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P29539

- RIF1_YEAST

UniProt

P29539 - RIF1_YEAST

Protein

Telomere length regulator protein RIF1

Gene

RIF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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 the balance of transcriptional silencing at telomeres and the silent mating type locus HMR, which is mediated by SIR (Silent Information Regulator) proteins including SIR3 and SIR4. RIF1 competes with SIR proteins for binding to the C-terminus of RAP1. In the absence of RIF1, a limiting cellular pool of SIR proteins may preferentially associate with RAP1 at sub-telomeric loci, causing enhanced telomeric silencing and attenuated silencing of the HMR locus.5 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. telomeric DNA binding Source: SGD

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. chromatin silencing at silent mating-type cassette Source: SGD
    3. DNA double-strand break processing Source: SGD
    4. telomere capping Source: SGD
    5. telomere maintenance Source: SGD

    Keywords - Biological processi

    Cell cycle

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29196-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Telomere length regulator protein RIF1
    Alternative name(s):
    RAP1-interacting factor 1
    Gene namesi
    Name:RIF1
    Ordered Locus Names:YBR275C
    ORF Names:YBR1743
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR275c.
    SGDiS000000479. RIF1.

    Subcellular locationi

    Nucleus. Chromosometelomere
    Note: Localizes to telomeres. Telomere association begins in G1/S, attains a peak during late G2/S phase of the cell cycle, and is lost during telophase. Localization to telomeres may be increased by telomere uncapping caused by expression of a mutant telomerase RNA subunit (TLC1).

    GO - Cellular componenti

    1. nuclear chromosome, telomeric region Source: SGD
    2. telosome Source: SGD

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 19161916Telomere length regulator protein RIF1PRO_0000097336Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei97 – 971Phosphoserine1 Publication
    Modified residuei1637 – 16371Phosphoserine4 Publications
    Modified residuei1795 – 17951Phosphoserine1 Publication
    Modified residuei1852 – 18521Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP29539.
    PaxDbiP29539.
    PeptideAtlasiP29539.

    Expressioni

    Gene expression databases

    GenevestigatoriP29539.

    Interactioni

    Subunit structurei

    Interacts with RIF2 and RAP1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAP1P119383EBI-2083307,EBI-14821

    Protein-protein interaction databases

    BioGridi32970. 70 interactions.
    DIPiDIP-801N.
    IntActiP29539. 8 interactions.
    MINTiMINT-2780441.
    STRINGi4932.YBR275C.

    Structurei

    Secondary structure

    1
    1916
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1859 – 18613
    Helixi1866 – 187611
    Helixi1880 – 18856
    Helixi1888 – 190720

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BJSX-ray1.94A/B/C/D1857-1916[»]
    4BJTX-ray1.61D/E/F1752-1771[»]
    ProteinModelPortaliP29539.
    SMRiP29539. Positions 1857-1911.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Phylogenomic databases

    eggNOGiNOG73322.
    KOiK11118.
    OrthoDBiEOG7R838T.

    Family and domain databases

    InterProiIPR022031. Rif1_N.
    [Graphical view]
    PfamiPF12231. Rif1_N. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P29539-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKDFSDKKK HTIDRIDQHI LRRSQHDNYS NGSSPWMKTN LPPPSPQAHM     50
    HIQSDLSPTP KRRKLASSSD CENKQFDLSA INKNLYPEDT GSRLMQSLPE 100
    LSASNSDNVS PVTKSVAFSD RIESSPIYRI PGSSPKPSPS SKPGKSILRN 150
    RLPSVRTVSD LSYNKLQYTQ HKLHNGNIFT SPYKETRVNP RALEYWVSGE 200
    IHGLVDNESV SEFKEIIEGG LGILRQESED YVARRFEVYA TFNNIIPILT 250
    TKNVNEVDQK FNILIVNIES IIEICIPHLQ IAQDTLLSSS EKKNPFVIRL 300
    YVQIVRFFSA IMSNFKIVKW LTKRPDLVNK LKVIYRWTTG ALRNENSNKI 350
    IITAQVSFLR DEKFGTFFLS NEEIKPIIST FTEIMEINSH NLIYEKLLLI 400
    RGFLSKYPKL MIETVTSWLP GEVLPRIIIG DEIYSMKILI TSIVVLLELL 450
    KKCLDFVDEH ERIYQCIMLS PVCETIPEKF LSKLPLNSYD SANLDKVTIG 500
    HLLTQQIKNY IVVKNDNKIA MDLWLSMTGL LYDSGKRVYD LTSESNKVWF 550
    DLNNLCFINN HPKTRLMSIK VWRIITYCIC TKISQKNQEG NKSLLSLLRT 600
    PFQMTLPYVN DPSAREGIIY HLLGVVYTAF TSNKNLSTDM FELFWDHLIT 650
    PIYEDYVFKY DSIHLQNVLF TVLHLLIGGK NADVALERKY KKHIHPMSVI 700
    ASEGVKLKDI SSLPPQIIKR EYDKIMKVVF QAVEVAISNV NLAHDLILTS 750
    LKHLPEDRKD QTHLESFSSL ILKVTQNNKD TPIFRDFFGA VTSSFVYTFL 800
    DLFLRKNDSS LVNFNIQISK VGISQGNMTL DLLKDVIRKA RNETSEFLII 850
    EKFLELDDKK TEVYAQNWVG STLLPPNISF REFQSLANIV NKVPNENSIE 900
    NFLDLCLKLS FPVNLFTLLH VSMWSNNNFI YFIQSYVSKN ENKLNVDLIT 950
    LLKTSLPGNP ELFSGLLPFL RRNKFMDILE YCIHSNPNLL NSIPDLNSDL 1000
    LLKLLPRSRA SYFAANIKLF KCSEQLTLVR WLLKGQQLEQ LNQNFSEIEN 1050
    VLQNASDSEL EKSEIIRELL HLAMANPIEP LFSGLLNFCI KNNMADHLDE 1100
    FCGNMTSEVL FKISPELLLK LLTYKEKPNG KLLAAVIEKI ENGDDDYILE 1150
    LLEKIIIQKE IQILEKLKEP LLVFFLNPVS SNMQKHKKST NMLRELVLLY 1200
    LTKPLSRSAA KKFFSMLISI LPPNPNYQTI DMVNLLIDLI KSHNRKFKDK 1250
    RTYNATLKTI GKWIQESGVV HQGDSSKEIE AIPDTKSMYI PCEGSENKLS 1300
    NLQRKVDSQD IQVPATQGMK EPPSSIQISS QISAKDSDSI SLKNTAIMNS 1350
    SQQESHANRS RSIDDETLEE VDNESIREID QQMKSTQLDK NVANHSNICS 1400
    TKSDEVDVTE LHESIDTQSS EVNAYQPIEV LTSELKAVTN RSIKTNPDHN 1450
    VVNSDNPLKR PSKETPTSEN KRSKGHETMV DVLVSEEQAV SPSSDVICTN 1500
    IKSIANEESS LALRNSIKVE TNCNENSLNV TLDLDQQTIT KEDGKGQVEH 1550
    VQRQENQESM NKINSKSFTQ DNIAQYKSVK KARPNNEGEN NDYACNVEQA 1600
    SPVRNEVPGD GIQIPSGTIL LNSSKQTEKS KVDDLRSDED EHGTVAQEKH 1650
    QVGAINSRNK NNDRMDSTPI QGTEEESREV VMTEEGINVR LEDSGTCELN 1700
    KNLKGPLKGD KDANINDDFV PVEENVRDEG FLKSMEHAVS KETGLEEQPE 1750
    VADISVLPEI RIPIFNSLKM QGSKSQIKEK LKKRLQRNEL MPPDSPPRMT 1800
    ENTNINAQNG LDTVPKTIGG KEKHHEIQLG QAHTEADGEP LLGGDGNEDA 1850
    TSREATPSLK VHFFSKKSRR LVARLRGFTP GDLNGISVEE RRNLRIELLD 1900
    FMMRLEYYSN RDNDMN 1916
    Length:1,916
    Mass (Da):217,931
    Last modified:July 27, 2011 - v3
    Checksum:i07070AF02361D96F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti580 – 5801C → S in CAA47121. (PubMed:1577274)Curated
    Sequence conflicti732 – 7321A → T in CAA85238. (PubMed:7813418)Curated
    Sequence conflicti732 – 7321A → T in CAA53638. (PubMed:8091861)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66501 Genomic DNA. Translation: CAA47121.1.
    Z36144 Genomic DNA. Translation: CAA85238.1.
    Z36145 Genomic DNA. Translation: CAA85240.1.
    X76053 Genomic DNA. Translation: CAA53638.1.
    BK006936 Genomic DNA. Translation: DAA07391.2.
    PIRiS46157.
    RefSeqiNP_009834.4. NM_001178623.4.

    Genome annotation databases

    EnsemblFungiiYBR275C; YBR275C; YBR275C.
    GeneIDi852578.
    KEGGisce:YBR275C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66501 Genomic DNA. Translation: CAA47121.1 .
    Z36144 Genomic DNA. Translation: CAA85238.1 .
    Z36145 Genomic DNA. Translation: CAA85240.1 .
    X76053 Genomic DNA. Translation: CAA53638.1 .
    BK006936 Genomic DNA. Translation: DAA07391.2 .
    PIRi S46157.
    RefSeqi NP_009834.4. NM_001178623.4.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BJS X-ray 1.94 A/B/C/D 1857-1916 [» ]
    4BJT X-ray 1.61 D/E/F 1752-1771 [» ]
    ProteinModelPortali P29539.
    SMRi P29539. Positions 1857-1911.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32970. 70 interactions.
    DIPi DIP-801N.
    IntActi P29539. 8 interactions.
    MINTi MINT-2780441.
    STRINGi 4932.YBR275C.

    Proteomic databases

    MaxQBi P29539.
    PaxDbi P29539.
    PeptideAtlasi P29539.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR275C ; YBR275C ; YBR275C .
    GeneIDi 852578.
    KEGGi sce:YBR275C.

    Organism-specific databases

    CYGDi YBR275c.
    SGDi S000000479. RIF1.

    Phylogenomic databases

    eggNOGi NOG73322.
    KOi K11118.
    OrthoDBi EOG7R838T.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29196-MONOMER.

    Miscellaneous databases

    NextBioi 971718.

    Gene expression databases

    Genevestigatori P29539.

    Family and domain databases

    InterProi IPR022031. Rif1_N.
    [Graphical view ]
    Pfami PF12231. Rif1_N. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A RAP1-interacting protein involved in transcriptional silencing and telomere length regulation."
      Hardy C.F.J., Sussel L., Shore D.
      Genes Dev. 6:801-814(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH RAP1.
      Strain: ATCC 204510 / AB320.
    2. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 732.
      Strain: ATCC 204508 / S288c.
    4. "The sequence of a 32,420 bp segment located on the right arm of chromosome II from Saccharomyces cerevisiae."
      Holmstroem K., Brandt T., Kallesoe T.
      Yeast 10:S47-S62(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1096.
      Strain: ATCC 204508 / S288c.
    5. "Action of a RAP1 carboxy-terminal silencing domain reveals an underlying competition between HMR and telomeres in yeast."
      Buck S.W., Shore D.
      Genes Dev. 9:370-384(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "A novel Rap1p-interacting factor, Rif2p, cooperates with Rif1p to regulate telomere length in Saccharomyces cerevisiae."
      Wotton D., Shore D.
      Genes Dev. 11:748-760(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RAP1 AND RIF2.
    7. "Sir proteins, Rif proteins, and Cdc13p bind Saccharomyces telomeres in vivo."
      Bourns B.D., Alexander M.K., Smith A.M., Zakian V.A.
      Mol. Cell. Biol. 18:5600-5608(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "Yeast Ku protein plays a direct role in telomeric silencing and counteracts inhibition by rif proteins."
      Mishra K., Shore D.
      Curr. Biol. 9:1123-1126(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "Telomeric protein distributions and remodeling through the cell cycle in Saccharomyces cerevisiae."
      Smith C.D., Smith D.L., DeRisi J.L., Blackburn E.H.
      Mol. Biol. Cell 14:556-570(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "Counting of Rif1p and Rif2p on Saccharomyces cerevisiae telomeres regulates telomere length."
      Levy D.L., Blackburn E.H.
      Mol. Cell. Biol. 24:10857-10867(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    12. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1637, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97; SER-1637 AND SER-1795, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1637 AND SER-1852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRIF1_YEAST
    AccessioniPrimary (citable) accession number: P29539
    Secondary accession number(s): D6VQS1, P89507
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 115 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3