Q9H611 (PIF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent DNA helicase PIF1
EC=3.6.4.12

Alternative name(s):
PIF1/RRM3 DNA helicase-like protein

Gene names

Name:	PIF1
Synonyms:	C15orf20

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	641 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA-dependent ATPase and DNA helicase inhibiting telomerase activity by unwinding DNA/RNA duplex formed by telomerase RNA and telomeric DNA in a 5' to 3' polarity. Negatively regulates telomere length and such inhibition requires its ATPase activity. Tightly cell cycle regulated and expressed in late S/G2 phase. Ref.1 Ref.5
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Interacts with telomerase. Ref.5
Subcellular location	Nucleus Ref.1 Ref.5.
Tissue specificity	Weak ubiquitous expression.
Sequence similarities	Belongs to the helicase family.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of telomerase activity Inferred from direct assay Ref.1. Source: HGNC regulation of telomere maintenance Inferred from direct assay Ref.1. Source: HGNC
Cellular_component	nuclear chromosome, telomeric region Inferred from direct assay Ref.1. Source: HGNC
Molecular_function	ATP binding Inferred from direct assay Ref.1. Source: HGNC ATP-dependent 5'-3' DNA helicase activity Inferred from direct assay Ref.1. Source: HGNC ATP-dependent 5'-3' DNA/RNA helicase activity Inferred from direct assay Ref.1. Source: BHF-UCL magnesium ion binding Inferred from direct assay Ref.1. Source: HGNC single-stranded DNA-dependent ATP-dependent DNA helicase activity Inferred from direct assay Ref.1. Source: HGNC telomeric DNA binding Inferred from direct assay Ref.1. Source: HGNC
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H611-1)

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.

Isoform 2 (identifier: Q9H611-2)

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

Isoform 3 (identifier: Q9H611-3)

Also known as: Isoform beta;

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 641	641	ATP-dependent DNA helicase PIF1		PRO_0000089980
Regions
	Nucleotide binding	228 – 235	8	ATP Potential
	Region	167 – 641	475	Hydrolyzes ATP in the presence of both magnesium and single-stranded DNA; weak activity in the presence of RNA or double-stranded DNA; No unwinding activity
Amino acid modifications
	Modified residue	27	1	Phosphoserine Ref.7
	Modified residue	151	1	Phosphoserine Ref.6 Ref.7 Ref.8
Natural variations
	Alternative sequence	232 – 266	35	TGKSY…HIGGT → SGGREEVGGQWWGGIEEQGD LSNFAPVQEQGSHIC in isoform 2.		VSP_026715
	Alternative sequence	267 – 641	375	Missing in isoform 2.		VSP_026716
	Alternative sequence	623 – 641	19	ESPDD…MDPIL → AAEGRGNEDRCSGSSIRALG GDWWGLRLGAASKQRTELRC VSTARPSLAQPRTNTLQSLT KEHKLQNVHPYFKLLFQGIN SVWGH in isoform 3.		VSP_026717
	Natural variant	640	1	I → N. Corresponds to variant rs17802279 [ dbSNP | Ensembl ].		VAR_033206
Experimental info
	Mutagenesis	234	1	K → A: Loss of ATPase activity. Lower activity for single-stranded DNA. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Isoform alpha) [UniParc]. Last modified July 10, 2007. Version 2. Checksum: D755470008BA3CA8	FASTA	641	69,799
	10 20 30 40 50 60 MLSGIEAAAG EYEDSELRCR VAVEELSPGG QPRRRQALRT AELSLGRNER RELMLRLQAP 70 80 90 100 110 120 GPAGRPRCFP LRAARLFTRF AEAGRSTLRL PAHDTPGAGA VQLLLSDCPP DRLRRFLRTL 130 140 150 160 170 180 RLKLAAAPGP GPASARAQLL GPRPRDFVTI SPVQPEERRL RAATRVPDTT LVKRPVEPQA 190 200 210 220 230 240 GAEPSTEAPR WPLPVKRLSL PSTKPQLSEE QAAVLRAVLK GQSIFFTGSA GTGKSYLLKR 250 260 270 280 290 300 ILGSLPPTGT VATASTGVAA CHIGGTTLHA FAGIGSGQAP LAQCVALAQR PGVRQGWLNC 310 320 330 340 350 360 QRLVIDEISM VEADLFDKLE AVARAVRQQN KPFGGIQLII CGDFLQLPPV TKGSQPPRFC 370 380 390 400 410 420 FQSKSWKRCV PVTLELTKVW RQADQTFISL LQAVRLGRCS DEVTRQLQAT ASHKVGRDGI 430 440 450 460 470 480 VATRLCTHQD DVALTNERRL QELPGKVHRF EAMDSNPELA STLDAQCPVS QLLQLKLGAQ 490 500 510 520 530 540 VMLVKNLSVS RGLVNGARGV VVGFEAEGRG LPQVRFLCGV TEVIHADRWT VQATGGQLLS 550 560 570 580 590 600 RQQLPLQLAW AMSIHKSQGM TLDCVEISLG RVFASGQAYV ALSRARSLQG LRVLDFDPMA 610 620 630 640 VRCDPRVLHF YATLRRGRSL SLESPDDDEA ASDQENMDPI L
	Isoform 2 [UniParc]. Checksum: 0A291FB7E1339D56	FASTA	266	28,907
	10 20 30 40 50 60 MLSGIEAAAG EYEDSELRCR VAVEELSPGG QPRRRQALRT AELSLGRNER RELMLRLQAP 70 80 90 100 110 120 GPAGRPRCFP LRAARLFTRF AEAGRSTLRL PAHDTPGAGA VQLLLSDCPP DRLRRFLRTL 130 140 150 160 170 180 RLKLAAAPGP GPASARAQLL GPRPRDFVTI SPVQPEERRL RAATRVPDTT LVKRPVEPQA 190 200 210 220 230 240 GAEPSTEAPR WPLPVKRLSL PSTKPQLSEE QAAVLRAVLK GQSIFFTGSA GSGGREEVGG 250 260 QWWGGIEEQG DLSNFAPVQE QGSHIC
	Isoform 3 (Isoform beta) [UniParc]. Checksum: DA015E47D50F8541	FASTA	707	77,125
	10 20 30 40 50 60 MLSGIEAAAG EYEDSELRCR VAVEELSPGG QPRRRQALRT AELSLGRNER RELMLRLQAP 70 80 90 100 110 120 GPAGRPRCFP LRAARLFTRF AEAGRSTLRL PAHDTPGAGA VQLLLSDCPP DRLRRFLRTL 130 140 150 160 170 180 RLKLAAAPGP GPASARAQLL GPRPRDFVTI SPVQPEERRL RAATRVPDTT LVKRPVEPQA 190 200 210 220 230 240 GAEPSTEAPR WPLPVKRLSL PSTKPQLSEE QAAVLRAVLK GQSIFFTGSA GTGKSYLLKR 250 260 270 280 290 300 ILGSLPPTGT VATASTGVAA CHIGGTTLHA FAGIGSGQAP LAQCVALAQR PGVRQGWLNC 310 320 330 340 350 360 QRLVIDEISM VEADLFDKLE AVARAVRQQN KPFGGIQLII CGDFLQLPPV TKGSQPPRFC 370 380 390 400 410 420 FQSKSWKRCV PVTLELTKVW RQADQTFISL LQAVRLGRCS DEVTRQLQAT ASHKVGRDGI 430 440 450 460 470 480 VATRLCTHQD DVALTNERRL QELPGKVHRF EAMDSNPELA STLDAQCPVS QLLQLKLGAQ 490 500 510 520 530 540 VMLVKNLSVS RGLVNGARGV VVGFEAEGRG LPQVRFLCGV TEVIHADRWT VQATGGQLLS 550 560 570 580 590 600 RQQLPLQLAW AMSIHKSQGM TLDCVEISLG RVFASGQAYV ALSRARSLQG LRVLDFDPMA 610 620 630 640 650 660 VRCDPRVLHF YATLRRGRSL SLAAEGRGNE DRCSGSSIRA LGGDWWGLRL GAASKQRTEL 670 680 690 700 RCVSTARPSL AQPRTNTLQS LTKEHKLQNV HPYFKLLFQG INSVWGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
[2]	Snow B.E., Erdmann N., Harrington L. Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"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).
[4]	"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.
[5]	"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.
[6]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ437529 mRNA. Translation: ABD92708.1. AY498716 mRNA. Translation: AAS77398.1. AB185926 mRNA. Translation: BAE47454.1. AB185927 mRNA. Translation: BAE47455.1. AK026345 mRNA. Translation: BAB15456.1.
IPI	IPI00017925. IPI00746514. IPI00793711.
RefSeq	NP_079325.2. NM_025049.2.
UniGene	Hs.112160.
3D structure databases
ProteinModelPortal	Q9H611.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000268043.
PTM databases
PhosphoSite	Q9H611.
Polymorphism databases
DMDM	152031656.
Proteomic databases
PaxDb	Q9H611.
PRIDE	Q9H611.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000268043; ENSP00000268043; ENSG00000140451. ENST00000333425; ENSP00000328174; ENSG00000140451. ENST00000559239; ENSP00000452792; ENSG00000140451.
GeneID	80119.
KEGG	hsa:80119.
UCSC	uc002ans.2. human. uc002anu.3. human.
Organism-specific databases
CTD	80119.
GeneCards	GC15M065107.
H-InvDB	HIX0017918.
HGNC	HGNC:26220. PIF1.
HPA	CAB018701.
MIM	610953. gene.
neXtProt	NX_Q9H611.
PharmGKB	PA162399475.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0507.
HOGENOM	HOG000132960.
HOVERGEN	HBG106706.
KO	K15255.
OMA	TEAPRWP.
OrthoDB	EOG4S4PFR.
Gene expression databases
ArrayExpress	Q9H611.
Bgee	Q9H611.
CleanEx	HS_PIF1.
Genevestigator	Q9H611.
GermOnline	ENSG00000140451. Homo sapiens.
Family and domain databases
InterPro	IPR003840. DNA_helicase. IPR010285. DNA_helicase_PIF1. [Graphical view]
Pfam	PF02689. Herpes_Helicase. 1 hit. PF05970. PIF1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	80119.
NextBio	70350.
SOURCE	Search...

Entry information

Entry name

PIF1_HUMAN

Accession

Primary (citable) accession number: Q9H611
Secondary accession number(s): Q1W5B6, Q330H5, Q33E24

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 10, 2007
Last modified:	May 1, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.