ST8SIA3
entrez
51046
canonical
uniprot
O43173
canonical
ensembl
ENSG00000177511
resolver
ensp
ENSP00000320431
resolver
enst
ENST00000324000
resolver
genesymbol
ST8SIA3
resolver
genesymbol_syn
SIAT8C
resolver
hgnc
HGNC:14269
resolver
uniprot
A8K0F2
resolver
uniprot
Q59GW3
resolver
uniprot
Q6B085
resolver
uniprot
Q9NS41
resolver
uniprot_entry
Q59GW3_HUMAN
resolver
uniprot_entry
SIA8C_HUMAN
resolver
uniprot_sec
A8K0F2
resolver
uniprot_sec
Q6B085
resolver
uniprot_sec
Q9NS41
resolver
amino_acid_sequence
MRNCKMARVASVLGLVMLSVALLILSLISYVSLKKENIFTTPKYASPGAPRMYMFHAGFRSQFALKFLDPSFVPITNSLTQELQEKPSKWKFNRTAFLHQRQEILQHVDVIKNFSLTKNSVRIGQLMHYDYSSHKYVFSISNNFRSLLPDVSPIMNKHYNICAVVGNSGILTGSQCGQEIDKSDFVFRCNFAPTEAFQRDVGRKTNLTTFNPSILEKYYNNLLTIQDRNNFFLSLKKLDGAILWIPAFFFHTSATVTRTLVDFFVEHRGQLKVQLAWPGNIMQHVNRYWKNKHLSPKRLSTGILMYTLASAICEEIHLYGFWPFGFDPNTREDLPYHYYDKKGTKFTTKWQESHQLPAEFQLLYRMHGEGLTKLTLSHCA
uniprot
proteins
ec_number
2.4.3.-
uniprot
proteins
ec_number
2.4.3.8
uniprot
proteins
function
FUNCTION: Catalyzes the transfer of sialic acid from a CMP-linked sialic acid donor onto a terminal alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid of an acceptor, such as N-linked oligosaccharides of glycoproteins and glycolipids through alpha-2,8-linkages (PubMed:10766765, PubMed:26192331, PubMed:9826427). Forms oligosialic and polysialic acid on various sialylated N-acetyllactosamine oligosaccharides of glycoproteins, including FETUB N-glycans, a2-HS-glycoprotein (AHSG) and alpha 2,3-sialylated glycosphingolipids, such as alpha 2,3-sialylparagloboside and ganglioside GM3 and to a lesser extent NCAM1 N-glycans (PubMed:10766765, PubMed:9826427). However, it is much more specific to N-linked oligosaccharides of glycoproteins than glycosphingolipids (By similarity). 2,3-sialylparagloboside serves as the best acceptor substrate among the glycolipids (By similarity). alpha-Neu5Ac-(2->8)-alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-6S-D-GlcNAc and monosialyl and disialyl N-acetyllactosamines are the best acceptor substrates among glycoproteins (PubMed:10766765, PubMed:26192331). May play a critical role in the striatum by mediating the formation of disialylated and trisialylated terminal glycotopes on N- and O-glycans of specific striatal proteins, regulating their distribution in lipid rafts, affecting their interaction with other binding partners, and subsequently modulating striatal functions (By similarity). {ECO:0000250|UniProtKB:Q64689, ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:26192331, ECO:0000269|PubMed:9826427}.
uniprot
proteins
mass_dalton
43970
uniprot
proteins
mutagenesis
MUTAGEN 190; /note="N->A: Loss of alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity."; /evidence="ECO:0000269|PubMed:26192331"; MUTAGEN 337; /note="H->A: Loss of alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity."; /evidence="ECO:0000269|PubMed:26192331"; MUTAGEN 354; /note="H->A: Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:26192331
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:9826427, ECO:0000305|PubMed:10766765, ECO:0000305|PubMed:26192331}.
uniprot
proteins
post_translational_modification
PTM: Autopolysialylated. {ECO:0000269|PubMed:10766765}.
uniprot
proteins
protein_family
Glycosyltransferase 29 family
uniprot
proteins
pubmed
10766765
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
26192331
uniprot
proteins
pubmed
9826427
uniprot
proteins
sequence_length
380
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|PubMed:10766765}; Single-pass type II membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 10..33; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins