HELQ_HUMAN
ID HELQ_HUMAN Reviewed; 1101 AA.
AC Q8TDG4; Q05DF9; Q502W9; Q659B8; Q6ZQX4; Q6ZTS4; Q96EX7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Helicase POLQ-like {ECO:0000305|PubMed:11751861};
DE EC=3.6.4.12 {ECO:0000269|PubMed:11751861, ECO:0000269|PubMed:34316696, ECO:0000269|PubMed:34937945};
DE AltName: Full=Mus308-like helicase {ECO:0000303|PubMed:11751861};
DE AltName: Full=POLQ-like helicase {ECO:0000303|PubMed:11751861};
GN Name=HELQ {ECO:0000303|PubMed:24005041, ECO:0000312|HGNC:HGNC:18536};
GN Synonyms=HEL308 {ECO:0000303|PubMed:11751861};
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, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, MUTAGENESIS OF LYS-365, AND VARIANT GLU-35.
RX PubMed=11751861; DOI=10.1074/jbc.m110271200;
RA Marini F., Wood R.D.;
RT "A human DNA helicase homologous to the DNA cross-link sensitivity protein
RT Mus308.";
RL J. Biol. Chem. 277:8716-8723(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Liver, and Uterus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND VARIANT
RP GLU-35.
RC TISSUE=Chondrosarcoma, and Duodenum;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 391-522 (ISOFORM 1).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, AND INTERACTION WITH POLN.
RX PubMed=19995904; DOI=10.1128/mcb.01124-09;
RA Moldovan G.L., Madhavan M.V., Mirchandani K.D., McCaffrey R.M.,
RA Vinciguerra P., D'Andrea A.D.;
RT "DNA polymerase POLN participates in cross-link repair and homologous
RT recombination.";
RL Mol. Cell. Biol. 30:1088-1096(2010).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21398521; DOI=10.1074/jbc.m111.228189;
RA Tafel A.A., Wu L., McHugh P.J.;
RT "Human HEL308 localizes to damaged replication forks and unwinds lagging
RT strand structures.";
RL J. Biol. Chem. 286:15832-15840(2011).
RN [8]
RP FUNCTION, AND INTERACTION WITH RAD51B AND RAD51C.
RX PubMed=24005041; DOI=10.1093/nar/gkt676;
RA Luebben S.W., Kawabata T., Akre M.K., Lee W.L., Johnson C.S.,
RA O'Sullivan M.G., Shima N.;
RT "Helq acts in parallel to Fancc to suppress replication-associated genome
RT instability.";
RL Nucleic Acids Res. 41:10283-10297(2013).
RN [9]
RP FUNCTION.
RX PubMed=24005565; DOI=10.1038/ncomms3338;
RA Takata K., Reh S., Tomida J., Person M.D., Wood R.D.;
RT "Human DNA helicase HELQ participates in DNA interstrand crosslink
RT tolerance with ATR and RAD51 paralogs.";
RL Nat. Commun. 4:2338-2338(2013).
RN [10]
RP MUTAGENESIS OF 818-TYR-LYS-819.
RX PubMed=28738244; DOI=10.1016/j.dnarep.2017.07.005;
RA Northall S.J., Buckley R., Jones N., Penedo J.C., Soultanas P., Bolt E.L.;
RT "DNA binding and unwinding by Hel308 helicase requires dual functions of a
RT winged helix domain.";
RL DNA Repair 57:125-132(2017).
RN [11]
RP FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, INTERACTION WITH THE RPA COMPLEX,
RP AND MUTAGENESIS OF ASP-463.
RX PubMed=34316696; DOI=10.1093/narcan/zcaa043;
RA Jenkins T., Northall S.J., Ptchelkine D., Lever R., Cubbon A., Betts H.,
RA Taresco V., Cooper C.D.O., McHugh P.J., Soultanas P., Bolt E.L.;
RT "The HelQ human DNA repair helicase utilizes a PWI-like domain for DNA
RT loading through interaction with RPA, triggering DNA unwinding by the HelQ
RT helicase core.";
RL NAR Cancer 3:zcaa043-zcaa043(2021).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH RAD51
RP AND THE RPA COMPLEX, AND MUTAGENESIS OF LYS-365.
RX PubMed=34937945; DOI=10.1038/s41586-021-04261-0;
RA Anand R., Buechelmaier E., Belan O., Newton M., Vancevska A.,
RA Kaczmarczyk A., Takaki T., Rueda D.S., Powell S.N., Boulton S.J.;
RT "HELQ is a dual-function DSB repair enzyme modulated by RPA and RAD51.";
RL Nature 601:268-273(2022).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-565.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Single-stranded 3'-5' DNA helicase that plays a key role in
CC homology-driven double-strand break (DSB) repair (PubMed:11751861,
CC PubMed:19995904, PubMed:21398521, PubMed:24005041, PubMed:24005565,
CC PubMed:34316696, PubMed:34937945). Involved in different DSB repair
CC mechanisms that are guided by annealing of extensive stretches of
CC complementary bases at break ends, such as microhomology-mediated end-
CC joining (MMEJ), single-strand annealing (SSA) or synthesis-dependent
CC strand annealing (SDSA) (PubMed:34937945). Possesses both DNA unwinding
CC and annealing activities (PubMed:34937945). Forms a complex with RAD51,
CC stimulating HELQ DNA helicase activity and ability to unwing DNA
CC (PubMed:34937945). Efficiently unwinds substrates containing 3'
CC overhangs or a D-loop (PubMed:21398521, PubMed:34937945). In contrast,
CC interaction with the replication protein A (RPA/RP-A) complex inhibits
CC DNA unwinding by HELQ but strongly stimulates DNA strand annealing
CC (PubMed:34937945). Triggers displacement of RPA from single-stranded
CC DNA to facilitate annealing of complementary sequences
CC (PubMed:34316696, PubMed:34937945). {ECO:0000269|PubMed:11751861,
CC ECO:0000269|PubMed:19995904, ECO:0000269|PubMed:21398521,
CC ECO:0000269|PubMed:24005041, ECO:0000269|PubMed:24005565,
CC ECO:0000269|PubMed:34316696, ECO:0000269|PubMed:34937945}.
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:0000269|PubMed:11751861, ECO:0000269|PubMed:34316696,
CC ECO:0000269|PubMed:34937945};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000269|PubMed:34316696, ECO:0000269|PubMed:34937945,
CC ECO:0000305|PubMed:11751861};
CC -!- ACTIVITY REGULATION: ATPase activity is strongly stimulated by single-
CC stranded DNA (PubMed:11751861). Presence of ATP and Mg cofactor are
CC required for helicase activity allowing to unwind duplex
CC oligonucleotides up to 60-70-mer (PubMed:11751861). This helicase
CC activity is stimulated by replication protein A (RPA/RP-A) complex that
CC binds to unwound regions and inhibits re-annealing (PubMed:11751861).
CC {ECO:0000269|PubMed:11751861}.
CC -!- SUBUNIT: Homodimer (PubMed:34316696). Interacts with POLN
CC (PubMed:19995904). Interacts with RAD51B and RAD51C; promoting
CC association with the BCDX2 complex (PubMed:24005041). Interacts with
CC the replication protein A (RPA/RP-A) complex (PubMed:34316696,
CC PubMed:34937945). Interacts with RAD51; stimulating HELQ DNA helicase
CC activity and ability to unwing DNA (PubMed:34937945).
CC {ECO:0000269|PubMed:19995904, ECO:0000269|PubMed:24005041,
CC ECO:0000269|PubMed:34316696, ECO:0000269|PubMed:34937945}.
CC -!- INTERACTION:
CC Q8TDG4; O43502: RAD51C; NbExp=6; IntAct=EBI-2802156, EBI-2267048;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21398521}. Chromosome
CC {ECO:0000269|PubMed:21398521, ECO:0000269|PubMed:34937945}.
CC Note=Localizes to sites of DNA damage; localizes to damaged replication
CC forks. {ECO:0000269|PubMed:21398521, ECO:0000269|PubMed:34937945}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8TDG4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TDG4-2; Sequence=VSP_032942, VSP_032947, VSP_032948;
CC Name=3;
CC IsoId=Q8TDG4-4; Sequence=VSP_032941, VSP_032947, VSP_032948;
CC Name=4;
CC IsoId=Q8TDG4-5; Sequence=VSP_032943, VSP_032944;
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF436845; AAL85274.1; -; mRNA.
DR EMBL; AK128665; BAC87559.1; -; mRNA.
DR EMBL; AC096768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015428; AAH15428.1; -; mRNA.
DR EMBL; BC095473; AAH95473.1; -; mRNA.
DR EMBL; AL512702; CAH56359.1; -; mRNA.
DR CCDS; CCDS3603.1; -. [Q8TDG4-1]
DR RefSeq; NP_001284687.1; NM_001297758.1. [Q8TDG4-2]
DR RefSeq; NP_001284688.1; NM_001297759.1.
DR RefSeq; NP_598375.2; NM_133636.3. [Q8TDG4-1]
DR AlphaFoldDB; Q8TDG4; -.
DR SMR; Q8TDG4; -.
DR BioGRID; 125250; 15.
DR DIP; DIP-60603N; -.
DR IntAct; Q8TDG4; 12.
DR MINT; Q8TDG4; -.
DR STRING; 9606.ENSP00000295488; -.
DR GlyConnect; 2045; 3 N-Linked glycans (1 site).
DR GlyGen; Q8TDG4; 2 sites, 6 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q8TDG4; -.
DR PhosphoSitePlus; Q8TDG4; -.
DR BioMuta; HELQ; -.
DR DMDM; 296434521; -.
DR EPD; Q8TDG4; -.
DR jPOST; Q8TDG4; -.
DR MassIVE; Q8TDG4; -.
DR MaxQB; Q8TDG4; -.
DR PaxDb; Q8TDG4; -.
DR PeptideAtlas; Q8TDG4; -.
DR PRIDE; Q8TDG4; -.
DR ProteomicsDB; 74283; -. [Q8TDG4-1]
DR ProteomicsDB; 74284; -. [Q8TDG4-2]
DR ProteomicsDB; 74285; -. [Q8TDG4-4]
DR ProteomicsDB; 74286; -. [Q8TDG4-5]
DR Antibodypedia; 25213; 61 antibodies from 16 providers.
DR DNASU; 113510; -.
DR Ensembl; ENST00000295488.8; ENSP00000295488.3; ENSG00000163312.11. [Q8TDG4-1]
DR GeneID; 113510; -.
DR KEGG; hsa:113510; -.
DR MANE-Select; ENST00000295488.8; ENSP00000295488.3; NM_133636.5; NP_598375.3.
DR UCSC; uc003hom.4; human. [Q8TDG4-1]
DR CTD; 113510; -.
DR DisGeNET; 113510; -.
DR GeneCards; HELQ; -.
DR HGNC; HGNC:18536; HELQ.
DR HPA; ENSG00000163312; Low tissue specificity.
DR MIM; 606769; gene.
DR neXtProt; NX_Q8TDG4; -.
DR OpenTargets; ENSG00000163312; -.
DR PharmGKB; PA164720529; -.
DR VEuPathDB; HostDB:ENSG00000163312; -.
DR eggNOG; KOG0950; Eukaryota.
DR GeneTree; ENSGT00940000157350; -.
DR HOGENOM; CLU_006553_1_0_1; -.
DR InParanoid; Q8TDG4; -.
DR OMA; MFLNANI; -.
DR OrthoDB; 179246at2759; -.
DR PhylomeDB; Q8TDG4; -.
DR TreeFam; TF105018; -.
DR BRENDA; 3.6.4.12; 2681.
DR PathwayCommons; Q8TDG4; -.
DR SignaLink; Q8TDG4; -.
DR BioGRID-ORCS; 113510; 19 hits in 1082 CRISPR screens.
DR ChiTaRS; HELQ; human.
DR GenomeRNAi; 113510; -.
DR Pharos; Q8TDG4; Tbio.
DR PRO; PR:Q8TDG4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8TDG4; protein.
DR Bgee; ENSG00000163312; Expressed in calcaneal tendon and 172 other tissues.
DR ExpressionAtlas; Q8TDG4; baseline and differential.
DR Genevisible; Q8TDG4; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:1990518; F:single-stranded 3'-5' DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0010792; P:DNA double-strand break processing involved in repair via single-strand annealing; IDA:UniProtKB.
DR GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IDA:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromosome; DNA damage; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1101
FT /note="Helicase POLQ-like"
FT /id="PRO_0000329060"
FT DOMAIN 346..518
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 566..758
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 212..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 463..466
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 214..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 359..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032941"
FT VAR_SEQ 63..99
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032942"
FT VAR_SEQ 100..136
FT /note="PNDSEVDMFGDYDSFTENSFIAQVDDLEQKYMQLPEH -> VRRTWNLKLQT
FT FGILPRCKELTSFIAFVYFSRLRYRC (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032943"
FT VAR_SEQ 137..1101
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032944"
FT VAR_SEQ 338..353
FT /note="EWQHTCLTLNSVQERK -> GNAFCWNKKIFFLSLP (in isoform 2
FT and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032947"
FT VAR_SEQ 354..1101
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032948"
FT VARIANT 35
FT /note="V -> E (in dbSNP:rs6831595)"
FT /evidence="ECO:0000269|PubMed:11751861,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_061213"
FT VARIANT 235
FT /note="L -> P (in dbSNP:rs17006837)"
FT /id="VAR_055892"
FT VARIANT 565
FT /note="D -> N (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_042643"
FT VARIANT 585
FT /note="P -> S (in dbSNP:rs6817280)"
FT /id="VAR_055893"
FT VARIANT 1094
FT /note="V -> M (in dbSNP:rs17006794)"
FT /id="VAR_055894"
FT MUTAGEN 365
FT /note="K->M: Abolishes ATPase and DNA helicase activity."
FT /evidence="ECO:0000269|PubMed:11751861,
FT ECO:0000269|PubMed:34937945"
FT MUTAGEN 463
FT /note="D->A: Abolished ATPase and DNA helicase activity."
FT /evidence="ECO:0000269|PubMed:34316696"
FT MUTAGEN 818..819
FT /note="YK->SD: Abolished double-stranded DNA-binding."
FT /evidence="ECO:0000269|PubMed:28738244"
FT CONFLICT 306
FT /note="V -> I (in Ref. 1; AAL85274, 2; BAC87559 and 4;
FT AAH95473)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1101 AA; 124131 MW; B9B4B7829B021C3A CRC64;
MDECGSRIRR RVSLPKRNRP SLGCIFGAPT AAELVPGDEG KEEEEMVAEN RRRKTAGVLP
VEVQPLLLSD SPECLVLGGG DTNPDLLRHM PTDRGVGDQP NDSEVDMFGD YDSFTENSFI
AQVDDLEQKY MQLPEHKKHA TDFATENLCS ESIKNKLSIT TIGNLTELQT DKHTENQSGY
EGVTIEPGAD LLYDVPSSQA IYFENLQNSS NDLGDHSMKE RDWKSSSHNT VNEELPHNCI
EQPQQNDESS SKVRTSSDMN RRKSIKDHLK NAMTGNAKAQ TPIFSRSKQL KDTLLSEEIN
VAKKTVESSS NDLGPFYSLP SKVRDLYAQF KGIEKLYEWQ HTCLTLNSVQ ERKNLIYSLP
TSGGKTLVAE ILMLQELLCC RKDVLMILPY VAIVQEKISG LSSFGIELGF FVEEYAGSKG
RFPPTKRREK KSLYIATIEK GHSLVNSLIE TGRIDSLGLV VVDELHMIGE GSRGATLEMT
LAKILYTSKT TQIIGMSATL NNVEDLQKFL QAEYYTSQFR PVELKEYLKI NDTIYEVDSK
AENGMTFSRL LNYKYSDTLK KMDPDHLVAL VTEVIPNYSC LVFCPSKKNC ENVAEMICKF
LSKEYLKHKE KEKCEVIKNL KNIGNGNLCP VLKRTIPFGV AYHHSGLTSD ERKLLEEAYS
TGVLCLFTCT STLAAGVNLP ARRVILRAPY VAKEFLKRNQ YKQMIGRAGR AGIDTIGESI
LILQEKDKQQ VLELITKPLE NCYSHLVQEF TKGIQTLFLS LIGLKIATNL DDIYHFMNGT
FFGVQQKVLL KEKSLWEITV ESLRYLTEKG LLQKDTIYKS EEEVQYNFHI TKLGRASFKG
TIDLAYCDIL YRDLKKGLEG LVLESLLHLI YLTTPYDLVS QCNPDWMIYF RQFSQLSPAE
QNVAAILGVS ESFIGKKASG QAIGKKVDKN VVNRLYLSFV LYTLLKETNI WTVSEKFNMP
RGYIQNLLTG TASFSSCVLH FCEELEEFWV YRALLVELTK KLTYCVKAEL IPLMEVTGVL
EGRAKQLYSA GYKSLMHLAN ANPEVLVRTI DHLSRRQAKQ IVSSAKMLLH EKAEALQEEV
EELLRLPSDF PGAVASSTDK A
