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
NEM1Nuclear envelope morphology protein 1; Probable catalytic subunit of Nem1p-Spo7p phosphatase holoenzyme; regulates nuclear growth by controlling phospholipid biosynthesis, required for normal nuclear envelope morphology and sporulation; homolog of the human protein Dullard; Belongs to the Dullard family. (446 aa)    
Predicted Functional Partners:
Sporulation-specific protein SPO7; Putative regulatory subunit of Nem1p-Spo7p phosphatase holoenzyme; regulates nuclear growth by controlling phospholipid biosynthesis, required for normal nuclear envelope morphology, premeiotic replication, and sporulation.
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.
Protein of unknown function; expressed during sporulation; not required for sporulation, but gene exhibits genetic interactions with other genes required for sporulation.
Diacylglycerol kinase; localized to the endoplasmic reticulum (ER); overproduction induces enlargement of ER-like membrane structures and suppresses a temperature-sensitive sly1 mutation; contains a CTP transferase domain; Belongs to the DGK1 family.
TFIIF (Transcription Factor II) largest subunit; involved in both transcription initiation and elongation of RNA polymerase II; homologous to human RAP74.
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.
Nuclear mRNA export protein THP1; Nuclear pore-associated protein; component of TREX-2 complex (Sac3p-Thp1p-Sus1p-Cdc31p) involved in transcription elongation and mRNA export from the nucleus; involved in post-transcriptional tethering of active genes to the nuclear periphery and to non-nascent mRNP; contains a PAM domain implicated in protein-protein binding.
Protein ICE2; Integral ER membrane protein with type-III transmembrane domains; required for maintenance of ER zinc homeostasis; necessary for efficient targeting of Trm1p tRNA methyltransferase to inner nuclear membrane; mutations cause defects in cortical ER morphology in both the mother and daughter cells.
Phosphatidate cytidylyltransferase (CDP-diglyceride synthetase); an enzyme that catalyzes that conversion of CTP + phosphate into diphosphate + CDP-diaclglyerol, a critical step in the synthesis of all major yeast phospholipids; human homolog CDS1 can complement yeast cds1 null mutant.
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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