ST8SIA1
entrez
6489
canonical
uniprot
Q92185
canonical
ensembl
ENSG00000111728
resolver
ensp
ENSP00000379353
resolver
genesymbol
ST8SIA1
resolver
genesymbol_syn
SIAT8
resolver
genesymbol_syn
SIAT8A
resolver
hgnc
HGNC:10869
resolver
uniprot
A8K4H6
resolver
uniprot
Q17RL0
resolver
uniprot
Q6PZN5
resolver
uniprot
Q93064
resolver
uniprot_entry
SIA8A_HUMAN
resolver
uniprot_sec
A8K4H6
resolver
uniprot_sec
Q17RL0
resolver
uniprot_sec
Q6PZN5
resolver
uniprot_sec
Q93064
resolver
amino_acid_sequence
MSPCGRARRQTSRGAMAVLAWKFPRTRLPMGASALCVVVLCWLYIFPVYRLPNEKEIVQGVLQQGTAWRRNQTAARAFRKQMEDCCDPAHLFAMTKMNSPMGKSMWYDGEFLYSFTIDNSTYSLFPQATPFQLPLKKCAVVGNGGILKKSGCGRQIDEANFVMRCNLPPLSSEYTKDVGSKSQLVTANPSIIRQRFQNLLWSRKTFVDNMKIYNHSYIYMPAFSMKTGTEPSLRVYYTLSDVGANQTVLFANPNFLRSIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVAIYGFWPFSVNMHEQPISHHYYDNVLPFSGFHAMPEEFLQLWYLHKIGALRMQLDPCEDTSLQPTS
uniprot
proteins
ec_number
2.4.3.8
uniprot
proteins
function
FUNCTION: Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphingolipds that contain one or more residues of sialic acid (PubMed:18348864, PubMed:22885356, PubMed:7937974, PubMed:8058740, PubMed:8195250, PubMed:8631981, PubMed:8706663). Can catalyze the addition of a second alpha-2,8-sialic acid to GD3 to form GT3 (PubMed:8631981). Can use GM1b, GD1a and GT1b as acceptor substrates to synthesize GD1c, GT1a and GQ1b respectively (PubMed:8706663). Can synthesize unusual tetra- and pentasialylated lactosylceramide derivatives identified as GQ3 (II3Neu5Ac4-Gg2Cer) and GP3 (II3Neu5Ac5-Gg2Cer) in breast cancer cells (PubMed:22885356). {ECO:0000269|PubMed:18348864, ECO:0000269|PubMed:22885356, ECO:0000269|PubMed:7937974, ECO:0000269|PubMed:8058740, ECO:0000269|PubMed:8195250, ECO:0000269|PubMed:8631981, ECO:0000269|PubMed:8706663}.
uniprot
proteins
mass_dalton
40519
uniprot
proteins
mutagenesis
MUTAGEN 188; /note="N->D: Enzyme activity is 42% of the wild-type. A 2.5-fold increase in Km value for CMP-N-acetyl-beta-neuraminate. A 2.3-fold decrease in Vmax for both CMP-N-acetyl-beta-neuraminate and ganglioside GM3."; /evidence="ECO:0000269|PubMed:18348864"; MUTAGEN 189; /note="P->A: Enzyme activity is 91% of the wild-type."; /evidence="ECO:0000269|PubMed:18348864"; MUTAGEN 190; /note="S->A: Enzyme activity is 33% of the wild-type. A 2-fold increase in Km value for ganglioside GM3 and 1.25 fold increase in Km value for CMP-N-acetyl-beta-neuraminate. A 3-fold decrease in Vmax for both CMP-N-acetyl-beta-neuraminate and ganglioside GM3."; MUTAGEN 272; /note="R->A: Enzyme activity is 20% of the wild-type. A 10-fold increase in Km value for ganglioside GM3. A 5-fold decrease in Vmax for both CMP-N-acetyl-beta-neuraminate and ganglioside GM3."; /evidence="ECO:0000269|PubMed:18348864"; MUTAGEN 272; /note="R->I: Enzyme activity is 19% of the wild-type."; /evidence="ECO:0000269|PubMed:18348864"; MUTAGEN 272; /note="R->K: Enzyme activity is 98% of the wild-type."; /evidence="ECO:0000269|PubMed:18348864
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation.; PATHWAY: Lipid metabolism; sphingolipid metabolism.
uniprot
proteins
protein_family
Glycosyltransferase 29 family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15843597
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
18348864
uniprot
proteins
pubmed
22885356
uniprot
proteins
pubmed
7937974
uniprot
proteins
pubmed
8058740
uniprot
proteins
pubmed
8195250
uniprot
proteins
pubmed
8631981
uniprot
proteins
pubmed
8706663
uniprot
proteins
sequence_length
356
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 30..48; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins