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 22-FEB-2023, entry version 226. DE RecName: Full=Chromodomain-helicase-DNA-binding protein 3; DE Short=CHD-3; DE EC=3.6.4.12 {ECO:0000269|PubMed:28977666, 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 FUNCTION, IDENTIFICATION IN THE NURD COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=16428440; DOI=10.1128/mcb.26.3.843-851.2006; RA Le Guezennec X., Vermeulen M., Brinkman A.B., Hoeijmakers W.A., Cohen A., RA Lasonder E., Stunnenberg H.G.; RT "MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical RT and functional properties."; RL Mol. Cell. Biol. 26:843-851(2006). RN [12] 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 [13] 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE NURD COMPLEX, RP INTERACTION WITH CBX1; CBX3; CBX5; MTA2; HDAC1 AND RBBP7, IDENTIFICATION BY RP MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=28977666; DOI=10.1093/nar/gkx711; RA Hoffmeister H., Fuchs A., Erdel F., Pinz S., Groebner-Ferreira R., RA Bruckmann A., Deutzmann R., Schwartz U., Maldonado R., Huber C., RA Dendorfer A.S., Rippe K., Laengst G.; RT "CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping RT functionality."; RL Nucleic Acids Res. 45:10534-10554(2017). RN [26] RP IDENTIFICATION IN THE NURD COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, RP AND SUBCELLULAR LOCATION. RX PubMed=33283408; DOI=10.1111/febs.15650; RA Spruijt C.G., Graewe C., Kleinendorst S.C., Baltissen M.P.A., Vermeulen M.; RT "Cross-linking mass spectrometry reveals the structural topology of RT peripheral NuRD subunits relative to the core complex."; RL FEBS J. 288:3231-3245(2021). RN [27] RP VARIANT SNIBCPS TRP-1169, AND INVOLVEMENT IN SNIBCPS. 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 [28] RP VARIANTS SNIBCPS 457-GLU--ASP-2000 DEL; ARG-886; PHE-915; LYS-921; GLU-961; RP GLN-985; TRP-985; GLY-1109 DEL; HIS-1120; PRO-1121; ILE-1136; ARG-1158; RP LYS-1159; ARG-1161; TRP-1169; ARG-1171; GLN-1172; PRO-1187; PRO-1236; RP GLN-1342 AND LEU-1881, FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN RP SNIBCPS, 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: ATP-dependent helicase that binds and distorts nucleosomal CC DNA (PubMed:28977666). Acts as a component of the histone deacetylase CC NuRD complex which participates in the remodeling of chromatin CC (PubMed:9804427, PubMed:30397230, PubMed:16428440, PubMed:28977666). CC Involved in transcriptional repression as part of the NuRD complex CC (PubMed:27068747). Required for anchoring centrosomal pericentrin in CC both interphase and mitosis, for spindle organization and centrosome CC integrity (PubMed:17626165). {ECO:0000269|PubMed:16428440, CC ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:27068747, CC ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:30397230, CC 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:28977666, ECO:0000269|PubMed:30397230}; CC -!- SUBUNIT: Component of the nucleosome remodeling and deacetylase (NuRD) CC repressor complex, composed of core proteins MTA1, MTA2, MTA3, RBBP4, CC RBBP7, HDAC1, HDAC2, MBD2, MBD3, and peripherally associated proteins CC CDK2AP1, CDK2AP2, GATAD2A, GATAD2B, CHD3, CHD4 and CHD5 CC (PubMed:33283408, PubMed:9804427, PubMed:27068747, PubMed:28977666, CC PubMed:16428440). The exact stoichiometry of the NuRD complex is CC unknown, and some subunits such as MBD2 and MBD3, GATAD2A and GATAD2B, CC and CHD3, CHD4 and CHD5 define mutually exclusive NuRD complexes CC (PubMed:28977666, PubMed:16428440, PubMed:33283408). Interacts with CC CBX1 (PubMed:28977666). Interacts with CBX3 (PubMed:28977666). CC Interacts with CBX5 (PubMed:28977666). Interacts (via its C-terminal) CC with HABP4 (PubMed:12505151). Interacts with HDAC1 (PubMed:28977666). CC Interacts with MTA1 (PubMed:28977666). Interacts with PCNT; the CC interaction regulates centrosome integrity (PubMed:17626165). Interacts CC with RBBP7 (PubMed:28977666). Interacts with SERBP1 (PubMed:12505151). CC Interacts with TRIM28 (PubMed:11230151). Interacts with ZBED1/hDREF CC (PubMed:27068747). {ECO:0000269|PubMed:11230151, CC ECO:0000269|PubMed:12505151, ECO:0000269|PubMed:16428440, CC ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:27068747, CC ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:33283408, CC 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, ECO:0000269|PubMed:28977666, CC ECO:0000269|PubMed:33283408}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:17626165}. CC Note=Associates with centrosomes in interphase and mitosis CC (PubMed:17626165). Localizes to sites of DNA damage (PubMed:28977666). CC {ECO:0000269|PubMed:17626165, ECO:0000269|PubMed:28977666}. 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:28977666, CC 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}; 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; 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; 743. 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; 158. DR MINT; Q12873; -. DR STRING; 9606.ENSP00000369716; -. DR MoonDB; Q12873; Predicted. DR GlyCosmos; Q12873; 1 site, 1 glycan. 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 ProteomicsDB; 20268; -. DR ProteomicsDB; 58995; -. [Q12873-1] DR ProteomicsDB; 58996; -. [Q12873-2] DR ABCD; Q12873; 1 sequenced antibody. DR Antibodypedia; 12273; 315 antibodies from 38 providers. DR DNASU; 1107; -. DR Ensembl; ENST00000330494.12; ENSP00000332628.7; ENSG00000170004.19. [Q12873-1] DR Ensembl; ENST00000358181.8; ENSP00000350907.4; ENSG00000170004.19. [Q12873-2] DR Ensembl; ENST00000380358.9; ENSP00000369716.4; ENSG00000170004.19. [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 AGR; HGNC:1918; -. 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 Orphanet; 599082; CHD3-related developmental delay-speech delay-intellectual disability-abnormalities of vision-facial dysmorphism syndrome. 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; 2910821at2759; -. 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; 17 hits in 1183 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:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. 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:0045892; P:negative regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:0042659; P:regulation of cell fate specification; NAS:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:2000736; P:regulation of stem cell differentiation; NAS:ComplexPortal. DR GO; GO:0007051; P:spindle organization; IDA:UniProtKB. DR CDD; cd18667; CD1_tandem_CHD3-4_like; 1. DR CDD; cd18662; CD2_tandem_CHD3-4_like; 1. DR CDD; cd18055; DEXHc_CHD3; 1. DR CDD; cd15531; PHD1_CHD_II; 1. DR CDD; cd15532; PHD2_CHD_II; 1. DR CDD; cd18793; SF2_C_SNF; 1. DR Gene3D; 2.40.50.40; -; 2. DR Gene3D; 1.10.30.10; High mobility group box domain; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2. 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 PANTHER; PTHR45623:SF9; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3; 1. DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1. DR Pfam; PF08074; CHDCT2; 1. DR Pfam; PF06461; CHDII_SANT-like; 1. DR Pfam; PF08073; CHDNT; 1. DR Pfam; PF00385; Chromo; 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; SSF54160; Chromo domain-like; 2. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF47095; HMG-box; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. 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 //