo sapiens pyruvate kinase, muscle (PKM2), mRNA (Pyruvate kinase, muscle, isoform CRA_e)
MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVET
LKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIR
TGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGL
ISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMV
FASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIE
IPAEKVFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIM
LSGETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEAS
FKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQE
AWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
Enzyme 112 Number of Residues 531
Enzyme 112 Molecular Weight 57938
Enzyme 112 Theoretical pI 7.94
Enzyme 112 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 112 General Function Carbohydrate transport and metabolism
Enzyme 112 Specific Function Not Available
Enzyme 112 Pathways Not Available
Enzyme 112 Reactions Not Available
Enzyme 112 Pfam Domain Function
Enzyme 112 Signals
  • None
Enzyme 112 Transmembrane Regions
  • None
Enzyme 112 Essentiality Not Available
Enzyme 112 GenBank ID Protein Not Available
Enzyme 112 UniProtKB/Swiss-Prot ID B2R5N8 Link Image
Enzyme 112 UniProtKB/Swiss-Prot Entry Name B2R5N8_HUMAN Link Image
Enzyme 112 PDB ID 1F3X Link Image
Enzyme 112 PDB File Show
Enzyme 112 3D Structure
Enzyme 112 Cellular Location Not Available
Enzyme 112 Gene Sequence Not Available
Enzyme 112 GenBank Gene ID AK312253 Link Image
Enzyme 112 GeneCard ID B2R5N8 Link Image
Enzyme 112 GenAtlas ID Not Available
Enzyme 112 HGNC ID Not Available
Enzyme 112 Chromosome Location 15
Enzyme 112 Locus 15q22
Enzyme 112 SNPs SNPJam Report Link Image
Enzyme 112 General References Not Available
Enzyme 112 Metabolite References Not Available
Enzyme 113 [top]
Enzyme 113 ID 16488
Enzyme 113 Name 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)
Enzyme 113 Synonyms Not Available
Enzyme 113 Gene Name B4GALT1
Enzyme 113 Protein Sequence >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)
MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPL
QGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVP
HTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAI
IIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYD
YTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTI
NGFPNNYWGWGGEDDDIFNRLVFRGMSISRPNAVVGRCRMIRHSRDKKNEPNPQRFDRIA
HTKETMLSDGLNSLTYQVLDVQRYPLYTQITVDIGTPS
Enzyme 113 Number of Residues 398
Enzyme 113 Molecular Weight 43921
Enzyme 113 Theoretical pI 8.77
Enzyme 113 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 113 General Function Not Available
Enzyme 113 Specific Function Not Available
Enzyme 113 Pathways Not Available
Enzyme 113 Reactions Not Available
Enzyme 113 Pfam Domain Function
Enzyme 113 Signals
  • None
Enzyme 113 Transmembrane Regions
  • None
Enzyme 113 Essentiality Not Available
Enzyme 113 GenBank ID Protein Not Available
Enzyme 113 UniProtKB/Swiss-Prot ID B2R710 Link Image
Enzyme 113 UniProtKB/Swiss-Prot Entry Name B2R710_HUMAN Link Image
Enzyme 113 PDB ID 1FR8 Link Image
Enzyme 113 PDB File Show
Enzyme 113 3D Structure
Enzyme 113 Cellular Location Not Available
Enzyme 113 Gene Sequence Not Available
Enzyme 113 GenBank Gene ID AK312797 Link Image
Enzyme 113 GeneCard ID B2R710 Link Image
Enzyme 113 GenAtlas ID Not Available
Enzyme 113 HGNC ID Not Available
Enzyme 113 Chromosome Location Not Available
Enzyme 113 Locus Not Available
Enzyme 113 SNPs SNPJam Report Link Image
Enzyme 113 General References Not Available
Enzyme 113 Metabolite References Not Available
Enzyme 114 [top]
Enzyme 114 ID 16489
Enzyme 114 Name cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-)
Enzyme 114 Synonyms
  1. SubName: UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 2, isoform CRA_a
Enzyme 114 Gene Name B4GALT2
Enzyme 114 Protein Sequence >cDNA FLJ38554 fis, clone HCHON2002496, highly similar to Beta-1,4-galactosyltransferase 2 (EC 2.4.1.-)
MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSARGPAHALHPAASS
SSSSSNCSRPNATASSSGLPEVPSALPGPTAPTLPPCPDSPPGLVGRLLIEFTSPMPLER
VQRENPGVLMGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPILRRQRLRYGVYV
INQHGEDTFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIA
MDKFGFRLPYAGYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPD
IRIGRYRMIKHDRDKHNEPNPQRFTKIQNTKLTMKRDGIGSVRYQVLEVSRQPLFTNITV
DIGRPPSWPPRG
Enzyme 114 Number of Residues 372
Enzyme 114 Molecular Weight 41973
Enzyme 114 Theoretical pI 9.66
Enzyme 114 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 114 General Function Not Available
Enzyme 114 Specific Function Not Available
Enzyme 114 Pathways Not Available
Enzyme 114 Reactions Not Available
Enzyme 114 Pfam Domain Function
Enzyme 114 Signals
  • None
Enzyme 114 Transmembrane Regions
  • None
Enzyme 114 Essentiality Not Available
Enzyme 114 GenBank ID Protein Not Available
Enzyme 114 UniProtKB/Swiss-Prot ID B3KTP0 Link Image
Enzyme 114 UniProtKB/Swiss-Prot Entry Name B3KTP0_HUMAN Link Image
Enzyme 114 PDB ID Not Available
Enzyme 114 Cellular Location Not Available
Enzyme 114 Gene Sequence Not Available
Enzyme 114 GenBank Gene ID AK095873 Link Image
Enzyme 114 GeneCard ID B3KTP0 Link Image
Enzyme 114 GenAtlas ID Not Available
Enzyme 114 HGNC ID Not Available
Enzyme 114 Chromosome Location Not Available
Enzyme 114 Locus Not Available
Enzyme 114 SNPs SNPJam Report Link Image
Enzyme 114 General References Not Available
Enzyme 114 Metabolite References Not Available
Enzyme 115 [top]
Enzyme 115 ID 16517
Enzyme 115 Name UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4
Enzyme 115 Synonyms
  1. SubName: UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4, isoform CRA_a
  2. SubName: cDNA, FLJ95212, Homo sapiens UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase,polypeptide 4 (B4GALT4), mRNA
Enzyme 115 Gene Name B4GALT4
Enzyme 115 Protein Sequence >UDP-Gal:betaGlcNAc beta 1,4-galactosyltransferase, polypeptide 4
MGFNLTFHLSYKFRLLLLLTLCLTVVGWATSNYFVGAIQEIPKAKEFMANFHKTLILGKG
KTLTNEASTKKVELDNCPSVSPYLRGQSKLIFKPDLTLEEVQAENPKVSRGRYRPQECKA
LQRVAILVPHRNREKHLMYLLEHLHPFLQRQQLDYGIYVIHQAEGKKFNRAKLLNVGYLE
ALKEENWDCFIFHDVDLVPENDFNLYKCEEHPKHLVVGRNSTGYRLRYSGYFGGVTALSR
EQFFKVNGFSNNYWGWGGEDDDLRLRVELQRMKISRPLPEVGKYTMVFHTRDKGNEVNAE
RMKLLHQVSRVWRTDGLSSCSYKLVSVEHNPLYINITVDFWFGA
Enzyme 115 Number of Residues 344
Enzyme 115 Molecular Weight 40040.9
Enzyme 115 Theoretical pI 9.42
Enzyme 115 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 115 General Function Involved in transferase activity, transferring glycosyl groups
Enzyme 115 Specific Function Not Available
Enzyme 115 Pathways Not Available
Enzyme 115 Reactions Not Available
Enzyme 115 Pfam Domain Function
Enzyme 115 Signals
  • None
Enzyme 115 Transmembrane Regions
  • None
Enzyme 115 Essentiality Not Available
Enzyme 115 GenBank ID Protein 189069376 Link Image
Enzyme 115 UniProtKB/Swiss-Prot ID B2RAZ5 Link Image
Enzyme 115 UniProtKB/Swiss-Prot Entry Name B2RAZ5_HUMAN Link Image
Enzyme 115 PDB ID Not Available
Enzyme 115 Cellular Location Not Available
Enzyme 115 Gene Sequence >1035 bp
ATGGGCTTCAACCTGACTTTCCACCTTTCCTACAAATTCCGATTACTGTTGCTGTTGACT
TTGTGCCTGACAGTGGTTGGGTGGGCCACCAGTAACTACTTCGTGGGTGCCATTCAAGAG
ATTCCTAAAGCAAAGGAGTTCATGGCTAATTTCCATAAGACCCTCATTTTGGGGAAGGGA
AAAACTCTGACTAATGAAGCATCCACGAAGAAGGTAGAACTTGACAACTGCCCTTCTGTG
TCTCCTTACCTCAGAGGCCAGAGCAAGCTCATTTTCAAACCAGATCTCACTTTGGAAGAG
GTACAGGCAGAAAATCCCAAAGTGTCCAGAGGCCGGTATCGCCCTCAGGAATGTAAAGCT
TTACAGAGGGTCGCCATCCTCGTTCCCCACCGGAACAGAGAGAAACACCTGATGTACCTG
CTGGAACATCTGCATCCCTTCCTGCAGAGGCAGCAGCTGGATTATGGCATCTACGTCATC
CACCAGGCTGAAGGTAAAAAGTTTAATCGAGCCAAACTCTTGAATGTGGGCTATCTAGAA
GCCCTCAAGGAAGAAAATTGGGACTGCTTTATATTCCACGATGTGGACCTGGTACCCGAG
AATGACTTTAACCTTTACAAGTGTGAGGAGCATCCCAAGCATCTGGTGGTTGGCAGGAAC
AGCACTGGGTACAGGTTACGTTACAGTGGATATTTTGGGGGTGTTACTGCCCTAAGCAGA
GAGCAGTTTTTCAAGGTGAATGGATTCTCTAACAACTACTGGGGATGGGGAGGCGAAGAC
GATGACCTCAGACTCAGGGTTGAGCTCCAAAGAATGAAAATTTCCCGGCCCCTGCCTGAA
GTGGGTAAATATACAATGGTCTTCCACACTAGAGACAAAGGCAATGAGGTGAACGCAGAA
CGGATGAAGCTCTTACACCAAGTGTCACGAGTCTGGAGAACAGATGGGTTGAGTAGTTGT
TCTTATAAATTAGTATCTGTGGAACACAATCCTTTATATATCAACATCACAGTGGATTTC
TGGTTTGGTGCATGA
Enzyme 115 GenBank Gene ID AK314425 Link Image
Enzyme 115 GeneCard ID B4GALT4 Link Image
Enzyme 115 GenAtlas ID B4GALT4 Link Image
Enzyme 115 HGNC ID HGNC:927 Link Image
Enzyme 115 Chromosome Location 3
Enzyme 115 Locus 3q13.3
Enzyme 115 SNPs SNPJam Report Link Image
Enzyme 115 General References
  1. Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed Link Image]
Enzyme 115 Metabolite References Not Available
Enzyme 116 [top]
Enzyme 116 ID 16544
Enzyme 116 Name Glycosyltransferase 28 domain containing 1, isoform CRA_b
Enzyme 116 Synonyms
  1. SubName: cDNA, FLJ92520, Homo sapiens uncharacterized hematopoietic stem/progenitor cellsprotein MDS031 (MDS031), mRNA
Enzyme 116 Gene Name GLT28D1
Enzyme 116 Protein Sequence >Glycosyltransferase 28 domain containing 1, isoform CRA_b
MKCVFVTVGTTSFDDLIACVSAPDSLQKIESLGYNRLILQIGRGTVVPEPFSTESFTLDV
YRYKDSLKEDIQKADLVISHAGAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEG
HLFYCTCSTLPGLLQSMDLSTLKCYPPGQPEKFSAFLDKVVGLQK
Enzyme 116 Number of Residues 165
Enzyme 116 Molecular Weight 18225
Enzyme 116 Theoretical pI 6.50
Enzyme 116 GO Classification
Function
  • binding
  • carbohydrate binding
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • carbohydrate metabolism
  • lipid glycosylation
  • lipid modification
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
Enzyme 116 General Function Not Available
Enzyme 116 Specific Function Not Available
Enzyme 116 Pathways Not Available
Enzyme 116 Reactions Not Available
Enzyme 116 Pfam Domain Function
Enzyme 116 Signals
  • None
Enzyme 116 Transmembrane Regions
  • None
Enzyme 116 Essentiality Not Available
Enzyme 116 GenBank ID Protein Not Available
Enzyme 116 UniProtKB/Swiss-Prot ID B2R5L5 Link Image
Enzyme 116 UniProtKB/Swiss-Prot Entry Name B2R5L5_HUMAN Link Image
Enzyme 116 PDB ID Not Available
Enzyme 116 Cellular Location Not Available
Enzyme 116 Gene Sequence Not Available
Enzyme 116 GenBank Gene ID AK312229 Link Image
Enzyme 116 GeneCard ID B2R5L5 Link Image
Enzyme 116 GenAtlas ID Not Available
Enzyme 116 HGNC ID Not Available
Enzyme 116 Chromosome Location Not Available
Enzyme 116 Locus Not Available
Enzyme 116 SNPs SNPJam Report Link Image
Enzyme 116 General References Not Available
Enzyme 116 Metabolite References Not Available
Enzyme 117 [top]
Enzyme 117 ID 16545
Enzyme 117 Name 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)
Enzyme 117 Synonyms Not Available
Enzyme 117 Gene Name MGAT2
Enzyme 117 Protein Sequence >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)
MRFRIYKRKVLILTLVVAACGFVLWSSNGRQRKNEALAPPLLDAEPARGAGGRGGDHPSV
AVGIRRVSNVSAASLVPAVPQPEADNLTLRYRSLVYQLNFDQTLRNVDKAGTWAPRELVL
VVQVHNRPEYLRLLLDSLRKAQGIDNVLVIFSHDFWSTEINQLIAGVNFCPVLQVFFPFS
IQLYPNEFPGSDPRDCPRDLPKNAALKLGCINAEYPDSFGHYREAKFSQTKHHWWWKLHF
VWERVKILRDYAGLILFLEEDHYLAPDFYHVFKKMWKLKQQECPECDVLSLGTYSASRSF
YGMADKVDVKTWKSTEHNMGLALTRNAYQKLIECTDTFCTYDDYNWDWTLQYLTVSCLPK
FWKVLVPQIPRIFHAGDCGMHHKKTCRPSTQSAQIESLLNNNKQYMFPETLTISEKFTVV
AISPPRKNGGWGDIRDHELCKSYRRLQ
Enzyme 117 Number of Residues 447
Enzyme 117 Molecular Weight 51551
Enzyme 117 Theoretical pI 8.94
Enzyme 117 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • alpha-1,6-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • oligosaccharide biosynthesis
  • oligosaccharide metabolism
  • physiological process
Component
  • Golgi apparatus
  • Golgi stack
  • cell
  • integral to membrane
  • intracellular membrane-bound organelle
  • intrinsic to membrane
  • membrane
  • membrane-bound organelle
  • organelle
Enzyme 117 General Function Not Available
Enzyme 117 Specific Function Not Available
Enzyme 117 Pathways Not Available
Enzyme 117 Reactions Not Available
Enzyme 117 Pfam Domain Function
Enzyme 117 Signals
  • None
Enzyme 117 Transmembrane Regions
  • None
Enzyme 117 Essentiality Not Available
Enzyme 117 GenBank ID Protein Not Available
Enzyme 117 UniProtKB/Swiss-Prot ID B3KPC5 Link Image
Enzyme 117 UniProtKB/Swiss-Prot Entry Name B3KPC5_HUMAN Link Image
Enzyme 117 PDB ID Not Available
Enzyme 117 Cellular Location Not Available
Enzyme 117 Gene Sequence Not Available
Enzyme 117 GenBank Gene ID AK056167 Link Image
Enzyme 117 GeneCard ID B3KPC5 Link Image
Enzyme 117 GenAtlas ID Not Available
Enzyme 117 HGNC ID Not Available
Enzyme 117 Chromosome Location 14
Enzyme 117 Locus 14q21
Enzyme 117 SNPs SNPJam Report Link Image
Enzyme 117 General References Not Available
Enzyme 117 Metabolite References Not Available
Enzyme 118 [top]
Enzyme 118 ID 16546
Enzyme 118 Name cDNA, FLJ93340, Homo sapiens exostoses (multiple)-like 2 (EXTL2), mRNA (Exostoses (Multiple)-like 2, isoform CRA_a)
Enzyme 118 Synonyms Not Available
Enzyme 118 Gene Name EXTL2
Enzyme 118 Protein Sequence >cDNA, FLJ93340, Homo sapiens exostoses (multiple)-like 2 (EXTL2), mRNA (Exostoses (Multiple)-like 2, isoform CRA_a)
MRCCHICKLPGRVMGIRVLRLSLVVILVLLLVAGALTALLPSVKEDKMLMLRREIKSQGK
STMDSFTLIMQTYNRTDLLLKLLNHYQAVPNLHKVIVVWNNIGEKAPDELWNSLGPHPIP
VIFKQQTANRMRNRLQVFPELETNAVLMVDDDTLISTPDLVFAFSVWQQFPDQIVGFVPR
KHVSTSSGIYSYGSFEMQAPGSGNGDQYSMVLIGASFFNSKYLELFQRQPAAVHALIDDT
QNCDDIAMNFIIAKHIGKTSGIFVKPVNMDNLEKETNSGYSGMWHRAEHALQRSYCINKL
VNIYDSMPLRYSNIMISQFGFPYANYKRKI
Enzyme 118 Number of Residues 330
Enzyme 118 Molecular Weight 37466
Enzyme 118 Theoretical pI 9.24
Enzyme 118 GO Classification Not Available
Enzyme 118 General Function Not Available
Enzyme 118 Specific Function Not Available
Enzyme 118 Pathways Not Available
Enzyme 118 Reactions Not Available
Enzyme 118 Pfam Domain Function
Enzyme 118 Signals
  • None
Enzyme 118 Transmembrane Regions
  • None
Enzyme 118 Essentiality Not Available
Enzyme 118 GenBank ID Protein Not Available
Enzyme 118 UniProtKB/Swiss-Prot ID B2R795 Link Image
Enzyme 118 UniProtKB/Swiss-Prot Entry Name B2R795_HUMAN Link Image
Enzyme 118 PDB ID Not Available
Enzyme 118 Cellular Location Not Available
Enzyme 118 Gene Sequence Not Available
Enzyme 118 GenBank Gene ID AK312895 Link Image
Enzyme 118 GeneCard ID B2R795 Link Image
Enzyme 118 GenAtlas ID Not Available
Enzyme 118 HGNC ID Not Available
Enzyme 118 Chromosome Location Not Available
Enzyme 118 Locus Not Available
Enzyme 118 SNPs SNPJam Report Link Image
Enzyme 118 General References Not Available
Enzyme 118 Metabolite References Not Available
Enzyme 119 [top]
Enzyme 119 ID 16547
Enzyme 119 Name cDNA, FLJ93616, highly similar to Homo sapiens exostoses (multiple) 1 (EXT1), mRNA (Exostoses (Multiple) 1)
Enzyme 119 Synonyms Not Available
Enzyme 119 Gene Name EXT1
Enzyme 119 Protein Sequence >cDNA, FLJ93616, highly similar to Homo sapiens exostoses (multiple) 1 (EXT1), mRNA (Exostoses (Multiple) 1)
MQAKKRYFILLSAGSCLALLFYFGGLQFRASRSHSRREEHSGRNGLHHPSPDHFWPRFPD
ALRPFVPWDQLENEDSSVHISPRQKRDANSSIYKGKKCRMESCFDFTLCKKNGFKVYVYP
QQKGEKIAESYQNILAAIEGSRFYTSDPSQACLFVLSLDTLDRDQLSPQYVHNLRSKVQS
LHLWNNGRNHLIFNLYSGTWPDYTEDVGFDIGQAMLAKASISTENFRPNFDVSIPLFSKD
HPRTGGERGFLKFNTIPPLRKYMLVFKGKRYLTGIGSDTRNALYHVHNGEDVVLLTTCKH
GKDWQKHKDSRCDRDNTEYEKYDYREMLHNATFCLVPRGRRLGSFRFLEALQAACVPVML
SNGWELPFSEVINWNQAAVIGDERLLLQIPSTIRSIHQDKILALRQQTQFLWEAYFSSVE
KIVLTTLEIIQDRIFKHISRNSLIWNKHPGGLFVLPQYSSYLGDFPYYYANLGLKPPSKF
TAVIHAVTPLVSQSQPVLKLLVAAAKSQYCAQIIVLWNCDKPLPAKHRWPATAVPVVVIE
GESKVMSSRFLPYDNIITDAVLSLDEDTVLSTTEVDFAFTVWQSFPERIVGYPARSHFWD
NSKERWGYTSKWTNDYSMVLTGAAIYHKYYHYLYSHYLPASLKNMVDQLANCEDILMNFL
VSAVTKLPPIKVTQKKQYKETMMGQTSRASRWADPDHFAQRQSCMNTFASWFGYMPLIHS
QMRLDPVLFKDQVSILRKKYRDIERL
Enzyme 119 Number of Residues 746
Enzyme 119 Molecular Weight 86256
Enzyme 119 Theoretical pI 9.34
Enzyme 119 GO Classification
Function
Process
Component
  • cell
  • membrane
Enzyme 119 General Function Not Available
Enzyme 119 Specific Function Not Available
Enzyme 119 Pathways Not Available
Enzyme 119 Reactions Not Available
Enzyme 119 Pfam Domain Function
Enzyme 119 Signals
  • None
Enzyme 119 Transmembrane Regions
  • None
Enzyme 119 Essentiality Not Available
Enzyme 119 GenBank ID Protein Not Available
Enzyme 119 UniProtKB/Swiss-Prot ID B2R7V2 Link Image
Enzyme 119 UniProtKB/Swiss-Prot Entry Name B2R7V2_HUMAN Link Image
Enzyme 119 PDB ID Not Available
Enzyme 119 Cellular Location Not Available
Enzyme 119 Gene Sequence Not Available
Enzyme 119 GenBank Gene ID AK313129 Link Image
Enzyme 119 GeneCard ID B2R7V2 Link Image
Enzyme 119 GenAtlas ID Not Available
Enzyme 119 HGNC ID Not Available
Enzyme 119 Chromosome Location Not Available
Enzyme 119 Locus Not Available
Enzyme 119 SNPs SNPJam Report Link Image
Enzyme 119 General References Not Available
Enzyme 119 Metabolite References Not Available
Enzyme 120 [top]
Enzyme 120 ID 16549
Enzyme 120 Name UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 8 (GalNAc-T8)
Enzyme 120 Synonyms Not Available
Enzyme 120 Gene Name GALNT8
Enzyme 120 Protein Sequence >UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 8 (GalNAc-T8)
MMFWRKLPKALFIGLTLAIAVNLLLVFSSKGTLQNLFTGGLHRELPLHLNKRYGAVIKRL
SHLEVELQDLKESMKLALRQQENVNSTLKRAKDEVRPLLKAMETKVNETKKHKTQMKLFP
HSQLFRQWGEDLSEAQQKAAQDLFRKFGYNAYLSNQLPLNRTIPDTRDYRCLRKTYPSQL
PSLSVILIFVNEALSIIQRAITSIINRTPSRLLKEIILVDDFSSNGELKVHLDEKIKLYN
QKYPGLLKIIRHPERKGLAQARNTGWEAATADVVAILDAHIEVNVGWAEPILARIQEDRT
VIVSPVFDNIRFDTFKLDKYELAVDGFNWELWCRYDALPQAWIDLHDVTAPVKSPSIMGI
LAANRHFLGEIGSLDGGMLIYGGENVELSLRVWQCGGKVEILPCSRIAHLERHHKPYALD
LTAALKRNALRVAEIWMDEHKHMVYLAWNIPLQNSGIDFGDVSSRMALREKLKCKTFDWY
LKNVYPLLKPLHTIVGYGRMKNLLDENVCLDQGPVPGNTPIMYYCHEFSSQNVYYHLTGE
LYVGQLIAEASASDRCLTDPGKAEKPTLEPCSKAAKNRLHIYWDFKPGGAVINRDTKRCL
EMKKDLLGSHVLVLQTCSTQVWEIQHTVRDWGQTNSQ
Enzyme 120 Number of Residues 637
Enzyme 120 Molecular Weight 72852
Enzyme 120 Theoretical pI 9.16
Enzyme 120 GO Classification Not Available
Enzyme 120 General Function Cell wall/membrane/envelope biogenesis
Enzyme 120 Specific Function Not Available
Enzyme 120 Pathways Not Available
Enzyme 120 Reactions Not Available
Enzyme 120 Pfam Domain Function
Enzyme 120 Signals
  • None
Enzyme 120 Transmembrane Regions
  • None
Enzyme 120 Essentiality Not Available
Enzyme 120 GenBank ID Protein Not Available
Enzyme 120 UniProtKB/Swiss-Prot ID B2RU02 Link Image
Enzyme 120 UniProtKB/Swiss-Prot Entry Name B2RU02_HUMAN Link Image
Enzyme 120 PDB ID Not Available
Enzyme 120 Cellular Location Not Available
Enzyme 120 Gene Sequence Not Available
Enzyme 120 GenBank Gene ID BC140888 Link Image
Enzyme 120 GeneCard ID B2RU02 Link Image
Enzyme 120 GenAtlas ID GALNT8 Link Image
Enzyme 120 HGNC ID HGNC:4130 Link Image
Enzyme 120 Chromosome Location 12
Enzyme 120 Locus 12p13.3
Enzyme 120 SNPs SNPJam Report Link Image
Enzyme 120 General References Not Available
Enzyme 120 Metabolite References Not Available
Enzyme 121 [top]
Enzyme 121 ID 16550
Enzyme 121 Name cDNA PSEC0182 fis, clone OVARC1001636, highly similar to N-acetylgalactosaminyltransferase 7 (EC 2.4.1.-)
Enzyme 121 Synonyms
  1. SubName: UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 7 (GalNAc-T7)
Enzyme 121 Gene Name GALNT7
Enzyme 121 Protein Sequence >cDNA PSEC0182 fis, clone OVARC1001636, highly similar to N-acetylgalactosaminyltransferase 7 (EC 2.4.1.-)
MRLKIGFILRSLLVVGSFLGLVVLWSSLTPRPDDPSPLSRMREDRDVNDPMPNRGGNGLA
PGEDRFKPVVPWPHVEGVEVDLESIRRINKAKNEQEHHAGGDSQKDIMQRQYLTFKPQTF
TYHDPVLRPGILGNFEPKEPEPPGVVGGPGEKAKPLVLGPEFKQAIQASIKEFGFNMVAS
DMISLDRSVNDLRQEECKYWHYDENLLTSSVVIVFHNEGWSTLMRTVHSVIKRTPRKYLA
EIVLIDDFSNKEHLKEKLDEYIKLWNGLVKVFRNERREGLIQARSIGAQKAKLGQVLIYL
DAHCEVAVNWYAPLVAPISKDRTICTVPLIDVINGNTYEIIPQGGGDEDGYARGAWDWSM
LWKRVPLTPQEKRLRKTKTEPYRSPAMAGGLFAIEREFFFELGLYDPGLQIWGGENFEIS
YKIWQCGGKLLFVPCSRVGHIYRLEGWQGNPPPIYVGSSPTLKNYVRVVEVWWDEYKDYF
YASRPESQALPYGDISELKKFREDHNCKSFKWFMEEIAYDITSHYPLPPKNVDWGEIRGF
ETAYCIDSMGKTNGGFVELGPCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHC
NLNEFKEWQYFKNLHRFTHIPSGKCLDRSEVLHQVFISNCDSSKTTQKWEMNNIHSV
Enzyme 121 Number of Residues 657
Enzyme 121 Molecular Weight 75390
Enzyme 121 Theoretical pI 7.12
Enzyme 121 GO Classification Not Available
Enzyme 121 General Function Not Available
Enzyme 121 Specific Function Not Available
Enzyme 121 Pathways Not Available
Enzyme 121 Reactions Not Available
Enzyme 121 Pfam Domain Function
Enzyme 121 Signals
  • None
Enzyme 121 Transmembrane Regions
  • None
Enzyme 121 Essentiality Not Available
Enzyme 121 GenBank ID Protein Not Available
Enzyme 121 UniProtKB/Swiss-Prot ID B3KQU3 Link Image
Enzyme 121 UniProtKB/Swiss-Prot Entry Name B3KQU3_HUMAN Link Image
Enzyme 121 PDB ID Not Available
Enzyme 121 Cellular Location Not Available
Enzyme 121 Gene Sequence Not Available
Enzyme 121 GenBank Gene ID AK075488 Link Image
Enzyme 121 GeneCard ID B3KQU3 Link Image
Enzyme 121 GenAtlas ID Not Available
Enzyme 121 HGNC ID Not Available
Enzyme 121 Chromosome Location Not Available
Enzyme 121 Locus Not Available
Enzyme 121 SNPs SNPJam Report Link Image
Enzyme 121 General References Not Available
Enzyme 121 Metabolite References Not Available
Enzyme 122 [top]
Enzyme 122 ID 16551
Enzyme 122 Name cDNA FLJ42944 fis, clone BRSTN2004863, highly similar to PolypeptideN-acetylgalactosaminyltransferase 11 (EC 2.4.1.41)
Enzyme 122 Synonyms Not Available
Enzyme 122 Gene Name Not Available
Enzyme 122 Protein Sequence >cDNA FLJ42944 fis, clone BRSTN2004863, highly similar to PolypeptideN-acetylgalactosaminyltransferase 11 (EC 2.4.1.41)
MGSVTVRYFCYGCLFTSATWTVLLFVYFNFSEVTQPLKNVPVKGSGPHGPSPKKFYPRFT
RGPSRVLEPQFKANKIDDVIDSRVEDPEEGHLKLSSELGMIFNERDQELRDLGYQKHAFN
MLISDRLGYHRDVPDTRNAACKEKFYPPDLPAASVVICFYNEAFSALLRTVHSVIDRTPA
HLLHEIILVDDDSDFDDLKGELDEYVQKYLPGKIKVIRNTKREGLIRGRMIGAAHATGEV
LVFLDSHCEVNVMWLQPLLAAIREDRHTVVCPVIDIISADTLAYSSSPVVRGGFNWGLHF
KWDLVPLSELGRAEGATAPIKSPTMAGGLFAMNRQYFHELGQYDSGMDIWGGENLEISFR
IWMCGGKLFIIPCSRVGHIFRKRRPYGSPEGQDTMTHNSLRLAHVWLDEYKEQYFSLRPD
LKTKSYGNISERVELRKKLGCKSFKWYLDNVYPEMQISGSHAKPQQPIFVNRGPKRPKVL
QRGRLYHLQTNKCLVAQGRPSQKGGLVVLKACDYSDPNQIWIYNEEHELVLNSLLCLDMS
ETRSSDPPRLMKCHGSGGSQQWTFGKNNRLYQVSVGQCLRAVDPLGQKGSVAMAICDGSS
SQQWHLEG
Enzyme 122 Number of Residues 608
Enzyme 122 Molecular Weight 68884.3
Enzyme 122 Theoretical pI 8.27
Enzyme 122 GO Classification Not Available
Enzyme 122 General Function Involved in sugar binding
Enzyme 122 Specific Function Not Available
Enzyme 122 Pathways Not Available
Enzyme 122 Reactions Not Available
Enzyme 122 Pfam Domain Function
Enzyme 122 Signals
  • None
Enzyme 122 Transmembrane Regions
  • None
Enzyme 122 Essentiality Not Available
Enzyme 122 GenBank ID Protein 193784963 Link Image
Enzyme 122 UniProtKB/Swiss-Prot ID B3KWF4 Link Image
Enzyme 122 UniProtKB/Swiss-Prot Entry Name B3KWF4_HUMAN Link Image
Enzyme 122 PDB ID Not Available
Enzyme 122 Cellular Location Not Available
Enzyme 122 Gene Sequence >1827 bp
ATGGGAAGTGTCACAGTTCGGTATTTCTGTTATGGGTGCCTTTTTACATCTGCGACCTGG
ACAGTTTTGCTTTTTGTTTATTTCAACTTCAGTGAAGTGACTCAGCCACTTAAGAATGTG
CCCGTCAAGGGGTCTGGGCCCCACGGACCATCTCCAAAAAAATTCTATCCCCGTTTCACT
CGAGGCCCAAGTCGAGTGCTCGAGCCACAGTTCAAAGCAAACAAAATTGACGATGTGATA
GACAGTCGTGTTGAAGATCCAGAAGAAGGCCACTTGAAACTCTCTTCTGAATTAGGTATG
ATTTTTAATGAACGCGATCAAGAGTTGAGAGACTTGGGCTATCAGAAACATGCTTTTAAT
ATGCTTATCAGTGACCGCTTGGGCTACCACAGAGATGTGCCAGACACAAGGAATGCAGCA
TGTAAAGAAAAGTTCTACCCACCTGACCTGCCAGCTGCTAGTGTTGTTATCTGTTTCTAT
AATGAAGCGTTTTCTGCCTTGCTTCGGACAGTGCACAGTGTCATAGACCGCACGCCAGCA
CACCTGCTTCATGAGATCATCCTTGTGGATGATGATAGTGACTTTGATGATTTGAAAGGA
GAACTAGATGAATATGTCCAAAAATACCTCCCTGGAAAAATTAAAGTCATAAGAAATACA
AAGCGTGAGGGGTTGATTCGAGGGAGAATGATTGGCGCGGCCCACGCGACAGGAGAAGTC
CTTGTGTTCCTGGACAGCCACTGTGAAGTGAATGTGATGTGGCTGCAGCCCTTGCTGGCC
GCCATCCGTGAGGACCGGCACACCGTGGTGTGCCCAGTGATTGACATCATCAGCGCCGAC
ACGCTGGCCTACAGCTCGTCCCCTGTCGTCCGCGGAGGGTTCAACTGGGGACTGCACTTC
AAATGGGATCTTGTCCCCCTTTCTGAGCTAGGACGAGCGGAGGGAGCCACTGCACCAATA
AAGTCACCAACAATGGCTGGAGGTTTGTTTGCCATGAACAGACAGTATTTCCATGAACTT
GGACAGTATGATAGTGGCATGGATATCTGGGGAGGAGAAAATTTGGAAATATCATTTCGG
ATCTGGATGTGTGGCGGTAAGCTCTTCATCATCCCTTGCTCTAGAGTAGGACACATTTTC
CGAAAAAGGCGACCATATGGATCTCCCGAAGGCCAGGACACCATGACACACAACTCTTTG
CGGCTGGCACATGTCTGGTTGGATGAATACAAGGAGCAGTATTTTTCCTTAAGACCTGAC
CTGAAGACGAAAAGCTATGGCAATATCAGTGAGCGTGTGGAACTGAGAAAGAAGTTGGGC
TGTAAATCATTTAAATGGTATTTGGATAATGTATACCCAGAGATGCAGATATCTGGGTCC
CACGCCAAACCCCAACAACCCATTTTTGTCAATAGAGGGCCAAAACGACCCAAAGTCCTT
CAACGTGGAAGGCTCTATCACCTCCAGACCAACAAATGCCTGGTGGCCCAGGGCCGCCCA
AGTCAGAAGGGAGGTCTCGTGGTGCTTAAGGCCTGTGACTACAGTGACCCAAATCAGATC
TGGATCTATAATGAAGAGCATGAATTGGTTTTAAATAGTCTCCTTTGTCTAGATATGTCA
GAGACTCGCTCATCAGACCCGCCACGGCTCATGAAATGCCACGGGTCAGGAGGATCCCAG
CAGTGGACCTTTGGGAAAAACAATCGGCTATACCAGGTGTCGGTTGGACAGTGCCTGAGA
GCAGTGGATCCCCTGGGTCAGAAGGGCTCTGTCGCCATGGCGATCTGCGATGGCTCCTCT
TCACAGCAGTGGCATTTGGAAGGTTAA
Enzyme 122 GenBank Gene ID AK124934 Link Image
Enzyme 122 GeneCard ID Not Available
Enzyme 122 GenAtlas ID Not Available
Enzyme 122 HGNC ID HGNC:19875 Link Image
Enzyme 122 Chromosome Location Not Available
Enzyme 122 Locus Not Available
Enzyme 122 SNPs Not Available
Enzyme 122 General References Not Available
Enzyme 122 Metabolite References Not Available
Enzyme 123 [top]
Enzyme 123 ID 16552
Enzyme 123 Name cDNA FLJ46085 fis, clone TESTI2007490, highly similar to 2-hydroxyacylsphingosine1-beta-galactosyltransferase (EC 2.4.1.45)
Enzyme 123 Synonyms
  1. SubName: UDP glycosyltransferase 8 (UDP-galactose ceramide galactosyltransferase)
Enzyme 123 Gene Name UGT8
Enzyme 123 Protein Sequence >cDNA FLJ46085 fis, clone TESTI2007490, highly similar to 2-hydroxyacylsphingosine1-beta-galactosyltransferase (EC 2.4.1.45)
MKSYTPYFILLWSAVGIAKAAKIIIVPPIMFESHMYIFKTLASALHERGHHTVFLLSEGR
DIAPSNHYSLQRYPGIFNSTTSDAFLQSKMRNIFSGRLTAIELFDILDHYTKNCDLMVGN
HALIQGLKKEKFDLLLVDPNDMCGFVIAHLLGVKYAVFSTGLWYPAEVGAPAPLAYVPEF
NSLLTDRMNLLQRMKNTGVYLISRLGVSFLVLPKYERIMQKYNLLPEKSMYDLVHGSSLW
MLCTDVALEFPRPTLPNVVYVGGILTKPASPLPEDLQRWVNGANEHGFVLVSFGAGVKYL
SEDIANKLAGALGRLPQKVIWRFSGPKPKNLGNNTKLIEWLPQNDLLGHSKIKAFLSHGG
LNSIFETMYHGVPVVGIPLFGDHYDTMTRVQAKGMGILLEWKTVTEKELYEALVKVINNP
SYRQRAQKLSEIHKDQPGHPVNRTIYWIDYIIRHNGAHHLRAAVHQISFCQYFLLDIAFV
LLLGAALLYFLLSWVTKFIYRKIKSLWSRNKHSTVNGHYHNGILNGKYKRNGHIKHEKKV
K
Enzyme 123 Number of Residues 541
Enzyme 123 Molecular Weight 61457
Enzyme 123 Theoretical pI 9.97
Enzyme 123 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • metabolism
  • physiological process
Component
Enzyme 123 General Function Carbohydrate transport and metabolism
Enzyme 123 Specific Function Not Available
Enzyme 123 Pathways Not Available
Enzyme 123 Reactions
  • UDP-galactose + 2-(2-hydroxyacyl)sphingosine = UDP + 1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine [RN:R04322] ALL_REAC R04322
Enzyme 123 Pfam Domain Function
Enzyme 123 Signals
  • None
Enzyme 123 Transmembrane Regions
  • None
Enzyme 123 Essentiality Not Available
Enzyme 123 GenBank ID Protein Not Available
Enzyme 123 UniProtKB/Swiss-Prot ID B3KXU7 Link Image
Enzyme 123 UniProtKB/Swiss-Prot Entry Name B3KXU7_HUMAN Link Image
Enzyme 123 PDB ID Not Available
Enzyme 123 Cellular Location Not Available
Enzyme 123 Gene Sequence Not Available
Enzyme 123 GenBank Gene ID AK127970 Link Image
Enzyme 123 GeneCard ID B3KXU7 Link Image
Enzyme 123 GenAtlas ID Not Available
Enzyme 123 HGNC ID Not Available
Enzyme 123 Chromosome Location Not Available
Enzyme 123 Locus Not Available
Enzyme 123 SNPs SNPJam Report Link Image
Enzyme 123 General References Not Available
Enzyme 123 Metabolite References Not Available
Enzyme 124 [top]
Enzyme 124 ID 16553
Enzyme 124 Name cDNA FLJ90831 fis, clone Y79AA1001795, highly similar to Beta-1,3-galactosyltransferase 4 (EC 2.4.1.62)
Enzyme 124 Synonyms Not Available
Enzyme 124 Gene Name Not Available
Enzyme 124 Protein Sequence >cDNA FLJ90831 fis, clone Y79AA1001795, highly similar to Beta-1,3-galactosyltransferase 4 (EC 2.4.1.62)
MQLRLFRRLLLAALLLVIVWTLFGPSGLGEELLSLSLASLLPAPASPGPPLALPRLLIPN
QEACSGPGAPPFLLILVCTAPENLNQRNAIRASWGGLREARGLRVQTLFLLGEPNAQHPV
WGSQGSDLASESAAQGDILQAAFQDSYRNLTLKTLSGLNWAEKHCPMARYVLKTDDDVYV
NVPELVSELVLRGGRWGQWEGSTEPQREAEQEGGQVLHSEEVPLLYLGRVHWRVNPSRTP
GGRHRVSEEQWPHTWGPFPPYASGTGYVLSASAVQLILKVASRAPLLPLEDVFVGVSARR
GGLAPTQCVKLAGATHYPLDRCCYGKFLLTSHRLDPWKMQEAWKLVGGSDGERTAPFCSW
FQGVLGILRCRAIAWLQS
Enzyme 124 Number of Residues 378
Enzyme 124 Molecular Weight 41437.3
Enzyme 124 Theoretical pI 8.22
Enzyme 124 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • membrane
Enzyme 124 General Function Involved in galactosyltransferase activity
Enzyme 124 Specific Function Not Available
Enzyme 124 Pathways Not Available
Enzyme 124 Reactions Not Available
Enzyme 124 Pfam Domain Function
Enzyme 124 Signals
  • None
Enzyme 124 Transmembrane Regions
  • None
Enzyme 124 Essentiality Not Available
Enzyme 124 GenBank ID Protein 193786784 Link Image
Enzyme 124 UniProtKB/Swiss-Prot ID B3KQP5 Link Image
Enzyme 124 UniProtKB/Swiss-Prot Entry Name B3KQP5_HUMAN Link Image
Enzyme 124 PDB ID Not Available
Enzyme 124 Cellular Location Not Available
Enzyme 124 Gene Sequence >1137 bp
ATGCAGCTCAGGCTCTTCCGGCGCCTCCTTCTCGCCGCTTTGCTGCTGGTGATCGTCTGG
ACCCTCTTCGGGCCTTCGGGGTTGGGGGAGGAGCTGCTGAGCCTCTCACTAGCCTCCCTG
CTCCCAGCCCCCGCCTCACCGGGGCCGCCCCTGGCCCTGCCCCGCCTCTTGATCCCCAAC
CAGGAAGCTTGCAGTGGTCCCGGGGCCCCTCCCTTCCTGCTCATCCTGGTGTGCACGGCT
CCGGAGAACCTGAACCAGAGAAACGCCATTCGGGCTTCGTGGGGCGGGCTGCGCGAGGCC
CGGGGGCTCAGGGTACAGACGCTATTCTTGCTGGGAGAGCCGAACGCACAGCACCCCGTG
TGGGGTTCCCAGGGGAGTGACCTGGCCTCGGAGTCAGCAGCCCAGGGGGATATCTTGCAG
GCCGCCTTCCAGGACTCCTACCGCAACCTCACCCTAAAGACCCTCAGCGGGCTGAACTGG
GCTGAGAAACACTGCCCCATGGCCCGATACGTCCTCAAGACGGACGATGATGTGTATGTC
AACGTCCCTGAACTGGTATCAGAGCTGGTCTTGCGAGGGGGCCGTTGGGGGCAATGGGAG
GGAAGCACGGAACCCCAGAGAGAGGCTGAGCAGGAAGGAGGCCAGGTTTTGCACAGCGAG
GAAGTGCCTCTTCTGTACTTGGGCCGGGTGCACTGGCGCGTGAACCCCTCTCGGACACCG
GGGGGCAGGCACCGCGTATCAGAGGAGCAGTGGCCTCACACCTGGGGCCCCTTTCCACCC
TATGCCTCAGGCACGGGGTATGTGCTGTCAGCGTCTGCTGTGCAGCTCATTCTCAAGGTG
GCCAGCCGGGCACCCCTTCTCCCATTAGAGGATGTCTTTGTGGGGGTAAGTGCCCGACGA
GGAGGCCTCGCCCCAACACAGTGTGTCAAGCTGGCTGGTGCCACCCACTACCCGCTAGAC
CGGTGCTGCTATGGGAAATTCCTGCTGACGTCCCACAGGCTGGACCCCTGGAAGATGCAG
GAAGCCTGGAAGCTGGTGGGTGGCTCTGACGGGGAAAGGACTGCGCCCTTTTGCTCCTGG
TTCCAGGGAGTCCTGGGCATCCTGCGGTGTCGAGCAATAGCCTGGCTTCAGAGCTGA
Enzyme 124 GenBank Gene ID AK075312 Link Image
Enzyme 124 GeneCard ID Not Available
Enzyme 124 GenAtlas ID Not Available
Enzyme 124 HGNC ID HGNC:919 Link Image
Enzyme 124 Chromosome Location Not Available
Enzyme 124 Locus Not Available
Enzyme 124 SNPs Not Available
Enzyme 124 General References
  1. Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed Link Image]
Enzyme 124 Metabolite References Not Available
Enzyme 125 [top]
Enzyme 125 ID 16554
Enzyme 125 Name Chondroitin synthase-3 (Chondroitin sulfate glucuronyltransferase, isoform CRA_b)
Enzyme 125 Synonyms Not Available
Enzyme 125 Gene Name ChSy-3
Enzyme 125 Protein Sequence >Chondroitin synthase-3 (Chondroitin sulfate glucuronyltransferase, isoform CRA_b)
MRLSSLLALLRPALPLILGLSLGCSLSLLRVSWIQGEGEDPCVEAVGERGGPQNPDSRAR
LDQSDEDFKPRIVPYYRDPNKPYKKVLRTRYIQTELGSRERLLVAVLTSRATLSTLAVAV
NRTVAHHFPRLLYFTGQRGARAPAGMQVVSHGDERPAWLMSETLRHLHTHFGADYDWFFI
MQDDTYVQAPRLAALAGHLSINQDLYLGRAEEFIGAGEQARYCHGGFGYLLSRSLLLRLR
PHLDGCRGDILSARPDEWLGRCLIDSLGVGCVSQHQGQQYRSFELAKNRDPEKEGSSAFL
SAFAVHPVSEGTLMYRLHKRFSALELERAYSEIEQLQAQIRNLTVLTPEGEAGLSWPVGL
PAPFTPHSRFEVLGWDYFTEQHTFSCADGAPKCPLQGASRADVGDALETALEQLNRRYQP
RLRFQKQRLLNGYRRFDPARGMEYTLDLLLECVTQRGHRRALARRVSLLRPLSRVEILPM
PYVTEATRVQLVLPLLVAEAAAAPAFLEAFAANVLEPREHALLTLLLVYGPREGGRGAPD
PFLGVKAAAAELERRYPGTRLAWLAVRAEAPSQVRLMDVVSKKHPVDTLFFLTTVWTRPG
PEVLNRCRMNAISGWQAFFPVHFQEFNPALSPQRSPPGPPGAGPDPPSPPGADPSRGAPI
GGRFDRQASAEGCFYNADYLAARARLAGELAGQEEEEALEGLEVMDVFLRFSGLHLFRAV
EPGLVQKFSLRDCSPRLSEELYHRCRLSNLEGLGGRAQLAMALFEQEQANST
Enzyme 125 Number of Residues 772
Enzyme 125 Molecular Weight 85949
Enzyme 125 Theoretical pI 7.88
Enzyme 125 GO Classification Not Available
Enzyme 125 General Function Not Available
Enzyme 125 Specific Function Not Available
Enzyme 125 Pathways Not Available
Enzyme 125 Reactions Not Available
Enzyme 125 Pfam Domain Function
Enzyme 125 Signals
  • None
Enzyme 125 Transmembrane Regions
  • None
Enzyme 125 Essentiality Not Available
Enzyme 125 GenBank ID Protein Not Available
Enzyme 125 UniProtKB/Swiss-Prot ID B2DBD8 Link Image
Enzyme 125 UniProtKB/Swiss-Prot Entry Name B2DBD8_HUMAN Link Image
Enzyme 125 PDB ID Not Available
Enzyme 125 Cellular Location Not Available
Enzyme 125 Gene Sequence Not Available
Enzyme 125 GenBank Gene ID AB095812 Link Image
Enzyme 125 GeneCard ID B2DBD8 Link Image
Enzyme 125 GenAtlas ID Not Available
Enzyme 125 HGNC ID Not Available
Enzyme 125 Chromosome Location Not Available
Enzyme 125 Locus Not Available
Enzyme 125 SNPs SNPJam Report Link Image
Enzyme 125 General References Not Available
Enzyme 125 Metabolite References Not Available
Enzyme 126 [top]
Enzyme 126 ID 16555
Enzyme 126 Name cDNA, FLJ93377, Homo sapiens alpha 1,4-galactosyltransferase (A4GALT), mRNA (Alpha 1,4-galactosyltransferase) (Globotriaosylceramide synthase)
Enzyme 126 Synonyms Not Available
Enzyme 126 Gene Name A4GALT
Enzyme 126 Protein Sequence >cDNA, FLJ93377, Homo sapiens alpha 1,4-galactosyltransferase (A4GALT), mRNA (Alpha 1,4-galactosyltransferase) (Globotriaosylceramide synthase)
MSKPPDLLLRLLRGAPRQRVCTLFIIGFKFTFFVSIMIYWHVVGEPKEKGQLYNLPAEIP
CPTLTPPTPPSHGPTPGNIFFLETSDRTNPNFLFMCSVESAARTHPESHVLVLMKGLPGG
NASLPRHLGISLLSCFPNVQMLPLDLRELFRDTPLADWYAAVQGRWEPYLLPVLSDASRI
ALMWKFGGIYLDTDFIVLKNLRNLTNVLGTQSRYVLNGAFLAFERRHEFMALCMRDFVDH
YNGWIWGHQGPQLLTRVFKKWCSIRSLAESRACRGVTTLPPEAFYPIPWQDWKKYFEDIN
PEELPRLLSATYAVHVWNKKSQGTRFEATSRALLAQLHARYCPTTHEAMKMYL
Enzyme 126 Number of Residues 353
Enzyme 126 Molecular Weight 40500
Enzyme 126 Theoretical pI 9.18
Enzyme 126 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
Component
  • Golgi apparatus
  • Golgi stack
  • intracellular membrane-bound organelle
  • membrane-bound organelle
  • organelle
Enzyme 126 General Function Not Available
Enzyme 126 Specific Function Not Available
Enzyme 126 Pathways Not Available
Enzyme 126 Reactions Not Available
Enzyme 126 Pfam Domain Function
Enzyme 126 Signals
  • None
Enzyme 126 Transmembrane Regions
  • None
Enzyme 126 Essentiality Not Available
Enzyme 126 GenBank ID Protein Not Available
Enzyme 126 UniProtKB/Swiss-Prot ID B2R7C4 Link Image
Enzyme 126 UniProtKB/Swiss-Prot Entry Name B2R7C4_HUMAN Link Image
Enzyme 126 PDB ID Not Available
Enzyme 126 Cellular Location Not Available
Enzyme 126 Gene Sequence Not Available
Enzyme 126 GenBank Gene ID AK312927 Link Image
Enzyme 126 GeneCard ID B2R7C4 Link Image
Enzyme 126 GenAtlas ID Not Available
Enzyme 126 HGNC ID Not Available
Enzyme 126 Chromosome Location 22
Enzyme 126 Locus 22q11.2-q13.2
Enzyme 126 SNPs SNPJam Report Link Image
Enzyme 126 General References Not Available
Enzyme 126 Metabolite References Not Available
Enzyme 127 [top]
Enzyme 127 ID 21008
Enzyme 127 Name UDP-N-acetylglucosamine transferase subunit ALG13 homolog
Enzyme 127 Synonyms
  1. Asparagine-linked glycosylation 13 homolog
  2. Glycosyltransferase 28 domain-containing protein 1
Enzyme 127 Gene Name ALG13
Enzyme 127 Protein Sequence >UDP-N-acetylglucosamine transferase subunit ALG13 homolog
MKCVFVTVGTTSFDDLIACVSAPDSLQKIESLGYNRLILQIGRGTVVPEPFSTESFTLDV
YRYKDSLKEDIQKADLVISHAGAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEG
HLFYCTCRVLTCPGQAKSIASAPGKCQDSAALTSTAFSGLDFGLLSGYLHKQALVTATHP
TCTLLFPSCHAFFPLPLTPTLYKMHKGWKNYCSQKSLNEASMDEYLGSLGLFRKLTAKDA
SCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQ
LEIRALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLCYSSSGHYDSVYSKQFQSSAAV
CQAVLYEILYKDVFVVDEEELKTAIKLFRSGSKKNRNNAVTGSEDAHTDYKSSNQNRMEE
WGACYNAENIPEGYNKGTEETKSPENPSKMPFPYKVLKALDPEIYRNVEFDVWLDSRKEL
QKSDYMEYAGRQYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLA
NLKPVTQVMSVPAWNAMPSRKGRGYQKMPGGYVPEIVISEMDIKQQKKMFKKIRGKEVYM
TMAYGKGDPLLPPRLQHSMHYGHDPPMHYSQTAGNVMSNEHFHPQHPSPRQGRGYGMPRN
SSRFINRHNMPGPKVDFYPGPGKRCCQSYDNFSYRSRSFRRSHRQMSCVNKESQYGFTPG
NGQMPRGLEETITFYEVEEGDETAYPTLPNHGGPSTMVPATSGYCVGRRGHSSGKQTLNL
EEGNGQSENGRYHEEYLYRAEPDYETSGVYSTTASTANLSLQDRKSCSMSPQDTVTSYNY
PQKMMGNIAAVAASCANNVPAPVLSNGAAANQAISTTSVSSQNAIQPLFVSPPTHGRPVI
ASPSYPCHSAIPHAGASLPPPPPPPPPPPPPPPPPPPPPPPPPPPALDVGETSNLQPPPP
LPPPPYSCDPSGSDLPQDTKVLQYYFNLGLQCYYHSYWHSMVYVPQMQQQLHVENYPVYT
EPPLVDQTVPQCYSEVRREDGIQAEASANDTFPNADSSSVPHGAVYYPVMSDPYGQPPLP
GFDSCLPVVPDYSCVPPWHPVGTAYGGSSQIHGAINPGPIGCIAPSPPASHYVPQGM
Enzyme 127 Number of Residues 1137
Enzyme 127 Molecular Weight 126055.3
Enzyme 127 Theoretical pI 6.73
Enzyme 127 GO Classification
Function
  • binding
  • carbohydrate binding
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolic process
  • cellular lipid metabolic process
  • lipid glycosylation
  • lipid metabolic process
  • lipid modification
  • metabolic process
  • primary metabolic process
Component
Enzyme 127 General Function Involved in transferase activity, transferring hexosyl groups
Enzyme 127 Specific Function Isoform 2 may be involved in protein N-glycosylation, second step of the dolichol-linked oligosaccharide pathway
Enzyme 127 Pathways Not Available
Enzyme 127 Reactions
  • UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-diphosphodolichol = UDP + N,N'-diacetylchitobiosyl-diphosphodolichol [RN:R04494 R05970]
Enzyme 127 Pfam Domain Function
Enzyme 127 Signals
  • None
Enzyme 127 Transmembrane Regions
  • None
Enzyme 127 Essentiality Not Available
Enzyme 127 GenBank ID Protein 153791910 Link Image
Enzyme 127 UniProtKB/Swiss-Prot ID Q9NP73 Link Image
Enzyme 127 UniProtKB/Swiss-Prot Entry Name ALG13_HUMAN Link Image
Enzyme 127 PDB ID Not Available
Enzyme 127 Cellular Location Not Available
Enzyme 127 Gene Sequence >3414 bp
ATGAAGTGCGTGTTTGTTACCGTAGGGACCACCAGCTTTGACGACCTCATTGCGTGTGTG
TCGGCGCCCGACAGTCTGCAAAAAATCGAGAGCCTTGGTTACAACCGACTTATCCTGCAA
ATTGGTAGAGGAACGGTGGTACCTGAACCCTTCAGTACTGAGTCGTTTACTCTGGATGTT
TACAGGTACAAGGATTCCTTGAAAGAAGACATTCAGAAAGCAGATCTTGTTATTAGTCAC
GCAGGTGCAGGAAGCTGTTTGGAGACTCTGGAAAAAGGAAAGCCACTCGTAGTGGTTATA
AACGAAAAGTTGATGAACAATCATCAGCTGGAACTGGCAAAGCAGCTACACAAAGAGGGT
CATCTCTTCTATTGTACCTGCAGGGTCCTGACTTGTCCTGGGCAAGCCAAGTCCATTGCT
TCTGCTCCTGGGAAGTGCCAAGATTCTGCAGCGCTGACTTCAACTGCCTTTTCAGGCCTA
GACTTTGGGCTGCTTTCCGGATACCTGCATAAGCAAGCCCTTGTTACTGCTACCCATCCT
ACCTGCACCCTGCTTTTTCCCTCTTGCCACGCTTTTTTTCCTCTCCCTCTTACCCCCACC
CTGTACAAAATGCATAAAGGATGGAAAAACTACTGCAGCCAGAAGTCTTTGAATGAGGCA
TCAATGGATGAATATTTAGGCAGCTTAGGGCTGTTTCGAAAGCTGACTGCCAAGGATGCC
TCTTGCCTCTTTCGGGCCATTTCGGAGCAGTTGTTTTGCAGCCAGGTCCATCATTTGGAA
ATCAGGAAGGCTTGTGTCTCATATATGAGGGAAAATCAACAAACTTTTGAGTCTTATGTG
GAGGGATCTTTTGAGAAATACCTGGAACGGTTGGGAGATCCCAAGGAAAGTGCTGGCCAG
CTGGAAATAAGAGCTCTTTCTCTAATTTATAATCGGGATTTCATTCTTTATCGCTTTCCT
GGAAAACCTCCAACTTATGTCACAGATAATGGCTATGAAGACAAGATTCTACTCTGCTAC
TCAAGTAGTGGTCACTATGATTCTGTGTACTCAAAACAATTTCAGTCAAGTGCAGCTGTT
TGTCAGGCTGTATTGTACGAAATTCTCTATAAAGATGTGTTTGTTGTGGATGAAGAAGAG
TTGAAGACTGCGATTAAATTGTTTCGAAGTGGTTCTAAGAAGAACAGAAATAATGCTGTA
ACTGGAAGCGAGGATGCCCATACTGATTACAAGAGTTCAAATCAGAATAGGATGGAAGAG
TGGGGTGCCTGCTACAATGCTGAAAATATACCAGAGGGCTACAATAAAGGAACAGAAGAA
ACAAAGTCTCCAGAAAATCCATCAAAGATGCCCTTCCCCTATAAGGTGCTCAAAGCCCTG
GATCCAGAAATCTATCGTAATGTAGAATTTGATGTTTGGTTGGACAGCAGAAAAGAACTT
CAAAAATCTGATTACATGGAGTATGCTGGGAGACAGTACTATTTGGGAGACAAGTGTCAG
GTTTGCTTGGAATCAGAAGGAAGATATTATAATGCTCATATCCAGGAAGTTGGAAATGAG
AACAATTCAGTAACAGTCTTCATTGAAGAATTGGCGGAAAAGCATGTTGTTCCACTGGCT
AACTTAAAACCAGTTACCCAAGTGATGTCTGTTCCTGCCTGGAATGCTATGCCCAGTCGG
AAAGGAAGAGGTTACCAGAAAATGCCTGGGGGTTATGTCCCGGAAATAGTTATATCAGAG
ATGGACATAAAGCAACAGAAGAAGATGTTCAAGAAAATTCGAGGGAAAGAAGTTTACATG
ACTATGGCTTACGGCAAGGGAGACCCCCTCCTCCCACCCAGGCTGCAGCACAGTATGCAT
TATGGGCACGATCCTCCAATGCACTACTCACAGACAGCTGGCAATGTTATGTCTAATGAA
CATTTTCATCCTCAGCATCCATCTCCGAGACAAGGTCGGGGATATGGGATGCCCAGGAAT
TCATCTCGGTTTATAAACAGGCACAACATGCCGGGCCCTAAAGTTGATTTTTACCCAGGC
CCAGGTAAAAGGTGCTGCCAGAGCTATGATAACTTCTCTTATAGATCTCGTTCATTTAGA
CGTAGTCACCGCCAGATGAGTTGTGTGAATAAGGAGTCCCAGTATGGATTTACCCCAGGG
AATGGACAGATGCCCAGGGGCTTGGAAGAAACTATTACTTTTTATGAAGTTGAAGAAGGG
GATGAGACTGCTTATCCAACTTTACCTAATCATGGAGGTCCCTCTACAATGGTTCCTGCT
ACTTCAGGATACTGTGTTGGAAGGCGGGGACATAGCTCAGGCAAACAGACTTTGAATTTA
GAGGAGGGCAATGGCCAGAGTGAAAATGGGCGATATCATGAAGAATATCTTTATCGTGCA
GAGCCAGACTATGAAACTTCAGGTGTTTATAGCACAACTGCATCTACAGCAAACTTGTCT
CTTCAGGACAGAAAGTCATGTTCTATGTCTCCTCAGGACACAGTTACCTCATACAACTAC
CCCCAGAAGATGATGGGAAATATTGCAGCAGTTGCAGCTTCCTGTGCCAATAATGTTCCA
GCTCCAGTCTTATCTAACGGTGCAGCGGCTAATCAAGCTATTAGTACCACTTCAGTTTCC
TCACAGAATGCTATACAGCCTCTCTTTGTATCTCCACCTACACACGGCAGGCCAGTGATT
GCCTCACCATCCTATCCATGCCATTCTGCTATTCCTCATGCTGGTGCCTCTCTACCACCA
CCACCACCACCACCACCACCACCACCACCACCACCACCTCCTCCTCCTCCTCCTCCTCCT
CCTCCTCCTCCTCCTGCTCTTGATGTGGGAGAGACTTCAAACTTACAACCACCACCACCA
CTACCACCTCCACCTTATTCCTGTGATCCAAGCGGCAGTGATTTGCCTCAAGATACAAAA
GTTTTGCAGTACTATTTCAATCTAGGATTGCAGTGCTATTACCACAGCTACTGGCACTCC
ATGGTCTATGTGCCACAGATGCAGCAGCAGCTTCATGTAGAGAATTATCCAGTCTATACT
GAGCCACCTCTGGTAGATCAAACCGTTCCTCAATGCTACAGTGAGGTGAGGAGAGAAGAT
GGCATACAGGCGGAAGCATCAGCAAATGATACTTTTCCGAATGCTGATTCTTCATCTGTC
CCTCATGGAGCAGTCTATTATCCAGTAATGTCAGATCCCTATGGGCAGCCACCTTTGCCA
GGTTTTGACTCCTGCCTTCCGGTTGTGCCAGATTATTCCTGTGTTCCCCCCTGGCATCCA
GTTGGTACAGCATATGGTGGTTCTTCTCAAATTCATGGTGCTATAAATCCTGGGCCAATT
GGCTGTATTGCTCCATCTCCCCCAGCTTCTCATTATGTACCTCAGGGTATGTAA
Enzyme 127 GenBank Gene ID NM_001099922.2 Link Image
Enzyme 127 GeneCard ID ALG13 Link Image
Enzyme 127 GenAtlas ID ALG13 Link Image
Enzyme 127 HGNC ID HGNC:30881 Link Image
Enzyme 127 Chromosome Location Not Available
Enzyme 127 Locus Not Available
Enzyme 127 SNPs SNPJam Report Link Image
Enzyme 127 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  2. Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Gao XD, Tachikawa H, Sato T, Jigami Y, Dean N: Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation. J Biol Chem. 2005 Oct 28;280(43):36254-62. Epub 2005 Aug 12. [PubMed Link Image]
Enzyme 127 Metabolite References Not Available