IN80D_HUMAN
ID IN80D_HUMAN Reviewed; 1027 AA.
AC Q53TQ3; B3KU68; B9EG77; Q6PJC6; Q6PJU1; Q6PKA1; Q9NXD5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=INO80 complex subunit D {ECO:0000305};
GN Name=INO80D {ECO:0000312|HGNC:HGNC:25997};
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 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].
RC TISSUE=Muscle, and Testis;
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 1-878, AND VARIANT VAL-358.
RC TISSUE=Fetal brain, and Hepatoma;
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 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 [6]
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 [7]
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, 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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-87, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Putative regulatory component of the chromatin remodeling
CC INO80 complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair.
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC specifically part of a complex module associated with the N-terminus of
CC INO80. {ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:18922472,
CC ECO:0000269|PubMed:21303910}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18922472}.
CC -!- SIMILARITY: Belongs to the INO80D family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04193.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH11687.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH11687.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH17290.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAX93069.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAA91079.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91079.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA91079.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=EAW70375.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007679; AAX93069.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC092677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471063; EAW70375.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC004193; AAH04193.2; ALT_SEQ; mRNA.
DR EMBL; BC011687; AAH11687.1; ALT_SEQ; mRNA.
DR EMBL; BC017290; AAH17290.2; ALT_SEQ; mRNA.
DR EMBL; BC136278; AAI36279.1; -; mRNA.
DR EMBL; AK000316; BAA91079.1; ALT_SEQ; mRNA.
DR EMBL; AK096585; BAG53330.1; -; mRNA.
DR CCDS; CCDS46500.1; -.
DR RefSeq; NP_060229.3; NM_017759.4.
DR RefSeq; XP_011509672.1; XM_011511370.2.
DR RefSeq; XP_011509673.1; XM_011511371.2.
DR RefSeq; XP_011509675.1; XM_011511373.2.
DR RefSeq; XP_011509677.1; XM_011511375.2.
DR RefSeq; XP_011509678.1; XM_011511376.2.
DR AlphaFoldDB; Q53TQ3; -.
DR BioGRID; 120238; 24.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR CORUM; Q53TQ3; -.
DR IntAct; Q53TQ3; 18.
DR MINT; Q53TQ3; -.
DR STRING; 9606.ENSP00000384198; -.
DR iPTMnet; Q53TQ3; -.
DR PhosphoSitePlus; Q53TQ3; -.
DR BioMuta; INO80D; -.
DR DMDM; 189045499; -.
DR EPD; Q53TQ3; -.
DR jPOST; Q53TQ3; -.
DR MassIVE; Q53TQ3; -.
DR MaxQB; Q53TQ3; -.
DR PaxDb; Q53TQ3; -.
DR PeptideAtlas; Q53TQ3; -.
DR PRIDE; Q53TQ3; -.
DR Antibodypedia; 51926; 55 antibodies from 14 providers.
DR DNASU; 54891; -.
DR Ensembl; ENST00000403263.6; ENSP00000384198.1; ENSG00000114933.16.
DR Ensembl; ENST00000636453.2; ENSP00000490850.1; ENSG00000283510.2.
DR GeneID; 54891; -.
DR KEGG; hsa:54891; -.
DR MANE-Select; ENST00000403263.6; ENSP00000384198.1; NM_017759.5; NP_060229.3.
DR UCSC; uc002vaz.4; human.
DR CTD; 54891; -.
DR DisGeNET; 54891; -.
DR GeneCards; INO80D; -.
DR HGNC; HGNC:25997; INO80D.
DR HPA; ENSG00000114933; Tissue enhanced (bone).
DR MIM; 619207; gene.
DR neXtProt; NX_Q53TQ3; -.
DR OpenTargets; ENSG00000114933; -.
DR PharmGKB; PA162392147; -.
DR VEuPathDB; HostDB:ENSG00000114933; -.
DR eggNOG; ENOG502QQC5; Eukaryota.
DR GeneTree; ENSGT00940000157974; -.
DR HOGENOM; CLU_329723_0_0_1; -.
DR InParanoid; Q53TQ3; -.
DR OMA; VKARHQM; -.
DR OrthoDB; 172254at2759; -.
DR PhylomeDB; Q53TQ3; -.
DR TreeFam; TF324169; -.
DR PathwayCommons; Q53TQ3; -.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; Q53TQ3; -.
DR BioGRID-ORCS; 54891; 18 hits in 1082 CRISPR screens.
DR ChiTaRS; INO80D; human.
DR GenomeRNAi; 54891; -.
DR Pharos; Q53TQ3; Tdark.
DR PRO; PR:Q53TQ3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q53TQ3; protein.
DR Bgee; ENSG00000114933; Expressed in bone marrow cell and 105 other tissues.
DR ExpressionAtlas; Q53TQ3; baseline and differential.
DR Genevisible; Q53TQ3; HS.
DR GO; GO:0031011; C:Ino80 complex; IDA:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IEA:Ensembl.
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:0000723; P:telomere maintenance; IEA:Ensembl.
DR InterPro; IPR025927; Potential_DNA-bd.
DR Pfam; PF13891; zf-C3Hc3H; 2.
PE 1: Evidence at protein level;
KW DNA damage; DNA recombination; DNA repair; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1027
FT /note="INO80 complex subunit D"
FT /id="PRO_0000319585"
FT REGION 193..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..558
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 358
FT /note="A -> V (in dbSNP:rs2909111)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_039012"
FT CONFLICT 517
FT /note="F -> S (in Ref. 4; BAA91079)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="T -> A (in Ref. 4; BAG53330)"
FT /evidence="ECO:0000305"
FT CONFLICT 822..828
FT /note="HSSPHGS -> AILPHPQ (in Ref. 4; BAA91079)"
FT /evidence="ECO:0000305"
FT CONFLICT 859..878
FT /note="TFSAEMPIMAQHLLPTQLEV -> PVCFRGYHRPASVAWGLLLN (in
FT Ref. 4; BAG53330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1027 AA; 113202 MW; FC5E886AF361295D CRC64;
MYEGKHIHFS EVDNKPLCSY SPKLCKQRRL NGYAFCIRHV LEDKTAPFKQ CEYVAKYNSQ
RCTNPIPKSE DRRYCNSHLQ VLGFIPKKER KKKNDPIDEV KVRHQMDTMA FSLTVPTLAL
KMPNGLDGMS LSPPGARVPL HYLETELEDP FAFNEEDDDL KKGATVRKKL QSKLAQNRQR
QRETEILKVR QEHFSPPPAP SQQQPPQQHS HLSPLSTSLK PPAPPQGSVC KSPQPQNTSL
PMQGVAPTTH TIAQARQLSH KRPLPLLPSS RAPTVDPPRT DRILMKATAF SPHFSCISRL
QRLVKLCTQK HQLDTDLFPH LGLDWSEESG EEPEDSEQAS PYQVAWSIRE TLRYQRHASD
DDDAESRSSR VTQLCTYFQQ KYKHLCRLER AESRQKKCRH TFRKALLQAA SKEPECTGQL
IQELRRAACS RTSISRTKLR EVEPAACSGT VKGEQCANKA LPFTRHCFQH ILLNHSQQLF
SSCTAKFADG QQCSVPVFDI THQTPLCEEH AKKMDNFLRG DNSRKVQHQQ QRKPRKKTKP
PALTKKHKKK RRRGPRRPQK PIPPAVPQGN LSMPASVSLP VEASHIRSPS TPELSADELP
DDIANEITDI PHDLELNQED FSDVLPRLPD DLQDFDFFEG KNGDLLPTTE EAEELERALQ
AVTSLECLST IGVLAQSDGV PVQELSDRGI GVFSTGTGAS GIQSLSREVN TDLGELLNGR
IVHDNFSSLE LDENLLRSAT LSNPPTPLAG QIQGQFSAPA NVGLTSATLI SQSALGERAF
PGQFHGLHDG SHASQRPHPA QLLSKADDLI TSRQQYSSDH SHSSPHGSHY DSEHVPSPYS
DHITSPHTTS YSGDNMAATF SAEMPIMAQH LLPTQLEVPL GGVVNPRTHW GNLPVNLGDP
SPFSNLLGAD GHLLSTSLST PPTTSNSETT QPAFATVTPS SSSVLPGLPQ TSFSGMGPSA
ELMASTSPKQ QLPQFSAAFG HQLSSHSGIP KDLQPSHSSI APPTGFTVTG ATATSTNNAS
SPFPSPN
