Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9H611

- PIF1_HUMAN

UniProt

Q9H611 - PIF1_HUMAN

Protein

ATP-dependent DNA helicase PIF1

Gene

PIF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (10 Jul 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.7 PublicationsUniRule annotation

    Catalytic activityi

    ATP + H2O = ADP + phosphate.1 PublicationUniRule annotation

    Cofactori

    Magnesium.1 PublicationUniRule annotation

    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

    1. ATP binding Source: HGNC
    2. ATP-dependent 5'-3' DNA/RNA helicase activity Source: BHF-UCL
    3. ATP-dependent 5'-3' DNA helicase activity Source: HGNC
    4. G-quadruplex DNA binding Source: UniProtKB-HAMAP
    5. magnesium ion binding Source: HGNC
    6. single-stranded DNA-dependent ATP-dependent DNA helicase activity Source: HGNC
    7. telomerase inhibitor activity Source: UniProtKB-HAMAP
    8. telomeric DNA binding Source: HGNC

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. DNA duplex unwinding Source: GOC
    3. DNA recombination Source: UniProtKB-HAMAP
    4. DNA repair Source: UniProtKB-HAMAP
    5. mitochondrial genome maintenance Source: UniProtKB-HAMAP
    6. negative regulation of telomerase activity Source: HGNC
    7. negative regulation of telomere maintenance via telomerase Source: UniProtKB-HAMAP
    8. regulation of telomere maintenance Source: HGNC
    9. telomere maintenance Source: InterPro

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    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: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:26220. PIF1.

    Subcellular locationi

    Nucleus 3 PublicationsUniRule annotation
    Isoform 4 : Mitochondrion 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. nuclear chromosome, telomeric region Source: HGNC

    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.

    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

    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

    ArrayExpressiQ9H611.
    BgeeiQ9H611.
    CleanExiHS_PIF1.
    GenevestigatoriQ9H611.

    Organism-specific databases

    HPAiCAB018701.

    Interactioni

    Subunit structurei

    Monomer. Interacts with telomerase.2 PublicationsUniRule annotation

    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.
    HOGENOMiHOG000132960.
    HOVERGENiHBG106706.
    KOiK15255.
    OMAiAMDSNPE.
    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. Align

    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

    MLSGIEAAAG EYEDSELRCR VAVEELSPGG QPRRRQALRT AELSLGRNER    50
    RELMLRLQAP GPAGRPRCFP LRAARLFTRF AEAGRSTLRL PAHDTPGAGA 100
    VQLLLSDCPP DRLRRFLRTL RLKLAAAPGP GPASARAQLL GPRPRDFVTI 150
    SPVQPEERRL RAATRVPDTT LVKRPVEPQA GAEPSTEAPR WPLPVKRLSL 200
    PSTKPQLSEE QAAVLRAVLK GQSIFFTGSA GTGKSYLLKR ILGSLPPTGT 250
    VATASTGVAA CHIGGTTLHA FAGIGSGQAP LAQCVALAQR PGVRQGWLNC 300
    QRLVIDEISM VEADLFDKLE AVARAVRQQN KPFGGIQLII CGDFLQLPPV 350
    TKGSQPPRFC FQSKSWKRCV PVTLELTKVW RQADQTFISL LQAVRLGRCS 400
    DEVTRQLQAT ASHKVGRDGI VATRLCTHQD DVALTNERRL QELPGKVHRF 450
    EAMDSNPELA STLDAQCPVS QLLQLKLGAQ VMLVKNLSVS RGLVNGARGV 500
    VVGFEAEGRG LPQVRFLCGV TEVIHADRWT VQATGGQLLS RQQLPLQLAW 550
    AMSIHKSQGM TLDCVEISLG RVFASGQAYV ALSRARSLQG LRVLDFDPMA 600
    VRCDPRVLHF YATLRRGRSL SLESPDDDEA ASDQENMDPI L 641
    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi152031656.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS10195.2. [Q9H611-1 ]
    CCDS66797.1. [Q9H611-3 ]
    RefSeqi NP_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 ]
    UniGenei Hs.112160.

    3D structure databases

    ProteinModelPortali Q9H611.
    SMRi Q9H611. Positions 222-247.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9H611. 1 interaction.
    STRINGi 9606.ENSP00000268043.

    PTM databases

    PhosphoSitei Q9H611.

    Polymorphism databases

    DMDMi 152031656.

    Proteomic databases

    PaxDbi Q9H611.
    PRIDEi Q9H611.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268043 ; ENSP00000268043 ; ENSG00000140451 . [Q9H611-1 ]
    ENST00000333425 ; ENSP00000328174 ; ENSG00000140451 . [Q9H611-3 ]
    ENST00000559239 ; ENSP00000452792 ; ENSG00000140451 . [Q9H611-1 ]
    GeneIDi 80119.
    KEGGi hsa:80119.
    UCSCi uc002ans.2. human. [Q9H611-1 ]
    uc002anu.3. human. [Q9H611-2 ]

    Organism-specific databases

    CTDi 80119.
    GeneCardsi GC15M065107.
    H-InvDB HIX0017918.
    HGNCi HGNC:26220. PIF1.
    HPAi CAB018701.
    MIMi 610953. gene.
    neXtProti NX_Q9H611.
    PharmGKBi PA162399475.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0507.
    HOGENOMi HOG000132960.
    HOVERGENi HBG106706.
    KOi K15255.
    OMAi AMDSNPE.
    OrthoDBi EOG7RZ5PJ.
    PhylomeDBi Q9H611.
    TreeFami TF319207.

    Miscellaneous databases

    GenomeRNAii 80119.
    NextBioi 70350.
    PROi Q9H611.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H611.
    Bgeei Q9H611.
    CleanExi HS_PIF1.
    Genevestigatori Q9H611.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 hits.
    HAMAPi MF_03176. PIF1.
    InterProi IPR003840. DNA_helicase.
    IPR010285. DNA_helicase_pif1_like.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF02689. Herpes_Helicase. 1 hit.
    PF05970. PIF1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 89 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