Dolichol-phosphate mannosyltransferase is an enzyme that in humans is encoded by the DPM1gene.
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.
^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 Chem273 (15): 9249–54. doi:10.1074/jbc.273.15.9249. PMID9535917.
^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". Cell154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMID23870131.
Ashida H, Maeda Y, Kinoshita T (2006). "DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered to and stabilized on the endoplasmic reticulum membrane by DPM3". J. Biol. Chem.281 (2): 896–904. doi:10.1074/jbc.M511311200. PMID16280320.