St6gal1
entrez
25197
canonical
uniprot
P13721
canonical
ensembl
ENSRNOG00000001823
resolver
ensp
ENSRNOP00000002496
resolver
genesymbol
St6gal1
resolver
genesymbol_syn
Siat1
resolver
uniprot
D4ABR2
resolver
uniprot
G3V680
resolver
uniprot_entry
SIAT1_RAT
resolver
uniprot_sec
D4ABR2
resolver
uniprot_sec
G3V680
resolver
amino_acid_sequence
MIHTNLKKKFSLFILVFLLFAVICVWKKGSDYEALTLQAKEFQMPKSQEKVAMGSASQVVFSNSKQDPKEDIPILSYHRVTAKVKPQPSFQVWDKDSTYSKLNPRLLKIWRNYLNMNKYKVSYKGPGPGVKFSVEALRCHLRDHVNVSMIEATDFPFNTTEWEGYLPKENFRTKVGPWQRCAVVSSAGSLKNSQLGREIDNHDAVLRFNGAPTDNFQQDVGSKTTIRLMNSQLVTTEKRFLKDSLYTEGILIVWDPSVYHADIPKWYQKPDYNFFETYKSYRRLNPSQPFYILKPQMPWELWDIIQEISADLIQPNPPSSGMLGIIIMMTLCDQVDIYEFLPSKRKTDVCYYHQKFFDSACTMGAYHPLLFEKNMVKHLNEGTDEDIYLFGKATLSGFRNIRC
uniprot
proteins
ec_number
2.4.3.1
uniprot
proteins
function
FUNCTION: Transfers sialic acid from CMP-sialic acid to galactose-containing acceptor substrates (PubMed:11278697, PubMed:24155237, PubMed:3121604). Sialylates complex-type N-glycans attached on the fragment crystallizable (Fc) of IgGs conferring anti-inflammatory effector functions. Preferentially monosialylates the alpha(1->3) mannose antenna of Fc glycoforms with subsequent disialylation occurring at a much slower rate (By similarity). {ECO:0000250|UniProtKB:P15907, ECO:0000269|PubMed:11278697, ECO:0000269|PubMed:24155237, ECO:0000269|PubMed:3121604}.
uniprot
proteins
mass_dalton
46754
uniprot
proteins
mutagenesis
MUTAGEN 119; /note="Y->A: Protein destabilization."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 119; /note="Y->F: No effect on protein stability, nor on catalytic activity."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 180; /note="R->A: Small decrease of sialyltransferase activity."; /evidence="ECO:0000269|PubMed:11278697"; MUTAGEN 181; /note="C->A: Loss of sialyltransferase activity and aberrant subcellular location."; /evidence="ECO:0000269|PubMed:11278697"; MUTAGEN 208; /note="F->A: Reduced KM/kcat values for CMP-Neu5Ac, no effect on kinetic constants for beta-Gal1,4-GlcNAc."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 230; /note="N->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 231; /note="S->A: Protein destabilization."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 232; /note="Q->A: Decreased catalytic activity."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 271; /note="D->A: Decreased catalytic activity."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 272; /note="Y->A: Strongly decreased catalytic activity."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 319; /note="S->A: Protein destabilization."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 332; /note="C->A: Loss of sialyltransferase activity and aberrant subcellular location."; /evidence="ECO:0000269|PubMed:11278697"; MUTAGEN 332; /note="C->S: Loss of sialyltransferase activity."; /evidence="ECO:0000269|PubMed:11278697"; MUTAGEN 333; /note="D->A: Small decrease of sialyltransferase activity."; /evidence="ECO:0000269|PubMed:11278697"; MUTAGEN 350; /note="C->A: Loss of catalytic activity; when associated with A-361."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 354; /note="Q->A: No effect on catalytic activity."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 355; /note="K->A: No effect on catalytic activity."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 361; /note="C->A: Loss of catalytic activity; when associated with A-350."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 366; /note="Y->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:24155237"; MUTAGEN 367; /note="H->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:24155237
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:3121604}.
uniprot
proteins
post_translational_modification
PTM: The soluble form derives from the membrane form by proteolytic processing. {ECO:0000269|PubMed:3121604}.; PTM: N-glycosylated. {ECO:0000269|PubMed:3121604}.
uniprot
proteins
protein_family
Glycosyltransferase 29 family
uniprot
proteins
pubmed
11278697
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
1733948
uniprot
proteins
pubmed
1983783
uniprot
proteins
pubmed
24155237
uniprot
proteins
pubmed
2793863
uniprot
proteins
pubmed
3121604
uniprot
proteins
sequence_length
403
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:3121604}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:11278697, ECO:0000269|PubMed:3121604}. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid. Colocalizes with MGAT3 and B4GALT1 in the Golgi stacks of cisternae, including the cis-part of the Golgi stacks. {ECO:0000250|UniProtKB:P15907, ECO:0000269|PubMed:11278697, ECO:0000269|PubMed:3121604}.
uniprot
proteins
transmembrane_region
TRANSMEM 10..26; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins