Details of the Target
General Information of Target
Target ID | LDTP00699 | |||||
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Target Name | Alpha-N-acetylneuraminate alpha-2,8-sialyltransferase ST8SIA3 (ST8SIA3) | |||||
Gene Name | ST8SIA3 | |||||
Gene ID | 51046 | |||||
Synonyms |
SIAT8C; Alpha-N-acetylneuraminate alpha-2,8-sialyltransferase ST8SIA3; EC 2.4.3.-; Alpha-2,8-sialyltransferase 8C; Alpha-2,8-sialyltransferase III; Ganglioside GD3 synthase ST8SIA3; EC 2.4.3.8; ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3; Sia-a2,3-Gal-b1,4-Glc-NAc-R:a2,8-sialyltransferase; hST8Sia III; Sialyltransferase 8C; SIAT8-C; Sialyltransferase St8Sia III; ST8SiaIII
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3D Structure | ||||||
Sequence |
MRNCKMARVASVLGLVMLSVALLILSLISYVSLKKENIFTTPKYASPGAPRMYMFHAGFR
SQFALKFLDPSFVPITNSLTQELQEKPSKWKFNRTAFLHQRQEILQHVDVIKNFSLTKNS VRIGQLMHYDYSSHKYVFSISNNFRSLLPDVSPIMNKHYNICAVVGNSGILTGSQCGQEI DKSDFVFRCNFAPTEAFQRDVGRKTNLTTFNPSILEKYYNNLLTIQDRNNFFLSLKKLDG AILWIPAFFFHTSATVTRTLVDFFVEHRGQLKVQLAWPGNIMQHVNRYWKNKHLSPKRLS TGILMYTLASAICEEIHLYGFWPFGFDPNTREDLPYHYYDKKGTKFTTKWQESHQLPAEF QLLYRMHGEGLTKLTLSHCA |
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Target Bioclass |
Enzyme
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Family |
Glycosyltransferase 29 family
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Subcellular location |
Golgi apparatus membrane
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Function |
Catalyzes the transfer of 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 acceptor, such as N-linked oligosaccharides of glycoproteins and glycolipids through alpha-2,8-linkages. Forms oligosialic and polysialic acid on various sialylated N-acetyllactosamine oligosaccharides of glycoproteins, including FETUB N-glycans, a2-HS-glycoprotein (AHSG) and alpha 2,3-sialylated glycosphingolipids, such as alpha 2,3-sialylparagloboside and ganglioside GM3 and to a lesser extent NCAM1 N-glycans. However, it is much more specific to N-linked oligosaccharides of glycoproteins than glycosphingolipids. 2,3-sialylparagloboside serves as the best acceptor substrate among the glycolipids. alpha-Neu5Ac-(2->8)-alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-6S-D-GlcNAc and monosialyl and disialyl N-acetyllactosamines are the best acceptor substrates among glycoproteins. May plays critical role in the striatum by mediating the formation of disialylated and trisialylated terminal glycotopes on N- and O-glycans of specific striatal proteins, regulating their distribution in lipid rafts, affecting their interaction with other binding partners, and subsequently modulating striatal functions.
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Uniprot ID | ||||||
Ensemble ID | ||||||
HGNC ID |
Probe(s) Labeling This Target
ABPP Probe
Probe name | Structure | Binding Site(Ratio) | Interaction ID | Ref | |
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FBPP2 Probe Info |
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4.47 | LDD0318 | [1] |
The Interaction Atlas With This Target