ID CHD1_HUMAN Reviewed; 1710 AA. AC O14646; Q17RZ3; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 2. DT 27-MAR-2024, entry version 212. DE RecName: Full=Chromodomain-helicase-DNA-binding protein 1; DE Short=CHD-1; DE EC=3.6.4.12; DE AltName: Full=ATP-dependent helicase CHD1; GN Name=CHD1 {ECO:0000312|HGNC:HGNC:1915}; 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 GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Cerebellum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP INTERACTION WITH H3K4ME2 AND H3K4ME3. RX PubMed=16263726; DOI=10.1074/jbc.c500395200; RA Sims R.J. III, Chen C.-F., Santos-Rosa H., Kouzarides T., Patel S.S., RA Reinberg D.; RT "Human but not yeast CHD1 binds directly and selectively to histone H3 RT methylated at lysine 4 via its tandem chromodomains."; RL J. Biol. Chem. 280:41789-41792(2005). RN [5] RP 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 [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [7] RP DOMAIN, AND INTERACTION WITH HISTONE H3K4ME3. RX PubMed=17433364; DOI=10.1016/j.jmb.2007.03.024; RA Flanagan J.F., Blus B.J., Kim D., Clines K.L., Rastinejad F., RA Khorasanizadeh S.; RT "Molecular implications of evolutionary differences in CHD double RT chromodomains."; RL J. Mol. Biol. 369:334-342(2007). RN [8] RP FUNCTION, AND INTERACTION WITH H3K4ME3; PAF1; SFA3A1; SFA3A2; SFA3A3; SNF2 RP AND SSRP1. RX PubMed=18042460; DOI=10.1016/j.molcel.2007.11.010; RA Sims R.J. III, Millhouse S., Chen C.-F., Lewis B.A., Erdjument-Bromage H., RA Tempst P., Manley J.L., Reinberg D.; RT "Recognition of trimethylated histone H3 lysine 4 facilitates the RT recruitment of transcription postinitiation factors and pre-mRNA RT splicing."; RL Mol. Cell 28:665-676(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1040; SER-1081 AND SER-1677, RP AND 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237; SER-241; SER-1040; RP SER-1096; SER-1098; SER-1100 AND SER-1677, AND IDENTIFICATION BY MASS RP 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 [11] RP 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-250; SER-252; SER-1025; RP SER-1040 AND SER-1677, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-216; SER-1096; RP SER-1098; SER-1100; SER-1102; SER-1353; SER-1355; SER-1356; SER-1360; RP SER-1363 AND SER-1371, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471; SER-1040; SER-1081; RP SER-1096; SER-1098; SER-1102; SER-1161; SER-1622; SER-1677 AND SER-1689, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1688 (ISOFORM 2), AND RP 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1677, 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 [17] RP FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN PILBOS, VARIANTS PILBOS RP GLY-141; LYS-460; GLN-618 AND GLN-1708, AND CHARACTERIZATION OF VARIANT RP PILBOS GLN-618. RX PubMed=28866611; DOI=10.1136/jmedgenet-2017-104759; RA Pilarowski G.O., Vernon H.J., Applegate C.D., Boukas L., Cho M.T., RA Gurnett C.A., Benke P.J., Beaver E., Heeley J.M., Medne L., Krantz I.D., RA Azage M., Niyazov D., Henderson L.B., Wentzensen I.M., Baskin B., RA Sacoto M.J.G., Bowman G.D., Bjornsson H.T.; RT "Missense variants in the chromatin remodeler CHD1 are associated with RT neurodevelopmental disability."; RL J. Med. Genet. 55:561-566(2018). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 268-443, AND INTERACTION WITH RP HISTONE H3K4ME3. RX PubMed=16372014; DOI=10.1038/nature04290; RA Flanagan J.F., Mi L.-Z., Chruszcz M., Cymborowski M., Clines K.L., Kim Y., RA Minor W., Rastinejad F., Khorasanizadeh S.; RT "Double chromodomains cooperate to recognize the methylated histone H3 RT tail."; RL Nature 438:1181-1185(2005). RN [19] {ECO:0007744|PDB:2N39} RP STRUCTURE BY NMR OF 1409-1511, DOMAIN, DNA-BINDING, AND MUTAGENESIS OF RP 1418-LYS--LYS-1425; 1429-LYS--LYS-1436; 1491-ARG--LYS-1495 AND RP 1498-LYS--LYS-1503. RX PubMed=27591891; DOI=10.1016/j.jmb.2016.08.028; RA Mohanty B., Helder S., Silva A.P., Mackay J.P., Ryan D.P.; RT "The Chromatin Remodelling Protein CHD1 Contains a Previously Unrecognised RT C-Terminal Helical Domain."; RL J. Mol. Biol. 428:4298-4314(2016). CC -!- FUNCTION: ATP-dependent chromatin-remodeling factor which functions as CC substrate recognition component of the transcription regulatory histone CC acetylation (HAT) complex SAGA. Regulates polymerase II transcription. CC Also required for efficient transcription by RNA polymerase I, and more CC specifically the polymerase I transcription termination step. Regulates CC negatively DNA replication. Not only involved in transcription-related CC chromatin-remodeling, but also required to maintain a specific CC chromatin configuration across the genome. Is also associated with CC histone deacetylase (HDAC) activity (By similarity). Required for the CC bridging of SNF2, the FACT complex, the PAF complex as well as the U2 CC snRNP complex to H3K4me3. Functions to modulate the efficiency of pre- CC mRNA splicing in part through physical bridging of spliceosomal CC components to H3K4me3 (PubMed:18042460, PubMed:28866611). Required for CC maintaining open chromatin and pluripotency in embryonic stem cells (By CC similarity). {ECO:0000250|UniProtKB:P40201, CC ECO:0000269|PubMed:18042460, ECO:0000269|PubMed:28866611}. 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: Component of the SAGA complex (By similarity). Interacts with CC BCLAF1, NCoR, SRP20 and SAFB (By similarity). Specifically interacts CC with methylated H3K4me2 and H3K4me3. Interacts with the FACT complex, CC the PAF complex and the U2 snRNP. Interacts directly with PAF1, SFA3A1, CC SFA3A2, SFA3A3, SNF2 and SSRP1. {ECO:0000250, CC ECO:0000269|PubMed:16263726, ECO:0000269|PubMed:16372014, CC ECO:0000269|PubMed:17433364, ECO:0000269|PubMed:18042460}. CC -!- INTERACTION: CC O14646; O60341-1: KDM1A; NbExp=8; IntAct=EBI-1560858, EBI-15599570; CC O14646; B2BUF1: NS1; Xeno; NbExp=3; IntAct=EBI-1560858, EBI-4291940; CC O14646-2; P28799: GRN; NbExp=3; IntAct=EBI-10961487, EBI-747754; CC O14646-2; O76024: WFS1; NbExp=3; IntAct=EBI-10961487, EBI-720609; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40201}. Cytoplasm CC {ECO:0000250|UniProtKB:P40201}. Note=Is released into the cytoplasm CC when cells enter mitosis and is reincorporated into chromatin during CC telophase-cytokinesis. {ECO:0000250|UniProtKB:P40201}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O14646-1; Sequence=Displayed; CC Name=2; CC IsoId=O14646-2; Sequence=VSP_038432; CC -!- TISSUE SPECIFICITY: Expressed in many tissues including in the brain, CC where the highest level of expression is found in the cerebellum and CC basal ganglia. {ECO:0000269|PubMed:28866611}. CC -!- DOMAIN: The 2 chromodomains are involved in the binding to the histone CC H3 methyllysine at position 4 (H3K4me3). {ECO:0000269|PubMed:17433364}. CC -!- DOMAIN: The CHD1 helical C-terminal domain (CHCT) binds DNA and CC nucleosomes. {ECO:0000269|PubMed:27591891}. CC -!- DISEASE: Pilarowski-Bjornsson syndrome (PILBOS) [MIM:617682]: An CC autosomal dominant disorder characterized by developmental delay, CC speech apraxia, intellectual disability, autism, and facial dysmorphic CC features. Some patients may have seizures. CC {ECO:0000269|PubMed:28866611}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {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; AF006513; AAB87381.1; -; mRNA. DR EMBL; AC022121; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC117134; AAI17135.1; -; mRNA. DR CCDS; CCDS34204.1; -. [O14646-1] DR RefSeq; NP_001261.2; NM_001270.2. [O14646-1] DR RefSeq; XP_005271924.1; XM_005271867.4. DR PDB; 2B2T; X-ray; 2.45 A; A/B=268-443, C=268-373. DR PDB; 2B2U; X-ray; 2.95 A; A/B=268-443, C=268-373. DR PDB; 2B2V; X-ray; 2.65 A; A/B=268-443, C=268-373. DR PDB; 2B2W; X-ray; 2.40 A; A/B=268-443, C=268-373. DR PDB; 2B2Y; X-ray; 2.35 A; A/B=268-443, C=268-373. DR PDB; 2N39; NMR; -; A=1409-1511. DR PDB; 4B4C; X-ray; 1.62 A; A=1119-1327. DR PDB; 4NW2; X-ray; 1.90 A; A/C=268-443. DR PDB; 4O42; X-ray; 1.87 A; A=268-443. DR PDB; 5AFW; X-ray; 1.60 A; A=270-443. DR PDBsum; 2B2T; -. DR PDBsum; 2B2U; -. DR PDBsum; 2B2V; -. DR PDBsum; 2B2W; -. DR PDBsum; 2B2Y; -. DR PDBsum; 2N39; -. DR PDBsum; 4B4C; -. DR PDBsum; 4NW2; -. DR PDBsum; 4O42; -. DR PDBsum; 5AFW; -. DR AlphaFoldDB; O14646; -. DR SMR; O14646; -. DR BioGRID; 107530; 125. DR DIP; DIP-38922N; -. DR IntAct; O14646; 28. DR MINT; O14646; -. DR STRING; 9606.ENSP00000483667; -. DR ChEMBL; CHEMBL4523123; -. DR CarbonylDB; O14646; -. DR GlyGen; O14646; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O14646; -. DR MetOSite; O14646; -. DR PhosphoSitePlus; O14646; -. DR SwissPalm; O14646; -. DR BioMuta; CHD1; -. DR EPD; O14646; -. DR jPOST; O14646; -. DR MassIVE; O14646; -. DR MaxQB; O14646; -. DR PaxDb; 9606-ENSP00000483667; -. DR PeptideAtlas; O14646; -. DR ProteomicsDB; 48142; -. [O14646-1] DR ProteomicsDB; 48143; -. [O14646-2] DR Pumba; O14646; -. DR ABCD; O14646; 1 sequenced antibody. DR Antibodypedia; 25129; 238 antibodies from 35 providers. DR DNASU; 1105; -. DR Ensembl; ENST00000614616.5; ENSP00000483667.1; ENSG00000153922.12. [O14646-1] DR GeneID; 1105; -. DR KEGG; hsa:1105; -. DR MANE-Select; ENST00000614616.5; ENSP00000483667.1; NM_001270.4; NP_001261.2. DR UCSC; uc003knf.3; human. [O14646-1] DR AGR; HGNC:1915; -. DR CTD; 1105; -. DR DisGeNET; 1105; -. DR GeneCards; CHD1; -. DR HGNC; HGNC:1915; CHD1. DR HPA; ENSG00000153922; Low tissue specificity. DR MalaCards; CHD1; -. DR MIM; 602118; gene. DR MIM; 617682; phenotype. DR neXtProt; NX_O14646; -. DR OpenTargets; ENSG00000153922; -. DR Orphanet; 529965; Intellectual disability-autism-speech apraxia-craniofacial dysmorphism syndrome. DR PharmGKB; PA26451; -. DR VEuPathDB; HostDB:ENSG00000153922; -. DR eggNOG; KOG0384; Eukaryota. DR GeneTree; ENSGT00940000156579; -. DR HOGENOM; CLU_000315_8_1_1; -. DR InParanoid; O14646; -. DR OMA; WVQIRDD; -. DR OrthoDB; 5482994at2759; -. DR PhylomeDB; O14646; -. DR TreeFam; TF313461; -. DR PathwayCommons; O14646; -. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR SignaLink; O14646; -. DR SIGNOR; O14646; -. DR BioGRID-ORCS; 1105; 146 hits in 1186 CRISPR screens. DR ChiTaRS; CHD1; human. DR EvolutionaryTrace; O14646; -. DR GeneWiki; CHD1; -. DR GenomeRNAi; 1105; -. DR Pharos; O14646; Tbio. DR PRO; PR:O14646; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; O14646; Protein. DR Bgee; ENSG00000153922; Expressed in calcaneal tendon and 197 other cell types or tissues. DR ExpressionAtlas; O14646; baseline and differential. DR GO; GO:0000785; C:chromatin; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IDA:CACAO. DR GO; GO:0000228; C:nuclear chromosome; IDA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:CACAO. 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; IBA:GO_Central. DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB. DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central. DR GO; GO:0043923; P:positive regulation by host of viral transcription; IMP:CACAO. 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; cd18793; SF2_C_SNF; 1. DR Gene3D; 2.40.50.40; -; 2. 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 IDEAL; IID00003; -. 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:SF7; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 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. DR Genevisible; O14646; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Chromatin regulator; KW Cytoplasm; Disease variant; DNA-binding; Helicase; Hydrolase; KW Intellectual disability; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation. FT CHAIN 1..1710 FT /note="Chromodomain-helicase-DNA-binding protein 1" FT /id="PRO_0000080224" FT DOMAIN 272..364 FT /note="Chromo 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053" FT DOMAIN 389..452 FT /note="Chromo 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053" FT DOMAIN 493..663 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 792..943 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REPEAT 1628..1632 FT /note="1" FT REPEAT 1634..1638 FT /note="2" FT REPEAT 1640..1644 FT /note="3" FT REGION 1..252 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1080..1120 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1321..1408 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1409..1511 FT /note="CHD1 helical C-terminal domain (CHCT)" FT /evidence="ECO:0000269|PubMed:27591891, FT ECO:0007744|PDB:2N39" FT REGION 1502..1710 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1628..1644 FT /note="3 X 5 AA repeats of H-S-D-H-R" FT MOTIF 614..617 FT /note="DEAH box" FT COMPBIAS 12..63 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 64..78 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 92..125 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 133..150 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 163..190 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 191..206 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 226..252 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1087..1108 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1343..1386 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1507..1521 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1524..1666 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1667..1688 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1691..1710 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 506..513 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT MOD_RES 215 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 216 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 237 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 241 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 250 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 252 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 471 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1025 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1040 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1081 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1085 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O14647" FT MOD_RES 1096 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1098 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1100 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1102 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1161 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1353 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1355 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1356 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1360 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1363 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1371 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 1373 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O14647" FT MOD_RES 1622 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1677 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 1689 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1684 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9326634" FT /id="VSP_038432" FT VARIANT 141 FT /note="R -> G (in PILBOS; dbSNP:rs1064795875)" FT /evidence="ECO:0000269|PubMed:28866611" FT /id="VAR_080265" FT VARIANT 264 FT /note="P -> T (in dbSNP:rs10062803)" FT /id="VAR_055652" FT VARIANT 460 FT /note="R -> K (in PILBOS; dbSNP:rs1554078856)" FT /evidence="ECO:0000269|PubMed:28866611" FT /id="VAR_080266" FT VARIANT 618 FT /note="R -> Q (in PILBOS; patient cells show a global FT increase of methylated histone binding; FT dbSNP:rs1554078349)" FT /evidence="ECO:0000269|PubMed:28866611" FT /id="VAR_080267" FT VARIANT 1708 FT /note="R -> Q (in PILBOS; dbSNP:rs1293161341)" FT /evidence="ECO:0000269|PubMed:28866611" FT /id="VAR_080268" FT MUTAGEN 1418..1425 FT /note="KERMRPVK->AERMAPVA: Abolishes DNA-binding." FT /evidence="ECO:0000269|PubMed:27591891" FT MUTAGEN 1429..1436 FT /note="KQLDRPEK->AQLDAPEA: Abolishes DNA-binding." FT /evidence="ECO:0000269|PubMed:27591891" FT MUTAGEN 1491..1495 FT /note="RKLHK->AALHA: Abolishes DNA-binding." FT /evidence="ECO:0000269|PubMed:27591891" FT MUTAGEN 1498..1503 FT /note="KHAIKK->AHAIAA: Abolishes DNA-binding." FT /evidence="ECO:0000269|PubMed:27591891" FT CONFLICT 392 FT /note="E -> G (in Ref. 1; AAB87381)" FT /evidence="ECO:0000305" FT STRAND 273..284 FT /evidence="ECO:0007829|PDB:5AFW" FT HELIX 290..292 FT /evidence="ECO:0007829|PDB:5AFW" FT HELIX 294..300 FT /evidence="ECO:0007829|PDB:5AFW" FT TURN 303..306 FT /evidence="ECO:0007829|PDB:5AFW" FT TURN 309..311 FT /evidence="ECO:0007829|PDB:5AFW" FT STRAND 314..322 FT /evidence="ECO:0007829|PDB:5AFW" FT HELIX 327..329 FT /evidence="ECO:0007829|PDB:5AFW" FT STRAND 331..333 FT /evidence="ECO:0007829|PDB:5AFW" FT HELIX 335..340 FT /evidence="ECO:0007829|PDB:5AFW" FT HELIX 347..360 FT /evidence="ECO:0007829|PDB:5AFW" FT TURN 363..365 FT /evidence="ECO:0007829|PDB:2B2W" FT HELIX 375..387 FT /evidence="ECO:0007829|PDB:5AFW" FT STRAND 390..401 FT /evidence="ECO:0007829|PDB:5AFW" FT STRAND 407..413 FT /evidence="ECO:0007829|PDB:5AFW" FT HELIX 418..420 FT /evidence="ECO:0007829|PDB:5AFW" FT STRAND 422..425 FT /evidence="ECO:0007829|PDB:5AFW" FT HELIX 426..442 FT /evidence="ECO:0007829|PDB:5AFW" FT HELIX 1128..1138 FT /evidence="ECO:0007829|PDB:4B4C" FT HELIX 1144..1146 FT /evidence="ECO:0007829|PDB:4B4C" FT HELIX 1148..1154 FT /evidence="ECO:0007829|PDB:4B4C" FT HELIX 1162..1180 FT /evidence="ECO:0007829|PDB:4B4C" FT STRAND 1201..1204 FT /evidence="ECO:0007829|PDB:4B4C" FT STRAND 1207..1210 FT /evidence="ECO:0007829|PDB:4B4C" FT HELIX 1211..1227 FT /evidence="ECO:0007829|PDB:4B4C" FT HELIX 1232..1236 FT /evidence="ECO:0007829|PDB:4B4C" FT STRAND 1249..1251 FT /evidence="ECO:0007829|PDB:4B4C" FT HELIX 1255..1268 FT /evidence="ECO:0007829|PDB:4B4C" FT HELIX 1273..1278 FT /evidence="ECO:0007829|PDB:4B4C" FT STRAND 1280..1283 FT /evidence="ECO:0007829|PDB:4B4C" FT TURN 1285..1287 FT /evidence="ECO:0007829|PDB:4B4C" FT HELIX 1299..1324 FT /evidence="ECO:0007829|PDB:4B4C" FT HELIX 1411..1420 FT /evidence="ECO:0007829|PDB:2N39" FT HELIX 1425..1432 FT /evidence="ECO:0007829|PDB:2N39" FT HELIX 1440..1463 FT /evidence="ECO:0007829|PDB:2N39" FT HELIX 1468..1484 FT /evidence="ECO:0007829|PDB:2N39" FT STRAND 1486..1488 FT /evidence="ECO:0007829|PDB:2N39" FT HELIX 1490..1504 FT /evidence="ECO:0007829|PDB:2N39" FT MOD_RES O14646-2:1688 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" SQ SEQUENCE 1710 AA; 196688 MW; D888AAA46FDA31B1 CRC64; MNGHSDEESV RNSSGESSQS DDDSGSASGS GSGSSSGSSS DGSSSQSGSS DSDSGSESGS QSESESDTSR ENKVQAKPPK VDGAEFWKSS PSILAVQRSA ILKKQQQQQQ QQQHQASSNS GSEEDSSSSE DSDDSSSEVK RKKHKDEDWQ MSGSGSPSQS GSDSESEEER EKSSCDETES DYEPKNKVKS RKPQNRSKSK NGKKILGQKK RQIDSSEEDD DEEDYDNDKR SSRRQATVNV SYKEDEEMKT DSDDLLEVCG EDVPQPEEEE FETIERFMDC RIGRKGATGA TTTIYAVEAD GDPNAGFEKN KEPGEIQYLI KWKGWSHIHN TWETEETLKQ QNVRGMKKLD NYKKKDQETK RWLKNASPED VEYYNCQQEL TDDLHKQYQI VERIIAHSNQ KSAAGYPDYY CKWQGLPYSE CSWEDGALIS KKFQACIDEY FSRNQSKTTP FKDCKVLKQR PRFVALKKQP SYIGGHEGLE LRDYQLNGLN WLAHSWCKGN SCILADEMGL GKTIQTISFL NYLFHEHQLY GPFLLVVPLS TLTSWQREIQ TWASQMNAVV YLGDINSRNM IRTHEWTHHQ TKRLKFNILL TTYEILLKDK AFLGGLNWAF IGVDEAHRLK NDDSLLYKTL IDFKSNHRLL ITGTPLQNSL KELWSLLHFI MPEKFSSWED FEEEHGKGRE YGYASLHKEL EPFLLRRVKK DVEKSLPAKV EQILRMEMSA LQKQYYKWIL TRNYKALSKG SKGSTSGFLN IMMELKKCCN HCYLIKPPDN NEFYNKQEAL QHLIRSSGKL ILLDKLLIRL RERGNRVLIF SQMVRMLDIL AEYLKYRQFP FQRLDGSIKG ELRKQALDHF NAEGSEDFCF LLSTRAGGLG INLASADTVV IFDSDWNPQN DLQAQARAHR IGQKKQVNIY RLVTKGSVEE DILERAKKKM VLDHLVIQRM DTTGKTVLHT GSAPSSSTPF NKEELSAILK FGAEELFKEP EGEEQEPQEM DIDEILKRAE THENEPGPLT VGDELLSQFK VANFSNMDED DIELEPERNS KNWEEIIPED QRRRLEEEER QKELEEIYML PRMRNCAKQI SFNGSEGRRS RSRRYSGSDS DSISEGKRPK KRGRPRTIPR ENIKGFSDAE IRRFIKSYKK FGGPLERLDA IARDAELVDK SETDLRRLGE LVHNGCIKAL KDSSSGTERT GGRLGKVKGP TFRISGVQVN AKLVISHEEE LIPLHKSIPS DPEERKQYTI PCHTKAAHFD IDWGKEDDSN LLIGIYEYGY GSWEMIKMDP DLSLTHKILP DDPDKKPQAK QLQTRADYLI KLLSRDLAKK EALSGAGSSK RRKARAKKNK AMKSIKVKEE IKSDSSPLPS EKSDEDDDKL SESKSDGRER SKKSSVSDAP VHITASGEPV PISEESEELD QKTFSICKER MRPVKAALKQ LDRPEKGLSE REQLEHTRQC LIKIGDHITE CLKEYTNPEQ IKQWRKNLWI FVSKFTEFDA RKLHKLYKHA IKKRQESQQN SDQNSNLNPH VIRNPDVERL KENTNHDDSS RDSYSSDRHL TQYHDHHKDR HQGDSYKKSD SRKRPYSSFS NGKDHRDWDH YKQDSRYYSD REKHRKLDDH RSRDHRSNLE GSLKDRSHSD HRSHSDHRLH SDHRSSSEYT HHKSSRDYRY HSDWQMDHRA SSSGPRSPLD QRSPYGSRSP FEHSVEHKST PEHTWSSRKT //