DPM2

Protein-coding gene in the species Homo sapiens
DPM2
Identifiers
AliasesDPM2, CDG1U, dolichyl-phosphate mannosyltransferase polypeptide 2, regulatory subunit, dolichyl-phosphate mannosyltransferase subunit 2, regulatory
External IDsOMIM: 603564; MGI: 1330238; HomoloGene: 99726; GeneCards: DPM2; OMA:DPM2 - orthologs
Gene location (Human)
Chromosome 9 (human)
Chr.Chromosome 9 (human)[1]
Chromosome 9 (human)
Genomic location for DPM2
Genomic location for DPM2
Band9q34.11Start127,935,099 bp[1]
End127,938,484 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for DPM2
Genomic location for DPM2
Band2|2 BStart32,460,870 bp[2]
End32,463,591 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
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
BioGPS
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
SpeciesHumanMouse
Entrez

8818

13481

Ensembl

ENSG00000136908

ENSMUSG00000026810

UniProt

O94777

Q9Z324

RefSeq (mRNA)

NM_152690
NM_003863

NM_010073

RefSeq (protein)

NP_003854
NP_001365365
NP_001365366

NP_034203

Location (UCSC)Chr 9: 127.94 – 127.94 MbChr 2: 32.46 – 32.46 Mb
PubMed 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]

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

  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".

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.


  • v
  • t
  • e