DPM1

From Wikipedia, the free encyclopedia

Dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit

Identifiers

DPM1; CDGIE; MPDS

External IDs

OMIM: 603503 MGI: 1330239 HomoloGene: 2865

Gene ontology
Molecular Function:	• dolichyl-phosphate-mannose-protein mannosyltransferase activity • dolichyl-phosphate beta-D-mannosyltransferase activity • protein binding • transferase activity, transferring glycosyl groups
Cellular Component:	• endoplasmic reticulum • endoplasmic reticulum membrane • mannosyltransferase complex
Biological Process:	• GPI anchor biosynthetic process • protein amino acid C-linked glycosylation via 2'-alpha-mannosyl-L-tryptophan • protein amino acid O-linked mannosylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_003859 (mRNA)
NP_003850 (protein)

NM_010072 (mRNA)
NP_034202 (protein)

Location

Chr 20: 48.98 - 49.01 Mb

n/a

Pubmed search

[1]

[2]

Dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit, also known as DPM1, is a human gene.^[1]

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. Dol-P-Man is synthesized from GDP-mannose and dolichol-phosphate on the cytosolic side of the ER by the enzyme dolichyl-phosphate mannosyltransferase. Human DPM1 lacks a carboxy-terminal transmembrane domain and signal sequence and is regulated by DPM2.^[1]

[edit] References

^ ^a ^b Entrez Gene: DPM1 dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit.

[edit] Further reading

Colussi PA, Taron CH, Mack JC, Orlean P (1997). "Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe.". Proc. Natl. Acad. Sci. U.S.A. 94 (15): 7873–8. PMID 9223280.
Tomita S, Inoue N, Maeda Y, et al. (1998). "A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for synthesis of dolichol-phosphate-mannose in mammalian cells.". J. Biol. Chem. 273 (15): 9249–54. PMID 9535917.
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. PMID 9724629.
Kim S, Westphal V, Srikrishna G, et al. (2000). "Dolichol phosphate mannose synthase (DPM1) mutations define congenital disorder of glycosylation Ie (CDG-Ie)". J. Clin. Invest. 105 (2): 191–8. PMID 10642597.
Imbach T, Schenk B, Schollen E, et al. (2000). "Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie.". J. Clin. Invest. 105 (2): 233–9. PMID 10642602.
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. PMID 10835346.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. doi:10.1073/pnas.242603899. PMID 12477932.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
García-Silva MT, Matthijs G, Schollen E, et al. (2005). "Congenital disorder of glycosylation (CDG) type Ie. A new patient.". J. Inherit. Metab. Dis. 27 (5): 591–600. PMID 15669674.
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.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.