IN80C_HUMAN
ID IN80C_HUMAN Reviewed; 192 AA.
AC Q6PI98; B4DUI4; E9PCS7; Q86WR1; Q8N994;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=INO80 complex subunit C;
DE AltName: Full=IES6 homolog;
DE Short=hIes6;
GN Name=INO80C; Synonyms=C18orf37;
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] (ISOFORMS 2 AND 3).
RC TISSUE=Fetal brain, and Skeletal muscle;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
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 IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
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).
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.
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. Component of some
CC MLL1/MLL complex, at least composed of the core components KMT2A/MLL1,
CC ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative
CC components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1,
CC MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10.
CC {ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:16230350,
CC ECO:0000269|PubMed:18922472, ECO:0000269|PubMed:21303910}.
CC -!- INTERACTION:
CC Q6PI98; P50454: SERPINH1; NbExp=3; IntAct=EBI-722540, EBI-350723;
CC Q6PI98; P37173: TGFBR2; NbExp=3; IntAct=EBI-722540, EBI-296151;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18922472}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6PI98-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PI98-3; Sequence=VSP_014531;
CC Name=3;
CC IsoId=Q6PI98-4; Sequence=VSP_044967;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK095502; BAC04560.1; -; mRNA.
DR EMBL; AK300660; BAG62346.1; -; mRNA.
DR EMBL; AC007998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039404; AAH39404.1; -; mRNA.
DR CCDS; CCDS11914.1; -. [Q6PI98-1]
DR CCDS; CCDS45853.1; -. [Q6PI98-4]
DR RefSeq; NP_001092287.1; NM_001098817.1. [Q6PI98-4]
DR RefSeq; NP_919257.2; NM_194281.3. [Q6PI98-1]
DR AlphaFoldDB; Q6PI98; -.
DR SMR; Q6PI98; -.
DR BioGRID; 125928; 36.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR CORUM; Q6PI98; -.
DR IntAct; Q6PI98; 22.
DR STRING; 9606.ENSP00000467041; -.
DR iPTMnet; Q6PI98; -.
DR PhosphoSitePlus; Q6PI98; -.
DR BioMuta; INO80C; -.
DR DMDM; 68565181; -.
DR EPD; Q6PI98; -.
DR jPOST; Q6PI98; -.
DR MassIVE; Q6PI98; -.
DR MaxQB; Q6PI98; -.
DR PaxDb; Q6PI98; -.
DR PeptideAtlas; Q6PI98; -.
DR PRIDE; Q6PI98; -.
DR ProteomicsDB; 19504; -.
DR ProteomicsDB; 67147; -. [Q6PI98-1]
DR ProteomicsDB; 67148; -. [Q6PI98-3]
DR Antibodypedia; 62486; 31 antibodies from 14 providers.
DR DNASU; 125476; -.
DR Ensembl; ENST00000334598.12; ENSP00000334473.6; ENSG00000153391.16. [Q6PI98-1]
DR Ensembl; ENST00000441607.6; ENSP00000391457.1; ENSG00000153391.16. [Q6PI98-4]
DR Ensembl; ENST00000592173.5; ENSP00000465273.1; ENSG00000153391.16. [Q6PI98-3]
DR GeneID; 125476; -.
DR KEGG; hsa:125476; -.
DR MANE-Select; ENST00000334598.12; ENSP00000334473.6; NM_194281.4; NP_919257.2.
DR UCSC; uc002kyw.2; human. [Q6PI98-1]
DR CTD; 125476; -.
DR DisGeNET; 125476; -.
DR GeneCards; INO80C; -.
DR HGNC; HGNC:26994; INO80C.
DR HPA; ENSG00000153391; Low tissue specificity.
DR neXtProt; NX_Q6PI98; -.
DR OpenTargets; ENSG00000153391; -.
DR PharmGKB; PA162392132; -.
DR VEuPathDB; HostDB:ENSG00000153391; -.
DR eggNOG; KOG4137; Eukaryota.
DR GeneTree; ENSGT00390000014303; -.
DR HOGENOM; CLU_071116_0_1_1; -.
DR InParanoid; Q6PI98; -.
DR OMA; ATTQAQM; -.
DR OrthoDB; 1560268at2759; -.
DR PhylomeDB; Q6PI98; -.
DR TreeFam; TF323529; -.
DR PathwayCommons; Q6PI98; -.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; Q6PI98; -.
DR BioGRID-ORCS; 125476; 45 hits in 1095 CRISPR screens.
DR ChiTaRS; INO80C; human.
DR GenomeRNAi; 125476; -.
DR Pharos; Q6PI98; Tdark.
DR PRO; PR:Q6PI98; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q6PI98; protein.
DR Bgee; ENSG00000153391; Expressed in left testis and 179 other tissues.
DR ExpressionAtlas; Q6PI98; baseline and differential.
DR Genevisible; Q6PI98; HS.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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; IPR029525; INO80C/Ies6.
DR InterPro; IPR013272; Vps72/YL1_C.
DR PANTHER; PTHR31200; PTHR31200; 1.
DR Pfam; PF08265; YL1_C; 1.
DR SMART; SM00993; YL1_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA recombination; DNA repair; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..192
FT /note="INO80 complex subunit C"
FT /id="PRO_0000079317"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 52
FT /note="Q -> QTCLSPSTMIVRPPQPRGTTCLLPSAMIVRPPQPRGN (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044967"
FT VAR_SEQ 150..192
FT /note="ANYTDPQSKLRFSTIEEFSYIRRLPSDVVTGYLALRKATSIVP -> EPPNC
FT FPQRLHQLTFPLAMDEGSNFSRCSPTLVNFGFVFIMAILVGVK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014531"
FT CONFLICT 107
FT /note="N -> Y (in Ref. 1; BAG62346)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 20643 MW; 6EED290EB9E4E68E CRC64;
MAAQIPIVAT TSTPGIVRNS KKRPASPSHN GSSGGGYGAS KKKKASASSF AQGISMEAMS
ENKMVPSEFS TGPVEKAAKP LPFKDPNFVH SGHGGAVAGK KNRTWKNLKQ ILASERALPW
QLNDPNYFSI DAPPSFKPAK KYSDVSGLLA NYTDPQSKLR FSTIEEFSYI RRLPSDVVTG
YLALRKATSI VP