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Protein

ATP-dependent DNA helicase PIF1

Gene

PIF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Appears to move along DNA in single nucleotide or base pair steps, powered by hydrolysis of 1 molecule of ATP. Processes at an unwinding rate of about 75 bp/s. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Involved in the maintenance of ribosomal (rDNA). Required for efficient fork arrest at the replicaion fork barrier within rDNA. Involved in the maintenance of mitochondrial (mtDNA). Required to maintain mtDNA under conditions that introduce dsDNA breaks in mtDNA, either preventing or repairing dsDNA breaks. May inhibit replication progression to allow time for repair. May have a general role in chromosomal replication by affecting Okazaki fragment maturation. May have a role in conjunction with DNA2 helicase/nuclease in 5'-flap extension during Okazaki fragment processing.UniRule annotation23 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation3 Publications

Cofactori

Mg2+UniRule annotation1 Publication, Mn2+UniRule annotation1 PublicationNote: Mg2+. To a lesser extent, can also use Mn2+.UniRule annotation1 Publication

Kineticsi

  1. KM=1.3 mM for ATP1 Publication
  2. KM=0.4 mM for dATP1 Publication

    pH dependencei

    Optimum pH is 7.5-9.5.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi258 – 2658ATPUniRule annotation
    DNA bindingi727 – 74620UniRule annotationAdd
    BLAST

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-HAMAP
    • ATP-dependent 5'-3' DNA helicase activity Source: GO_Central
    • DNA helicase activity Source: SGD
    • G-quadruplex DNA binding Source: SGD
    • single-stranded DNA binding Source: SGD
    • telomerase inhibitor activity Source: SGD

    GO - Biological processi

    • chromosome organization Source: SGD
    • DNA recombination Source: SGD
    • DNA strand renaturation Source: SGD
    • double-strand break repair via break-induced replication Source: SGD
    • G-quadruplex DNA unwinding Source: SGD
    • mitochondrial genome maintenance Source: SGD
    • negative regulation of telomere maintenance via telomerase Source: SGD
    • replication fork reversal Source: SGD
    • telomere maintenance Source: SGD
    • telomere maintenance via recombination Source: SGD
    Complete GO annotation...

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32656-MONOMER.
    BRENDAi3.6.4.12. 984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent DNA helicase PIF1UniRule annotation (EC:3.6.4.12UniRule annotation)
    Alternative name(s):
    DNA repair and recombination helicase PIF1UniRule annotation
    Petite integration frequency protein 1
    Telomere stability protein 1
    Gene namesi
    Name:PIF1UniRule annotation
    Synonyms:TST1
    Ordered Locus Names:YML061C
    ORF Names:YM9958.01C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XIII

    Organism-specific databases

    EuPathDBiFungiDB:YML061C.
    SGDiS000004526. PIF1.

    Subcellular locationi

    Isoform Nuclear :
    Isoform Mitochondrial :

    GO - Cellular componenti

    • mitochondrial inner membrane Source: UniProtKB-SubCell
    • mitochondrial membrane Source: SGD
    • mitochondrion Source: SGD
    • nuclear replication fork Source: SGD
    • nucleolus Source: UniProtKB-SubCell
    • nucleus Source: SGD
    • replication fork Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1 – 11M → A in PIF1-m1; loss of mitochondrial function. 1 Publication
    Mutagenesisi40 – 401M → A in PIF1-m2; loss of nuclear function. 1 Publication
    Mutagenesisi264 – 2641K → A or R: Abolishes helicase activity resulting in elongated telomeres; binds normally to DNA substrates. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4545Mitochondrion1 PublicationAdd
    BLAST
    Chaini46 – 859814ATP-dependent DNA helicase PIF1PRO_0000013269Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701PhosphoserineCombined sources
    Modified residuei72 – 721PhosphoserineCombined sources
    Modified residuei169 – 1691PhosphoserineCombined sources
    Modified residuei584 – 5841PhosphoserineCombined sources

    Post-translational modificationi

    Phosphorylated. Undergoes RAD53-dependent phosphorylation in response to loss of mtDNA.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP07271.

    PTM databases

    iPTMnetiP07271.

    Expressioni

    Inductioni

    Cell cycle-regulated. The nuclear isoform is present in very low amounts in G1 phase cells, but increases as cells progress through S phase, with a peak in late S/G2. The mitochondrial isoform follows a similar, but less pronounced induction pattern. The nuclear isoform is prone to APC/C-dependent degradation in G1, whereas the mitochondrial isoform is not.1 Publication

    Interactioni

    Subunit structurei

    Monomer in solution. DNA binding induces dimerization. Associates with mitochondrial and telomeric DNA. Binding to mtDNA is non-specific and the protein seems to coat the entire mtDNA molecule. Binds to the telomerase RNA TLC1. Interacts with the mitochondrial single-strand DNA-binding protein RIM1.UniRule annotation4 Publications

    Protein-protein interaction databases

    BioGridi35105. 107 interactions.
    DIPiDIP-4448N.
    IntActiP07271. 1 interaction.
    MINTiMINT-496209.

    Structurei

    3D structure databases

    ProteinModelPortaliP07271.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the helicase family. PIF1 subfamily.UniRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    GeneTreeiENSGT00530000063561.
    InParanoidiP07271.
    KOiK15255.
    OMAiRVQLPLM.
    OrthoDBiEOG76MKKK.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    HAMAPiMF_03176. PIF1.
    InterProiIPR003840. DNA_helicase.
    IPR010285. DNA_helicase_pif1-like.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR23274. PTHR23274. 2 hits.
    PfamiPF05970. PIF1. 2 hits.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

    Isoform Mitochondrial (identifier: P07271-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MPKWIRSTLN HIIPRRPFIC SFNSFLLLKN VSHAKLSFSM SSRGFRSNNF
    60 70 80 90 100
    IQAQLKHPSI LSKEDLDLLS DSDDWEEPDC IQLETEKQEK KIITDIHKED
    110 120 130 140 150
    PVDKKPMRDK NVMNFINKDS PLSWNDMFKP SIIQPPQLIS ENSFDQSSQK
    160 170 180 190 200
    KSRSTGFKNP LRPALKKESS FDELQNNSIS QERSLEMINE NEKKKMQFGE
    210 220 230 240 250
    KIAVLTQRPS FTELQNDQDD SNLNPHNGVK VKIPICLSKE QESIIKLAEN
    260 270 280 290 300
    GHNIFYTGSA GTGKSILLRE MIKVLKGIYG RENVAVTAST GLAACNIGGI
    310 320 330 340 350
    TIHSFAGIGL GKGDADKLYK KVRRSRKHLR RWENIGALVV DEISMLDAEL
    360 370 380 390 400
    LDKLDFIARK IRKNHQPFGG IQLIFCGDFF QLPPVSKDPN RPTKFAFESK
    410 420 430 440 450
    AWKEGVKMTI MLQKVFRQRG DVKFIDMLNR MRLGNIDDET EREFKKLSRP
    460 470 480 490 500
    LPDDEIIPAE LYSTRMEVER ANNSRLSKLP GQVHIFNAID GGALEDEELK
    510 520 530 540 550
    ERLLQNFLAP KELHLKVGAQ VMMVKNLDAT LVNGSLGKVI EFMDPETYFC
    560 570 580 590 600
    YEALTNDPSM PPEKLETWAE NPSKLKAAME REQSDGEESA VASRKSSVKE
    610 620 630 640 650
    GFAKSDIGEP VSPLDSSVFD FMKRVKTDDE VVLENIKRKE QLMQTIHQNS
    660 670 680 690 700
    AGKRRLPLVR FKASDMSTRM VLVEPEDWAI EDENEKPLVS RVQLPLMLAW
    710 720 730 740 750
    SLSIHKSQGQ TLPKVKVDLR RVFEKGQAYV ALSRAVSREG LQVLNFDRTR
    760 770 780 790 800
    IKAHQKVIDF YLTLSSAESA YKQLEADEQV KKRKLDYAPG PKYKAKSKSK
    810 820 830 840 850
    SNSPAPISAT TQSNNGIAAM LQRHSRKRFQ LKKESNSNQV HSLVSDEPRG

    QDTEDHILE
    Length:859
    Mass (Da):97,682
    Last modified:July 1, 2008 - v2
    Checksum:iD7E4CAE499822C2C
    GO
    Isoform Nuclear (identifier: P07271-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: Missing.

    Note: Produced by alternative initiation at Met-40 of isoform Mitochondrial.1 Publication
    Show »
    Length:820
    Mass (Da):93,099
    Checksum:iEF75E0595E9150DC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti309 – 3091Missing in CAA28953 (PubMed:3038524).Curated
    Sequence conflicti322 – 3221V → VG in CAA28953 (PubMed:3038524).Curated
    Sequence conflicti426 – 4261D → E in CAA28953 (PubMed:3038524).Curated
    Sequence conflicti800 – 8012Missing in CAA28953 (PubMed:3038524).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3939Missing in isoform Nuclear. CuratedVSP_034601Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X05342 Genomic DNA. Translation: CAA28953.1.
    Z46729 Genomic DNA. Translation: CAA86714.1.
    Z38114 Genomic DNA. Translation: CAA86260.1.
    BK006946 Genomic DNA. Translation: DAA09836.1.
    PIRiA29457.
    RefSeqiNP_013650.1. NM_001182420.1. [P07271-1]

    Genome annotation databases

    EnsemblFungiiYML061C; YML061C; YML061C. [P07271-1]
    GeneIDi854941.
    KEGGisce:YML061C.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X05342 Genomic DNA. Translation: CAA28953.1.
    Z46729 Genomic DNA. Translation: CAA86714.1.
    Z38114 Genomic DNA. Translation: CAA86260.1.
    BK006946 Genomic DNA. Translation: DAA09836.1.
    PIRiA29457.
    RefSeqiNP_013650.1. NM_001182420.1. [P07271-1]

    3D structure databases

    ProteinModelPortaliP07271.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi35105. 107 interactions.
    DIPiDIP-4448N.
    IntActiP07271. 1 interaction.
    MINTiMINT-496209.

    PTM databases

    iPTMnetiP07271.

    Proteomic databases

    MaxQBiP07271.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYML061C; YML061C; YML061C. [P07271-1]
    GeneIDi854941.
    KEGGisce:YML061C.

    Organism-specific databases

    EuPathDBiFungiDB:YML061C.
    SGDiS000004526. PIF1.

    Phylogenomic databases

    GeneTreeiENSGT00530000063561.
    InParanoidiP07271.
    KOiK15255.
    OMAiRVQLPLM.
    OrthoDBiEOG76MKKK.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32656-MONOMER.
    BRENDAi3.6.4.12. 984.

    Miscellaneous databases

    PROiP07271.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    HAMAPiMF_03176. PIF1.
    InterProiIPR003840. DNA_helicase.
    IPR010285. DNA_helicase_pif1-like.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR23274. PTHR23274. 2 hits.
    PfamiPF05970. PIF1. 2 hits.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and sequencing of the PIF gene involved in repair and recombination of yeast mitochondrial DNA."
      Foury F., Lahaye A.
      EMBO J. 6:1441-1449(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN MITOCHONDRIAL DNA REPAIR.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "PIF1 DNA helicase from Saccharomyces cerevisiae. Biochemical characterization of the enzyme."
      Lahaye A., Leterme S., Foury F.
      J. Biol. Chem. 268:26155-26161(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    5. "PIF1: a DNA helicase in yeast mitochondria."
      Lahaye A., Stahl H., Thines-Sempoux D., Foury F.
      EMBO J. 10:997-1007(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    6. "The Saccharomyces PIF1 DNA helicase inhibits telomere elongation and de novo telomere formation."
      Schulz V.P., Zakian V.A.
      Cell 76:145-155(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TELOMERE LENGTH REGULATION, MUTAGENESIS OF MET-1 AND MET-40, ALTERNATIVE PRODUCT.
    7. "The Saccharomyces Pif1p DNA helicase and the highly related Rrm3p have opposite effects on replication fork progression in ribosomal DNA."
      Ivessa A.S., Zhou J.-Q., Zakian V.A.
      Cell 100:479-489(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN RIBOSOMAL DNA MAINTENANCE.
    8. "Pif1p helicase, a catalytic inhibitor of telomerase in yeast."
      Zhou J.-Q., Monson E.K., Teng S.-C., Schulz V.P., Zakian V.A.
      Science 289:771-774(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TELOMERE LENGTH REGULATION, MUTAGENESIS OF LYS-264.
    9. "Multiple pathways cooperate in the suppression of genome instability in Saccharomyces cerevisiae."
      Myung K., Chen C., Kolodner R.D.
      Nature 411:1073-1076(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN GENOMIC DNA MAINTENANCE.
    10. "Mitochondrial dysfunction due to oxidative mitochondrial DNA damage is reduced through cooperative actions of diverse proteins."
      O'Rourke T.W., Doudican N.A., Mackereth M.D., Doetsch P.W., Shadel G.S.
      Mol. Cell. Biol. 22:4086-4093(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MITOCHONDRIAL DNA REPAIR.
    11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Strain: ATCC 76625 / YPH499.
    14. "Differential involvement of the related DNA helicases Pif1p and Rrm3p in mtDNA point mutagenesis and stability."
      O'Rourke T.W., Doudican N.A., Zhang H., Eaton J.S., Doetsch P.W., Shadel G.S.
      Gene 354:86-92(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MITOCHONDRIAL DNA REPAIR.
    15. "Oxidative DNA damage causes mitochondrial genomic instability in Saccharomyces cerevisiae."
      Doudican N.A., Song B., Shadel G.S., Doetsch P.W.
      Mol. Cell. Biol. 25:5196-5204(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MITOCHONDRIAL DNA REPAIR.
    16. "The yeast Pif1p helicase removes telomerase from telomeric DNA."
      Boule J.-B., Vega L.R., Zakian V.A.
      Nature 438:57-61(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TELOMERE LENGTH REGULATION, MUTAGENESIS OF LYS-264.
    17. "The absence of Top3 reveals an interaction between the Sgs1 and Pif1 DNA helicases in Saccharomyces cerevisiae."
      Wagner M., Price G., Rothstein R.
      Genetics 174:555-573(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-264, SUBCELLULAR LOCATION.
    18. "Evidence suggesting that Pif1 helicase functions in DNA replication with the Dna2 helicase/nuclease and DNA polymerase delta."
      Budd M.E., Reis C.C., Smith S., Myung K., Campbell J.L.
      Mol. Cell. Biol. 26:2490-2500(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA REPLICATION.
    19. Cited for: FUNCTION IN TELOMERE LENGTH REGULATION, INTERACTION WITH TELOMERASE RNA.
    20. "The role of Pif1p, a DNA helicase in Saccharomyces cerevisiae, in maintaining mitochondrial DNA."
      Cheng X., Dunaway S., Ivessa A.S.
      Mitochondrion 7:211-222(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MITOCHONDRIAL DNA MAINTENANCE, DNA-BINDING.
    21. "The yeast Pif1p DNA helicase preferentially unwinds RNA-DNA substrates."
      Boule J.-B., Zakian V.A.
      Nucleic Acids Res. 35:5809-5818(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Sensitivity of yeast strains with long G-tails to levels of telomere-bound telomerase."
      Vega L.R., Phillips J.A., Thornton B.R., Benanti J.A., Onigbanjo M.T., Toczyski D.P., Zakian V.A.
      PLoS Genet. 3:1065-1075(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TELOMERE LENGTH REGULATION, INDUCTION.
    23. "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-584, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "The yeast Pif1 helicase prevents genomic instability caused by G-quadruplex-forming CEB1 sequences in vivo."
      Ribeyre C., Lopes J., Boule J.B., Piazza A., Guedin A., Zakian V.A., Mergny J.L., Nicolas A.
      PLoS Genet. 5:E1000475-E1000475(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN G4-UNWINDING.
    25. "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-70; SER-72 AND SER-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "DNA binding induces dimerization of Saccharomyces cerevisiae Pif1."
      Barranco-Medina S., Galletto R.
      Biochemistry 49:8445-8454(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    27. "Association of the yeast DNA helicase Pif1p with mitochondrial membranes and mitochondrial DNA."
      Cheng X., Ivessa A.S.
      Eur. J. Cell Biol. 89:742-747(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    28. "Characterization of the helicase activity and anti-telomerase properties of yeast Pif1p in vitro."
      Boule J.B., Zakian V.A.
      Methods Mol. Biol. 587:359-376(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TELOMERE LENGTH REGULATION.
    29. "DNA replication through G-quadruplex motifs is promoted by the Saccharomyces cerevisiae Pif1 DNA helicase."
      Paeschke K., Capra J.A., Zakian V.A.
      Cell 145:678-691(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN G4-UNWINDING.
    30. "Rad53 is essential for a mitochondrial DNA inheritance checkpoint regulating G1 to S progression."
      Crider D.G., Garcia-Rodriguez L.J., Srivastava P., Peraza-Reyes L., Upadhyaya K., Boldogh I.R., Pon L.A.
      J. Cell Biol. 198:793-798(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    31. "Yeast Pif1 helicase exhibits a one-base-pair stepping mechanism for unwinding duplex DNA."
      Ramanagoudr-Bhojappa R., Chib S., Byrd A.K., Aarattuthodiyil S., Pandey M., Patel S.S., Raney K.D.
      J. Biol. Chem. 288:16185-16195(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    32. "Pif1 family helicases suppress genome instability at G-quadruplex motifs."
      Paeschke K., Bochman M.L., Garcia P.D., Cejka P., Friedman K.L., Kowalczykowski S.C., Zakian V.A.
      Nature 497:458-462(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN G4-UNWINDING.
    33. "Physical and functional interaction between yeast Pif1 helicase and Rim1 single-stranded DNA binding protein."
      Ramanagoudr-Bhojappa R., Blair L.P., Tackett A.J., Raney K.D.
      Nucleic Acids Res. 41:1029-1046(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RIM1.
    34. "Translocation of Saccharomyces cerevisiae Pif1 helicase monomers on single-stranded DNA."
      Galletto R., Tomko E.J.
      Nucleic Acids Res. 41:4613-4627(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiPIF1_YEAST
    AccessioniPrimary (citable) accession number: P07271
    Secondary accession number(s): D6VZB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: July 1, 2008
    Last modified: July 6, 2016
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 259 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.