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INO80_HUMAN
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   03-AUG-2022, entry version 175.
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).
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   -!- 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   PDBsum; 6HTS; -.
DR   AlphaFoldDB; Q9ULG1; -.
DR   SMR; Q9ULG1; -.
DR   BioGRID; 120076; 80.
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.ENSP00000355205; -.
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; Q9ULG1; -.
DR   PeptideAtlas; Q9ULG1; -.
DR   PRIDE; Q9ULG1; -.
DR   ProteomicsDB; 85013; -.
DR   Antibodypedia; 42067; 90 antibodies from 24 providers.
DR   DNASU; 54617; -.
DR   Ensembl; ENST00000401393.7; ENSP00000384686.3; ENSG00000128908.18.
DR   Ensembl; ENST00000648947.1; ENSP00000497609.1; ENSG00000128908.18.
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   CTD; 54617; -.
DR   DisGeNET; 54617; -.
DR   GeneCards; INO80; -.
DR   HGNC; HGNC:26956; INO80.
DR   HPA; ENSG00000128908; Low tissue specificity.
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; 188211at2759; -.
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   BioGRID-ORCS; 54617; 500 hits in 1105 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 190 other 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: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; IEA:Ensembl.
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; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
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: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; IEA:Ensembl.
DR   GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:UniProtKB.
DR   GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR   GO; GO:0051225; P:spindle assembly; IMP:UniProtKB.
DR   GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0070914; P:UV-damage excision repair; IMP:UniProtKB.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR020838; DBINO.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR031047; Ino80.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45685:SF2; PTHR45685:SF2; 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; SSF52540; 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; Hydrolase; Microtubule;
KW   Mitosis; Nucleotide-binding; Nucleus; 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
 
 
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