DPM2

DPM2
Identifiers
Aliases	DPM2, CDG1U, dolichyl-phosphate mannosyltransferase polypeptide 2, regulatory subunit, dolichyl-phosphate mannosyltransferase subunit 2, regulatory
External IDs	OMIM: 603564; MGI: 1330238; HomoloGene: 99726; GeneCards: DPM2; OMA:DPM2 - orthologs
Gene location (Human)
Chr.	Chromosome 9 (human)
End	127,938,484 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	32,463,591 bp
RNA expression pattern
	Top expressed in
	body of pancreas; ; left lobe of thyroid gland; ; right lobe of thyroid gland; ; body of stomach; ; right uterine tube; ; mucosa of transverse colon; ; islet of Langerhans; ; stromal cell of endometrium; ; right frontal lobe; ; minor salivary glands;
	Top expressed in
	yolk sac; ; perirhinal cortex; ; entorhinal cortex; ; granulocyte; ; superior frontal gyrus; ; primary visual cortex; ; neural tube; ; CA3 field; ; internal carotid artery; ; lip;
	More reference expression data
	n/a
Gene ontology
Molecular function	dolichyl-phosphate beta-D-mannosyltransferase activity; protein binding; enzyme regulator activity;
Cellular component	integral component of membrane; endoplasmic reticulum membrane; membrane; integral component of endoplasmic reticulum membrane; endoplasmic reticulum; dolichol-phosphate-mannose synthase complex; glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex;
Biological process	preassembly of GPI anchor in ER membrane; regulation of protein stability; protein O-linked mannosylation; protein glycosylation; GPI anchor biosynthetic process; regulation of catalytic activity; dolichol metabolic process; protein N-linked glycosylation via asparagine;
	Sources:Amigo / QuickGO
Orthologs
	8818
	13481
	ENSG00000136908
	ENSMUSG00000026810
	O94777
	Q9Z324
	NM_152690; NM_003863
	NM_010073
	NP_003854; NP_001365365; NP_001365366
	NP_034203
	Wikidata
View/Edit Human	View/Edit Mouse

Dolichol phosphate-mannose biosynthesis regulatory protein is a protein that in humans is encoded by the DPM2 gene.^[5]

Function

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, defective N-linked glycosylation and deficient O-mannosylation of α-dystroglycan. 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.^[5]

Clinical significance

Mutations in this gene are associated with congenital disorder of glycosylation.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000136908 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000026810 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: dolichyl-phosphate mannosyltransferase polypeptide 2".

Suzuki H, Fukunishi Y, Kagawa I, et al. (2001). "Protein-protein interaction panel using mouse full-length cDNAs". Genome Res. 11 (10): 1758–65. doi:10.1101/gr.180101. PMC 311163. PMID 11591653.
Maeda Y, Tanaka S, Hino J, et al. (2000). "Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3". EMBO J. 19 (11): 2475–82. doi:10.1093/emboj/19.11.2475. PMC 212771. PMID 10835346.
Watanabe R, Murakami Y, Marmor MD, et al. (2000). "Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2". EMBO J. 19 (16): 4402–11. doi:10.1093/emboj/19.16.4402. PMC 302040. PMID 10944123.
Kinoshita T, Inoue N (2000). "Dissecting and manipulating the pathway for glycosylphos-phatidylinositol-anchor biosynthesis". Curr Opin Chem Biol. 4 (6): 632–8. doi:10.1016/s1367-5931(00)00151-4. PMID 11102867.
Ashida H, Maeda Y, Kinoshita T (2006). "DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3". J. Biol. Chem. 281 (2): 896–904. doi:10.1074/jbc.M511311200. PMID 16280320.
Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Lennon G, Auffray C, Polymeropoulos M, Soares MB (1996). "The I.M.A.G.E. Consortium: an integrated molecular analysis of genomes and their expression". Genomics. 33 (1): 151–2. doi:10.1006/geno.1996.0177. PMID 8617505.
Maeda Y, Tomita S, Watanabe R, et al. (1998). "DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate". EMBO J. 17 (17): 4920–9. doi:10.1093/emboj/17.17.4920. PMC 1170821. PMID 9724629.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

This article on a gene on human chromosome 9 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000136908 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000026810 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: dolichyl-phosphate mannosyltransferase polypeptide 2".

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Function

Clinical significance

References

Further reading