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Human Metabolome Database Version 2.5

 

Showing metabocard for Cytidine monophosphate N-acetylneuraminic acid (HMDB01176)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:36
Accession Number HMDB01176
Secondary Accession Numbers HMDB01040
Common Name Cytidine monophosphate N-acetylneuraminic acid
Description A nucleoside monophosphate sugar which donates N-acetylneuraminic acid to the terminal sugar of a ganglioside or glycoprotein.
Synonyms
  1. CMP-N-acetylneuraminate
  2. CMP-N-acylneuraminate
  3. Cytidine Monophosphate N-Acetylneuraminate
  4. Cytidine Monophosphate N-Acetylneuraminic acid
  5. Cytidine 5'-monophosphate N-acetylneuraminic acid
  6. CMP-NeuNAc
Chemical IUPAC Name 5-acetylamino-2-[[5-(4-amino-2-oxo-pyrimidin-1-yl)-3,4-dihydroxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-4-hydroxy-6-(1,2,3-trihydroxypropyl)oxane-2-carboxylic acid
Chemical Formula C20H31N4O16P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Nucleosides and Nucleoside conjugates
Class
  • Nucleotides
Sub Class
  • Nucleotide monophosphates
Family
  • Mammalian Metabolite
Species
  • primary alcohol
  • secondary alcohol
  • 1,2-diol
  • primary amine
  • primary aromatic amine
  • carboxylic acid
  • secondary carboxylic acid amide
  • oxo(het)arene
  • phosphoric acid ester
  • aromatic compound
  • heterocyclic compound
Biofunction
  • Component of Aminosugars metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 614.451
Monoisotopic Molecular Weight 614.147278
Isomeric SMILES CC(=O)N[C@@H]1[C@@H](O)C[C@@](O[C@H]1[C@H](O)[C@H](O)CO)(OP(O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)N1C=CC(N)=NC1=O)C(O)=O
Canonical SMILES CC(=O)NC1C(O)CC(OC1C(O)C(O)CO)(OP(O)(=O)OCC1OC(C(O)C1O)N1C=CC(N)=NC1=O)C(O)=O
KEGG Compound ID C00128 Link Image
BioCyc ID CMP-N-ACETYL-NEURAMINATE Link Image
BiGG ID 33954 Link Image
Wikipedia Link Not Available
NuGOwiki Link HMDB01176 Link Image
Metagene Link HMDB01176 Link Image
METLIN ID 6057 Link Image
PubChem Compound 316 Link Image
PubChem Substance 2246 Link Image
ChEBI ID 16556 Link Image
CAS Registry Number 22-12-8
InChI Identifier InChI=1/C20H31N4O16P/c1-7(26)22-12-8(27)4-20(18(32)33,39-16(12)13(29)9(28)5-25)40-41(35,36)37-6-10-14(30)15(31)17(38-10)24-3-2-11(21)23-19(24)34/h2-3,8-10,12-17,25,27-31H,4-6H2,1H3,(H,22,26)(H,32,33)(H,35,36)(H2,21,23,34)/t8-,9+,10+,12+,13+,14+,15+,16+,17+,20+/m0/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 36.300003 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -2
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.70 [Predicted by ALOGPS]; -6.9 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
  • golgi apparatus
  • nucleus
Biofluid Location Not Available
Tissue Location Not Available
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Amino Sugar Metabolism SMP00045 Link Image map00520 Link Image
General References Not Available
Metabolic Enzymes
  1. CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3- sialyltransferase
  2. N-acylneuraminate cytidylyltransferase
  3. Lactosylceramide alpha-2,3-sialyltransferase
  4. CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
  5. CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
  6. cDNA FLJ77291, highly similar to Homo sapiens ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 (ST6GAL1), transcript variant 2, mRNA (ST6 beta-galactosamide alpha-2,6-sialyltranferase 1, isoform CRA_d)
  7. ST6 neuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide alpha- 2,6-sialyltransferase 4 (ST6 (Alpha-N-acetyl-neuraminyl-2,3-beta- galactosyl-1, 3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, isoform CRA_a)
  8. cDNA FLJ77944, highly similar to H.sapiens GD3 synthase mRNA (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1, isoform CRA_a)
  9. cDNA FLJ45393 fis, clone BRHIP3027105, highly similar to CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3- sialyltransferase (EC 2.4.99.-)
  10. ST3 beta-galactoside alpha-2,3-sialyltransferase 6, isoform CRA_a
Enzyme 1 [top]
Enzyme 1 ID 5439
Enzyme 1 Name CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3- sialyltransferase
Enzyme 1 Synonyms
  1. N-acetyllactosaminide alpha-2,3- sialyltransferase
  2. Gal beta-1,3(4GlcNAc alpha-2,3 sialyltransferase
  3. ST3N
  4. ST3GalIII
  5. Sialyltransferase 6
Enzyme 1 Gene Name ST3GAL3
Enzyme 1 Protein Sequence >CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3- sialyltransferase 
MGLLVFVRNLLLALCLFLVLGFLYYSAWKLHLLQWEEDSNSVVLSFDSAGQTLGSEYDRL
GFLLNLDSKLPAELATKYANFSEGACKPGYASALMTAIFPRFSKPAPMFLDDSFRKWARI
REFVPPFGIKGQDNLIKAILSVTKEYRLTPALDSLRCRRCIIVGNGGVLANKSLGSRIDD
YDIVVRLNSAPVKGFEKDVGSKTTLRITYPEGAMQRPEQYERDSLFVLAGFKWQDFKWLK
YIVYKERVSASDGFWKSVATRVPKEPPEIRILNPYFIQEAAFTLIGLPFNNGLMGRGNIP
TLGSVAVTMALHGCDEVAVAGFGYDMSTPNAPLHYYETVRMAAIKESWTHNIQREKEFLR
KLVKARVITDLSSGI
Enzyme 1 Number of Residues 375
Enzyme 1 Molecular Weight 42171
Enzyme 1 Theoretical pI 9.31
Enzyme 1 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta- 1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- or NeuAc-alpha- 2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3- GalNAc
Enzyme 1 Pathways
  • Glycosphingolipid biosynthesis - lactoseries (map00601 Link Image)
  • Keratan sulfate biosynthesis (map00533 Link Image)
Enzyme 1 Reactions
  • CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-21
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 388015 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q11203 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name SIAT6_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1128 bp 
ATGGGACTCTTGGTATTTGTGCGCAATCTGCTGCTAGCCCTCTGCCTCTTTCTGGTACTG
GGATTTTTGTATTATTCTGCGTGGAAGCTACACTTACTCCAGTGGGAGGAGGACTCCAAT
TCAGTGGTTCTTTCCTTTGACTCCGCTGGACAAACACTAGGCTCAGAGTATGATCGGTTG
GGCTTCCTCCTGAATCTGGACTCTAAACTGCCTGCTGAATTAGCCACCAAGTACGCAAAC
TTTTCAGAGGGAGCTTGCAAGCCTGGCTATGCTTCAGCCTTGATGACGGCCATCTTCCCC
CGGTTCTCCAAGCCAGCACCCATGTTCCTGGATGACTCCTTTCGCAAGTGGGCTAGAATC
CGGGAGTTCGTGCCGCCTTTTGGGATCAAAGGTCAAGACAATCTGATCAAAGCCATCTTG
TCAGTCACCAAAGAGTACCGCCTGACCCCTGCCTTGGACAGCCTCCGCTGCCGCCGCTGC
ATCATCGTGGGCAATGGAGGCGTTCTTGCCAACAAGTCTCTGGGGTCACGAATTGACGAC
TATGACATTGTGGTGAGACTGAATTCAGCACCAGTGAAAGGCTTTGAGAAGGACGTGGGC
AGCAAAACGACACTGCGCATCACCTACCCCGAGGGCGCCATGCAGCGGCCTGAGCAGTAC
GAGCGCGATTCTCTCTTTGTCCTCGCCGGCTTCAAGTGGCAGGACTTTAAGTGGTTGAAA
TACATCGTCTACAAGGAGAGAGTGAGTGCATCGGATGGCTTCTGGAAATCTGTGGCCACT
CGAGTGCCCAAGGAGCCCCCTGAGATTCGAATCCTCAACCCATATTTCATCCAGGAGGCC
GCCTTCACCCTCATTGGCCTGCCCTTCAACAATGGCCTCATGGGCCGGGGGAACATCCCT
ACCCTTGGCAGTGTGGCAGTGACCATGGCACTACACGGCTGTGACGAGGTGGCAGTCGCA
GGATTTGGCTATGACATGAGCACACCCAACGCACCCCTGCACTACTATGAGACCGTTCGC
ATGGCAGCCATCAAAGAGTCCTGGACGCACAATATCCAGCGAGAGAAAGAGTTTCTGCGG
AAGCTGGTGAAAGCTCGCGTCATCACTGATCTAAGCAGTGGCATCTGA
Enzyme 1 GenBank Gene ID L23768 Link Image
Enzyme 1 GeneCard ID ST3GAL3 Link Image
Enzyme 1 GenAtlas ID ST3GAL3 Link Image
Enzyme 1 HGNC ID HGNC:10866 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p34.1
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Kitagawa H, Paulson JC: Cloning and expression of human Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase. Biochem Biophys Res Commun. 1993 Jul 15;194(1):375-82. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 5636
Enzyme 2 Name N-acylneuraminate cytidylyltransferase
Enzyme 2 Synonyms
  1. CMP-N- acetylneuraminic acid synthetase
  2. CMP-NeuNAc synthetase
Enzyme 2 Gene Name CMAS
Enzyme 2 Protein Sequence >N-acylneuraminate cytidylyltransferase 
MDSVEKGAATSVSNPRGRPSRGRPPKLQRNSRGGQGRGVEKPPHLAALILARGGSKGIPL
KNIKHLAGVPLIGWVLRAALDSGAFQSVWVSTDHDEIENVAKQFGAQVHRRSSEVSKDSS
TSLDAIIEFLNYHNEVDIVGNIQATSPCLHPTDLQKVAEMIREEGYDSVFSVVRRHQFRW
SEIQKGVREVTEPLNLNPAKRPRRQDWDGELYENGSFYFAKRHLIEMGYLQGGKMAYYEM
RAEHSVDIDVDIDWPIAEQRVLRYGYFGKEKLKEIKLLVCNIDGCLTNGHIYVSGDQKEI
ISYDVKDAIGISLLKKSGIEVRLISERACSKQTLSSLKLDCKMEVSVSDKLAVVDEWRKE
MGLCWKEVAYLGNEVSDEECLKRVGLSGAPADACSTAQKAVGYICKCNGGRGAIREFAEH
ICLLMEKVNNSCQK
Enzyme 2 Number of Residues 434
Enzyme 2 Molecular Weight 48380
Enzyme 2 Theoretical pI 8.02
Enzyme 2 GO Classification
Function
—
Process
  • carbohydrate biosynthesis
  • lipopolysaccharide biosynthesis
  • macromolecule biosynthesis
  • macromolecule metabolism
  • metabolism
  • physiological process
  • polysaccharide biosynthesis
Component
—
Enzyme 2 General Function Not Available
Enzyme 2 Specific Function Catalyzes the activation of N-acetylneuraminic acid (NeuNAc) to cytidine 5'-monophosphate N-acetylneuraminic acid (CMP-NeuNAc), a substrate required for the addition of sialic acid. Has some activity toward NeuNAc, N-glycolylneuraminic acid (Neu5Gc) or 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN)
Enzyme 2 Pathways
Enzyme 2 Reactions
  • CTP + N-acylneuraminate = diphosphate + CMP-N-acylneuraminate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 22085790 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q8NFW8 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name NEUA_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1305 bp 
ATGGACTCGGTGGAGAAGGGGGCCGCCACCTCCGTCTCCAACCCGCGGGGGCGACCGTCC
CGGGGCCGGCCGCCGAAGCTGCAGCGCAACTCTCGCGGCGGCCAGGGCCGAGGTGTGGAG
AAGCCCCCGCACCTGGCAGCCCTAATTCTGGCCCGGGGAGGCAGCAAAGGCATCCCCCTG
AAGAACATTAAGCACCTGGCGGGGGTCCCGCTCATTGGCTGGGTCCTGCGTGCGGCCCTG
GATTCAGGGGCCTTCCAGAGTGTATGGGTTTCGACAGACCATGATGAAATTGAGAATGTG
GCCAAACAATTTGGTGCACAAGTTCATCGAAGAAGTTCTGAAGTTTCAAAAGACAGCTCT
ACCTCACTAGATGCCATCATAGAATTTCTTAATTATYATAATGAGGKTGACATTGTAGGA
AATATTCAAGCTACTTCTYCATGTTTACATCCTACTGATCTTCAAAAAGTTGCAGAAATG
ATTCGAGAAGAAGGATATGATTCTGKTTTCTCTGTTGTGAGACGCCATCAGTTTCGATGG
AGTGAAATTCAGAAAGGAGTTCGTGAAGTGACCGAACCTCTGAATTTAAATCCAGCTAAA
CGGCCTCGTCGACAAGACTGGGATGGAGAATTATATGAAAATGGCTCATTTTATTTTGCT
AAAAGACATTTGATAGAGATGGGTTACTTGCAGGGTGGAAAAATGGCATACTACGAAATG
CGAGCTGAACATAGTGTGGATATAGATGTGGATATTGATTGGCCTATTGCAGAGCAAAGA
GTATTAAGATATGGCTATTTTGGCAAAGAGAAGCTTAAGGAAATAAAACTTTTGGTTTGC
AATATTGATGGATGTCTCACCAATGGCCACATTTATGTATCAGGAGACCAAAAAGAAATA
ATATCTTATGATGTAAAAGATGCTATTGGGATAAGTTTATTAAAGAAAAGTGGTATTGAG
GTGAGGCTAATCTCAGAAAGGGCCTGTTCAAAGCAGACGCTGTCTTCTTTAAAACTGGAT
TGCAAAATGGAAGTCAGTGTATCAGACAAGCTAGCAGTTGTAGATGAATGGAGAAAAGAA
ATGGGCCTGTGCTGGAAAGAAGTGGCATATCTTGGAAATGAAGTGTCTGATGAAGAGTGC
TTGAAGAGAGTGGGCCTAAGTGGCGCTCCTGCTGATGCCTGTTCCTACGCCCAGAAGGCT
GTTGGATACATTTGCAAATGTAATGGTGGCCGTGGTGCCATCCGAGAATTTGCAGAGCAC
ATTTGCCTACTAATGGAAAAAGTTAATAATTCATGCCAAAAATAG
Enzyme 2 GenBank Gene ID AF397212 Link Image
Enzyme 2 GeneCard ID CMAS Link Image
Enzyme 2 GenAtlas ID CMAS Link Image
Enzyme 2 HGNC ID HGNC:18290 Link Image
Enzyme 2 Chromosome Location Not Available
Enzyme 2 Locus Not Available
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 6051
Enzyme 3 Name Lactosylceramide alpha-2,3-sialyltransferase
Enzyme 3 Synonyms
  1. CMP- NeuAc:lactosylceramide alpha-2,3-sialyltransferase
  2. Ganglioside GM3 synthase
  3. ST3Gal V
  4. Sialyltransferase 9
Enzyme 3 Gene Name ST3GAL5
Enzyme 3 Protein Sequence >Lactosylceramide alpha-2,3-sialyltransferase 
MRRPSLLLKDILKCTLLVFGVWILYILKLNYTTEECDMKKMHYVDPDHVKRAQKYAQQVL
QKECRPKFAKTSMALLFEHRYSVDLLPFVQKAPKDSEAESKYDPPFGFRKFSSKVQTLLE
LLPEHDLPEHLKAKTCRRCVVIGSGGILHGLELGHTLNQFDVVIRLNSAPVEGYSEHVGN
KTTIRMTYPEGAPLSDLEYYSNDLFVAVLFKSVDFNWLQAMVKKETLPFWVRLFFWKQVA
EKIPLQPKHFRILNPVIIKETAFDILQYSEPQSRFWGRDKNVPTIGVIAVVLATHLCDEV
SLAGFGYDLNQPRTPLHYFDSQCMAAMNFQTMHNVTTETKFLLKLVKEGVVKDLSGGIDR
EF
Enzyme 3 Number of Residues 362
Enzyme 3 Molecular Weight 41736
Enzyme 3 Theoretical pI 8.62
Enzyme 3 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 3 General Function Not Available
Enzyme 3 Specific Function Catalyzes the formation of ganglioside GM3 (alpha-N- acetylneuraminyl-2,3-beta-D-galactosyl-1, 4-beta-D- glucosylceramide)
Enzyme 3 Pathways
Enzyme 3 Reactions
  • CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • 1-32
Enzyme 3 Transmembrane Regions Not Available
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 3779139 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID Q9UNP4 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name SIAT9_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence >1089 bp 
ATGAGAAGGCCCAGCTTGTTATTAAAAGACATCCTCAAATGTACATTGCTTGTGTTTGGA
GTGTGGATCCTTTATATCCTCAAGTTAAATTATACTACTGAAGAATGTGACATGAAAAAA
ATGCATTATGTGGACCCTGACCGTGTAAAGAGAGCTCAGAAATATGCTCAGCAAGTCTTG
CAGAAGGAATGTCGTCCCAAGTTTGCCAAGACATCAATGGCGCTGTTATTTGAGCACAGG
TATAGCGTGGACTTACTCCCTTTTGTGCAGAAGGCCCCCAAAGACAGTGAAGCTGAGTCC
AAGTACGATCCTCCTTTTGGGTTCCGGAAGTTCTCCAGTAAAGTCCAGACCCTCTTGGAA
CTCTTGCCAGAGCACGACCTCCCTGAACACTTGAAAGCCAAGACCTGTCGGCGCTGTGTG
GTTATTGGAAGCGGAGGAATACTGCACGGATTAGAACTGGGCCACACCCTGAACCAGTTC
GATGTTGTGATAAGGTTAAACAGTGCACCAGTTGAGGGATATTCAGAACATGTTGGAAAT
AAAACTACTATAAGGATGACTTATCCAGAGGGCGCACCACTGTCTGACCTTGAATATTAT
TCCAATGACTTATTTGTTGCTGTTTTATTTAAGAGTGTTGATTTCAACTGGCTTCAAGCA
ATGGTAAAAAAGGAAACCCTGCCATTCTGGGTACGACTCTTCTTTTGGAAGCAGGTGGCA
GAAAAAATCCCACTGCAGCCAAAACATTTCAGGATTTTGAATCCAGTTATCATCAAAGAG
ACTGCCTTTGACATCCTTCAGTACTCAGAGCCTCAGTCAAGGTTCTGGGGCCGAGATAAG
AACGTCCCCACAATCGGTGTCATTGCCGTTGTCTTAGCCACACATCTGTGCGATGAAGTC
AGTTTGGCGGGTTTTGGATATGACCTCAATCAACCCAGAACACCTTTGCACTACTTCGAC
AGTCAATGCATGGCTGCTATGAACTTTCAGACCATGCATAATGTGACAACGGAAACCAAG
TTCCTCTTAAAGCTGGTCAAAGAGGGAGTGGTGAAAGATCTCAGTGGAGGCATTGATCGT
GAATTTTGA
Enzyme 3 GenBank Gene ID AB018356 Link Image
Enzyme 3 GeneCard ID ST3GAL5 Link Image
Enzyme 3 GenAtlas ID ST3GAL5 Link Image
Enzyme 3 HGNC ID HGNC:10872 Link Image
Enzyme 3 Chromosome Location 2
Enzyme 3 Locus 2p11.2
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Ishii A, Ohta M, Watanabe Y, Matsuda K, Ishiyama K, Sakoe K, Nakamura M, Inokuchi J, Sanai Y, Saito M: Expression cloning and functional characterization of human cDNA for ganglioside GM3 synthase. J Biol Chem. 1998 Nov 27;273(48):31652-5. [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 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 7696
Enzyme 4 Name CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
Enzyme 4 Synonyms
  1. Beta-galactoside alpha-2,3-sialyltransferase
  2. Alpha 2,3-ST
  3. Gal-NAc6S
  4. Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase
  5. ST3GalIA
  6. ST3O
  7. ST3GalA.1
  8. SIAT4-A
  9. ST3Gal I
  10. SIATFL
Enzyme 4 Gene Name ST3GAL1
Enzyme 4 Protein Sequence >CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 
MVTLRKRTLKVLTFLVLFIFLTSFFLNYSHTMVATTWFPKQMVLELSENLKRLIKHRPCT
CTHCIGQRKLSAWFDERFNQTMQPLLTAQNALLEDDTYRWWLRLQREKKPNNLNDTIKEL
FRVVPGNVDPMLEKRSVGCRRCAVVGNSGNLRESSYGPEIDSHDFVLRMNKAPTAGFEAD
VGTKTTHHLVYPESFRELGDNVSMILVPFKTIDLEWVVSAITTGTISHTYIPVPAKIRVK
QDKILIYHPAFIKYVFDNWLQGHGRYPSTGILSVIFSMHVCDEVDLYGFGADSKGNWHHY
WENNPSAGAFRKTGVHDADFESNVTATLASINKIRIFKGR
Enzyme 4 Number of Residues 340
Enzyme 4 Molecular Weight 39075
Enzyme 4 Theoretical pI 9.45
Enzyme 4 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function It may be responsible for the synthesis of the sequence NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found on sugar chains O- linked to Thr or Ser and also as a terminal sequence on certain gangliosides. SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values
Enzyme 4 Pathways
Enzyme 4 Reactions
  • CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • 1-31
Enzyme 4 Transmembrane Regions Not Available
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 522197 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID Q11201 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SIA4A_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >1023 bp 
ATGGTGACCCTGCGGAAGAGGACCCTGAAAGTCGTCACCTTCCTCGTGCTCTTCATCTTC
CTCACCTCCTTCTTCCTGAACTACTCCCACACCATGGTGGCCACCACCTGGTTCCCCAAG
CAGATGGTCCTGGAGCTCTCCGAGAACCTGAAGAGACTGATCAAGCACAGGCCTTGCACC
TGCACCCACTGCATCGGGCAGCGCAAGCTCTCGGCCTGGTTCGATGAGAGGTTCAACCAG
ACCATGCAGCCGCTGCTGACTGCCCAGAACGCGCTCTTGGAGGACGACACCTACCGATGG
TGGCTGAGGCTCCAGCGGGAGAAGAAGCCCAATAACTTGAATGACACCATCAAGGAGCTG
TTCAGAGTGGTGCCTGGGAATGTGGACCCTATGCTGGAGAAGAGGTCGGTGGGCTGCCGG
CGCTGCGCCGTTGTGGGCAACTCGGGCAACCTGAGGGAGTCTTCTTATGGGCCTGAGATA
GACAGTCACGACTTTGTCCTCAGGATGAACAAGGCGCCCACGGCAGGGTTTGAAGCTGAT
GTTGGGACCAAGACCACCCACCATCTGGTGTACCCTGAGAGCTTCCGGGAGCTGGGAGAT
AATGTCAGCATGATCCTGGTGCCCTTCAAGACCATCGACTTGGAGTGGGTGGTGAGCGCC
ATCACCACGGGCACCATTTCCCACACCTACATCCCGGTTCCTGCAAAGATCAGAGTGAAA
CAGGATAAGATCCTGATCTACCACCCAGCCTTCATCAAGTATGTCTTTGACAACTGGCTG
CAAGGGCACGGGCGATACCCATCTACCGGCATCCTCTCGGTCATCTTCTCAATGCATGTC
TGCGATGAGGTGGACTTGTACGGCTTCGGGGCAGACAGCAAAGGGAACTGGCACCACTAC
TGGGAGAACAACCCATCCGCGGGGGCTTTTCGCAAGACGGGGGTGCACGATGCAGACTTT
GAGTCTAACGTGACGGCCACCTTGGCCTCCATCAATAAAATCCGGATCTTCAAGGGGAGA
TGA
Enzyme 4 GenBank Gene ID L29555 Link Image
Enzyme 4 GeneCard ID ST3GAL1 Link Image
Enzyme 4 GenAtlas ID ST3GAL1 Link Image
Enzyme 4 HGNC ID HGNC:10862 Link Image
Enzyme 4 Chromosome Location 8
Enzyme 4 Locus 8q24.22
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Kitagawa H, Paulson JC: Differential expression of five sialyltransferase genes in human tissues. J Biol Chem. 1994 Jul 8;269(27):17872-8. [PubMed Link Image]
  2. Chang ML, Eddy RL, Shows TB, Lau JT: Three genes that encode human beta-galactoside alpha 2,3-sialyltransferases. Structural analysis and chromosomal mapping studies. Glycobiology. 1995 May;5(3):319-25. [PubMed Link Image]
  3. Shang J, Qiu R, Wang J, Liu J, Zhou R, Ding H, Yang S, Zhang S, Jin C: Molecular cloning and expression of Galbeta1,3GalNAc alpha2, 3-sialyltransferase from human fetal liver. Eur J Biochem. 1999 Oct;265(2):580-8. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 8660
Enzyme 5 Name CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase
Enzyme 5 Synonyms
  1. Beta-galactoside alpha-2,3-sialyltransferase
  2. Alpha 2,3-sialyltransferase IV
  3. Alpha 2,3-ST
  4. Gal-NAc6S
  5. STZ
  6. SIAT4-C
  7. ST3Gal III
  8. SAT-3
  9. ST-4
Enzyme 5 Gene Name ST3GAL4
Enzyme 5 Protein Sequence >CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 
MVSKSRWKLLAMLALVLVVMVWYSISREDRYIELFYFPIPEKKEPCLQGEAESKASKLFG
NYSRDQPIFLRLEDYFWVKTPSAYELPYGTKGSEDLLLRVLAITSSSIPKNIQSLRCRRC
VVVGNGHRLRNSSLGDAINKYDVVIRLNNAPVAGYEGDVGSKTTMRLFYPESAHFDPKVE
NNPDTLLVLVAFKAMDFHWIETILSDKKRVRKGFWKQPPLIWDVNPKQIRILNPFFMEIA
ADKLLSLPMQQPRKIKQKPTTGLLAITLALHLCDLVHIAGFGYPDAYNKKQTIHYYEQIT
LKSMAGSGHNVSQEALAIKRMLEMGAIKNLTSF
Enzyme 5 Number of Residues 333
Enzyme 5 Molecular Weight 38046
Enzyme 5 Theoretical pI 9.88
Enzyme 5 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 5 General Function Not Available
Enzyme 5 Specific Function It may catalyze the formation of the NeuAc-alpha-2,3- Gal-beta-1,3-GalNAc- or NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. It may be involved in the biosynthesis of the sialyl Lewis X determinant
Enzyme 5 Pathways Not Available
Enzyme 5 Reactions Not Available
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • 1-26
Enzyme 5 Transmembrane Regions
  • 9-26
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 431315 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q11206 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name SIA4C_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >999 bp 
ATGTGTCCTGCAGGCTGGAAGCTCCTGGCCATGTTGGCTCTGGTCCTGGTCGTCATGGTG
TGGTATTCCATCTCCCGGGAAGACAGGTACATCGAGCTTTTTTATTTTCCCATCCCAGAG
AAGAAGGAGCCGTGCCTCCAGGGTGAGGCAGAGAGCAAGGCCTCTAAGCTCTTTGGCAAC
TACTCCCGGGATCAGCCCATCTTCCTGCGGCTTGAGGATTATTTCTGGGTCAAGACGCCA
TCTGCTTACGAGCTGCCCTATGGGACCAAGGGGAGTGAGGATCTGCTCCTCCGGGTGCTA
GCCATCACCAGCTCCTCCATCCCCAAGAACATCCAGAGCCTCAGGTGCCGCCGCTGTGTG
GTCGTGGGGAACGGGCACCGGCTGCGGAACAGCTCACTGGGAGATGCCATCAACAAGTAC
GATGTGGTCATCAGATTGAACAATGCCCCAGTGGCTGGCTATGAGGGTGACGTGGGCTCC
AAGACCACCATGCGTCTCTTCTACCCTGAATCTGCCCACTTCGACCCCAAAGTAGAAAAC
AACCCAGACACACTCCTCGTCCTGGTAGCTTTCAAGGCAATGGACTTCCACTGGATTGAG
ACCATCCTGAGTGATAAGAAGCGGGTGCGAAAGGGTTTCTGGAAACAGCCTCCCCTCATC
TGGGATGTCAATCCTAAACAGATTCGGATTCTCAACCCCTTCTTCATGGAGATTGCAGCT
GACAAACTGCTGAGCCTGCCAATGCAACAGCCACGGAAGATTAAGCAGAAGCCCACCACG
GGCCTGTTGGCCATCACGCTGGCCCTCCACCTCTGTGACTTGGTGCACATTGCCGGCTTT
GGCTACCCAGACGCCTACAACAAGAAGCAGACCATTCACTACTATGAGCAGATCACGCTC
AAGTCCATGGCGGGGTCAGGCCATAATGTCTCCCAAGAGGCCCTGGCCATTAAGCGGATG
CTGGAGATGGGAGCTATCAAGAACCTCACGTCCTTCTGA
Enzyme 5 GenBank Gene ID L23767 Link Image
Enzyme 5 GeneCard ID ST3GAL4 Link Image
Enzyme 5 GenAtlas ID ST3GAL4 Link Image
Enzyme 5 HGNC ID HGNC:10864 Link Image
Enzyme 5 Chromosome Location 11
Enzyme 5 Locus 11q23-q24
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 General References
  1. Kitagawa H, Mattei MG, Paulson JC: Genomic organization and chromosomal mapping of the Gal beta 1,3GalNAc/Gal beta 1,4GlcNAc alpha 2,3-sialyltransferase. J Biol Chem. 1996 Jan 12;271(2):931-8. [PubMed Link Image]
  2. Kitagawa H, Paulson JC: Cloning of a novel alpha 2,3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups. J Biol Chem. 1994 Jan 14;269(2):1394-401. [PubMed Link Image]
  3. Sasaki K, Watanabe E, Kawashima K, Sekine S, Dohi T, Oshima M, Hanai N, Nishi T, Hasegawa M: Expression cloning of a novel Gal beta (1-3/1-4) GlcNAc alpha 2,3-sialyltransferase using lectin resistance selection. J Biol Chem. 1993 Oct 25;268(30):22782-7. [PubMed Link Image]
  4. Basu SS, Basu M, Li Z, Basu S: Characterization of two glycolipid: alpha 2-3sialyltransferases, SAT-3 (CMP-NeuAc:nLcOse4Cer alpha 2-3sialyltransferase) and SAT-4 (CMP-NeuAc:GgOse4Cer alpha 2-3sialyltransferase), from human colon carcinoma (Colo 205) cell line. Biochemistry. 1996 Apr 23;35(16):5166-74. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 15201
Enzyme 6 Name cDNA FLJ77291, highly similar to Homo sapiens ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 (ST6GAL1), transcript variant 2, mRNA (ST6 beta-galactosamide alpha-2,6-sialyltranferase 1, isoform CRA_d)
Enzyme 6 Synonyms Not Available
Enzyme 6 Gene Name ST6GAL1
Enzyme 6 Protein Sequence >cDNA FLJ77291, highly similar to Homo sapiens ST6 beta-galactosamide alpha-2,6-sialyltranferase 1 (ST6GAL1), transcript variant 2, mRNA (ST6 beta-galactosamide alpha-2,6-sialyltranferase 1, isoform CRA_d) 
MIHTNLKKKFSCCVLVFLLFAVICVWKEKKKGSYYDSFKLQTKEFQVLKSLGKLAMGSDS
QSVSSSSTQDPHRGRQTLGSLRGLAKAKPEASFQVWNKDSSSKNLIPRLQKIWKNYLSMN
KYKVSYKGPGPGIKFSAEALRCHLRDHVNVSMVEVTDFPFNTSEWEGYLPKESIRTKAGP
WGRCAVVSSAGSLKSSQLGREIDDHDAVLRFNGAPTANFQQDVGTKTTIRLMNSQLVTTE
KRFLKDSLYNEGILIVWDPSVYHSDIPKWYQNPDYNFFNNYKTYRKLHPNQPFYILKPQM
PWELWDILQEISPEEIQPNPPSSGMLGIIIMMTLCDQVDIYEFLPSKRKTDVCYYYQKFF
DSACTMGAYHPLLYEKNLVKHLNQGTDEDIYLLGKATLPGFRTIHC
Enzyme 6 Number of Residues 406
Enzyme 6 Molecular Weight 46605
Enzyme 6 Theoretical pI 9.35
Enzyme 6 GO Classification Not Available
Enzyme 6 General Function Not Available
Enzyme 6 Specific Function Not Available
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function Not Available
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • None
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 158259219 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID A8KA14 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name A8KA14_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1221 bp 
ATGATTCACACCAACCTGAAGAAAAAGTTCAGCTGCTGCGTCCTGGTCTTTCTTCTGTTT
GCAGTCATCTGTGTGTGGAAGGAAAAGAAGAAAGGGAGTTACTATGATTCCTTTAAATTG
CAAACCAAGGAATTCCAGGTGTTAAAGAGTCTGGGGAAATTGGCCATGGGGTCTGATTCC
CAGTCTGTATCCTCAAGCAGCACCCAGGACCCCCACAGGGGCCGCCAGACCCTCGGCAGT
CTCAGAGGCCTAGCCAAGGCCAAACCAGAGGCCTCCTTCCAGGTGTGGAACAAGGACAGC
TCTTCCAAAAACCTTATCCCTAGGCTGCAAAAGATCTGGAAGAATTACCTAAGCATGAAC
AAGTACAAAGTGTCCTACAAGGGGCCAGGACCAGGCATCAAGTTCAGTGCAGAGGCCCTG
CGCTGCCACCTCCGGGACCATGTGAATGTATCCATGGTAGAGGTCACAGATTTTCCCTTC
AATACCTCTGAATGGGAGGGTTATCTGCCCAAGGAGAGCATTAGGACCAAGGCTGGGCCT
TGGGGCAGGTGTGCTGTTGTGTCGTCAGCGGGATCTCTGAAGTCCTCCCAACTAGGCAGA
GAAATCGATGATCATGACGCAGTCCTGAGGTTTAATGGGGCACCCACAGCCAACTTCCAA
CAAGATGTGGGCACAAAAACTACCATTCGCCTGATGAACTCTCAGTTGGTTACCACAGAG
AAGCGCTTCCTCAAAGACAGTTTGTACAATGAAGGAATCCTAATTGTATGGGACCCATCT
GTATACCACTCAGATATCCCAAAGTGGTACCAGAATCCGGATTATAATTTCTTTAACAAC
TACAAGACTTATCGTAAGCTGCACCCCAATCAGCCCTTTTACATCCTCAAGCCCCAGATG
CCTTGGGAGCTATGGGACATTCTTCAAGAAATCTCCCCAGAAGAGATTCAGCCAAACCCC
CCATCCTCTGGGATGCTTGGTATCATCATCATGATGACGCTGTGTGACCAGGTGGATATT
TATGAGTTCCTCCCATCCAAGCGCAAGACTGACGTGTGCTACTACTACCAGAAGTTCTTC
GATAGTGCCTGCACGATGGGTGCCTACCACCCGCTGCTCTATGAGAAGAATTTGGTGAAG
CATCTCAACCAGGGCACAGATGAGGACATCTACCTGCTTGGAAAAGCCACACTGCCTGGC
TTCCGGACCATTCACTGCTAA
Enzyme 6 GenBank Gene ID AK292879 Link Image
Enzyme 6 GeneCard ID A8KA14 Link Image
Enzyme 6 GenAtlas ID Not Available
Enzyme 6 HGNC ID Not Available
Enzyme 6 Chromosome Location Not Available
Enzyme 6 Locus Not Available
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 General References Not Available
Enzyme 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 15202
Enzyme 7 Name ST6 neuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide alpha- 2,6-sialyltransferase 4 (ST6 (Alpha-N-acetyl-neuraminyl-2,3-beta- galactosyl-1, 3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, isoform CRA_a)
Enzyme 7 Synonyms Not Available
Enzyme 7 Gene Name ST6GALNAC4
Enzyme 7 Protein Sequence >ST6 neuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminide alpha- 2,6-sialyltransferase 4 (ST6 (Alpha-N-acetyl-neuraminyl-2,3-beta- galactosyl-1, 3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 4, isoform CRA_a) 
MKAPGRLVLIILCSVVFSAVYILLCCWAGLPLCLATCLDHHFPTGSRPTVPGPLHFSGYS
SVPDGKPLVREPCRSCAVVSSSGQMLGSGLGAEIDSAECVFRMNQAPTVGFEADVGQRST
LRVVSHTSVPLLLRNYSHYFQKARDTLYMVWGQGRHMDRVLGGRTYRTLLQLTRMYPGLQ
VYTFTERMMAYCDQIFQDETGKNRRQSGSFLSTGWFTMILALELCEEIVVYGMVSDSYCR
EKSHPSVPYHYFEKGRLDECQMYLAHEQAPRSAHRFITEKAVFSRWAKKRPIVFAHPSWR
TE
Enzyme 7 Number of Residues 302
Enzyme 7 Molecular Weight 34201
Enzyme 7 Theoretical pI 8.65
Enzyme 7 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 7 General Function Not Available
Enzyme 7 Specific Function Not Available
Enzyme 7 Pathways Not Available
Enzyme 7 Reactions Not Available
Enzyme 7 Pfam Domain Function
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 55958253 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID Q5T9D0 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name Q5T9D0_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 Gene Sequence >909 bp 
ATGAAGGCTCCGGGTCGGCTCGTGCTCATCATCCTGTGCTCCGTGGTCTTCTCTGCCGTC
TACATCCTCCTGTGCTGCTGGGCCGGCCTGCCCCTCTGCCTGGCCACCTGCCTGGACCAC
CACTTCCCCACAGGCTCCAGGCCCACTGTGCCGGGACCCCTGCACTTCAGTGGATATAGC
AGTGTGCCAGATGGGAAGCCGCTGGTCCGCGAGCCCTGCCGCAGCTGTGCCGTGGTGTCC
AGCTCCGGCCAAATGCTGGGCTCAGGCCTGGGTGCTGAGATCGACAGTGCCGAGTGCGTG
TTCCGCATGAACCAGGCGCCCACCGTGGGCTTTGAGGCGGATGTGGGCCAGCGCAGCACC
CTGCGTGTCGTCTCACACACAAGCGTGCCGCTGCTGCTGCGCAACTATTCACACTACTTC
CAGAAGGCCCGAGACACGCTCTACATGGTGTGGGGCCAGGGCAGGCACATGGACCGGGTG
CTCGGCGGCCGCACCTACCGCACGCTGCTGCAGCTCACCAGGATGTACCCCGGCCTGCAG
GTGTACACCTTCACGGAGCGCATGATGGCCTACTGCGACCAGATCTTCCAGGACGAGACG
GGCAAGAACCGGAGGCAGTCGGGCTCCTTCCTCAGCACCGGCTGGTTCACCATGATCCTC
GCGCTGGAGCTGTGTGAGGAGATCGTGGTCTATGGGATGGTCAGCGACAGCTACTGCAGG
GAGAAGAGCCACCCCTCAGTGCCTTACCACTACTTTGAGAAGGGCCGGCTAGATGAGTGT
CAGATGTACCTGGCACACGAGCAGGCGCCCCGAAGCGCCCACCGCTTCATCACTGAGAAG
GCGGTCTTCTCCCGCTGGGCCAAGAAGAGGCCCATCGTGTTCGCCCATCCGTCCTGGAGG
ACTGAGTAG
Enzyme 7 GenBank Gene ID AL157935 Link Image
Enzyme 7 GeneCard ID Q5T9D0 Link Image
Enzyme 7 GenAtlas ID ST6GALNAC4 Link Image
Enzyme 7 HGNC ID HGNC:17846 Link Image
Enzyme 7 Chromosome Location Not Available
Enzyme 7 Locus Not Available
Enzyme 7 SNPs SNPJam Report Link Image
Enzyme 7 General References Not Available
Enzyme 7 Metabolite References Not Available
Enzyme 8 [top]
Enzyme 8 ID 15203
Enzyme 8 Name cDNA FLJ77944, highly similar to H.sapiens GD3 synthase mRNA (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1, isoform CRA_a)
Enzyme 8 Synonyms Not Available
Enzyme 8 Gene Name ST8SIA1
Enzyme 8 Protein Sequence >cDNA FLJ77944, highly similar to H.sapiens GD3 synthase mRNA (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1, isoform CRA_a) 
MSPCGRARRQTSRGAMAVLAWKFPRTRLPMGASALCVVVLCWLYIFPVYRLPNEKEIVQG
VLQQGTAWRRNQTAARAFRKQMEDCCDPAHLFAMTKMNSPMGKSMWYDGEFLYSFTIDNS
TYSLFPQATPFQLPLKKCAVVGNGGILKKSGCGRQIDEANFVMRCNLPPLSSEYTKDVGS
KSQLVTANPSIIRQRFQNLLWSRKTFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLS
DVGANQTVLFANPNFLRSIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVAIYGFWPFSV
NMHEQPISHHYYDNVLPFSGFHAMPEEFLQLWYLHKIGALRMQLDPCEDTSLQPTS
Enzyme 8 Number of Residues 356
Enzyme 8 Molecular Weight 40519
Enzyme 8 Theoretical pI 9.61
Enzyme 8 GO Classification Not Available
Enzyme 8 General Function Not Available
Enzyme 8 Specific Function Not Available
Enzyme 8 Pathways Not Available
Enzyme 8 Reactions Not Available
Enzyme 8 Pfam Domain Function Not Available
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 158255318 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID A8K4H6 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name A8K4H6_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >1071 bp 
ATGAGCCCCTGCGGGCGGGCCCGGCGACAAACGTCCAGAGGGGCCATGGCTGTACTGGCG
TGGAAGTTCCCGCGGACCCGGCTGCCCATGGGAGCCAGTGCCCTCTGTGTCGTGGTCCTC
TGTTGGCTCTACATCTTCCCCGTCTACCGGCTGCCCAACGAGAAAGAGATCGTGCAGGGG
GTGCTGCAACAGGGCACGGCGTGGAGGAGGAACCAGACCGCGGCCAGAGCGTTCAGGAAA
CAAATGGAAGACTGCTGCGACCCTGCTCATCTCTTTGCTATGACTAAAATGAATTCCCCT
ATGGGGAAGAGCATGTGGTATGACGGGGAGTTTTTATACTCATTCACCATTGACAATTCA
ACTTACTCTCTCTTCCCACAGGCAACCCCATTCCAGCTGCCATTGAAGAAATGCGCGGTG
GTGGGAAATGGTGGGATTCTGAAGAAGAGTGGCTGTGGCCGTCAAATAGATGAAGCAAAT
TTTGTCATGCGATGCAATCTCCCTCCTTTGTCAAGTGAATACACTAAGGATGTTGGATCC
AAAAGTCAGTTAGTGACAGCTAATCCCAGCATAATTCGGCAAAGGTTTCAGAACCTTCTG
TGGTCCAGAAAGACATTTGTGGACAACATGAAAATCTATAACCACAGTTACATCTACATG
CCTGCCTTTTCTATGAAGACAGGAACAGAGCCATCTTTGAGGGTTTATTATACACTGTCA
GATGTTGGTGCCAATCAAACAGTGCTGTTTGCCAACCCCAACTTTCTGCGTAGCATTGGA
AAGTTCTGGAAAAGTAGAGGAATCCATGCCAAGCGCCTGTCCACAGGACTTTTTCTGGTG
AGCGCAGCTCTGGGTCTCTGTGAAGAGGTGGCCATCTATGGCTTCTGGCCCTTCTCTGTG
AATATGCATGAGCAGCCCATCAGCCACCACTACTATGACAACGTCTTACCCTTTTCTGGC
TTCCATGCCATGCCCGAGGAATTTCTCCAACTCTGGTATCTTCATAAAATCGGTGCACTG
AGAATGCAGCTGGACCCATGTGAAGATACCTCACTCCAGCCCACTTCCTAG
Enzyme 8 GenBank Gene ID AK290941 Link Image
Enzyme 8 GeneCard ID A8K4H6 Link Image
Enzyme 8 GenAtlas ID Not Available
Enzyme 8 HGNC ID Not Available
Enzyme 8 Chromosome Location 12
Enzyme 8 Locus 12p12.1-p11.2
Enzyme 8 SNPs SNPJam Report Link Image
Enzyme 8 General References Not Available
Enzyme 8 Metabolite References Not Available
Enzyme 9 [top]
Enzyme 9 ID 16481
Enzyme 9 Name cDNA FLJ45393 fis, clone BRHIP3027105, highly similar to CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3- sialyltransferase (EC 2.4.99.-)
Enzyme 9 Synonyms Not Available
Enzyme 9 Gene Name Not Available
Enzyme 9 Protein Sequence >cDNA FLJ45393 fis, clone BRHIP3027105, highly similar to CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3- sialyltransferase (EC 2.4.99.-) 
MKCSLRVWFLSVAFLLVFIMSLLFTYSHHSMATLPYLDSGALDGTHRVKLVPGYAGLQRL
SKERLSGKSCACRRCMGDAGASDWFDSHFDGNISPVWTRENMDLPPDVQRWWMMLQPQFK
SHNTNEVLEKLFQIVPGENPYRFRDPHQCRRCAVVGNSGNLRGSGYGQDVDGHNFIMRMN
QAPTVGFEQDVGSRTTHHFMYPESAKNLPANVSFVLVPFKVQDLLWIASALSTGQIRFTY
APVKSFLRVDKEKVQIYNPAFFKYIHDRWTEHHGRYPSTGMLVLFFALHVCDEVNVYGFG
ADSRGNWHHYWENNRYAGEFRKTGVHDADFEAHIIDMLAKASKIEVYRGN
Enzyme 9 Number of Residues 350
Enzyme 9 Molecular Weight 40188
Enzyme 9 Theoretical pI 8.47
Enzyme 9 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 9 General Function Not Available
Enzyme 9 Specific Function Not Available
Enzyme 9 Pathways Not Available
Enzyme 9 Reactions Not Available
Enzyme 9 Pfam Domain Function
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein Not Available
Enzyme 9 UniProtKB/Swiss-Prot ID B3KXG9 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name B3KXG9_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence Not Available
Enzyme 9 GenBank Gene ID AK127322 Link Image
Enzyme 9 GeneCard ID B3KXG9 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location Not Available
Enzyme 9 Locus Not Available
Enzyme 9 SNPs Not Available
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 16482
Enzyme 10 Name ST3 beta-galactoside alpha-2,3-sialyltransferase 6, isoform CRA_a
Enzyme 10 Synonyms
  1. SubName: cDNA, FLJ96071, Homo sapiens alpha2,3-sialyltransferase (ST3GALVI), mRNA
Enzyme 10 Gene Name ST3GAL6
Enzyme 10 Protein Sequence >ST3 beta-galactoside alpha-2,3-sialyltransferase 6, isoform CRA_a 
MRGYLVAIFLSAVFLYYVLHCILWGTNVYWVAPVEMKRRNKIQPCLSKPAFASLLRFHQF
HPFLCAADFRKIASLYGSDKFDLPYGMRTSAEYFRLALSKLQSCDLFDEFDNIPCKKCVV
VGNGGVLKNKTLGEKIDSYDVIIRMNNGPVLGHEEEVGRRTTFRLFYPESVFSDPIHNDP
NTTVILTAFKPHDLRWLLELLMGDKINTNGFWKKPALNLIYKPYQIRILDPFIIRTAAYE
LLHFPKVFPKNQKPKHPTTGIIAITLAFYICHEVHLAGFKYNFSDLKSPLHYYGNATMSL
MNKNAYHNVTAEQLFLKDIIEKNLVINLTQD
Enzyme 10 Number of Residues 331
Enzyme 10 Molecular Weight 38214
Enzyme 10 Theoretical pI 9.30
Enzyme 10 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • biopolymer metabolism
  • biopolymer modification
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein amino acid glycosylation
  • protein modification
Component
  • cell
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane
Enzyme 10 General Function Not Available
Enzyme 10 Specific Function Not Available
Enzyme 10 Pathways Not Available
Enzyme 10 Reactions Not Available
Enzyme 10 Pfam Domain Function
Enzyme 10 Signals
  • None
Enzyme 10 Transmembrane Regions
  • None
Enzyme 10 Essentiality Not Available
Enzyme 10 GenBank ID Protein Not Available
Enzyme 10 UniProtKB/Swiss-Prot ID B2RCH2 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name B2RCH2_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence Not Available
Enzyme 10 GenBank Gene ID AK315111 Link Image
Enzyme 10 GeneCard ID B2RCH2 Link Image
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID Not Available
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs SNPJam Report Link Image
Enzyme 10 General References Not Available
Enzyme 10 Metabolite References Not Available