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TAN1 protein (Saccharomyces cerevisiae) - STRING interaction network
"TAN1" - Putative tRNA acetyltransferase, RNA-binding protein required for the formation of the modified nucleoside N(4)-acetylcytidine in serine and leucine tRNAs but not required for the same modification in 18S rRNA in Saccharomyces cerevisiae
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Known Interactions
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
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protein homology
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TAN1Putative tRNA acetyltransferase, RNA-binding protein required for the formation of the modified nucleoside N(4)-acetylcytidine in serine and leucine tRNAs but not required for the same modification in 18S rRNA; Probable tRNA acetyltransferase required for the formation of the modified nucleoside N(4)-acetylcytidine in serine and leucine tRNAs. Binds RNA (289 aa)    
Predicted Functional Partners:
SSN3
Cyclin-dependent protein kinase, component of RNA polymerase II holoenzyme; involved in phosphorylation of the RNA polymerase II C-terminal domain; involved in glucose repression; Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II- dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the h [...] (555 aa)
       
      0.921
PRE10
Alpha 7 subunit of the 20S proteasome; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity (288 aa)
       
      0.921
PRE6
Alpha 4 subunit of the 20S proteasome; may replace alpha 3 subunit (Pre9p) under stress conditions to create a more active proteasomal isoform; GFP-fusion protein relocates from cytosol to the mitochondrial surface upon oxidative stress; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving [...] (254 aa)
       
      0.921
PRE5
Alpha 6 subunit of the 20S proteasome; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity (234 aa)
       
      0.921
PRE8
Alpha 2 subunit of the 20S proteasome; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity (250 aa)
       
      0.921
MAD2
Component of the spindle-assembly checkpoint complex; delays the onset of anaphase in cells with defects in mitotic spindle assembly; forms a complex with Mad1p; regulates APC/C activity during prometaphase and metaphase of meiosis I; Central component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Thought to be recruited to unattached kinetochores by MAD1. During checkpoint activity, MAD2 is relayed from the MAD1-MAD2 complex to the mitotic checkpoint complex (MCC). MCC and presumably the MA [...] (196 aa)
       
      0.921
PUP2
Alpha 5 subunit of the 20S proteasome involved in ubiquitin-dependent catabolism; human homolog is subunit zeta; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity (260 aa)
       
      0.921
SCL1
Alpha 1 subunit of the 20S proteasome involved in the degradation of ubiquitinated substrates; 20S proteasome is the core complex of the 26S proteasome; essential for growth; detected in the mitochondria; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basi [...] (252 aa)
       
      0.921
TRM1
tRNA methyltransferase; two forms of the protein are made by alternative translation starts; localizes to both the nucleus and mitochondrion to produce the modified base N2,N2-dimethylguanosine in tRNAs in both compartments; Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. Required for the modification of both mitochondrial and cytoplasmic tRNAs (570 aa)
     
 
  0.905
PUS4
Pseudouridine synthase, catalyzes only the formation of pseudouridine-55 (Psi55), a highly conserved tRNA modification, in mitochondrial and cytoplasmic tRNAs; PUS4 overexpression leads to translational derepression of GCN4 (Gcd- phenotype); Responsible for synthesis of pseudouridine from uracil- 55 in the psi GC loop of transfer RNAs (403 aa)
     
 
  0.884
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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