DPM1

Protein-coding gene in the species Homo sapiens
DPM1
Identifiers
AliasesDPM1, CDGIE, MPDS, dolichyl-phosphate mannosyltransferase polypeptide 1, catalytic subunit, dolichyl-phosphate mannosyltransferase subunit 1, catalytic
External IDsOMIM: 603503; MGI: 1330239; HomoloGene: 2865; GeneCards: DPM1; OMA:DPM1 - orthologs
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for DPM1
Genomic location for DPM1
Band20q13.13Start50,934,867 bp[1]
End50,959,140 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for DPM1
Genomic location for DPM1
Band2|2 H3Start168,050,968 bp[2]
End168,072,511 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • epithelium of nasopharynx

  • germinal epithelium

  • sperm

  • Skeletal muscle tissue of biceps brachii

  • oral cavity

  • skin of hip

  • gums

  • gingival epithelium

  • amniotic fluid

  • mucosa of pharynx
Top expressed in
  • spermatocyte

  • spermatid

  • yolk sac

  • morula

  • blastocyst

  • right kidney

  • muscle of thigh

  • neural layer of retina

  • embryo

  • lip
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • glycosyltransferase activity
  • dolichyl-phosphate beta-D-mannosyltransferase activity
  • protein binding
  • dolichyl-phosphate-mannose-protein mannosyltransferase activity
Cellular component
  • endoplasmic reticulum membrane
  • membrane
  • endoplasmic reticulum
  • dolichol-phosphate-mannose synthase complex
  • nucleus
Biological process
  • protein O-linked mannosylation
  • protein N-linked glycosylation via asparagine
  • protein glycosylation
  • GPI anchor biosynthetic process
  • protein mannosylation
  • dolichol metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8813

13480

Ensembl

ENSG00000000419

ENSMUSG00000078919

UniProt

O60762

O70152

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 MbChr 2: 168.05 – 168.07 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000000419 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000078919 – 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.
  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. Bibcode:1997PNAS...94.7873C. 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. ^ a b "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

  • GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview
  • v
  • t
  • e
2.4.1: Hexosyl-
transferases
Glucosyl-
Galactosyl-
Glucuronosyl-
Fucosyl-
Mannosyl-
2.4.2: Pentosyl-
transferases
Ribose
ADP-ribosyltransferase
Phosphoribosyltransferase
Other
Other
2.4.99: Sialyl
transferases


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