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Entry
map00512                    Pathway                                

Name
Mucin type O-Glycan biosynthesis
Description
O-glycans are a class of glycans that modify serine or threonine residues of proteins. Biosynthesis of O-glycans starts from the transfer of N-acetylgalactosamine (GalNAc) to serine or threonine. The first GalNAc may be extended with sugars including galactose, N-acetylglucosamine, fucose, or sialic acid, but not mannose, glucose, or xylose. Depending on the sugars added, there are four common O-glycan core structures, cores 1 through 4, and an additional four, cores 5 though 8. Mucins are highly O-glycosylated glycoproteins ubiquitous in mucous secretions on cell surfaces and in body fluids. Mucin O-glycans can be branched, and many sugars or groups of sugars are antigenic. Important modifications of mucin O-glycans include O-acetylation of sialic acid and O-sulfation of galactose and N-acetylglucosamine.
Class
Metabolism; Glycan biosynthesis and metabolism
BRITE hierarchy
Pathway map
Mucin type O-Glycan biosynthesis
map00512

All organismsOrtholog table
Module
M00056  
O-glycan biosynthesis, mucin type core [PATH:map00512]
Disease
H01188  
Tn syndrome
H01193  
Familial tumoral calcinosis (FTC)
Other DBs
GO: 
Reference
  Authors
Brockhausen I.
  Title
Pathways of O-glycan biosynthesis in cancer cells.
  Journal
Biochim Biophys Acta 1473:67-95 (1999)
Reference
  Authors
Iwai T, Inaba N, Naundorf A, Zhang Y, Gotoh M, Iwasaki H, Kudo T, Togayachi A, Ishizuka Y, Nakanishi H, Narimatsu H.
  Title
Molecular cloning and characterization of a novel UDP-GlcNAc:GalNAc-peptide beta1,3-N-acetylglucosaminyltransferase (beta 3Gn-T6), an enzyme synthesizing the core 3 structure of O-glycans.
  Journal
J Biol Chem 277:12802-9 (2002)
Reference
  Authors
Korekane H, Taguchi T, Sakamoto Y, Honke K, Dohmae N, Salminen H, Toivonen S, Helin J, Takio K, Renkonen O, Taniguchi N.
  Title
Purification and cDNA cloning of UDP-GlcNAc:GlcNAcbeta1-3Galbeta1-4Glc(NAc)-R [GlcNAc to Gal]beta1,6N-acetylglucosaminyltransferase from rat small intestine: a major carrier of dIGnT activity in rat small intestine.
  Journal
Glycobiology 13:387-400 (2003)
Reference
  Authors
van Die I, van Tetering A, Schiphorst WE, Sato T, Furukawa K, van den Eijnden DH.
  Title
The acceptor substrate specificity of human beta4-galactosyltransferase V indicates its potential function in O-glycosylation.
  Journal
FEBS Lett 450:52-6 (1999)
KO pathway
 

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