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SGT1 SGT1 HSC82 HSC82 HSP82 HSP82 SKP1 SKP1 CYR1 CYR1 CTF13 CTF13 CDC37 CDC37 AHA1 AHA1 STI1 STI1 CEP3 CEP3 ERG12 ERG12
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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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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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SGT1Cochaperone protein; regulates activity of adenylyl cyclase Cyr1p; involved in kinetochore complex assembly; associates with the SCF (Skp1p/Cdc53p/F box protein) ubiquitin ligase complex; acts as a linker between Skp1p and HSP90 complexes; protein abundance increases in response to DNA replication stress; Belongs to the SGT1 family. (395 aa)    
Predicted Functional Partners:
HSC82
ATP-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.
   
 
 0.999
HSP82
ATP-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.
   
 0.999
SKP1
Evolutionarily conserved kinetochore protein; part of multiple protein complexes, including the SCF ubiquitin ligase complex, the CBF3 complex that binds centromeric DNA, and the RAVE complex that regulates assembly of the V-ATPase; protein abundance increases in response to DNA replication stress.
   
 
 0.997
CYR1
Adenylate 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.
    
 
 0.983
CTF13
Subunit of the CBF3 complex; CBF3 binds to the CDE III element of centromeres, bending the DNA upon binding, and may be involved in sister chromatid cohesion during mitosis.
    
 
 0.881
CDC37
Essential Hsp90p co-chaperone; necessary for passage through the START phase of the cell cycle; stabilizes protein kinase nascent chains and participates along with Hsp90p in their folding; Belongs to the CDC37 family.
   
 
 0.866
AHA1
Hsp90 co-chaperone AHA1; Co-chaperone that binds Hsp82p and activates its ATPase activity; plays a role in determining prion variants; similar to Hch1p; expression is regulated by stresses such as heat shock; protein abundance increases in response to DNA replication stress; Belongs to the AHA1 family.
   
 
 0.859
STI1
Heat shock protein STI1; Hsp90 cochaperone; regulates spatial organization of amyloid-like proteins in the cytosol, thereby buffering the proteotoxicity caused by amyloid-like proteins; interacts with the Ssa group of the cytosolic Hsp70 chaperones and activates Ssa1p ATPase activity; interacts with Hsp90 chaperones and inhibits their ATPase activity; homolog of mammalian Hop.
   
 
 0.824
CEP3
Essential kinetochore protein; component of the CBF3 complex that binds the CDEIII region of the centromere; contains an N-terminal Zn2Cys6 type zinc finger domain, a C-terminal acidic domain, and a putative coiled coil dimerization domain.
    
 
 0.812
ERG12
Mevalonate kinase; acts in the biosynthesis of isoprenoids and sterols, including ergosterol, from mevalonate; human MVK functionally complements the lethality of the erg12 null mutation.
   
 
 0.790
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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