DPM1
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
Gene location (Human) Chr. Chromosome 20 (human)[1] Band 20q13.13 Start 50,934,867 bp[1] End 50,959,140 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 H3 Start 168,050,968 bp[2] End 168,072,511 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in germinal epithelium sperm oral cavity gums amniotic fluid superior surface of tongue parietal pleura palpebral conjunctiva bronchial epithelial cell body of tongue Top expressed in spermatocyte spermatid yolk sac morula blastocyst lip proximal tubule esophagus facial motor nucleus neural tube 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 Species Human Mouse 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 Mb Chr 2: 168.05 – 168.07 Mb PubMed search [3] [4]
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]