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Dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit
Symbols DPM1 ; CDGIE; MPDS
External IDs OMIM603503 MGI1330239 HomoloGene2865 ChEMBL: 2572 GeneCards: DPM1 Gene
EC number
RNA expression pattern
PBB GE DPM1 202673 at tn.png
More reference expression data
Species Human Mouse
Entrez 8813 13480
Ensembl ENSG00000000419 ENSMUSG00000078919
UniProt O60762 O70152
RefSeq (mRNA) NM_003859 NM_001310084
RefSeq (protein) NP_003850 NP_001297013
Location (UCSC) Chr 20:
50.93 – 50.96 Mb
Chr 2:
168.21 – 168.23 Mb
PubMed search [1] [2]

Dolichol-phosphate mannosyltransferase is an enzyme that in humans is encoded by the DPM1 gene.[1][2][3]

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.[3]

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.[4] Male and female animals underwent a standardized phenotypic screen[5] to determine the effects of deletion.[6][7][8][9] Additional screens performed: - In-depth immunological phenotyping[10]


  1. ^ Colussi PA, Taron CH, Mack JC, Orlean P (Aug 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. doi:10.1073/pnas.94.15.7873. PMC 21522. PMID 9223280. 
  2. ^ Tomita S, Inoue N, Maeda Y, Ohishi K, Takeda J, Kinoshita T (May 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. doi:10.1074/jbc.273.15.9249. PMID 9535917. 
  3. ^ a b "Entrez Gene: DPM1 dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit". 
  4. ^ Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Opthalmologica 88: 925-7.doi:10.1111/j.1755-3768.2010.4142.x: Wiley. 
  5. ^ a b "International Mouse Phenotyping Consortium". 
  6. ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V et al. (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. 
  7. ^ Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718. 
  8. ^ 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. 
  9. ^ White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN et al. (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. PMID 23870131. 
  10. ^ a b "Infection and Immunity Immunophenotyping (3i) Consortium". 

Further reading[edit]

External links[edit]