Aliases for DPM1 Gene
- Dolichyl-Phosphate Mannosyltransferase Subunit 1, Catalytic 2 3 5
- Dolichyl-Phosphate Beta-D-Mannosyltransferase Subunit 1 3 4
- Dolichol-Phosphate Mannosyltransferase Subunit 1 3 4
- Dolichol-Phosphate Mannose Synthase Subunit 1 3 4
- DPM Synthase Complex, Catalytic Subunit 2 3
- Mannose-P-Dolichol Synthase Subunit 1 3 4
- DPM Synthase Subunit 1 3 4
External Ids for DPM1 Gene
Previous GeneCards Identifiers for DPM1 Gene
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. Mutations in this gene are associated with congenital disorder of glycosylation type Ie. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2015]
GeneCards Summary for DPM1 Gene
DPM1 (Dolichyl-Phosphate Mannosyltransferase Subunit 1, Catalytic) is a Protein Coding gene. Diseases associated with DPM1 include Congenital Disorder Of Glycosylation, Type Ie and Acquired Polycythemia. Among its related pathways are Transport to the Golgi and subsequent modification and Metabolism of proteins. Gene Ontology (GO) annotations related to this gene include transferase activity, transferring glycosyl groups and dolichyl-phosphate-mannose-protein mannosyltransferase activity. An important paralog of this gene is ALG5.
UniProtKB/Swiss-Prot Summary for DPM1 Gene
Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins; catalytic subunit of the dolichol-phosphate mannose (DPM) synthase complex.