STRING protein interaction network
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
TGL2Lipase 2; Triacylglycerol lipase that is localized to the mitochondria; has lipolytic activity towards triacylglycerols and diacylglycerols when expressed in E. coli. (326 aa)    
Predicted Functional Partners:
Lipase 4; Multifunctional lipase/hydrolase/phospholipase; triacylglycerol lipase, steryl ester hydrolase, and Ca2+-independent phospholipase A2; catalyzes acyl-CoA dependent acylation of LPA to PA; required with Tgl3p for timely bud formation; phosphorylated and activated by Cdc28p; TGL4 has a paralog, TGL5, that arose from the whole genome duplication.
Lipase 3; Bifunctional triacylglycerol lipase and LPE acyltransferase; major lipid particle-localized triacylglycerol (TAG) lipase; catalyzes acylation of lysophosphatidylethanolamine (LPE), a function which is essential for sporulation; protein level and stability of Tgl3p are markedly reduced in the absence of lipid droplets; required with Tgl4p for timely bud formation.
Lipase 5; Bifunctional triacylglycerol lipase and LPA acyltransferase; lipid particle-localized triacylglycerol (TAG) lipase involved in triacylglycerol mobilization; catalyzes acylation of lysophosphatidic acid (LPA); potential Cdc28p substrate; TGL5 has a paralog, TGL4, that arose from the whole genome duplication.
Monoglyceride lipase (MGL); functional ortholog of mammalian MGL, localizes to lipid particles and membranes, also member of the eukaryotic serine hydrolase family; Belongs to the AB hydrolase superfamily. Monoacylglycerol lipase family.
Diacylglycerol O-acyltransferase 1; Diacylglycerol acyltransferase; catalyzes the terminal step of triacylglycerol (TAG) formation, acylates diacylglycerol using acyl-CoA as an acyl donor; Lro1p and Dga1p can O-acylate ceramides; localized to lipid particles.
Acyltransferase that catalyzes diacylglycerol esterification; one of several acyltransferases that contribute to triglyceride synthesis; Lro1p and Dga1p can O-acylate ceramides; putative homolog of human lecithin cholesterol acyltransferase.
Lipid phosphate phosphatase; catalyzes Mg(2+)-independent dephosphorylation of phosphatidic acid (PA), lysophosphatidic acid, and diacylglycerol pyrophosphate; involved in control of the cellular levels of phosphatidylinositol and PA.
Diacylglycerol pyrophosphate (DGPP) phosphatase; zinc-regulated vacuolar membrane-associated lipid phosphatase, dephosphorylates DGPP to phosphatidate (PA) and Pi, then PA to diacylglycerol; involved in lipid signaling and cell metabolism; Belongs to the PA-phosphatase related phosphoesterase family.
Phosphatidic acid phosphohydrolase 1; Mg2+-dependent phosphatidate (PA) phosphatase; dephosphorylates PA to yield diacylglycerol; regulates phospholipid synthesis, nuclear/ER membrane growth, lipid droplet formation, triacylglycerol synthesis, vacuolar homeostasis and cell wall integrity; phosphorylated by Pho85p/Pho80p, Cdc28p/Cyclin B, PKA, PKC, and CKII, regulating activity, localization, and proteosomal degradation; homolog of mammalian lipins 1 and 2; human homologs LPIN1, LPIN2, LPIN3 complement the null.
Phosphate metabolism protein 8; Lysophosphatidic acid (LPA) phosphatase, nucleotidase; principle and physiological nucleotidase working on GMP, UMP and CMP; involved in LPA hydrolysis in response to phosphate starvation and ribose salvage pathway; phosphatase activity is soluble and Mg2+ dependent; expression is induced by low phosphate levels and by inactivation of Pho85p; repressed by Gcn4p under normal conditions; PHM8 has a paralog, SDT1, that arose from the whole genome duplication.
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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