ID RECQ1_HUMAN Reviewed; 649 AA.
AC P46063; A8K6G2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 3.
DT 27-MAR-2024, entry version 224.
DE RecName: Full=ATP-dependent DNA helicase Q1 {ECO:0000305|PubMed:7527136, ECO:0000305|PubMed:8056767};
DE EC=5.6.2.4 {ECO:0000269|PubMed:35025765, ECO:0000269|PubMed:8056767, ECO:0000305|PubMed:7527136};
DE AltName: Full=DNA 3'-5' helicase Q1 {ECO:0000305};
DE AltName: Full=DNA helicase, RecQ-like type 1;
DE Short=RecQ1;
DE AltName: Full=DNA-dependent ATPase Q1 {ECO:0000303|PubMed:8056767};
DE AltName: Full=RecQ protein-like 1;
GN Name=RECQL {ECO:0000303|PubMed:7961977}; Synonyms=RECQ1, RECQL1;
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], PROTEIN SEQUENCE OF 34-38; 186-193; 293-304;
RP 396-404; 431-439 AND 594-599, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND VARIANT THR-487.
RC TISSUE=Cervix carcinoma;
RX PubMed=7961977; DOI=10.1016/s0021-9258(18)43957-9;
RA Puranam K.L., Blackshear P.J.;
RT "Cloning and characterization of RECQL, a potential human homologue of the
RT Escherichia coli DNA helicase RecQ.";
RL J. Biol. Chem. 269:29838-29845(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS A
RP HELICASE, AND CATALYTIC ACTIVITY.
RX PubMed=7527136; DOI=10.1093/nar/22.22.4566;
RA Seki M., Miyazawa H., Tada S., Yanagisawa J., Yamaoka T., Hoshino S.,
RA Ozawa K., Eki T., Nogami M., Okumura K., Taguchi H., Hanaoka F.,
RA Enomoto T.;
RT "Molecular cloning of cDNA encoding human DNA helicase Q1 which has
RT homology to Escherichia coli Rec Q helicase and localization of the gene at
RT chromosome 12p12.";
RL Nucleic Acids Res. 22:4566-4573(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [8]
RP FUNCTION AS A 3'-5' HELICASE, FUNCTION AS AN ATPASE, CATALYTIC ACTIVITY,
RP AND COFACTOR.
RX PubMed=8056767; DOI=10.1093/oxfordjournals.jbchem.a124369;
RA Seki M., Yanagisawa J., Kohda T., Sonoyama T., Ui M., Enomoto T.;
RT "Purification of two DNA-dependent adenosinetriphosphatases having DNA
RT helicase activity from HeLa cells and comparison of the properties of the
RT two enzymes.";
RL J. Biochem. 115:523-531(1994).
RN [9]
RP FUNCTION, INTERACTION WITH EXO1 AND MLH1, AND MUTAGENESIS OF LYS-119.
RX PubMed=15886194; DOI=10.1074/jbc.m500265200;
RA Doherty K.M., Sharma S., Uzdilla L.A., Wilson T.M., Cui S., Vindigni A.,
RA Brosh R.M. Jr.;
RT "RECQ1 helicase interacts with human mismatch repair factors that regulate
RT genetic recombination.";
RL J. Biol. Chem. 280:28085-28094(2005).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-514 AND LYS-522, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, AND IDENTIFICATION BY
RP 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [14]
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 [15]
RP INVOLVEMENT IN RECON, VARIANT RECON SER-459, CHARACTERIZATION OF VARIANT
RP RECON SER-459, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH
RP PARP1, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=35025765; DOI=10.1172/jci147301;
RA Abu-Libdeh B., Jhujh S.S., Dhar S., Sommers J.A., Datta A., Longo G.M.,
RA Grange L.J., Reynolds J.J., Cooke S.L., McNee G.S., Hollingworth R.,
RA Woodward B.L., Ganesh A.N., Smerdon S.J., Nicolae C.M.,
RA Durlacher-Betzer K., Molho-Pessach V., Abu-Libdeh A., Meiner V.,
RA Moldovan G.L., Roukos V., Harel T., Brosh R.M. Jr., Stewart G.S.;
RT "RECON syndrome is a genome instability disorder caused by mutations in the
RT DNA helicase RECQL1.";
RL J. Clin. Invest. 132:0-0(2022).
RN [16] {ECO:0007744|PDB:2V1X}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 49-616 IN COMPLEX WITH ADP AND
RP ZN(2+), FUNCTION, SUBSTRATE SPECIFICITY, POSSIBLE ACTIVE SITE,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, DOMAIN, AND MUTAGENESIS
RP OF 555-LEU--ILE-572; 560-SER--ILE-567 AND TYR-564.
RX PubMed=19151156; DOI=10.1073/pnas.0806908106;
RA Pike A.C., Shrestha B., Popuri V., Burgess-Brown N., Muzzolini L.,
RA Costantini S., Vindigni A., Gileadi O.;
RT "Structure of the human RECQ1 helicase reveals a putative strand-separation
RT pin.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:1039-1044(2009).
RN [17] {ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 48-619 IN COMPLEX WITH ZN(2+) AND
RP DNA, FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF 511-THR--LYS-514 AND
RP ARG-528.
RX PubMed=25831490; DOI=10.1073/pnas.1417594112;
RA Pike A.C., Gomathinayagam S., Swuec P., Berti M., Zhang Y., Schnecke C.,
RA Marino F., von Delft F., Renault L., Costa A., Gileadi O., Vindigni A.;
RT "Human RECQ1 helicase-driven DNA unwinding, annealing, and branch
RT migration: insights from DNA complex structures.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4286-4291(2015).
CC -!- FUNCTION: DNA helicase that plays a role in DNA damage repair and
CC genome stability (PubMed:7961977, PubMed:7527136, PubMed:8056767,
CC PubMed:15886194, PubMed:35025765). Exhibits a magnesium- and ATP-
CC dependent DNA-helicase activity that unwinds single- and double-
CC stranded DNA in a 3'-5' direction (PubMed:7527136, PubMed:8056767,
CC PubMed:35025765, PubMed:19151156). Full-length protein unwinds forked
CC DNA substrates, resolves Holliday junctions, and has DNA strand
CC annealing activity (PubMed:19151156, PubMed:25831490). Plays a role in
CC restoring regressed replication forks (PubMed:35025765). Required to
CC restart stalled replication forks induced by abortive topoisomerase 1
CC and 2 lesions (PubMed:35025765). May play a role in the repair of DNA
CC that is damaged by ultraviolet light or other mutagens (PubMed:7961977,
CC PubMed:15886194). {ECO:0000269|PubMed:15886194,
CC ECO:0000269|PubMed:19151156, ECO:0000269|PubMed:25831490,
CC ECO:0000269|PubMed:35025765, ECO:0000269|PubMed:7527136,
CC ECO:0000269|PubMed:7961977, ECO:0000269|PubMed:8056767}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
CC Evidence={ECO:0000269|PubMed:35025765, ECO:0000269|PubMed:8056767};
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;
CC Evidence={ECO:0000269|PubMed:35025765, ECO:0000269|PubMed:7527136,
CC ECO:0000269|PubMed:8056767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000269|PubMed:35025765, ECO:0000305|PubMed:8056767};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dATP + H2O = dADP + H(+) + phosphate; Xref=Rhea:RHEA:51908,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57667, ChEBI:CHEBI:61404;
CC Evidence={ECO:0000269|PubMed:7527136, ECO:0000269|PubMed:8056767};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51909;
CC Evidence={ECO:0000305|PubMed:8056767};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8056767};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:8056767};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19151156, ECO:0000269|PubMed:25831490,
CC ECO:0000312|PDB:2V1X, ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D};
CC Note=Binds 1 Zn(2+) per monomer (PubMed:19151156).
CC {ECO:0000269|PubMed:19151156, ECO:0000269|PubMed:25831490};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=95.3 uM for ATP {ECO:0000269|PubMed:35025765};
CC KM=115 uM for ATP {ECO:0000269|PubMed:19151156};
CC Vmax=84 nmol/min/ng enzyme with ATP as substrate
CC {ECO:0000269|PubMed:35025765};
CC Note=kcat is 103.5 sec(-1) for ATP (PubMed:35025765). kcat is 90
CC min(-1) (PubMed:19151156). {ECO:0000269|PubMed:19151156,
CC ECO:0000269|PubMed:35025765};
CC -!- SUBUNIT: May form homodimers or higher order oligomers
CC (PubMed:35025765, PubMed:19151156). Forms a dimer in complex with
CC tailed duplex DNA; the DNA only mkaes contact with one of the monomers
CC (PubMed:25831490). Probably forms flat tetramers on Holliday junction
CC DNA (PubMed:25831490) (Probable). Interacts with EXO1
CC (PubMed:15886194). Interacts with MLH1 (PubMed:15886194). Interacts
CC with PARP1 (PubMed:35025765, PubMed:19151156, PubMed:25831490).
CC {ECO:0000269|PubMed:15886194, ECO:0000269|PubMed:19151156,
CC ECO:0000269|PubMed:25831490, ECO:0000269|PubMed:35025765,
CC ECO:0000305|PubMed:25831490}.
CC -!- INTERACTION:
CC P46063; P52292: KPNA2; NbExp=2; IntAct=EBI-2823728, EBI-349938;
CC P46063; O00629: KPNA4; NbExp=2; IntAct=EBI-2823728, EBI-396343;
CC P46063; P09874: PARP1; NbExp=8; IntAct=EBI-2823728, EBI-355676;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:35025765,
CC ECO:0000269|PubMed:7961977}.
CC -!- TISSUE SPECIFICITY: High expression in heart, lung, skeletal muscle and
CC kidney, low expression in brain. {ECO:0000269|PubMed:7961977}.
CC -!- DOMAIN: A helical hairpin (residues 554-573) in the winged-helix proble
CC DNA-binding domain couples the ATPase (and probably ssDNA
CC translocation) to DNA unwinding (PubMed:19151156). The isolated WH
CC domain (residues 481-624) anneals DNA as well as full-length protein
CC (PubMed:25831490). {ECO:0000269|PubMed:19151156,
CC ECO:0000269|PubMed:25831490}.
CC -!- DISEASE: RECON progeroid syndrome (RECON) [MIM:620370]: An autosomal
CC recessive syndrome characterized by short stature, progeroid facial
CC features, a hypoplastic nose, xeroderma, skin photosensitivity, muscle
CC wasting with reduced subcutaneous fat, and slender elongated thumbs.
CC {ECO:0000269|PubMed:35025765}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60261.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/283/RECQL";
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DR EMBL; L36140; AAA60261.1; ALT_FRAME; mRNA.
DR EMBL; D37984; BAA07200.1; -; mRNA.
DR EMBL; BT007119; AAP35783.1; -; mRNA.
DR EMBL; AK291627; BAF84316.1; -; mRNA.
DR EMBL; AC006559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96434.1; -; Genomic_DNA.
DR EMBL; BC001052; AAH01052.1; -; mRNA.
DR CCDS; CCDS31756.1; -.
DR PIR; A58836; A55311.
DR RefSeq; NP_002898.2; NM_002907.3.
DR RefSeq; NP_116559.1; NM_032941.2.
DR RefSeq; XP_005253518.1; XM_005253461.3.
DR RefSeq; XP_005253519.1; XM_005253462.4.
DR RefSeq; XP_005253520.1; XM_005253463.3.
DR RefSeq; XP_005253521.1; XM_005253464.3.
DR PDB; 2V1X; X-ray; 2.00 A; A/B=49-616.
DR PDB; 2WWY; X-ray; 2.90 A; A/B=49-616.
DR PDB; 4U7D; X-ray; 3.40 A; A/B/C/D=49-616.
DR PDB; 6JTZ; X-ray; 2.80 A; A/B=282-616.
DR PDBsum; 2V1X; -.
DR PDBsum; 2WWY; -.
DR PDBsum; 4U7D; -.
DR PDBsum; 6JTZ; -.
DR AlphaFoldDB; P46063; -.
DR SMR; P46063; -.
DR BioGRID; 111897; 112.
DR DIP; DIP-29216N; -.
DR IntAct; P46063; 44.
DR MINT; P46063; -.
DR STRING; 9606.ENSP00000416739; -.
DR BindingDB; P46063; -.
DR ChEMBL; CHEMBL1293236; -.
DR GlyGen; P46063; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P46063; -.
DR MetOSite; P46063; -.
DR PhosphoSitePlus; P46063; -.
DR SwissPalm; P46063; -.
DR BioMuta; RECQL; -.
DR DMDM; 218512113; -.
DR EPD; P46063; -.
DR jPOST; P46063; -.
DR MassIVE; P46063; -.
DR MaxQB; P46063; -.
DR PaxDb; 9606-ENSP00000416739; -.
DR PeptideAtlas; P46063; -.
DR ProteomicsDB; 55713; -.
DR Pumba; P46063; -.
DR TopDownProteomics; P46063; -.
DR Antibodypedia; 4055; 118 antibodies from 21 providers.
DR CPTC; P46063; 1 antibody.
DR DNASU; 5965; -.
DR Ensembl; ENST00000421138.6; ENSP00000395449.2; ENSG00000004700.16.
DR Ensembl; ENST00000444129.7; ENSP00000416739.2; ENSG00000004700.16.
DR GeneID; 5965; -.
DR KEGG; hsa:5965; -.
DR MANE-Select; ENST00000444129.7; ENSP00000416739.2; NM_002907.4; NP_002898.2.
DR UCSC; uc001rex.4; human.
DR AGR; HGNC:9948; -.
DR CTD; 5965; -.
DR DisGeNET; 5965; -.
DR GeneCards; RECQL; -.
DR HGNC; HGNC:9948; RECQL.
DR HPA; ENSG00000004700; Low tissue specificity.
DR MalaCards; RECQL; -.
DR MIM; 600537; gene.
DR MIM; 620370; phenotype.
DR neXtProt; NX_P46063; -.
DR OpenTargets; ENSG00000004700; -.
DR PharmGKB; PA34315; -.
DR VEuPathDB; HostDB:ENSG00000004700; -.
DR eggNOG; KOG0353; Eukaryota.
DR GeneTree; ENSGT00940000157013; -.
DR HOGENOM; CLU_001103_12_5_1; -.
DR InParanoid; P46063; -.
DR OMA; FKLSTMV; -.
DR OrthoDB; 5474026at2759; -.
DR PhylomeDB; P46063; -.
DR TreeFam; TF323555; -.
DR BRENDA; 3.6.4.12; 2681.
DR PathwayCommons; P46063; -.
DR SignaLink; P46063; -.
DR BioGRID-ORCS; 5965; 7 hits in 1151 CRISPR screens.
DR ChiTaRS; RECQL; human.
DR EvolutionaryTrace; P46063; -.
DR GeneWiki; RECQL; -.
DR GenomeRNAi; 5965; -.
DR Pharos; P46063; Tbio.
DR PRO; PR:P46063; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P46063; Protein.
DR Bgee; ENSG00000004700; Expressed in buccal mucosa cell and 209 other cell types or tissues.
DR ExpressionAtlas; P46063; baseline and differential.
DR Genevisible; P46063; HS.
DR GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; 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:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IDA:GO_Central.
DR GO; GO:0036121; F:double-stranded DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
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:0031297; P:replication fork processing; IDA:UniProtKB.
DR CDD; cd18015; DEXHc_RecQ1; 1.
DR CDD; cd18794; SF2_C_RecQ; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
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; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF72; ATP-DEPENDENT DNA HELICASE Q1; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Direct protein sequencing;
KW Disease variant; DNA-binding; Helicase; Hydrolase; Isomerase;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..649
FT /note="ATP-dependent DNA helicase Q1"
FT /id="PRO_0000205049"
FT DOMAIN 100..275
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 300..451
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 481..592
FT /note="Winged-helix domain"
FT /evidence="ECO:0000269|PubMed:19151156"
FT REGION 595..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 219..222
FT /note="DEVH box"
FT COMPBIAS 606..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 119
FT /evidence="ECO:0000305|PubMed:19151156"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:19151156,
FT ECO:0007744|PDB:2V1X"
FT BINDING 93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:19151156,
FT ECO:0007744|PDB:2V1X"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:19151156,
FT ECO:0007744|PDB:2V1X"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:19151156,
FT ECO:0007744|PDB:2V1X"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:19151156,
FT ECO:0007744|PDB:2V1X"
FT BINDING 119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:19151156,
FT ECO:0007744|PDB:2V1X"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:19151156,
FT ECO:0007744|PDB:2V1X"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:19151156,
FT ECO:0000269|PubMed:25831490, ECO:0007744|PDB:2V1X,
FT ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D"
FT BINDING 471
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:19151156,
FT ECO:0000269|PubMed:25831490, ECO:0007744|PDB:2V1X,
FT ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D"
FT BINDING 475
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:19151156,
FT ECO:0000269|PubMed:25831490, ECO:0007744|PDB:2V1X,
FT ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D"
FT BINDING 478
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:19151156,
FT ECO:0000269|PubMed:25831490, ECO:0007744|PDB:2V1X,
FT ECO:0007744|PDB:2WWY, ECO:0007744|PDB:4U7D"
FT MOD_RES 514
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 522
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AYJ1"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VARIANT 102
FT /note="V -> I (in dbSNP:rs1065751)"
FT /id="VAR_034679"
FT VARIANT 372
FT /note="V -> I (in dbSNP:rs2230003)"
FT /id="VAR_051732"
FT VARIANT 459
FT /note="A -> S (in RECON; likely pathogenic; reduces DNA
FT helicase activity on a forked duplex DNA substrate;
FT decreases ATPase activity; reduces DNA-binding; defect in
FT repairing abortive TOP1/topoisomerase 1 and TOP2/
FT topoisomerase 2 cleavage complexes; failure to efficiently
FT restart replication following exposure to genotoxins, such
FT as hydroxyurea (HU) and methyl methane sulfonate (MMS); no
FT impact on nuclear localization and interaction with PARP1;
FT no effect on capacity to promote single-strand DNA
FT annealing; dbSNP:rs1055710310)"
FT /evidence="ECO:0000269|PubMed:35025765"
FT /id="VAR_088584"
FT VARIANT 487
FT /note="K -> T (in dbSNP:rs6501)"
FT /evidence="ECO:0000269|PubMed:7961977"
FT /id="VAR_016140"
FT VARIANT 495
FT /note="D -> H (in dbSNP:rs6499)"
FT /id="VAR_016141"
FT MUTAGEN 119
FT /note="K->A: Abrogates helicase activity."
FT /evidence="ECO:0000269|PubMed:15886194"
FT MUTAGEN 511..514
FT /note="TPLK->APLA: Considerably reduced DNA unwinding and
FT branch migration on Holliday junctions, small change in DNA
FT annealing."
FT /evidence="ECO:0000269|PubMed:25831490"
FT MUTAGEN 528
FT /note="R->A: Reduced DNA unwinding and branch migration on
FT Holliday junctions, small change in DNA annealing."
FT /evidence="ECO:0000269|PubMed:25831490"
FT MUTAGEN 555..572
FT /note="LKEDYSFTAYATISYLKI->AA: Complete loss of DNA fork
FT unwinding, retains ATPase activity (in a 49-616 residue
FT fragment)."
FT /evidence="ECO:0000269|PubMed:19151156"
FT MUTAGEN 560..567
FT /note="SFTAYATI->AA: Complete loss of DNA fork unwinding,
FT retains ATPase activity (in a 49-616 residue fragment)."
FT /evidence="ECO:0000269|PubMed:19151156"
FT MUTAGEN 564
FT /note="Y->A: Nearly complete loss of DNA fork unwinding,
FT retains ATPase activity (in a 49-616 residue fragment)."
FT /evidence="ECO:0000269|PubMed:19151156"
FT CONFLICT 1
FT /note="M -> S (in Ref. 2; BAA07200)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="A -> D (in Ref. 1; AAA60261)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="C -> S (in Ref. 1; AAA60261)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="T -> A (in Ref. 1; AAA60261)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="E -> K (in Ref. 3; AAP35783 and 7; AAH01052)"
FT /evidence="ECO:0000305"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 96..104
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 191..195
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 198..209
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2WWY"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 240..244
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:2V1X"
FT TURN 309..314
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 395..402
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:2V1X"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:6JTZ"
FT HELIX 436..447
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 450..452
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 454..462
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 484..488
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 490..505
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 512..519
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 539..551
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 554..561
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 566..572
FT /evidence="ECO:0007829|PDB:2V1X"
FT HELIX 574..580
FT /evidence="ECO:0007829|PDB:2V1X"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:2V1X"
SQ SEQUENCE 649 AA; 73457 MW; F616DC3191F79391 CRC64;
MASVSALTEE LDSITSELHA VEIQIQELTE RQQELIQKKK VLTKKIKQCL EDSDAGASNE
YDSSPAAWNK EDFPWSGKVK DILQNVFKLE KFRPLQLETI NVTMAGKEVF LVMPTGGGKS
LCYQLPALCS DGFTLVICPL ISLMEDQLMV LKQLGISATM LNASSSKEHV KWVHAEMVNK
NSELKLIYVT PEKIAKSKMF MSRLEKAYEA RRFTRIAVDE VHCCSQWGHD FRPDYKALGI
LKRQFPNASL IGLTATATNH VLTDAQKILC IEKCFTFTAS FNRPNLYYEV RQKPSNTEDF
IEDIVKLING RYKGQSGIIY CFSQKDSEQV TVSLQNLGIH AGAYHANLEP EDKTTVHRKW
SANEIQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ ESGRAGRDDM KADCILYYGF
GDIFRISSMV VMENVGQQKL YEMVSYCQNI SKCRRVLMAQ HFDEVWNSEA CNKMCDNCCK
DSAFERKNIT EYCRDLIKIL KQAEELNEKL TPLKLIDSWM GKGAAKLRVA GVVAPTLPRE
DLEKIIAHFL IQQYLKEDYS FTAYATISYL KIGPKANLLN NEAHAITMQV TKSTQNSFRA
ESSQTCHSEQ GDKKMEEKNS GNFQKKAANM LQQSGSKNTG AKKRKIDDA
//
