ID CHD2_HUMAN Reviewed; 1828 AA.
AC O14647; C6G482; Q96IP5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 27-MAR-2024, entry version 202.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 2;
DE Short=CHD-2;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase CHD2;
GN Name=CHD2;
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).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Skin;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1635-1828 (ISOFORM 1).
RC TISSUE=T-cell;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-240 AND SER-242, AND
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-208, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-208; THR-240 AND
RP SER-242, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1365; SER-1386 AND SER-1807,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-208; SER-1085 AND
RP SER-1087, AND IDENTIFICATION BY 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 [14]
RP VARIANTS DEE94 121-ARG--THR-1828 DEL; ARG-548 AND PRO-823.
RX PubMed=23708187; DOI=10.1038/ng.2646;
RA Carvill G.L., Heavin S.B., Yendle S.C., McMahon J.M., O'Roak B.J., Cook J.,
RA Khan A., Dorschner M.O., Weaver M., Calvert S., Malone S., Wallace G.,
RA Stanley T., Bye A.M., Bleasel A., Howell K.B., Kivity S., Mackay M.T.,
RA Rodriguez-Casero V., Webster R., Korczyn A., Afawi Z., Zelnick N.,
RA Lerman-Sagie T., Lev D., Moeller R.S., Gill D., Andrade D.M., Freeman J.L.,
RA Sadleir L.G., Shendure J., Berkovic S.F., Scheffer I.E., Mefford H.C.;
RT "Targeted resequencing in epileptic encephalopathies identifies de novo
RT mutations in CHD2 and SYNGAP1.";
RL Nat. Genet. 45:825-830(2013).
RN [15]
RP VARIANT DEE94 112-SER--THR-1828 DEL.
RX PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
RA Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C., Patry L.,
RA Massicotte C., Ambalavanan A., Spiegelman D., Diallo O., Henrion E.,
RA Dionne-Laporte A., Fougerat A., Pshezhetsky A.V., Venkateswaran S.,
RA Rouleau G.A., Michaud J.L.;
RT "De novo mutations in moderate or severe intellectual disability.";
RL PLoS Genet. 10:E1004772-E1004772(2014).
RN [16]
RP VARIANT 178-ARG--THR-1828 DEL.
RX PubMed=33798445; DOI=10.1016/j.ajhg.2021.03.013;
RA Courage C., Oliver K.L., Park E.J., Cameron J.M., Grabinska K.A., Muona M.,
RA Canafoglia L., Gambardella A., Said E., Afawi Z., Baykan B., Brandt C.,
RA di Bonaventura C., Chew H.B., Criscuolo C., Dibbens L.M., Castellotti B.,
RA Riguzzi P., Labate A., Filla A., Giallonardo A.T., Berecki G.,
RA Jackson C.B., Joensuu T., Damiano J.A., Kivity S., Korczyn A., Palotie A.,
RA Striano P., Uccellini D., Giuliano L., Andermann E., Scheffer I.E.,
RA Michelucci R., Bahlo M., Franceschetti S., Sessa W.C., Berkovic S.F.,
RA Lehesjoki A.E.;
RT "Progressive myoclonus epilepsies-Residual unsolved cases have marked
RT genetic heterogeneity including dolichol-dependent protein glycosylation
RT pathway genes.";
RL Am. J. Hum. Genet. 108:722-738(2021).
CC -!- FUNCTION: DNA-binding helicase that specifically binds to the promoter
CC of target genes, leading to chromatin remodeling, possibly by promoting
CC deposition of histone H3.3. Involved in myogenesis via interaction with
CC MYOD1: binds to myogenic gene regulatory sequences and mediates
CC incorporation of histone H3.3 prior to the onset of myogenic gene
CC expression, promoting their expression (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Interacts with MYOD1. Interacts with histone H3.3 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O14647; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-1210503, EBI-10181188;
CC O14647; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-1210503, EBI-10172526;
CC O14647; Q13148: TARDBP; NbExp=2; IntAct=EBI-1210503, EBI-372899;
CC O14647; Q969V4: TEKT1; NbExp=3; IntAct=EBI-1210503, EBI-10180409;
CC O14647; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-1210503, EBI-741515;
CC O14647; Q8WV44: TRIM41; NbExp=4; IntAct=EBI-1210503, EBI-725997;
CC O14647-3; Q8IYF1: ELOA2; NbExp=3; IntAct=EBI-11985957, EBI-741705;
CC O14647-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11985957, EBI-16439278;
CC O14647-3; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-11985957, EBI-2130429;
CC O14647-3; Q8TD17: ZNF398; NbExp=3; IntAct=EBI-11985957, EBI-8643207;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Binds to myogenic
CC gene promoters. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O14647-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14647-2; Sequence=VSP_021918, VSP_021919;
CC Name=3;
CC IsoId=O14647-3; Sequence=VSP_042791;
CC -!- DOMAIN: The CHD1 helical C-terminal domain (CHCT) may bind DNA and
CC nucleosomes. {ECO:0000250|UniProtKB:O14646}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 94 (DEE94)
CC [MIM:615369]: A form of epileptic encephalopathy, a heterogeneous group
CC of early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE94 is an autosomal dominant, severe form
CC characterized by onset of multiple seizure types in the first few years
CC of life. {ECO:0000269|PubMed:23708187, ECO:0000269|PubMed:25356899}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AF006514; AAB87382.1; -; mRNA.
DR EMBL; BT007050; AAP35699.1; -; mRNA.
DR EMBL; FJ515838; ACS13730.1; -; Genomic_DNA.
DR EMBL; AC013394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471101; EAX02160.1; -; Genomic_DNA.
DR EMBL; BC007347; AAH07347.1; -; mRNA.
DR EMBL; CR978407; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS10374.2; -. [O14647-1]
DR CCDS; CCDS45356.1; -. [O14647-3]
DR RefSeq; NP_001036037.1; NM_001042572.2. [O14647-3]
DR RefSeq; NP_001262.3; NM_001271.3. [O14647-1]
DR AlphaFoldDB; O14647; -.
DR SMR; O14647; -.
DR BioGRID; 107531; 58.
DR IntAct; O14647; 27.
DR MINT; O14647; -.
DR STRING; 9606.ENSP00000377747; -.
DR GlyGen; O14647; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O14647; -.
DR MetOSite; O14647; -.
DR PhosphoSitePlus; O14647; -.
DR SwissPalm; O14647; -.
DR BioMuta; CHD2; -.
DR EPD; O14647; -.
DR jPOST; O14647; -.
DR MassIVE; O14647; -.
DR MaxQB; O14647; -.
DR PaxDb; 9606-ENSP00000377747; -.
DR PeptideAtlas; O14647; -.
DR ProteomicsDB; 48144; -. [O14647-1]
DR ProteomicsDB; 48145; -. [O14647-2]
DR ProteomicsDB; 48146; -. [O14647-3]
DR Pumba; O14647; -.
DR ABCD; O14647; 1 sequenced antibody.
DR Antibodypedia; 29044; 235 antibodies from 35 providers.
DR DNASU; 1106; -.
DR Ensembl; ENST00000394196.9; ENSP00000377747.4; ENSG00000173575.24. [O14647-1]
DR Ensembl; ENST00000420239.7; ENSP00000406581.2; ENSG00000173575.24. [O14647-3]
DR Ensembl; ENST00000626874.2; ENSP00000486629.1; ENSG00000173575.24. [O14647-2]
DR GeneID; 1106; -.
DR KEGG; hsa:1106; -.
DR MANE-Select; ENST00000394196.9; ENSP00000377747.4; NM_001271.4; NP_001262.3.
DR UCSC; uc002bsn.4; human. [O14647-1]
DR AGR; HGNC:1917; -.
DR CTD; 1106; -.
DR DisGeNET; 1106; -.
DR GeneCards; CHD2; -.
DR GeneReviews; CHD2; -.
DR HGNC; HGNC:1917; CHD2.
DR HPA; ENSG00000173575; Low tissue specificity.
DR MalaCards; CHD2; -.
DR MIM; 602119; gene.
DR MIM; 615369; phenotype.
DR neXtProt; NX_O14647; -.
DR OpenTargets; ENSG00000173575; -.
DR Orphanet; 2382; Lennox-Gastaut syndrome.
DR Orphanet; 1942; Myoclonic-astatic epilepsy.
DR PharmGKB; PA26453; -.
DR VEuPathDB; HostDB:ENSG00000173575; -.
DR eggNOG; KOG0384; Eukaryota.
DR GeneTree; ENSGT00940000155888; -.
DR HOGENOM; CLU_645515_0_0_1; -.
DR InParanoid; O14647; -.
DR OMA; REICQQH; -.
DR OrthoDB; 5482994at2759; -.
DR PhylomeDB; O14647; -.
DR TreeFam; TF313461; -.
DR PathwayCommons; O14647; -.
DR SignaLink; O14647; -.
DR SIGNOR; O14647; -.
DR BioGRID-ORCS; 1106; 32 hits in 1174 CRISPR screens.
DR ChiTaRS; CHD2; human.
DR GeneWiki; CHD2; -.
DR GenomeRNAi; 1106; -.
DR Pharos; O14647; Tbio.
DR PRO; PR:O14647; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O14647; Protein.
DR Bgee; ENSG00000173575; Expressed in calcaneal tendon and 179 other cell types or tissues.
DR ExpressionAtlas; O14647; baseline and differential.
DR Genevisible; O14647; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS: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; IBA: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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0006974; P:DNA damage response; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; ISS:UniProtKB.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd18666; CD1_tandem_CHD1-2_like; 1.
DR CDD; cd18661; CD2_tandem_CHD1-2_like; 1.
DR CDD; cd18054; DEXHc_CHD2; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 6.10.140.1440; -; 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 InterPro; IPR040793; CDH1_2_SANT_HL1.
DR InterPro; IPR025260; CHD1-like_C.
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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF19; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 2; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18375; CDH1_2_SANT_HL1; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Chromatin regulator; Disease variant;
KW DNA-binding; Epilepsy; Helicase; Hydrolase; Myogenesis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..1828
FT /note="Chromodomain-helicase-DNA-binding protein 2"
FT /id="PRO_0000080226"
FT DOMAIN 261..353
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 378..456
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 496..666
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 795..946
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1464..1566
FT /note="CHD1 helical C-terminal domain (CHCT)"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT REGION 1556..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1680..1828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 617..620
FT /note="DEAH box"
FT COMPBIAS 14..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..200
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1798..1813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1814..1828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 509..516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 240
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1807
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 502..1828
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_042791"
FT VAR_SEQ 1719..1739
FT /note="HHHDSKRRRSDEFRPQNYHQQ -> YAKGCETPGANLCQELFLGRK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:9326634"
FT /id="VSP_021918"
FT VAR_SEQ 1740..1828
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9326634"
FT /id="VSP_021919"
FT VARIANT 112..1828
FT /note="Missing (in DEE94)"
FT /evidence="ECO:0000269|PubMed:25356899"
FT /id="VAR_078614"
FT VARIANT 121..1828
FT /note="Missing (in DEE94)"
FT /evidence="ECO:0000269|PubMed:23708187"
FT /id="VAR_078615"
FT VARIANT 178..1828
FT /note="Missing (found in a patient with progressive
FT myoclonus epilepsy; uncertain significance)"
FT /evidence="ECO:0000269|PubMed:33798445"
FT /id="VAR_085039"
FT VARIANT 548
FT /note="W -> R (in DEE94; dbSNP:rs864309537)"
FT /evidence="ECO:0000269|PubMed:23708187"
FT /id="VAR_070209"
FT VARIANT 823
FT /note="L -> P (in DEE94; dbSNP:rs864309540)"
FT /evidence="ECO:0000269|PubMed:23708187"
FT /id="VAR_070210"
FT VARIANT 1574
FT /note="G -> A (in dbSNP:rs56227200)"
FT /id="VAR_061099"
FT CONFLICT 1156
FT /note="I -> L (in Ref. 1; AAB87382)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1828 AA; 211344 MW; 13139D6059210F00 CRC64;
MMRNKDKSQE EDSSLHSNAS SHSASEEASG SDSGSQSESE QGSDPGSGHG SESNSSSESS
ESQSESESES AGSKSQPVLP EAKEKPASKK ERIADVKKMW EEYPDVYGVR RSNRSRQEPS
RFNIKEEASS GSESGSPKRR GQRQLKKQEK WKQEPSEDEQ EQGTSAESEP EQKKVKARRP
VPRRTVPKPR VKKQPKTQRG KRKKQDSSDE DDDDDEAPKR QTRRRAAKNV SYKEDDDFET
DSDDLIEMTG EGVDEQQDNS ETIEKVLDSR LGKKGATGAS TTVYAIEANG DPSGDFDTEK
DEGEIQYLIK WKGWSYIHST WESEESLQQQ KVKGLKKLEN FKKKEDEIKQ WLGKVSPEDV
EYFNCQQELA SELNKQYQIV ERVIAVKTSK STLGQTDFPA HSRKPAPSNE PEYLCKWMGL
PYSECSWEDE ALIGKKFQNC IDSFHSRNNS KTIPTRECKA LKQRPRFVAL KKQPAYLGGE
NLELRDYQLE GLNWLAHSWC KNNSVILADE MGLGKTIQTI SFLSYLFHQH QLYGPFLIVV
PLSTLTSWQR EFEIWAPEIN VVVYIGDLMS RNTIREYEWI HSQTKRLKFN ALITTYEILL
KDKTVLGSIN WAFLGVDEAH RLKNDDSLLY KTLIDFKSNH RLLITGTPLQ NSLKELWSLL
HFIMPEKFEF WEDFEEDHGK GRENGYQSLH KVLEPFLLRR VKKDVEKSLP AKVEQILRVE
MSALQKQYYK WILTRNYKAL AKGTRGSTSG FLNIVMELKK CCNHCYLIKP PEENERENGQ
EILLSLIRSS GKLILLDKLL TRLRERGNRV LIFSQMVRML DILAEYLTIK HYPFQRLDGS
IKGEIRKQAL DHFNADGSED FCFLLSTRAG GLGINLASAD TVVIFDSDWN PQNDLQAQAR
AHRIGQKKQV NIYRLVTKGT VEEEIIERAK KKMVLDHLVI QRMDTTGRTI LENNSGRSNS
NPFNKEELTA ILKFGAEDLF KELEGEESEP QEMDIDEILR LAETRENEVS TSATDELLSQ
FKVANFATME DEEELEERPH KDWDEIIPEE QRKKVEEEER QKELEEIYML PRIRSSTKKA
QTNDSDSDTE SKRQAQRSSA SESETEDSDD DKKPKRRGRP RSVRKDLVEG FTDAEIRRFI
KAYKKFGLPL ERLECIARDA ELVDKSVADL KRLGELIHNS CVSAMQEYEE QLKENASEGK
GPGKRRGPTI KISGVQVNVK SIIQHEEEFE MLHKSIPVDP EEKKKYCLTC RVKAAHFDVE
WGVEDDSRLL LGIYEHGYGN WELIKTDPEL KLTDKILPVE TDKKPQGKQL QTRADYLLKL
LRKGLEKKGA VTGGEEAKLK KRKPRVKKEN KVPRLKEEHG IELSSPRHSD NPSEEGEVKD
DGLEKSPMKK KQKKKENKEN KEKQMSSRKD KEGDKERKKS KDKKEKPKSG DAKSSSKSKR
SQGPVHITAG SEPVPIGEDE DDDLDQETFS ICKERMRPVK KALKQLDKPD KGLNVQEQLE
HTRNCLLKIG DRIAECLKAY SDQEHIKLWR RNLWIFVSKF TEFDARKLHK LYKMAHKKRS
QEEEEQKKKD DVTGGKKPFR PEASGSSRDS LISQSHTSHN LHPQKPHLPA SHGPQMHGHP
RDNYNHPNKR HFSNADRGDW QRERKFNYGG GNNNPPWGSD RHHQYEQHWY KDHHYGDRRH
MDAHRSGSYR PNNMSRKRPY DQYSSDRDHR GHRDYYDRHH HDSKRRRSDE FRPQNYHQQD
FRRMSDHRPA MGYHGQGPSD HYRSFHTDKL GEYKQPLPPL HPAVSDPRSP PSQKSPHDSK
SPLDHRSPLE RSLEQKNNPD YNWNVRKT
//
