Protein-coding gene in the species Homo sapiens
DPM2 |
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Identifiers |
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Aliases | DPM2, CDG1U, dolichyl-phosphate mannosyltransferase polypeptide 2, regulatory subunit, dolichyl-phosphate mannosyltransferase subunit 2, regulatory |
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External IDs | OMIM: 603564; MGI: 1330238; HomoloGene: 99726; GeneCards: DPM2; OMA:DPM2 - orthologs |
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Gene location (Human) |
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| Chr. | Chromosome 9 (human)[1] |
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| Band | 9q34.11 | Start | 127,935,099 bp[1] |
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End | 127,938,484 bp[1] |
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Gene location (Mouse) |
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| Chr. | Chromosome 2 (mouse)[2] |
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| Band | 2|2 B | Start | 32,460,870 bp[2] |
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End | 32,463,591 bp[2] |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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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
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| Top expressed in | - yolk sac
- perirhinal cortex
- entorhinal cortex
- granulocyte
- superior frontal gyrus
- primary visual cortex
- neural tube
- CA3 field
- internal carotid artery
- lip
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| More reference expression data |
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BioGPS | |
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Gene ontology |
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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 |
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Orthologs |
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Species | Human | Mouse |
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Entrez | | |
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Ensembl | | |
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UniProt | | |
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RefSeq (mRNA) | | |
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RefSeq (protein) | |
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NP_003854 NP_001365365 NP_001365366 |
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Location (UCSC) | Chr 9: 127.94 – 127.94 Mb | Chr 2: 32.46 – 32.46 Mb |
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PubMed search | [3] | [4] |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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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".
Further reading
- 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.