CHD3_HUMAN
ID CHD3_HUMAN Reviewed; 2000 AA.
AC Q12873; D3DTQ9; E9PG89; Q9Y4I0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 3.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 3;
DE Short=CHD-3;
DE EC=3.6.4.12 {ECO:0000269|PubMed:30397230};
DE AltName: Full=ATP-dependent helicase CHD3;
DE AltName: Full=Mi-2 autoantigen 240 kDa protein;
DE AltName: Full=Mi2-alpha;
DE AltName: Full=Zinc finger helicase;
DE Short=hZFH;
GN Name=CHD3;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=9688266; DOI=10.1046/j.1432-1327.1998.2540558.x;
RA Aubry F., Mattei M.-G., Galibert F.;
RT "Identification of a human 17p-located cDNA encoding a protein of the Snf2-
RT like helicase family.";
RL Eur. J. Biochem. 254:558-564(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1966 (ISOFORM 2).
RC TISSUE=Fetus;
RX PubMed=9326634; DOI=10.1073/pnas.94.21.11472;
RA Woodage T., Basrai M.A., Baxevanis A.D., Hieter P., Collins F.S.;
RT "Characterization of the CHD family of proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:11472-11477(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 121-654.
RC TISSUE=Thymus;
RX PubMed=7560064; DOI=10.1172/jci118218;
RA Ge Q., Nilasena D.S., O'Brien C.A., Frank M.B., Targoff I.N.;
RT "Molecular analysis of a major antigenic region of the 240 kD protein of
RT Mi-2 autoantigen.";
RL J. Clin. Invest. 96:1730-1737(1995).
RN [6]
RP IDENTIFICATION AS A COMPONENT OF THE NURD COMPLEX, AND FUNCTION.
RX PubMed=9804427; DOI=10.1038/27699;
RA Tong J.K., Hassig C.A., Schnitzler G.R., Kingston R.E., Schreiber S.L.;
RT "Chromatin deacetylation by an ATP-dependent nucleosome remodelling
RT complex.";
RL Nature 395:917-921(1998).
RN [7]
RP INTERACTION WITH TRIM28.
RX PubMed=11230151; DOI=10.1101/gad.869501;
RA Schultz D.C., Friedman J.R., Rauscher F.J. III;
RT "Targeting histone deacetylase complexes via KRAB-zinc finger proteins: the
RT PHD and bromodomains of KAP-1 form a cooperative unit that recruits a novel
RT isoform of the Mi-2alpha subunit of NuRD.";
RL Genes Dev. 15:428-443(2001).
RN [8]
RP INTERACTION WITH HANTAAN HANTAVIRUS NUCLEOPROTEIN (MICROBIAL INFECTION),
RP AND INTERACTION WITH SEOUL HANTAVIRUS NUCLEOPROTEIN (MICROBIAL INFECTION).
RX PubMed=14609633; DOI=10.1016/j.virusres.2003.09.001;
RA Lee B.H., Yoshimatsu K., Maeda A., Ochiai K., Morimatsu M., Araki K.,
RA Ogino M., Morikawa S., Arikawa J.;
RT "Association of the nucleocapsid protein of the Seoul and Hantaan
RT hantaviruses with small ubiquitin-like modifier-1-related molecules.";
RL Virus Res. 98:83-91(2003).
RN [9]
RP INTERACTION WITH HABP4 AND SERBP1.
RX PubMed=12505151; DOI=10.1016/s0014-5793(02)03737-7;
RA Lemos T.A., Passos D.O., Nery F.C., Kobarg J.;
RT "Characterization of a new family of proteins that interact with the C-
RT terminal region of the chromatin-remodeling factor CHD-3.";
RL FEBS Lett. 533:14-20(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324; SER-1601 AND SER-1605,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INTERACTION WITH PCNT, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17626165; DOI=10.1091/mbc.e06-07-0604;
RA Sillibourne J.E., Delaval B., Redick S., Sinha M., Doxsey S.J.;
RT "Chromatin remodeling proteins interact with pericentrin to regulate
RT centrosome integrity.";
RL Mol. Biol. Cell 18:3667-3680(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1601, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-1367; SER-1601 AND
RP SER-1605, AND IDENTIFICATION BY 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713; SER-1601 AND SER-1605,
RP AND 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1601 AND SER-1605, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-597; SER-713;
RP SER-1601; SER-1605 AND THR-1646, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1601, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1308, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-721, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [22]
RP FUNCTION, IDENTIFICATION IN THE NURD COMPLEX, INTERACTION WITH ZBED1,
RP SUBCELLULAR LOCATION, SUMOYLATION AT LYS-1971, AND MUTAGENESIS OF LYS-1971.
RX PubMed=27068747; DOI=10.1074/jbc.m115.713370;
RA Yamashita D., Moriuchi T., Osumi T., Hirose F.;
RT "Transcription Factor hDREF Is a Novel SUMO E3 Ligase of Mi2alpha.";
RL J. Biol. Chem. 291:11619-11634(2016).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-627; LYS-1308 AND LYS-1988, 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).
RN [24]
RP INVOLVEMENT IN SNIBCPS, AND VARIANT SNIBCPS TRP-1169.
RX PubMed=29463886; DOI=10.1038/s41380-018-0020-x;
RA Eising E., Carrion-Castillo A., Vino A., Strand E.A., Jakielski K.J.,
RA Scerri T.S., Hildebrand M.S., Webster R., Ma A., Mazoyer B., Francks C.,
RA Bahlo M., Scheffer I.E., Morgan A.T., Shriberg L.D., Fisher S.E.;
RT "A set of regulatory genes co-expressed in embryonic human brain is
RT implicated in disrupted speech development.";
RL Mol. Psychiatry 24:1065-1078(2019).
RN [25]
RP FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN SNIBCPS, VARIANTS SNIBCPS
RP 457-GLU--ASP-2000 DEL; ARG-886; PHE-915; LYS-921; GLU-961; GLN-985;
RP TRP-985; GLY-1109 DEL; HIS-1120; PRO-1121; ILE-1136; ARG-1158; LYS-1159;
RP ARG-1161; TRP-1169; ARG-1171; GLN-1172; PRO-1187; PRO-1236; GLN-1342 AND
RP LEU-1881, AND CHARACTERIZATION OF VARIANTS SNIBCPS PHE-915; PRO-1121;
RP ARG-1158; LYS-1159; GLN-1172 AND PRO-1187.
RX PubMed=30397230; DOI=10.1038/s41467-018-06014-6;
RA Snijders Blok L., Rousseau J., Twist J., Ehresmann S., Takaku M.,
RA Venselaar H., Rodan L.H., Nowak C.B., Douglas J., Swoboda K.J.,
RA Steeves M.A., Sahai I., Stumpel C.T.R.M., Stegmann A.P.A., Wheeler P.,
RA Willing M., Fiala E., Kochhar A., Gibson W.T., Cohen A.S.A., Agbahovbe R.,
RA Innes A.M., Au P.Y.B., Rankin J., Anderson I.J., Skinner S.A., Louie R.J.,
RA Warren H.E., Afenjar A., Keren B., Nava C., Buratti J., Isapof A.,
RA Rodriguez D., Lewandowski R., Propst J., van Essen T., Choi M., Lee S.,
RA Chae J.H., Price S., Schnur R.E., Douglas G., Wentzensen I.M., Zweier C.,
RA Reis A., Bialer M.G., Moore C., Koopmans M., Brilstra E.H., Monroe G.R.,
RA van Gassen K.L.I., van Binsbergen E., Newbury-Ecob R., Bownass L.,
RA Bader I., Mayr J.A., Wortmann S.B., Jakielski K.J., Strand E.A., Kloth K.,
RA Bierhals T., Roberts J.D., Petrovich R.M., Machida S., Kurumizaka H.,
RA Lelieveld S., Pfundt R., Jansen S., Deriziotis P., Faive L., Thevenon J.,
RA Assoum M., Shriberg L., Kleefstra T., Brunner H.G., Wade P.A., Fisher S.E.,
RA Campeau P.M.;
RT "CHD3 helicase domain mutations cause a neurodevelopmental syndrome with
RT macrocephaly and impaired speech and language.";
RL Nat. Commun. 9:4619-4619(2018).
CC -!- FUNCTION: Component of the histone deacetylase NuRD complex which
CC participates in the remodeling of chromatin by deacetylating histones
CC (PubMed:9804427, PubMed:30397230). Involved in transcriptional
CC repressiobn as part of the NuRD complex (PubMed:27068747). Required for
CC anchoring centrosomal pericentrin in both interphase and mitosis, for
CC spindle organization and centrosome integrity (PubMed:17626165).
CC {ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:27068747,
CC ECO:0000269|PubMed:30397230, ECO:0000269|PubMed:9804427}.
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; EC=3.6.4.12;
CC Evidence={ECO:0000269|PubMed:30397230};
CC -!- SUBUNIT: Central component of the nucleosome remodeling and histone
CC deacetylase (NuRD) repressive complex (PubMed:9804427,
CC PubMed:27068747). Interacts with TRIM28 (PubMed:11230151). Interacts
CC with SERBP1 (PubMed:12505151). Interacts (via its C-terminal) with
CC HABP4 (PubMed:12505151). Interacts with PCNT; the interaction regulates
CC centrosome integrity (PubMed:17626165). Interacts with ZBED1/hDREF
CC (PubMed:27068747). {ECO:0000269|PubMed:11230151,
CC ECO:0000269|PubMed:12505151, ECO:0000269|PubMed:17626165,
CC ECO:0000269|PubMed:27068747, ECO:0000269|PubMed:9804427}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Hantaan hantavirus
CC nucleoprotein. {ECO:0000269|PubMed:14609633}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Seoul hantavirus
CC nucleoprotein. {ECO:0000269|PubMed:14609633}.
CC -!- INTERACTION:
CC Q12873; Q99728: BARD1; NbExp=2; IntAct=EBI-523590, EBI-473181;
CC Q12873; P17844: DDX5; NbExp=4; IntAct=EBI-523590, EBI-351962;
CC Q12873; Q9Y2X7: GIT1; NbExp=2; IntAct=EBI-523590, EBI-466061;
CC Q12873; P42858: HTT; NbExp=3; IntAct=EBI-523590, EBI-466029;
CC Q12873; O60341: KDM1A; NbExp=4; IntAct=EBI-523590, EBI-710124;
CC Q12873; O75400: PRPF40A; NbExp=2; IntAct=EBI-523590, EBI-473291;
CC Q12873; Q8NC51: SERBP1; NbExp=5; IntAct=EBI-523590, EBI-523558;
CC Q12873; P61956: SUMO2; NbExp=3; IntAct=EBI-523590, EBI-473220;
CC Q12873; Q13263: TRIM28; NbExp=4; IntAct=EBI-523590, EBI-78139;
CC Q12873; O95365: ZBTB7A; NbExp=2; IntAct=EBI-523590, EBI-2795384;
CC -!- SUBCELLULAR LOCATION: Nucleus, PML body {ECO:0000269|PubMed:27068747}.
CC Nucleus {ECO:0000269|PubMed:17626165}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:17626165}. Note=Associates with centrosomes in
CC interphase and mitosis. {ECO:0000269|PubMed:17626165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q12873-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12873-2; Sequence=VSP_017231;
CC Name=3;
CC IsoId=Q12873-3; Sequence=VSP_047097;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9688266}.
CC -!- PTM: Sumoylation at Lys-1971 results in dissociation from chromatin and
CC suppression of transcriptional repression.
CC {ECO:0000269|PubMed:27068747}.
CC -!- DISEASE: Snijders Blok-Campeau syndrome (SNIBCPS) [MIM:618205]: An
CC autosomal dominant neurodevelopmental disorder characterized by
CC intellectual disability with a wide range of severity, developmental
CC delay, and impaired speech and language skills. Speech-related problems
CC include dysarthria, speech apraxia, oromotor problems, and stuttering.
CC Additional clinical features are macrocephaly, characteristic facial
CC features such as prominent forehead and hypertelorism, hypotonia, and
CC joint laxity. {ECO:0000269|PubMed:29463886,
CC ECO:0000269|PubMed:30397230}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: One of the main antigens reacting with anti-MI-2
CC positive sera of dermatomyositis. {ECO:0000269|PubMed:7560064}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB87383.1; Type=Miscellaneous discrepancy; Note=Differs from position 1967 onward for unknown reasons.; Evidence={ECO:0000305};
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DR EMBL; U91543; AAC39923.1; -; mRNA.
DR EMBL; AC104581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90114.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90116.1; -; Genomic_DNA.
DR EMBL; AF006515; AAB87383.1; ALT_TERM; mRNA.
DR EMBL; U08379; AAC50228.1; -; mRNA.
DR CCDS; CCDS32553.2; -. [Q12873-3]
DR CCDS; CCDS32554.1; -. [Q12873-1]
DR CCDS; CCDS32555.1; -. [Q12873-2]
DR RefSeq; NP_001005271.2; NM_001005271.2. [Q12873-3]
DR RefSeq; NP_001005273.1; NM_001005273.2. [Q12873-1]
DR RefSeq; NP_005843.2; NM_005852.3. [Q12873-2]
DR AlphaFoldDB; Q12873; -.
DR SMR; Q12873; -.
DR BioGRID; 107532; 726.
DR ComplexPortal; CPX-880; MBD2/NuRD nucleosome remodeling and deacetylase complex.
DR ComplexPortal; CPX-922; MBD3/NuRD nucleosome remodeling and deacetylase complex.
DR CORUM; Q12873; -.
DR DIP; DIP-32496N; -.
DR ELM; Q12873; -.
DR IntAct; Q12873; 157.
DR MINT; Q12873; -.
DR STRING; 9606.ENSP00000369716; -.
DR MoonDB; Q12873; Predicted.
DR GlyGen; Q12873; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12873; -.
DR MetOSite; Q12873; -.
DR PhosphoSitePlus; Q12873; -.
DR SwissPalm; Q12873; -.
DR BioMuta; CHD3; -.
DR DMDM; 88911273; -.
DR EPD; Q12873; -.
DR jPOST; Q12873; -.
DR MassIVE; Q12873; -.
DR MaxQB; Q12873; -.
DR PaxDb; Q12873; -.
DR PeptideAtlas; Q12873; -.
DR PRIDE; Q12873; -.
DR ProteomicsDB; 20268; -.
DR ProteomicsDB; 58995; -. [Q12873-1]
DR ProteomicsDB; 58996; -. [Q12873-2]
DR ABCD; Q12873; 1 sequenced antibody.
DR Antibodypedia; 12273; 314 antibodies from 38 providers.
DR DNASU; 1107; -.
DR Ensembl; ENST00000330494.12; ENSP00000332628.7; ENSG00000170004.18. [Q12873-1]
DR Ensembl; ENST00000358181.8; ENSP00000350907.4; ENSG00000170004.18. [Q12873-2]
DR Ensembl; ENST00000380358.9; ENSP00000369716.4; ENSG00000170004.18. [Q12873-3]
DR GeneID; 1107; -.
DR KEGG; hsa:1107; -.
DR MANE-Select; ENST00000330494.12; ENSP00000332628.7; NM_001005273.3; NP_001005273.1.
DR UCSC; uc002gjd.3; human. [Q12873-1]
DR CTD; 1107; -.
DR DisGeNET; 1107; -.
DR GeneCards; CHD3; -.
DR HGNC; HGNC:1918; CHD3.
DR HPA; ENSG00000170004; Low tissue specificity.
DR MalaCards; CHD3; -.
DR MIM; 602120; gene.
DR MIM; 618205; phenotype.
DR neXtProt; NX_Q12873; -.
DR OpenTargets; ENSG00000170004; -.
DR PharmGKB; PA26454; -.
DR VEuPathDB; HostDB:ENSG00000170004; -.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000158001; -.
DR HOGENOM; CLU_000315_22_2_1; -.
DR InParanoid; Q12873; -.
DR OMA; MIRKPVE; -.
DR OrthoDB; 54215at2759; -.
DR PhylomeDB; Q12873; -.
DR TreeFam; TF106448; -.
DR PathwayCommons; Q12873; -.
DR Reactome; R-HSA-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; Q12873; -.
DR SIGNOR; Q12873; -.
DR BioGRID-ORCS; 1107; 14 hits in 1097 CRISPR screens.
DR ChiTaRS; CHD3; human.
DR GeneWiki; CHD3; -.
DR GenomeRNAi; 1107; -.
DR Pharos; Q12873; Tbio.
DR PRO; PR:Q12873; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q12873; protein.
DR Bgee; ENSG00000170004; Expressed in cortical plate and 175 other tissues.
DR ExpressionAtlas; Q12873; baseline and differential.
DR Genevisible; Q12873; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IDA:BHF-UCL.
DR GO; GO:0016605; C:PML body; IDA: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:0140658; F:ATP-dependent chromatin remodeler activity; IDA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004386; F:helicase activity; NAS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0007098; P:centrosome cycle; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0016575; P:histone deacetylation; IDA:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042659; P:regulation of cell fate specification; IC:ComplexPortal.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0007051; P:spindle organization; IDA:UniProtKB.
DR Gene3D; 1.10.30.10; -; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06461; DUF1086; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF47095; SSF47095; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromatin regulator; Cytoplasm;
KW Cytoskeleton; Disease variant; DNA-binding; Helicase;
KW Host-virus interaction; Hydrolase; Intellectual disability;
KW Isopeptide bond; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..2000
FT /note="Chromodomain-helicase-DNA-binding protein 3"
FT /id="PRO_0000080227"
FT DOMAIN 494..594
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 631..673
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 748..932
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1064..1229
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 379..426
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 456..503
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 23..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1513..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1566..1966
FT /note="Required for interaction with PCNT"
FT /evidence="ECO:0000269|PubMed:17626165"
FT MOTIF 883..886
FT /note="DEAH box"
FT COMPBIAS 30..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..67
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..117
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..290
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..452
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1376..1396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1631..1707
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 761..768
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PDQ2"
FT MOD_RES 1367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 1538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT MOD_RES 1601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1646
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 627
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 721
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 721
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1238
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1308
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1573
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1585
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1876
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14839"
FT CROSSLNK 1971
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:27068747"
FT CROSSLNK 1988
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..32
FT /note="MKAADTVILWARSKNDQLRISFPPGLCWGDRM -> MASPLRDEEEEEEEMV
FT VSEEEEEEEEEGDEEEEEEVEAADEDDEEDDDEGVLGRGPGHDRGRDRHSPPGCHLFPP
FT PPPPPPPLPPPPPPPP (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047097"
FT VAR_SEQ 1642..1675
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9326634,
FT ECO:0000303|PubMed:9688266"
FT /id="VSP_017231"
FT VARIANT 3
FT /note="A -> V (in dbSNP:rs931543)"
FT /id="VAR_048728"
FT VARIANT 457..2000
FT /note="Missing (in SNIBCPS)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081506"
FT VARIANT 886
FT /note="H -> R (in SNIBCPS; dbSNP:rs1567855081)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081507"
FT VARIANT 915
FT /note="L -> F (in SNIBCPS; increased function in chromatin
FT remodeling; dbSNP:rs1567855669)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081508"
FT VARIANT 921
FT /note="E -> K (in SNIBCPS; dbSNP:rs1567855704)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081509"
FT VARIANT 961
FT /note="G -> E (in SNIBCPS; dbSNP:rs1567856045)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081510"
FT VARIANT 985
FT /note="R -> Q (in SNIBCPS; dbSNP:rs1567856331)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081511"
FT VARIANT 985
FT /note="R -> W (in SNIBCPS; dbSNP:rs1555611722)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081512"
FT VARIANT 1109
FT /note="Missing (in SNIBCPS; unknown pathological
FT significance; dbSNP:rs1567859975)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081513"
FT VARIANT 1120
FT /note="D -> H (in SNIBCPS; the patient also carries a
FT truncating variant in CIC; both variants may contribute to
FT disease phenotype)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081514"
FT VARIANT 1121
FT /note="R -> P (in SNIBCPS; decreased function in chromatin
FT remodeling; decreased ATPase activity; dbSNP:rs1567860112)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081515"
FT VARIANT 1136
FT /note="T -> I (in SNIBCPS; dbSNP:rs1567860640)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081516"
FT VARIANT 1158
FT /note="W -> R (in SNIBCPS; highly decreased function in
FT chromatin remodeling; dbSNP:rs1567860891)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081517"
FT VARIANT 1159
FT /note="N -> K (in SNIBCPS; highly decreased function in
FT chromatin remodeling; dbSNP:rs754919272)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081518"
FT VARIANT 1161
FT /note="H -> R (in SNIBCPS; dbSNP:rs1567860919)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081519"
FT VARIANT 1169
FT /note="R -> W (in SNIBCPS; dbSNP:rs1567861468)"
FT /evidence="ECO:0000269|PubMed:29463886,
FT ECO:0000269|PubMed:30397230"
FT /id="VAR_081520"
FT VARIANT 1171
FT /note="H -> R (in SNIBCPS; dbSNP:rs1567861489)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081521"
FT VARIANT 1172
FT /note="R -> Q (in SNIBCPS; decreased function in chromatin
FT remodeling; decreased ATPase activity; dbSNP:rs1567861501)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081522"
FT VARIANT 1187
FT /note="R -> P (in SNIBCPS; unknown pathological
FT significance; does not affect function in chromatin
FT remodeling; no effect on ATPase activity;
FT dbSNP:rs1567861571)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081523"
FT VARIANT 1236
FT /note="L -> P (in SNIBCPS; dbSNP:rs1567861894)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081524"
FT VARIANT 1342
FT /note="R -> Q (in SNIBCPS; dbSNP:rs1567863732)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081525"
FT VARIANT 1881
FT /note="R -> L (in SNIBCPS; dbSNP:rs1567877108)"
FT /evidence="ECO:0000269|PubMed:30397230"
FT /id="VAR_081526"
FT MUTAGEN 1971
FT /note="K->R: Abolishes sumoylation by ZBED1/hDREF and
FT increases binding to chromatin."
FT /evidence="ECO:0000269|PubMed:27068747"
FT CONFLICT 121..126
FT /note="GEGDGG -> PHFQQK (in Ref. 5; AAC50228)"
FT /evidence="ECO:0000305"
FT CONFLICT 309..312
FT /note="Missing (in Ref. 5; AAC50228)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="W -> G (in Ref. 5; AAC50228)"
FT /evidence="ECO:0000305"
FT CONFLICT 1704
FT /note="K -> N (in Ref. 1; AAC39923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2000 AA; 226592 MW; 4494F56E5D0E7083 CRC64;
MKAADTVILW ARSKNDQLRI SFPPGLCWGD RMPDKDDIRL LPSALGVKKR KRGPKKQKEN
KPGKPRKRKK RDSEEEFGSE RDEYREKSES GGSEYGTGPG RKRRRKHREK KEKKTKRRKK
GEGDGGQKQV EQKSSATLLL TWGLEDVEHV FSEEDYHTLT NYKAFSQFMR PLIAKKNPKI
PMSKMMTILG AKWREFSANN PFKGSAAAVA AAAAAAAAAV AEQVSAAVSS ATPIAPSGPP
ALPPPPAADI QPPPIRRAKT KEGKGPGHKR RSKSPRVPDG RKKLRGKKMA PLKIKLGLLG
GKRKKGGSYV FQSDEGPEPE AEESDLDSGS VHSASGRPDG PVRTKKLKRG RPGRKKKKVL
GCPAVAGEEE VDGYETDHQD YCEVCQQGGE IILCDTCPRA YHLVCLDPEL DRAPEGKWSC
PHCEKEGVQW EAKEEEEEYE EEGEEEGEKE EEDDHMEYCR VCKDGGELLC CDACISSYHI
HCLNPPLPDI PNGEWLCPRC TCPVLKGRVQ KILHWRWGEP PVAVPAPQQA DGNPDVPPPR
PLQGRSEREF FVKWVGLSYW HCSWAKELQL EIFHLVMYRN YQRKNDMDEP PPLDYGSGED
DGKSDKRKVK DPHYAEMEEK YYRFGIKPEW MTVHRIINHS VDKKGNYHYL VKWRDLPYDQ
STWEEDEMNI PEYEEHKQSY WRHRELIMGE DPAQPRKYKK KKKELQGDGP PSSPTNDPTV
KYETQPRFIT ATGGTLHMYQ LEGLNWLRFS WAQGTDTILA DEMGLGKTIQ TIVFLYSLYK
EGHTKGPFLV SAPLSTIINW EREFQMWAPK FYVVTYTGDK DSRAIIRENE FSFEDNAIKG
GKKAFKMKRE AQVKFHVLLT SYELITIDQA ALGSIRWACL VVDEAHRLKN NQSKFFRVLN
GYKIDHKLLL TGTPLQNNLE ELFHLLNFLT PERFNNLEGF LEEFADISKE DQIKKLHDLL
GPHMLRRLKA DVFKNMPAKT ELIVRVELSP MQKKYYKYIL TRNFEALNSR GGGNQVSLLN
IMMDLKKCCN HPYLFPVAAM ESPKLPSGAY EGGALIKSSG KLMLLQKMLR KLKEQGHRVL
IFSQMTKMLD LLEDFLDYEG YKYERIDGGI TGALRQEAID RFNAPGAQQF CFLLSTRAGG
LGINLATADT VIIFDSDWNP HNDIQAFSRA HRIGQANKVM IYRFVTRASV EERITQVAKR
KMMLTHLVVR PGLGSKAGSM SKQELDDILK FGTEELFKDE NEGENKEEDS SVIHYDNEAI
ARLLDRNQDA TEDTDVQNMN EYLSSFKVAQ YVVREEDKIE EIEREIIKQE ENVDPDYWEK
LLRHHYEQQQ EDLARNLGKG KRVRKQVNYN DAAQEDQDNQ SEYSVGSEEE DEDFDERPEG
RRQSKRQLRN EKDKPLPPLL ARVGGNIEVL GFNTRQRKAF LNAVMRWGMP PQDAFTTQWL
VRDLRGKTEK EFKAYVSLFM RHLCEPGADG SETFADGVPR EGLSRQQVLT RIGVMSLVKK
KVQEFEHING RWSMPELMPD PSADSKRSSR ASSPTKTSPT TPEASATNSP CTSKPATPAP
SEKGEGIRTP LEKEEAENQE EKPEKNSRIG EKMETEADAP SPAPSLGERL EPRKIPLEDE
VPGVPGEMEP EPGYRGDREK SATESTPGER GEEKPLDGQE HRERPEGETG DLGKREDVKG
DRELRPGPRD EPRSNGRREE KTEKPRFMFN IADGGFTELH TLWQNEERAA ISSGKLNEIW
HRRHDYWLLA GIVLHGYARW QDIQNDAQFA IINEPFKTEA NKGNFLEMKN KFLARRFKLL
EQALVIEEQL RRAAYLNLSQ EPAHPAMALH ARFAEAECLA ESHQHLSKES LAGNKPANAV
LHKVLNQLEE LLSDMKADVT RLPATLSRIP PIAARLQMSE RSILSRLASK GTEPHPTPAY
PPGPYATPPG YGAAFSAAPV GALAAAGANY SQMPAGSFIT AATNGPPVLV KKEKEMVGAL
VSDGLDRKEP RAGEVICIDD
