Version 5.4
Homo sapiens Protein: GLT25D2
Summary
InnateDB Protein IDBP-105342.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol GLT25D2
Protein Name glycosyltransferase 25 domain containing 2
Synonyms C1orf17; GLT25D2;
Species Homo sapiens
Ensembl Protein ENSP00000354960
InnateDB Gene IDBG-105336 (GLT25D2)
Protein Structure
UniProt Annotation
Function Has a beta-galactosyltransferase activity; transfers beta-galactose to hydroxylysine residues on collagen. {ECO:0000269PubMed:19075007}.
Subcellular Localization Endoplasmic reticulum lumen {ECO:0000255PROSITE-ProRule:PRU10138}.
Disease Associations
Tissue Specificity Expressed in brain and skeletal muscle. {ECO:0000269PubMed:19075007}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 2 experimentally validated interaction(s) in this database.
Experimentally validated
Total 2 [view]
Protein-Protein 1 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0050211 procollagen galactosyltransferase activity
Biological Process
GO:0009103 lipopolysaccharide biosynthetic process
GO:0030198 extracellular matrix organization
Cellular Component
GO:0005788 endoplasmic reticulum lumen
Protein Structure and Domains
PDB ID
InterPro IPR002654 Glycosyl transferase, family 25
IPR029044 Nucleotide-diphospho-sugar transferases
PFAM PF01755
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8IYK4
PhosphoSite PhosphoSite-Q8IYK4
TrEMBL Q5SXQ5
UniProt Splice Variant
Entrez Gene 23127
UniGene Hs.387995
RefSeq NP_055916
HUGO HGNC:16790
OMIM
CCDS CCDS1360
HPRD 13583
IMGT
EMBL AB011156 AF288389 AK095192 AL157943 AL592299 BC035672 CH471067
GenPept AAG60609 AAH35672 BAA25510 BAG53004 CAI14722 CAI17872 EAW91171 EAW91172

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca