Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Combined Automated Annotation using Multiple IEA Methods
YeastPathways to GO-CAM conversion
Global analysis of protein localization in budding yeast.
The yeast lipin Smp2 couples phospholipid biosynthesis to nuclear membrane growth.
The Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme.
Colorimetric determination of pure Mg(2+)-dependent phosphatidate phosphatase activity.
The cellular functions of the yeast lipin homolog PAH1p are dependent on its phosphatidate phosphatase activity.
A phosphorylation-regulated amphipathic helix controls the membrane translocation and function of the yeast phosphatidate phosphatase.
The yeast lipin orthologue Pah1p is important for biogenesis of lipid droplets.
A role for phosphatidic acid in the formation of "supersized" lipid droplets.
Yeast lipin 1 orthologue pah1p regulates vacuole homeostasis and membrane fusion.
PAH1-encoded phosphatidate phosphatase plays a role in the growth phase- and inositol-mediated regulation of lipid synthesis in Saccharomyces cerevisiae.
Seipin is involved in the regulation of phosphatidic acid metabolism at a subdomain of the nuclear envelope in yeast.
One library to make them all: streamlining the creation of yeast libraries via a SWAp-Tag strategy.
Tip60-mediated lipin 1 acetylation and ER translocation determine triacylglycerol synthesis rate.
Mutant phosphatidate phosphatase Pah1-W637A exhibits altered phosphorylation, membrane association, and enzyme function in yeast.
Protein kinase Hsl1 phosphorylates Pah1 to inhibit phosphatidate phosphatase activity and regulate lipid synthesis in Saccharomyces cerevisiae.
The antidepressant drug sertraline is a novel inhibitor of yeast Pah1 and human lipin 1 phosphatidic acid phosphatases.
A gene, SMP2, involved in plasmid maintenance and respiration in Saccharomyces cerevisiae encodes a highly charged protein.