A CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q11201]
Alpha 2,3-ST 1;
Beta-galactoside alpha-2,3-sialyltransferase 1;
EC 2.4.99.4;
Gal-NAc6S;
Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase;
Monosialoganglioside sialyltransferase;
2.4.99.2;
SIATFL;
ST3Gal I;
ST3GalI;
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (100.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| 2,3-dihydroxybenzoic acid | Homo sapiens (human) | IC50 | 200.0000 | 1 | 1 |
| protocatechuic acid | Homo sapiens (human) | IC50 | 137.0000 | 1 | 1 |
| gallic acid | Homo sapiens (human) | IC50 | 65.0086 | 1 | 7 |
| beta-resorcylic acid | Homo sapiens (human) | IC50 | 200.0000 | 1 | 1 |
| 2,5-dihydroxybenzoic acid | Homo sapiens (human) | IC50 | 115.0000 | 1 | 1 |
| veratric acid | Homo sapiens (human) | IC50 | 200.0000 | 1 | 1 |
| methyl gallate | Homo sapiens (human) | IC50 | 26.5000 | 1 | 2 |
| 3,4,5-trimethoxybenzoic acid | Homo sapiens (human) | IC50 | 200.0000 | 1 | 1 |
| syringic acid | Homo sapiens (human) | IC50 | 200.0000 | 1 | 1 |
| epigallocatechin gallate | Homo sapiens (human) | IC50 | 7.2833 | 1 | 6 |
| guanosine diphosphate | Homo sapiens (human) | IC50 | 125.2600 | 1 | 5 |
This protein enables 3 target(s):
| Target | Category | Definition |
|---|---|---|
| beta-galactoside (CMP) alpha-2,3-sialyltransferase activity | molecular function | Catalysis of the reaction: CMP-N-acetylneuraminate + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R. [EC:2.4.3.4] |
| sialyltransferase activity | molecular function | Catalysis of the transfer of sialic acid to an acceptor molecule, typically the terminal portions of the sialylated glycolipids (gangliosides) or to the N- or O-linked sugar chains of glycoproteins. [GOC:cjm, PMID:26192491] |
| beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminide alpha-2,3- sialyltransferase | molecular function | Catalysis of the reaction: beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl derivative + CMP-N-acetyl-beta-neuraminate = N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl derivative + CMP + H+. [EC:2.4.3.2, MetaCyc:2.4.99.2-RXN] |
This protein is located in 6 target(s):
| Target | Category | Definition |
|---|---|---|
| Golgi membrane | cellular component | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. [GOC:mah] |
| membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
| trans-Golgi network membrane | cellular component | The lipid bilayer surrounding any of the compartments that make up the trans-Golgi network. [GOC:mah] |
| extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
| Golgi medial cisterna membrane | cellular component | The lipid bilayer surrounding any of the thin, flattened compartments that form the medial portion of the Golgi complex. [GOC:bhm, PMID:16038056, PMID:24119662] |
| Golgi trans cisterna membrane | cellular component | The lipid bilayer surrounding any of the thin, flattened compartments that form the trans portion of the Golgi complex. [GOC:bhm, PMID:16038056, PMID:24119662] |
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|---|---|
| membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
This protein is involved in 12 target(s):
| Target | Category | Definition |
|---|---|---|
| memory B cell differentiation | biological process | The process in which a B cell acquires the specialized features of a memory B cell. Memory B cells are cells that can respond rapidly to antigen re-exposure by production of high-affinity antibody. [GOC:jal, ISBN:0781735149] |
| N-acetylneuraminate metabolic process | biological process | The chemical reactions and pathways involving N-acetylneuraminate, the anion of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid. [ISBN:0198506732] |
| protein N-linked glycosylation | biological process | A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the N4 atom of peptidyl-asparagine, the omega-N of arginine, or the N1' atom peptidyl-tryptophan. [GOC:pr, RESID:AA0151, RESID:AA0156, RESID:AA0327] |
| ganglioside biosynthetic process via lactosylceramide | biological process | The chemical reactions and pathways resulting in the formation of gangliosides that begins with the formation of lactosylceramides, Gal-beta-(1->4)-Glc-beta-(1->1') ceramides, any compound formed by the replacement of the glycosidic C1 hydroxyl group of lactose by a ceramide group. [GOC:bf, GOC:dph, GOC:tb] |
| O-glycan processing | biological process | The stepwise addition of carbohydrate or carbohydrate derivative residues to the initially added O-linked residue (usually GalNAc) to form a core O-glycan structure. [GOC:mah, GOC:pr, PMID:10580130] |
| keratan sulfate biosynthetic process | biological process | The chemical reactions and pathways resulting in the formation of keratan sulfate, a glycosaminoglycan with repeat units consisting of beta-1,4-linked D-galactopyranosyl-beta-(1,4)-N-acetyl-D-glucosamine 6-sulfate and with variable amounts of fucose, sialic acid and mannose units; keratan sulfate chains are covalently linked by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylose to peptidyl-threonine or serine residues. [ISBN:0198547684, RESID:AA0247] |
| viral protein processing | biological process | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein. [GOC:bf, GOC:jl, ISBN:0781702534] |
| protein modification process | biological process | The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). [GOC:bf, GOC:jl] |
| sialylation | biological process | The covalent attachment of sialic acid to a substrate molecule. [GOC:cjm] |
| negative regulation of activated CD8-positive, alpha-beta T cell apoptotic process | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of activated CD8-positive, alpha-beta T cell apoptotic process. [GO_REF:0000058, GOC:TermGenie, PMID:24187568] |
| protein sialylation | biological process | A protein modification process that results in the addition of a sialic acid unit to the end of an oligosaccharide chain in a glycoprotein. [PMID:21930713] |
| protein glycosylation | biological process | A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins. [GOC:curators, GOC:pr] |