The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
Functional site class:
O-Glycosylation site
Functional site description:
Site for attachment of a glucose residue to a serine.
ELM Description:
Site for attachment of a glucose residue to a serine
Pattern: C.(S).PC
Pattern Probability: 9.232e-07
Present in taxons: Cricetulus griseus Eumetazoa Gallus gallus Homo sapiens Mus musculus Rattus norvegicus Spodoptera frugiperda
Interaction Domain:
Galactosyl_T_2 (PF02709) Galactosyltransferase (Stochiometry: 1 : 1)
o See 2 Instances for MOD_OGLYCOS
o Abstract
O-Glucose is an unusual form of post-translational modification consisting of glucose directly attached to protein through O-linkage to a serine residue. Several serum proteins contain this unique modification on their epidermal growth factor (EGF)-like repeats. The enzymatic activity capable of adding glucose to EGF repeats is UDP-glucose:protein O-glucosyltransferase. The glucose is added in O-linkage to the EGF repeat. The two cysteines of the motif are the first and second of the six conserved cysteines of the EGF repeat. The enzyme recognizes not only the consensus sequence but also the 3D structure of the EGF repeat. O-glucosyltransferase activity has been detected in extracts of cell lines from insects to humans and a variety of rat tissues. Numerous secreted and cell surface proteins are predicted to bear O-glucose.
o 1 selected reference:

o 1 GO-Term:

o 2 Instances for MOD_OGLYCOS
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
P00740 F9
97 102 QYVDGDQCESNPCLNGGSCK TP 1 Homo sapiens (Human)
P08709 F7
110 115 SYSDGDQCASSPCQNGGSCK TP 1 Homo sapiens (Human)
Please cite: ELM 2016-data update and new functionality of the eukaryotic linear motif resource. (PMID:26615199)

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