IN80B_HUMAN
ID IN80B_HUMAN Reviewed; 356 AA.
AC Q9C086;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=INO80 complex subunit B;
DE AltName: Full=High mobility group AT-hook 1-like 4;
DE AltName: Full=IES2 homolog;
DE Short=hIes2;
DE AltName: Full=PAP-1-associated protein 1;
DE Short=PAPA-1;
DE AltName: Full=Zinc finger HIT domain-containing protein 4;
GN Name=INO80B; Synonyms=HMGA1L4, PAPA1, ZNHIT4;
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-356, SUBCELLULAR LOCATION, INTERACTION WITH
RP RP9, AND FUNCTION.
RC TISSUE=Colon tumor;
RX PubMed=15556297; DOI=10.1016/j.gene.2004.05.025;
RA Kuroda T.S., Maita H., Tabata T., Taira T., Kitaura H., Ariga H.,
RA Iguchi-Ariga S.M.M.;
RT "A novel nucleolar protein, PAPA-1, induces growth arrest as a result of
RT cell cycle arrest at the G1 phase.";
RL Gene 340:83-98(2004).
RN [4]
RP IDENTIFICATION IN INO80 COMPLEX, AND IDENTIFICATION BY MASS 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 [5]
RP IDENTIFICATION IN THE INO80 COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS 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 [6]
RP IDENTIFICATION IN THE INO80 COMPLEX.
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).
CC -!- FUNCTION: Induces growth and cell cycle arrests at the G1 phase of the
CC cell cycle. {ECO:0000269|PubMed:15556297}.
CC -!- FUNCTION: Proposed core component of the chromatin remodeling INO80
CC complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. {ECO:0000269|PubMed:15556297}.
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC specifically part of a complex module associated with the helicase ATP-
CC binding and the helicase C-terminal domain of INO80. Interacts with
CC RP9. {ECO:0000269|PubMed:15556297, ECO:0000269|PubMed:16230350,
CC ECO:0000269|PubMed:18922472, ECO:0000269|PubMed:21303910}.
CC -!- INTERACTION:
CC Q9C086; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-715611, EBI-11096309;
CC Q9C086; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-715611, EBI-11524452;
CC Q9C086; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-715611, EBI-11519926;
CC Q9C086; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-715611, EBI-2548012;
CC Q9C086; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-715611, EBI-11983447;
CC Q9C086; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-715611, EBI-11530605;
CC Q9C086; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-715611, EBI-2559016;
CC Q9C086; Q15834: CCDC85B; NbExp=3; IntAct=EBI-715611, EBI-739674;
CC Q9C086; Q01850: CDR2; NbExp=3; IntAct=EBI-715611, EBI-1181367;
CC Q9C086; Q86X02: CDR2L; NbExp=3; IntAct=EBI-715611, EBI-11063830;
CC Q9C086; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-715611, EBI-739624;
CC Q9C086; P67870: CSNK2B; NbExp=3; IntAct=EBI-715611, EBI-348169;
CC Q9C086; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-715611, EBI-3867333;
CC Q9C086; Q7L190: DPPA4; NbExp=3; IntAct=EBI-715611, EBI-710457;
CC Q9C086; Q92997: DVL3; NbExp=3; IntAct=EBI-715611, EBI-739789;
CC Q9C086; Q96Q35-2: FLACC1; NbExp=3; IntAct=EBI-715611, EBI-11533409;
CC Q9C086; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-715611, EBI-5916454;
CC Q9C086; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-715611, EBI-2549423;
CC Q9C086; Q9UGU5: HMGXB4; NbExp=3; IntAct=EBI-715611, EBI-7261162;
CC Q9C086; P49639: HOXA1; NbExp=5; IntAct=EBI-715611, EBI-740785;
CC Q9C086; O75031: HSF2BP; NbExp=3; IntAct=EBI-715611, EBI-7116203;
CC Q9C086; P18065: IGFBP2; NbExp=4; IntAct=EBI-715611, EBI-2504392;
CC Q9C086; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-715611, EBI-2556193;
CC Q9C086; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-715611, EBI-11954971;
CC Q9C086; O76011: KRT34; NbExp=3; IntAct=EBI-715611, EBI-1047093;
CC Q9C086; Q6A162: KRT40; NbExp=3; IntAct=EBI-715611, EBI-10171697;
CC Q9C086; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-715611, EBI-10171774;
CC Q9C086; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-715611, EBI-10176379;
CC Q9C086; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-715611, EBI-12811111;
CC Q9C086; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-715611, EBI-11962084;
CC Q9C086; Q969G2: LHX4; NbExp=3; IntAct=EBI-715611, EBI-2865388;
CC Q9C086; P48059-3: LIMS1; NbExp=3; IntAct=EBI-715611, EBI-12864460;
CC Q9C086; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-715611, EBI-741037;
CC Q9C086; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-715611, EBI-10172526;
CC Q9C086; Q13064: MKRN3; NbExp=3; IntAct=EBI-715611, EBI-2340269;
CC Q9C086; Q6PF18: MORN3; NbExp=3; IntAct=EBI-715611, EBI-9675802;
CC Q9C086; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-715611, EBI-11522433;
CC Q9C086; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-715611, EBI-6952711;
CC Q9C086; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-715611, EBI-22310682;
CC Q9C086; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-715611, EBI-79165;
CC Q9C086; P78356-2: PIP4K2B; NbExp=3; IntAct=EBI-715611, EBI-11532361;
CC Q9C086; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-715611, EBI-2876622;
CC Q9C086; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-715611, EBI-302345;
CC Q9C086; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-715611, EBI-302355;
CC Q9C086; Q14498: RBM39; NbExp=3; IntAct=EBI-715611, EBI-395290;
CC Q9C086; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-715611, EBI-10182375;
CC Q9C086; Q9UN79: SOX13; NbExp=3; IntAct=EBI-715611, EBI-3928516;
CC Q9C086; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-715611, EBI-2212028;
CC Q9C086; Q96MF2: STAC3; NbExp=3; IntAct=EBI-715611, EBI-745680;
CC Q9C086; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-715611, EBI-741515;
CC Q9C086; Q08117-2: TLE5; NbExp=5; IntAct=EBI-715611, EBI-11741437;
CC Q9C086; Q63HR2: TNS2; NbExp=3; IntAct=EBI-715611, EBI-949753;
CC Q9C086; Q12933: TRAF2; NbExp=3; IntAct=EBI-715611, EBI-355744;
CC Q9C086; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-715611, EBI-492476;
CC Q9C086; P14373: TRIM27; NbExp=3; IntAct=EBI-715611, EBI-719493;
CC Q9C086; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-715611, EBI-947459;
CC Q9C086; P26368-2: U2AF2; NbExp=3; IntAct=EBI-715611, EBI-11097439;
CC Q9C086; Q495M9: USH1G; NbExp=3; IntAct=EBI-715611, EBI-8601749;
CC Q9C086; Q8IY57-5: YAF2; NbExp=3; IntAct=EBI-715611, EBI-12111538;
CC Q9C086; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-715611, EBI-11035148;
CC Q9C086; Q9H707: ZNF552; NbExp=3; IntAct=EBI-715611, EBI-2555731;
CC Q9C086; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-715611, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15556297,
CC ECO:0000269|PubMed:18922472}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:15556297}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21111.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC005041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050666; AAH50666.2; -; mRNA.
DR EMBL; BC064425; AAH64425.2; -; mRNA.
DR EMBL; AB054538; BAB21111.1; ALT_INIT; mRNA.
DR CCDS; CCDS1942.2; -.
DR RefSeq; NP_112578.2; NM_031288.3.
DR PDB; 6HTS; EM; 4.80 A; R=1-356.
DR PDBsum; 6HTS; -.
DR AlphaFoldDB; Q9C086; -.
DR SMR; Q9C086; -.
DR BioGRID; 123646; 302.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR CORUM; Q9C086; -.
DR IntAct; Q9C086; 92.
DR MINT; Q9C086; -.
DR STRING; 9606.ENSP00000233331; -.
DR iPTMnet; Q9C086; -.
DR PhosphoSitePlus; Q9C086; -.
DR BioMuta; INO80B; -.
DR DMDM; 229462939; -.
DR EPD; Q9C086; -.
DR jPOST; Q9C086; -.
DR MassIVE; Q9C086; -.
DR MaxQB; Q9C086; -.
DR PaxDb; Q9C086; -.
DR PeptideAtlas; Q9C086; -.
DR PRIDE; Q9C086; -.
DR ProteomicsDB; 79964; -.
DR Antibodypedia; 51509; 65 antibodies from 14 providers.
DR DNASU; 83444; -.
DR Ensembl; ENST00000233331.12; ENSP00000233331.7; ENSG00000115274.15.
DR GeneID; 83444; -.
DR KEGG; hsa:83444; -.
DR MANE-Select; ENST00000233331.12; ENSP00000233331.7; NM_031288.4; NP_112578.2.
DR UCSC; uc002slg.3; human.
DR CTD; 83444; -.
DR DisGeNET; 83444; -.
DR GeneCards; INO80B; -.
DR HGNC; HGNC:13324; INO80B.
DR HPA; ENSG00000115274; Low tissue specificity.
DR MIM; 616456; gene.
DR neXtProt; NX_Q9C086; -.
DR OpenTargets; ENSG00000115274; -.
DR PharmGKB; PA162392117; -.
DR VEuPathDB; HostDB:ENSG00000115274; -.
DR eggNOG; ENOG502QUQX; Eukaryota.
DR GeneTree; ENSGT00390000001754; -.
DR HOGENOM; CLU_070409_0_0_1; -.
DR InParanoid; Q9C086; -.
DR OMA; PDAKICA; -.
DR OrthoDB; 1111317at2759; -.
DR PhylomeDB; Q9C086; -.
DR TreeFam; TF105373; -.
DR PathwayCommons; Q9C086; -.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; Q9C086; -.
DR BioGRID-ORCS; 83444; 272 hits in 1087 CRISPR screens.
DR GenomeRNAi; 83444; -.
DR Pharos; Q9C086; Tbio.
DR PRO; PR:Q9C086; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9C086; protein.
DR Bgee; ENSG00000115274; Expressed in sural nerve and 92 other tissues.
DR ExpressionAtlas; Q9C086; baseline and differential.
DR Genevisible; Q9C086; HS.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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 InterPro; IPR029523; INO80B/Ies2.
DR InterPro; IPR006880; INO80B_C.
DR InterPro; IPR007529; Znf_HIT.
DR PANTHER; PTHR21561; PTHR21561; 1.
DR Pfam; PF04795; PAPA-1; 1.
DR Pfam; PF04438; zf-HIT; 1.
DR SMART; SM01406; PAPA-1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; DNA damage; DNA recombination; DNA repair;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..356
FT /note="INO80 complex subunit B"
FT /id="PRO_0000173554"
FT ZN_FING 305..336
FT /note="HIT-type"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 213..245
FT /evidence="ECO:0000255"
FT COMPBIAS 32..51
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..310
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PT3"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PT3"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PT3"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PT3"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PT3"
FT VARIANT 152
FT /note="W -> G (in dbSNP:rs1054209)"
FT /id="VAR_055083"
FT CONFLICT 2
FT /note="S -> G (in Ref. 3; BAB21111)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 38637 MW; 235C836556B5F91F CRC64;
MSKLWRRGST SGAMEAPEPG EALELSLAGA HGHGVHKKKH KKHKKKHKKK HHQEEDAGPT
QPSPAKPQLK LKIKLGGQVL GTKSVPTFTV IPEGPRSPSP LMVVDNEEEP MEGVPLEQYR
AWLDEDSNLS PSPLRDLSGG LGGQEEEEEQ RWLDALEKGE LDDNGDLKKE INERLLTARQ
RALLQKARSQ PSPMLPLPVA EGCPPPALTE EMLLKREERA RKRRLQAARR AEEHKNQTIE
RLTKTAATSG RGGRGGARGE RRGGRAAAPA PMVRYCSGAQ GSTLSFPPGV PAPTAVSQRP
SPSGPPPRCS VPGCPHPRRY ACSRTGQALC SLQCYRINLQ MRLGGPEGPG SPLLAT
