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InterPro: IPR007006 Glycosyltransferase, ALG10

Protein matchesHelp
UniProtKB
Matches:
127 proteins
AccessionHelp IPR007006 Glycosyltransferase_ALG10
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Children IPR016900 Alpha-1, 2 glucosyltransferase Alg10
GO Term annotationHelp
Function GO:0016758 transferase activity, transferring hexosyl groups
Component GO:0016021 integral to membrane
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Members of this entry are glycosyltransferases, belonging to the ALG10 family. The majority of the members are annotated as alpha-1,2 glucosyltransferas. The ALG10 protein from Saccharomyces cerevisiae (Baker's yeast) encodes the alpha-1,2 glucosyltransferase of the endoplasmic reticulum. This protein has been characterised in Rat as potassium channel regulator 1 [1].

Database linksHelp
Enzyme: EC:2.4.1
PANDIT: PF04922
Pfam Clan: CL0111.7

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR007006 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O88788 Putative alpha-1,2-glucosyltransferase ALG10-B

P0C147 Alpha-1,2 glucosyltransferase ALG10

P50076 Alpha-1,2 glucosyltransferase ALG10

Q3UGP8 Putative alpha-1,2-glucosyltransferase ALG10-B

Q5BKT4 Alpha-1,2-glucosyltransferase ALG10-A

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR007006 Glycosyltransferase, ALG10
IPR016900 Alpha-1, 2 glucosyltransferase Alg10
ModBase

PublicationsHelp
1. Hoshi N, Takahashi H, Shahidullah M, Yokoyama S, Higashida H.
KCR1, a membrane protein that facilitates functional expression of non-inactivating K+ currents associates with rat EAG voltage-dependent K+ channels.
J. Biol. Chem. 273 23080-5 1998 [PubMed: 9722534]
http://dx.doi.org/10.1074/jbc.273.36.23080

Additional ReadingHelp
Burda P, Aebi M.
The ALG10 locus of Saccharomyces cerevisiae encodes the alpha-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation.
Glycobiology 8 1998 455-62 [PubMed: 9597543]
http://dx.doi.org/10.1093/glycob/8.5.455
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InterPro 23.1