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DPM1








DPM1


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DPM1
Identifiers
Aliases
DPM1, CDGIE, MPDS, dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit, dolichyl-phosphate mannosyltransferase subunit 1, catalytic
External IDs MGI: 1330239 HomoloGene: 2865 GeneCards: DPM1


















Gene location (Human)
Chromosome 20 (human)
Chr. Chromosome 20 (human)[1]

Chromosome 20 (human)
Genomic location for DPM1

Genomic location for DPM1

Band 20q13.13 Start 50,934,867 bp[1]
End 50,958,555 bp[1]























RNA expression pattern
PBB GE DPM1 202673 at fs.png
More reference expression data















Orthologs
Species Human Mouse
Entrez





Ensembl





UniProt





RefSeq (mRNA)


NM_003859
NM_001317034
NM_001317035
NM_001317036




NM_010072
NM_001310084

RefSeq (protein)


NP_001303963
NP_001303964
NP_001303965
NP_003850




NP_001297013
NP_034202

Location (UCSC) Chr 20: 50.93 – 50.96 Mb Chr 2: 168.21 – 168.23 Mb

PubMed search
[3] [4]
Wikidata



View/Edit Human View/Edit Mouse

Dolichol-phosphate mannosyltransferase is an enzyme that in humans is encoded by the DPM1 gene.[5][6][7]




Contents






  • 1 Function


  • 2 Model organisms


  • 3 References


  • 4 Further reading


  • 5 External links





Function[edit]


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]



Model organisms[edit]


Model organisms have been used in the study of DPM1 function. A conditional knockout mouse line called Dpm1tm1b(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute.[8] Male and female animals underwent a standardized phenotypic screen[9] to determine the effects of deletion.[10][11][12][13] Additional screens performed: - In-depth immunological phenotyping[14]


















































































































References[edit]





  1. ^ abc GRCh38: Ensembl release 89: ENSG00000000419 - Ensembl, May 2017


  2. ^ abc GRCm38: Ensembl release 89: ENSMUSG00000078919 - Ensembl, May 2017


  3. ^ "Human PubMed Reference:"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output q{quotes:"""""""'""'"}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-limited a,.mw-parser-output .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}


  4. ^ "Mouse PubMed Reference:".


  5. ^ 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. doi:10.1073/pnas.94.15.7873. PMC 21522. PMID 9223280.


  6. ^ 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.


  7. ^ ab "Entrez Gene: DPM1 dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit".


  8. ^ Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.


  9. ^ ab "International Mouse Phenotyping Consortium".


  10. ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.


  11. ^ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.


  12. ^ Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.


  13. ^ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.


  14. ^ ab "Infection and Immunity Immunophenotyping (3i) Consortium".




Further reading[edit]


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  • 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.


  • 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.


  • 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[edit]


  • GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview












Retrieved from "https://en.wikipedia.org/w/index.php?title=DPM1&oldid=798055789"





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