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TY3A-I protein (Saccharomyces cerevisiae) - STRING interaction network
"TY3A-I" - Retrotransposon TYA Gag gene co-transcribed with TYB Pol in Saccharomyces cerevisiae
Nodes:
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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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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
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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 each other.
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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Cooccurence
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[Homology]
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TY3A-IRetrotransposon TYA Gag gene co-transcribed with TYB Pol; translated as TYA or TYA-TYB polyprotein; Gag is a nucleocapsid protein that is the structural constituent of virus-like particles (VLPs); similar to retroviral Gag; Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome (290 aa)    
Predicted Functional Partners:
YIL060W
Putative protein of unknown function; mutant accumulates less glycogen than does wild type; null mutation results in a decrease in plasma membrane electron transport; YIL060W is not an essential gene (144 aa)
           
  0.519
YDR537C
Dubious open reading frame unlikely to encode a protein, almost completely overlaps verified ORF PAD1/YDR538W (201 aa)
           
  0.519
YDR124W
Putative protein of unknown function; non-essential gene; expression is strongly induced by alpha factor (324 aa)
           
  0.487
YLR334C
Dubious open reading frame unlikely to encode a protein, based on available experimental and comparative sequence data; overlaps a stand-alone long terminal repeat sequence whose presence indicates a retrotransposition event occurred here (126 aa)
           
  0.485
YER084W
Protein of unknown function; expressed at both mRNA and protein levels (128 aa)
           
  0.443
HSP60
Tetradecameric mitochondrial chaperonin required for ATP-dependent folding of precursor polypeptides and complex assembly; prevents aggregation and mediates protein refolding after heat shock; role in mtDNA transmission; phosphorylated; May participate in assembly and/or disassembly of proteins imported into the mitochondrion. HSP60 are ATPases and have affinity for unfolded proteins (572 aa)
     
 
  0.420
CCT5
Subunit of the cytosolic chaperonin Cct ring complex, related to Tcp1p, required for the assembly of actin and tubulins in vivo; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (562 aa)
     
 
  0.420
CCT7
Subunit of the cytosolic chaperonin Cct ring complex, related to Tcp1p, required for the assembly of actin and tubulins in vivo; mutant has increased aneuploidy tolerance; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (By similarity) (550 aa)
     
 
  0.420
CCT3
Subunit of the cytosolic chaperonin Cct ring complex, related to Tcp1p, required for the assembly of actin and tubulins in vivo; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (534 aa)
     
 
  0.420
CCT2
Subunit beta of the cytosolic chaperonin Cct ring complex, related to Tcp1p, required for the assembly of actin and tubulins in vivo; Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation (527 aa)
     
 
  0.420
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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