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

Last updated October 12, 2024

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.

Related Research Articles

A congenital disorder of glycosylation is one of several rare inborn errors of metabolism in which glycosylation of a variety of tissue proteins and/or lipids is deficient or defective. Congenital disorders of glycosylation are sometimes known as CDG syndromes. They often cause serious, sometimes fatal, malfunction of several different organ systems in affected infants. The most common sub-type is PMM2-CDG where the genetic defect leads to the loss of phosphomannomutase 2 (PMM2), the enzyme responsible for the conversion of mannose-6-phosphate into mannose-1-phosphate.

Dolichol refers to any of a group of long-chain mostly unsaturated organic compounds that are made up of varying numbers of isoprene units terminating in an α-saturated isoprenoid group, containing an alcohol functional group.

In enzymology, a dolichyl-phosphate beta-D-mannosyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a dolichyl-phosphate-mannose-protein mannosyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a dolichol kinase is an enzyme that catalyzes the chemical reaction

UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosaminephosphotransferase is an enzyme that in humans is encoded by the DPAGT1 gene.

Protein O-mannosyl-transferase 1 is an enzyme that in humans is encoded by the POMT1 gene. It is a member of the dolichyl-phosphate-mannose-protein mannosyltransferases.

Alpha-1,3/1,6-mannosyltransferase ALG2 is an enzyme that is encoded by the ALG2 gene. Mutations in the human gene are associated with congenital defects in glycosylation The protein encoded by the ALG2 gene belongs to two classes of enzymes: GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase and GDP-Man:Man2GlcNAc2-PP-dolichol alpha-1,6-mannosyltransferase.

Nucleotide exchange factor SIL1 is a protein that in humans is encoded by the SIL1 gene.

Dolichol-phosphate mannosyltransferase is an enzyme that in humans is encoded by the DPM1 gene.

Phosphatidylinositol N-acetylglucosaminyltransferase subunit C is an enzyme that in humans is encoded by the PIGC gene.

Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase is an enzyme that in humans is encoded by the ALG12 gene.

GPI transamidase component PIG-S is an enzyme that in humans is encoded by the PIGS gene. This gene encodes a protein that is involved in GPI-anchor biosynthesis.

Dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase is an enzyme that, in humans, is encoded by the ALG3 gene.

GPI mannosyltransferase 3 is an enzyme that in humans is encoded by the PIGB gene.

Chitobiosyldiphosphodolichol beta-mannosyltransferase is an enzyme that is encoded by ALG1 whose structure and function has been conserved from lower to higher organisms.

N-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom, in a process called N-glycosylation, studied in biochemistry. The resulting protein is called an N-linked glycan, or simply an N-glycan.

dolichyl-phosphate mannosyltransferase polypeptide 3, also known as DPM3, is a human gene.

Asparagine-linked glycosylation protein 11 is an enzyme encoded by the ALG11 gene.

Dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase is an enzyme with systematic name dolichyl beta-D-mannosyl phosphate:D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha- )-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-mannosyltransferase. This enzyme catalyses the following chemical reaction

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000136908 – Ensembl, May 2017
1 2 3 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.
1 2 "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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000136908 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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] 1 2 "Entrez Gene: dolichyl-phosphate mannosyltransferase polypeptide 2".

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DPM2

Contents

Function

Clinical significance

Related Research Articles

References

Further reading