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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1

UniprotKB/SwissProt ID: Q02745 (Q02745)

Gene Name: ST3GAL1

Organism: Sus scrofa (Pig)

Function: A beta-galactoside alpha2->3 sialyltransferase involved in terminal sialylation of glycoproteins and glycolipids (PubMed:19820709, PubMed:8288606). Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid; Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates through an alpha2-3 linkage (PubMed:19820709, PubMed:8288606). Adds sialic acid to the core 1 O-glycan, Galbeta-(1->3)-GalNAc-O-Ser/Thr, which is a major structure of mucin-type O-glycans (PubMed:19820709, PubMed:8288606). As part of a homeostatic mechanism that regulates CD8-positive T cell numbers, sialylates core 1 O-glycans of T cell glycoproteins, SPN/CD43 and PTPRC/CD45. Prevents premature apoptosis of thymic CD8-positive T cells prior to peripheral emigration, whereas in the secondary lymphoid organs controls the survival of CD8-positive memory T cells generated following a successful immune response (By similarity). Transfers sialic acid to asialofetuin, presumably onto Galbeta-(1->3)-GalNAc-O-Ser (PubMed:8288606). Sialylates GM1a, GA1 and GD1b gangliosides to form GD1a, GM1b and GT1b, respectively (By similarity) (PubMed:8288606)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Golgi apparatus, Golgi stack membrane. Golgi apparatus, trans-Golgi network membrane. Secreted

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR051757 Beta-gal_alpha2-3_sialyltrans
IPR001675 Glyco_trans_29
IPR038578 GT29-like_sf
IPR012163 Sialyl_trans