DPM2 (original) (raw)

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Protein-coding gene in the species Homo sapiens

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)[1]Band9q34.11Start127,935,099 bp[1]End127,938,484 bp[1]
Gene location (Mouse)Chr.Chromosome 2 (mouse)[2]Band2|2 BStart32,460,870 bp[2]End32,463,591 bp[2]
RNA expression patternBgeeHuman Mouse (ortholog)Top expressed inbody of pancreasleft lobe of thyroid glandright lobe of thyroid glandbody of stomachright uterine tubemucosa of transverse colonislet of Langerhansstromal cell of endometriumright frontal lobeminor salivary glandsTop expressed inyolk sacperirhinal cortexentorhinal cortexgranulocytesuperior frontal gyrusprimary visual cortexneural tubeCA3 fieldinternal carotid arterylipMore reference expression dataBioGPSn/a
Gene ontologyMolecular 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
OrthologsSpeciesHuman MouseEntrez881813481EnsemblENSG00000136908ENSMUSG00000026810UniProtO94777Q9Z324RefSeq (mRNA)NM_152690NM_003863NM_010073RefSeq (protein)NP_003854NP_001365365NP_001365366NP_034203Location (UCSC)Chr 9: 127.94 – 127.94 MbChr 2: 32.46 – 32.46 MbPubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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

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

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000136908 – Ensembl, May 2017
2. ^ a b c 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.
5. ^ 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.