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TPK2 TPK2 HSC82 HSC82 SOK2 SOK2 ERG6 ERG6 FKS1 FKS1 TPK3 TPK3 TPK1 TPK1 CYR1 CYR1 ERG9 ERG9 ERG7 ERG7 ERG11 ERG11 ERG25 ERG25 GSC2 GSC2 CMD1 CMD1 HSP82 HSP82
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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TPK2cAMP-dependent protein kinase catalytic subunit; promotes vegetative growth in response to nutrients via the Ras-cAMP signaling pathway; partially redundant with Tpk1p and Tpk3p; localizes to P-bodies during stationary phase; relocalizes to the cytosol in response to hypoxia. (380 aa)
HSC82ATP-dependent molecular chaperone HSC82; Cytoplasmic chaperone of the Hsp90 family; plays a role in determining prion variants; redundant in function and nearly identical with Hsp82p, and together they are essential; expressed constitutively at 10-fold higher basal levels than HSP82 and induced 2-3 fold by heat shock; contains two acid-rich unstructured regions that promote the solubility of chaperone-substrate complexes; HSC82 has a paralog, HSP82, that arose from the whole genome duplication. (705 aa)
SOK2Nuclear protein that negatively regulates pseudohyphal differentiation; plays a regulatory role in the cyclic AMP (cAMP)-dependent protein kinase (PKA) signal transduction pathway; relocalizes to the cytosol in response to hypoxia; SOK2 has a paralog, PHD1, that arose from the whole genome duplication. (785 aa)
ERG6Delta(24)-sterol C-methyltransferase; converts zymosterol to fecosterol in the ergosterol biosynthetic pathway by methylating position C-24; localized to lipid particles, the plasma membrane-associated endoplasmic reticulum, and the mitochondrial outer membrane; Belongs to the class I-like SAM-binding methyltransferase superfamily. Erg6/SMT family. (383 aa)
FKS11,3-beta-glucan synthase component FKS1; Catalytic subunit of 1,3-beta-D-glucan synthase; functionally redundant with alternate catalytic subunit Gsc2p; binds to regulatory subunit Rho1p; involved in cell wall synthesis and maintenance; localizes to sites of cell wall remodeling; FKS1 has a paralog, GSC2, that arose from the whole genome duplication. (1876 aa)
TPK3cAMP-dependent protein kinase catalytic subunit; promotes vegetative growth in response to nutrients via the Ras-cAMP signaling pathway; partially redundant with Tpk1p and Tpk2p; localizes to P-bodies during stationary phase; TPK3 has a paralog, TPK1, that arose from the whole genome duplication. (398 aa)
TPK1cAMP-dependent protein kinase catalytic subunit; promotes vegetative growth in response to nutrients via the Ras-cAMP signaling pathway; inhibited by regulatory subunit Bcy1p in the absence of cAMP; phosphorylates and inhibits Whi3p to promote G1/S phase passage; partially redundant with Tpk2p and Tpk3p; phosphorylates pre-Tom40p, which impairs its import into mitochondria under non-respiratory conditions; TPK1 has a paralog, TPK3, that arose from the whole genome duplication. (397 aa)
CYR1Adenylate cyclase; required for cAMP production and cAMP-dependent protein kinase signaling; the cAMP pathway controls a variety of cellular processes, including metabolism, cell cycle, stress response, stationary phase, and sporulation. (2026 aa)
ERG9Squalene synthase; Farnesyl-diphosphate farnesyl transferase (squalene synthase); joins two farnesyl pyrophosphate moieties to form squalene in the sterol biosynthesis pathway. (444 aa)
ERG7Lanosterol synthase; an essential enzyme that catalyzes the cyclization of squalene 2,3-epoxide, a step in ergosterol biosynthesis; human LSS functionally complements the lethality of the erg7 null mutation; Belongs to the terpene cyclase/mutase family. (731 aa)
ERG11Lanosterol 14-alpha-demethylase; catalyzes C-14 demethylation of lanosterol to form 4,4''-dimethyl cholesta-8,14,24-triene-3-beta-ol in ergosterol biosynthesis pathway; transcriptionally down-regulated when ergosterol is in excess; member of cytochrome P450 family; associated and coordinately regulated with the P450 reductase Ncp1p; human CYP51A1 functionally complements the lethality of the erg11 null mutation. (530 aa)
ERG25Methylsterol monooxygenase; C-4 methyl sterol oxidase; catalyzes the first of three steps required to remove two C-4 methyl groups from an intermediate in ergosterol biosynthesis; mutants accumulate the sterol intermediate 4,4-dimethylzymosterol; human MSMO1 functionally complements the growth defect caused by repression of ERG25 expression. (309 aa)
GSC2Catalytic subunit of 1,3-beta-glucan synthase; involved in formation of the inner layer of the spore wall; activity positively regulated by Rho1p and negatively by Smk1p; GSC2 has a paralog, FKS1, that arose from the whole genome duplication; Belongs to the glycosyltransferase 48 family. (1895 aa)
CMD1Calmodulin; Ca2+ binding protein that regulates Ca2+ independent processes (mitosis, bud growth, actin organization, endocytosis, etc.) and Ca2+ dependent processes (stress-activated pathways), targets include Nuf1p, Myo2p and calcineurin; binds to the Hog1p MAPK in response to hyperosmotic stress; potentiates membrane tubulation and constriction mediated by the Rvs161p-Rvs167p complex; human CALM1 or CALM2 functionally complement repression induced inviability. (147 aa)
HSP82ATP-dependent molecular chaperone HSP82; Hsp90 chaperone; redundant in function with Hsc82p; required for pheromone signaling, negative regulation of Hsf1p; docks with Tom70p for mitochondrial preprotein delivery; promotes telomerase DNA binding, nucleotide addition; protein abundance increases in response to DNA replication stress; contains two acid-rich unstructured regions that promote solubility of chaperone-substrate complexes; HSP82 has a paralog, HSC82, that arose from the whole genome duplication. (709 aa)
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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