Proteins > Beta-galactoside alpha-2,6-sialyltransferase 1
Page last updated: 2024-08-07 10:15:33

Beta-galactoside alpha-2,6-sialyltransferase 1

A beta-galactoside alpha-2,6-sialyltransferase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P15907]

Synonyms

Alpha 2,6-ST 1;
EC 2.4.99.1;
B-cell antigen CD75;
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1;
ST6Gal I;
ST6GalI;
Sialyltransferase 1

Research

Bioassay Publications (2)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's0 (0.00)24.3611
2020's2 (100.00)2.80

Compounds (1)

Drugs with Other Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
cytidine monophosphate n-acetylneuraminic acidHomo sapiens (human)Km37.100022

Enables

This protein enables 4 target(s):

TargetCategoryDefinition
beta-galactoside alpha-2,6-sialyltransferase activitymolecular functionCatalysis of the reaction: CMP-N-acetylneuraminate + beta-D-galactoside = N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP + H+. [EC:2.4.3.1, RHEA:11836]
protein bindingmolecular functionBinding to a protein. [GOC:go_curators]
sialyltransferase activitymolecular functionCatalysis 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]
protein homodimerization activitymolecular functionBinding to an identical protein to form a homodimer. [GOC:jl]

Located In

This protein is located in 5 target(s):

TargetCategoryDefinition
Golgi trans cisternacellular componentThe Golgi cisterna farthest from the endoplasmic reticulum; the final processing compartment through which proteins pass before exiting the Golgi apparatus; the compartment in which N-linked protein glycosylation is completed. [ISBN:0815316194]
Golgi membranecellular componentThe lipid bilayer surrounding any of the compartments of the Golgi apparatus. [GOC:mah]
extracellular regioncellular componentThe space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators]
Golgi medial cisternacellular componentThe middle Golgi cisterna (or cisternae). [ISBN:0815316194]
Golgi cisterna membranecellular componentThe lipid bilayer surrounding any of the thin, flattened compartments that form the central portion of the Golgi complex. [GOC:ecd, GOC:mah]

Active In

This protein is active in 1 target(s):

TargetCategoryDefinition
Golgi apparatuscellular componentA membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. [ISBN:0198506732]

Involved In

This protein is involved in 11 target(s):

TargetCategoryDefinition
N-acetylneuraminate metabolic processbiological processThe 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]
humoral immune responsebiological processAn immune response mediated through a body fluid. [GOC:hb, ISBN:0198506732]
O-glycan processingbiological processThe 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]
protein N-linked glycosylation via asparaginebiological processThe glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification. [GOC:jsg, RESID:AA0151, RESID:AA0420, RESID:AA0421]
viral protein processingbiological processAny protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein. [GOC:bf, GOC:jl, ISBN:0781702534]
positive regulation of mononuclear cell proliferationbiological processAny process that activates or increases the frequency, rate or extent of mononuclear cell proliferation. [GOC:add]
response to ethanolbiological processAny process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an ethanol stimulus. [GOC:go_curators]
negative regulation of chemotaxisbiological processAny process that stops, prevents, or reduces the frequency, rate or extent of the directed movement of a motile cell or organism in response to a specific chemical concentration gradient. [GOC:ai]
sialylationbiological processThe covalent attachment of sialic acid to a substrate molecule. [GOC:cjm]
regulation of substrate adhesion-dependent cell spreadingbiological processAny process that modulates the frequency, rate or extent of substrate adhesion-dependent cell spreading. [GOC:TermGenie, GOC:yaf]
negative regulation of macrophage apoptotic processbiological processAny process that stops, prevents, or reduces the frequency, rate or extent of macrophage apoptotic process. [GOC:BHF, GOC:mtg_apoptosis]