ID INO80_HUMAN Reviewed; 1556 AA.
AC Q9ULG1; A6H8X4; Q9NTG6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 27-MAR-2024, entry version 184.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000305};
DE Short=hINO80;
DE EC=3.6.4.- {ECO:0000269|PubMed:16298340, ECO:0000269|PubMed:21303910};
DE AltName: Full=DNA helicase-related INO80 complex homolog 1 {ECO:0000305};
DE AltName: Full=DNA helicase-related protein INO80 {ECO:0000305};
DE AltName: Full=INO80 complex subunit A;
GN Name=INO80; Synonyms=INO80A, INOC1, KIAA1259;
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 [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1302-1556.
RC TISSUE=Testis;
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 [5]
RP FUNCTION, IDENTIFICATION IN INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16230350; DOI=10.1074/jbc.m509128200;
RA Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K.,
RA Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A., Washburn M.P.,
RA Conaway R.C., Conaway J.W.;
RT "A mammalian chromatin remodeling complex with similarities to the yeast
RT INO80 complex.";
RL J. Biol. Chem. 280:41207-41212(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, DNA-BINDING, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=16298340; DOI=10.1016/j.bbrc.2005.10.206;
RA Bakshi R., Mehta A.K., Sharma R., Maiti S., Pasha S., Brahmachari V.;
RT "Characterization of a human SWI2/SNF2 like protein hINO80: demonstration
RT of catalytic and DNA binding activity.";
RL Biochem. Biophys. Res. Commun. 339:313-320(2006).
RN [7]
RP FUNCTION, AND INTERACTION WITH YY1.
RX PubMed=17721549; DOI=10.1038/nsmb1276;
RA Cai Y., Jin J., Yao T., Gottschalk A.J., Swanson S.K., Wu S., Shi Y.,
RA Washburn M.P., Florens L., Conaway R.C., Conaway J.W.;
RT "YY1 functions with INO80 to activate transcription.";
RL Nat. Struct. Mol. Biol. 14:872-874(2007).
RN [8]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE INO80 COMPLEX, AND INTERACTION
RP WITH YY1.
RX PubMed=18026119; DOI=10.1038/nsmb1332;
RA Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H.,
RA Wang W., Nickoloff J.A., Wu C., Shi Y.;
RT "A YY1-INO80 complex regulates genomic stability through homologous
RT recombination-based repair.";
RL Nat. Struct. Mol. Biol. 14:1165-1172(2007).
RN [9]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18922472; DOI=10.1016/j.molcel.2008.08.027;
RA Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P.,
RA Florens L., Conaway R.C., Cohen R.E., Conaway J.W.;
RT "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the
RT proteasome and in the Ino80 chromatin-remodeling complex.";
RL Mol. Cell 31:909-917(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1512, 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-118, AND IDENTIFICATION BY MASS
RP 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 [13]
RP SUBCELLULAR LOCATION.
RX PubMed=20971067; DOI=10.1016/j.bbrc.2010.10.066;
RA Kashiwaba S., Kitahashi K., Watanabe T., Onoda F., Ohtsu M., Murakami Y.;
RT "The mammalian INO80 complex is recruited to DNA damage sites in an ARP8
RT dependent manner.";
RL Biochem. Biophys. Res. Commun. 402:619-625(2010).
RN [14]
RP FUNCTION IN DNA REPAIR.
RX PubMed=20687897; DOI=10.1042/bj20100988;
RA Park E.J., Hur S.K., Kwon J.;
RT "Human INO80 chromatin-remodelling complex contributes to DNA double-strand
RT break repair via the expression of Rad54B and XRCC3 genes.";
RL Biochem. J. 431:179-187(2010).
RN [15]
RP FUNCTION, INTERACTION WITH TUBULIN ALPHA, AND SUBCELLULAR LOCATION.
RX PubMed=20237820; DOI=10.1007/s00018-010-0337-3;
RA Hur S.K., Park E.J., Han J.E., Kim Y.A., Kim J.D., Kang D., Kwon J.;
RT "Roles of human INO80 chromatin remodeling enzyme in DNA replication and
RT chromosome segregation suppress genome instability.";
RL Cell. Mol. Life Sci. 67:2283-2296(2010).
RN [16]
RP FUNCTION IN DNA REPAIR, INTERACTION WITH DDB1, AND FUNCTION OF THE INO80
RP COMPLEX.
RX PubMed=20855601; DOI=10.1073/pnas.1008388107;
RA Jiang Y., Wang X., Bao S., Guo R., Johnson D.G., Shen X., Li L.;
RT "INO80 chromatin remodeling complex promotes the removal of UV lesions by
RT the nucleotide excision repair pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:17274-17279(2010).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, IDENTIFICATION IN THE
RP INO80 COMPLEX, AND MUTAGENESIS OF GLU-653.
RX PubMed=21303910; DOI=10.1074/jbc.m111.222505;
RA Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
RA Conaway J.W., Conaway R.C.;
RT "Subunit organization of the human INO80 chromatin remodeling complex: An
RT evolutionarily conserved core complex catalyzes ATP-dependent nucleosome
RT remodeling.";
RL J. Biol. Chem. 286:11283-11289(2011).
RN [18]
RP INTERACTION WITH YY1AP1.
RX PubMed=27939641; DOI=10.1016/j.ajhg.2016.11.008;
RG University of Washington Center for Mendelian Genomics;
RA Guo D.C., Duan X.Y., Regalado E.S., Mellor-Crummey L., Kwartler C.S.,
RA Kim D., Lieberman K., de Vries B.B., Pfundt R., Schinzel A., Kotzot D.,
RA Shen X., Yang M.L., Bamshad M.J., Nickerson D.A., Gornik H.L., Ganesh S.K.,
RA Braverman A.C., Grange D.K., Milewicz D.M.;
RT "Loss-of-function mutations in YY1AP1 lead to Grange Syndrome and a
RT fibromuscular dysplasia-like vascular disease.";
RL Am. J. Hum. Genet. 100:21-30(2017).
RN [19]
RP INTERACTION WITH EPSTEIN-BARR VIRUS BZLF1 (MICROBIAL INFECTION).
RX PubMed=30926617; DOI=10.26508/lsa.201800108;
RA Schaeffner M., Mrozek-Gorska P., Buschle A., Woellmer A., Tagawa T.,
RA Cernilogar F.M., Schotta G., Krietenstein N., Lieleg C., Korber P.,
RA Hammerschmidt W.;
RT "BZLF1 interacts with chromatin remodelers promoting escape from latent
RT infections with EBV.";
RL Life. Sci Alliance 2:0-0(2019).
CC -!- FUNCTION: ATPase component of the chromatin remodeling INO80 complex
CC which is involved in transcriptional regulation, DNA replication and
CC DNA repair (PubMed:16230350, PubMed:16298340, PubMed:17721549,
CC PubMed:20855601, PubMed:20237820). Binds DNA (PubMed:16298340,
CC PubMed:21303910). As part of the INO80 complex, remodels chromatin by
CC shifting nucleosomes (PubMed:16230350, PubMed:21303910). Regulates
CC transcription upon recruitment by YY1 to YY1-activated genes, where it
CC acts as an essential coactivator (PubMed:17721549). Involved in UV-
CC damage excision DNA repair (PubMed:20855601). The contribution to DNA
CC double-strand break repair appears to be largely indirect through
CC transcriptional regulation (PubMed:20687897). Involved in DNA
CC replication (PubMed:20237820). Required for microtubule assembly during
CC mitosis thereby regulating chromosome segregation cycle
CC (PubMed:20237820). {ECO:0000269|PubMed:16230350,
CC ECO:0000269|PubMed:16298340, ECO:0000269|PubMed:17721549,
CC ECO:0000269|PubMed:20237820, ECO:0000269|PubMed:20687897,
CC ECO:0000269|PubMed:20855601, ECO:0000269|PubMed:21303910}.
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:16298340, ECO:0000269|PubMed:21303910};
CC -!- ACTIVITY REGULATION: Activated upon binding to double stranded DNA or
CC nucleosomes. {ECO:0000269|PubMed:16298340,
CC ECO:0000269|PubMed:21303910}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=167 uM for ATP {ECO:0000269|PubMed:16298340};
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:16298340};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:16298340};
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex; three
CC different complex modules assemble on different domains of INO80
CC (PubMed:16230350, PubMed:18026119, PubMed:18922472, PubMed:21303910).
CC Interacts with DDB1 (PubMed:20855601). Interacts with transcriptional
CC repressor protein YY1; the interaction recruits the INO80 complex to
CC YY1 target genes (PubMed:17721549, PubMed:18026119). Interacts with
CC YY1AP1 (PubMed:27939641). Interacts with tubulin alpha
CC (PubMed:20237820). {ECO:0000269|PubMed:16230350,
CC ECO:0000269|PubMed:17721549, ECO:0000269|PubMed:18026119,
CC ECO:0000269|PubMed:18922472, ECO:0000269|PubMed:20237820,
CC ECO:0000269|PubMed:20855601, ECO:0000269|PubMed:21303910,
CC ECO:0000269|PubMed:27939641}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein Barr virus (EBV)
CC lytic switch protein BZLF1; this interaction participates to the
CC activation of early lytic viral genes by BZLF1.
CC {ECO:0000269|PubMed:30926617}.
CC -!- INTERACTION:
CC Q9ULG1; Q9H9F9: ACTR5; NbExp=8; IntAct=EBI-769345, EBI-769418;
CC Q9ULG1; Q16531: DDB1; NbExp=5; IntAct=EBI-769345, EBI-350322;
CC Q9ULG1; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-769345, EBI-742388;
CC Q9ULG1; P25490: YY1; NbExp=9; IntAct=EBI-769345, EBI-765538;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20237820}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00746, ECO:0000269|PubMed:16298340,
CC ECO:0000269|PubMed:18026119, ECO:0000269|PubMed:20237820,
CC ECO:0000269|PubMed:20971067}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:20237820}. Chromosome
CC {ECO:0000269|PubMed:20237820}. Note=Localizes to the cytoplasm in
CC quiescent cell (PubMed:20237820). Associates with spindle microtubules
CC during mitosis (PubMed:20237820). Colocalizes with PCNA at replication
CC forks during S-phase (PubMed:20237820). Recruited to DNA damage sites
CC in a ACTR8-dependent manner (PubMed:20971067).
CC {ECO:0000269|PubMed:20237820, ECO:0000269|PubMed:20971067}.
CC -!- TISSUE SPECIFICITY: According to PubMed:10574462, widely expressed.
CC According to PubMed:16298340, specifically expressed in brain, liver
CC and pancreas. {ECO:0000269|PubMed:10574462,
CC ECO:0000269|PubMed:16298340}.
CC -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC {ECO:0000269|PubMed:16298340}.
CC -!- MISCELLANEOUS: Although the ATP-dependent helicase activity displayed
CC by the INO80 complex requires INO80 ATPase activity, it is likely that
CC the helicase function is carried out by the other components of the
CC complex, RUVBL1 and RUVBL2, and not by INO80 itself.
CC {ECO:0000269|PubMed:16230350}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86573.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB033085; BAA86573.1; ALT_INIT; mRNA.
DR EMBL; CH471125; EAW92469.1; -; Genomic_DNA.
DR EMBL; BC146785; AAI46786.1; -; mRNA.
DR EMBL; AL137280; CAB70675.1; -; mRNA.
DR CCDS; CCDS10071.1; -.
DR PIR; T46350; T46350.
DR RefSeq; NP_060023.1; NM_017553.2.
DR PDB; 6HTS; EM; 4.80 A; G=267-1556.
DR PDB; 7ZI4; EM; 3.20 A; G=1-1556.
DR PDBsum; 6HTS; -.
DR PDBsum; 7ZI4; -.
DR AlphaFoldDB; Q9ULG1; -.
DR EMDB; EMD-14737; -.
DR EMDB; EMD-3954; -.
DR SMR; Q9ULG1; -.
DR BioGRID; 120076; 91.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR CORUM; Q9ULG1; -.
DR DIP; DIP-34296N; -.
DR IntAct; Q9ULG1; 35.
DR MINT; Q9ULG1; -.
DR STRING; 9606.ENSP00000497609; -.
DR GlyGen; Q9ULG1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9ULG1; -.
DR PhosphoSitePlus; Q9ULG1; -.
DR BioMuta; INO80; -.
DR DMDM; 114149322; -.
DR EPD; Q9ULG1; -.
DR jPOST; Q9ULG1; -.
DR MassIVE; Q9ULG1; -.
DR MaxQB; Q9ULG1; -.
DR PaxDb; 9606-ENSP00000355205; -.
DR PeptideAtlas; Q9ULG1; -.
DR ProteomicsDB; 85013; -.
DR Pumba; Q9ULG1; -.
DR Antibodypedia; 42067; 119 antibodies from 24 providers.
DR DNASU; 54617; -.
DR Ensembl; ENST00000648947.1; ENSP00000497609.1; ENSG00000128908.19.
DR GeneID; 54617; -.
DR KEGG; hsa:54617; -.
DR MANE-Select; ENST00000648947.1; ENSP00000497609.1; NM_017553.3; NP_060023.1.
DR UCSC; uc001zni.5; human.
DR AGR; HGNC:26956; -.
DR CTD; 54617; -.
DR DisGeNET; 54617; -.
DR GeneCards; INO80; -.
DR HGNC; HGNC:26956; INO80.
DR HPA; ENSG00000128908; Low tissue specificity.
DR MalaCards; INO80; -.
DR MIM; 610169; gene.
DR neXtProt; NX_Q9ULG1; -.
DR OpenTargets; ENSG00000128908; -.
DR Orphanet; 157949; Combined immunodeficiency with granulomatosis.
DR PharmGKB; PA162392040; -.
DR VEuPathDB; HostDB:ENSG00000128908; -.
DR eggNOG; KOG0388; Eukaryota.
DR GeneTree; ENSGT00900000141110; -.
DR HOGENOM; CLU_000315_19_1_1; -.
DR InParanoid; Q9ULG1; -.
DR OMA; FWKKNER; -.
DR OrthoDB; 5475375at2759; -.
DR PhylomeDB; Q9ULG1; -.
DR TreeFam; TF324408; -.
DR PathwayCommons; Q9ULG1; -.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; Q9ULG1; -.
DR SIGNOR; Q9ULG1; -.
DR BioGRID-ORCS; 54617; 524 hits in 1187 CRISPR screens.
DR ChiTaRS; INO80; human.
DR GenomeRNAi; 54617; -.
DR Pharos; Q9ULG1; Tbio.
DR PRO; PR:Q9ULG1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9ULG1; Protein.
DR Bgee; ENSG00000128908; Expressed in cardiac muscle of right atrium and 191 other cell types or tissues.
DR ExpressionAtlas; Q9ULG1; baseline and differential.
DR Genevisible; Q9ULG1; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043014; F:alpha-tubulin binding; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:UniProtKB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IMP:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:ComplexPortal.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IMP:UniProtKB.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; ISO:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; ISO:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IMP:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; ISO:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; ISO:ComplexPortal.
DR GO; GO:0070914; P:UV-damage excision repair; IMP:UniProtKB.
DR CDD; cd18002; DEXQc_INO80; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR031047; DEXQc_INO80.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45685:SF2; CHROMATIN-REMODELING ATPASE INO80; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF13892; DBINO; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51413; DBINO; 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; Actin-binding; ATP-binding; Cell cycle;
KW Cell division; Chromosome; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Host-virus interaction;
KW Hydrolase; Microtubule; Mitosis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1556
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000248829"
FT DOMAIN 280..405
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 530..701
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1105..1260
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..266
FT /note="Assembles INO80 complex module with putative
FT regulatory components INO80E, INO80F, UCHL5, NFRKB, MCRS1
FT and IN80D"
FT /evidence="ECO:0000269|PubMed:21303910"
FT REGION 46..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..526
FT /note="Assembles INO80 complex module consisting of
FT conserved components ACTR8, ACTL6A and YY1"
FT /evidence="ECO:0000269|PubMed:21303910"
FT REGION 219..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..1556
FT /note="Assembles INO80 complex module consisting of
FT conserved components INO80B, INO80C, ACTR5, RVBL1, RVBL2"
FT /evidence="ECO:0000269|PubMed:21303910"
FT REGION 1283..1316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1388..1408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..245
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1508..1556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 543..550
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 882
FT /note="I -> V (in dbSNP:rs34153025)"
FT /id="VAR_049500"
FT VARIANT 1108
FT /note="V -> G (in dbSNP:rs34178030)"
FT /id="VAR_061233"
FT MUTAGEN 653
FT /note="E->Q: Abolishes DNA-dependent ATPase and nucleosome
FT remodeling activities."
FT /evidence="ECO:0000269|PubMed:21303910"
SQ SEQUENCE 1556 AA; 176753 MW; 712A1EEA26D6A720 CRC64;
MASELGARDD GGCTELAKPL YLQYLERALR LDHFLRQTSA IFNRNISSDD SEDGLDDSNP
LLPQSGDPLI QVKEEPPNSL LGETSGAGSS GMLNTYSLNG VLQSESKCDK GNLYNFSKLK
KSRKWLKSIL LSDESSEADS QSEDDDEEEL NLSREELHNM LRLHKYKKLH QNKYSKDKEL
QQYQYYSAGL LSTYDPFYEQ QRHLLGPKKK KFKEEKKLKA KLKKVKKKRR RDEELSSEES
PRRHHHQTKV FAKFSHDAPP PGTKKKHLSI EQLNARRRKV WLSIVKKELP KANKQKASAR
NLFLTNSRKL AHQCMKEVRR AALQAQKNCK ETLPRARRLT KEMLLYWKKY EKVEKEHRKR
AEKEALEQRK LDEEMREAKR QQRKLNFLIT QTELYAHFMS RKRDMGHDGI QEEILRKLED
SSTQRQIDIG GGVVVNITQE DYDSNHFKAQ ALKNAENAYH IHQARTRSFD EDAKESRAAA
LRAANKSGTG FGESYSLANP SIRAGEDIPQ PTIFNGKLKG YQLKGMNWLA NLYEQGINGI
LADEMGLGKT VQSIALLAHL AERENIWGPF LIISPASTLN NWHQEFTRFV PKFKVLPYWG
NPHDRKVIRR FWSQKTLYTQ DAPFHVVITS YQLVVQDVKY FQRVKWQYMV LDEAQALKSS
SSVRWKILLQ FQCRNRLLLT GTPIQNTMAE LWALLHFIMP TLFDSHEEFN EWFSKDIESH
AENKSAIDEN QLSRLHMILK PFMLRRIKKD VENELSDKIE ILMYCQLTSR QKLLYQALKN
KISIEDLLQS SMGSTQQAQN TTSSLMNLVM QFRKVCNHPE LFERQETWSP FHISLKPYHI
SKFIYRHGQI RVFNHSRDRW LRVLSPFAPD YIQRSLFHRK GINEESCFSF LRFIDISPAE
MANLMLQGLL ARWLALFLSL KASYRLHQLR SWGAPEGESH QRYLRNKDFL LGVNFPLSFP
NLCSCPLLKS LVFSSHCKAV SGYSDQVVHQ RRSATSSLRR CLLTELPSFL CVASPRVTAV
PLDSYCNDRS AEYERRVLKE GGSLAAKQCL LNGAPELAAD WLNRRSQFFP EPAGGLWSIR
PQNGWSFIRI PGKESLITDS GKLYALDVLL TRLKSQGHRV LIYSQMTRMI DLLEEYMVYR
KHTYMRLDGS SKISERRDMV ADFQNRNDIF VFLLSTRAGG LGINLTAADT VIFYDSDWNP
TVDQQAMDRA HRLGQTKQVT VYRLICKGTI EERILQRAKE KSEIQRMVIS GGNFKPDTLK
PKEVVSLLLD DEELEKKLRL RQEEKRQQEE TNRVKERKRK REKYAEKKKK EDELDGKRRK
EGVNLVIPFV PSADNSNLSA DGDDSFISVD SAMPSPFSEI SISSELHTGS IPLDESSSDM
LVIVDDPASS APQSRATNSP ASITGSVSDT VNGISIQEMP AAGRGHSARS RGRPKGSGST
AKGAGKGRSR KSTAGSAAAM AGAKAGAAAA SAAAYAAYGY NVSKGISASS PLQTSLVRPA
GLADFGPSSA SSPLSSPLSK GNNVPGNPKN LHMTSSLAPD SLVRKQGKGT NPSGGR
//
