RECQ5_HUMAN
ID RECQ5_HUMAN Reviewed; 991 AA.
AC O94762; Q6P4G0; Q9H0B1; Q9P1W7; Q9UNC8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=ATP-dependent DNA helicase Q5;
DE EC=3.6.4.12;
DE AltName: Full=DNA helicase, RecQ-like type 5;
DE Short=RecQ5;
DE AltName: Full=RecQ protein-like 5;
GN Name=RECQL5; Synonyms=RECQ5;
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 ALPHA).
RC TISSUE=Testis;
RX PubMed=9878247; DOI=10.1006/geno.1998.5595;
RA Kitao S., Ohsugi I., Ichikawa K., Goto M., Furuichi Y., Shimamoto A.;
RT "Cloning of two new human helicase genes of the RecQ family: biological
RT significance of multiple species in higher eukaryotes.";
RL Genomics 54:443-452(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND GAMMA).
RX PubMed=10471747; DOI=10.1093/nar/27.18.3762;
RA Sekelsky J.J., Brodsky M.H., Rubin G.M., Hawley R.S.;
RT "Drosophila and human RecQ5 exist in different isoforms generated by
RT alternative splicing.";
RL Nucleic Acids Res. 27:3762-3769(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA), SUBCELLULAR
RP LOCATION, AND INTERACTION WITH TOP3A AND TOP3B.
RC TISSUE=Testis;
RX PubMed=10710432; DOI=10.1093/nar/28.7.1647;
RA Shimamoto A., Nishikawa K., Kitao S., Furuichi Y.;
RT "Human RecQ5-beta, a large isomer of RecQ5 DNA helicase, localizes in the
RT nucleoplasm and interacts with topoisomerases 3-alpha and 3-beta.";
RL Nucleic Acids Res. 28:1647-1655(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GAMMA AND 4).
RC TISSUE=Duodenum, and Uterus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-991.
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815, 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 [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20643585; DOI=10.1016/j.dnarep.2010.06.009;
RA Blundred R., Myers K., Helleday T., Goldman A.S., Bryant H.E.;
RT "Human RECQL5 overcomes thymidine-induced replication stress.";
RL DNA Repair 9:964-975(2010).
RN [10]
RP INTERACTION WITH RAD51, MUTAGENESIS OF PHE-666, AND FUNCTION.
RX PubMed=20348101; DOI=10.1074/jbc.m110.110478;
RA Schwendener S., Raynard S., Paliwal S., Cheng A., Kanagaraj R.,
RA Shevelev I., Stark J.M., Sung P., Janscak P.;
RT "Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-
RT recombinase activity.";
RL J. Biol. Chem. 285:15739-15745(2010).
RN [11]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH RNA POLYMERASE II, INTERACTION
RP WITH POLR2A AND RAD51, MUTAGENESIS OF ARG-550; GLU-584; TYR-597 AND
RP LEU-602, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20231364; DOI=10.1128/mcb.01583-09;
RA Islam M.N., Fox D. III, Guo R., Enomoto T., Wang W.;
RT "RecQL5 promotes genome stabilization through two parallel mechanisms--
RT interacting with RNA polymerase II and acting as a helicase.";
RL Mol. Cell. Biol. 30:2460-2472(2010).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22973052; DOI=10.1091/mbc.e12-02-0110;
RA Tadokoro T., Ramamoorthy M., Popuri V., May A., Tian J., Sykora P.,
RA Rybanska I., Wilson D.M. III, Croteau D.L., Bohr V.A.;
RT "Human RECQL5 participates in the removal of endogenous DNA damage.";
RL Mol. Biol. Cell 23:4273-4285(2012).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP TOP2A.
RX PubMed=22013166; DOI=10.1093/nar/gkr844;
RA Ramamoorthy M., Tadokoro T., Rybanska I., Ghosh A.K., Wersto R., May A.,
RA Kulikowicz T., Sykora P., Croteau D.L., Bohr V.A.;
RT "RECQL5 cooperates with Topoisomerase II alpha in DNA decatenation and cell
RT cycle progression.";
RL Nucleic Acids Res. 40:1621-1635(2012).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23715498; DOI=10.1093/carcin/bgt183;
RA Ramamoorthy M., May A., Tadokoro T., Popuri V., Seidman M.M., Croteau D.L.,
RA Bohr V.A.;
RT "The RecQ helicase RECQL5 participates in psoralen-induced interstrand
RT cross-link repair.";
RL Carcinogenesis 34:2218-2230(2013).
RN [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH WRN.
RX PubMed=23180761; DOI=10.1093/nar/gks1134;
RA Popuri V., Huang J., Ramamoorthy M., Tadokoro T., Croteau D.L., Bohr V.A.;
RT "RECQL5 plays co-operative and complementary roles with WRN syndrome
RT helicase.";
RL Nucleic Acids Res. 41:881-899(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727; SER-815 AND THR-839, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491 AND SER-815, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP FUNCTION, AND INTERACTION WITH POLR1A.
RX PubMed=27502483; DOI=10.1083/jcb.201507099;
RA Urban V., Dobrovolna J., Huehn D., Fryzelkova J., Bartek J., Janscak P.;
RT "RECQ5 helicase promotes resolution of conflicts between replication and
RT transcription in human cells.";
RL J. Cell Biol. 214:401-415(2016).
RN [19]
RP FUNCTION, INTERACTION WITH MUS81, MUTAGENESIS OF SER-727, AND
RP PHOSPHORYLATION AT SER-727 BY CDK1.
RX PubMed=28575661; DOI=10.1016/j.molcel.2017.05.006;
RA Di Marco S., Hasanova Z., Kanagaraj R., Chappidi N., Altmannova V.,
RA Menon S., Sedlackova H., Langhoff J., Surendranath K., Huehn D.,
RA Bhowmick R., Marini V., Ferrari S., Hickson I.D., Krejci L., Janscak P.;
RT "RECQ5 Helicase Cooperates with MUS81 Endonuclease in Processing Stalled
RT Replication Forks at Common Fragile Sites during Mitosis.";
RL Mol. Cell 66:658-671.e8(2017).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 515-620, STRUCTURE BY ELECTRON
RP MICROSCOPY IN COMPLEX WITH RNA POLYMERASE II AND DNA, INTERACTION WITH
RP POLR2A, SUBUNIT, FUNCTION, AND MUTAGENESIS OF ASP-157; TRP-504; TYR-508;
RP ARG-515; LYS-516; HIS-552; LEU-556; LYS-598; LEU-602 AND LYS-603.
RX PubMed=23748380; DOI=10.1038/nsmb.2596;
RA Kassube S.A., Jinek M., Fang J., Tsutakawa S., Nogales E.;
RT "Structural mimicry in transcription regulation of human RNA polymerase II
RT by the DNA helicase RECQL5.";
RL Nat. Struct. Mol. Biol. 20:892-899(2013).
CC -!- FUNCTION: DNA helicase that plays an important role in DNA replication,
CC transcription and repair (PubMed:20643585, PubMed:22973052). Binds to
CC the RNA polymerase II subunit POLR2A during transcription elongation
CC and suppresses transcription-associated genomic instability
CC (PubMed:20231364). Associates also with POLR1A and enforces the
CC stability of ribosomal DNA arrays (PubMed:27502483). Plays an important
CC role in mitotic chromosome separation after cross-over events and cell
CC cycle progress (PubMed:22013166). Mechanistically, removes RAD51
CC filaments protecting stalled replication forks at common fragile sites
CC and stimulates MUS81-EME1 endonuclease leading to mitotic DNA synthesis
CC (PubMed:28575661). Required for efficient DNA repair, including repair
CC of inter-strand cross-links (PubMed:23715498). Stimulates DNA
CC decatenation mediated by TOP2A. Prevents sister chromatid exchange and
CC homologous recombination. {ECO:0000269|PubMed:20231364,
CC ECO:0000269|PubMed:20348101, ECO:0000269|PubMed:20643585,
CC ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22973052,
CC ECO:0000269|PubMed:23715498, ECO:0000269|PubMed:23748380,
CC ECO:0000269|PubMed:27502483, ECO:0000269|PubMed:28575661}.
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:22013166};
CC -!- SUBUNIT: Monomer. Interacts with TOP2A, TOP3A and TOP3B
CC (PubMed:20231364, PubMed:10710432). Isoform beta interacts with RNA
CC polymerase II subunit POLR2A (PubMed:20348101, PubMed:20231364,
CC PubMed:23748380). Identified in a complex with the RNA polymerase II
CC core bound to DNA (PubMed:20348101, PubMed:20231364). Interacts (via C-
CC terminus) with POLR1A (PubMed:27502483). Isoform beta interacts with
CC RAD51 (PubMed:20348101, PubMed:20231364). Interacts with WRN; this
CC interaction stimulates WRN helicase activity on DNA fork duplexes
CC (PubMed:23180761). Interacts with MUS1; this interaction promotes
CC MUS81-dependent mitotic DNA synthesis (PubMed:28575661).
CC {ECO:0000269|PubMed:10710432, ECO:0000269|PubMed:20231364,
CC ECO:0000269|PubMed:20348101, ECO:0000269|PubMed:22013166,
CC ECO:0000269|PubMed:23180761, ECO:0000269|PubMed:23748380,
CC ECO:0000269|PubMed:27502483, ECO:0000269|PubMed:28575661}.
CC -!- INTERACTION:
CC O94762-1; P24928: POLR2A; NbExp=8; IntAct=EBI-15710057, EBI-295301;
CC O94762-1; O94762-1: RECQL5; NbExp=2; IntAct=EBI-15710057, EBI-15710057;
CC -!- SUBCELLULAR LOCATION: [Isoform Beta]: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:10710432, ECO:0000269|PubMed:23180761,
CC ECO:0000269|PubMed:23715498}. Nucleus {ECO:0000269|PubMed:23180761}.
CC Note=Recruited to sites of DNA damage, such as single-strand breaks and
CC inter-strand cross-links, and at stalled replication forks. Re-
CC localizes from the nucleolus into the nucleus after replicative stress
CC and significantly associates with WRN during S-phase (PubMed:23180761).
CC {ECO:0000269|PubMed:20643585, ECO:0000269|PubMed:22013166,
CC ECO:0000269|PubMed:22973052, ECO:0000269|PubMed:23180761,
CC ECO:0000269|PubMed:23715498}.
CC -!- SUBCELLULAR LOCATION: [Isoform Alpha]: Cytoplasm
CC {ECO:0000269|PubMed:10710432}.
CC -!- SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm
CC {ECO:0000269|PubMed:10710432}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Beta;
CC IsoId=O94762-1; Sequence=Displayed;
CC Name=Alpha; Synonyms=RecQ5b;
CC IsoId=O94762-2; Sequence=VSP_005568;
CC Name=Gamma; Synonyms=RecQ5a;
CC IsoId=O94762-3; Sequence=VSP_005569, VSP_005570;
CC Name=4;
CC IsoId=O94762-4; Sequence=VSP_057431;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated by CDK1 at Ser-727; this phosphorylation is
CC required for RECQL5-mediated disruption of RAD51 filaments on stalled
CC replication forks. {ECO:0000269|PubMed:28575661}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RECQL5ID286.html";
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DR EMBL; AB006533; BAA74454.1; -; mRNA.
DR EMBL; AF135183; AAD43061.1; -; mRNA.
DR EMBL; AF135183; AAD43062.1; -; mRNA.
DR EMBL; AB042823; BAA95952.1; -; mRNA.
DR EMBL; AB042824; BAA95953.1; -; mRNA.
DR EMBL; AB042825; BAA95954.1; -; mRNA.
DR EMBL; AC087749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89292.1; -; Genomic_DNA.
DR EMBL; BC016911; AAH16911.1; -; mRNA.
DR EMBL; BC063440; AAH63440.1; -; mRNA.
DR EMBL; AL136869; CAB66803.3; -; mRNA.
DR CCDS; CCDS32735.1; -. [O94762-3]
DR CCDS; CCDS42380.1; -. [O94762-1]
DR CCDS; CCDS45777.1; -. [O94762-2]
DR RefSeq; NP_001003715.1; NM_001003715.3. [O94762-3]
DR RefSeq; NP_001003716.1; NM_001003716.3. [O94762-2]
DR RefSeq; NP_004250.4; NM_004259.6. [O94762-1]
DR RefSeq; XP_016880832.1; XM_017025343.1.
DR RefSeq; XP_016880833.1; XM_017025344.1.
DR PDB; 4BK0; X-ray; 1.90 A; A/B=515-620.
DR PDB; 5LB3; X-ray; 1.80 A; B/E=11-453.
DR PDB; 5LB5; X-ray; 2.00 A; A/B/C/D=11-453.
DR PDB; 5LB8; X-ray; 3.40 A; A/D=11-526.
DR PDB; 5LBA; X-ray; 2.50 A; A/B/C/D=11-453.
DR PDBsum; 4BK0; -.
DR PDBsum; 5LB3; -.
DR PDBsum; 5LB5; -.
DR PDBsum; 5LB8; -.
DR PDBsum; 5LBA; -.
DR AlphaFoldDB; O94762; -.
DR SMR; O94762; -.
DR BioGRID; 114797; 106.
DR DIP; DIP-32964N; -.
DR IntAct; O94762; 44.
DR MINT; O94762; -.
DR STRING; 9606.ENSP00000317636; -.
DR iPTMnet; O94762; -.
DR PhosphoSitePlus; O94762; -.
DR BioMuta; RECQL5; -.
DR EPD; O94762; -.
DR jPOST; O94762; -.
DR MassIVE; O94762; -.
DR MaxQB; O94762; -.
DR PaxDb; O94762; -.
DR PeptideAtlas; O94762; -.
DR PRIDE; O94762; -.
DR ProteomicsDB; 50425; -. [O94762-1]
DR ProteomicsDB; 50426; -. [O94762-2]
DR ProteomicsDB; 50427; -. [O94762-3]
DR Antibodypedia; 19590; 180 antibodies from 26 providers.
DR DNASU; 9400; -.
DR Ensembl; ENST00000317905.10; ENSP00000317636.5; ENSG00000108469.15. [O94762-1]
DR Ensembl; ENST00000340830.9; ENSP00000341983.5; ENSG00000108469.15. [O94762-3]
DR Ensembl; ENST00000420326.6; ENSP00000414933.2; ENSG00000108469.15. [O94762-2]
DR Ensembl; ENST00000423245.6; ENSP00000394820.2; ENSG00000108469.15. [O94762-4]
DR Ensembl; ENST00000584999.1; ENSP00000462248.1; ENSG00000108469.15. [O94762-3]
DR GeneID; 9400; -.
DR KEGG; hsa:9400; -.
DR MANE-Select; ENST00000317905.10; ENSP00000317636.5; NM_004259.7; NP_004250.4.
DR UCSC; uc002joz.5; human. [O94762-1]
DR UCSC; uc060jzt.1; human.
DR CTD; 9400; -.
DR DisGeNET; 9400; -.
DR GeneCards; RECQL5; -.
DR HGNC; HGNC:9950; RECQL5.
DR HPA; ENSG00000108469; Low tissue specificity.
DR MIM; 603781; gene.
DR neXtProt; NX_O94762; -.
DR OpenTargets; ENSG00000108469; -.
DR PharmGKB; PA34317; -.
DR VEuPathDB; HostDB:ENSG00000108469; -.
DR eggNOG; KOG0352; Eukaryota.
DR GeneTree; ENSGT00940000157800; -.
DR HOGENOM; CLU_001103_4_1_1; -.
DR InParanoid; O94762; -.
DR OMA; QNITRFF; -.
DR OrthoDB; 445763at2759; -.
DR PhylomeDB; O94762; -.
DR TreeFam; TF317614; -.
DR PathwayCommons; O94762; -.
DR SignaLink; O94762; -.
DR BioGRID-ORCS; 9400; 13 hits in 1075 CRISPR screens.
DR ChiTaRS; RECQL5; human.
DR GeneWiki; RECQL5; -.
DR GenomeRNAi; 9400; -.
DR Pharos; O94762; Tbio.
DR PRO; PR:O94762; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O94762; protein.
DR Bgee; ENSG00000108469; Expressed in lower esophagus mucosa and 120 other tissues.
DR ExpressionAtlas; O94762; baseline and differential.
DR Genevisible; O94762; HS.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016591; C:RNA polymerase II, holoenzyme; IDA:UniProtKB.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0072757; P:cellular response to camptothecin; IEA:Ensembl.
DR GO; GO:1901655; P:cellular response to ketone; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0051304; P:chromosome separation; IMP:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR GO; GO:0006259; P:DNA metabolic process; NAS:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010716; RECQ5.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF06959; RecQ5; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00614; recQ_fam; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cytoplasm; DNA damage; DNA repair; DNA replication; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..991
FT /note="ATP-dependent DNA helicase Q5"
FT /id="PRO_0000205055"
FT DOMAIN 39..213
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 241..403
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 490..620
FT /note="Interaction with POLR2A"
FT REGION 613..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..725
FT /note="Interaction with RAD51"
FT REGION 681..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 157..160
FT /note="DEAH box"
FT COMPBIAS 681..698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D4ACP5"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 727
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:28575661,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 839
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 43..69
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057431"
FT VAR_SEQ 411..991
FT /note="Missing (in isoform Alpha)"
FT /evidence="ECO:0000303|PubMed:10471747,
FT ECO:0000303|PubMed:10710432, ECO:0000303|PubMed:9878247"
FT /id="VSP_005568"
FT VAR_SEQ 411..435
FT /note="CRHAAIAKYFGDALPACAKGCDHCQ -> RWGRGHGKSLRAAWCSQVVSRHA
FT EL (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:10471747,
FT ECO:0000303|PubMed:10710432, ECO:0000303|PubMed:15489334"
FT /id="VSP_005569"
FT VAR_SEQ 436..991
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:10471747,
FT ECO:0000303|PubMed:10710432, ECO:0000303|PubMed:15489334"
FT /id="VSP_005570"
FT VARIANT 480
FT /note="D -> G (in dbSNP:rs820196)"
FT /id="VAR_024272"
FT VARIANT 628
FT /note="S -> N (in dbSNP:rs35566780)"
FT /id="VAR_051733"
FT MUTAGEN 157
FT /note="D->A: Abolishes helicase activity."
FT MUTAGEN 504
FT /note="W->A: Abolishes interaction with POLR2A."
FT MUTAGEN 508
FT /note="Y->A: Abolishes interaction with POLR2A."
FT MUTAGEN 515
FT /note="R->E: Abolishes interaction with POLR2A."
FT MUTAGEN 516
FT /note="K->E: Abolishes interaction with POLR2A."
FT MUTAGEN 550
FT /note="R->A: Impairs protein folding and abolishes
FT interaction with POLR2A."
FT /evidence="ECO:0000269|PubMed:20231364"
FT MUTAGEN 552
FT /note="H->A: Abolishes interaction with POLR2A."
FT MUTAGEN 556
FT /note="L->E: Abolishes interaction with POLR2A."
FT MUTAGEN 584
FT /note="E->A,D: Abolishes interaction with POLR2A."
FT /evidence="ECO:0000269|PubMed:20231364"
FT MUTAGEN 597
FT /note="Y->A: Reduces interaction with POLR2A."
FT /evidence="ECO:0000269|PubMed:20231364"
FT MUTAGEN 598
FT /note="K->E: Abolishes interaction with POLR2A."
FT MUTAGEN 602
FT /note="L->D,E: Abolishes interaction with POLR2A."
FT /evidence="ECO:0000269|PubMed:20231364"
FT MUTAGEN 603
FT /note="K->E: Abolishes interaction with POLR2A."
FT MUTAGEN 666
FT /note="F->A: Abolishes interaction with RAD51."
FT /evidence="ECO:0000269|PubMed:20348101"
FT MUTAGEN 727
FT /note="S->A: Loss of phosphorylation in early mitosis."
FT /evidence="ECO:0000269|PubMed:28575661"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 48..51
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 106..116
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:5LB3"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:5LB3"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:5LBA"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 269..282
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:5LBA"
FT HELIX 295..306
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 309..316
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 328..335
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 340..347
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 365..386
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 392..407
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 412..420
FT /evidence="ECO:0007829|PDB:5LB3"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:5LB8"
FT HELIX 432..435
FT /evidence="ECO:0007829|PDB:5LB3"
FT HELIX 437..450
FT /evidence="ECO:0007829|PDB:5LB3"
FT TURN 535..538
FT /evidence="ECO:0007829|PDB:4BK0"
FT HELIX 547..589
FT /evidence="ECO:0007829|PDB:4BK0"
FT HELIX 594..613
FT /evidence="ECO:0007829|PDB:4BK0"
SQ SEQUENCE 991 AA; 108858 MW; 983668133DED865A CRC64;
MSSHHTTFPF DPERRVRSTL KKVFGFDSFK TPLQESATMA VVKGNKDVFV CMPTGAGKSL
CYQLPALLAK GITIVVSPLI ALIQDQVDHL LTLKVRVSSL NSKLSAQERK ELLADLEREK
PQTKILYITP EMAASSSFQP TLNSLVSRHL LSYLVVDEAH CVSQWGHDFR PDYLRLGALR
SRLGHAPCVA LTATATPQVQ EDVFAALHLK KPVAIFKTPC FRANLFYDVQ FKELISDPYG
NLKDFCLKAL GQEADKGLSG CGIVYCRTRE ACEQLAIELS CRGVNAKAYH AGLKASERTL
VQNDWMEEKV PVIVATISFG MGVDKANVRF VAHWNIAKSM AGYYQESGRA GRDGKPSWCR
LYYSRNDRDQ VSFLIRKEVA KLQEKRGNKA SDKATIMAFD ALVTFCEELG CRHAAIAKYF
GDALPACAKG CDHCQNPTAV RRRLEALERS SSWSKTCIGP SQGNGFDPEL YEGGRKGYGD
FSRYDEGSGG SGDEGRDEAH KREWNLFYQK QMQLRKGKDP KIEEFVPPDE NCPLKEASSR
RIPRLTVKAR EHCLRLLEEA LSSNRQSTRT ADEADLRAKA VELEHETFRN AKVANLYKAS
VLKKVADIHR ASKDGQPYDM GGSAKSCSAQ AEPPEPNEYD IPPASHVYSL KPKRVGAGFP
KGSCPFQTAT ELMETTRIRE QAPQPERGGE HEPPSRPCGL LDEDGSEPLP GPRGEVPGGS
AHYGGPSPEK KAKSSSGGSS LAKGRASKKQ QLLATAAHKD SQSIARFFCR RVESPALLAS
APEAEGACPS CEGVQGPPMA PEKYTGEEDG AGGHSPAPPQ TEECLRERPS TCPPRDQGTP
EVQPTPAKDT WKGKRPRSQQ ENPESQPQKR PRPSAKPSVV AEVKGSVSAS EQGTLNPTAQ
DPFQLSAPGV SLKEAANVVV KCLTPFYKEG KFASKELFKG FARHLSHLLT QKTSPGRSVK
EEAQNLIRHF FHGRARCESE ADWHGLCGPQ R
