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Database: UniProt
Entry: P46063
LinkDB: P46063
Original site: P46063 
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   13-NOV-2019, entry version 201.
DE   RecName: Full=ATP-dependent DNA helicase Q1;
DE            EC=3.6.4.12;
DE   AltName: Full=DNA helicase, RecQ-like type 1;
DE            Short=RecQ1;
DE   AltName: Full=DNA-dependent ATPase Q1;
DE   AltName: Full=RecQ protein-like 1;
GN   Name=RECQL; Synonyms=RECQ1, RECQL1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-38; 186-193;
RP   293-304; 396-404; 431-439 AND 594-599, FUNCTION, TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND VARIANT THR-487.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=7961977;
RA   Puranam K.L., Blackshear P.J.;
RT   "Cloning and characterization of RECQL, a potential human homologue of
RT   the Escherichia coli DNA helicase RecQ.";
RL   J. Biol. Chem. 269:29838-29845(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
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
RT   gene at 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
RT   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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   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.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   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.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION.
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
RT   the 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.,
RA   Vindigni A., Brosh R.M. Jr.;
RT   "RECQ1 helicase interacts with human mismatch repair factors that
RT   regulate 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.,
RA   Walther T.C., 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
RP   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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation 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.,
RA   Buerckstuemmer T., 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
RP   BY 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: DNA helicase that may play a role in the repair of DNA
CC       that is damaged by ultraviolet light or other mutagens. Exhibits a
CC       magnesium-dependent ATP-dependent DNA-helicase activity that
CC       unwinds single- and double-stranded DNA in a 3'-5' direction.
CC       {ECO:0000269|PubMed:15886194, ECO:0000269|PubMed:7961977,
CC       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; EC=3.6.4.12;
CC   -!- SUBUNIT: Interacts with EXO1 and MLH1.
CC       {ECO:0000269|PubMed:15886194}.
CC   -!- INTERACTION:
CC       P52292:KPNA2; NbExp=2; IntAct=EBI-2823728, EBI-349938;
CC       O00629:KPNA4; NbExp=2; IntAct=EBI-2823728, EBI-396343;
CC       P09874:PARP1; NbExp=8; IntAct=EBI-2823728, EBI-355676;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7961977}.
CC   -!- TISSUE SPECIFICITY: High expression in heart, lung, skeletal
CC       muscle and kidney, low expression in brain.
CC       {ECO:0000269|PubMed:7961977}.
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
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/RECQLID283.html";
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   PDBsum; 2V1X; -.
DR   PDBsum; 2WWY; -.
DR   PDBsum; 4U7D; -.
DR   SMR; P46063; -.
DR   BioGrid; 111897; 43.
DR   DIP; DIP-29216N; -.
DR   IntAct; P46063; 36.
DR   MINT; P46063; -.
DR   STRING; 9606.ENSP00000416739; -.
DR   BindingDB; P46063; -.
DR   ChEMBL; CHEMBL1293236; -.
DR   iPTMnet; 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; P46063; -.
DR   PeptideAtlas; P46063; -.
DR   PRIDE; P46063; -.
DR   ProteomicsDB; 55713; -.
DR   TopDownProteomics; P46063; -.
DR   DNASU; 5965; -.
DR   Ensembl; ENST00000421138; ENSP00000395449; ENSG00000004700.
DR   Ensembl; ENST00000444129; ENSP00000416739; ENSG00000004700.
DR   GeneID; 5965; -.
DR   KEGG; hsa:5965; -.
DR   UCSC; uc001rex.4; human.
DR   CTD; 5965; -.
DR   DisGeNET; 5965; -.
DR   GeneCards; RECQL; -.
DR   HGNC; HGNC:9948; RECQL.
DR   HPA; CAB009743; -.
DR   HPA; HPA030960; -.
DR   HPA; HPA064259; -.
DR   MIM; 600537; gene.
DR   neXtProt; NX_P46063; -.
DR   OpenTargets; ENSG00000004700; -.
DR   PharmGKB; PA34315; -.
DR   eggNOG; KOG0351; Eukaryota.
DR   eggNOG; COG0514; LUCA.
DR   GeneTree; ENSGT00940000157013; -.
DR   HOGENOM; HOG000044388; -.
DR   InParanoid; P46063; -.
DR   KO; K10899; -.
DR   OMA; IKLCYVT; -.
DR   OrthoDB; 445763at2759; -.
DR   PhylomeDB; P46063; -.
DR   TreeFam; TF323555; -.
DR   BRENDA; 3.6.4.12; 2681.
DR   ChiTaRS; RECQL; human.
DR   EvolutionaryTrace; P46063; -.
DR   GeneWiki; RECQL; -.
DR   GenomeRNAi; 5965; -.
DR   Pharos; P46063; -.
DR   PRO; PR:P46063; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000004700; Expressed in 233 organ(s), highest expression level in buccal mucosa cell.
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; IBA:GO_Central.
DR   GO; GO:0036310; F:annealing helicase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0032508; P:DNA duplex unwinding; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0000733; P:DNA strand renaturation; IDA: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   Gene3D; 1.10.10.10; -; 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   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; SSF52540; 2.
DR   TIGRFAMs; TIGR00614; recQ_fam; 1.
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; Complete proteome;
KW   Direct protein sequencing; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome.
FT   CHAIN         1    649       ATP-dependent DNA helicase Q1.
FT                                /FTId=PRO_0000205049.
FT   DOMAIN      100    275       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      300    451       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   NP_BIND     113    120       ATP. {ECO:0000305}.
FT   MOTIF       219    222       DEVH box.
FT   MOD_RES     514    514       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     522    522       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     597    597       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     602    602       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q6AYJ1}.
FT   MOD_RES     634    634       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   VARIANT     102    102       V -> I (in dbSNP:rs1065751).
FT                                /FTId=VAR_034679.
FT   VARIANT     372    372       V -> I (in dbSNP:rs2230003).
FT                                /FTId=VAR_051732.
FT   VARIANT     487    487       K -> T (in dbSNP:rs6501).
FT                                {ECO:0000269|PubMed:7961977}.
FT                                /FTId=VAR_016140.
FT   VARIANT     495    495       D -> H (in dbSNP:rs6499).
FT                                /FTId=VAR_016141.
FT   MUTAGEN     119    119       K->A: Abrogates helicase activity.
FT                                {ECO:0000269|PubMed:15886194}.
FT   CONFLICT      1      1       M -> S (in Ref. 2; BAA07200).
FT                                {ECO:0000305}.
FT   CONFLICT    175    175       A -> D (in Ref. 1; AAA60261).
FT                                {ECO:0000305}.
FT   CONFLICT    453    453       C -> S (in Ref. 1; AAA60261).
FT                                {ECO:0000305}.
FT   CONFLICT    566    566       T -> A (in Ref. 1; AAA60261).
FT                                {ECO:0000305}.
FT   CONFLICT    617    617       E -> K (in Ref. 3; AAP35783 and 7;
FT                                AAH01052). {ECO:0000305}.
FT   HELIX        65     68       {ECO:0000244|PDB:2V1X}.
FT   HELIX        76     85       {ECO:0000244|PDB:2V1X}.
FT   HELIX        96    104       {ECO:0000244|PDB:2V1X}.
FT   STRAND      109    112       {ECO:0000244|PDB:2V1X}.
FT   HELIX       121    128       {ECO:0000244|PDB:2V1X}.
FT   STRAND      130    137       {ECO:0000244|PDB:2V1X}.
FT   HELIX       141    154       {ECO:0000244|PDB:2V1X}.
FT   STRAND      158    160       {ECO:0000244|PDB:2V1X}.
FT   HELIX       167    178       {ECO:0000244|PDB:2V1X}.
FT   STRAND      186    189       {ECO:0000244|PDB:2V1X}.
FT   HELIX       191    195       {ECO:0000244|PDB:2V1X}.
FT   HELIX       198    209       {ECO:0000244|PDB:2V1X}.
FT   STRAND      213    219       {ECO:0000244|PDB:2V1X}.
FT   HELIX       221    224       {ECO:0000244|PDB:2V1X}.
FT   HELIX       226    228       {ECO:0000244|PDB:2WWY}.
FT   HELIX       233    239       {ECO:0000244|PDB:2V1X}.
FT   HELIX       240    244       {ECO:0000244|PDB:2V1X}.
FT   STRAND      248    256       {ECO:0000244|PDB:2V1X}.
FT   HELIX       259    268       {ECO:0000244|PDB:2V1X}.
FT   STRAND      275    278       {ECO:0000244|PDB:2V1X}.
FT   STRAND      286    292       {ECO:0000244|PDB:2V1X}.
FT   HELIX       297    308       {ECO:0000244|PDB:2V1X}.
FT   TURN        309    314       {ECO:0000244|PDB:2V1X}.
FT   STRAND      316    320       {ECO:0000244|PDB:2V1X}.
FT   HELIX       324    336       {ECO:0000244|PDB:2V1X}.
FT   STRAND      341    344       {ECO:0000244|PDB:2V1X}.
FT   HELIX       350    361       {ECO:0000244|PDB:2V1X}.
FT   STRAND      364    370       {ECO:0000244|PDB:2V1X}.
FT   STRAND      383    390       {ECO:0000244|PDB:2V1X}.
FT   HELIX       395    402       {ECO:0000244|PDB:2V1X}.
FT   STRAND      412    418       {ECO:0000244|PDB:2V1X}.
FT   HELIX       420    429       {ECO:0000244|PDB:2V1X}.
FT   TURN        430    432       {ECO:0000244|PDB:2V1X}.
FT   HELIX       436    447       {ECO:0000244|PDB:2V1X}.
FT   STRAND      450    452       {ECO:0000244|PDB:2V1X}.
FT   HELIX       454    462       {ECO:0000244|PDB:2V1X}.
FT   HELIX       476    479       {ECO:0000244|PDB:2V1X}.
FT   STRAND      484    488       {ECO:0000244|PDB:2V1X}.
FT   HELIX       490    505       {ECO:0000244|PDB:2V1X}.
FT   HELIX       512    519       {ECO:0000244|PDB:2V1X}.
FT   HELIX       525    527       {ECO:0000244|PDB:2V1X}.
FT   HELIX       539    551       {ECO:0000244|PDB:2V1X}.
FT   STRAND      554    561       {ECO:0000244|PDB:2V1X}.
FT   STRAND      566    572       {ECO:0000244|PDB:2V1X}.
FT   HELIX       574    580       {ECO:0000244|PDB:2V1X}.
FT   STRAND      587    591       {ECO:0000244|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
//
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