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:
some 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
VID24Vacuolar import and degradation protein 24; GID Complex regulatory subunit; binds GID Complex in response to glucose through interactions with complex member Vid28p; regulates fructose-1,6-bisphosphatase (FBPase) targeting to the vacuole; promotes proteasome-dependent catabolite degradation of FBPase; peripheral membrane protein located at Vid (vacuole import and degradation) vesicles; To yeast YGR066c and S.pombe SpAC3H1.14 (362 aa)    
Predicted Functional Partners:
Vacuolar import and degradation protein 30; Central component of GID Complex, involved in FBPase degradation; interacts strongly with Gid8p to serve as a scaffold for other GID Complex subunits; contains SPRY domain and 3 domains that are also found in Gid8p - LisH, CTLH, and CRA; required for association of Vid vesicles and actin patches in vacuole import and degradation pathway; shifts the balance of nitrogen metabolism toward glutamate production; localizes to the nucleus and the cytoplasm
Vacuolar import and degradation protein 28; GID Complex subunit, serves as adaptor for regulatory subunit Vid24p; protein involved in proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBPase); localized to the nucleus and the cytoplasm
Protein FYV10; Subunit of GID complex; involved in proteasome-dependent catabolite inactivation of gluconeogenic enzymes FBPase, PEPCK, and c-MDH; forms dimer with Rmd5p that is then recruited to GID Complex by Gid8p; contains a degenerate RING finger motif needed for GID complex ubiquitin ligase activity in vivo, as well as CTLH and CRA domains; plays role in anti-apoptosis; required for survival upon exposure to K1 killer toxin
Glucose-induced degradation protein 8; Subunit of GID Complex, binds strongly to central component Vid30p; GID Complex is involved in proteasome-dependent catabolite inactivation of fructose-1,6-bisphosphatase; recruits Rmd5p, Fyv10 and Vid28p to GID Complex; contains LisH, CTLH, and CRA domains that mediate binding to Vid30p (LisH) and Rmd5p and Vid28p (CTLH and CRA); dosage-dependent regulator of START; Belongs to the GID8 family
Glucose-induced degradation protein 7; Subunit of GID Complex that binds directly to central component Vid30p; GID complex is involved in proteasome-dependent catabolite inactivation of fructose-1,6-bisphosphatase; Gid7p contains six WD40 repeats; computational analysis suggests that Gid7p and Moh1p have similar functions
E3 ubiquitin-protein transferase RMND5; Sporulation protein RMD5; Component of GID Complex that confers ubiquitin ligase (U3) activity; necessary for polyubiquitination and degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase; forms dimer with Fyv10p that is then recruited to GID Complex by Gid8p; also required for sporulation; conserved protein that has a degenerate RING finger domain
Isocitrate lyase; catalyzes the formation of succinate and glyoxylate from isocitrate, a key reaction of the glyoxylate cycle; expression of ICL1 is induced by growth on ethanol and repressed by growth on glucose
Epsilon-COP subunit of the coatomer; regulates retrograde Golgi-to-ER protein traffic; stabilizes Cop1p, the alpha-COP and the coatomer complex; non-essential for cell growth; protein abundance increases in response to DNA replication stress
Fructose-1,6-bisphosphatase; key regulatory enzyme in the gluconeogenesis pathway, required for glucose metabolism; undergoes either proteasome-mediated or autophagy-mediated degradation depending on growth conditions; glucose starvation results in redistribution to the periplasm; interacts with Vid30p; Belongs to the FBPase class 1 family
Cytoplasmic malate dehydrogenase; one of three isozymes that catalyze interconversion of malate and oxaloacetate; involved in the glyoxylate cycle and gluconeogenesis during growth on two-carbon compounds; interacts with Pck1p and Fbp1
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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