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GCR1 protein (Saccharomyces cerevisiae) - STRING interaction network
"GCR1" - Transcriptional activator of genes involved in glycolysis in Saccharomyces cerevisiae
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Known Interactions
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experimentally determined
Predicted Interactions
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textmining
co-expression
protein homology
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GCR1Transcriptional activator of genes involved in glycolysis; DNA-binding protein that interacts and functions with the transcriptional activator Gcr2p; Transcriptional activator required for the expression of glycolytic and ribosomal genes. Forms a transcriptional activation complex with RAP1, RAP1 providing the specific DNA-binding function and GCR1 providing the activation function. Can also bind itself to DNA to a core 5’-CTTCC-3’ sequence (CT box). CT box- binding is not essential, but enhances the activation function of the RAP1-GCR1 complex in promoters that contain both DNA signal [...] (785 aa)    
Predicted Functional Partners:
GCR2
Transcriptional activator of genes involved in glycolysis; interacts and functions with the DNA-binding protein Gcr1p; Transcriptional activator required for the expression of glycolytic genes. Enhances the CT box-dependent transcriptional activation of a RAP1-GCR1 complex. Required for GCR1 phosphorylation (534 aa)
       
 
  0.976
RAP1
DNA-binding protein involved in either activation or repression of transcription, depending on binding site context; also binds telomere sequences and plays a role in telomeric position effect (silencing) and telomere structure; Essential regulatory protein in yeast whose DNA-binding sites are found at three types of chromosomal elements- promoters, silencers, and telomeres. RAP1 is also involved in the regulation of telomere structure, where its binding sites are found within the terminal poly[C(1-3)A] sequences. The opposite regulatory functions of RAP1 are not intrinsic to its bindi [...] (827 aa)
       
 
  0.919
NUP84
Subunit of the nuclear pore complex (NPC); forms a subcomplex with Nup85p, Nup120p, Nup145p-C, Sec13p, and Seh1p that plays a role in nuclear mRNA export, and NPC biogenesis; required also for transcription elongation as demonstrated by the G-less-b /.../un-on (GLRO) assay; Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP84 is involved in nuclear poly(A)+ RNA expor [...] (726 aa)
       
 
  0.764
NUP53
Subunit of the nuclear pore complex (NPC), interacts with karyopherin Kap121p or with Nup170p via overlapping regions of Nup53p, involved in activation of the spindle checkpoint mediated by the Mad1p-Mad2p complex; Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transpor [...] (475 aa)
       
 
  0.746
PHO85
Cyclin-dependent kinase, with ten cyclin partners; involved in regulating the cellular response to nutrient levels and environmental conditions and progression through the cell cycle; Cyclin-dependent protein kinase (CDK) catalytic subunit that regulates multiple cell cycle and metabolic processes in response to nutrient availability. Associates with different cyclins, that control kinase activity, substrate specificity and subcellular location of the kinase. Favorable growth conditions always result in activated cyclin-CDK complexes. Regulates metabolic processes when associated with [...] (305 aa)
       
 
  0.740
NUP133
Subunit of the Nup84p subcomplex of the nuclear pore complex (NPC); localizes to both sides of the NPC, required to establish a normal nucleocytoplasmic concentration gradient of the GTPase Gsp1p; required also for transcription elongation as demons /.../ by the G-less-based run-on (GLRO) assay; Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP133 is involved in nuc [...] (1157 aa)
       
 
  0.727
NUP120
Subunit of the Nup84p subcomplex of the nuclear pore complex (NPC); required for even distribution of NPCs around the nuclear envelope, involved in establishment of a normal nucleocytoplasmic concentration gradient of the GTPase Gsp1p; the Nup84 sub /.../x has a role in transcription elongation; Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP120 is involved in nuc [...] (1037 aa)
       
 
  0.719
NUP42
Subunit of the nuclear pore complex (NPC) that localizes exclusively to the cytoplasmic side; involved in RNA export, most likely at a terminal step; interacts with Gle1p; Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport co [...] (430 aa)
       
 
  0.693
SUC2
Invertase, sucrose hydrolyzing enzyme; a secreted, glycosylated form is regulated by glucose repression, and an intracellular, nonglycosylated enzyme is produced constitutively (532 aa)
           
  0.655
TPI1
Triose phosphate isomerase, abundant glycolytic enzyme; mRNA half-life is regulated by iron availability; transcription is controlled by activators Reb1p, Gcr1p, and Rap1p through binding sites in the 5’ non-coding region; inhibition of Tpi1p activi /.../PEP (phosphoenolpyruvate) stimulates redox metabolism in respiring cells; E104D mutation in human TPI causes a rare autosomal disease (248 aa)
           
  0.653
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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