BAIT
PMT4
L000002623, YJR143C
Protein O-mannosyltransferase; transfers mannose residues from dolichyl phosphate-D-mannose to protein serine/threonine residues; appears to form homodimers in vivo and does not complex with other Pmt proteins; target for new antifungals
GO Process (3)
GO Function (1)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
PMT3
dolichyl-phosphate-mannose-protein mannosyltransferase PMT3, L000002622, YOR321W
Protein O-mannosyltransferase; transfers mannose residues from dolichyl phosphate-D-mannose to protein serine/threonine residues; acts in a complex with Pmt5p, can instead interact with Pmt1p in some conditions; antifungal drug target; PMT3 has a paralog, PMT2, that arose from the whole genome duplication
GO Process (2)
GO Function (1)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
Synthetic Lethality
A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.
Publication
The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital.
The transfer of mannose to seryl and threonyl residues of secretory proteins is catalyzed by a family of protein mannosyltransferases coded for by seven genes (PMT1-7). Mannose dolichylphosphate is the sugar donor of the reaction, which is localized at the endoplasmic reticulum. By gene disruption and crosses all single, double and triple mutants of genes PMT1-4 were constructed. Two of ... [more]
EMBO J. Nov. 01, 1996; 15(21);5752-9 [Pubmed: 8918452]
Throughput
- Low Throughput
Ontology Terms
- phenotype: inviable (APO:0000112)
Additional Notes
- pmtlpmt2pmt4 and pmt2pmt3pmt4 triple mutants are lethal
Curated By
- BioGRID