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Human Metabolome Database Version 2.5

 

Showing metabocard for Uridine diphosphate-N-acetylglucosamine (HMDB00290)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-25 16:11:25
Accession Number HMDB00290
Secondary Accession Numbers Not Available
Common Name Uridine diphosphate-N-acetylglucosamine
Description Uridine 5'-diphosphate-GlcNAc (UDP-Glc-NAc )respond to nutrient excess to activate O-GlcNAcylation (addition of O-linked N-acetylglucosamine) in the hexosamine signaling pathway (HSP). O-GlcNAc addition (and removal) is key to histone remodeling, transcription, proliferation, apoptosis, and proteasomal degradation. This nutrient-responsive signaling pathway also modulates important cellular pathways, including the insulin signaling cascade in. Alterations in O-GlcNAc metabolism are associated with various human diseases including diabetes mellitus and neurodegeneration. (PMID: 16317114) The incidence of type 2 diabetes (non-insulin-dependent diabetes mellitus) has increased to epidemic proportions, being described as a disease of 'chronic overnutrition'. Due to the chemical makeup of UDP-GlcNAc,it is well positioned to serve as a glucose sensor in that it is a high-energy compound that requires and/or responds to glucose, amino acid, fatty acid and nucleotide metabolism for synthesis. UDP-Glc-NAc is the donor substrate for modification of nucleocytoplasmic proteins at serine and threonine residues with N-acetylglucosamine. Elevated levels of O-GlcNAc have an effect on insulin-stimulated glucose uptake. (PMID: 12678487)
Synonyms
  1. N-[2-[[[5-[(2,4-dioxo-1H-pyrimidin-1-yl)]-3,4-dihydroxy-tetrahydrofuran-2-yl]methoxy-hydroxy-phosphinoyl]oxy-hydroxy-phosphinoyl]oxy-4,5-dihydroxy-6-(hydroxymethyl)tetrahydropyran-3-yl]acetamide
  2. UDP-GlcNAc
  3. UDP-N-acetyl-D-glucosamine
  4. UDP-N-acetyl-glucosamine
  5. UDP-N-acetylglucosamine
  6. UDP-a-D-N-acetylglucosamine
  7. UDP-acetyl-D-glucosamine
  8. UDP-acetylglucosamine
  9. UPPAG
  10. Uridine 5'-diphospho-N-acetylglucosamine
  11. Uridine diphosphate N-acetyl-D-glucosamine
  12. Uridine diphosphate N-acetylglucosamine
  13. Uridine diphospho-2-acetamido-2-deoxy-D-glucose
  14. Uridine diphospho-N-acetyl-D-glucosamine
  15. Uridine diphospho-N-acetylglucosamine
  16. Uridine pyrophosphate 2-acetamido-2-deoxy-a-D-glucopyranosyl ester
  17. Uridine pyrophosphoacetylglucosamine
  18. [[3-acetylamino-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-hydroxy-phosphoryl]oxy-[[5-(2,4-dioxopyrimidin-1-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy]phosphinate
  19. [[3-acetylamino-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-hydroxy-phosphoryl]oxy-[[5-(2,4-dioxopyrimidin-1-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy]phosphinic acid
  20. uridine diphosphoacetylglucosamine
  21. Uridine 5'-Diphospho-N-Acetlyglucosamine
  22. UDP-N-acetyl-delta-glucosamine
  23. UDP-alpha-delta-N-acetylglucosamine
  24. UDP-acetyl-delta-glucosamine
  25. Uridine diphosphate N-acetyl-delta-glucosamine
  26. Uridine diphospho-2-acetamido-2-deoxy-delta-glucose
  27. Uridine diphospho-N-acetyl-delta-glucosamine
  28. Uridine pyrophosphate 2-acetamido-2-deoxy-alpha-delta-glucopyranosyl ester
  29. UDP-alpha-D-N-acetylglucosamine
  30. Uridine pyrophosphate 2-acetamido-2-deoxy-alpha-D-glucopyranosyl ester
Chemical IUPAC Name [[(2S,3R,4R,5S,6R)-3-acetamido-4,5-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy
Chemical Formula C17H27N3O17P2
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide diphosphates
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • secondary carboxylic acid amide
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Aminosugars metabolism
  • Component of Chondroitin / Heparan sulfate biosynthesis
  • Component of N-Glycan biosynthesis
  • Component of O-Glycan biosynthesis
Application
Source
  • Endogenous
Average Molecular Weight 607.354
Monoisotopic Molecular Weight 607.081543
Isomeric SMILES CC(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OP(O)(=O)OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=CC(=O)NC1=O
Canonical SMILES CC(=O)NC1C(O)C(O)C(CO)OC1OP(O)(=O)OP(O)(=O)OCC1OC(C(O)C1O)N1C=CC(=O)NC1=O
KEGG Compound ID C00043 Link Image
BioCyc ID UDP-N-ACETYL-D-GLUCOSAMINE Link Image
BiGG ID 33638 Link Image
Wikipedia Link UDP-N-acetylglucosamine Link Image
NuGOwiki Link HMDB00290 Link Image
Metagene Link HMDB00290 Link Image
METLIN ID 5281 Link Image
PubChem Compound 10705 Link Image
PubChem Substance 154007 Link Image
ChEBI ID 16264 Link Image
CAS Registry Number 528-04-1
InChI Identifier InChI=1/C17H27N3O17P2/c1-6(22)18-10-13(26)11(24)7(4-21)35-16(10)36-39(31,32)37-38(29,30)33-5-8-12(25)14(27)15(34-8)20-3-2-9(23)19-17(20)28/h2-3,7-8,10-16,21,24-27H,4-5H2,1H3,(H,18,22)(H,29,30)(H,31,32)(H,19,23,28)/t7-,8-,10-,11-,12-,13-,14-,15-,16-/m1/s1
Synthesis Reference Takenouchi, Kenji; Ishige, Kazuya; Midorikawa, Yuichiro; Okuyama, Kiyoshi; Hamamoto, Tomoki; Noguchi, Toshitada. Process for producing uridine diphosphate-N-acetylglucosamine. PCT Int. Appl. (1999), 38 pp.
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 11.4 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.41 [Predicted by ALOGPS]; -6.3 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Varian)
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 Not Available
Simplified TOCSY Spectrum Show Image
Show Peaklist
BMRB Spectrum Show Image
Show Peaklist
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • golgi apparatus
Biofluid Location Not Available
Tissue Location
Tissue References
Adipose Tissue
Liver
Muscle
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Amino Sugar Metabolism SMP00045 Link Image map00520 Link Image
General References
  1. Kobayashi T, Sleeman JE, Coughtrie MW, Burchell B: Molecular and functional characterization of microsomal UDP-glucuronic acid uptake by members of the nucleotide sugar transporter (NST) family. Biochem J. 2006 Dec 1;400(2):281-9. [PubMed Link Image]
  2. Kim CH: Increased expression of N-acetylglucosaminyltransferase-V in human hepatoma cells by retinoic acid and 1alpha,25-dihydroxyvitamin D3. Int J Biochem Cell Biol. 2004 Nov;36(11):2307-19. [PubMed Link Image]
  3. Jamieson JC, Kaplan HA, Woloski BM, Hellman M, Ham K: Glycoprotein biosynthesis during the acute-phase response to inflammation. Can J Biochem Cell Biol. 1983 Sep;61(9):1041-8. [PubMed Link Image]
  4. Wikipedia Link Image
Metabolic Enzymes
  1. Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
  2. Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
  3. UDP-N-acetylhexosamine pyrophosphorylase
  4. UDP-N-acetylglucosamine--dolichyl-phosphate N- acetylglucosaminephosphotransferase
  5. Hyaluronan synthase 1
  6. Exostosin-like 3
  7. Exostosin-2
  8. Exostosin-like 1
  9. N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase
  10. Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase V
  11. Hyaluronan synthase 3
  12. Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
  13. Hyaluronan synthase 2
  14. N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
  15. UDP-N-acetylglucosamine transporter
  16. Beta-1,3-N-acetylglucosaminyltransferase bGnT-2
  17. Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
  18. Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
  19. UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
  20. N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
  21. cDNA FLJ75238, highly similar to Homo sapiens asparagine-linked glycosylation 14 homolog (yeast) (ALG14), mRNA (Asparagine-linked glycosylation 14 homolog (Yeast), isoform CRA_b)
  22. cDNA FLJ78031, highly similar to Homo sapiens beta3GnT6 beta-1,3-N- acetylglucosaminyltransferase 6 (HCG2018639)
  23. UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (EC 5.1.3.14) (Glucosamine (UDP-N-acetyl)-2-epimerase/N- acetylmannosamine kinase, isoform CRA_a)
  24. cDNA, FLJ93080, highly similar to Homo sapiens UDP-N-acteylglucosamine pyrophosphorylase 1 (UAP1), mRNA (UDP-N-acteylglucosamine pyrophosphorylase 1, isoform CRA_a)
  25. Glycosyltransferase 28 domain containing 1, isoform CRA_b
  26. 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)
  27. cDNA, FLJ93340, Homo sapiens exostoses (multiple)-like 2 (EXTL2), mRNA (Exostoses (Multiple)-like 2, isoform CRA_a)
  28. cDNA, FLJ93616, highly similar to Homo sapiens exostoses (multiple) 1 (EXT1), mRNA (Exostoses (Multiple) 1)
Enzyme 1 [top]
Enzyme 1 ID 5568
Enzyme 1 Name Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Enzyme 1 Synonyms
  1. UDP-GlcNAc-2-epimerase/ManAc kinase[Includes: UDP-N- acetylglucosamine 2-epimerase
  2. Uridine diphosphate-N- acetylglucosamine-2-epimerase
  3. UDP-GlcNAc-2-epimerase
  4. N- acetylmannosamine kinase
  5. ManAc kinase]
Enzyme 1 Gene Name GNE
Enzyme 1 Protein Sequence >Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNTYRM
IEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALA
TSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILL
AGCPSYDKLLSAKNKDYMSIIRMWLGDDVKSKDYIVALQHPVTTDIKHSIKMFELTLDAL
ISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGN
SSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKI
YGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLR
VAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNP
REGIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTL
ITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREA
KKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTM
NPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASMVLDYTTRR
IY
Enzyme 1 Number of Residues 722
Enzyme 1 Molecular Weight 79276
Enzyme 1 Theoretical pI 6.79
Enzyme 1 GO Classification
Function
  • UDP-N-acetylglucosamine 2-epimerase activity
  • catalytic activity
  • isomerase activity
  • racemase and epimerase activity
  • racemase and epimerase activity, acting on carbohydrates and derivatives
Process
  • N-acetylglucosamine metabolism
  • UDP-N-acetylglucosamine metabolism
  • amine metabolism
  • amino sugar metabolism
  • carbohydrate biosynthesis
  • glucosamine metabolism
  • lipopolysaccharide biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • nitrogen compound metabolism
  • physiological process
  • polysaccharide biosynthesis
Component
Enzyme 1 General Function Cell wall/membrane/envelope biogenesis
Enzyme 1 Specific Function Regulates and initiates biosynthesis of N- acetylneuraminic acid (NeuAc), a precursor of sialic acids. Plays an essential role in early development. Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells
Enzyme 1 Pathways
Enzyme 1 Reactions
  • UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 4775362 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q9Y223 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name GLCNE_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >2169 bp
ATGGAGAAGAATGGAAATAACCGAAAGCTGCGGGTTTGTGTTGCTACTTGTAACCGTGCA
GATTATTCTAAACTTGCCCCGATCATGTTTGGCATTAAAACCGAACCTGAGTTCTTTGAA
CTTGATGTTGTGGTACTTGGCTCTCACCTGATAGATGACTATGGAAATACATATCGAATG
ATTGAACAAGATGACTTTGACATTAACACCAGGCTACACACAATTGTGAGGGGAGAAGAT
GAGGCAGCCATGGTGGAGTCAGTAGGCCTGGCCCTAGTGAAGCTGCCAGATGTCCTTAAT
CGCCTGAAGCCTGATATCATGATTGTTCATGGAGACAGGTTTGATGCCCTGGCTCTGGCC
ACATCTGCTGCCTTGATGAACATCCGAATCCTTCACATTGAAGGTGGGGAAGTCAGTGGG
ACCATTGATGACTCTATCAGACATGCCATAACAAAACTGGCTCATTATCATGTGTGCTGC
ACCCGCAGTGCAGAGCAGCACCTGATATCCATGTGTGAGGACCATGATCGCATCCTTTTG
GCAGGCTGCCCTTCCTATGACAAACTTCTCTCAGCCAAGAACAAAGACTACATGAGCATC
ATTCGCATGTGGCTAGGTGATGATGTAAAATCTAAAGATTACATTGTTGCACTACAGCAC
CCTGTGACCACTGACATTAAGCATTCCATAAAAATGTTTGAATTAACATTGGATGCACTT
ATCTCATTTAACAAGCGGACCCTAGTCCTGTTTCCAAATATTGACGCAGGGAGCAAAGAG
ATGGTTCGAGTGATGCGGAAGAAGGGCATTGAGCATCATCCCAACTTTCGTGCAGTTAAA
CACGTCCCATTTGACCAGTTTATACAGTTGGTTGCCCATGCTGGCTGTATGATTGGGAAC
AGCAGCTGTGGGGTTCGAGAAGTTGGAGCTTTTGGAACACCTGTGATCAACCTGGGAACA
CGTCAGATTGGAAGAGAAACAGGGGAGAATGTTCTTCATGTCCGGGATGCTGACACCCAA
GACAAAATATTGCAAGCACTGCACCTTCAGTTTGGTAAACAGTACCCTTGTTCAAAGATA
TATGGGGATGGAAATGCTGTTCCAAGGATTTTGAAGTTTCTCAAATCTATCGATCTTCAA
GAGCCACTGCAAAAGAAATTCTGCTTTCCTCCTGTGAAGGAGAATATCTCTCAAGATATT
GACCATATTCTTGAAACTCTAAGTGCCTTGGCCGTTGATCTTGGCGGGACGAACCTCCGA
GTTGCAATAGTCAGCATGAAGGGTGAAATAGTTAAGAAGTATACTCAGTTCAATCCTAAA
ACCTATGAAGAGAGGATTAATTTAATCCTACAGATGTGTGTGGAAGCTGCAGCAGAAGCT
GTAAAACTGAACTGCAGAATTTTGGGAGTAGGCATTTCCACAGGTGGCCGTGTAAATCCT
CGGGAAGGAATTGTGCTGCATTCAACCAAACTGATCCAAGAGTGGAACTCTGTGGACCTT
AGGACCCCCCTTTCTGACACTTTGCATCTCCCTGTGTGGGTAGACAATGATGGCAACTGT
GCTGCCCTGGCGGAAAGGAAATTTGGCCAAGGAAAGGGACTGGAAAACTTTGTTACACTT
ATCACAGGCACAGGAATCGGTGGTGGAATTATCCATCAGCATGAATTGATCCACGGAAGC
TCCTTCTGTGCTGCAGAACTGGGCCACCTTGTTGTGTCTCTGGATGGGCCTGATTGTTCC
TGTGGAAGCCATGGGTGCATTGAAGCATACGCCTCTGGAATGGCCTTGCAGAGGGAGGCA
AAAAAGCTCCATGATGAGGACCTGCTCTTGGTGGAAGGGATGTCAGTGCCAAAAGATGAG
GCTGTGGGTGCGCTCCATCTCATCCAAGCTGCGAAACTTGGCAATGCGAAGGCCCAGAGC
ATCCTAAGAACAGCTGGAACAGCTTTGGGTCTTGGGGTTGTGAACATCCTCCATACCATG
AATCCCTCCCTTGTGATCCTCTCCGGAGTCCTGGCCAGTCACTATATCCACATTGTCAAA
GACGTCATTCGCCAGCAGGCCTTGTCCTCCGTGCAGGACGTGGATGTGGTGGTTTCGGAT
TTGGTTGACCCCGCCCTGCTGGGTGCTGCCAGCATGGTTCTGGACTACACAACACGCAGG
ATCTACTAG
Enzyme 1 GenBank Gene ID AJ238764 Link Image
Enzyme 1 GeneCard ID GNE Link Image
Enzyme 1 GenAtlas ID GNE Link Image
Enzyme 1 HGNC ID HGNC:23657 Link Image
Enzyme 1 Chromosome Location 9
Enzyme 1 Locus 9p13.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Seppala R, Lehto VP, Gahl WA: Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the disease sialuria and the allosteric site of the enzyme. Am J Hum Genet. 1999 Jun;64(6):1563-9. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6229
Enzyme 2 Name Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
Enzyme 2 Synonyms
  1. GlcNAc-PI synthesis protein
  2. Phosphatidylinositol- glycan biosynthesis class A protein
  3. PIG-A
Enzyme 2 Gene Name PIGA
Enzyme 2 Protein Sequence >Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCL
IERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRE
RVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNH
IICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGI
DLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLV
QGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLE
KAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHC
GPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEI
SETR
Enzyme 2 Number of Residues 484
Enzyme 2 Molecular Weight 54127
Enzyme 2 Theoretical pI 8.41
Enzyme 2 GO Classification
Function
Process
  • biosynthesis
  • metabolism
  • physiological process
Component
Enzyme 2 General Function Cell wall/membrane/envelope biogenesis
Enzyme 2 Specific Function Necessary for the synthesis of N-acetylglucosaminyl- phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis
Enzyme 2 Pathways Not Available
Enzyme 2 Reactions
  • UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • 422-442
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 219994 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID P37287 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name PIGA_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 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 2 GenBank Gene ID D11466 Link Image
Enzyme 2 GeneCard ID PIGA Link Image
Enzyme 2 GenAtlas ID PIGA Link Image
Enzyme 2 HGNC ID HGNC:8957 Link Image
Enzyme 2 Chromosome Location X
Enzyme 2 Locus Xp22.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Miyata T, Takeda J, Iida Y, Yamada N, Inoue N, Takahashi M, Maeda K, Kitani T, Kinoshita T: The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis. Science. 1993 Feb 26;259(5099):1318-20. [PubMed Link Image]
  2. Bessler M, Hillmen P, Longo L, Luzzatto L, Mason PJ: Genomic organization of the X-linked gene (PIG-A) that is mutated in paroxysmal nocturnal haemoglobinuria and of a related autosomal pseudogene mapped to 12q21. Hum Mol Genet. 1994 May;3(5):751-7. [PubMed Link Image]
  3. Iida Y, Takeda J, Miyata T, Inoue N, Nishimura J, Kitani T, Maeda K, Kinoshita T: Characterization of genomic PIG-A gene: a gene for glycosylphosphatidylinositol-anchor biosynthesis and paroxysmal nocturnal hemoglobinuria. Blood. 1994 Jun 1;83(11):3126-31. [PubMed Link Image]
  4. Yu J, Nagarajan S, Ueda E, Knez JJ, Petersen RB, Medof ME: Characterization of alternatively spliced PIG-A transcripts in normal and paroxysmal nocturnal hemoglobinuria cells. Braz J Med Biol Res. 1994 Feb;27(2):195-201. [PubMed Link Image]
  5. Takeda J, Miyata T, Kawagoe K, Iida Y, Endo Y, Fujita T, Takahashi M, Kitani T, Kinoshita T: Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell. 1993 May 21;73(4):703-11. [PubMed Link Image]
  6. Bessler M, Mason PJ, Hillmen P, Miyata T, Yamada N, Takeda J, Luzzatto L, Kinoshita T: Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene. EMBO J. 1994 Jan 1;13(1):110-7. [PubMed Link Image]
  7. Ware RE, Rosse WF, Howard TA: Mutations within the Piga gene in patients with paroxysmal nocturnal hemoglobinuria. Blood. 1994 May 1;83(9):2418-22. [PubMed Link Image]
  8. Nafa K, Bessler M, Castro-Malaspina H, Jhanwar S, Luzzatto L: The spectrum of somatic mutations in the PIG-A gene in paroxysmal nocturnal hemoglobinuria includes large deletions and small duplications. Blood Cells Mol Dis. 1998 Sep;24(3):370-84. [PubMed Link Image]
  9. Yoon JH, Cho HI, Park SS, Chang YH, Kim BK: Mutation analysis of the PIG-A gene in Korean patients with paroxysmal nocturnal haemoglobinuria. J Clin Pathol. 2002 Jun;55(6):410-3. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6368
Enzyme 3 Name UDP-N-acetylhexosamine pyrophosphorylase
Enzyme 3 Synonyms
  1. Antigen X
  2. AGX
  3. Sperm- associated antigen 2[Includes: UDP-N-acetylgalactosamine pyrophosphorylase
  4. AGX-1
  5. UDP-N-acetylglucosamine pyrophosphorylase
  6. AGX-2]
Enzyme 3 Gene Name UAP1
Enzyme 3 Protein Sequence >UDP-N-acetylhexosamine pyrophosphorylase
MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSS
HQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAY
PKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTK
HKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDME
QRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQ
VVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPY
VDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTT
ARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRSATNGKSETITADVNHNLKDANDVPIQ
CEISPLISYAGEGLESYVADKEFHAPLIIDENGVHELVKNGI
Enzyme 3 Number of Residues 522
Enzyme 3 Molecular Weight 58770
Enzyme 3 Theoretical pI 6.29
Enzyme 3 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolism
  • physiological process
Component
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Converts UDP and GlcNAc-1-P into UDP-GlcNAc, and UDP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P
Enzyme 3 Pathways
Enzyme 3 Reactions
  • UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-D-glucosamine
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 7717462 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q16222 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name UAP1_HUMAN Link Image
Enzyme 3 PDB ID 1JVG Link Image
Enzyme 3 PDB File Show
Enzyme 3 3D Structure
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1518 bp
ATGAACATTAATGACCTCAAACTCACGTTGTCCAAAGCTGGGCAAGAGCACCTACTACGT
TTCTGGAATGAGCTTGAAGAAGCCCAACAGGTAGAACTTTATGCAGAGCTCCAGGCCATG
AACTTTGAGGAGCTGAACTTCTTTTTCCAAAAGGCCATTGAAGGTTTTAACCAGTCTTCT
CACCAAAAGAATGTGGATGCACGAATGGAACCTGTGCCTCGAGAGGTATTAGGCAGTGCT
ACAAGGGATCAAGATCAGCTCCAGGCCTGGGAAAGTGAAGGACTTTTCCAGATTTCTCAG
AATAAAGTAGCAGTTCTTCTTCTAGCTGGTGGGCAGGGGACAAGACTCGGCGTTGCATAT
CCTAAGGGGATGTATGATGTTGGTTTGCCATCCCGTAAGACACTTTTTCAGATTCAAGCA
GAGCGTATCCTGAAGCTACAGCAGGTTGCTGAAAAATATTATGGCAACAAATGCATTATT
CCATGGTATATAATGACCAGTGGCAGAACAATGGAATCTACAAAGGAGTTCTTCACCAAG
CACAAGTACTTTGGTTTAAAAAAAGAGAATGTAATCTTTTTTCAGCAAGGAATGCTCCCC
GCCATGAGTTTTGATGGGAAAATTATTTTGGAAGAGAAGAACAAAGTTTCTATGGCTCCA
GATGGGAATGGTGGTCTTTATCGGGCACTTGCAGCCCAGAATATTGTGGAGGATATGGAG
CAAAGAGGCATTTGGAGCATTCATGTCTATTGTGTTGACAACATATTAGTAAAAGTGGCA
GACCCACGGTTCATTGGATTTTGCATTCAGAAAGGAGCAGACTGTGGAGCAAAGGTGGTA
GAGAAAACGAACCCTACAGAACCAGTTGGAGTGGTTTGCCGAGTGGATGGAGTTTACCAG
GTGGTAGAATATAGTGAGATTTCCCTGGCAACAGCTCAAAAACGAAGCTCAGACGGACGA
CTGCTGTTCAATGCGGGGAACATTGCCAACCATTTCTTCACTGTACCATTTCTGAGAGAT
GTTGTCAATGTTTATGAACCTCAGTTGCAGCACCATGTGGCTCAAAAGAAGATTCCTTAT
GTGGATACCCAAGGACAGTTAATTAAGCCAGACAAACCCAATGGAATAAAGATGGAAAAA
TTTGTCTTTGACATCTTCCAGTTTGCAAAGAAGTTTGTGGTATATGAAGTATTGCGAGAA
GATGAGTTTTCCCCACTAAAGAATGCTGATAGTCAGAATGGGAAAGACAACCCTACTACT
GCAAGGCATGCTTTGATGTCCCTTCATCATTGCTGGGTCCTCAATGCAGGGGGCCATTTC
ATAGATGAAAATAGCTCTCGCCTTCCAGCAATTCCCCGCTTGAAGGATGCCAATGATGTA
CCAATCCAATGTGAAATCTCTCCTCTTATCTCCTATGCTGGAGAAGGATTAGAAAGTTAT
GTGGCAGATAAAGAATTCCATGCACCTCTAATCATCGATGAGAATGGAGTTCATGAGCTG
GTGAAAAATGGTATTTGA
Enzyme 3 GenBank Gene ID S73498 Link Image
Enzyme 3 GeneCard ID UAP1 Link Image
Enzyme 3 GenAtlas ID UAP1 Link Image
Enzyme 3 HGNC ID HGNC:12457 Link Image
Enzyme 3 Chromosome Location 1
Enzyme 3 Locus 1q23.3
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Diekman AB, Goldberg E: Characterization of a human antigen with sera from infertile patients. Biol Reprod. 1994 May;50(5):1087-93. [PubMed Link Image]
  2. Mio T, Yabe T, Arisawa M, Yamada-Okabe H: The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, protein expression, and catalytic mechanism. J Biol Chem. 1998 Jun 5;273(23):14392-7. [PubMed Link Image]
  3. Wang-Gillam A, Pastuszak I, Elbein AD: A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc. J Biol Chem. 1998 Oct 16;273(42):27055-7. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6385
Enzyme 4 Name UDP-N-acetylglucosamine--dolichyl-phosphate N- acetylglucosaminephosphotransferase
Enzyme 4 Synonyms
  1. GPT
  2. G1PT
  3. N- acetylglucosamine-1-phosphate transferase
  4. GlcNAc-1-P transferase
Enzyme 4 Gene Name DPAGT1
Enzyme 4 Protein Sequence >UDP-N-acetylglucosamine--dolichyl-phosphate N- acetylglucosaminephosphotransferase
MWAFSELPMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLNKTSRQQIPESQGV
ISGAVFLIILFCFIPFPFLNCFVKEQCKAFPHHEFVALIGALLAICCMIFLGFADDVLNL
RWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPKPFRPILGLHLDLGILYYVYMGLLAVFC
TNAINILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSLYFMIPFFFTTLGLLY
HNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCP
RHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQLVTVHQSETEDGEFTECNN
MTLINLLLKVLGPIHERNLTLLLLLLQILGSAITFSIRYQLVRLFYDV
Enzyme 4 Number of Residues 408
Enzyme 4 Molecular Weight 46091
Enzyme 4 Theoretical pI 8.07
Enzyme 4 GO Classification
Function
  • catalytic activity
Process
  • lipid metabolism
  • metabolism
  • physiological process
  • primary metabolism
Component
  • cell
  • membrane
Enzyme 4 General Function Cell wall/membrane/envelope biogenesis
Enzyme 4 Specific Function Catalyzes the initial step in the synthesis of dolichol- P-P-oligosaccharides
Enzyme 4 Pathways
Enzyme 4 Reactions
  • UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-D-glucosaminyl-diphosphodolichol
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-25
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 2239119 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q9H3H5 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name GPT_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1203 bp
ATGCCGCTGCTGATCAATTTGATCGTCTCGCTGCTGGGATTTGTGGCCACAGTCACCCTC
ATCCCGGCCTTCCTGGGCCACTTCATTGCTGCGCGCCTCTGTGGTCAGGACCTCAACAAA
ACCAGCCGACAGCAGATCCCAGAATCCCAGGGAGTGATCAGCGGTGCTGTTTTCCTTATC
ATCCTCTTCTGCTTCATCCCTTTCCCCTTCCTGAACTGCTTTGTGAAGGAGCAGTGTAAG
GCATTCCCCCACCATGAATTTGTGGCCCTGATAGGTGCCCTCCTTGCCATCTGCTGCATG
ATCTTCCTGGGCTTTGCGGATGATGTACTGAATCTGCGCTGGCGCCATAAGCTGCTGCTA
CCTACAGCTGCCTCACTACCTCTCCTCATGGTCTATTTCACCAACTTTGGCAACACGACC
ATTGTGGTGCCCAAGCCCTTCCGCCCGATACTTGGCCTGCATCTGGACTTGGGAATCCTG
TACTATGTCTACATGGGGCTGCTGGCAGTGTTCTGTACCAATGCCATCAATATCCTAGCA
GGAATTAACGGCCTAGAGGCTGGCCAGTCACTAGTCATTTCTGCTTCCATCATTGTCTTC
AACCTGGTAGAGTTGGAAGGTGATTGTCGGGATGATCATGTCTTTTCCCTCTACTTCATG
ATACCCTTTTTTTTCACCACTTTGGGATTGCTCTACCACAACTGGTACCCATCACGGGTG
TTTGTGGGAGATACCTTCTGTTACTTTGCTGGCATGACCTTTGCCGTGGTGGGCATCTTG
GGACACTTCAGCAAGACCATGCTACTATTCTTCATGCCCCAGGTGTTCAACTTCCTCTAC
TCACTGCCTCAGCTCCTGCATATCATCCCCTGCCCTCGCCACCGCATACCCAGACTCAAT
ATCAAGACAGGCAAACTGGAGATGAGCTATTCCAAGTTCAAGACCAAGAGCCTCTCTTTC
TTGGGCACCTTTATTTTAAAGGTGGCAGAGAGCCTCCAGCTGGTGACAGTACACCAGAGT
GAGACTGAAGATGGTGAATTCACTGAATGTAACAACATGACCCTCATCAACTTGCTACTT
AAAGTCCTTGGGCCCATACATGAGAGAAACCTCACATTGCTCCTGCTGCTGCTGCAGATC
CTGGGCAGTGCCATCACCTTCTCCATTCGATATCAGCTCGTTCGACTCTTCTATGATGTC
TGA
Enzyme 4 GenBank Gene ID Z82022 Link Image
Enzyme 4 GeneCard ID DPAGT1 Link Image
Enzyme 4 GenAtlas ID DPAGT1 Link Image
Enzyme 4 HGNC ID HGNC:2995 Link Image
Enzyme 4 Chromosome Location 11
Enzyme 4 Locus 11q23.3
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Eckert V, Blank M, Mazhari-Tabrizi R, Mumberg D, Funk M, Schwarz RT: Cloning and functional expression of the human GlcNAc-1-P transferase, the enzyme for the committed step of the dolichol cycle, by heterologous complementation in Saccharomyces cerevisiae. Glycobiology. 1998 Jan;8(1):77-85. [PubMed Link Image]
  2. Wu X, Rush JS, Karaoglu D, Krasnewich D, Lubinsky MS, Waechter CJ, Gilmore R, Freeze HH: Deficiency of UDP-GlcNAc:Dolichol Phosphate N-Acetylglucosamine-1 Phosphate Transferase (DPAGT1) causes a novel congenital disorder of Glycosylation Type Ij. Hum Mutat. 2003 Aug;22(2):144-50. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 7038
Enzyme 5 Name Hyaluronan synthase 1
Enzyme 5 Synonyms
  1. Hyaluronate synthase 1
  2. Hyaluronic acid synthase 1
  3. HA synthase 1
  4. HuHAS1
Enzyme 5 Gene Name HAS1
Enzyme 5 Protein Sequence >Hyaluronan synthase 1
MRQQDAPKPTPAARRCSGLARRVLTIAFALLILGLMTWAYAAGVPLASDRYGLLAFGLYG
AFLSAHLVAQSLFAYLEHRRVAAAARGPLDAATARSVALTISAYQEDPAYLRQCLASARA
LLYPRARLRVLMVVDGNRAEDLYMVDMFREVFADEDPATYVWDGNYHQPWEPAAAGAVGA
GAYREVEAEDPGRLAVEALVRTRRCVCVAQRWGGKREVMYTAFKALGDSVDYVQVCDSDT
RLDPMALLELVRVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFH
CVSCISGPLGLYRNNLLQQFLEAWYNQKFLGTHCTFGDDRHLTNRMLSMGYATKYTSRSR
CYSETPSSFLRWLSQQTRWSKSYFREWLYNALWWHRHHAWMTYEAVVSGLFPFFVAATVL
RLFYAGRPWALLWVLLCVQGVALAKAAFAAWLRGCLRMVLLSLYAPLYMCGLLPAKFLAL
VTMNQSGWGTSGRRKLAANYVPLLPLALWALLLLGGLVRSVAHEARADWSGPSRAAEAYH
LAAGAGAYVGYWVAMLTLYWVGVRRLCRRRTGGYRVQV
Enzyme 5 Number of Residues 578
Enzyme 5 Molecular Weight 64886
Enzyme 5 Theoretical pI 9.47
Enzyme 5 GO Classification Not Available
Enzyme 5 General Function Cell wall/membrane/envelope biogenesis
Enzyme 5 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 5 Pathways Not Available
Enzyme 5 Reactions
  • n UDP-N-acetyl-D-glucosamine + n UDP-D-glucuronate = [beta-N-acetyl-D-glucosaminyl(1-> 4)beta-D-glucuronosyl(1-> 3)]n+ 2n UDP
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 26-46 53-73 400-420 431-451 458-478 498-518 541-561
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 1556465 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q92839 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name HAS1_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1737 bp
ATGAGACAGCAGGACGCGCCCAAGCCCACTCCTGCAGCCCGCCGCTGCTCCGGCCTGGCC
CGGAGGGTGCTGACCATCGCCTTCGCCCTGCTCATCCTGGGCCTCATGACCTGGGCCTAC
GCCGCCGGGGTGCCGCTGGCCTCCGATCGCTACGGCCTCCTGGCCTTCGGCCTCTACGGG
GCCTTCCTTTCAGCGCACCTGGTGGCGCAGAGCCTCTTCGCGTACCTGGAGCACCGGCGG
GTGGCGGCGGCGGCGCGGGGGCCGCTGGATGCAGCCACCGCGCGCAGTGTGGCGCTGACC
ATCTCCGCCTACCAGGAGGACCCCGCGTACCTGCGCCAGTGCCTGGCGTCCGCCCGCGCC
CTGCTGTACCCGCGCGCGCGGCTGCGCGTCCTCATGGTGGTGGATGGCAACCGCGCCGAG
GACCTCTACATGGTCGACATGTTCCGCGAGGTCTTCGCTGACGAGGACCCCGCCACGTAC
GTGTGGGACGGCAACTACCACCAGCCCTGGGAACCCGCGGCGGCGGGCGCGGTGGGCGCC
GGAGCCTATCGGGAGGTGGAGGCGGAGGATCCTGGGCGGCTGGCAGTGGAGGCGCTGGTG
AGGACTCGCAGGTGCGTGTGCGTGGCGCAGCGCTGGGGCGGCAAGCGCGAGGTCATGTAC
ACAGCCTTCAAGGCGCTCGGAGATTCGGTGGACTACGTGCAGGTCTGTGACTCGGACACA
AGGTTGGACCCCATGGCACTGCTGGAGCTCGTGCGGGTACTGGACGAGGACCCCCGGGTA
GGGGCTGTTGGTGGGGACGTGCGGATCCTTAACCCTCTGGACTCCTGGGTCAGCTTCCTA
AGCAGCCTGCGATACTGGGTAGCCTTCAATGTGGAGCGGGCTTGTCAGAGCTACTTCCAC
TGTGTATCCTGCATCAGCGGTCCTCTAGGCCTATATAGGAATAACCTCTTGCAGCAGTTT
CTTGAGGCCTGGTACAACCAGAAGTTCCTGGGTACCCACTGTACTTTTGGGGATGACCGG
CACCTCACCAACCGCATGCTCAGCATGGGTTATGCTACCAAGTACACCTCCAGGTCCCGC
TGCTACTCAGAGACGCCCTCGTCCTTCCTGCGGTGGCTGAGCCAGCAGACACGCTGGTCC
AAGTCGTACTTCCGTGAGTGGCTGTACAACGCGCTCTGGTGGCACCGGCACCATGCGTGG
ATGACCTACGAGGCGGTGGTCTCCGGCCTGTTCCCCTTCTTCGTGGCGGCCACTGTGCTG
CGTCTGTTCTACGCGGGCCGCCCTTGGGCGCTGCTGTGGGTGCTGCTGTGCGTGCAGGGC
GTGGCACTGGCCAAGGCGGCCTTCGCGGCCTGGCTGCGGGGCTGCCTGCGCATGGTGCTT
CTCTCGCTCTACGCGCCCCTCTACATGTGTGGCCTCCTGCCTGCCAAGTTCCTGGCGCTA
GTCACCATGAACCAGAGTGGCTGGGGCACCTCGGGCCGGCGGAAGCTGGCCGCTAACTAC
GTCCCTCTGCTGCCCCTGGCGCTCTGGGCGCTGCTGCTGCTTGGGGGCCTGGTCCGCAGC
GTAGCACACGAGGCCAGGGCCGACTGGAGCGGCCCTTCCCGCGCAGCCGAGGCCTACCAC
TTGGCCGCGGGGGCCGGCGCCTACGTGGGCTACTGGGTGGCCATGTTGACGCTGTACTGG
GTGGGCGTGCGGAGGCTTTGCCGGCGGCGGACCGGGGGCTACCGCGTCCAGGTGTGA
Enzyme 5 GenBank Gene ID U59269 Link Image
Enzyme 5 GeneCard ID HAS1 Link Image
Enzyme 5 GenAtlas ID HAS1 Link Image
Enzyme 5 HGNC ID HGNC:4818 Link Image
Enzyme 5 Chromosome Location 19
Enzyme 5 Locus 19q13.4
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Shyjan AM, Heldin P, Butcher EC, Yoshino T, Briskin MJ: Functional cloning of the cDNA for a human hyaluronan synthase. J Biol Chem. 1996 Sep 20;271(38):23395-9. [PubMed Link Image]
  2. Itano N, Kimata K: Molecular cloning of human hyaluronan synthase. Biochem Biophys Res Commun. 1996 May 24;222(3):816-20. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 7039
Enzyme 6 Name Exostosin-like 3
Enzyme 6 Synonyms
  1. Glucuronyl-galactosyl-proteoglycan 4- alpha-N-acetylglucosaminyltransferase
  2. Putative tumor suppressor protein EXTL3
  3. Multiple exostosis-like protein 3
  4. Hereditary multiple exostoses gene isolog
  5. EXT-related protein 1
Enzyme 6 Gene Name EXTL3
Enzyme 6 Protein Sequence >Exostosin-like 3
MTGYTMLRNGGAGNGGQTCMLRWSNRIRLTWLSFTLFVILVFFPLIAHYYLTTLDEADEA
GKRIFGPRVGNELCEVKHVLDLCRIRESVSEELLQLEAKRQELNSEIAKLNLKIEACKKS
IENAKQDLLQLKNVISQTEHSYKELMAQNQPKLSLPIRLLPEKDDAGLPPPKATRGCRLH
NCFDYSRCPLTSGFPVYVYDSDQFVFGSYLDPLVKQAFQATARANVYVTENADIACLYVI
LVGEMQEPVVLRPAELEKQLYSLPHWRTDGHNHVIINLSRKSDTQNLLYNVSTGRAMVAQ
STFYTVQYRPGFDLVVSPLVHAMSEPNFMEIPPQVPVKRKYLFTFQGEKIESLRSSLQEA
RSFEEEMEGDPPADYDDRIIATLKAVQDSKLDQVLVEFTCKNQPKPSLPTEWALCGERED
RLELLKLSTFALIITPGDPRLVISSGCATRLFEALEVGAVPVVLGEQVQLPYQDMLQWNE
AALVVPKPRVTEVHFLLRSLSDSDLLAMRRQGRFLWETYFSTADSIFNTVLAMIRTRIQI
PAAPIREEAAAEIPHRSGKAAGTDPNMADNGDLDLGPVETEPPYASPRYLRNFTLTVTDF
YRSWNCAPGPFHLFPHTPFDPVLPSEAKFLGSGTGFRPIGGGAGGSGKEFQAALGGNVPR
EQFTVVMLTYEREEVLMNSLERLNGLPYLNKVVVVWNSPKLPSEDLLWPDIGVPIMVVRT
EKNSLNNRFLPWNEIETEAILSIDDDAHLRHDEIMFGFRVWREARDRIVGFPGRYHAWDI
PHQSWLYNSNYSCELSMVLTGAAFFHKYYAYLYSYVMPQAIRDMVDEYINCEDIAMNFLV
SHITRKPPIKVTSRWTFRCPGCPQALSHDDSHFHERHKCINFFVKVYGYMPLLYTQFRVD
SVLFKTRLPHDKTKCFKFI
Enzyme 6 Number of Residues 919
Enzyme 6 Molecular Weight 104750
Enzyme 6 Theoretical pI 6.48
Enzyme 6 GO Classification
Function
Process
Component
  • cell
  • membrane
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Probable glycosyltransferase
Enzyme 6 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 6 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
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 31-51
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 2897905 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID O43909 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name EXTL3_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >2760 bp
ATGACAGGCTATACCATGCTGCGGAATGGGGGCGCGGGGAACGGAGGTCAGACCTGCATG
CTGCGCTGGTCCAACCGCATCCGCCTCACGTGGCTCAGCTTCACGCTCTTTGTCATCCTG
GTCTTCTTCCCGCTCATCGCCCACTATTACCTCACCACTCTGGATGAGGCTGATGAGGCA
GGCAAGCGGATTTTTGGTCCCCGGGTGGGGAACGAGCTGTGCGAGGTGAAGCACGTGCTG
GATCTGTGCCGCATCCGGGAGTCGGTGAGTGAAGAGCTCCTGCAGCTGGAGGCCAAGCGC
CAAGAGCTGAACAGCGAGATCGCCAAGCTGAATCTGAAGATCGAAGCCTGTAAGAAGAGC
ATTGAGAACGCCAAGCAGGACCTGCTCCAGCTCAAGAATGTCATCAGCCAGACCGAGCAT
TCCTACAAGGAGCTCATGGCCCAGAACCAGCCCAAGCTGTCCCTGCCCATCCGACTGCTC
CCAGAGAAGGACGATGCCGGCCTCCCTCCCCCGAAGGCCACTCGGGGCTGCCGGCTACAC
AACTGCTTTGATTATTCTCGTTGCCCTCTCACCTCTGGCTTCCCGGTCTACGTCTATGAC
AGTGACCAGTTTGTCTTTGGCAGCTACCTGGATCCCTTGGTCAAGCAGGCTTTTCAGGCG
ACAGCACGAGCTAACGTTTATGTTACAGAAAATGCAGACATCGCCTGCCTTTACGTGATA
CTAGTGGGAGAGATGCAGGAGCCGGTGGTGCTGCGGCCTGCTGAGCTGGAGAAGCAGTTG
TATTCCCTGCCACACTGGCGGACGGATGGACACAACCATGTCATCATCAATCTGTCACGT
AAGTCAGATACACAGAACCTTCTCTATAACGTCAGTACTGGCCGTGCCATGGTGGCCCAG
TCCACCTTCTACACTGTCCAGTACAGACCTGGCTTTGACTTGGTCGTATCACCGCTGGTC
CATGCCATGTCTGAGCCCAACTTCATGGAAATCCCACCACAGGTGCCGGTGAAGCGGAAA
TATCTCTTCACCTTCCAGGGCGAGAAGATTGAGTCTCTGAGGTCTAGCCTTCAGGAGGCC
CGCTCCTTCGAAGAGGAAATGGAGGGCGACCCTCCCGCCGACTACGATGACCGGATCATT
GCCACCCTGAAGGCGGTGCAGGACAGCAAGCTGGATCAGGTCCTGGTGGAATTCACCTGC
AAAAACCAGCCCAAACCCAGCCTGCCGACTGAGTGGGCACTGTGTGGAGAGCGGGAGGAC
CGCTTGGAATTGCTGAAGCTCTCCACCTTCGCCCTCATCATTACCCCCGGGGACCCTCGC
TTGGTTATTTCCTCTGGGTGTGCAACACGGCTCTTCGAAGCCCTGGAAGTCGGTGCCGTC
CCGGTGGTGCTGGGGGAGCAGGTCCAGCTTCCCTACCAGGACATGCTGCAGTGGAACGAG
GCGGCCCTGGTGGTGCCAAAGCCTCGTGTTACCGAGGTTCATTTCCTGCTCAGAAGCCTC
TCCGATAGTGACCTCCTGGCTATGAGGCGGCAAGGCCGCTTTCTCTGGGAGACTTACTTC
TCCACTGCTGACAGTATTTTTAATACCGTGCTGGCTATGATTAGGACTCGCATCCAGATC
CCAGCCGCTCCCATCCGGGAAGAGGCGGCAGCTGAGATCCCCCACCGTTCAGGCAAGGCG
GCTGGAACTGACCCCAACATGGCTGACAACGGGGACCTGGACCTGGGGCCAGTGGAGACG
GAGCCGCCCTACGCCTCACCCAGATACCTCCGCAATTTCACTCTGACTGTCACTGACTTT
TACCGCAGCTGGAACTGTGCTCCAGGGCCTTTCCATCTTTTCCCCCACACTCCCTTTGAC
CCTGTGTTGCCCTCAGAGGCCAAATTCTTGGGCTCAGGGACTGGCTTTCGGCCTATTGGT
GGTGGAGCTGGGGGTTCTGGCAAGGAATTTCAGGCAGCGCTTGGAGGCAATGTTCCCCGA
GAGCAGTTCACGGTGGTGATGTTGACTTATGAGCGGGAGGAAGTGCTTATGAACTCTTTA
GAGAGGCTGAATGGCCTCCCTTACCTGAACAAGGTCGTGGTGGTGTGGAATTCTCCCAAG
CTGCCATCAGAGGACCTTCTGTGGCCTGACATTGGCGTCCCCATCATGGTGGTCCGTACT
GAGAAGAACAGTTTGAACAACCGATTCTTACCCTGGAATGAAATTGAGACAGAGGCCATC
CTGTCCATTGATGACGATGCTCACCTCCGCCATGACGAAATCATGTTTGGGTTCCGGGTG
TGGAGAGAAGCTCGGGACCGCATCGTGGGCTTCCCTGGCCGTTACCACGCATGGGACATC
CCCCATCAGTCCTGGCTCTACAACTCCAACTACTCCTGTGAGCTGTCCATGGTGCTGACA
GGTGCTGCCTTCTTTCACAAGTATTATGCCTACCTGTATTCTTATGTGATGCCCCAGGCC
ATCCGGGACATGGTGGATGAATACATCAACTGTGAGGACATTGCCATGAACTTCCTTGTC
TCCCACATCACTCGGAAGCCCCCCATCAAGGTGACCTCACGGTGGACATTCCGATGCCCA
GGATGCCCTCAGGCCCTGTCTCATGATGACTCCCACTTCCACGAGCGGCACAAGTGCATC
AACTTCTTCGTGAAGGTGTACGGCTACATGCCCCTCCTGTACACGCAGTTCAGGGTGGAT
TCTGTGCTCTTCAAGACACGCCTGCCCCATGACAAGACCAAGTGCTTCAAGTTCATCTAG
Enzyme 6 GenBank Gene ID AF001690 Link Image
Enzyme 6 GeneCard ID EXTL3 Link Image
Enzyme 6 GenAtlas ID EXTL3 Link Image
Enzyme 6 HGNC ID HGNC:3518 Link Image
Enzyme 6 Chromosome Location 8
Enzyme 6 Locus 8p21
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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. 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 7040
Enzyme 7 Name Exostosin-2
Enzyme 7 Synonyms
  1. Glucuronosyl-N- acetylglucosaminyl-proteoglycan/N-acetylglucosaminyl-proteoglycan 4- alpha-N-acetylglucosaminyltransferase
  2. Putative tumor suppressor protein EXT2
  3. Multiple exostoses protein 2
Enzyme 7 Gene Name EXT2
Enzyme 7 Protein Sequence >Exostosin-2
MCASVKYNIRGPALIPRMKTKHRIYYITLFSIVLLGLIATGMFQFWPHSIESSNDWNVEK
RSIRDVPVVRLPADSPIPERGDLSCRMHTCFDVYRCGFNPKNKIKVYIYALKKYVDDFGV
SVSNTISREYNELLMAISDSDYYTDDINRACLFVPSIDVLNQNTLRIKETAQAMAQLSRW
DRGTNHLLFNMLPGGPPDYNTALDVPRDRALLAGGGFSTWTYRQGYDVSIPVYSPLSAEV
DLPEKGPGPRQYFLLSSQVGLHPEYREDLEALQVKHGESVLVLDKCTNLSEGVLSVRKRC
HKHQVFDYPQVLQEATFCVVLRGARLGQAVLSDVLQAGCVPVVIADSYILPFSEVLDWKR
ASVVVPEEKMSDVYSILQSIPQRQIEEMQRQARWFWEAYFQSIKAIALATLQIINDRIYP
YAAISYEEWNDPPAVKWGSVSNPLFLPLIPPQSQGFTAIVLTYDRVESLFRVITEVSKVP
SLSKLLVVWNNQNKNPPEDSLWPKIRVPLKVVRTAENKLSNRFFPYDEIETEAVLAIDDD
IIMLTSDELQFGYEVWREFPDRLVGYPGRLHLWDHEMNKWKYESEWTNEVSMVLTGAAFY
HKYFNYLYTYKMPGDIKNWVDAHMNCEDIAMNFLVANVTGKAVIKVTPRKKFKCPECTAI
DGLSLDQTHMVERSECINKFASVFGTMPLKVVEHRADPVLYKDDFPEKLKSFPNIGSL
Enzyme 7 Number of Residues 718
Enzyme 7 Molecular Weight 82255
Enzyme 7 Theoretical pI 6.51
Enzyme 7 GO Classification
Function
Process
Component
  • cell
  • membrane
Enzyme 7 General Function Not Available
Enzyme 7 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 7 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 7 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
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • 1-39
Enzyme 7 Transmembrane Regions Not Available
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 1518042 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q93063 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name EXT2_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID U62740 Link Image
Enzyme 7 GeneCard ID EXT2 Link Image
Enzyme 7 GenAtlas ID EXT2 Link Image
Enzyme 7 HGNC ID HGNC:3513 Link Image
Enzyme 7 Chromosome Location 11
Enzyme 7 Locus 11p12-p11
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 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. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 7041
Enzyme 8 Name Exostosin-like 1
Enzyme 8 Synonyms
  1. Glucuronosyl-N-acetylglucosaminyl- proteoglycan 4-alpha-N-acetylglucosaminyltransferase
  2. Exostosin-L
  3. Multiple exostosis-like protein
Enzyme 8 Gene Name EXTL1
Enzyme 8 Protein Sequence >Exostosin-like 1
MQSWRRRKSLWLALSASWLLLVLLGGFSLLRLALPPRPRPGASQGWPRWLDAELLQSFSQ
PGELPEDAVSPPQAPHGGSCNWESCFDTSKCRGDGLKVFVYPAVGTISETHRRILASIEG
SRFYTFSPAGACLLLLLSLDAQTGECSSMPLQWNRGRNHLVLRLHPAPCPRTFQLGQAMV
AEASPTVDSFRPGFDVALPFLPEAHPLRGGAPGQLRQHSPQPGVALLALEEERGGWRTAD
TGSSACPWDGRCEQDPGPGQTQRQETLPNATFCLISGHRPEAASRFLQALQAGCIPVLLS
PRWELPFSEVIDWTKAAIVADERLPLQVLAALQEMSPARVLALRQQTQFLWDAYFSSVEK
VIHTTLEVIQDRIFGTSAHPSLLWNSPPGALLALSTFSTSPQDFPFYYLQQGSRPEGRFS
ALIWVGPPGQPPLKLIQAVAGSQHCAQILVLWSNERPLPSRWPETAVPLTVIDGHRKVSD
RFYPYSTIRTDAILSLDARSSLSTSEVDFAFLVWQSFPERMVGFLTSSHFWDEAHGGWGY
TAERTNEFSMVLTTAAFYHRYYHTLFTHSLPKALRTLADEAPTCVDVLMNFIVAAVTKLP
PIKVPYGKQRQEAAPLAPGGPGPRPKPPAPAPDCINQIAAAFGHMPLLSSRLRLDPVLFK
DPVSVQRKKYRSLEKP
Enzyme 8 Number of Residues 676
Enzyme 8 Molecular Weight 74697
Enzyme 8 Theoretical pI 8.26
Enzyme 8 GO Classification
Function
Process
Component
  • cell
  • membrane
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Probable glycosyltransferase
Enzyme 8 Pathways
  • Chondroitin / Heparan sulfate biosynthesis (map00532 Link Image)
Enzyme 8 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
Enzyme 8 Pfam Domain Function
Enzyme 8 Signals
  • 1-33
Enzyme 8 Transmembrane Regions Not Available
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 1524413 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q92935 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name EXTL1_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 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 8 GenBank Gene ID U67191 Link Image
Enzyme 8 GeneCard ID EXTL1 Link Image
Enzyme 8 GenAtlas ID EXTL1 Link Image
Enzyme 8 HGNC ID HGNC:3515 Link Image
Enzyme 8 Chromosome Location 1
Enzyme 8 Locus 1p36.1
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 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]
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 7042
Enzyme 9 Name N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase
Enzyme 9 Synonyms
  1. Poly-N-acetyllactosamine extension enzyme
  2. I-beta- 1,3-N-acetylglucosaminyltransferase
  3. iGnT
  4. UDP-GlcNAc:betaGal beta- 1,3-N-acetylglucosaminyltransferase 1
Enzyme 9 Gene Name B3GNT1
Enzyme 9 Protein Sequence >N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase
MQMSYAIRCAFYQLLLAALMLVAMLQLLYLSLLSGLHGQEEQDQYFEFFPPSPRSVDQVK
AQLRTALASGGVLDASGDYRVYRGLLKTTMDPNDVILATHASVDNLLHLSGLLERWEGPL
SVSVFAATKEEAQLATVLAYALSSHCPDMRARVAMHLVCPSRYEAAVPDPREPGEFALLR
SCQEVFDKLARVAQPGINYALGTNVSYPNNLLRNLAREGANYALVIDVDMVPSEGLWRGL
REMLDQSNQWGGTALVVPAFEIRRARRMPMNKNELVQLYQVGEVRPFYYGLCTPCQAPTN
YSRWVNLPEESLLRPAYVVPWQDPWEPFYVAGGKVPTFDERFRQYGFNRISQACELHVAG
FDFEVLNEGFLVHKGFKEALKFHPQKEAENQHNKILYRQFKQELKAKYPNSPRRC
Enzyme 9 Number of Residues 415
Enzyme 9 Molecular Weight 47120
Enzyme 9 Theoretical pI 7.22
Enzyme 9 GO Classification Not Available
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Can initiate the synthesis or the elongation of the linear poly-N-acetyllactosaminoglycans
Enzyme 9 Pathways
  • Blood group glycolipid biosynthesis-neolactoseries (map00602 Link Image)
  • Keratan sulfate biosynthesis (map00533 Link Image)
Enzyme 9 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
Enzyme 9 Pfam Domain Function Not Available
Enzyme 9 Signals
  • 1-38
Enzyme 9 Transmembrane Regions Not Available
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 2745741 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID O43505 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name B3GN1_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 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 9 GenBank Gene ID AF029893 Link Image
Enzyme 9 GeneCard ID B3GNT1 Link Image
Enzyme 9 GenAtlas ID B3GNT1 Link Image
Enzyme 9 HGNC ID HGNC:15685 Link Image
Enzyme 9 Chromosome Location 11
Enzyme 9 Locus 11q13.1
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 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]
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 7043
Enzyme 10 Name Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase V
Enzyme 10 Synonyms
  1. Mannoside acetylglucosaminyltransferase 5
  2. Alpha- mannoside beta-1,6-N-acetylglucosaminyltransferase
  3. N- acetylglucosaminyl-transferase V
  4. GNT-V
  5. GlcNAc-T V
Enzyme 10 Gene Name MGAT5
Enzyme 10 Protein Sequence >Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase V
MALFTPWKLSSQKLGFFLVTFGFIWGMMLLHFTIQQRTQPESSSMLREQILDLSKRYIKA
LAEENRNVVDGPYAGVMTAYDLKKTLAVLLDNILQRIGKLESKVDNLVVNGTGTNSTNST
TAVPSLVALEKINVADIINGAQEKCVLPPMDGYPHCEGKIKWMKDMWRSDPCYADYGVDG
STCSFFIYLSEVENWCPHLPWRAKNPYEEADHNSLAEIRTDFNILYSMMKKHEEFRWMRL
RIRRMADAWIQAIKSLAEKQNLEKRKRKKVLVHLGLLTKESGFKIAETAFSGGPLGELVQ
WSDLITSLYLLGHDIRISASLAELKEIMKKVVGNRSGCPTVGDRIVELIYIDIVGLAQFK
KTLGPSWVHYQCMLRVLDSFGTEPEFNHANYAQSKGHKTPWGKWNLNPQQFYTMFPHTPD
NSFLGFVVEQHLNSSDIHHINEIKRQNQSLVYGKVDSFWKNKKIYLDIIHTYMEVHATVY
GSSTKNIPSYVKNHGILSGRDLQFLLRETKLFVGLGFPYEGPAPLEAIANGCAFLNPKFN
PPKSSKNTDFFIGKPTLRELTSQHPYAEVFIGRPHVWTVDLNNQEEVEDAVKAILNQKIE
PYMPYEFTCEGMLQRINAFIEKQDFCHGQVMWPPLSALQVKLAEPGQSCKQVCQESQLIC
EPSFFQHLNKDKDMLKYKVTCQSSELAKDILVPSFDPKNKHCVFQGDLLLFSCAGAHPRH
QRVCPCRDFIKGQVALCKDCL
Enzyme 10 Number of Residues 741
Enzyme 10 Molecular Weight 84544
Enzyme 10 Theoretical pI 8.21
Enzyme 10 GO Classification Not Available
Enzyme 10 General Function Not Available
Enzyme 10 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 10 Pathways
Enzyme 10 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
Enzyme 10 Pfam Domain Function Not Available
Enzyme 10 Signals
  • 1-26
Enzyme 10 Transmembrane Regions Not Available
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein 870752 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID Q09328 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name MGAT5_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >2226 bp
ATGGCTCTCTTCACTCCGTGGAAGTTGTCCTCTCAGAAGCTGGGCTTTTTCCTGGTGACT
TTTGGCTTCATTTGGGGTATGATGCTTCTGCACTTTACCATCCAGCAGCGAACTCAGCCT
GAAAGCAGCTCCATGCTGCGCGAGCAGATCCTGGACCTCAGCAAAAGGTACATCAAGGCA
CTGGCAGAAGAAAACAGGAATGTGGTGGATGGGCCATACGCTGGAGTCATGACAGCTTAT
GATCTGAAGAAAACCCTTGCTGTGTTATTAGATAACATTTTGCAGCGCATTGGCAAGTTG
GAGTCGAAGGTGGACAATCTTGTTGTCAATGGCACCGGAACAAACTCAACCAACTCCACT
ACAGCTGTTCCCAGCTTGGTTGCACTTGAGAAAATTAATGTGGCAGATATCATTAACGGA
GCTCAAGAAAAATGTGTATTGCCTCCTATGGACGGCTACCCTCACTGTGAGGGAAAGATC
AAGTGGATGAAAGACATGTGGCGTTCAGATCCCTGCTACGCAGACTATGGAGTGGATGGA
TCCACCTGCTCTTTTTTTATTTACCTCAGTGAGGTTGAAAATTGGTGTCCTCATTTACCT
TGGAGAGCAAAAAATCCCTACGAAGAAGCTGATCATAATTCATTGGCGGAAATTCGTACA
GATTTTAATATTCTCTACAGTATGATGAAAAAGCATGAAGAATTCCGGTGGATGAGACTA
CGGATCCGGCGAATGGCTGACGCATGGATCCAAGCAATCAAGTCCCTGGCAGAAAAGCAG
AACCTTGAAAAGAGAAAGCGGAAGAAAGTCCTCGTTCACCTGGGACTCCTGACCAAGGAA
TCTGGATTTAAGATTGCAGAGACAGCTTTCAGTGGTGGCCCTCTTGGTGAATTAGTTCAA
TGGAGTGATTTAATTACATCTCTGTACTTACTGGGCCATGACATTAGGATTTCAGCTTCA
CTGGCTGAGCTCAAGGAAATCATGAAGAAGGTTGTAGGAAACCGATCTGGCTGCCCAACT
GTAGGAGACAGAATTGTTGAGCTCATTTACATTGATATTGTAGGACTTGCTCAATTCAAG
AAAACTCTTGGACCATCCTGGGTTCATTACCAGTGCATGCTCCGAGTCCTTGATTCATTT
GGTACTGAACCCGAATTTAATCATGCAAATTATGCCCAATCGAAAGGCCACAAGACCCCT
TGGGGAAAATGGAATCTGAACCCTCAGCAGTTTTATACCATGTTCCCTCATACCCCAGAC
AACAGCTTTCTGGGGTTTGTGGTTGAGCAGCACCTGAACTCCAGTGATATCCACCACATT
AATGAAATCAAAAGGCAGAACCAGTCCCTTGTGTATGGCAAAGTGGATAGCTTCTGGAAG
AATAAGAAGATCTACTTGGACATTATTCACACATACATGGAAGTGCATGCAACTGTTTAT
GGCTCCAGCACAAAGAATATTCCCAGTTACGTGAAAAACCATGGTATCCTCAGTGGACGG
GACCTGCAGTTCCTTCTTCGAGAAACCAAGTTGTTTGTTGGACTTGGGTTCCCTTACGAG
GGCCCAGCTCCCCTGGAAGCTATCGCAAATGGATGTGCTTTTCTGAATCCCAAGTTCAAC
CCACCCAAAAGCAGCAAAAACACAGACTTTTTCATTGGCAAGCCAACTCTGAGAGAGCTG
ACATCCCAGCATCCTTACGCTGAAGTTTTCATCGGGCGGCCACATGTGTGGACTGTTGAC
CTCAACAATCAGGAGGAAGTAGAGGATGCAGTGAAAGCAATTTTAAATCAGAAGATTGAG
CCATACATGCCATATGAATTTACGTGCGAGGGGATGCTACAGAGAATCAATGCTTTCATT
GAAAAACAGGACTTCTGCCATGGGCAAGTGATGTGGCCACCCCTCAGCGCCCTACAGGTC
AAGCTTGCTGAGCCCGGGCAGTCCTGCAAGCAGGTGTGCCAGGAGAGCCAGCTCATCTGC
GAGCCTTCTTTCTTCCAGCACCTCAACAAGGACAAGGACATGCTGAAGTACAAGGTGACC
TGCCAAAGCTCAGAGCTGGCCAAGGACATCCTGGTGCCCTCCTTTGACCCTAAGAATAAG
CACTGTGTGTTTCAAGGTGACCTCCTGCTCTTCAGCTGTGCAGGCGCCCACCCCAGGCAC
CAGAGGGTCTGCCCCTGCCGGGACTTCATCAAGGGCCAGGTGGCTCTCTGCAAAGACTGC
CTATAG
Enzyme 10 GenBank Gene ID D17716 Link Image
Enzyme 10 GeneCard ID MGAT5 Link Image
Enzyme 10 GenAtlas ID MGAT5 Link Image
Enzyme 10 HGNC ID HGNC:7049 Link Image
Enzyme 10 Chromosome Location 2
Enzyme 10 Locus 2q21
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 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 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 7046
Enzyme 11 Name Hyaluronan synthase 3
Enzyme 11 Synonyms
  1. Hyaluronate synthase 3
  2. Hyaluronic acid synthase 3
  3. HA synthase 3
Enzyme 11 Gene Name HAS3
Enzyme 11 Protein Sequence >Hyaluronan synthase 3
MPVQLTTALRVVGTSLFALAVLGGILAAYVTGYQFIHTEKHYLSFGLYGAILGLHLLIQS
LFAFLEHRRMRRAGQALKLPSPRRGSVALCIAAYQEDPDYLRKCLRSAQRISFPDLKVVM
VVDGNRQEDAYMLDIFHEVLGGTEQAGFFVWRSNFHEAGEGETEASLQEGMDRVRDVVRA
STFSCIMQKWGGKREVMYTAFKALGDSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGG
VGGDVQILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLE
DWYHQKFLGSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTKYLRWLNQQTRWSKS
YFREWLYNSLWFHKHHLWMTYESVVTGFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVG
IIKATYACFLRGNAEMIFMSLYSLLYMSSLLPAKIFAIATINKSGWGTSGRKTIVVNFIG
LIPVSIWVAVLLEGLAYTAYCQDLFSETELAFLVSGAILYGCYWVALLMLYLAIIARRCG
KKPEQYSLAFAEV
Enzyme 11 Number of Residues 553
Enzyme 11 Molecular Weight 63071
Enzyme 11 Theoretical pI 8.48
Enzyme 11 GO Classification Not Available
Enzyme 11 General Function Cell wall/membrane/envelope biogenesis
Enzyme 11 Specific Function Plays a role in hyaluronan/hyaluronic acid (HA) synthesis
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions
  • n UDP-N-acetyl-D-glucosamine + n UDP-D-glucuronate = [beta-N-acetyl-D-glucosaminyl(1-> 4)beta-D-glucuronosyl(1-> 3)]n+ 2n UDP
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • 1-27
Enzyme 11 Transmembrane Regions Not Available
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein 7110558 Link Image
Enzyme 11 UniProtKB/Swiss-Prot ID O00219 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name HAS3_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 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 11 GenBank Gene ID AF232772 Link Image
Enzyme 11 GeneCard ID HAS3 Link Image
Enzyme 11 GenAtlas ID HAS3 Link Image
Enzyme 11 HGNC ID HGNC:4820 Link Image
Enzyme 11 Chromosome Location 16
Enzyme 11 Locus 16q22.1
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References
  1. Spicer AP, Olson JS, McDonald JA: Molecular cloning and characterization of a cDNA encoding the third putative mammalian hyaluronan synthase. J Biol Chem. 1997 Apr 4;272(14):8957-61. [PubMed Link Image]
Enzyme 11 Metabolite References Not Available
Enzyme 12 [top]
Enzyme 12 ID 7047
Enzyme 12 Name Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
Enzyme 12 Synonyms
  1. N-glycosyl-oligosaccharide-glycoprotein N- acetylglucosaminyltransferase III
  2. N-acetylglucosaminyltransferase III
  3. GNT-III
  4. GlcNAc-T III
Enzyme 12 Gene Name MGAT3
Enzyme 12 Protein Sequence >Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase
MKMRRYKLFLMFCMAGLCLISFLHFFKTLSYVTFPRELASLSPNLVSSFFWNNAPVTPQA
SPEPGGPDLLRTPLYSHSPLLQPLPPSKAAEELHRVDLVLPEDTTEYFVRTKAGGVCFKP
GTKMLERPPPGRPEEKPEGANGSSARRPPRYLLSARERTGGRGARRKWVECVCLPGWHGP
SCGVPTVVQYSNLPTKERLVPREVPRRVINAINVNHEFDLLDVRFHELGDVVDAFVVCES
NFTAYGEPRPLKFREMLTNGTFEYIRHKVLYVFLDHFPPGGRQDGWIADDYLRTFLTQDG
VSRLRNLRPDDVFIIDDADEIPARDGVLFLKLYDGWTEPFAFHMRKSLYGFFWKQPGTLE
VVSGCTVDMLQAVYGLDGIRLRRRQYYTMPNFRQYENRTGHILVQWSLGSPLHFAGWHCS
WCFTPEGIYFKLVSAQNGDFPRWGDYEDKRDLNYIRGLIRTGGWFDGTQQEYPPADPSEH
MYAPKYLLKNYDRFHYLLDNPYQEPRSTAAGGWRHRGPEGRPPARGKLDEAEV
Enzyme 12 Number of Residues 533
Enzyme 12 Molecular Weight 61314
Enzyme 12 Theoretical pI 8.37
Enzyme 12 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
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid N-linked glycosylation
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 12 General Function Not Available
Enzyme 12 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 12 Pathways
Enzyme 12 Reactions
  • UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R = UDP + 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R
Enzyme 12 Pfam Domain Function
Enzyme 12 Signals
  • 1-30
Enzyme 12 Transmembrane Regions Not Available
Enzyme 12 Essentiality Not Available
Enzyme 12 GenBank ID Protein 398138 Link Image
Enzyme 12 UniProtKB/Swiss-Prot ID Q09327 Link Image
Enzyme 12 UniProtKB/Swiss-Prot Entry Name MGAT3_HUMAN Link Image
Enzyme 12 PDB ID Not Available
Enzyme 12 Cellular Location Not Available
Enzyme 12 Gene Sequence >1596 bp
ATGAGACGCTACAAGCTCTTTCTCATGTTCTGTATGGCCGGCCTGTGCCTCATCTCCTTC
CTGCACTTCTTCAAGACCCTGTCCTATGTCACCTTCCCCCGAGAACTGGCCTCCCTCAGC
CCTAACCTGGTGTCCAGCTTTTTCTGGAACAATGCCCCGGTCACGCCCCAGGCCAGCCCC
GAGCCAGGAGGCCCTGACCTGCTGCGTACCCCACTCTACTCCCACTCGCCCCTGCTGCAG
CCGCTGCCGCCCAGCAAGGCGGCCGAGGAGCTCCACCGGGTGGACTTGGTGCTGCCCGAG
GACACCACCGAGTATTTCGTGCGCACCAAGGCCGGCGGCGTCTGCTTCAAACCCGGCACC
AAGATGCTGGAGAGGCCGCCCCCGGGACGGCCGGAGGAGAAGCCTGAGGGGGCCAACGGC
TCCTCGGCCCGGCGGCCACCCCGGTACCTCCTGAGCGCCCGGGAGCGCACGGGGGGCCGA
GGCGCCCGGCGCAAGTGGGTGGAGTGCGTGTGCCTGCCCGGCTGGCACGGACCCAGCTGC
GGCGTGCCCACTGTGGTGCAGTACTCCAACCTGCCCACCAAGGAGCGGCTGGTGCCCAGG
GAGGTGCCGCGCCGCGTCATCAACGCCATCAACGTCAACCACGAGTTCGACCTGCTGGAC
GTGCGCTTCCACGAGCTGGGCGACGTGGTGGACGCCTTTGTGGTGTGCGAGTCCAACTTC
ACGGCTTATGGGGAGCCGCGGCCGCTCAAGTTCCGGGAGATGCTGACCAATGGCACCTTC
GAGTACATCCGCCACAAGGTGCTCTATGTCTTCCTGGACCACTTCCCGCCCGGCGGCCGG
CAGGACGGCTGGATCGCCGACGACTACCTGCGCACCTTCCTCACCCAGGACGGCGTCTCG
CGGCTGCGCAACCTGCGGCCCGACGACGTCTTCATCATTGACGATGCGGACGAGATCCCG
GCCCGTGACGGCGTCCTTTTCCTCAAGCTCTACGATGGCTGGACCGAGCCCTTCGCCTTC
CACATGCGCACGTCGCTCTACGGCTTCTTCTGGAAGCAGCCGGGCACCCTGGAGGTGGTG
TCAGGCTGCACGGTGGACATGCTGCAGGCAGTGTATGGGCTGGACGGCATCCGCCTGCGC
CGCCGCCAGTACTACACCATGCCCAACTTCAGACAGTATGAGAACCGCACCGGCCACATC
CTGGTGCAGTGGTCGCTGGGCAGCCCCCTGCACTTCGCCGGCTGGCACTGCTCCTGGTGC
TTCACGCCCGAGGGCATCTACTTCAAGCTCGTGTCCGCCCAGAATGGCGACTTCCCACGC
TGGGGTGACTACGAGGACAAGCGGGACCTGAACTACATCCGCGGCCTGATCCGCACCGGG
GGCTGGTTCGACGGCACGCAGCAGGAGTACCCGCCTGCAGACCCCAGCGAGCACATGTAT
GCGCCCAAGTACCTGCTGAAGAACTACGACCGGTTCCACTACCTGCTGGACAACCCCTAC
CAGGAGCCCAGGAGCACGGCGGCGGGCGGGTGGCGCCACAGGGGTCCCGAGGGAAGGCCG
CCCGCCCGGGGCAAACTGGACGAGGCGGAAGTCTAG
Enzyme 12 GenBank Gene ID D13789 Link Image
Enzyme 12 GeneCard ID MGAT3 Link Image
Enzyme 12 GenAtlas ID MGAT3 Link Image
Enzyme 12 HGNC ID HGNC:7046 Link Image
Enzyme 12 Chromosome Location 22
Enzyme 12 Locus 22q13.1
Enzyme 12 SNPs SNPJam Report Link Image
Enzyme 12 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. 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]
Enzyme 12 Metabolite References Not Available
Enzyme 13 [top]
Enzyme 13 ID 7269
Enzyme 13 Name Hyaluronan synthase 2
Enzyme 13 Synonyms
  1. Hyaluronate synthase 2
  2. Hyaluronic acid synthase 2
  3. HA synthase 2
Enzyme 13 Gene Name HAS2
Enzyme 13 Protein Sequence >Hyaluronan synthase 2
MHCERFLCILRIIGTTLFGVSLLLGITAAYIVGYQFIQTDNYYFSFGLYGAFLASHLIIQ
SLFAFLEHRKMKKSLETPIKLNKTVALCIAAYQEDPDYLRKCLQSVKRLTYPGIKVVMVI
DGNSEDDLYMMDIFSEVMGRDKSATYIWKNNFHEKGPGETDESHKESSQHVTQLVLSNKS
ICIMQKWGGKREVMYTAFRALGRSVDYVQVCDSDTMLDPASSVEMVKVLEEDPMVGGVGG
DVQILNKYDSWISFLSSVRYWMAFNIERACQSYFGCVQCISGPLGMYRNSLLHEFVEDWY
NQEFMGNQCSFGDDRHLTNRVLSLGYATKYTARSKCLTETPIEYLRWLNQQTRWSKSYFR
EWLYNAMWFHKHHLWMTYEAIITGFFPFFLIATVIQLFYRGKIWNILLFLLTVQLVGLIK
SSFASCLRGNIVMVFMSLYSVLYMSSLLPAKMFAIATINKAGWGTSGRKTIVVNFIGLIP
VSVWFTILLGGVIFTIYKESKRPFSESKQTVLIVGTLLYACYWVMLLTLYVVLINKCGRR
KKGQQYDMVLDV
Enzyme 13 Number of Residues 552
Enzyme 13 Molecular Weight 63567
Enzyme 13 Theoretical pI 8.74
Enzyme 13 GO Classification Not Available
Enzyme 13 General Function Cell wall/membrane/envelope biogenesis
Enzyme 13 Specific Function Plays a role in hyaluronan/hyaluronic acid (HA) synthesis
Enzyme 13 Pathways Not Available
Enzyme 13 Reactions
  • n UDP-N-acetyl-D-glucosamine + n UDP-D-glucuronate = [beta-N-acetyl-D-glucosaminyl(1-> 4)beta-D-glucuronosyl(1-> 3)]n+ 2n UDP
Enzyme 13 Pfam Domain Function
Enzyme 13 Signals
  • 1-29
Enzyme 13 Transmembrane Regions Not Available
Enzyme 13 Essentiality Not Available
Enzyme 13 GenBank ID Protein 1543068 Link Image
Enzyme 13 UniProtKB/Swiss-Prot ID Q92819 Link Image
Enzyme 13 UniProtKB/Swiss-Prot Entry Name HAS2_HUMAN Link Image
Enzyme 13 PDB ID Not Available
Enzyme 13 Cellular Location Not Available
Enzyme 13 Gene Sequence >1659 bp
ATGCATTGTGAGAGGTTTCTATGTATCCTGAGAATAATTGGAACCACACTCTTTGGAGTC
TCTCTCCTCCTTGGAATCACAGCTGCTTATATTGTTGGCTACCAGTTTATCCAAACGGAT
AATTACTATTTCTCTTTTGGACTGTATGGTGCCTTTTTGGCATCACACCTCATCATCCAA
AGCCTGTTTGCCTTTTTGGAGCACCGAAAAATGAAAAAATCCCTAGAAACCCCCATAAAG
TTGAACAAAACAGTTGCCCTTTGCATCGCTGCCTATCAAGAAGATCCAGACTACTTAAGG
AAATGTTTGCAATCTGTGAAAAGGCTAACCTACCCTGGGATTAAAGTTGTCATGGTCATA
GATGGGAACTCAGAAGATGACCTTTACATGATGGACATCTTCAGTGAAGTCATGGGCAGA
GACAAATCAGCCACTTATATCTGGAAGAACAACTTCCACGAAAAGGGTCCCGGTGAGACA
GATGAGTCACATAAAGAAAGCTCGCAACACGTAACGCAATTGGTCTTGTCCAACAAAAGT
ATCTGCATCATGCAAAAATGGGGTGGAAAAAGAGAAGTCATGTACACAGCCTTCAGAGCA
CTGGGACGAAGTGTGGATTATGTACAGGTTTGTGATTCAGACACTATGCTTGACCCAGCC
TCATCTGTGGAGATGGTAAAAGTTTTAGAAGAAGATCCCATGGTTGGAGGTGTTGGGGGA
GATGTCCAGATTTTAAACAAGTACGATTCCTGGATCTCATTCCTCAGCAGTGTAAGATAT
TGGATGGCTTTTAATATAGAAAGGGCCTGTCAGTCTTATTTTGGGTGTGTTCAGTGCATT
AGTGGACCTCTGGGAATGTACAGAAACTCCTTGTTGCATGAGTTTGTGGAAGATTGGTAC
AATCAAGAATTTATGGGCAACCAATGTAGCTTTGGTGATGACAGGCATCTCACGAACCGG
GTGCTGAGCCTGGGCTATGCAACAAAATACACAGCTCGATCTAAGTGCCTTACTGAAACA
CCTATAGAGTATCTCAGATGGCTAAACCAGCAGACCCGTTGGAGCAAGTCCTACTTCCGA
GAATGGCTGTACAATGCAATGTGGTTTCACAAACATCACTTGTGGATGACCTACGAAGCG
ATTATCACTGGATTCTTTCCTTTCTTTCTCATTGCCACAGTAATCCAGCTCTTCTACCGG
GGTAAAATTTGGAACATTCTCCTCTTCTTGTTAACTGTCCAGCTAGTAGGTCTCATAAAA
TCATCTTTTGCCAGCTGCCTTAGAGGAAATATCGTCATGGTCTTCATGTCTCTCTACTCA
GTGTTATACATGTCGAGTTTACTTCCCGCCAAGATGTTTGCAATTGCAACAATAAACAAA
GCTGGGTGGGGCACATCAGGAAGGAAAACCATTGTTGTTAATTTCATAGGACTCATTCCA
GTATCAGTTTGGTTTACAATCCTCCTGGGTGGTGTGATTTTCACCATTTATAAGGAGTCT
AAAAGGCCATTTTCAGAATCCAAACAGACAGTTCTAATTGTTGGAACGTTGCTCTATGCA
TGCTATTGGGTCATGCTTTTGACGCTGTATGTAGTTCTCATCAATAAGTGTGGCAGGCGG
AAGAAGGGACAACAATATGACATGGTGCTTGATGTATGA
Enzyme 13 GenBank Gene ID U54804 Link Image
Enzyme 13 GeneCard ID HAS2 Link Image
Enzyme 13 GenAtlas ID HAS2 Link Image
Enzyme 13 HGNC ID HGNC:4819 Link Image
Enzyme 13 Chromosome Location 8
Enzyme 13 Locus 8q24.12
Enzyme 13 SNPs SNPJam Report Link Image
Enzyme 13 General References
  1. Watanabe K, Yamaguchi Y: Molecular identification of a putative human hyaluronan synthase. J Biol Chem. 1996 Sep 20;271(38):22945-8. [PubMed Link Image]
Enzyme 13 Metabolite References Not Available
Enzyme 14 [top]
Enzyme 14 ID 8392
Enzyme 14 Name N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
Enzyme 14 Synonyms
  1. N-acetylglucosaminyltransferase
  2. I-branching enzyme
  3. IGNT
Enzyme 14 Gene Name GCNT2
Enzyme 14 Protein Sequence >N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
MPLSMRYLFIISVSSVIIFIVFSVFNFGGDPSFQRLNISDPLRLTQVCTSFINGKTRFLW
KNKLMIHEKSSCKEYLTQSHYITAPLSKEEADFPLAYIMVIHHHFDTFARLFRAIYMPQN
IYCVHVDEKATTEFKDAVEQLLSCFPNAFLASKMEPVVYGGISRLQADLNCIRDLSAFEV
SWKYVINTCGQDFPLKTNKEIVQYLKGFKGKNITPGVLPPAHAIGRTKYVHQEHLGKELS
YVIRTTALKPPPPHNLTIYFGSAYVALSREFANFVLHDPRAVDLLQWSKDTFSPDEHFWV
TLNRIPGVPGSMPNASWTGNLRAIKWSDMEDRHGGCHGHYVHGICIYGNGDLKWLVNSPS
LFANKFELNTYPLTVECLELRHRERTLNQSETAIQPSWYF
Enzyme 14 Number of Residues 400
Enzyme 14 Molecular Weight 45855
Enzyme 14 Theoretical pI 8.32
Enzyme 14 GO Classification
Function
  • UDP-glycosyltransferase activity
  • acetylglucosaminyltransferase activity
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
Component
  • cell
  • membrane
Enzyme 14 General Function Not Available
Enzyme 14 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
Enzyme 14 Pathways
  • Blood group glycolipid biosynthesis-neolactoseries (map00602 Link Image)
Enzyme 14 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
Enzyme 14 Pfam Domain Function
Enzyme 14 Signals
  • 1-23
Enzyme 14 Transmembrane Regions Not Available
Enzyme 14 Essentiality Not Available
Enzyme 14 GenBank ID Protein 307298 Link Image
Enzyme 14 UniProtKB/Swiss-Prot ID Q06430 Link Image
Enzyme 14 UniProtKB/Swiss-Prot Entry Name GCNT2_HUMAN Link Image
Enzyme 14 PDB ID Not Available
Enzyme 14 Cellular Location Not Available
Enzyme 14 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 14 GenBank Gene ID L19659 Link Image
Enzyme 14 GeneCard ID GCNT2 Link Image
Enzyme 14 GenAtlas ID GCNT2 Link Image
Enzyme 14 HGNC ID HGNC:4204 Link Image
Enzyme 14 Chromosome Location 6
Enzyme 14 Locus 6p24
Enzyme 14 SNPs SNPJam Report Link Image
Enzyme 14 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. 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 14 Metabolite References Not Available
Enzyme 15 [top]
Enzyme 15 ID 8492
Enzyme 15 Name UDP-N-acetylglucosamine transporter
Enzyme 15 Synonyms
  1. Golgi UDP-GlcNAc transporter
  2. Solute carrier family 35 member A3
Enzyme 15 Gene Name SLC35A3
Enzyme 15 Protein Sequence >UDP-N-acetylglucosamine transporter
MFANLKYVSLGILVFQTTSLVLTMRYSRTLKEEGPRYLSSTAVVVAELLKIMACILLVYK
DSKCSLRALNRVLHDEILNKPMETLKLAIPSGIYTLQNNLLYVALSNLDAATYQVTYQLK
ILTTALFSVSMLSKKLGVYQWLSLVILMTGVAFVQWPSDSQLDSKELSAGSQFVGLMAVL
TACFSSGFAGVYFEKILKETKQSVWIRNIQLGFFGSIFGLMGVYIYDGELVSKNGFFQGY
NRLTWIVVVLQALGGLVIAAVIKYADNILKGFATSLSIILSTLISYFWLQDFVPTSVFFL
GAILVITATFLYGYDPKPAGNPTKA
Enzyme 15 Number of Residues 325
Enzyme 15 Molecular Weight 35985
Enzyme 15 Theoretical pI 9.51
Enzyme 15 GO Classification
Function
  • carbohydrate transporter activity
  • carrier activity
  • electrochemical potential-driven transporter activity
  • nucleotide-sugar transporter activity
  • porter activity
  • sugar porter activity
  • transporter activity
Process
  • carbohydrate transport
  • cellular physiological process
  • nucleotide-sugar transport
  • physiological process
  • transport
Component
  • Golgi membrane
  • cell
  • integral to membrane
  • intrinsic to membrane
  • membrane
  • organelle membrane
Enzyme 15 General Function Carbohydrate transport and metabolism
Enzyme 15 Specific Function Uridine diphosphate-N-acetylglucosamine transporter in the Golgi apparatus
Enzyme 15 Pathways Not Available
Enzyme 15 Reactions Not Available
Enzyme 15 Pfam Domain Function
Enzyme 15 Signals
  • 1-19
Enzyme 15 Transmembrane Regions
  • 8-24 42-58 138-154 173-189 209-225 246-262 268-284 295-311
Enzyme 15 Essentiality Not Available
Enzyme 15 GenBank ID Protein 4903004 Link Image
Enzyme 15 UniProtKB/Swiss-Prot ID Q9Y2D2 Link Image
Enzyme 15 UniProtKB/Swiss-Prot Entry Name S35A3_HUMAN Link Image
Enzyme 15 PDB ID Not Available
Enzyme 15 Cellular Location Not Available
Enzyme 15 Gene Sequence >978 bp
ATGTTCGCCAACCTAAAATACGTTTCCCTGGGAATTTTGGTCTTTCAGACTACCAGTTTG
GTTCTAACAATGCGTTATTCCAGAACTTTAAAAGAAGAAGGACCTCGTTATCTATCTTCT
ACAGCAGTGGTTGTTGCTGAACTTTTGAAGATAATGGCCTGCATTTTATTGGTCTACAAA
GACAGCAAATGTAGTCTAAGAGCACTGAATCGAGTACTACATGATGAAATTCTTAATAAA
CCTATGGAAACACTTAAACTTGCTATTCCATCAGGGATCTATACTCTTCAGAATAATTTA
CTGTATGTGGCACTATCAAATCTAGATGCAGCTACTTATCAGGTCACGTATCAGTTAAAA
ATTCTTACAACAGCATTATTTTCTGTGTCTATGCTTAGTAAAAAATTGGGTGTATACCAG
TGGCTGTCCCTAGTAATTTTGATGACAGGAGTTGCTTTTGTACAGTGGCCCTCAGATTCT
CAGCTTGATTCTAAGGAACTTTCAGCTGGTTCTCAATTTGTAGGACTCATGGCAGTTCTC
ACAGCATGTTTTTCAAGTGGCTTTGCTGGGGTTTACTTTGAGAAAATCTTAAAAGAAACA
AAACAATCAGTGTGGATAAGAAATATTCAGCTTGGTTTCTTTGGAAGTATATTTGGATTA
ATGGGTGTATACATTTATGATGGAGAACTGGTATCAAAGAATGGATTTTTTCAGGGATAT
AACCGACTGACCTGGATAGTAGTTGTTCTTCAGGCACTTGGAGGCCTTGTAATAGCTGCT
GTTATTAAGTATGCAGATAATATTTTAAAAGGATTTGCAACCTCTTTATCGATAATATTA
TCAACATTGATCTCCTATTTTTGGCTTCAAGATTTTGTGCCAACCAGTGTCTTTTTCCTT
GGAGCCATCCTTGTAATAACAGCTACTTTTTTGTATGGTTATGATCCCAAACCTGCAGGA
AATCCCACTAAAGCATAG
Enzyme 15 GenBank Gene ID AB021981 Link Image
Enzyme 15 GeneCard ID SLC35A3 Link Image
Enzyme 15 GenAtlas ID SLC35A3 Link Image
Enzyme 15 HGNC ID HGNC:11023 Link Image
Enzyme 15 Chromosome Location 1
Enzyme 15 Locus 1p21
Enzyme 15 SNPs SNPJam Report Link Image
Enzyme 15 General References
  1. Ishida N, Yoshioka S, Chiba Y, Takeuchi M, Kawakita M: Molecular cloning and functional expression of the human Golgi UDP-N-acetylglucosamine transporter. J Biochem. 1999 Jul;126(1):68-77. [PubMed Link Image]
Enzyme 15 Metabolite References Not Available
Enzyme 16 [top]
Enzyme 16 ID 8792
Enzyme 16 Name Beta-1,3-N-acetylglucosaminyltransferase bGnT-2
Enzyme 16 Synonyms
  1. Hypothetical protein B3GNT1
Enzyme 16 Gene Name bGnT-2
Enzyme 16 Protein Sequence >Beta-1,3-N-acetylglucosaminyltransferase bGnT-2
MSVGRRRIKLLGILMMANVFIYFIMEVSKSSSQEKNGKGEVIIPKEKFWKISTPPEAYWN
REQEKLNRQYNPILSMLTNQTGEAGRLSNISHLNYCEPDLRVTSVVTGFNNLPDRFKDFL
LYLRCRNYSLLIDQPDKCAKKPFLLLAIKSLTPHFARRQAIRESWGQESNAGNQTVVRVF
LLGQTPPEDNHPDLSDMLKFESEKHQDILMWNYRDTFFNLSLKEVLFLRWVSTSCPDTEF
VFKGDDDVFVNTHHILNYLNSLSKTKAKDLFIGDVIHNAGPHRDKKLKYYIPEVVYSGLY
PPYAGGGGFLYSGHLALRLYHITDQVHLYPIDDVYTGMCLQKLGLVPEKHKGFRTFDIEE
KNKNNICSYVDLMLVHSRKPQEMIDIWSQLQSAHLKC
Enzyme 16 Number of Residues 397
Enzyme 16 Molecular Weight 46023
Enzyme 16 Theoretical pI 8.75
Enzyme 16 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 16 General Function Not Available
Enzyme 16 Specific Function Not Available
Enzyme 16 Pathways Not Available
Enzyme 16 Reactions Not Available
Enzyme 16 Pfam Domain Function
Enzyme 16 Signals
  • 1-32
Enzyme 16 Transmembrane Regions
  • 7-24
Enzyme 16 Essentiality Not Available
Enzyme 16 GenBank ID Protein 12619294 Link Image
Enzyme 16 UniProtKB/Swiss-Prot ID Q54AC1 Link Image
Enzyme 16 UniProtKB/Swiss-Prot Entry Name Q54AC1_HUMAN Link Image
Enzyme 16 PDB ID Not Available
Enzyme 16 Cellular Location Not Available
Enzyme 16 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 16 GenBank Gene ID AB049584 Link Image
Enzyme 16 GeneCard ID bGnT-2 Link Image
Enzyme 16 GenAtlas ID bGnT-2 Link Image
Enzyme 16 HGNC ID HGNC:15629 Link Image
Enzyme 16 Chromosome Location Not Available
Enzyme 16 Locus Not Available
Enzyme 16 SNPs SNPJam Report Link Image
Enzyme 16 General References
  1. 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]
Enzyme 16 Metabolite References Not Available
Enzyme 17 [top]
Enzyme 17 ID 11945
Enzyme 17 Name Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
Enzyme 17 Synonyms
  1. UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta- 1,4-N-acetylglucosaminyltransferase IVa
  2. N-glycosyl-oligosaccharide- glycoprotein N-acetylglucosaminyltransferase IVa
  3. N- acetylglucosaminyltransferase IVa
  4. GnT-IVa
  5. GlcNAc-T IVa[Contains: Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form]
Enzyme 17 Gene Name MGAT4A
Enzyme 17 Protein Sequence >Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A
MRLRNGTVATALAFITSFLTLSWYTTWQNGKEKLIAYQREFLALKERLRIAEHRISQRSS
ELNTIVQQFKRVGAETNGSKDALNKFSDNTLKLLKELTSKKSLQVPSIYYHLPHLLKNEG
SLQPAVQIGNGRTGVSIVMGIPTVKREVKSYLIETLHSLIDNLYPEEKLDCVIVVFIGET
DIDYVHGVVANLEKEFSKEISSGLVEVISPPESYYPDLTNLKETFGDSKERVRWRTKQNL
DYCFLMMYAQEKGIYYIQLEDDIIVKQNYFNTIKNFALQLSSEEWMILEFSQLGFIGKMF
QAPDLTLIVEFIFMFYKEKPIDWLLDHILWVKVCNPEKDAKHCDRQKANLRIRFRPSLFQ
HVGLHSSLSGKIQKLTDKDYMKPLLLKIHVNPPAEVSTSLKVYQGHTLEKTYMGEDFFWA
ITPIAGDYILFKFDKPVNVESYLFHSGNQEHPGDILLNTTVEVLPFKSEGLEISKETKDK
RLEDGYFRIGKFENGVAEGMVDPSLNPISAFRLSVIQNSAVWAILNEIHIKKATN
Enzyme 17 Number of Residues 535
Enzyme 17 Molecular Weight 61545
Enzyme 17 Theoretical pI Not Available
Enzyme 17 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • cell
  • membrane
Enzyme 17 General Function Not Available
Enzyme 17 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 17 Pathways
Enzyme 17 Reactions
  • ((N-acetyl-D-glucosaminyl)2-(alpha-D-mannosyl)2-beta-D-mannosyl-diacetylchitobiosyl)-L-asparagine (protein) + UDP-N-acetyl-D-glucosamine --> H+ + ((N-acetyl-D-glucosaminyl)3-(alpha-D-mannosyl)2-beta-D-mannosyl-diacetylchitobiosyl)-L-asparagine (protein) + UDP
Enzyme 17 Pfam Domain Function
Enzyme 17 Signals
  • None
Enzyme 17 Transmembrane Regions
  • 5-27
Enzyme 17 Essentiality Not Available
Enzyme 17 GenBank ID Protein 6329074 Link Image
Enzyme 17 UniProtKB/Swiss-Prot ID Q9UM21 Link Image
Enzyme 17 UniProtKB/Swiss-Prot Entry Name MGT4A_HUMAN Link Image
Enzyme 17 PDB ID Not Available
Enzyme 17 Cellular Location Not Available
Enzyme 17 Gene Sequence Not Available
Enzyme 17 GenBank Gene ID AB000616 Link Image
Enzyme 17 GeneCard ID Not Available
Enzyme 17 GenAtlas ID MGAT4A Link Image
Enzyme 17 HGNC ID HGNC:7047 Link Image
Enzyme 17 Chromosome Location Not Available
Enzyme 17 Locus Not Available
Enzyme 17 SNPs SNPJam Report Link Image
Enzyme 17 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]
Enzyme 17 Metabolite References Not Available
Enzyme 18 [top]
Enzyme 18 ID 11946
Enzyme 18 Name Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
Enzyme 18 Synonyms
  1. UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta- 1,4-N-acetylglucosaminyltransferase IVb
  2. N-glycosyl-oligosaccharide- glycoprotein N-acetylglucosaminyltransferase IVb
  3. N- acetylglucosaminyltransferase IVb
  4. GnT-IVb
  5. GlcNAc-T IVb
Enzyme 18 Gene Name MGAT4B
Enzyme 18 Protein Sequence >Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B
MRLRNGTFLTLLLFCLCAFLSLSWYAALSGQKGDVVDVYQREFLALRDRLHAAEQESLKR
SKELNLVLDEIKRAVSERQALRDGDGNRTWGRLTEDPRLKPWNGSHRHVLHLPTVFHHLP
HLLAKESSLQPAVRVGQGRTGVSVVMGIPSVRREVHSYLTDTLHSLISELSPQEKEDSVI
VVLIAETDSQYTSAVTENIKALFPTEIHSGLLEVISPSPHFYPDFSRLRESFGDPKERVR
WRTKQNLDYCFLMMYAQSKGIYYVQLEDDIVAKPNYLSTMKNFALQQPSEDWMILEFSQL
GFIGKMFKSLDLSLIVEFILMFYRDKPIDWLLDHILWVKVCNPEKDAKHCDRQKANLRIR
FKPSLFQHVGTHSSLAGKIQKLKDKDFGKQALRKEHVNPPAEVSTSLKTYQHFTLEKAYL
REDFFWAFTPAAGDFIRFRFFQPLRLERFFFRSGNIEHPEDKLFNTSVEVLPFDNPQSDK
EALQEGRTATLRYPRSPDGYLQIGSFYKGVAEGEVDPAFGPLEALRLSIQTDSPVWVILS
EIFLKKAD
Enzyme 18 Number of Residues 548
Enzyme 18 Molecular Weight 63199
Enzyme 18 Theoretical pI Not Available
Enzyme 18 GO Classification
Function
  • catalytic activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • carbohydrate metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
Component
  • cell
  • membrane
Enzyme 18 General Function Not Available
Enzyme 18 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 18 Pathways
Enzyme 18 Reactions
  • ((N-acetyl-D-glucosaminyl)2-(alpha-D-mannosyl)2-beta-D-mannosyl-diacetylchitobiosyl)-L-asparagine (protein) + UDP-N-acetyl-D-glucosamine --> H+ + ((N-acetyl-D-glucosaminyl)3-(alpha-D-mannosyl)2-beta-D-mannosyl-diacetylchitobiosyl)-L-asparagine (protein) + UDP
Enzyme 18 Pfam Domain Function
Enzyme 18 Signals
  • None
Enzyme 18 Transmembrane Regions
  • 8-28
Enzyme 18 Essentiality Not Available
Enzyme 18 GenBank ID Protein 5748487 Link Image
Enzyme 18 UniProtKB/Swiss-Prot ID Q9UQ53 Link Image
Enzyme 18 UniProtKB/Swiss-Prot Entry Name MGT4B_HUMAN Link Image
Enzyme 18 PDB ID Not Available
Enzyme 18 Cellular Location Not Available
Enzyme 18 Gene Sequence Not Available
Enzyme 18 GenBank Gene ID AB000624 Link Image
Enzyme 18 GeneCard ID Not Available
Enzyme 18 GenAtlas ID MGAT4B Link Image
Enzyme 18 HGNC ID HGNC:7048 Link Image
Enzyme 18 Chromosome Location Not Available
Enzyme 18 Locus Not Available
Enzyme 18 SNPs SNPJam Report Link Image
Enzyme 18 General References
  1. 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]
Enzyme 18 Metabolite References Not Available
Enzyme 19 [top]
Enzyme 19 ID 11996
Enzyme 19 Name UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
Enzyme 19 Synonyms
  1. Beta3Gn-T5
  2. BGnT-5
  3. Beta-1,3-N- acetylglucosaminyltransferase-5
  4. Lactotriaosylceramide synthase
  5. Lc(3Cer synthase
  6. Lc3 synthase
Enzyme 19 Gene Name B3GNT5
Enzyme 19 Protein Sequence >UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
MRMLVSGRRVKKWQLIIQLFATCFLASLMFFWEPIDNHIVSHMKSYSYRYLINSYDFVND
TLSLKHTSAGPRYQYLINHKEKCQAQDVLLLLFVKTAPENYDRRSGIRRTWGNENYVRSQ
LNANIKTLFALGTPNPLEGEELQRKLAWEDQRYNDIIQQDFVDSFYNLTLKLLMQFSWAN
TYCPHAKFLMTADDDIFIHMPNLIEYLQSLEQIGVQDFWIGRVHRGAPPIRDKSSKYYVS
YEMYQWPAYPDYTAGAAYVISGDVAAKVYEASQTLNSSLYIDDVFMGLCANKIGIVPQDH
VFFSGEGKTPYHPCIYEKMMTSHGHLEDLQDLWKNATDPKVKTISKGFFGQIYCRLMKII
LLCKISYVDTYPCRAAFI
Enzyme 19 Number of Residues 378
Enzyme 19 Molecular Weight 44053
Enzyme 19 Theoretical pI Not Available
Enzyme 19 GO Classification
Function
  • catalytic activity
  • galactosyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
  • transferase activity, transferring hexosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • membrane
Enzyme 19 General Function Not Available
Enzyme 19 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 19 Pathways Not Available
Enzyme 19 Reactions
  • galactosyl glucosyl ceramide + UDP-N-acetyl-D-glucosamine --> (Gal)1 (Glc)1 (GlcNAc)1 (Cer)1 + H+ + UDP
Enzyme 19 Pfam Domain Function
Enzyme 19 Signals
  • None
Enzyme 19 Transmembrane Regions
  • 15-35
Enzyme 19 Essentiality Not Available
Enzyme 19 GenBank ID Protein 13568434 Link Image
Enzyme 19 UniProtKB/Swiss-Prot ID Q9BYG0 Link Image
Enzyme 19 UniProtKB/Swiss-Prot Entry Name B3GN5_HUMAN Link Image
Enzyme 19 PDB ID Not Available
Enzyme 19 Cellular Location Not Available
Enzyme 19 Gene Sequence Not Available
Enzyme 19 GenBank Gene ID AB045278 Link Image
Enzyme 19 GeneCard ID Not Available
Enzyme 19 GenAtlas ID B3GNT5 Link Image
Enzyme 19 HGNC ID HGNC:15684 Link Image
Enzyme 19 Chromosome Location Not Available
Enzyme 19 Locus Not Available
Enzyme 19 SNPs SNPJam Report Link Image
Enzyme 19 General References
  1. 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]
Enzyme 19 Metabolite References Not Available
Enzyme 20 [top]
Enzyme 20 ID 15260
Enzyme 20 Name N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
Enzyme 20 Synonyms
  1. GlcNAc-1-phosphotransferase subunits alpha/beta
  2. Stealth protein GNPTAB
  3. UDP-N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
  4. Contains: RecName: N-acetylglucosamine-1-phosphotransferase subunit alpha
  5. Contains: RecName: N-acetylglucosamine-1-phosphotransferase subunit beta
Enzyme 20 Gene Name GNPTAB
Enzyme 20 Protein Sequence >N-acetylglucosamine-1-phosphotransferase subunits alpha/beta
MLFKLLQRQTYTCLSHRYGLYVCFLGVVVTIVSAFQFGEVVLEWSRDQYHVLFDSYRDNI
AGKSFQNRLCLPMPIDVVYTWVNGTDLELLKELQQVREQMEEEQKAMREILGKNTTEPTK
KSEKQLECLLTHCIKVPMLVLDPALPANITLKDLPSLYPSFHSASDIFNVAKPKNPSTNV
SVVVFDSTKDVEDAHSGLLKGNSRQTVWRGYLTTDKEVPGLVLMQDLAFLSGFPPTFKET
NQLKTKLPENLSSKVKLLQLYSEASVALLKLNNPKDFQELNKQTKKNMTIDGKELTISPA
YLLWDLSAISQSKQDEDISASRFEDNEELRYSLRSIERHAPWVRNIFIVTNGQIPSWLNL
DNPRVTIVTHQDVFRNLSHLPTFSSPAIESHIHRIEGLSQKFIYLNDDVMFGKDVWPDDF
YSHSKGQKVYLTWPVPNCAEGCPGSWIKDGYCDKACNNSACDWDGGDCSGNSGGSRYIAG
GGGTGSIGVGQPWQFGGGINSVSYCNQGCANSWLADKFCDQACNVLSCGFDAGDCGQDHF
HELYKVILLPNQTHYIIPKGECLPYFSFAEVAKRGVEGAYSDNPIIRHASIANKWKTIHL
IMHSGMNATTIHFNLTFQNTNDEEFKMQITVEVDTREGPKLNSTAQKGYENLVSPITLLP
EAEILFEDIPKEKRFPKFKRHDVNSTRRAQEEVKIPLVNISLLPKDAQLSLNTLDLQLEH
GDITLKGYNLSKSALLRSFLMNSQHAKIKNQAIITDETNDSLVAPQEKQVHKSILPNSLG
VSERLQRLTFPAVSVKVNGHDQGQNPPLDLETTARFRVETHTQKTIGGNVTKEKPPSLIV
PLESQMTKEKKITGKEKENSRMEENAENHIGVTEVLLGRKLQHYTDSYLGFLPWEKKKYF
QDLLDEEESLKTQLAYFTDSKNTGRQLKDTFADSLRYVNKILNSKFGFTSRKVPAHMPHM
IDRIVMQELQDMFPEEFDKTSFHKVRHSEDMQFAFSYFYYLMSAVQPLNISQVFDEVDTD
QSGVLSDREIRTLATRIHELPLSLQDLTGLEHMLINCSKMLPADITQLNNIPPTQESYYD
PNLPPVTKSLVTNCKPVTDKIHKAYKDKNKYRFEIMGEEEIAFKMIRTNVSHVVGQLDDI
RKNPRKFVCLNDNIDHNHKDAQTVKAVLRDFYESMFPIPSQFELPREYRNRFLHMHELQE
WRAYRDKLKFWTHCVLATLIMFTIFSFFAEQLIALKRKIFPRRRIHKEASPNRIRV
Enzyme 20 Number of Residues 1256
Enzyme 20 Molecular Weight 143623
Enzyme 20 Theoretical pI 7.17
Enzyme 20 GO Classification
Function
  • binding
  • calcium ion binding
  • cation binding
  • ion binding
  • protein binding
  • transcription factor binding
Process
  • cell differentiation
  • cellular process
Component
  • cell
  • intracellular membrane-bound organelle
  • membrane
  • membrane-bound organelle
  • nucleus
  • organelle
Enzyme 20 General Function Not Available
Enzyme 20 Specific Function Catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus. M6P residues are required to bind to the M6P receptors (MPR), which mediate the vesicular transport of lysosomal enzymes to the endosomal/prelysosomal compartment
Enzyme 20 Pathways Not Available
Enzyme 20 Reactions Not Available
Enzyme 20 Pfam Domain Function
Enzyme 20 Signals
  • None
Enzyme 20 Transmembrane Regions
  • 22-42 1215-1235
Enzyme 20 Essentiality Not Available
Enzyme 20 GenBank ID Protein 74474848 Link Image
Enzyme 20 UniProtKB/Swiss-Prot ID Q3T906 Link Image
Enzyme 20 UniProtKB/Swiss-Prot Entry Name GNPTA_HUMAN Link Image
Enzyme 20 PDB ID Not Available
Enzyme 20 Cellular Location Not Available
Enzyme 20 Gene Sequence >3771 bp
ATGCTGTTCAAGCTCCTGCAGAGACAGACCTATACCTGCCTGTCCCACAGGTATGGGCTC
TACGTGTGCTTCTTGGGCGTCGTTGTCACCATCGTCTCCGCCTTCCAGTTCGGAGAGGTG
GTTCTGGAATGGAGCCGAGATCAATACCATGTTTTGTTTGATTCCTATAGAGACAATATT
GCTGGAAAGTCCTTTCAGAATCGGCTTTGTCTGCCCATGCCGATTGACGTTGTTTACACC
TGGGTGAATGGCACAGATCTTGAACTACTGAAGGAACTACAGCAGGTCAGAGAACAGATG
GAGGAGGAGCAGAAAGCAATGAGAGAAATCCTTGGGAAAAACACAACGGAACCTACTAAG
AAGAGTGAGAAGCAGTTAGAGTGTTTGCTAACACACTGCATTAAGGTGCCAATGCTTGTC
CTGGACCCAGCCCTGCCAGCCAACATCACCCTGAAGGACCTGCCATCTCTTTATCCTTCT
TTTCATTCTGCCAGTGACATTTTCAATGTTGCAAAACCAAAAAACCCTTCTACCAATGTC
TCAGTTGTTGTTTTTGACAGTACTAAGGATGTTGAAGATGCCCACTCTGGACTGCTTAAA
GGAAATAGCAGACAGACAGTATGGAGGGGCTACTTGACAACAGATAAAGAAGTCCCTGGA
TTAGTGCTAATGCAAGATTTGGCTTTCCTGAGTGGATTTCCACCAACATTCAAGGAAACA
AATCAACTAAAAACAAAATTGCCAGAAAATCTTTCCTCTAAAGTCAAACTGTTGCAGTTG
TATTCAGAGGCCAGTGTAGCGCTTCTAAAACTGAATAACCCCAAGGATTTTCAAGAATTG
AATAAGCAAACTAAGAAGAACATGACCATTGATGGAAAAGAACTGACCATAAGTCCTGCA
TATTTATTATGGGATCTGAGCGCCATCAGCCAGTCTAAGCAGGATGAAGACATCTCTGCC
AGTCGTTTTGAAGATAACGAAGAACTGAGGTACTCATTGCGATCTATCGAGAGGCATGCA
CCATGGGTTCGGAATATTTTCATTGTCACCAACGGGCAGATTCCATCCTGGCTGAACCTT
GACAATCCTCGAGTGACAATAGTAACACACCAGGATGTTTTTCGAAATTTGAGCCACTTG
CCTACCTTTAGTTCACCTGCTATTGAAAGTCACATTCATCGCATCGAAGGGCTGTCCCAG
AAGTTTATTTACCTAAATGATGATGTCATGTTTGGGAAGGATGTCTGGCCAGATGATTTT
TACAGTCACTCCAAAGGCCAGAAGGTTTATTTGACATGGCCTGTGCCAAACTGTGCCGAG
GGCTGCCCAGGTTCCTGGATTAAGGATGGCTATTGTGACAAGGCTTGTAATAATTCAGCC
TGCGATTGGGATGGTGGGGATTGCTCTGGAAACAGTGGAGGGAGTCGCTATATTGCAGGA
GGTGGAGGTACTGGGAGTATTGGAGTTGGACAGCCCTGGCAGTTTGGTGGAGGAATAAAC
AGTGTCTCTTACTGTAATCAGGGATGTGCGAATTCCTGGCTCGCTGATAAGTTCTGTGAC
CAAGCATGCAATGTCTTGTCCTGTGGGTTTGATGCTGGCGACTGTGGGCAAGATCATTTT
CATGAATTGTATAAAGTGATCCTTCTCCCAAACCAGACTCACTATATTATTCCAAAAGGT
GAATGCCTGCCTTATTTCAGCTTTGCAGAAGTAGCCAAAAGAGGAGTTGAAGGTGCCTAT
AGTGACAATCCAATAATTCGACATGCTTCTATTGCCAACAAGTGGAAAACCATCCACCTC
ATAATGCACAGTGGAATGAATGCCACCACAATACATTTTAATCTCACGTTTCAAAATACA
AACGATGAAGAGTTCAAAATGCAGATAACAGTGGAGGTGGACACAAGGGAGGGACCAAAA
CTGAATTCTACAGCCCAGAAGGGTTACGAAAATTTAGTTAGTCCCATAACACTTCTTCCA
GAGGCGGAAATCCTTTTTGAGGATATTCCCAAAGAAAAACGCTTCCCGAAGTTTAAGAGA
CATGATGTTAACTCAACAAGGAGAGCCCAGGAAGAGGTGAAAATTCCCCTGGTAAATATT
TCACTCCTTCCAAAAGACGCCCAGTTGAGTCTCAATACCTTGGATTTGCAACTGGAACAT
GGAGACATCACTTTGAAAGGATACAATTTGTCCAAGTCAGCCTTGCTGAGATCATTTCTG
ATGAACTCACAGCATGCTAAAATAAAAAATCAAGCTATAATAACAGATGAAACAAATGAC
AGTTTGGTGGCTCCACAGGAAAAACAGGTTCATAAAAGCATCTTGCCAAACAGCTTAGGA
GTGTCTGAAAGATTGCAGAGGTTGACTTTTCCTGCAGTGAGTGTAAAAGTGAATGGTCAT
GACCAGGGTCAGAATCCACCCCTGGACTTGGAGACCACAGCAAGATTTAGAGTGGAAACT
CACACCCAAAAAACCATAGGCGGAAATGTGACAAAAGAAAAGCCCCCATCTCTGATTGTT
CCACTGGAAAGCCAGATGACAAAAGAAAAGAAAATCACAGGGAAAGAAAAAGAGAACAGT
AGAATGGAGGAAAATGCTGAAAATCACATAGGCGTTACTGAAGTGTTACTTGGAAGAAAG
CTGCAGCATTACACAGATAGTTACTTGGGCTTTTTGCCATGGGAGAAAAAAAAGTATTTC
CAAGATCTTCTCGACGAAGAAGAGTCATTGAAGACACAATTGGCATACTTCACTGATAGC
AAAAATACTGGGAGGCAACTAAAAGATACATTTGCAGATTCCCTCAGATATGTAAATAAA
ATTCTAAATAGCAAGTTTGGATTCACATCGCGGAAAGTCCCTGCTCACATGCCTCACATG
ATTGACCGGATTGTTATGCAAGAACTGCAAGATATGTTCCCTGAAGAATTTGACAAGACG
TCATTTCACAAAGTGCGCCATTCTGAGGATATGCAGTTTGCCTTCTCTTATTTTTATTAT
CTCATGAGTGCAGTGCAGCCACTGAATATATCTCAAGTCTTTGATGAAGTTGATACAGAT
CAATCTGGTGTCTTGTCTGACAGAGAAATCCGAACACTGGCTACCAGAATTCACGAACTG
CCGTTAAGTTTGCAGGATTTGACAGGTCTGGAACACATGCTAATAAATTGCTCAAAAATG
CTTCCTGCTGATATCACGCAGCTAAATAATATTCCACCAACTCAGGAATCCTACTATGAT
CCCAACCTGCCACCGGTCACTAAAAGTCTAGTAACAAACTGTAAACCAGTAACTGACAAA
ATCCACAAAGCATATAAGGACAAAAACAAATATAGGTTTGAAATCATGGGAGAAGAAGAA
ATCGCTTTTAAAATGATTCGTACCAACGTTTCTCATGTGGTTGGCCAGTTGGATGACATA
AGAAAAAACCCTAGGAAGTTTGTTTGCCTGAATGACAACATTGACCACAATCATAAAGAT
GCTCAGACAGTGAAGGCTGTTCTCAGGGACTTCTATGAATCCATGTTCCCCATACCTTCC
CAATTTGAACTGCCAAGAGAGTATCGAAACCGTTTCCTTCATATGCATGAGCTGCAGGAA
TGGAGGGCTTATCGAGACAAATTGAAGTTTTGGACCCATTGTGTACTAGCAACATTGATT
ATGTTTACTATATTCTCATTTTTTGCTGAGCAGTTAATTGCACTTAAGCGGAAGATATTT
CCCAGAAGGAGGATACACAAAGAAGCTAGTCCCAATCGAATCAGAGTATAG
Enzyme 20 GenBank Gene ID AM085438 Link Image
Enzyme 20 GeneCard ID Q3T906 Link Image
Enzyme 20 GenAtlas ID GNPTAB Link Image
Enzyme 20 HGNC ID HGNC:29670 Link Image
Enzyme 20 Chromosome Location 12
Enzyme 20 Locus 12q23.2
Enzyme 20 SNPs SNPJam Report Link Image
Enzyme 20 General References
  1. Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed Link Image]
  2. Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed Link Image]
Enzyme 20 Metabolite References Not Available
Enzyme 21 [top]
Enzyme 21 ID 15261
Enzyme 21 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 21 Synonyms Not Available
Enzyme 21 Gene Name ALG14
Enzyme 21 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 21 Number of Residues 216
Enzyme 21 Molecular Weight 24151
Enzyme 21 Theoretical pI 9.16
Enzyme 21 GO Classification Not Available
Enzyme 21 General Function Not Available
Enzyme 21 Specific Function Not Available
Enzyme 21 Pathways Not Available
Enzyme 21 Reactions Not Available
Enzyme 21 Pfam Domain Function Not Available
Enzyme 21 Signals
  • None
Enzyme 21 Transmembrane Regions
  • None
Enzyme 21 Essentiality Not Available
Enzyme 21 GenBank ID Protein 158259813 Link Image
Enzyme 21 UniProtKB/Swiss-Prot ID A8K030 Link Image
Enzyme 21 UniProtKB/Swiss-Prot Entry Name A8K030_HUMAN Link Image
Enzyme 21 PDB ID Not Available
Enzyme 21 Cellular Location Not Available
Enzyme 21 Gene Sequence >651 bp
ATGGTGTGCGTTCTCGTTCTAGCTGCGGCCGCAGGAGCTGTGGCGGTTTTCCTAATCCTG
CGAATATGGGTAGTGCTTCGTTCCATGGACGTTACGCCCCGGGAGTCTCTCAGTATCTTG
GTAGTGGCTGGGTCCGGTGGGCATACCACTGAGATCCTGAGGCTGCTTGGGAGCTTGTCC
AATGCCTACTCACCTAGACATTATGTCATTGCTGACACTGATGAAATGAGTGCCAATAAA
ATAAATTCTTTTGAACTAGATCGAGCTGATAGAGACCCTAGTAACATGTATACCAAATAC
TACATTCACCGAATTCCAAGAAGCCGGGAGGTTCAGCAGTCCTGGCCCTCCACCGTTTTC
ACCACCTTGCACTCCATGTGGCTCTCCTTTCCCCTAATTCACAGGGTGAAGCCAGATTTG
GTGTTGTGTAACGGACCAGGAACATGTGTTCCTATCTGTGTATCTGCCCTTCTCCTTGGG
ATACTAGGAATAAAGAAAGTGATCATTGTCTACGTTGAAAGCATCTGCCGTGTAGAAACG
TTATCCATGTCCGGAAAGATTCTGTTTCATCTCTCAGATTACTTCATTGTTCAGTGGCCG
GCTCTGAAAGAAAAGTATCCCAAATCGGTGTACCTTGGGCGAATTGTTTGA
Enzyme 21 GenBank Gene ID AK289395 Link Image
Enzyme 21 GeneCard ID A8K030 Link Image
Enzyme 21 GenAtlas ID Not Available
Enzyme 21 HGNC ID Not Available
Enzyme 21 Chromosome Location Not Available
Enzyme 21 Locus Not Available
Enzyme 21 SNPs SNPJam Report Link Image
Enzyme 21 General References Not Available
Enzyme 21 Metabolite References Not Available
Enzyme 22 [top]
Enzyme 22 ID 15262
Enzyme 22 Name cDNA FLJ78031, highly similar to Homo sapiens beta3GnT6 beta-1,3-N- acetylglucosaminyltransferase 6 (HCG2018639)
Enzyme 22 Synonyms Not Available
Enzyme 22 Gene Name Not Available
Enzyme 22 Protein Sequence >cDNA FLJ78031, highly similar to Homo sapiens beta3GnT6 beta-1,3-N- acetylglucosaminyltransferase 6 (HCG2018639)
MAFPCRRSLTAKTLACLLVGVSFLALQQWFLQAPRSPREERSPQEETPEGPTDAPAADEP
PSELVPGPPCVANASANATADFEQLPARIQDFLRYRHCRHFPLLWDAPAKCAGGRGVFLL
LAVKSAPEHYERRELIRRTWGQERSYGGRPVRRLFLLGTPGPEDEARAERLAELVALEAR
EHGDVLQWAFADTFLNLTLKHLHLLDWLAARCPHARFLLSGDDDVFVHTANVVRFLQAQP
PGRHLFSGQLMEGSVPIRDSWSKYFVPPQLFPGSAYPVYCSGGGFLLSGPTARALRAAAR
HTPLFPIDDAYMGMCLERAGLAPSGHEGIRPFGVQLPGAQQSSFDPCMYRELLLVHRFAP
YEMLLMWKALHSPALSCDRGHRVS
Enzyme 22 Number of Residues 384
Enzyme 22 Molecular Weight 42748
Enzyme 22 Theoretical pI 7.76
Enzyme 22 GO Classification Not Available
Enzyme 22 General Function Not Available
Enzyme 22 Specific Function Not Available
Enzyme 22 Pathways Not Available
Enzyme 22 Reactions Not Available
Enzyme 22 Pfam Domain Function Not Available
Enzyme 22 Signals
  • None
Enzyme 22 Transmembrane Regions
  • None
Enzyme 22 Essentiality Not Available
Enzyme 22 GenBank ID Protein 158259007 Link Image
Enzyme 22 UniProtKB/Swiss-Prot ID A8K9Q8 Link Image
Enzyme 22 UniProtKB/Swiss-Prot Entry Name A8K9Q8_HUMAN Link Image
Enzyme 22 PDB ID Not Available
Enzyme 22 Cellular Location Not Available
Enzyme 22 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 22 GenBank Gene ID AK292773 Link Image
Enzyme 22 GeneCard ID A8K9Q8 Link Image
Enzyme 22 GenAtlas ID Not Available
Enzyme 22 HGNC ID Not Available
Enzyme 22 Chromosome Location Not Available
Enzyme 22 Locus Not Available
Enzyme 22 SNPs Not Available
Enzyme 22 General References Not Available
Enzyme 22 Metabolite References Not Available
Enzyme 23 [top]
Enzyme 23 ID 15263
Enzyme 23 Name UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (EC 5.1.3.14) (Glucosamine (UDP-N-acetyl)-2-epimerase/N- acetylmannosamine kinase, isoform CRA_a)
Enzyme 23 Synonyms Not Available
Enzyme 23 Gene Name GNE
Enzyme 23 Protein Sequence >UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (EC 5.1.3.14) (Glucosamine (UDP-N-acetyl)-2-epimerase/N- acetylmannosamine kinase, isoform CRA_a)
METYGYLQRESCFQGPHELYFKNLSKRNKQIMEKNGNNRKLRVCVATCNRADYSKLAPIM
FGIKTEPEFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVG
LALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHA
ITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDV
KSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKG
IEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGE
NVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCF
PPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLI
LQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHSTKLIQEWNSVDLRTPLSDTLH
LPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGH
LVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQ
AAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALS
SVQDVDVVVSDLVDPALLGAASMVLDYTTRRIY
Enzyme 23 Number of Residues 753
Enzyme 23 Molecular Weight 83067
Enzyme 23 Theoretical pI 6.93
Enzyme 23 GO Classification
Function
  • ATP binding
  • UDP-N-acetylglucosamine 2-epimerase activity
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • hexokinase activity
  • isomerase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide 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 metabolism
  • UDP-N-acetylglucosamine metabolism
  • alcohol metabolism
  • amine metabolism
  • amino sugar metabolism
  • carbohydrate biosynthesis
  • cellular metabolism
  • glucosamine metabolism
  • glucose catabolism
  • glucose metabolism
  • glycolysis
  • hexose metabolism
  • lipopolysaccharide biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • monosaccharide metabolism
  • nitrogen compound metabolism
  • physiological process
  • polysaccharide biosynthesis
Component
Enzyme 23 General Function Cell wall/membrane/envelope biogenesis
Enzyme 23 Specific Function Not Available
Enzyme 23 Pathways Not Available
Enzyme 23 Reactions
  • UDP-N-acetyl-D-glucosamine = UDP-N-acetyl-D-mannosamine [RN:R00420] ALL_REAC R00420
  • (other) R00414
Enzyme 23 Pfam Domain Function
Enzyme 23 Signals
  • None
Enzyme 23 Transmembrane Regions
  • None
Enzyme 23 Essentiality Not Available
Enzyme 23 GenBank ID Protein 150368575 Link Image
Enzyme 23 UniProtKB/Swiss-Prot ID A6PZH2 Link Image
Enzyme 23 UniProtKB/Swiss-Prot Entry Name A6PZH2_HUMAN Link Image
Enzyme 23 PDB ID Not Available
Enzyme 23 Cellular Location Not Available
Enzyme 23 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 23 GenBank Gene ID AM697708 Link Image
Enzyme 23 GeneCard ID A6PZH2 Link Image
Enzyme 23 GenAtlas ID Not Available
Enzyme 23 HGNC ID Not Available
Enzyme 23 Chromosome Location Not Available
Enzyme 23 Locus Not Available
Enzyme 23 SNPs SNPJam Report Link Image
Enzyme 23 General References Not Available
Enzyme 23 Metabolite References Not Available
Enzyme 24 [top]
Enzyme 24 ID 16538
Enzyme 24 Name cDNA, FLJ93080, highly similar to Homo sapiens UDP-N-acteylglucosamine pyrophosphorylase 1 (UAP1), mRNA (UDP-N-acteylglucosamine pyrophosphorylase 1, isoform CRA_a)
Enzyme 24 Synonyms Not Available
Enzyme 24 Gene Name UAP1
Enzyme 24 Protein Sequence >cDNA, FLJ93080, highly similar to Homo sapiens UDP-N-acteylglucosamine pyrophosphorylase 1 (UAP1), mRNA (UDP-N-acteylglucosamine pyrophosphorylase 1, isoform CRA_a)
MNINDLKLTLSKAGQEHLLRFWNELEEAQQVELYAELQAMNFEELNFFFQKAIEGFNQSS
HQKNVDARMEPVPREVLGSATRDQDQLQAWESEGLFQISQNKVAVLLLAGGQGTRLGVAY
PKGMYDVGLPSRKTLFQIQAERILKLQQVAEKYYGNKCIIPWYIMTSGRTMESTKEFFTK
HKYFGLKKENVIFFQQGMLPAMSFDGKIILEEKNKVSMAPDGNGGLYRALAAQNIVEDME
QRGIWSIHVYCVDNILVKVADPRFIGFCIQKGADCGAKVVEKTNPTEPVGVVCRVDGVYQ
VVEYSEISLATAQKRSSDGRLLFNAGNIANHFFTVPFLRDVVNVYEPQLQHHVAQKKIPY
VDTQGQLIKPDKPNGIKMEKFVFDIFQFAKKFVVYEVLREDEFSPLKNADSQNGKDNPTT
ARHALMSLHHCWVLNAGGHFIDENGSRLPAIPRLKDANDVPIQCEISPLISYAGEGLESY
VADKEFHAPLIIDENGVHELVKNGI
Enzyme 24 Number of Residues 505
Enzyme 24 Molecular Weight 57029
Enzyme 24 Theoretical pI 6.33
Enzyme 24 GO Classification
Function
  • catalytic activity
  • nucleotidyltransferase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • metabolism
  • physiological process
Component
Enzyme 24 General Function Not Available
Enzyme 24 Specific Function Not Available
Enzyme 24 Pathways Not Available
Enzyme 24 Reactions Not Available
Enzyme 24 Pfam Domain Function
Enzyme 24 Signals
  • None
Enzyme 24 Transmembrane Regions
  • None
Enzyme 24 Essentiality Not Available
Enzyme 24 GenBank ID Protein Not Available
Enzyme 24 UniProtKB/Swiss-Prot ID B2R6R8 Link Image
Enzyme 24 UniProtKB/Swiss-Prot Entry Name B2R6R8_HUMAN Link Image
Enzyme 24 PDB ID 1JV3 Link Image
Enzyme 24 PDB File Show
Enzyme 24 3D Structure
Enzyme 24 Cellular Location Not Available
Enzyme 24 Gene Sequence Not Available
Enzyme 24 GenBank Gene ID AK312685 Link Image
Enzyme 24 GeneCard ID B2R6R8 Link Image
Enzyme 24 GenAtlas ID Not Available
Enzyme 24 HGNC ID Not Available
Enzyme 24 Chromosome Location Not Available
Enzyme 24 Locus Not Available
Enzyme 24 SNPs SNPJam Report Link Image
Enzyme 24 General References Not Available
Enzyme 24 Metabolite References Not Available
Enzyme 25 [top]
Enzyme 25 ID 16544
Enzyme 25 Name Glycosyltransferase 28 domain containing 1, isoform CRA_b
Enzyme 25 Synonyms
  1. SubName: cDNA, FLJ92520, Homo sapiens uncharacterized hematopoietic stem/progenitor cellsprotein MDS031 (MDS031), mRNA
Enzyme 25 Gene Name GLT28D1
Enzyme 25 Protein Sequence >Glycosyltransferase 28 domain containing 1, isoform CRA_b
MKCVFVTVGTTSFDDLIACVSAPDSLQKIESLGYNRLILQIGRGTVVPEPFSTESFTLDV
YRYKDSLKEDIQKADLVISHAGAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEG
HLFYCTCSTLPGLLQSMDLSTLKCYPPGQPEKFSAFLDKVVGLQK
Enzyme 25 Number of Residues 165
Enzyme 25 Molecular Weight 18225
Enzyme 25 Theoretical pI 6.50
Enzyme 25 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 25 General Function Not Available
Enzyme 25 Specific Function Not Available
Enzyme 25 Pathways Not Available
Enzyme 25 Reactions Not Available
Enzyme 25 Pfam Domain Function
Enzyme 25 Signals
  • None
Enzyme 25 Transmembrane Regions
  • None
Enzyme 25 Essentiality Not Available
Enzyme 25 GenBank ID Protein Not Available
Enzyme 25 UniProtKB/Swiss-Prot ID B2R5L5 Link Image
Enzyme 25 UniProtKB/Swiss-Prot Entry Name B2R5L5_HUMAN Link Image
Enzyme 25 PDB ID Not Available
Enzyme 25 Cellular Location Not Available
Enzyme 25 Gene Sequence Not Available
Enzyme 25 GenBank Gene ID AK312229 Link Image
Enzyme 25 GeneCard ID B2R5L5 Link Image
Enzyme 25 GenAtlas ID Not Available
Enzyme 25 HGNC ID Not Available
Enzyme 25 Chromosome Location Not Available
Enzyme 25 Locus Not Available
Enzyme 25 SNPs SNPJam Report Link Image
Enzyme 25 General References Not Available
Enzyme 25 Metabolite References Not Available
Enzyme 26 [top]
Enzyme 26 ID 16545
Enzyme 26 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 26 Synonyms Not Available
Enzyme 26 Gene Name MGAT2
Enzyme 26 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 26 Number of Residues 447
Enzyme 26 Molecular Weight 51551
Enzyme 26 Theoretical pI 8.94
Enzyme 26 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 26 General Function Not Available
Enzyme 26 Specific Function Not Available
Enzyme 26 Pathways Not Available
Enzyme 26 Reactions Not Available
Enzyme 26 Pfam Domain Function
Enzyme 26 Signals
  • None
Enzyme 26 Transmembrane Regions
  • None
Enzyme 26 Essentiality Not Available
Enzyme 26 GenBank ID Protein Not Available
Enzyme 26 UniProtKB/Swiss-Prot ID B3KPC5 Link Image
Enzyme 26 UniProtKB/Swiss-Prot Entry Name B3KPC5_HUMAN Link Image
Enzyme 26 PDB ID Not Available
Enzyme 26 Cellular Location Not Available
Enzyme 26 Gene Sequence Not Available
Enzyme 26 GenBank Gene ID AK056167 Link Image
Enzyme 26 GeneCard ID B3KPC5 Link Image
Enzyme 26 GenAtlas ID Not Available
Enzyme 26 HGNC ID Not Available
Enzyme 26 Chromosome Location 14
Enzyme 26 Locus 14q21
Enzyme 26 SNPs SNPJam Report Link Image
Enzyme 26 General References Not Available
Enzyme 26 Metabolite References Not Available
Enzyme 27 [top]
Enzyme 27 ID 16546
Enzyme 27 Name cDNA, FLJ93340, Homo sapiens exostoses (multiple)-like 2 (EXTL2), mRNA (Exostoses (Multiple)-like 2, isoform CRA_a)
Enzyme 27 Synonyms Not Available
Enzyme 27 Gene Name EXTL2
Enzyme 27 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 27 Number of Residues 330
Enzyme 27 Molecular Weight 37466
Enzyme 27 Theoretical pI 9.24
Enzyme 27 GO Classification Not Available
Enzyme 27 General Function Not Available
Enzyme 27 Specific Function Not Available
Enzyme 27 Pathways Not Available
Enzyme 27 Reactions Not Available
Enzyme 27 Pfam Domain Function
Enzyme 27 Signals
  • None
Enzyme 27 Transmembrane Regions
  • None
Enzyme 27 Essentiality Not Available
Enzyme 27 GenBank ID Protein Not Available
Enzyme 27 UniProtKB/Swiss-Prot ID B2R795 Link Image
Enzyme 27 UniProtKB/Swiss-Prot Entry Name B2R795_HUMAN Link Image
Enzyme 27 PDB ID Not Available
Enzyme 27 Cellular Location Not Available
Enzyme 27 Gene Sequence Not Available
Enzyme 27 GenBank Gene ID AK312895 Link Image
Enzyme 27 GeneCard ID B2R795 Link Image
Enzyme 27 GenAtlas ID Not Available
Enzyme 27 HGNC ID Not Available
Enzyme 27 Chromosome Location Not Available
Enzyme 27 Locus Not Available
Enzyme 27 SNPs SNPJam Report Link Image
Enzyme 27 General References Not Available
Enzyme 27 Metabolite References Not Available
Enzyme 28 [top]
Enzyme 28 ID 16547
Enzyme 28 Name cDNA, FLJ93616, highly similar to Homo sapiens exostoses (multiple) 1 (EXT1), mRNA (Exostoses (Multiple) 1)
Enzyme 28 Synonyms Not Available
Enzyme 28 Gene Name EXT1
Enzyme 28 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 28 Number of Residues 746
Enzyme 28 Molecular Weight 86256
Enzyme 28 Theoretical pI 9.34
Enzyme 28 GO Classification
Function
Process
Component
  • cell
  • membrane
Enzyme 28 General Function Not Available
Enzyme 28 Specific Function Not Available
Enzyme 28 Pathways Not Available
Enzyme 28 Reactions Not Available
Enzyme 28 Pfam Domain Function
Enzyme 28 Signals
  • None
Enzyme 28 Transmembrane Regions
  • None
Enzyme 28 Essentiality Not Available
Enzyme 28 GenBank ID Protein Not Available
Enzyme 28 UniProtKB/Swiss-Prot ID B2R7V2 Link Image
Enzyme 28 UniProtKB/Swiss-Prot Entry Name B2R7V2_HUMAN Link Image
Enzyme 28 PDB ID Not Available
Enzyme 28 Cellular Location Not Available
Enzyme 28 Gene Sequence Not Available
Enzyme 28 GenBank Gene ID AK313129 Link Image
Enzyme 28 GeneCard ID B2R7V2 Link Image
Enzyme 28 GenAtlas ID Not Available
Enzyme 28 HGNC ID Not Available
Enzyme 28 Chromosome Location Not Available
Enzyme 28 Locus Not Available
Enzyme 28 SNPs SNPJam Report Link Image
Enzyme 28 General References Not Available
Enzyme 28 Metabolite References Not Available