ST8SIA2
entrez
8128
canonical
uniprot
Q92186
canonical
ensembl
ENSG00000140557
resolver
ensp
ENSP00000268164
resolver
ensp
ENSP00000437382
resolver
enst
ENST00000268164
resolver
enst
ENST00000539113
resolver
genesymbol
ST8SIA2
resolver
genesymbol_syn
SIAT8B
resolver
genesymbol_syn
STX
resolver
hgnc
HGNC:10870
resolver
uniprot
B2R9U8
resolver
uniprot
C6G488
resolver
uniprot
Q4VAY9
resolver
uniprot
Q4VAZ0
resolver
uniprot
Q92470
resolver
uniprot
Q92746
resolver
uniprot_entry
B2R9U8_HUMAN
resolver
uniprot_entry
C6G488_HUMAN
resolver
uniprot_entry
Q4VAY9_HUMAN
resolver
uniprot_entry
SIA8B_HUMAN
resolver
uniprot_sec
Q4VAZ0
resolver
uniprot_sec
Q92470
resolver
uniprot_sec
Q92746
resolver
amino_acid_sequence
MQLQFRSWMLAALTLLVVFLIFADISEIEEEIGNSGGRGTIRSAVNSLHSKSNRAEVVINGSSSPAVVDRSNESIKHNIQPASSKWRHNQTLSLRIRKQILKFLDAEKDISVLKGTLKPGDIIHYIFDRDSTMNVSQNLYELLPRTSPLKNKHFGTCAIVGNSGVLLNSGCGQEIDAHSFVIRCNLAPVQEYARDVGLKTDLVTMNPSVIQRAFEDLVNATWREKLLQRLHSLNGSILWIPAFMARGGKERVEWVNELILKHHVNVRTAYPSLRLLHAVRGYWLTNKVHIKRPTTGLLMYTLATRFCKQIYLYGFWPFPLDQNQNPVKYHYYDSLKYGYTSQASPHTMPLEFKALKSLHEQGALKLTVGQCDGAT
uniprot
proteins
ec_number
2.4.3.-
uniprot
proteins
function
FUNCTION: Catalyzes the transfer of a 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 N-linked glycan acceptor through alpha-2,8-linkages (Probable) (PubMed:10766765, PubMed:11744634, PubMed:9054414, PubMed:9774483). Therefore, participates in polysialic acid synthesis on various sialylated N-acetyllactosaminyl oligosaccharides (alpha-2,3-, alpha-2,6-, or alpha-2,8-linked sialic acid), including NCAM1, NCAM1 N-glycans, FETUB N-glycans, and to a lesser extent sialylparagloboside (SPG) and AHSG, which does not require the initial addition of an alpha 2,8-sialic acid (Probable) (PubMed:7559389). However, does not exhibit sialic acid-polymerase activity (By similarity). Catalyzes polysialic acid synthesis in the hippocampal on NCAM1 and supports neurite outgrowth (PubMed:9054414). ST8SIA2-mediated polysialylation influences on oligodendrocyte differentiation and may promote the integrity of myelin and axons (By similarity). {ECO:0000250|UniProtKB:O35696, ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:11744634, ECO:0000269|PubMed:7559389, ECO:0000269|PubMed:9054414, ECO:0000269|PubMed:9774483, ECO:0000305|PubMed:28810663}.
uniprot
proteins
mass_dalton
42430
uniprot
proteins
mutagenesis
MUTAGEN 60; /note="N->S: Does not affect autopolysialylation."; /evidence="ECO:0000269|PubMed:28810663"; MUTAGEN 72; /note="N->S: Does not affect autopolysialylation."; /evidence="ECO:0000269|PubMed:28810663"; MUTAGEN 89; /note="N->Q: Loss of autopolysialylation; when associated with Q-219 and Q-234. Loss of polysialylation activity; when associated with Q-89 and Q-219."; /evidence="ECO:0000269|PubMed:28810663"; MUTAGEN 89; /note="N->S: Decreases autopolysialylation. Does not affect localization at Golgi apparatus. Increases cell surface autopolysialylated protein. Loss of autopolysialylation; when associated with S-219 and S-234. Does not affect NCAM1 polysialylation activity."; /evidence="ECO:0000269|PubMed:28810663"; MUTAGEN 134; /note="N->S: Does not affect autopolysialylation."; /evidence="ECO:0000269|PubMed:28810663"; MUTAGEN 219; /note="N->Q: Loss of autopolysialylation; when associated with Q-89 and S-234. Loss of polysialylation activity; when associated with Q-89 and Q-219."; /evidence="ECO:0000269|PubMed:28810663"; MUTAGEN 219; /note="N->S: Decreases autopolysialylation. Does not affect localization at Golgi apparatus. Increases cell surface autopolysialylated protein at cell surface. Loss of autopolysialylation; when associated with S-89 and S-234. Does not affect NCAM1 polysialylation activity."; /evidence="ECO:0000269|PubMed:28810663"; MUTAGEN 234; /note="N->Q: Loss of autopolysialylation; when associated with Q-89 and Q-219. Loss of polysialylation activity; when associated with Q-89 and Q-219."; /evidence="ECO:0000269|PubMed:28810663"; MUTAGEN 234; /note="N->S: Decreases autopolysialylation. Does not affect localization at Golgi apparatus. Loss of autopolysialylation; when associated with S-89 and S-219. Does not affect NCAM1 polysialylation activity."; /evidence="ECO:0000269|PubMed:28810663
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:11744634, ECO:0000269|PubMed:28810663, ECO:0000269|PubMed:9054414, ECO:0000269|PubMed:9774483}.
uniprot
proteins
post_translational_modification
PTM: Autopolysialylated (PubMed:10766765, PubMed:11744634, PubMed:9852130). Autopolysialylation is not a prerequisite for the polysialylation acitity, but enhances the polysialylation acitity (PubMed:11744634). {ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:11744634, ECO:0000269|PubMed:9852130}.
uniprot
proteins
protein_family
Glycosyltransferase 29 family
uniprot
proteins
pubmed
10766765
uniprot
proteins
pubmed
11744634
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
28810663
uniprot
proteins
pubmed
7559389
uniprot
proteins
pubmed
8027041
uniprot
proteins
pubmed
9054414
uniprot
proteins
pubmed
9774483
uniprot
proteins
pubmed
9852130
uniprot
proteins
sequence_length
375
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:11744634, ECO:0000269|PubMed:9852130}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:11744634, ECO:0000269|PubMed:9852130}. Cell membrane {ECO:0000269|PubMed:11744634, ECO:0000269|PubMed:9852130}. Note=Also trafficks to the cell surface. {ECO:0000269|PubMed:11744634, ECO:0000269|PubMed:9852130}.
uniprot
proteins
transmembrane_region
TRANSMEM 7..23; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins