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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 Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum 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. Type 2 lactosamine alpha-2,3-sialyltransferase
  5. CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
  6. CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
  7. 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)
  8. 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)
  9. cDNA FLJ77944, highly similar to H.sapiens GD3 synthase mRNA (ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1, isoform CRA_a)
  10. cDNA FLJ45393 fis, clone BRHIP3027105, highly similar to CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3- sialyltransferase (EC 2.4.99.-)
  11. 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. Beta-galactoside alpha-2,3-sialyltransferase 3
  2. Alpha 2,3-ST 3
  3. Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase
  4. N-acetyllactosaminide alpha-2,3-sialyltransferase
  5. ST3Gal III
  6. ST3GalIII
  7. ST3N
  8. 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 42170.5
Enzyme 1 Theoretical pI 9.31
Enzyme 1 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 1 General Function Involved in sialyltransferase activity
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 [RN:R04596]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • None
Enzyme 1 Transmembrane Regions
  • 9-28
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 5454060 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 NM_006279.2 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]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 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 synthase
  2. CMP-NeuNAc synthase
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 48378.8
Enzyme 2 Theoretical pI 8.02
Enzyme 2 GO Classification
Function
Process
  • lipid biosynthetic process
  • lipid metabolic process
  • lipopolysaccharide biosynthetic process
  • metabolic process
  • primary metabolic process
Component
Enzyme 2 General Function Involved in lipopolysaccharide biosynthetic process
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 [RN:R02599]
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 8515843 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 1QWJ Link Image
Enzyme 2 PDB File Show
Enzyme 2 3D Structure
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1305 bp
ATGGACTCGGTGGAGAAGGGGGCCGCCACCTCCGTCTCCAACCCGCGGGGGCGACCGTCC
CGGGGCCGGCCGCCGAAGCTGCAGCGCAACTCTCGCGGCGGCCAGGGCCGAGGTGTGGAG
AAGCCCCCGCACCTGGCAGCCCTAATTCTGGCCCGGGGAGGCAGCAAAGGCATCCCCCTG
AAGAACATTAAGCACCTGGCGGGGGTCCCGCTCATTGGCTGGGTCCTGCGTGCGGCCCTG
GATTCAGGGGCCTTCCAGAGTGTATGGGTTTCGACAGACCATGATGAAATTGAGAATGTG
GCCAAACAATTTGGTGCACAAGTTCATCGAAGAAGTTCTGAAGTTTCAAAAGACAGCTCT
ACCTCACTAGATGCCATCATAGAATTTCTTAATTATCATAATGAGGTTGACATTGTAGGA
AATATTCAAGCTACTTCTCCATGTTTACATCCTACTGATCTTCAAAAAGTTGCAGAAATG
ATTCGAGAAGAAGGATATGATTCTGTTTTCTCTGTTGTGAGACGCCATCAGTTTCGATGG
AGTGAAATTCAGAAAGGAGTTCGTGAAGTGACCGAACCTCTGAATTTAAATCCAGCTAAA
CGGCCTCGTCGACAAGACTGGGATGGAGAATTATATGAAAATGGCTCATTTTATTTTGCT
AAAAGACATTTGATAGAGATGGGTTACTTGCAGGGTGGAAAAATGGCATACTACGAAATG
CGAGCTGAACATAGTGTGGATATAGATGTGGATATTGATTGGCCTATTGCAGAGCAAAGA
GTATTAAGATATGGCTATTTTGGCAAAGAGAAGCTTAAGGAAATAAAACTTTTGGTTTGC
AATATTGATGGATGTCTCACCAATGGCCACATTTATGTATCAGGAGACCAAAAAGAAATA
ATATCTTATGATGTAAAAGATGCTATTGGGATAAGTTTATTAAAGAAAAGTGGTATTGAG
GTGAGGCTAATCTCAGAAAGGGCCTGTTCAAAGCAGACGCTGTCTTCTTTAAAACTGGAT
TGCAAAATGGAAGTCAGTGTATCAGACAAGCTAGCAGTTGTAGATGAATGGAGAAAAGAA
ATGGGCCTGTGCTGGAAAGAAGTGGCATATCTTGGAAATGAAGTGTCTGATGAAGAGTGC
TTGAAGAGAGTGGGCCTAAGTGGCGCTCCTGCTGATGCCTGTTCTACTGCCCAGAAGGCT
GTTGGATACATTTGCAAATGTAATGGTGGCCGTGGTGCCATCCGAGAATTTGCAGAGCAC
ATTTGCCTACTAATGGAAAAGGTTAATAATTCATGCCAAAAATAG
Enzyme 2 GenBank Gene ID AF271388 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 1
Enzyme 2 Locus 12p12.1
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Lawrence SM, Huddleston KA, Tomiya N, Nguyen N, Lee YC, Vann WF, Coleman TA, Betenbaugh MJ: Cloning and expression of human sialic acid pathway genes to generate CMP-sialic acids in insect cells. Glycoconj J. 2001 Mar;18(3):205-13. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed Link Image]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
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. ST3GalV
  5. Sialyltransferase 9
Enzyme 3 Gene Name ST3GAL5
Enzyme 3 Protein Sequence >Lactosylceramide alpha-2,3-sialyltransferase
MRTKAAGCAERRPLQPRTEAAAAPAGRAMPSEYTYVKLRSDCSRPSLQWYTRAQSKMRRP
SLLLKDILKCTLLVFGVWILYILKLNYTTEECDMKKMHYVDPDHVKRAQKYAQQVLQKEC
RPKFAKTSMALLFEHRYSVDLLPFVQKAPKDSEAESKYDPPFGFRKFSSKVQTLLELLPE
HDLPEHLKAKTCRRCVVIGSGGILHGLELGHTLNQFDVVIRLNSAPVEGYSEHVGNKTTI
RMTYPEGAPLSDLEYYSNDLFVAVLFKSVDFNWLQAMVKKETLPFWVRLFFWKQVAEKIP
LQPKHFRILNPVIIKETAFDILQYSEPQSRFWGRDKNVPTIGVIAVVLATHLCDEVSLAG
FGYDLNQPRTPLHYFDSQCMAAMNFQTMHNVTTETKFLLKLVKEGVVKDLSGGIDREF
Enzyme 3 Number of Residues 418
Enzyme 3 Molecular Weight 47989.4
Enzyme 3 Theoretical pI 9.32
Enzyme 3 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 3 General Function Involved in sialyltransferase activity
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-glucosyl-(11)-ceramide = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D- glucosyl-(11)-ceramide [RN:R03488 R05937]
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • 62-82
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 109633044 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 >1257 bp
ATGCGGACGAAGGCGGCGGGCTGCGCGGAGCGGCGTCCCCTGCAGCCGCGGACCGAGGCA
GCGGCGGCACCTGCCGGCCGAGCAATGCCAAGTGAGTACACCTATGTGAAACTGAGAAGT
GATTGCTCGAGGCCTTCCCTGCAATGGTACACCCGAGCTCAAAGCAAGATGAGAAGGCCC
AGCTTGTTATTAAAAGACATCCTCAAATGTACATTGCTTGTGTTTGGAGTGTGGATCCTT
TATATCCTCAAGTTAAATTATACTACTGAAGAATGTGACATGAAAAAAATGCATTATGTG
GACCCTGACCATGTAAAGAGAGCTCAGAAATATGCTCAGCAAGTCTTGCAGAAGGAATGT
CGTCCCAAGTTTGCCAAGACATCAATGGCGCTGTTATTTGAGCACAGGTATAGCGTGGAC
TTACTCCCTTTTGTGCAGAAGGCCCCCAAAGACAGTGAAGCTGAGTCCAAGTACGATCCT
CCTTTTGGGTTCCGGAAGTTCTCCAGTAAAGTCCAGACCCTCTTGGAACTCTTGCCAGAG
CACGACCTCCCTGAACACTTGAAAGCCAAGACCTGTCGGCGCTGTGTGGTTATTGGAAGC
GGAGGAATACTGCACGGATTAGAACTGGGCCACACCCTGAACCAGTTCGATGTTGTGATA
AGGTTAAACAGTGCACCAGTTGAGGGATATTCAGAACATGTTGGAAATAAAACTACTATA
AGGATGACTTATCCAGAGGGCGCACCACTGTCTGACCTTGAATATTATTCCAATGACTTA
TTTGTTGCTGTTTTATTTAAGAGTGTTGATTTCAACTGGCTTCAAGCAATGGTAAAAAAG
GAAACCCTGCCATTCTGGGTACGACTCTTCTTTTGGAAGCAGGTGGCAGAAAAAATCCCA
CTGCAGCCAAAACATTTCAGGATTTTGAATCCAGTTATCATCAAAGAGACTGCCTTTGAC
ATCCTTCAGTACTCAGAGCCTCAGTCAAGGTTCTGGGGCCGAGATAAGAACGTCCCCACA
ATCGGTGTCATTGCCGTTGTCTTAGCCACACATCTGTGCGATGAAGTCAGTTTGGCGGGT
TTTGGATATGACCTCAATCAACCCAGAACACCTTTGCACTACTTCGACAGTCAATGCATG
GCTGCTATGAACTTTCAGACCATGCATAATGTGACAACGGAAACCAAGTTCCTCTTAAAG
CTGGTCAAAGAGGGAGTGGTGAAAGATCTCAGTGGAGGCATTGATCGTGAATTTTGA
Enzyme 3 GenBank Gene ID NM_003896.3 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. Berselli P, Zava S, Sottocornola E, Milani S, Berra B, Colombo I: Human GM3 synthase: a new mRNA variant encodes an NH2-terminal extended form of the protein. Biochim Biophys Acta. 2006 Jul;1759(7):348-58. Epub 2006 Jul 21. [PubMed Link Image]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  4. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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]
  7. Simpson MA, Cross H, Proukakis C, Priestman DA, Neville DC, Reinkensmeier G, Wang H, Wiznitzer M, Gurtz K, Verganelaki A, Pryde A, Patton MA, Dwek RA, Butters TD, Platt FM, Crosby AH: Infantile-onset symptomatic epilepsy syndrome caused by a homozygous loss-of-function mutation of GM3 synthase. Nat Genet. 2004 Nov;36(11):1225-9. Epub 2004 Oct 24. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 6052
Enzyme 4 Name Type 2 lactosamine alpha-2,3-sialyltransferase
Enzyme 4 Synonyms
  1. CMP-NeuAc:beta-galactoside alpha-2,3-sialyltransferase VI
  2. ST3Gal VI
  3. ST3GalVI
  4. Sialyltransferase 10
Enzyme 4 Gene Name ST3GAL6
Enzyme 4 Protein Sequence >Type 2 lactosamine alpha-2,3-sialyltransferase
MRGYLVAIFLSAVFLYYVLHCILWGTNVYWVAPVEMKRRNKIQPCLSKPAFASLLRFHQF
HPFLCAADFRKIASLYGSDKFDLPYGMRTSAEYFRLALSKLQSCDLFDEFDNIPCKKCVV
VGNGGVLKNKTLGEKIDSYDVIIRMNNGPVLGHEEEVGRRTTFRLFYPESVFSDPIHNDP
NTTVILTAFKPHDLRWLLELLMGDKINTNGFWKKPALNLIYKPYQIRILDPFIIRTAAYE
LLHFPKVFPKNQKPKHPTTGIIAITLAFYICHEVHLAGFKYNFSDLKSPLHYYGNATMSL
MNKNAYHNVTAEQLFLKDIIEKNLVINLTQD
Enzyme 4 Number of Residues 331
Enzyme 4 Molecular Weight 38213.3
Enzyme 4 Theoretical pI 9.30
Enzyme 4 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 4 General Function Involved in sialyltransferase activity
Enzyme 4 Specific Function Involved in the synthesis of sialyl-paragloboside, a precursor of sialyl-Lewis X determinant. Has a alpha-2,3- sialyltransferase activity toward Gal-beta1,4-GlcNAc structure on glycoproteins and glycolipids. Has a restricted substrate specificity, it utilizes Gal-beta1,4-GlcNAc on glycoproteins, and neolactotetraosylceramide and neolactohexaosylceramide, but not lactotetraosylceramide, lactosylceramide or asialo-GM1
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • 5-25
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein Not Available
Enzyme 4 UniProtKB/Swiss-Prot ID Q9Y274 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name SIA10_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >996 bp
ATGAGAGGGTATCTTGTGGCCATATTCCTGAGTGCTGTCTTCCTCTATTATGTACTGCAT
TGCATATTATGGGGAACGAATGTCTATTGGGTGGCACCTGTGGAAATGAAACGGAGAAAT
AAGATCCAGCCTTGTTTATCAAAGCCAGCTTTTGCCTCTCTGCTGAGGTTTCATCAGTTT
CACCCTTTTCTGTGTGCGGCTGATTTTAGAAAGATTGCTTCCTTGTATGGTAGCGATAAG
TTTGATTTGCCCTATGGGATGAGAACATCAGCGGAATATTTTCGACTTGCTCTTTCAAAA
CTGCAGAGTTGTGATCTCTTTGATGAGTTTGACAACATACCCTGTAAAAAGTGTGTGGTG
GTTGGTAATGGAGGAGTTTTGAAGAATAAGACATTAGGAGAAAAAATCGACTCCTATGAT
GTAATAATAAGAATGAATAATGGTCCTGTTTTAGGACATGAAGAAGAAGTTGGGAGAAGG
ACAACCTTCCGACTTTTTTATCCAGAATCTGTTTTTTCAGATCCTATTCACAATGACCCT
AATACGACAGTGATTCTCACTGCTTTTAAGCCACATGATTTAAGGTGGCTGTTGGAATTG
TTGATGGGTGACAAAATAAACACTAATGGTTTTTGGAAGAAACCAGCCTTAAACCTGATT
TATAAACCTTATCAAATCCGAATATTAGATCCTTTCATTATCAGAACAGCAGCTTATGAA
CTGCTTCATTTTCCAAAAGTGTTTCCCAAAAATCAGAAACCTAAACACCCAACAACAGGA
ATTATTGCCATCACATTGGCGTTTTACATATGTCACGAAGTTCACCTAGCTGGTTTTAAA
TACAACTTTTCTGACCTCAAGAGTCCTTTGCACTACTATGGGAATGCCACCATGTCTTTG
ATGAATAAGAACGCGTATCACAATGTGACTGCAGAGCAGCTCTTTTTGAAGGACATTATA
GAAAAAAACCTCGTAATCAACTTGACTCAAGATTGA
Enzyme 4 GenBank Gene ID AB022918 Link Image
Enzyme 4 GeneCard ID ST3GAL6 Link Image
Enzyme 4 GenAtlas ID ST3GAL6 Link Image
Enzyme 4 HGNC ID HGNC:18080 Link Image
Enzyme 4 Chromosome Location 3
Enzyme 4 Locus 3q12.1
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References
  1. Okajima T, Fukumoto S, Miyazaki H, Ishida H, Kiso M, Furukawa K, Urano T, Furukawa K: Molecular cloning of a novel alpha2,3-sialyltransferase (ST3Gal VI) that sialylates type II lactosamine structures on glycoproteins and glycolipids. J Biol Chem. 1999 Apr 23;274(17):11479-86. [PubMed Link Image]
  2. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed Link Image]
Enzyme 4 Metabolite References Not Available
Enzyme 5 [top]
Enzyme 5 ID 7696
Enzyme 5 Name CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
Enzyme 5 Synonyms
  1. Alpha 2,3-ST 1
  2. Beta-galactoside alpha-2,3-sialyltransferase 1
  3. Gal-NAc6S
  4. Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase
  5. SIATFL
  6. ST3Gal I
  7. ST3GalI
  8. ST3GalA.1
  9. ST3O
  10. Sialyltransferase 4A
  11. SIAT4-A
Enzyme 5 Gene Name ST3GAL1
Enzyme 5 Protein Sequence >CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
MVTLRKRTLKVLTFLVLFIFLTSFFLNYSHTMVATTWFPKQMVLELSENLKRLIKHRPCT
CTHCIGQRKLSAWFDERFNQTMQPLLTAQNALLEDDTYRWWLRLQREKKPNNLNDTIKEL
FRVVPGNVDPMLEKRSVGCRRCAVVGNSGNLRESSYGPEIDSHDFVLRMNKAPTAGFEAD
VGTKTTHHLVYPESFRELGDNVSMILVPFKTIDLEWVVSAITTGTISHTYIPVPAKIRVK
QDKILIYHPAFIKYVFDNWLQGHGRYPSTGILSVIFSMHVCDEVDLYGFGADSKGNWHHY
WENNPSAGAFRKTGVHDADFESNVTATLASINKIRIFKGR
Enzyme 5 Number of Residues 340
Enzyme 5 Molecular Weight 39074.7
Enzyme 5 Theoretical pI 9.45
Enzyme 5 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 5 General Function Involved in beta-galactoside alpha-2,3-sialyltransferas
Enzyme 5 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 5 Pathways
Enzyme 5 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 [RN:R04590 R05913]
Enzyme 5 Pfam Domain Function
Enzyme 5 Signals
  • None
Enzyme 5 Transmembrane Regions
  • 14-34
Enzyme 5 Essentiality Not Available
Enzyme 5 GenBank ID Protein 3169564 Link Image
Enzyme 5 UniProtKB/Swiss-Prot ID Q11201 Link Image
Enzyme 5 UniProtKB/Swiss-Prot Entry Name SIA4A_HUMAN Link Image
Enzyme 5 PDB ID Not Available
Enzyme 5 Cellular Location Not Available
Enzyme 5 Gene Sequence >1023 bp
ATGGTGACCCTGCGGAAGAGGACCCTGAAAGTGCTCACCTTCCTCGTGCTCTTCATCTTC
CTCACCTCCTTCTTCCTGAACTACTCCCACACCATGGTGGCCACCACCTGGTTCCCCAAG
CAGATGGTCCTGGAGCTCTCCGAGAACCTGAAGAGACTGATCAAGCACAGGCCTTGCACC
TGCACCCACTGCATCGGGCAGCGCAAGCTCTCGGCCTGGTTCGATGAGAGGTTCAACCAG
ACCATGCAGCCGCTCGTGACCGCCCAGAACGCGCTCTTGGAGGACGACACCTACCGATGG
TGGCTGAGGCTCCAGCGGGAGAAGAAGCCCAATAACTTGAATGACACCATCAAGGAGCTG
TTCAGAGTGGTGCCTGGGAATGTGGACCCTATGCTGGAGAAGAGGTCGGTGGGCTGCCGG
CGCTGCGCTGTGGTGGGCAACTCGGGCAACCTGAGGGAGTCTTCTTATGGGCCTGAGATA
GACAGTCACGACTTTGTCCTCAGGATGAACAAGGCGCCCACGGCAGGGTTTGAAGCTGAT
GTTGGGACCAAGACCACCCACCATCTGGTGTACCCTGAGAGCTTCCGGGAGCTGGGAGAT
AATGTCAGCATGATCCTGGTGCCCTTCAAGACCATCGACTTGGAGTGGGTGGTGAGGGCC
ATCACCACGGGCACCATTTCCCACACCTACATCCCGGTTCCTGCAAAGATCAGAGTGAAA
CAGGATAAGATCCTGATCTACCACCCAGCCTTCATCAAGTATGTCTTTGACAACTGGCTG
CAAGGGCACGGGCGATACCCATCTACCGGCATCCTCTCAGTCATCTTCTCAATGCATGTC
TGCGATGAGGTGGACTTGTACGGCTTCGGGGCAGACAGCAAAGGGAACTGGCACCACTAC
TGGGAGAACAACCCATCCGCGGGGGCTTTTCGCAAGACGGGGGTGCACGATGCAGACTTT
GAGTCTAACGTGACGGCCACCTTGGCCTCCATCAATAAAATCCGGATCTTCAAGGGGAGA
TGA
Enzyme 5 GenBank Gene ID AF059321 Link Image
Enzyme 5 GeneCard ID ST3GAL1 Link Image
Enzyme 5 GenAtlas ID Not Available
Enzyme 5 HGNC ID Not Available
Enzyme 5 Chromosome Location 8
Enzyme 5 Locus 8q24.22
Enzyme 5 SNPs SNPJam Report Link Image
Enzyme 5 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]
  4. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
Enzyme 5 Metabolite References Not Available
Enzyme 6 [top]
Enzyme 6 ID 8660
Enzyme 6 Name CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
Enzyme 6 Synonyms
  1. Alpha 2,3-ST 4
  2. Beta-galactoside alpha-2,3-sialyltransferase 4
  3. Alpha 2,3-sialyltransferase IV
  4. Gal-NAc6S
  5. Gal-beta-1,4-GalNAc-alpha-2,3-sialyltransferase
  6. SAT-3
  7. ST-4
  8. ST3Gal IV
  9. ST3GalIV
  10. ST3GalA.2
  11. STZ
  12. Sialyltransferase 4C
  13. SIAT4-C
Enzyme 6 Gene Name ST3GAL4
Enzyme 6 Protein Sequence >CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
MVSKSRWKLLAMLALVLVVMVWYSISREDRYIELFYFPIPEKKEPCLQGEAESKASKLFG
NYSRDQPIFLRLEDYFWVKTPSAYELPYGTKGSEDLLLRVLAITSSSIPKNIQSLRCRRC
VVVGNGHRLRNSSLGDAINKYDVVIRLNNAPVAGYEGDVGSKTTMRLFYPESAHFDPKVE
NNPDTLLVLVAFKAMDFHWIETILSDKKRVRKGFWKQPPLIWDVNPKQIRILNPFFMEIA
ADKLLSLPMQQPRKIKQKPTTGLLAITLALHLCDLVHIAGFGYPDAYNKKQTIHYYEQIT
LKSMAGSGHNVSQEALAIKRMLEMGAIKNLTSF
Enzyme 6 Number of Residues 333
Enzyme 6 Molecular Weight 38045.1
Enzyme 6 Theoretical pI 9.88
Enzyme 6 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 6 General Function Involved in sialyltransferase activity
Enzyme 6 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. Also acts on the corresponding 1,3- galactosyl derivative
Enzyme 6 Pathways Not Available
Enzyme 6 Reactions Not Available
Enzyme 6 Pfam Domain Function
Enzyme 6 Signals
  • None
Enzyme 6 Transmembrane Regions
  • 9-26
Enzyme 6 Essentiality Not Available
Enzyme 6 GenBank ID Protein 14714972 Link Image
Enzyme 6 UniProtKB/Swiss-Prot ID Q11206 Link Image
Enzyme 6 UniProtKB/Swiss-Prot Entry Name SIA4C_HUMAN Link Image
Enzyme 6 PDB ID Not Available
Enzyme 6 Cellular Location Not Available
Enzyme 6 Gene Sequence >1002 bp
ATGGTCAGCAAGTCCCGCTGGAAGCTCCTGGCCATGTTGGCTCTGGTCCTGGTCGTCATG
GTGTGGTATTCCATCTCCCGGGAAGACAGGTACATCGAGCTTTTTTATTTTCCCATCCCA
GAGAAGAAGGAGCCGTGCCTCCAGGGTGAGGCAGAGAGCAAGGCCTCTAAGCTCTTTGGC
AACTACTCCCGGGATCAGCCCATCTTCCTGCGGCTTGAGGATTATTTCTGGGTCAAGACG
CCATCTGCTTACGAGCTGCCCTATGGGACCAAGGGGAGTGAGGATCTGCTCCTCCGGGTG
CTAGCCATCACCAGCTCCTCCATCCCCAAGAACATCCAGAGCCTCAGGTGCCGCCGCTGT
GTGGTCGTGGGGAACGGGCACCGGCTGCGGAACAGCTCACTGGGAGATGCCATCAACAAG
TACGATGTGGTCATCAGATTGAACAATGCCCCAGTGGCTGGCTATGAGGGTGACGTGGGC
TCCAAGACCACCATGCGTCTCTTCTACCCTGAATCTGCCCACTTCGACCCCAAAGTAGAA
AACAACCCAGACACACTCCTCGTCCTGGTAGCTTTCAAGGCAATGGACTTCCACTGGATT
GAGACCATCCTGAGTGATAAGAAGCGGGTGCGAAAGGGTTTCTGGAAACAGCCTCCCCTC
ATCTGGGATGTCAATCCTAAACAGATTCGGATTCTCAACCCCTTCTTCATGGAGATTGCA
GCTGACAAACTGCTGAGCCTGCCAATGCAACAGCCACGGAAGATTAAGCAGAAGCCCACC
ACGGGCCTGTTGGCCATCACGCTGGCCCTCCACCTCTGTGACTTGGTGCACATTGCCGGC
TTTGGCTACCCAGACGCCTACAACAAGAAGCAGACCATTCACTACTATGAGCAGATCACG
CTCAAGTCCATGGCGGGGTCAGGCCATAATGTCTCCCAAGAGGCCCTGGCCATTAAGCGG
ATGCTGGAGATGGGAGCTATCAAGAACCTCACGTCCTTCTGA
Enzyme 6 GenBank Gene ID BC010645 Link Image
Enzyme 6 GeneCard ID ST3GAL4 Link Image
Enzyme 6 GenAtlas ID ST3GAL4 Link Image
Enzyme 6 HGNC ID HGNC:10864 Link Image
Enzyme 6 Chromosome Location 1
Enzyme 6 Locus 11q24.2
Enzyme 6 SNPs SNPJam Report Link Image
Enzyme 6 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. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  6. 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 6 Metabolite References Not Available
Enzyme 7 [top]
Enzyme 7 ID 15201
Enzyme 7 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 7 Synonyms Not Available
Enzyme 7 Gene Name ST6GAL1
Enzyme 7 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 7 Number of Residues 406
Enzyme 7 Molecular Weight 46605
Enzyme 7 Theoretical pI 9.35
Enzyme 7 GO Classification Not Available
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 Not Available
Enzyme 7 Signals
  • None
Enzyme 7 Transmembrane Regions
  • None
Enzyme 7 Essentiality Not Available
Enzyme 7 GenBank ID Protein 158259219 Link Image
Enzyme 7 UniProtKB/Swiss-Prot ID A8KA14 Link Image
Enzyme 7 UniProtKB/Swiss-Prot Entry Name A8KA14_HUMAN Link Image
Enzyme 7 PDB ID Not Available
Enzyme 7 Cellular Location Not Available
Enzyme 7 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 7 GenBank Gene ID AK292879 Link Image
Enzyme 7 GeneCard ID A8KA14 Link Image
Enzyme 7 GenAtlas ID Not Available
Enzyme 7 HGNC ID Not Available
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 15202
Enzyme 8 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 8 Synonyms Not Available
Enzyme 8 Gene Name ST6GALNAC4
Enzyme 8 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 8 Number of Residues 302
Enzyme 8 Molecular Weight 34201
Enzyme 8 Theoretical pI 8.65
Enzyme 8 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 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
Enzyme 8 Signals
  • None
Enzyme 8 Transmembrane Regions
  • None
Enzyme 8 Essentiality Not Available
Enzyme 8 GenBank ID Protein 55958253 Link Image
Enzyme 8 UniProtKB/Swiss-Prot ID Q5T9D0 Link Image
Enzyme 8 UniProtKB/Swiss-Prot Entry Name Q5T9D0_HUMAN Link Image
Enzyme 8 PDB ID Not Available
Enzyme 8 Cellular Location Not Available
Enzyme 8 Gene Sequence >909 bp
ATGAAGGCTCCGGGTCGGCTCGTGCTCATCATCCTGTGCTCCGTGGTCTTCTCTGCCGTC
TACATCCTCCTGTGCTGCTGGGCCGGCCTGCCCCTCTGCCTGGCCACCTGCCTGGACCAC
CACTTCCCCACAGGCTCCAGGCCCACTGTGCCGGGACCCCTGCACTTCAGTGGATATAGC
AGTGTGCCAGATGGGAAGCCGCTGGTCCGCGAGCCCTGCCGCAGCTGTGCCGTGGTGTCC
AGCTCCGGCCAAATGCTGGGCTCAGGCCTGGGTGCTGAGATCGACAGTGCCGAGTGCGTG
TTCCGCATGAACCAGGCGCCCACCGTGGGCTTTGAGGCGGATGTGGGCCAGCGCAGCACC
CTGCGTGTCGTCTCACACACAAGCGTGCCGCTGCTGCTGCGCAACTATTCACACTACTTC
CAGAAGGCCCGAGACACGCTCTACATGGTGTGGGGCCAGGGCAGGCACATGGACCGGGTG
CTCGGCGGCCGCACCTACCGCACGCTGCTGCAGCTCACCAGGATGTACCCCGGCCTGCAG
GTGTACACCTTCACGGAGCGCATGATGGCCTACTGCGACCAGATCTTCCAGGACGAGACG
GGCAAGAACCGGAGGCAGTCGGGCTCCTTCCTCAGCACCGGCTGGTTCACCATGATCCTC
GCGCTGGAGCTGTGTGAGGAGATCGTGGTCTATGGGATGGTCAGCGACAGCTACTGCAGG
GAGAAGAGCCACCCCTCAGTGCCTTACCACTACTTTGAGAAGGGCCGGCTAGATGAGTGT
CAGATGTACCTGGCACACGAGCAGGCGCCCCGAAGCGCCCACCGCTTCATCACTGAGAAG
GCGGTCTTCTCCCGCTGGGCCAAGAAGAGGCCCATCGTGTTCGCCCATCCGTCCTGGAGG
ACTGAGTAG
Enzyme 8 GenBank Gene ID AL157935 Link Image
Enzyme 8 GeneCard ID Q5T9D0 Link Image
Enzyme 8 GenAtlas ID ST6GALNAC4 Link Image
Enzyme 8 HGNC ID HGNC:17846 Link Image
Enzyme 8 Chromosome Location Not Available
Enzyme 8 Locus Not Available
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 15203
Enzyme 9 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 9 Synonyms Not Available
Enzyme 9 Gene Name ST8SIA1
Enzyme 9 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 9 Number of Residues 356
Enzyme 9 Molecular Weight 40519
Enzyme 9 Theoretical pI 9.61
Enzyme 9 GO Classification Not Available
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 Not Available
Enzyme 9 Signals
  • None
Enzyme 9 Transmembrane Regions
  • None
Enzyme 9 Essentiality Not Available
Enzyme 9 GenBank ID Protein 158255318 Link Image
Enzyme 9 UniProtKB/Swiss-Prot ID A8K4H6 Link Image
Enzyme 9 UniProtKB/Swiss-Prot Entry Name A8K4H6_HUMAN Link Image
Enzyme 9 PDB ID Not Available
Enzyme 9 Cellular Location Not Available
Enzyme 9 Gene Sequence >1071 bp
ATGAGCCCCTGCGGGCGGGCCCGGCGACAAACGTCCAGAGGGGCCATGGCTGTACTGGCG
TGGAAGTTCCCGCGGACCCGGCTGCCCATGGGAGCCAGTGCCCTCTGTGTCGTGGTCCTC
TGTTGGCTCTACATCTTCCCCGTCTACCGGCTGCCCAACGAGAAAGAGATCGTGCAGGGG
GTGCTGCAACAGGGCACGGCGTGGAGGAGGAACCAGACCGCGGCCAGAGCGTTCAGGAAA
CAAATGGAAGACTGCTGCGACCCTGCTCATCTCTTTGCTATGACTAAAATGAATTCCCCT
ATGGGGAAGAGCATGTGGTATGACGGGGAGTTTTTATACTCATTCACCATTGACAATTCA
ACTTACTCTCTCTTCCCACAGGCAACCCCATTCCAGCTGCCATTGAAGAAATGCGCGGTG
GTGGGAAATGGTGGGATTCTGAAGAAGAGTGGCTGTGGCCGTCAAATAGATGAAGCAAAT
TTTGTCATGCGATGCAATCTCCCTCCTTTGTCAAGTGAATACACTAAGGATGTTGGATCC
AAAAGTCAGTTAGTGACAGCTAATCCCAGCATAATTCGGCAAAGGTTTCAGAACCTTCTG
TGGTCCAGAAAGACATTTGTGGACAACATGAAAATCTATAACCACAGTTACATCTACATG
CCTGCCTTTTCTATGAAGACAGGAACAGAGCCATCTTTGAGGGTTTATTATACACTGTCA
GATGTTGGTGCCAATCAAACAGTGCTGTTTGCCAACCCCAACTTTCTGCGTAGCATTGGA
AAGTTCTGGAAAAGTAGAGGAATCCATGCCAAGCGCCTGTCCACAGGACTTTTTCTGGTG
AGCGCAGCTCTGGGTCTCTGTGAAGAGGTGGCCATCTATGGCTTCTGGCCCTTCTCTGTG
AATATGCATGAGCAGCCCATCAGCCACCACTACTATGACAACGTCTTACCCTTTTCTGGC
TTCCATGCCATGCCCGAGGAATTTCTCCAACTCTGGTATCTTCATAAAATCGGTGCACTG
AGAATGCAGCTGGACCCATGTGAAGATACCTCACTCCAGCCCACTTCCTAG
Enzyme 9 GenBank Gene ID AK290941 Link Image
Enzyme 9 GeneCard ID A8K4H6 Link Image
Enzyme 9 GenAtlas ID Not Available
Enzyme 9 HGNC ID Not Available
Enzyme 9 Chromosome Location 12
Enzyme 9 Locus 12p12.1-p11.2
Enzyme 9 SNPs SNPJam Report Link Image
Enzyme 9 General References Not Available
Enzyme 9 Metabolite References Not Available
Enzyme 10 [top]
Enzyme 10 ID 16481
Enzyme 10 Name cDNA FLJ45393 fis, clone BRHIP3027105, highly similar to CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3- sialyltransferase (EC 2.4.99.-)
Enzyme 10 Synonyms Not Available
Enzyme 10 Gene Name Not Available
Enzyme 10 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 10 Number of Residues 350
Enzyme 10 Molecular Weight 40187.5
Enzyme 10 Theoretical pI 8.47
Enzyme 10 GO Classification
Function
  • catalytic activity
  • sialyltransferase activity
  • transferase activity
  • transferase activity, transferring glycosyl groups
Process
  • macromolecule metabolic process
  • macromolecule modification
  • metabolic process
  • protein amino acid glycosylation
  • protein modification process
Component
  • cell part
  • integral to Golgi membrane
  • intrinsic to Golgi membrane
  • intrinsic to membrane
  • intrinsic to organelle membrane
  • membrane part
Enzyme 10 General Function Involved in sialyltransferase activity
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 193785328 Link Image
Enzyme 10 UniProtKB/Swiss-Prot ID B3KXG9 Link Image
Enzyme 10 UniProtKB/Swiss-Prot Entry Name B3KXG9_HUMAN Link Image
Enzyme 10 PDB ID Not Available
Enzyme 10 Cellular Location Not Available
Enzyme 10 Gene Sequence >1053 bp
ATGAAGTGCTCCCTGCGGGTGTGGTTCCTCTCCGTGGCCTTCCTGCTGGTGTTCATCATG
TCCCTGCTCTTCACCTACTCGCACCACAGCATGGCCACGCTCCCCTACCTGGACTCAGGG
GCCCTGGATGGGACGCACCGGGTGAAGCTGGTGCCCGGCTATGCCGGCCTGCAGCGCCTC
AGCAAGGAGAGGCTCTCGGGCAAGAGCTGTGCCTGTCGCCGCTGCATGGGCGATGCCGGT
GCCTCCGACTGGTTTGACAGCCACTTTGACGGTAACATTTCCCCCGTCTGGACCCGAGAG
AACATGGATCTTCCACCGGACGTCCAGAGGTGGTGGATGATGCTGCAGCCCCAGTTCAAG
TCACACAACACCAATGAGGTGCTGGAGAAGCTGTTCCAGATAGTGCCTGGCGAGAACCCC
TACCGCTTCCGGGACCCCCACCAGTGCCGGCGCTGTGCCGTGGTGGGGAACTCGGGCAAC
CTGCGGGGCTCTGGCTATGGGCAGGACGTGGACGGGCACAACTTCATCATGAGGATGAAT
CAGGCGCCAACCGTGGGCTTTGAGCAGGATGTTGGCAGCCGAACCACCCACCATTTCATG
TACCCTGAGAGTGCCAAGAACCTGCCCGCCAACGTCAGCTTCGTGCTGGTGCCCTTCAAG
GTCCAGGACCTTCTGTGGATCGCCAGCGCCTTGTCCACGGGGCAGATCCGATTCACCTAC
GCCCCAGTGAAGTCCTTCCTTCGAGTGGATAAAGAAAAGGTCCAGATCTACAACCCAGCC
TTCTTCAAGTATATCCACGACAGGTGGACAGAGCATCACGGGCGGTACCCTTCCACGGGG
ATGCTGGTGCTTTTCTTTGCCCTGCATGTGTGTGATGAGGTGAACGTGTACGGGTTCGGG
GCCGACAGCCGGGGCAACTGGCACCACTACTGGGAGAACAACCGGTACGCGGGCGAGTTC
CGGAAGACTGGCGTGCACGACGCGGACTTCGAGGCCCACATCATCGACATGCTGGCCAAG
GCCAGCAAGATCGAAGTCTACCGGGGCAACTGA
Enzyme 10 GenBank Gene ID AK127322 Link Image
Enzyme 10 GeneCard ID Not Available
Enzyme 10 GenAtlas ID Not Available
Enzyme 10 HGNC ID HGNC:10863 Link Image
Enzyme 10 Chromosome Location Not Available
Enzyme 10 Locus Not Available
Enzyme 10 SNPs Not Available
Enzyme 10 General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed Link Image]
Enzyme 10 Metabolite References Not Available
Enzyme 11 [top]
Enzyme 11 ID 16482
Enzyme 11 Name ST3 beta-galactoside alpha-2,3-sialyltransferase 6, isoform CRA_a
Enzyme 11 Synonyms
  1. SubName: cDNA, FLJ96071, Homo sapiens alpha2,3-sialyltransferase (ST3GALVI), mRNA
Enzyme 11 Gene Name ST3GAL6
Enzyme 11 Protein Sequence >ST3 beta-galactoside alpha-2,3-sialyltransferase 6, isoform CRA_a
MRGYLVAIFLSAVFLYYVLHCILWGTNVYWVAPVEMKRRNKIQPCLSKPAFASLLRFHQF
HPFLCAADFRKIASLYGSDKFDLPYGMRTSAEYFRLALSKLQSCDLFDEFDNIPCKKCVV
VGNGGVLKNKTLGEKIDSYDVIIRMNNGPVLGHEEEVGRRTTFRLFYPESVFSDPIHNDP
NTTVILTAFKPHDLRWLLELLMGDKINTNGFWKKPALNLIYKPYQIRILDPFIIRTAAYE
LLHFPKVFPKNQKPKHPTTGIIAITLAFYICHEVHLAGFKYNFSDLKSPLHYYGNATMSL
MNKNAYHNVTAEQLFLKDIIEKNLVINLTQD
Enzyme 11 Number of Residues 331
Enzyme 11 Molecular Weight 38214
Enzyme 11 Theoretical pI 9.30
Enzyme 11 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 11 General Function Not Available
Enzyme 11 Specific Function Not Available
Enzyme 11 Pathways Not Available
Enzyme 11 Reactions Not Available
Enzyme 11 Pfam Domain Function
Enzyme 11 Signals
  • None
Enzyme 11 Transmembrane Regions
  • None
Enzyme 11 Essentiality Not Available
Enzyme 11 GenBank ID Protein Not Available
Enzyme 11 UniProtKB/Swiss-Prot ID B2RCH2 Link Image
Enzyme 11 UniProtKB/Swiss-Prot Entry Name B2RCH2_HUMAN Link Image
Enzyme 11 PDB ID Not Available
Enzyme 11 Cellular Location Not Available
Enzyme 11 Gene Sequence Not Available
Enzyme 11 GenBank Gene ID AK315111 Link Image
Enzyme 11 GeneCard ID B2RCH2 Link Image
Enzyme 11 GenAtlas ID Not Available
Enzyme 11 HGNC ID Not Available
Enzyme 11 Chromosome Location Not Available
Enzyme 11 Locus Not Available
Enzyme 11 SNPs SNPJam Report Link Image
Enzyme 11 General References Not Available
Enzyme 11 Metabolite References Not Available