RIF1 protein (Saccharomyces cerevisiae) - STRING interaction network
"RIF1" - Protein that binds to the Rap1p C-terminus and acts synergistically with Rif2p to help control telomere length and establish telomeric silencing in Saccharomyces cerevisiae
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Known Interactions
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Predicted Interactions
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Gene Fusion
RIF1Protein 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)    
Predicted Functional Partners:
Protein 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)
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)
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)
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)
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)
DNA damage-dependent checkpoint protein, required for cell-cycle arrest in G1/S, intra-S, and G2/M; transmits checkpoint signal by activating Rad53p and Chk1p; hyperphosphorylated by Mec1p and Tel1p; potential Cdc28p substrate; Essential for cell cycle arrest at the G2 stage following DNA damage by X-irradiation or inactivation of DNA ligase (1309 aa)
Type 1 serine/threonine protein phosphatase catalytic subunit, involved in many processes (eg- glycogen metabolism, sporulation, mitosis); accumulates at mating projections by interaction with Afr1p; interacts with many regulatory subunits; Involved in control of glycogen metabolism, meiosis, translation, chromosome segregation, cell polarity and G2/M cell cycle progression. PP1 may act in opposition to the IPL1 protein kinase in regulating chromosome segregation by dephosphorylating H3S10ph. The BUD14-GLC7 complex is necessary to regulate microtubule dynamics at the cortex and may fun [...] (312 aa)
5’-3’ exonuclease and flap-endonuclease involved in recombination, double-strand break repair and DNA mismatch repair; member of the Rad2p nuclease family, with conserved N and I nuclease domains; 5’->3’ double-stranded DNA exonuclease involved in mismatch repair and eventually also in mitotic recombination between direct repeats. Also has a minor role in the correction of large DNA mismatches that occur in the heteroduplex DNA during meiotic recombination at the HIS4 locus (702 aa)
Telomere end-binding and capping protein, plays a key role with Pol12p in linking telomerase action with completion of lagging strand synthesis, and in a regulatory step required for telomere capping; Has a role in telomere length regulation and telomere end protection. Acts as an inhibitor of telomerase loading through its interaction with CDC13 (494 aa)
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)
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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