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P29539

- RIF1_YEAST

UniProt

P29539 - RIF1_YEAST

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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

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. 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
Complete GO annotation...

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
Complete GO annotation...

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 – 18613Combined sources
Helixi1866 – 187611Combined sources
Helixi1880 – 18856Combined sources
Helixi1888 – 190720Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP29539.
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

        10         20         30         40         50
MSKDFSDKKK HTIDRIDQHI LRRSQHDNYS NGSSPWMKTN LPPPSPQAHM
60 70 80 90 100
HIQSDLSPTP KRRKLASSSD CENKQFDLSA INKNLYPEDT GSRLMQSLPE
110 120 130 140 150
LSASNSDNVS PVTKSVAFSD RIESSPIYRI PGSSPKPSPS SKPGKSILRN
160 170 180 190 200
RLPSVRTVSD LSYNKLQYTQ HKLHNGNIFT SPYKETRVNP RALEYWVSGE
210 220 230 240 250
IHGLVDNESV SEFKEIIEGG LGILRQESED YVARRFEVYA TFNNIIPILT
260 270 280 290 300
TKNVNEVDQK FNILIVNIES IIEICIPHLQ IAQDTLLSSS EKKNPFVIRL
310 320 330 340 350
YVQIVRFFSA IMSNFKIVKW LTKRPDLVNK LKVIYRWTTG ALRNENSNKI
360 370 380 390 400
IITAQVSFLR DEKFGTFFLS NEEIKPIIST FTEIMEINSH NLIYEKLLLI
410 420 430 440 450
RGFLSKYPKL MIETVTSWLP GEVLPRIIIG DEIYSMKILI TSIVVLLELL
460 470 480 490 500
KKCLDFVDEH ERIYQCIMLS PVCETIPEKF LSKLPLNSYD SANLDKVTIG
510 520 530 540 550
HLLTQQIKNY IVVKNDNKIA MDLWLSMTGL LYDSGKRVYD LTSESNKVWF
560 570 580 590 600
DLNNLCFINN HPKTRLMSIK VWRIITYCIC TKISQKNQEG NKSLLSLLRT
610 620 630 640 650
PFQMTLPYVN DPSAREGIIY HLLGVVYTAF TSNKNLSTDM FELFWDHLIT
660 670 680 690 700
PIYEDYVFKY DSIHLQNVLF TVLHLLIGGK NADVALERKY KKHIHPMSVI
710 720 730 740 750
ASEGVKLKDI SSLPPQIIKR EYDKIMKVVF QAVEVAISNV NLAHDLILTS
760 770 780 790 800
LKHLPEDRKD QTHLESFSSL ILKVTQNNKD TPIFRDFFGA VTSSFVYTFL
810 820 830 840 850
DLFLRKNDSS LVNFNIQISK VGISQGNMTL DLLKDVIRKA RNETSEFLII
860 870 880 890 900
EKFLELDDKK TEVYAQNWVG STLLPPNISF REFQSLANIV NKVPNENSIE
910 920 930 940 950
NFLDLCLKLS FPVNLFTLLH VSMWSNNNFI YFIQSYVSKN ENKLNVDLIT
960 970 980 990 1000
LLKTSLPGNP ELFSGLLPFL RRNKFMDILE YCIHSNPNLL NSIPDLNSDL
1010 1020 1030 1040 1050
LLKLLPRSRA SYFAANIKLF KCSEQLTLVR WLLKGQQLEQ LNQNFSEIEN
1060 1070 1080 1090 1100
VLQNASDSEL EKSEIIRELL HLAMANPIEP LFSGLLNFCI KNNMADHLDE
1110 1120 1130 1140 1150
FCGNMTSEVL FKISPELLLK LLTYKEKPNG KLLAAVIEKI ENGDDDYILE
1160 1170 1180 1190 1200
LLEKIIIQKE IQILEKLKEP LLVFFLNPVS SNMQKHKKST NMLRELVLLY
1210 1220 1230 1240 1250
LTKPLSRSAA KKFFSMLISI LPPNPNYQTI DMVNLLIDLI KSHNRKFKDK
1260 1270 1280 1290 1300
RTYNATLKTI GKWIQESGVV HQGDSSKEIE AIPDTKSMYI PCEGSENKLS
1310 1320 1330 1340 1350
NLQRKVDSQD IQVPATQGMK EPPSSIQISS QISAKDSDSI SLKNTAIMNS
1360 1370 1380 1390 1400
SQQESHANRS RSIDDETLEE VDNESIREID QQMKSTQLDK NVANHSNICS
1410 1420 1430 1440 1450
TKSDEVDVTE LHESIDTQSS EVNAYQPIEV LTSELKAVTN RSIKTNPDHN
1460 1470 1480 1490 1500
VVNSDNPLKR PSKETPTSEN KRSKGHETMV DVLVSEEQAV SPSSDVICTN
1510 1520 1530 1540 1550
IKSIANEESS LALRNSIKVE TNCNENSLNV TLDLDQQTIT KEDGKGQVEH
1560 1570 1580 1590 1600
VQRQENQESM NKINSKSFTQ DNIAQYKSVK KARPNNEGEN NDYACNVEQA
1610 1620 1630 1640 1650
SPVRNEVPGD GIQIPSGTIL LNSSKQTEKS KVDDLRSDED EHGTVAQEKH
1660 1670 1680 1690 1700
QVGAINSRNK NNDRMDSTPI QGTEEESREV VMTEEGINVR LEDSGTCELN
1710 1720 1730 1740 1750
KNLKGPLKGD KDANINDDFV PVEENVRDEG FLKSMEHAVS KETGLEEQPE
1760 1770 1780 1790 1800
VADISVLPEI RIPIFNSLKM QGSKSQIKEK LKKRLQRNEL MPPDSPPRMT
1810 1820 1830 1840 1850
ENTNINAQNG LDTVPKTIGG KEKHHEIQLG QAHTEADGEP LLGGDGNEDA
1860 1870 1880 1890 1900
TSREATPSLK VHFFSKKSRR LVARLRGFTP GDLNGISVEE RRNLRIELLD
1910
FMMRLEYYSN RDNDMN
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P29539.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 117 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