PIF1_HUMAN
ID PIF1_HUMAN Reviewed; 641 AA.
AC Q9H611; B2RPL7; Q1W5B6; Q330H5; Q33E24;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ATP-dependent DNA helicase PIF1 {ECO:0000255|HAMAP-Rule:MF_03176};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03176};
DE AltName: Full=DNA repair and recombination helicase PIF1 {ECO:0000255|HAMAP-Rule:MF_03176};
DE AltName: Full=PIF1/RRM3 DNA helicase-like protein;
GN Name=PIF1 {ECO:0000255|HAMAP-Rule:MF_03176}; Synonyms=C15orf20;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, REGION, MUTAGENESIS OF
RP LYS-234, SUBCELLULAR LOCATION, AND COFACTOR.
RX PubMed=16522649; DOI=10.1093/nar/gkl029;
RA Zhang D.-H., Zhou B., Huang Y., Xu L.-X., Zhou J.-Q.;
RT "The human Pif1 helicase, a potential Escherichia coli RecD homologue,
RT inhibits telomerase activity.";
RL Nucleic Acids Res. 34:1393-1404(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PINT DOMAIN.
RX PubMed=18835853; DOI=10.1093/nar/gkn609;
RA Gu Y., Masuda Y., Kamiya K.;
RT "Biochemical analysis of human PIF1 helicase and functions of its N-
RT terminal domain.";
RL Nucleic Acids Res. 36:6295-6308(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Snow B.E., Erdmann N., Harrington L.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RA Futami K., Furuichi Y., Shimamoto A.;
RT "Human PIF1 DNA helicase.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TELOMERASE, AND INDUCTION.
RX PubMed=17172855; DOI=10.4161/cc.5.23.3524;
RA Mateyak M.K., Zakian V.A.;
RT "Human PIF helicase is cell cycle regulated and associates with
RT telomerase.";
RL Cell Cycle 5:2796-2804(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY.
RX PubMed=17827721; DOI=10.1248/bpb.30.1685;
RA Futami K., Shimamoto A., Furuichi Y.;
RT "Mitochondrial and nuclear localization of human Pif1 helicase.";
RL Biol. Pharm. Bull. 30:1685-1692(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=19700773; DOI=10.1093/nar/gkp671;
RA George T., Wen Q., Griffiths R., Ganesh A., Meuth M., Sanders C.M.;
RT "Human Pif1 helicase unwinds synthetic DNA structures resembling stalled
RT DNA replication forks.";
RL Nucleic Acids Res. 37:6491-6502(2009).
RN [11]
RP FUNCTION IN G4-UNWINDING.
RX PubMed=20524933; DOI=10.1042/bj20100612;
RA Sanders C.M.;
RT "Human Pif1 helicase is a G-quadruplex DNA-binding protein with G-
RT quadruplex DNA-unwinding activity.";
RL Biochem. J. 430:119-128(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-151, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-151, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP FUNCTION IN G4-UNWINDING AND TELOMERE LENGTH REGULATION.
RX PubMed=23657261; DOI=10.1038/nature12149;
RA Paeschke K., Bochman M.L., Garcia P.D., Cejka P., Friedman K.L.,
RA Kowalczykowski S.C., Zakian V.A.;
RT "Pif1 family helicases suppress genome instability at G-quadruplex
RT motifs.";
RL Nature 497:458-462(2013).
RN [16]
RP ALTERNATIVE INITIATION (ISOFORM 4), AND SUBCELLULAR LOCATION (ISOFORM 4).
RX PubMed=23275553; DOI=10.1093/nar/gks1347;
RA Kazak L., Reyes A., Duncan A.L., Rorbach J., Wood S.R., Brea-Calvo G.,
RA Gammage P.A., Robinson A.J., Minczuk M., Holt I.J.;
RT "Alternative translation initiation augments the human mitochondrial
RT proteome.";
RL Nucleic Acids Res. 41:2354-2369(2013).
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the
CC maintenance of both mitochondrial and nuclear genome stability.
CC Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA
CC hybrids. Resolves G4 structures, preventing replication pausing and
CC double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance
CC of telomeric DNA. Inhibits telomere elongation, de novo telomere
CC formation and telomere addition to DSBs via catalytic inhibition of
CC telomerase. Reduces the processivity of telomerase by displacing active
CC telomerase from DNA ends. Releases telomerase by unwinding the short
CC telomerase RNA/telomeric DNA hybrid that is the intermediate in the
CC telomerase reaction. Possesses an intrinsic strand annealing activity.
CC {ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:16522649,
CC ECO:0000269|PubMed:17172855, ECO:0000269|PubMed:17827721,
CC ECO:0000269|PubMed:18835853, ECO:0000269|PubMed:19700773,
CC ECO:0000269|PubMed:20524933, ECO:0000269|PubMed:23657261}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03176,
CC ECO:0000269|PubMed:17827721};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03176,
CC ECO:0000269|PubMed:16522649};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.17 mM for ATP {ECO:0000269|PubMed:18835853};
CC -!- SUBUNIT: Monomer. Interacts with telomerase. {ECO:0000255|HAMAP-
CC Rule:MF_03176, ECO:0000269|PubMed:17172855,
CC ECO:0000269|PubMed:18835853}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03176,
CC ECO:0000269|PubMed:16522649, ECO:0000269|PubMed:17172855,
CC ECO:0000269|PubMed:17827721}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Mitochondrion {ECO:0000255|HAMAP-
CC Rule:MF_03176, ECO:0000269|PubMed:23275553}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=1; Synonyms=Isoform alpha;
CC IsoId=Q9H611-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H611-2; Sequence=VSP_026715, VSP_026716;
CC Name=3; Synonyms=Isoform beta;
CC IsoId=Q9H611-3; Sequence=VSP_026717;
CC Name=4;
CC IsoId=Q9H611-4; Sequence=VSP_047457;
CC -!- TISSUE SPECIFICITY: Weak ubiquitous expression.
CC -!- INDUCTION: Tightly cell cycle regulated and expressed in late S/G2
CC phase. {ECO:0000269|PubMed:17172855}.
CC -!- DOMAIN: The PIF1 N-terminal (PINT) domain enhances the interaction with
CC ssDNA through intrinsic binding activity, it also harbors DNA strand-
CC annealing activity.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative initiation of
CC isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03176}.
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DR EMBL; DQ437529; ABD92708.1; -; mRNA.
DR EMBL; EU084033; ABW71293.1; -; mRNA.
DR EMBL; AY498716; AAS77398.1; -; mRNA.
DR EMBL; AB185926; BAE47454.1; -; mRNA.
DR EMBL; AB185927; BAE47455.1; -; mRNA.
DR EMBL; AK026345; BAB15456.1; -; mRNA.
DR EMBL; BC137503; AAI37504.1; -; mRNA.
DR EMBL; BC137504; AAI37505.1; -; mRNA.
DR CCDS; CCDS10195.2; -. [Q9H611-1]
DR CCDS; CCDS66797.1; -. [Q9H611-3]
DR RefSeq; NP_001273425.1; NM_001286496.1. [Q9H611-1]
DR RefSeq; NP_001273426.1; NM_001286497.1. [Q9H611-3]
DR RefSeq; NP_001273428.1; NM_001286499.1. [Q9H611-4]
DR RefSeq; NP_079325.2; NM_025049.3. [Q9H611-1]
DR RefSeq; XP_011520385.1; XM_011522083.2. [Q9H611-1]
DR RefSeq; XP_011520386.1; XM_011522084.2. [Q9H611-1]
DR PDB; 5FHH; X-ray; 3.60 A; A/B=200-641.
DR PDB; 6HPH; X-ray; 1.13 A; A=206-620.
DR PDB; 6HPQ; X-ray; 1.43 A; A/B=206-620.
DR PDB; 6HPT; X-ray; 1.44 A; A=206-641.
DR PDB; 6HPU; X-ray; 3.96 A; A/B=206-620.
DR PDBsum; 5FHH; -.
DR PDBsum; 6HPH; -.
DR PDBsum; 6HPQ; -.
DR PDBsum; 6HPT; -.
DR PDBsum; 6HPU; -.
DR AlphaFoldDB; Q9H611; -.
DR SMR; Q9H611; -.
DR BioGRID; 123122; 20.
DR IntAct; Q9H611; 2.
DR STRING; 9606.ENSP00000328174; -.
DR iPTMnet; Q9H611; -.
DR PhosphoSitePlus; Q9H611; -.
DR BioMuta; PIF1; -.
DR DMDM; 152031656; -.
DR EPD; Q9H611; -.
DR jPOST; Q9H611; -.
DR MassIVE; Q9H611; -.
DR MaxQB; Q9H611; -.
DR PaxDb; Q9H611; -.
DR PeptideAtlas; Q9H611; -.
DR PRIDE; Q9H611; -.
DR ProteomicsDB; 80948; -. [Q9H611-1]
DR ProteomicsDB; 80949; -. [Q9H611-2]
DR ProteomicsDB; 80950; -. [Q9H611-3]
DR Antibodypedia; 4360; 124 antibodies from 23 providers.
DR DNASU; 80119; -.
DR Ensembl; ENST00000268043.8; ENSP00000268043.4; ENSG00000140451.13. [Q9H611-1]
DR Ensembl; ENST00000333425.10; ENSP00000328174.6; ENSG00000140451.13. [Q9H611-3]
DR Ensembl; ENST00000559239.2; ENSP00000452792.1; ENSG00000140451.13. [Q9H611-1]
DR GeneID; 80119; -.
DR KEGG; hsa:80119; -.
DR MANE-Select; ENST00000559239.2; ENSP00000452792.1; NM_001286496.2; NP_001273425.1.
DR UCSC; uc002ant.4; human. [Q9H611-1]
DR CTD; 80119; -.
DR DisGeNET; 80119; -.
DR GeneCards; PIF1; -.
DR HGNC; HGNC:26220; PIF1.
DR HPA; ENSG00000140451; Tissue enhanced (lymphoid).
DR MIM; 610953; gene.
DR neXtProt; NX_Q9H611; -.
DR OpenTargets; ENSG00000140451; -.
DR PharmGKB; PA162399475; -.
DR VEuPathDB; HostDB:ENSG00000140451; -.
DR eggNOG; KOG0987; Eukaryota.
DR GeneTree; ENSGT00530000063561; -.
DR HOGENOM; CLU_001613_7_1_1; -.
DR InParanoid; Q9H611; -.
DR OMA; ITLHQFA; -.
DR OrthoDB; 931726at2759; -.
DR PhylomeDB; Q9H611; -.
DR TreeFam; TF319207; -.
DR BRENDA; 3.6.4.12; 2681.
DR PathwayCommons; Q9H611; -.
DR Reactome; R-HSA-171319; Telomere Extension By Telomerase.
DR SABIO-RK; Q9H611; -.
DR SignaLink; Q9H611; -.
DR BioGRID-ORCS; 80119; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; PIF1; human.
DR GenomeRNAi; 80119; -.
DR Pharos; Q9H611; Tbio.
DR PRO; PR:Q9H611; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9H611; protein.
DR Bgee; ENSG00000140451; Expressed in ventricular zone and 99 other tissues.
DR Genevisible; Q9H611; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:HGNC-UCL.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005657; C:replication fork; IBA:GO_Central.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IDA:HGNC-UCL.
DR GO; GO:0033678; F:5'-3' DNA/RNA helicase activity; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IDA:HGNC-UCL.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IDA:HGNC-UCL.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:HGNC-UCL.
DR GO; GO:0010521; F:telomerase inhibitor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:HGNC-UCL.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IBA:GO_Central.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0051974; P:negative regulation of telomerase activity; IDA:HGNC-UCL.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IDA:BHF-UCL.
DR GO; GO:0032204; P:regulation of telomere maintenance; IDA:HGNC-UCL.
DR GO; GO:0007004; P:telomere maintenance via telomerase; TAS:Reactome.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_03176; PIF1; 1.
DR InterPro; IPR003840; DNA_helicase.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02689; Herpes_Helicase; 1.
DR Pfam; PF05970; PIF1; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; ATP-binding;
KW DNA damage; DNA recombination; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..641
FT /note="ATP-dependent DNA helicase PIF1"
FT /id="PRO_0000089980"
FT DNA_BIND 577..596
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT REGION 1..180
FT /note="PINT"
FT REGION 167..641
FT /note="Hydrolyzes ATP in the presence of both magnesium and
FT single-stranded DNA; weak activity in the presence of RNA
FT or double-stranded DNA; No unwinding activity"
FT REGION 173..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 228..235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03176"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047457"
FT VAR_SEQ 232..266
FT /note="TGKSYLLKRILGSLPPTGTVATASTGVAACHIGGT -> SGGREEVGGQWWG
FT GIEEQGDLSNFAPVQEQGSHIC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026715"
FT VAR_SEQ 267..641
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026716"
FT VAR_SEQ 623..641
FT /note="ESPDDDEAASDQENMDPIL -> AAEGRGNEDRCSGSSIRALGGDWWGLRLG
FT AASKQRTELRCVSTARPSLAQPRTNTLQSLTKEHKLQNVHPYFKLLFQGINSVWGH
FT (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_026717"
FT VARIANT 640
FT /note="I -> N (in dbSNP:rs17802279)"
FT /id="VAR_033206"
FT MUTAGEN 234
FT /note="K->A: Loss of ATPase activity. Lower activity for
FT single-stranded DNA."
FT /evidence="ECO:0000269|PubMed:16522649"
FT HELIX 209..219
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 257..262
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 281..288
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 293..299
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 313..327
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 332..335
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 385..395
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 401..409
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 429..442
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 448..451
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 460..466
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 471..475
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 480..483
FT /evidence="ECO:0007829|PDB:6HPH"
FT TURN 489..492
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 498..504
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 527..532
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 534..536
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 538..543
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 562..568
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 577..583
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:6HPH"
FT STRAND 591..595
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 598..600
FT /evidence="ECO:0007829|PDB:6HPH"
FT HELIX 605..614
FT /evidence="ECO:0007829|PDB:6HPH"
FT TURN 615..617
FT /evidence="ECO:0007829|PDB:6HPH"
SQ SEQUENCE 641 AA; 69799 MW; D755470008BA3CA8 CRC64;
MLSGIEAAAG EYEDSELRCR VAVEELSPGG QPRRRQALRT AELSLGRNER RELMLRLQAP
GPAGRPRCFP LRAARLFTRF AEAGRSTLRL PAHDTPGAGA VQLLLSDCPP DRLRRFLRTL
RLKLAAAPGP GPASARAQLL GPRPRDFVTI SPVQPEERRL RAATRVPDTT LVKRPVEPQA
GAEPSTEAPR WPLPVKRLSL PSTKPQLSEE QAAVLRAVLK GQSIFFTGSA GTGKSYLLKR
ILGSLPPTGT VATASTGVAA CHIGGTTLHA FAGIGSGQAP LAQCVALAQR PGVRQGWLNC
QRLVIDEISM VEADLFDKLE AVARAVRQQN KPFGGIQLII CGDFLQLPPV TKGSQPPRFC
FQSKSWKRCV PVTLELTKVW RQADQTFISL LQAVRLGRCS DEVTRQLQAT ASHKVGRDGI
VATRLCTHQD DVALTNERRL QELPGKVHRF EAMDSNPELA STLDAQCPVS QLLQLKLGAQ
VMLVKNLSVS RGLVNGARGV VVGFEAEGRG LPQVRFLCGV TEVIHADRWT VQATGGQLLS
RQQLPLQLAW AMSIHKSQGM TLDCVEISLG RVFASGQAYV ALSRARSLQG LRVLDFDPMA
VRCDPRVLHF YATLRRGRSL SLESPDDDEA ASDQENMDPI L
