MGAT5
entrez
4249
canonical
uniprot
Q09328
canonical
ensembl
ENSG00000152127
resolver
ensp
ENSP00000281923
resolver
ensp
ENSP00000386377
resolver
ensp
ENSP00000527249
resolver
ensp
ENSP00000527250
resolver
enst
ENST00000281923
resolver
enst
ENST00000409645
resolver
enst
ENST00000857190
resolver
enst
ENST00000857191
resolver
genesymbol
MGAT5
resolver
genesymbol_syn
GGNT5
resolver
hgnc
HGNC:7049
resolver
uniprot
D3DP70
resolver
uniprot_entry
MGT5A_HUMAN
resolver
uniprot_sec
D3DP70
resolver
activity_regulation
ACTIVITY REGULATION: Activity is increased by Mn(2+) and Mg(2+). {ECO:0000269|PubMed:10395745}.
uniprot
proteins
amino_acid_sequence
MALFTPWKLSSQKLGFFLVTFGFIWGMMLLHFTIQQRTQPESSSMLREQILDLSKRYIKALAEENRNVVDGPYAGVMTAYDLKKTLAVLLDNILQRIGKLESKVDNLVVNGTGTNSTNSTTAVPSLVALEKINVADIINGAQEKCVLPPMDGYPHCEGKIKWMKDMWRSDPCYADYGVDGSTCSFFIYLSEVENWCPHLPWRAKNPYEEADHNSLAEIRTDFNILYSMMKKHEEFRWMRLRIRRMADAWIQAIKSLAEKQNLEKRKRKKVLVHLGLLTKESGFKIAETAFSGGPLGELVQWSDLITSLYLLGHDIRISASLAELKEIMKKVVGNRSGCPTVGDRIVELIYIDIVGLAQFKKTLGPSWVHYQCMLRVLDSFGTEPEFNHANYAQSKGHKTPWGKWNLNPQQFYTMFPHTPDNSFLGFVVEQHLNSSDIHHINEIKRQNQSLVYGKVDSFWKNKKIYLDIIHTYMEVHATVYGSSTKNIPSYVKNHGILSGRDLQFLLRETKLFVGLGFPYEGPAPLEAIANGCAFLNPKFNPPKSSKNTDFFIGKPTLRELTSQHPYAEVFIGRPHVWTVDLNNQEEVEDAVKAILNQKIEPYMPYEFTCEGMLQRINAFIEKQDFCHGQVMWPPLSALQVKLAEPGQSCKQVCQESQLICEPSFFQHLNKDKDMLKYKVTCQSSELAKDILVPSFDPKNKHCVFQGDLLLFSCAGAHPRHQRVCPCRDFIKGQVALCKDCL
uniprot
proteins
ec_number
2.4.1.155
uniprot
proteins
function
FUNCTION: Catalyzes the addition of N-acetylglucosamine (GlcNAc) in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides (PubMed:10395745, PubMed:30140003). Catalyzes an important step in the biosynthesis of branched, complex-type N-glycans, such as those found on EGFR, TGFR (TGF-beta receptor) and CDH2 (PubMed:10395745, PubMed:22614033, PubMed:30140003). Via its role in the biosynthesis of complex N-glycans, plays an important role in the activation of cellular signaling pathways, reorganization of the actin cytoskeleton, cell-cell adhesion and cell migration. MGAT5-dependent EGFR N-glycosylation enhances the interaction between EGFR and LGALS3 and thereby prevents rapid EGFR endocytosis and prolongs EGFR signaling. Required for efficient interaction between TGFB1 and its receptor. Enhances activation of intracellular signaling pathways by several types of growth factors, including FGF2, PDGF, IGF, TGFB1 and EGF. MGAT5-dependent CDH2 N-glycosylation inhibits CDH2-mediated homotypic cell-cell adhesion and contributes to the regulation of downstream signaling pathways. Promotes cell migration. Contributes to the regulation of the inflammatory response. MGAT5-dependent TCR N-glycosylation enhances the interaction between TCR and LGALS3, limits agonist-induced TCR clustering, and thereby dampens TCR-mediated responses to antigens. Required for normal leukocyte evasation and accumulation at sites of inflammation (By similarity). Inhibits attachment of monocytes to the vascular endothelium and subsequent monocyte diapedesis (PubMed:22614033). {ECO:0000250|UniProtKB:Q8R4G6, ECO:0000269|PubMed:10395745, ECO:0000269|PubMed:22614033, ECO:0000269|PubMed:30140003}.; FUNCTION: [Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A]: Promotes proliferation of umbilical vein endothelial cells and angiogenesis, at least in part by promoting the release of the growth factor FGF2 from the extracellular matrix. {ECO:0000269|PubMed:11872751}.
uniprot
proteins
mass_dalton
84543
uniprot
proteins
mutagenesis
MUTAGEN 29; /note="L->D: No effect on the biosynthesis of the secreted form."; /evidence="ECO:0000269|PubMed:17142794"; MUTAGEN 30; /note="L->D: No effect on the biosynthesis of the secreted form."; /evidence="ECO:0000269|PubMed:17142794"; MUTAGEN 31; /note="H->A: No effect on the biosynthesis of the secreted form."; /evidence="ECO:0000269|PubMed:17142794"; MUTAGEN 280; /note="E->A: Decreased catalytic activity."; /evidence="ECO:0000269|PubMed:30140003"; MUTAGEN 287; /note="E->A: Decreased catalytic activity."; /evidence="ECO:0000269|PubMed:30140003"; MUTAGEN 297; /note="E->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:30140003"; MUTAGEN 429; /note="E->A: Decreased catalytic activity."; /evidence="ECO:0000269|PubMed:30140003"; MUTAGEN 520; /note="E->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:30140003"; MUTAGEN 526; /note="E->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:30140003
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:10395745, ECO:0000269|PubMed:17142794, ECO:0000269|PubMed:30140003}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:10395745, ECO:0000269|PubMed:17142794, ECO:0000269|PubMed:30140003}.; PTM: A secreted form is released from the membrane after cleavage by gamma-secretase. {ECO:0000269|PubMed:17142794}.
uniprot
proteins
protein_family
Glycosyltransferase 18 family
uniprot
proteins
pubmed
10395745
uniprot
proteins
pubmed
11872751
uniprot
proteins
pubmed
17142794
uniprot
proteins
pubmed
22614033
uniprot
proteins
pubmed
30140003
uniprot
proteins
pubmed
8292036
uniprot
proteins
sequence_length
741
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:P97259}; Single-pass type II membrane protein {ECO:0000269|PubMed:17142794}.; SUBCELLULAR LOCATION: [Secreted alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase A]: Secreted {ECO:0000269|PubMed:17142794}.
uniprot
proteins
transmembrane_region
TRANSMEM 14..30; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins