P29539 · RIF1_YEAST

Function

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromosome, telomeric region
Cellular Componentnucleus
Cellular Componentshelterin complex
Molecular Functioncentromeric DNA binding
Molecular FunctionDNA replication origin binding
Molecular FunctionRNA polymerase II core promoter sequence-specific DNA binding
Molecular Functiontelomeric DNA binding
Biological ProcessDNA double-strand break processing
Biological ProcessDNA replication initiation
Biological Processnegative regulation of DNA-templated DNA replication initiation
Biological Processnegative regulation of mitotic DNA replication initiation from late origin
Biological Processprotein localization to chromosome, telomeric region
Biological Processregulation of DNA stability
Biological Processsilent mating-type cassette heterochromatin formation
Biological Processtelomere capping
Biological Processtelomere maintenance

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Telomere length regulator protein RIF1
  • Alternative names
    • RAP1-interacting factor 1

Gene names

    • Name
      RIF1
    • ORF names
      YBR1743
    • Ordered locus names
      YBR275C

Organism names

Accessions

  • Primary accession
    P29539
  • Secondary accessions
    • D6VQS1
    • P89507

Proteomes

Organism-specific databases

Subcellular Location

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).

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00000973361-1916Telomere length regulator protein RIF1
Modified residue97Phosphoserine
Modified residue1637Phosphoserine
Modified residue1795Phosphoserine
Modified residue1852Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with RAP1 (via C-terminus) (PubMed:1577274, PubMed:7867933, PubMed:9087429).
Interacts with RIF2 (PubMed:7867933, PubMed:9087429).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY P29539RAP1 P119383EBI-2083307, EBI-14821

Complex viewer

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region.

Type
IDPosition(s)Description
Compositional bias1-24Basic and acidic residues
Region1-71Disordered
Compositional bias46-64Polar residues
Region126-149Disordered
Compositional bias1314-1357Polar residues
Region1314-1372Disordered
Compositional bias1441-1461Polar residues
Region1441-1476Disordered
Compositional bias1462-1476Basic and acidic residues
Region1606-1678Disordered
Compositional bias1627-1647Basic and acidic residues
Compositional bias1650-1668Polar residues
Region1789-1811Disordered
Compositional bias1797-1811Polar residues
Region1829-1854Disordered

Sequence similarities

Belongs to the RIF1 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,916
  • Mass (Da)
    217,931
  • Last updated
    2011-07-27 v3
  • Checksum
    07070AF02361D96F
MSKDFSDKKKHTIDRIDQHILRRSQHDNYSNGSSPWMKTNLPPPSPQAHMHIQSDLSPTPKRRKLASSSDCENKQFDLSAINKNLYPEDTGSRLMQSLPELSASNSDNVSPVTKSVAFSDRIESSPIYRIPGSSPKPSPSSKPGKSILRNRLPSVRTVSDLSYNKLQYTQHKLHNGNIFTSPYKETRVNPRALEYWVSGEIHGLVDNESVSEFKEIIEGGLGILRQESEDYVARRFEVYATFNNIIPILTTKNVNEVDQKFNILIVNIESIIEICIPHLQIAQDTLLSSSEKKNPFVIRLYVQIVRFFSAIMSNFKIVKWLTKRPDLVNKLKVIYRWTTGALRNENSNKIIITAQVSFLRDEKFGTFFLSNEEIKPIISTFTEIMEINSHNLIYEKLLLIRGFLSKYPKLMIETVTSWLPGEVLPRIIIGDEIYSMKILITSIVVLLELLKKCLDFVDEHERIYQCIMLSPVCETIPEKFLSKLPLNSYDSANLDKVTIGHLLTQQIKNYIVVKNDNKIAMDLWLSMTGLLYDSGKRVYDLTSESNKVWFDLNNLCFINNHPKTRLMSIKVWRIITYCICTKISQKNQEGNKSLLSLLRTPFQMTLPYVNDPSAREGIIYHLLGVVYTAFTSNKNLSTDMFELFWDHLITPIYEDYVFKYDSIHLQNVLFTVLHLLIGGKNADVALERKYKKHIHPMSVIASEGVKLKDISSLPPQIIKREYDKIMKVVFQAVEVAISNVNLAHDLILTSLKHLPEDRKDQTHLESFSSLILKVTQNNKDTPIFRDFFGAVTSSFVYTFLDLFLRKNDSSLVNFNIQISKVGISQGNMTLDLLKDVIRKARNETSEFLIIEKFLELDDKKTEVYAQNWVGSTLLPPNISFREFQSLANIVNKVPNENSIENFLDLCLKLSFPVNLFTLLHVSMWSNNNFIYFIQSYVSKNENKLNVDLITLLKTSLPGNPELFSGLLPFLRRNKFMDILEYCIHSNPNLLNSIPDLNSDLLLKLLPRSRASYFAANIKLFKCSEQLTLVRWLLKGQQLEQLNQNFSEIENVLQNASDSELEKSEIIRELLHLAMANPIEPLFSGLLNFCIKNNMADHLDEFCGNMTSEVLFKISPELLLKLLTYKEKPNGKLLAAVIEKIENGDDDYILELLEKIIIQKEIQILEKLKEPLLVFFLNPVSSNMQKHKKSTNMLRELVLLYLTKPLSRSAAKKFFSMLISILPPNPNYQTIDMVNLLIDLIKSHNRKFKDKRTYNATLKTIGKWIQESGVVHQGDSSKEIEAIPDTKSMYIPCEGSENKLSNLQRKVDSQDIQVPATQGMKEPPSSIQISSQISAKDSDSISLKNTAIMNSSQQESHANRSRSIDDETLEEVDNESIREIDQQMKSTQLDKNVANHSNICSTKSDEVDVTELHESIDTQSSEVNAYQPIEVLTSELKAVTNRSIKTNPDHNVVNSDNPLKRPSKETPTSENKRSKGHETMVDVLVSEEQAVSPSSDVICTNIKSIANEESSLALRNSIKVETNCNENSLNVTLDLDQQTITKEDGKGQVEHVQRQENQESMNKINSKSFTQDNIAQYKSVKKARPNNEGENNDYACNVEQASPVRNEVPGDGIQIPSGTILLNSSKQTEKSKVDDLRSDEDEHGTVAQEKHQVGAINSRNKNNDRMDSTPIQGTEEESREVVMTEEGINVRLEDSGTCELNKNLKGPLKGDKDANINDDFVPVEENVRDEGFLKSMEHAVSKETGLEEQPEVADISVLPEIRIPIFNSLKMQGSKSQIKEKLKKRLQRNELMPPDSPPRMTENTNINAQNGLDTVPKTIGGKEKHHEIQLGQAHTEADGEPLLGGDGNEDATSREATPSLKVHFFSKKSRRLVARLRGFTPGDLNGISVEERRNLRIELLDFMMRLEYYSNRDNDMN

Features

Showing features for compositional bias, sequence conflict.

Type
IDPosition(s)Description
Compositional bias1-24Basic and acidic residues
Compositional bias46-64Polar residues
Sequence conflict580in Ref. 1; CAA47121
Sequence conflict732in Ref. 2; CAA85238 and 4; CAA53638
Compositional bias1314-1357Polar residues
Compositional bias1441-1461Polar residues
Compositional bias1462-1476Basic and acidic residues
Compositional bias1627-1647Basic and acidic residues
Compositional bias1650-1668Polar residues
Compositional bias1797-1811Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X66501
EMBL· GenBank· DDBJ
CAA47121.1
EMBL· GenBank· DDBJ
Genomic DNA
Z36144
EMBL· GenBank· DDBJ
CAA85238.1
EMBL· GenBank· DDBJ
Genomic DNA
Z36145
EMBL· GenBank· DDBJ
CAA85240.1
EMBL· GenBank· DDBJ
Genomic DNA
X76053
EMBL· GenBank· DDBJ
CAA53638.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006936
EMBL· GenBank· DDBJ
DAA07391.2
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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