IN80E_HUMAN
ID IN80E_HUMAN Reviewed; 244 AA.
AC Q8NBZ0; Q6Y2K3;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=INO80 complex subunit E;
DE AltName: Full=Coiled-coil domain-containing protein 95;
GN Name=INO80E; Synonyms=CCDC95;
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 [MRNA] (ISOFORM 2).
RA Wan D.F., Qin W.X., Zhou X.M., Zhang P.P., Jiang H.Q., Gu J.R.;
RT "Novel human cDNA clones with function of inhibiting growth of liver cancer
RT cells.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [6]
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 [7]
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 [8]
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 [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-159 AND LYS-171, AND
RP IDENTIFICATION BY MASS 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 -!- INTERACTION:
CC Q8NBZ0; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-769401, EBI-396137;
CC Q8NBZ0; Q86V42: FAM124A; NbExp=3; IntAct=EBI-769401, EBI-744506;
CC Q8NBZ0; Q3B820: FAM161A; NbExp=3; IntAct=EBI-769401, EBI-719941;
CC Q8NBZ0; P55040: GEM; NbExp=6; IntAct=EBI-769401, EBI-744104;
CC Q8NBZ0; P42858: HTT; NbExp=3; IntAct=EBI-769401, EBI-466029;
CC Q8NBZ0; P52292: KPNA2; NbExp=3; IntAct=EBI-769401, EBI-349938;
CC Q8NBZ0; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-769401, EBI-739832;
CC Q8NBZ0; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-769401, EBI-10268010;
CC Q8NBZ0; Q96EZ8: MCRS1; NbExp=8; IntAct=EBI-769401, EBI-348259;
CC Q8NBZ0; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-769401, EBI-10269566;
CC Q8NBZ0; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-769401, EBI-2339674;
CC Q8NBZ0; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-769401, EBI-79165;
CC Q8NBZ0; Q13526: PIN1; NbExp=3; IntAct=EBI-769401, EBI-714158;
CC Q8NBZ0; Q13131: PRKAA1; NbExp=3; IntAct=EBI-769401, EBI-1181405;
CC Q8NBZ0; P25786: PSMA1; NbExp=3; IntAct=EBI-769401, EBI-359352;
CC Q8NBZ0; O00560: SDCBP; NbExp=6; IntAct=EBI-769401, EBI-727004;
CC Q8NBZ0; Q05BL0: TBRG1; NbExp=3; IntAct=EBI-769401, EBI-10223693;
CC Q8NBZ0; Q08117-2: TLE5; NbExp=3; IntAct=EBI-769401, EBI-11741437;
CC Q8NBZ0; O95379: TNFAIP8; NbExp=3; IntAct=EBI-769401, EBI-1049336;
CC Q8NBZ0; Q9Y5K5: UCHL5; NbExp=7; IntAct=EBI-769401, EBI-1051183;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18922472}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NBZ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NBZ0-2; Sequence=VSP_055984;
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DR EMBL; AY189289; AAO86733.1; -; mRNA.
DR EMBL; AK075133; BAC11424.1; -; mRNA.
DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471238; EAW79953.1; -; Genomic_DNA.
DR EMBL; CH471238; EAW79956.1; -; Genomic_DNA.
DR EMBL; CH471238; EAW79959.1; -; Genomic_DNA.
DR EMBL; BC047712; AAH47712.1; -; mRNA.
DR CCDS; CCDS10665.1; -. [Q8NBZ0-1]
DR RefSeq; NP_001291491.1; NM_001304562.1.
DR RefSeq; NP_001291492.1; NM_001304563.1.
DR RefSeq; NP_775889.1; NM_173618.2. [Q8NBZ0-1]
DR AlphaFoldDB; Q8NBZ0; -.
DR BioGRID; 129701; 75.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR CORUM; Q8NBZ0; -.
DR IntAct; Q8NBZ0; 45.
DR MINT; Q8NBZ0; -.
DR STRING; 9606.ENSP00000457016; -.
DR iPTMnet; Q8NBZ0; -.
DR PhosphoSitePlus; Q8NBZ0; -.
DR BioMuta; INO80E; -.
DR DMDM; 74730149; -.
DR EPD; Q8NBZ0; -.
DR jPOST; Q8NBZ0; -.
DR MassIVE; Q8NBZ0; -.
DR MaxQB; Q8NBZ0; -.
DR PaxDb; Q8NBZ0; -.
DR PeptideAtlas; Q8NBZ0; -.
DR PRIDE; Q8NBZ0; -.
DR ProteomicsDB; 67833; -.
DR ProteomicsDB; 72835; -. [Q8NBZ0-1]
DR Antibodypedia; 51751; 36 antibodies from 10 providers.
DR DNASU; 283899; -.
DR Ensembl; ENST00000562441.5; ENSP00000456073.1; ENSG00000169592.15. [Q8NBZ0-2]
DR Ensembl; ENST00000563197.6; ENSP00000457016.1; ENSG00000169592.15. [Q8NBZ0-1]
DR Ensembl; ENST00000567065.5; ENSP00000454665.1; ENSG00000169592.15. [Q8NBZ0-2]
DR Ensembl; ENST00000620599.4; ENSP00000484187.1; ENSG00000169592.15. [Q8NBZ0-2]
DR GeneID; 283899; -.
DR KEGG; hsa:283899; -.
DR MANE-Select; ENST00000563197.6; ENSP00000457016.1; NM_173618.3; NP_775889.1.
DR UCSC; uc002dvg.2; human. [Q8NBZ0-1]
DR CTD; 283899; -.
DR DisGeNET; 283899; -.
DR GeneCards; INO80E; -.
DR HGNC; HGNC:26905; INO80E.
DR HPA; ENSG00000169592; Low tissue specificity.
DR neXtProt; NX_Q8NBZ0; -.
DR OpenTargets; ENSG00000169592; -.
DR PharmGKB; PA162392174; -.
DR VEuPathDB; HostDB:ENSG00000169592; -.
DR eggNOG; ENOG502RZ5F; Eukaryota.
DR GeneTree; ENSGT00390000011918; -.
DR InParanoid; Q8NBZ0; -.
DR OMA; EMNGQTD; -.
DR OrthoDB; 1299948at2759; -.
DR PhylomeDB; Q8NBZ0; -.
DR TreeFam; TF326931; -.
DR PathwayCommons; Q8NBZ0; -.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; Q8NBZ0; -.
DR BioGRID-ORCS; 283899; 50 hits in 1092 CRISPR screens.
DR ChiTaRS; INO80E; human.
DR GenomeRNAi; 283899; -.
DR Pharos; Q8NBZ0; Tdark.
DR PRO; PR:Q8NBZ0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8NBZ0; protein.
DR Bgee; ENSG00000169592; Expressed in granulocyte and 166 other tissues.
DR ExpressionAtlas; Q8NBZ0; baseline and differential.
DR Genevisible; Q8NBZ0; HS.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IPR026678; INO80E.
DR PANTHER; PTHR21812; PTHR21812; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA damage; DNA recombination;
KW DNA repair; Isopeptide bond; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..244
FT /note="INO80 complex subunit E"
FT /id="PRO_0000234292"
FT REGION 63..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 10..54
FT /evidence="ECO:0000255"
FT COMPBIAS 72..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 159
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 133..244
FT /note="LASSRYPPFPSDYLALQLPEPSPLRPKREKRPRLPRKLKMAVGPPDCPVGGP
FT LTFPGRGSGAGVGTTLTPLPPPKMPPPTILSTVPRQMFSDAGSGDDALDGDDDLVIDIP
FT E -> ERGQA (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_055984"
SQ SEQUENCE 244 AA; 26478 MW; F329B39D0F3EB253 CRC64;
MNGPADGEVD YKKKYRNLKR KLKFLIYEHE CFQEELRKAQ RKLLKVSRDK SFLLDRLLQY
ENVDEDSSDS DATASSDNSE TEGTPKLSDT PAPKRKRSPP LGGAPSPSSL SLPPSTGFPL
QASGVPSPYL SSLASSRYPP FPSDYLALQL PEPSPLRPKR EKRPRLPRKL KMAVGPPDCP
VGGPLTFPGR GSGAGVGTTL TPLPPPKMPP PTILSTVPRQ MFSDAGSGDD ALDGDDDLVI
DIPE
