Version 5.4
Homo sapiens Gene: DPM3
Summary
InnateDB Gene IDBG-103113.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol DPM3
Gene Name dolichyl-phosphate mannosyltransferase polypeptide 3
Synonyms
Species Homo sapiens
Ensembl Gene ENSG00000179085
Encoded Proteins
IDBP-103115
dolichyl-phosphate mannosyltransferase polypeptide 3
IDBP-103117
dolichyl-phosphate mannosyltransferase polypeptide 3
IDBP-103119
dolichyl-phosphate mannosyltransferase polypeptide 3
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary Dolichol-phosphate mannose (Dol-P-Man) serves as a donor of mannosyl residues on the lumenal side of the endoplasmic reticulum (ER). Lack of Dol-P-Man results in defective surface expression of GPI-anchored proteins. Dol-P-Man is synthesized from GDP-mannose and dolichol-phosphate on the cytosolic side of the ER by the enzyme dolichyl-phosphate mannosyltransferase. The protein encoded by this gene is a subunit of dolichyl-phosphate mannosyltransferase and acts as a stabilizer subunit of the dolichyl-phosphate mannosyltransferase complex. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 1:155139891-155140595
Strand Reverse strand
Band q22
Transcripts
ENST00000341298 ENSP00000344338
ENST00000368400 ENSP00000357385
ENST00000368399 ENSP00000357384
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 4 experimentally validated interaction(s) in this database.
Experimentally validated
Total 4 [view]
Protein-Protein 4 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0004582 dolichyl-phosphate beta-D-mannosyltransferase activity
GO:0005515 protein binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006488 dolichol-linked oligosaccharide biosynthetic process
GO:0006501 C-terminal protein lipidation
GO:0006506 GPI anchor biosynthetic process
GO:0018279 protein N-linked glycosylation via asparagine
GO:0018406 protein C-linked glycosylation via 2'-alpha-mannosyl-L-tryptophan
GO:0031647 regulation of protein stability
GO:0035268 protein mannosylation
GO:0035269 protein O-linked mannosylation
GO:0043687 post-translational protein modification
GO:0044267 cellular protein metabolic process
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane
GO:0030176 integral component of endoplasmic reticulum membrane
GO:0031501 mannosyltransferase complex
GO:0033185 dolichol-phosphate-mannose synthase complex
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000042737
View Gene Order
ENSBTAG00000003535
Not yet available
Pathways
NETPATH
REACTOME
REACT_2032
Synthesis of dolichyl-phosphate mannose pathway
REACT_22433
Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein pathway
REACT_22426
Asparagine N-linked glycosylation pathway
REACT_1853
Post-translational modification: synthesis of GPI-anchored proteins pathway
REACT_22161
Post-translational protein modification pathway
REACT_22387
Synthesis of substrates in N-glycan biosythesis pathway
REACT_17015
Metabolism of proteins pathway
KEGG
hsa00510
N-Glycan biosynthesis pathway
INOH
PID NCI
Cross-References
SwissProt Q9P2X0
TrEMBL B4DEH1 Q86TM7
UniProt Splice Variant
Entrez Gene 54344
UniGene
RefSeq NM_018973 NM_153741
HUGO HGNC:3007
OMIM 605951
CCDS CCDS1094 CCDS1095
HPRD
IMGT
EMBL AB028128 AF312922 AF312923 AK293625 AL691442 BC032223 BC104202 BC104203 CH471121
GenPept AAH32223 AAI04203 AAI04204 AAK28486 AAK28487 BAA96291 BAG57082 CAI15325 CAI15326 EAW53126
RNA Seq Atlas 54344

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