Version 5.4
Bos taurus Protein: DPM3
Summary
InnateDB Protein IDBP-683819.2
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol DPM3
Protein Name Dolichol-phosphate mannosyltransferase subunit 3
Synonyms
Species Bos taurus
Ensembl Protein ENSBTAP00000004597
InnateDB Gene IDBG-632218 (DPM3)
Protein Structure
UniProt Annotation
Function Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit DPM1 to the ER. {ECO:0000250}.
Subcellular Localization Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004582 dolichyl-phosphate beta-D-mannosyltransferase activity
GO:0005515 protein binding
Biological Process
GO:0006486 protein glycosylation
GO:0006506 GPI anchor biosynthetic process
GO:0031647 regulation of protein stability
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane
GO:0016021 integral component of membrane
GO:0030176 integral component of endoplasmic reticulum membrane
GO:0033185 dolichol-phosphate-mannose synthase complex
Protein Structure and Domains
PDB ID
InterPro IPR013174 Dolichol-phosphate mannosyltransferase subunit 3
PFAM PF08285
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q3ZC71
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 509745
UniGene Bt.49459
RefSeq NP_001029532
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL BC102881
GenPept AAI02882

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