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RIF2 protein (Saccharomyces cerevisiae) - STRING interaction network
"RIF2" - Protein that binds to the Rap1p C-terminus and acts synergistically with Rif1p to help control telomere length and establish telomeric silencing in Saccharomyces cerevisiae
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Predicted Interactions
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protein homology
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RIF2Protein that binds to the Rap1p C-terminus and acts synergistically with Rif1p to help control telomere length and establish telomeric silencing; deletion results in telomere elongation; Involved in transcriptional silencing and telomere length regulation. Its role in telomere length regulation results from either a block in elongation or promoting degradation of the telomere ends. Loss of RIF1 function results in derepression of an HMR silencer, whose ARS consensus element has been deleted, and in the elongation of telomeres. RAP1 may target the binding of RIF1 to silencers and telomeres (395 aa)    
Predicted Functional Partners:
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)
       
 
  0.972
RIF1
Protein that binds to the Rap1p C-terminus and acts synergistically with Rif2p to help control telomere length and establish telomeric silencing; deletion results in telomere elongation; Negatively regulates telomere length by preventing telomere elongation or promoting degradation of the telomere ends. Recruited to telomeres by interaction with the C-terminus of RAP1, which binds directly to telomeric repeat DNA. This may create a negative feedback loop in which the addition of new telomere repeats creates binding sites for inhibitors of telomere length extension. May also influence t [...] (1916 aa)
       
 
  0.961
CDC13
Single stranded DNA-binding protein found at TG1-3 telomere G-tails; regulates telomere replication through recruitment of specific sub-complexes, but the essential function is telomere capping; Single-stranded telomeric DNA-binding protein that regulates telomere replication. Has a role in both positive and negative regulation. Promotes [TG(1-3)] strand lengthening via interaction with EST1. Promotes [C(1-3)A] strand re-synthesis by DNA polymerase alpha via interaction with POL1. Negatively regulates telomere elongation of the G strand via binding with STN1 thereby inhibiting telomera [...] (924 aa)
       
 
  0.961
YKU70
Subunit of the telomeric Ku complex (Yku70p-Yku80p), involved in telomere length maintenance, structure and telomere position effect; relocates to sites of double-strand cleavage to promote nonhomologous end joining during DSB repair; Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appe [...] (602 aa)
       
 
  0.925
RAD50
Subunit of MRX complex, with Mre11p and Xrs2p, involved in processing double-strand DNA breaks in vegetative cells, initiation of meiotic DSBs, telomere maintenance, and nonhomologous end joining; Involved in DNA double-strand break repair (DSBR). The rad50/mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific exonuclease activity. Rad50 provides ATP-dependent control of mre11 by unwinding and/or repositioning DNA ends into the mre11 active site (1312 aa)
       
 
  0.890
MRE11
Subunit of a complex with Rad50p and Xrs2p (MRX complex) that functions in repair of DNA double-strand breaks and in telomere stability, exhibits nuclease activity that appears to be required for MRX function; widely conserved; Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand- specific 3’-5’ exonuclease activity. Also involved in meiotic DSB processing (692 aa)
       
 
  0.890
TEL1
Protein kinase primarily involved in telomere length regulation; contributes to cell cycle checkpoint control in response to DNA damage; functionally redundant with Mec1p; homolog of human ataxia telangiectasia (ATM) gene; Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Recruited by the MRX-complex to sites of DNA lesions immediately after damage to initiate non- homo [...] (2787 aa)
       
 
  0.862
SIR4
Silent information regulator that, together with SIR2 and SIR3, is involved in assembly of silent chromatin domains at telomeres and the silent mating-type loci; potentially phosphorylated by Cdc28p; some alleles of SIR4 prolong lifespan; The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form (1358 aa)
       
 
  0.842
YKU80
Subunit of the telomeric Ku complex (Yku70p-Yku80p), involved in telomere length maintenance, structure and telomere position effect; relocates to sites of double-strand cleavage to promote nonhomologous end joining during DSB repair; Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appe [...] (629 aa)
           
  0.795
HPR1
Subunit of THO/TREX complexes that couple transcription elongation with mitotic recombination and with mRNA metabolism and export, subunit of an RNA Pol II complex; regulates lifespan; involved in telomere maintenance; similar to Top1p; Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing format [...] (752 aa)
       
 
  0.789
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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