Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ATP-dependent DNA helicase PIF1

Gene

PIF1

Organism
Homo sapiens (Human)
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. 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. Possesses an intrinsic strand annealing activity.UniRule annotation7 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation1 Publication

Kineticsi

  1. KM=0.17 mM for ATP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi228 – 2358ATPUniRule annotation
    DNA bindingi577 – 59620UniRule annotationAdd
    BLAST

    GO - Molecular functioni

    • ATP binding Source: HGNC
    • ATP-dependent 5'-3' DNA/RNA helicase activity Source: BHF-UCL
    • ATP-dependent 5'-3' DNA helicase activity Source: HGNC
    • G-quadruplex DNA binding Source: UniProtKB-HAMAP
    • magnesium ion binding Source: HGNC
    • single-stranded DNA-dependent ATP-dependent DNA helicase activity Source: HGNC
    • telomerase inhibitor activity Source: UniProtKB-HAMAP
    • telomeric DNA binding Source: HGNC

    GO - Biological processi

    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

    BRENDAi3.6.4.12. 2681.

    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
    PIF1/RRM3 DNA helicase-like protein
    Gene namesi
    Name:PIF1UniRule annotation
    Synonyms:C15orf20
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:26220. PIF1.

    Subcellular locationi

    Isoform 4 :

    GO - Cellular componenti

    • mitochondrion Source: UniProtKB-SubCell
    • nuclear chromosome, telomeric region Source: HGNC
    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi234 – 2341K → A: Loss of ATPase activity. Lower activity for single-stranded DNA. 1 Publication

    Organism-specific databases

    PharmGKBiPA162399475.

    Polymorphism and mutation databases

    BioMutaiPIF1.
    DMDMi152031656.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 641641ATP-dependent DNA helicase PIF1PRO_0000089980Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271Phosphoserine1 Publication
    Modified residuei151 – 1511Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9H611.
    PaxDbiQ9H611.
    PRIDEiQ9H611.

    PTM databases

    PhosphoSiteiQ9H611.

    Expressioni

    Tissue specificityi

    Weak ubiquitous expression.

    Inductioni

    Tightly cell cycle regulated and expressed in late S/G2 phase.1 Publication

    Gene expression databases

    BgeeiQ9H611.
    CleanExiHS_PIF1.
    GenevestigatoriQ9H611.

    Organism-specific databases

    HPAiCAB018701.

    Interactioni

    Subunit structurei

    Monomer. Interacts with telomerase.UniRule annotation2 Publications

    Protein-protein interaction databases

    IntActiQ9H611. 1 interaction.
    STRINGi9606.ENSP00000268043.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H611.
    SMRiQ9H611. Positions 222-247.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 180180PINTAdd
    BLAST
    Regioni167 – 641475Hydrolyzes ATP in the presence of both magnesium and single-stranded DNA; weak activity in the presence of RNA or double-stranded DNA; No unwinding activityAdd
    BLAST

    Domaini

    The PIF1 N-terminal (PINT) domain enhances the interaction with ssDNA through intrinsic binding activity, it also harbors DNA strand-annealing activity.

    Sequence similaritiesi

    Belongs to the helicase family. PIF1 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0507.
    GeneTreeiENSGT00530000063561.
    HOGENOMiHOG000132960.
    HOVERGENiHBG106706.
    InParanoidiQ9H611.
    KOiK15255.
    OMAiGKCTVKL.
    OrthoDBiEOG7RZ5PJ.
    PhylomeDBiQ9H611.
    TreeFamiTF319207.

    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]
    PfamiPF02689. Herpes_Helicase. 1 hit.
    PF05970. PIF1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

    Isoform 1 (identifier: Q9H611-1) [UniParc]FASTAAdd to basket

    Also known as: Isoform alpha

    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
    MLSGIEAAAG EYEDSELRCR VAVEELSPGG QPRRRQALRT AELSLGRNER
    60 70 80 90 100
    RELMLRLQAP GPAGRPRCFP LRAARLFTRF AEAGRSTLRL PAHDTPGAGA
    110 120 130 140 150
    VQLLLSDCPP DRLRRFLRTL RLKLAAAPGP GPASARAQLL GPRPRDFVTI
    160 170 180 190 200
    SPVQPEERRL RAATRVPDTT LVKRPVEPQA GAEPSTEAPR WPLPVKRLSL
    210 220 230 240 250
    PSTKPQLSEE QAAVLRAVLK GQSIFFTGSA GTGKSYLLKR ILGSLPPTGT
    260 270 280 290 300
    VATASTGVAA CHIGGTTLHA FAGIGSGQAP LAQCVALAQR PGVRQGWLNC
    310 320 330 340 350
    QRLVIDEISM VEADLFDKLE AVARAVRQQN KPFGGIQLII CGDFLQLPPV
    360 370 380 390 400
    TKGSQPPRFC FQSKSWKRCV PVTLELTKVW RQADQTFISL LQAVRLGRCS
    410 420 430 440 450
    DEVTRQLQAT ASHKVGRDGI VATRLCTHQD DVALTNERRL QELPGKVHRF
    460 470 480 490 500
    EAMDSNPELA STLDAQCPVS QLLQLKLGAQ VMLVKNLSVS RGLVNGARGV
    510 520 530 540 550
    VVGFEAEGRG LPQVRFLCGV TEVIHADRWT VQATGGQLLS RQQLPLQLAW
    560 570 580 590 600
    AMSIHKSQGM TLDCVEISLG RVFASGQAYV ALSRARSLQG LRVLDFDPMA
    610 620 630 640
    VRCDPRVLHF YATLRRGRSL SLESPDDDEA ASDQENMDPI L
    Length:641
    Mass (Da):69,799
    Last modified:July 10, 2007 - v2
    Checksum:iD755470008BA3CA8
    GO
    Isoform 2 (identifier: Q9H611-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         232-266: TGKSYLLKRILGSLPPTGTVATASTGVAACHIGGT → SGGREEVGGQWWGGIEEQGDLSNFAPVQEQGSHIC
         267-641: Missing.

    Show »
    Length:266
    Mass (Da):28,907
    Checksum:i0A291FB7E1339D56
    GO
    Isoform 3 (identifier: Q9H611-3) [UniParc]FASTAAdd to basket

    Also known as: Isoform beta

    The sequence of this isoform differs from the canonical sequence as follows:
         623-641: ESPDDDEAASDQENMDPIL → AAEGRGNEDR...FQGINSVWGH

    Show »
    Length:707
    Mass (Da):77,125
    Checksum:iDA015E47D50F8541
    GO
    Isoform 4 (identifier: Q9H611-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: Missing.

    Note: Produced by alternative initiation of isoform 1.

    Show »
    Length:588
    Mass (Da):63,889
    Checksum:i706C693424557525
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti640 – 6401I → N.
    Corresponds to variant rs17802279 [ dbSNP | Ensembl ].
    VAR_033206

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5353Missing in isoform 4. CuratedVSP_047457Add
    BLAST
    Alternative sequencei232 – 26635TGKSY…HIGGT → SGGREEVGGQWWGGIEEQGD LSNFAPVQEQGSHIC in isoform 2. 1 PublicationVSP_026715Add
    BLAST
    Alternative sequencei267 – 641375Missing in isoform 2. 1 PublicationVSP_026716Add
    BLAST
    Alternative sequencei623 – 64119ESPDD…MDPIL → AAEGRGNEDRCSGSSIRALG GDWWGLRLGAASKQRTELRC VSTARPSLAQPRTNTLQSLT KEHKLQNVHPYFKLLFQGIN SVWGH in isoform 3. 1 PublicationVSP_026717Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DQ437529 mRNA. Translation: ABD92708.1.
    EU084033 mRNA. Translation: ABW71293.1.
    AY498716 mRNA. Translation: AAS77398.1.
    AB185926 mRNA. Translation: BAE47454.1.
    AB185927 mRNA. Translation: BAE47455.1.
    AK026345 mRNA. Translation: BAB15456.1.
    BC137503 mRNA. Translation: AAI37504.1.
    BC137504 mRNA. Translation: AAI37505.1.
    CCDSiCCDS10195.2. [Q9H611-1]
    CCDS66797.1. [Q9H611-3]
    RefSeqiNP_001273425.1. NM_001286496.1. [Q9H611-1]
    NP_001273426.1. NM_001286497.1. [Q9H611-3]
    NP_001273428.1. NM_001286499.1. [Q9H611-4]
    NP_079325.2. NM_025049.3. [Q9H611-1]
    UniGeneiHs.112160.

    Genome annotation databases

    EnsembliENST00000268043; ENSP00000268043; ENSG00000140451. [Q9H611-1]
    ENST00000333425; ENSP00000328174; ENSG00000140451. [Q9H611-3]
    ENST00000559239; ENSP00000452792; ENSG00000140451. [Q9H611-1]
    GeneIDi80119.
    KEGGihsa:80119.
    UCSCiuc002ans.2. human. [Q9H611-1]
    uc002anu.3. human. [Q9H611-2]

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DQ437529 mRNA. Translation: ABD92708.1.
    EU084033 mRNA. Translation: ABW71293.1.
    AY498716 mRNA. Translation: AAS77398.1.
    AB185926 mRNA. Translation: BAE47454.1.
    AB185927 mRNA. Translation: BAE47455.1.
    AK026345 mRNA. Translation: BAB15456.1.
    BC137503 mRNA. Translation: AAI37504.1.
    BC137504 mRNA. Translation: AAI37505.1.
    CCDSiCCDS10195.2. [Q9H611-1]
    CCDS66797.1. [Q9H611-3]
    RefSeqiNP_001273425.1. NM_001286496.1. [Q9H611-1]
    NP_001273426.1. NM_001286497.1. [Q9H611-3]
    NP_001273428.1. NM_001286499.1. [Q9H611-4]
    NP_079325.2. NM_025049.3. [Q9H611-1]
    UniGeneiHs.112160.

    3D structure databases

    ProteinModelPortaliQ9H611.
    SMRiQ9H611. Positions 222-247.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ9H611. 1 interaction.
    STRINGi9606.ENSP00000268043.

    PTM databases

    PhosphoSiteiQ9H611.

    Polymorphism and mutation databases

    BioMutaiPIF1.
    DMDMi152031656.

    Proteomic databases

    MaxQBiQ9H611.
    PaxDbiQ9H611.
    PRIDEiQ9H611.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000268043; ENSP00000268043; ENSG00000140451. [Q9H611-1]
    ENST00000333425; ENSP00000328174; ENSG00000140451. [Q9H611-3]
    ENST00000559239; ENSP00000452792; ENSG00000140451. [Q9H611-1]
    GeneIDi80119.
    KEGGihsa:80119.
    UCSCiuc002ans.2. human. [Q9H611-1]
    uc002anu.3. human. [Q9H611-2]

    Organism-specific databases

    CTDi80119.
    GeneCardsiGC15M065107.
    H-InvDBHIX0017918.
    HGNCiHGNC:26220. PIF1.
    HPAiCAB018701.
    MIMi610953. gene.
    neXtProtiNX_Q9H611.
    PharmGKBiPA162399475.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0507.
    GeneTreeiENSGT00530000063561.
    HOGENOMiHOG000132960.
    HOVERGENiHBG106706.
    InParanoidiQ9H611.
    KOiK15255.
    OMAiGKCTVKL.
    OrthoDBiEOG7RZ5PJ.
    PhylomeDBiQ9H611.
    TreeFamiTF319207.

    Enzyme and pathway databases

    BRENDAi3.6.4.12. 2681.

    Miscellaneous databases

    GenomeRNAii80119.
    NextBioi70350.
    PROiQ9H611.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9H611.
    CleanExiHS_PIF1.
    GenevestigatoriQ9H611.

    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]
    PfamiPF02689. Herpes_Helicase. 1 hit.
    PF05970. PIF1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 3 hits.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "The human Pif1 helicase, a potential Escherichia coli RecD homologue, inhibits telomerase activity."
      Zhang D.-H., Zhou B., Huang Y., Xu L.-X., Zhou J.-Q.
      Nucleic Acids Res. 34:1393-1404(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, REGION, MUTAGENESIS OF LYS-234, SUBCELLULAR LOCATION, COFACTOR.
    2. "Biochemical analysis of human PIF1 helicase and functions of its N-terminal domain."
      Gu Y., Masuda Y., Kamiya K.
      Nucleic Acids Res. 36:6295-6308(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, PINT DOMAIN.
    3. Snow B.E., Erdmann N., Harrington L.
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Human PIF1 DNA helicase."
      Futami K., Furuichi Y., Shimamoto A.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Small intestine.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain and Testis.
    7. "Human PIF helicase is cell cycle regulated and associates with telomerase."
      Mateyak M.K., Zakian V.A.
      Cell Cycle 5:2796-2804(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TELOMERASE, INDUCTION.
    8. "Mitochondrial and nuclear localization of human Pif1 helicase."
      Futami K., Shimamoto A., Furuichi Y.
      Biol. Pharm. Bull. 30:1685-1692(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Human Pif1 helicase unwinds synthetic DNA structures resembling stalled DNA replication forks."
      George T., Wen Q., Griffiths R., Ganesh A., Meuth M., Sanders C.M.
      Nucleic Acids Res. 37:6491-6502(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING.
    11. "Human Pif1 helicase is a G-quadruplex DNA-binding protein with G-quadruplex DNA-unwinding activity."
      Sanders C.M.
      Biochem. J. 430:119-128(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN G4-UNWINDING.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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 AND TELOMERE LENGTH REGULATION.
    15. Cited for: ALTERNATIVE INITIATION (ISOFORM 4), SUBCELLULAR LOCATION (ISOFORM 4).

    Entry informationi

    Entry nameiPIF1_HUMAN
    AccessioniPrimary (citable) accession number: Q9H611
    Secondary accession number(s): B2RPL7
    , Q1W5B6, Q330H5, Q33E24
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 10, 2007
    Last modified: May 27, 2015
    This is version 96 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.