Version 5.4
Bos taurus Gene: BT.20421
Summary
InnateDB Gene IDBG-639083.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol BT.20421
Gene Name dolichol phosphate-mannose biosynthesis regulatory protein
Synonyms
Species Bos taurus
Ensembl Gene ENSBTAG00000003388
Encoded Proteins
IDBP-691206
dolichol phosphate-mannose biosynthesis regulatory protein
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary This gene does not have any Entrez summary - the following is the summary from its human ortholog ENSG00000136908:
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 hydrophobic protein that contains 2 predicted transmembrane domains and a putative ER localization signal near the C terminus. This protein associates with DPM1 in vivo and is required for the ER localization and stable expression of DPM1 and also enhances the binding of dolichol-phosphate to DPM1. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 11:98612580-98615633
Strand Reverse strand
Band
Transcripts
ENSBTAT00000004393 ENSBTAP00000004393
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 4 interaction(s) predicted by orthology.
Predicted by orthology
Total 4 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004582 dolichyl-phosphate beta-D-mannosyltransferase activity
GO:0005515 protein binding
Biological Process
GO:0006506 GPI anchor biosynthetic process
GO:0009059 macromolecule biosynthetic process
GO:0031647 regulation of protein stability
Cellular Component
GO:0000506 glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex
GO:0030176 integral component of endoplasmic reticulum membrane
GO:0033185 dolichol-phosphate-mannose synthase complex
Orthologs
Species
Homo sapiens
Mus musculus
Gene ID
Gene Order
ENSG00000136908
View Gene Order
ENSMUSG00000026810
View Gene Order
Pathway Predictions based on Human Orthology Data
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_952
Synthesis of glycosylphosphatidylinositol (GPI) 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
REACT_248642
Synthesis of substrates in N-glycan biosythesis pathway
REACT_244576
Post-translational modification: synthesis of GPI-anchored proteins pathway
REACT_262413
Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein pathway
REACT_247926
Metabolism of proteins pathway
REACT_236283
Post-translational protein modification pathway
REACT_243945
Synthesis of glycosylphosphatidylinositol (GPI) pathway
REACT_251842
Synthesis of dolichyl-phosphate mannose pathway
REACT_237472
Asparagine N-linked glycosylation pathway
KEGG
hsa00563
Glycosylphosphatidylinositol(GPI)-anchor biosynthesis pathway
hsa00510
N-Glycan biosynthesis pathway
mmu00510
N-Glycan biosynthesis pathway
mmu00563
Glycosylphosphatidylinositol(GPI)-anchor biosynthesis pathway
INOH
PID NCI
Cross-References
SwissProt
TrEMBL F1MYZ5
UniProt Splice Variant
Entrez Gene 523737
UniGene Bt.20421
RefSeq NM_001046268
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL DAAA02032171
GenPept
RNA Seq Atlas 523737

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