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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | DPM1, CDGIE, MPDS, dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit, dolichyl-phosphate mannosyltransferase subunit 1, catalytic | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 603503 MGI: 1330239 HomoloGene: 2865 GeneCards: DPM1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Dolichol-phosphate mannosyltransferase is an enzyme that in humans is encoded by the DPM1 gene.[5][6][7]
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. 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.[7]
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000000419 - Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000078919 - 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.
- ↑ Colussi PA, Taron CH, Mack JC, Orlean P (Jul 1997). "Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe". Proceedings of the National Academy of Sciences of the United States of America. 94 (15): 7873–8. Bibcode:1997PNAS...94.7873C. doi:10.1073/pnas.94.15.7873. PMC 21522. PMID 9223280.
- ↑ Tomita S, Inoue N, Maeda Y, Ohishi K, Takeda J, Kinoshita T (Apr 1998). "A homologue of Saccharomyces cerevisiae Dpm1p is not sufficient for synthesis of dolichol-phosphate-mannose in mammalian cells". The Journal of Biological Chemistry. 273 (15): 9249–54. doi:10.1074/jbc.273.15.9249. PMID 9535917.
- 1 2 "Entrez Gene: DPM1 dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit".
Further reading
- Maeda Y, Tomita S, Watanabe R, Ohishi K, Kinoshita T (Sep 1998). "DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate". The EMBO Journal. 17 (17): 4920–9. doi:10.1093/emboj/17.17.4920. PMC 1170821. PMID 9724629.
- Kim S, Westphal V, Srikrishna G, Mehta DP, Peterson S, Filiano J, Karnes PS, Patterson MC, Freeze HH (Jan 2000). "Dolichol phosphate mannose synthase (DPM1) mutations define congenital disorder of glycosylation Ie (CDG-Ie)". The Journal of Clinical Investigation. 105 (2): 191–8. doi:10.1172/JCI7302. PMC 377427. PMID 10642597.
- Imbach T, Schenk B, Schollen E, Burda P, Stutz A, Grunewald S, Bailie NM, King MD, Jaeken J, Matthijs G, Berger EG, Aebi M, Hennet T (Jan 2000). "Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie". The Journal of Clinical Investigation. 105 (2): 233–9. doi:10.1172/JCI8691. PMC 377434. PMID 10642602.
- Maeda Y, Tanaka S, Hino J, Kangawa K, Kinoshita T (Jun 2000). "Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3". The EMBO Journal. 19 (11): 2475–82. doi:10.1093/emboj/19.11.2475. PMC 212771. PMID 10835346.
- García-Silva MT, Matthijs G, Schollen E, Cabrera JC, Sanchez del Pozo J, Martí Herreros M, Simón R, Maties M, Martín Hernández E, Hennet T, Briones P (2005). "Congenital disorder of glycosylation (CDG) type Ie. A new patient". Journal of Inherited Metabolic Disease. 27 (5): 591–600. doi:10.1023/B:BOLI.0000042984.42433.d8. PMID 15669674. S2CID 5878710.
- Ashida H, Maeda Y, Kinoshita T (Jan 2006). "DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3". The Journal of Biological Chemistry. 281 (2): 896–904. doi:10.1074/jbc.M511311200. PMID 16280320.
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 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. S2CID 7827573.
- Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
External links
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