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P29539 (RIF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Telomere length regulator protein RIF1
Alternative name(s):
RAP1-interacting factor 1
Gene names
Name:RIF1
Ordered Locus Names:YBR275C
ORF Names:YBR1743
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1916 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5 Ref.6 Ref.8 Ref.10

Subunit structure

Interacts with RIF2 and RAP1. Ref.1 Ref.6

Subcellular location

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). Ref.7 Ref.8 Ref.9

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RAP1P119383EBI-2083307,EBI-14821

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 19161916Telomere length regulator protein RIF1
PRO_0000097336

Amino acid modifications

Modified residue971Phosphoserine Ref.13
Modified residue16371Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14
Modified residue17951Phosphoserine Ref.13
Modified residue18521Phosphoserine Ref.14

Experimental info

Sequence conflict5801C → S in CAA47121. Ref.1
Sequence conflict7321A → T in CAA85238. Ref.2
Sequence conflict7321A → T in CAA53638. Ref.4

Secondary structure

......... 1916
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29539 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 07070AF02361D96F

FASTA1,916217,931
        10         20         30         40         50         60 
MSKDFSDKKK HTIDRIDQHI LRRSQHDNYS NGSSPWMKTN LPPPSPQAHM HIQSDLSPTP 

        70         80         90        100        110        120 
KRRKLASSSD CENKQFDLSA INKNLYPEDT GSRLMQSLPE LSASNSDNVS PVTKSVAFSD 

       130        140        150        160        170        180 
RIESSPIYRI PGSSPKPSPS SKPGKSILRN RLPSVRTVSD LSYNKLQYTQ HKLHNGNIFT 

       190        200        210        220        230        240 
SPYKETRVNP RALEYWVSGE IHGLVDNESV SEFKEIIEGG LGILRQESED YVARRFEVYA 

       250        260        270        280        290        300 
TFNNIIPILT TKNVNEVDQK FNILIVNIES IIEICIPHLQ IAQDTLLSSS EKKNPFVIRL 

       310        320        330        340        350        360 
YVQIVRFFSA IMSNFKIVKW LTKRPDLVNK LKVIYRWTTG ALRNENSNKI IITAQVSFLR 

       370        380        390        400        410        420 
DEKFGTFFLS NEEIKPIIST FTEIMEINSH NLIYEKLLLI RGFLSKYPKL MIETVTSWLP 

       430        440        450        460        470        480 
GEVLPRIIIG DEIYSMKILI TSIVVLLELL KKCLDFVDEH ERIYQCIMLS PVCETIPEKF 

       490        500        510        520        530        540 
LSKLPLNSYD SANLDKVTIG HLLTQQIKNY IVVKNDNKIA MDLWLSMTGL LYDSGKRVYD 

       550        560        570        580        590        600 
LTSESNKVWF DLNNLCFINN HPKTRLMSIK VWRIITYCIC TKISQKNQEG NKSLLSLLRT 

       610        620        630        640        650        660 
PFQMTLPYVN DPSAREGIIY HLLGVVYTAF TSNKNLSTDM FELFWDHLIT PIYEDYVFKY 

       670        680        690        700        710        720 
DSIHLQNVLF TVLHLLIGGK NADVALERKY KKHIHPMSVI ASEGVKLKDI SSLPPQIIKR 

       730        740        750        760        770        780 
EYDKIMKVVF QAVEVAISNV NLAHDLILTS LKHLPEDRKD QTHLESFSSL ILKVTQNNKD 

       790        800        810        820        830        840 
TPIFRDFFGA VTSSFVYTFL DLFLRKNDSS LVNFNIQISK VGISQGNMTL DLLKDVIRKA 

       850        860        870        880        890        900 
RNETSEFLII EKFLELDDKK TEVYAQNWVG STLLPPNISF REFQSLANIV NKVPNENSIE 

       910        920        930        940        950        960 
NFLDLCLKLS FPVNLFTLLH VSMWSNNNFI YFIQSYVSKN ENKLNVDLIT LLKTSLPGNP 

       970        980        990       1000       1010       1020 
ELFSGLLPFL RRNKFMDILE YCIHSNPNLL NSIPDLNSDL LLKLLPRSRA SYFAANIKLF 

      1030       1040       1050       1060       1070       1080 
KCSEQLTLVR WLLKGQQLEQ LNQNFSEIEN VLQNASDSEL EKSEIIRELL HLAMANPIEP 

      1090       1100       1110       1120       1130       1140 
LFSGLLNFCI KNNMADHLDE FCGNMTSEVL FKISPELLLK LLTYKEKPNG KLLAAVIEKI 

      1150       1160       1170       1180       1190       1200 
ENGDDDYILE LLEKIIIQKE IQILEKLKEP LLVFFLNPVS SNMQKHKKST NMLRELVLLY 

      1210       1220       1230       1240       1250       1260 
LTKPLSRSAA KKFFSMLISI LPPNPNYQTI DMVNLLIDLI KSHNRKFKDK RTYNATLKTI 

      1270       1280       1290       1300       1310       1320 
GKWIQESGVV HQGDSSKEIE AIPDTKSMYI PCEGSENKLS NLQRKVDSQD IQVPATQGMK 

      1330       1340       1350       1360       1370       1380 
EPPSSIQISS QISAKDSDSI SLKNTAIMNS SQQESHANRS RSIDDETLEE VDNESIREID 

      1390       1400       1410       1420       1430       1440 
QQMKSTQLDK NVANHSNICS TKSDEVDVTE LHESIDTQSS EVNAYQPIEV LTSELKAVTN 

      1450       1460       1470       1480       1490       1500 
RSIKTNPDHN VVNSDNPLKR PSKETPTSEN KRSKGHETMV DVLVSEEQAV SPSSDVICTN 

      1510       1520       1530       1540       1550       1560 
IKSIANEESS LALRNSIKVE TNCNENSLNV TLDLDQQTIT KEDGKGQVEH VQRQENQESM 

      1570       1580       1590       1600       1610       1620 
NKINSKSFTQ DNIAQYKSVK KARPNNEGEN NDYACNVEQA SPVRNEVPGD GIQIPSGTIL 

      1630       1640       1650       1660       1670       1680 
LNSSKQTEKS KVDDLRSDED EHGTVAQEKH QVGAINSRNK NNDRMDSTPI QGTEEESREV 

      1690       1700       1710       1720       1730       1740 
VMTEEGINVR LEDSGTCELN KNLKGPLKGD KDANINDDFV PVEENVRDEG FLKSMEHAVS 

      1750       1760       1770       1780       1790       1800 
KETGLEEQPE VADISVLPEI RIPIFNSLKM QGSKSQIKEK LKKRLQRNEL MPPDSPPRMT 

      1810       1820       1830       1840       1850       1860 
ENTNINAQNG LDTVPKTIGG KEKHHEIQLG QAHTEADGEP LLGGDGNEDA TSREATPSLK 

      1870       1880       1890       1900       1910 
VHFFSKKSRR LVARLRGFTP GDLNGISVEE RRNLRIELLD FMMRLEYYSN RDNDMN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS46157.
RefSeqNP_009834.4. NM_001178623.4.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BJSX-ray1.94A/B/C/D1857-1916[»]
4BJTX-ray1.61D/E/F1752-1771[»]
ProteinModelPortalP29539.
SMRP29539. Positions 1857-1911.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32970. 67 interactions.
DIPDIP-801N.
IntActP29539. 8 interactions.
MINTMINT-2780441.
STRING4932.YBR275C.

Proteomic databases

PaxDbP29539.
PeptideAtlasP29539.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR275C; YBR275C; YBR275C.
GeneID852578.
KEGGsce:YBR275C.

Organism-specific databases

CYGDYBR275c.
SGDS000000479. RIF1.

Phylogenomic databases

eggNOGNOG73322.
KOK11118.
OrthoDBEOG7R838T.

Enzyme and pathway databases

BioCycYEAST:G3O-29196-MONOMER.

Gene expression databases

GenevestigatorP29539.

Family and domain databases

InterProIPR022031. Rif1_N.
[Graphical view]
PfamPF12231. Rif1_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio971718.

Entry information

Entry nameRIF1_YEAST
AccessionPrimary (citable) accession number: P29539
Secondary accession number(s): D6VQS1, P89507
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PDB cross-references

Index of Protein Data Bank (PDB) cross-references