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Q9H611

- PIF1_HUMAN

UniProt

Q9H611 - PIF1_HUMAN

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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

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
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

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-HAMAP
  2. 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.

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.2 PublicationsUniRule annotation

Protein-protein interaction databases

IntActiQ9H611. 1 interaction.
STRINGi9606.ENSP00000268043.

Structurei

3D structure databases

ProteinModelPortaliQ9H611.
SMRiQ9H611. Positions 205-260.
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.
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

        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:
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 205-260.
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

MaxQBi Q9H611.
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.
GeneTreei ENSGT00530000063561.
HOGENOMi HOG000132960.
HOVERGENi HBG106706.
InParanoidi Q9H611.
KOi K15255.
OMAi AMDSNPE.
OrthoDBi EOG7RZ5PJ.
PhylomeDBi Q9H611.
TreeFami TF319207.

Miscellaneous databases

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

Gene expression databases

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

« 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: October 29, 2014
This is version 90 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