CHD1_HUMAN
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 03-AUG-2022, entry version 203.
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;
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).
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).
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}.
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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; 106.
DR DIP; DIP-38922N; -.
DR IntAct; O14646; 25.
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 BioMuta; CHD1; -.
DR EPD; O14646; -.
DR jPOST; O14646; -.
DR MassIVE; O14646; -.
DR MaxQB; O14646; -.
DR PaxDb; O14646; -.
DR PeptideAtlas; O14646; -.
DR PRIDE; O14646; -.
DR ProteomicsDB; 48142; -. [O14646-1]
DR ProteomicsDB; 48143; -. [O14646-2]
DR ABCD; O14646; 1 sequenced antibody.
DR Antibodypedia; 25129; 210 antibodies from 35 providers.
DR DNASU; 1105; -.
DR Ensembl; ENST00000284049.7; ENSP00000284049.3; ENSG00000153922.11. [O14646-1]
DR Ensembl; ENST00000614616.5; ENSP00000483667.1; ENSG00000153922.11. [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 CTD; 1105; -.
DR DisGeNET; 1105; -.
DR GeneCards; CHD1; -.
DR HGNC; HGNC:1915; CHD1.
DR HPA; ENSG00000153922; Tissue enhanced (bone).
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; CSWGARE; -.
DR OrthoDB; 57339at2759; -.
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; 127 hits in 1101 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 195 other tissues.
DR ExpressionAtlas; O14646; baseline and differential.
DR Genevisible; O14646; HS.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID00003; -.
DR InterPro; IPR040793; CDH1_2_SANT_HL1.
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; IPR025260; DUF4208.
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; IPR000330; SNF2_N.
DR Pfam; PF18375; CDH1_2_SANT_HL1; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF13907; DUF4208; 1.
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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 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 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 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 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
