ID   CHD8_HUMAN              Reviewed;        2581 AA.
AC   Q9HCK8; Q4G0D8; Q68DQ0; Q6DKH9; Q6P440; Q6ZNL7; Q8N3Z9; Q8NCY4; Q8TBR9;
AC   Q96F26;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 5.
DT   27-MAR-2024, entry version 211.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 8 {ECO:0000255|HAMAP-Rule:MF_03071};
DE            Short=CHD-8 {ECO:0000255|HAMAP-Rule:MF_03071};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03071};
DE   AltName: Full=ATP-dependent helicase CHD8 {ECO:0000255|HAMAP-Rule:MF_03071};
DE   AltName: Full=Helicase with SNF2 domain 1;
GN   Name=CHD8 {ECO:0000255|HAMAP-Rule:MF_03071};
GN   Synonyms=HELSNF1, KIAA1564;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lymph node, and Uterine endothelium;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-176 (ISOFORM 1).
RG   The Cancer Genome Anatomy Project (CGAP) at the National Cancer Institute;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 150-2581 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA   Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:273-281(2000).
RN   [5]
RP   SEQUENCE REVISION.
RX   PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
RN   [6]
RP   SEQUENCE REVISION.
RA   Ohara O., Nagase T., Kikuno R.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1038-2581.
RC   TISSUE=Spleen;
RA   Jikuya H., Takano J., Kikuno R., Nagase T., Ohara O.;
RT   "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1674-2581.
RC   TISSUE=Brain, Duodenum, Liver, Lung, and Spleen;
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   [9]
RP   IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX   PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA   Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA   Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT   "Physical association and coordinate function of the H3 K4
RT   methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL   Cell 121:873-885(2005).
RN   [10]
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   [11]
RP   INTERACTION WITH CTCF.
RX   PubMed=16949368; DOI=10.1016/j.molcel.2006.08.008;
RA   Ishihara K., Oshimura M., Nakao M.;
RT   "CTCF-dependent chromatin insulator is linked to epigenetic remodeling.";
RL   Mol. Cell 23:733-742(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2051, AND IDENTIFICATION BY
RP   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   [13]
RP   FUNCTION, AND INTERACTION WITH ZNF143.
RX   PubMed=17938208; DOI=10.1128/mcb.00846-07;
RA   Yuan C.-C., Zhao X., Florens L., Swanson S.K., Washburn M.P., Hernandez N.;
RT   "CHD8 associates with human Staf and contributes to efficient U6 RNA
RT   polymerase III transcription.";
RL   Mol. Cell. Biol. 27:8729-8738(2007).
RN   [14]
RP   POSSIBLE ASSOCIATION WITH DEVELOPMENTAL DELAY.
RX   PubMed=17545556; DOI=10.1136/jmg.2007.050823;
RA   Zahir F., Firth H.V., Baross A., Delaney A.D., Eydoux P., Gibson W.T.,
RA   Langlois S., Martin H., Willatt L., Marra M.A., Friedman J.M.;
RT   "Novel deletions of 14q11.2 associated with developmental delay, cognitive
RT   impairment and similar minor anomalies in three children.";
RL   J. Med. Genet. 44:556-561(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2182 AND SER-2211, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [16]
RP   FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1,
RP   IDENTIFICATION IN A COMPLEX WITH WDR5, AND MUTAGENESIS OF LYS-842.
RX   PubMed=18378692; DOI=10.1128/mcb.00322-08;
RA   Thompson B.A., Tremblay V., Lin G., Bochar D.A.;
RT   "CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-
RT   catenin target genes.";
RL   Mol. Cell. Biol. 28:3894-3904(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562; SER-1976; SER-2008;
RP   SER-2046 AND SER-2519, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [18]
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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-1420; SER-1424;
RP   THR-1993; SER-2008 AND SER-2200, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [20]
RP   INTERACTION WITH CHD7, AND SUBCELLULAR LOCATION.
RX   PubMed=20453063; DOI=10.1093/hmg/ddq189;
RA   Batsukh T., Pieper L., Koszucka A.M., von Velsen N., Hoyer-Fender S.,
RA   Elbracht M., Bergman J.E., Hoefsloot L.H., Pauli S.;
RT   "CHD8 interacts with CHD7, a protein which is mutated in CHARGE syndrome.";
RL   Hum. Mol. Genet. 19:2858-2866(2010).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1420; SER-1424; SER-2008 AND
RP   SER-2046, AND 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   [22]
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   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1420; SER-1424; SER-2046;
RP   SER-2069 AND SER-2071, 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   [24]
RP   INTERACTION WITH FAM124B.
RX   PubMed=23285124; DOI=10.1371/journal.pone.0052640;
RA   Batsukh T., Schulz Y., Wolf S., Rabe T.I., Oellerich T., Urlaub H.,
RA   Schaefer I.M., Pauli S.;
RT   "Identification and characterization of FAM124B as a novel component of a
RT   CHD7 and CHD8 containing complex.";
RL   PLoS ONE 7:E52640-E52640(2012).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432; SER-1978; SER-2046 AND
RP   SER-2519, 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   [26]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2256, 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   [27]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2025, AND IDENTIFICATION BY MASS
RP   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   [28]
RP   INTERACTION WITH TLK2.
RX   PubMed=33323470; DOI=10.1136/jmedgenet-2020-107281;
RA   Pavinato L., Villamor-Paya M., Sanchiz-Calvo M., Andreoli C., Gay M.,
RA   Vilaseca M., Arauz-Garofalo G., Ciolfi A., Bruselles A., Pippucci T.,
RA   Prota V., Carli D., Giorgio E., Radio F.C., Antona V., Giuffre M.,
RA   Ranguin K., Colson C., De Rubeis S., Dimartino P., Buxbaum J.D.,
RA   Ferrero G.B., Tartaglia M., Martinelli S., Stracker T.H., Brusco A.;
RT   "Functional analysis of TLK2 variants and their proximal interactomes
RT   implicates impaired kinase activity and chromatin maintenance defects in
RT   their pathogenesis.";
RL   J. Med. Genet. 59:170-179(2022).
RN   [29]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HNRNPL.
RX   PubMed=36537238; DOI=10.1093/nar/gkac1134;
RA   Kerschbamer E., Arnoldi M., Tripathi T., Pellegrini M., Maturi S.,
RA   Erdin S., Salviato E., Di Leva F., Sebestyen E., Dassi E., Zarantonello G.,
RA   Benelli M., Campos E., Basson M.A., Gusella J.F., Gustincich S., Piazza S.,
RA   Demichelis F., Talkowski M.E., Ferrari F., Biagioli M.;
RT   "CHD8 suppression impacts on histone H3 lysine 36 trimethylation and alters
RT   RNA alternative splicing.";
RL   Nucleic Acids Res. 50:12809-12828(2022).
RN   [30]
RP   STRUCTURE BY NMR OF 2291-2372.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the first BRK domain from human chromodomain-
RT   helicase-DNA-binding protein 8.";
RL   Submitted (OCT-2006) to the PDB data bank.
RN   [31]
RP   VARIANT IDDAM HIS-2498 DEL.
RX   PubMed=23160955; DOI=10.1126/science.1227764;
RA   O'Roak B.J., Vives L., Fu W., Egertson J.D., Stanaway I.B., Phelps I.G.,
RA   Carvill G., Kumar A., Lee C., Ankenman K., Munson J., Hiatt J.B.,
RA   Turner E.H., Levy R., O'Day D.R., Krumm N., Coe B.P., Martin B.K.,
RA   Borenstein E., Nickerson D.A., Mefford H.C., Doherty D., Akey J.M.,
RA   Bernier R., Eichler E.E., Shendure J.;
RT   "Multiplex targeted sequencing identifies recurrently mutated genes in
RT   autism spectrum disorders.";
RL   Science 338:1619-1622(2012).
RN   [32]
RP   VARIANT IDDAM ILE-744.
RX   PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009;
RA   D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T.,
RA   Sestan N., Walsh C.A.;
RT   "Targeted DNA Sequencing from Autism Spectrum Disorder Brains Implicates
RT   Multiple Genetic Mechanisms.";
RL   Neuron 88:910-917(2015).
CC   -!- FUNCTION: DNA helicase that acts as a chromatin remodeling factor and
CC       regulates transcription. Acts as a transcription repressor by
CC       remodeling chromatin structure and recruiting histone H1 to target
CC       genes. Suppresses p53/TP53-mediated apoptosis by recruiting histone H1
CC       and preventing p53/TP53 transactivation activity. Acts as a negative
CC       regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1)
CC       activity. Negatively regulates CTNNB1-targeted gene expression by being
CC       recruited specifically to the promoter regions of several CTNNB1
CC       responsive genes. Involved in both enhancer blocking and epigenetic
CC       remodeling at chromatin boundary via its interaction with CTCF. Acts as
CC       a suppressor of STAT3 activity by suppressing the LIF-induced STAT3
CC       transcriptional activity. Also acts as a transcription activator via
CC       its interaction with ZNF143 by participating in efficient U6 RNA
CC       polymerase III transcription. Regulates alternative splicing of a core
CC       group of genes involved in neuronal differentiation, cell cycle and DNA
CC       repair. Enables H3K36me3-coupled transcription elongation and co-
CC       transcriptional RNA processing likely via interaction with HNRNPL.
CC       {ECO:0000255|HAMAP-Rule:MF_03071, ECO:0000269|PubMed:17938208,
CC       ECO:0000269|PubMed:18378692, ECO:0000269|PubMed:36537238}.
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:0000255|HAMAP-Rule:MF_03071};
CC   -!- SUBUNIT: Interacts with p53/TP53, histone H1, CTNNB1, CTCF and PIAS3.
CC       Component of some MLL1/MLL complex, at least composed of the core
CC       components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as
CC       the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
CC       LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2,
CC       RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC       TEX10. Interacts with CHD7. Interacts with FAM124B (PubMed:23285124).
CC       Interacts with TLK2 (PubMed:33323470). Interacts with HNRNPL in an RNA-
CC       dependent manner. {ECO:0000255|HAMAP-Rule:MF_03071,
CC       ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:16949368,
CC       ECO:0000269|PubMed:17938208, ECO:0000269|PubMed:18378692,
CC       ECO:0000269|PubMed:20453063, ECO:0000269|PubMed:23285124,
CC       ECO:0000269|PubMed:33323470, ECO:0000269|PubMed:36537238}.
CC   -!- INTERACTION:
CC       Q9HCK8; O00154: ACOT7; NbExp=2; IntAct=EBI-1169146, EBI-948905;
CC       Q9HCK8; Q9UBL3: ASH2L; NbExp=2; IntAct=EBI-1169146, EBI-540797;
CC       Q9HCK8; Q15291: RBBP5; NbExp=2; IntAct=EBI-1169146, EBI-592823;
CC       Q9HCK8; P61964: WDR5; NbExp=3; IntAct=EBI-1169146, EBI-540834;
CC       Q9HCK8; O95365: ZBTB7A; NbExp=2; IntAct=EBI-1169146, EBI-2795384;
CC       Q9HCK8-2; Q9P2D1: CHD7; NbExp=3; IntAct=EBI-4410319, EBI-3951683;
CC       Q9HCK8-2; Q9H5Z6-1: FAM124B; NbExp=3; IntAct=EBI-4410319, EBI-30872379;
CC       Q9HCK8-2; Q9H5Z6-2: FAM124B; NbExp=2; IntAct=EBI-4410319, EBI-11986315;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03071,
CC       ECO:0000269|PubMed:18378692, ECO:0000269|PubMed:20453063,
CC       ECO:0000269|PubMed:36537238}. Note=Localizes to the promoter regions of
CC       several CTNNB1-responsive genes. Also present at known CTCF target
CC       sites. {ECO:0000255|HAMAP-Rule:MF_03071}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9HCK8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9HCK8-2; Sequence=VSP_017270;
CC   -!- PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_03071}.
CC   -!- DISEASE: Intellectual developmental disorder with autism and
CC       macrocephaly (IDDAM) [MIM:615032]: An autosomal dominant disorder
CC       characterized by impaired intellectual development, a highly penetrant
CC       autism spectrum phenotype, and macrocephaly. Other common features
CC       include tall stature, gastrointestinal symptoms, distinct facial
CC       features, sleep problems, and attention problems.
CC       {ECO:0000269|PubMed:23160955, ECO:0000269|PubMed:26637798}.
CC       Note=Disease susceptibility is associated with variants affecting the
CC       gene represented in this entry.
CC   -!- MISCELLANEOUS: Its gene is located in the 14q11.2 region of the genome
CC       which is associated with developmental delay, cognitive impairment and
CC       similar minor anomalies in some children, suggesting that it may be a
CC       good candidate for the phenotype.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. CHD8 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_03071}.
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DR   EMBL; CR749315; CAH18170.1; -; mRNA.
DR   EMBL; AL834524; CAD39180.1; -; mRNA.
DR   EMBL; AL135744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL161747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CB043942; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AB046784; BAB13390.3; -; mRNA.
DR   EMBL; AK131077; BAC85127.1; -; mRNA.
DR   EMBL; BC011695; AAH11695.2; -; mRNA.
DR   EMBL; BC025964; AAH25964.1; -; mRNA.
DR   EMBL; BC036920; AAH36920.1; -; mRNA.
DR   EMBL; BC063693; AAH63693.1; -; mRNA.
DR   EMBL; BC073903; AAH73903.1; -; mRNA.
DR   EMBL; BC098452; AAH98452.1; -; mRNA.
DR   CCDS; CCDS45081.1; -. [Q9HCK8-2]
DR   CCDS; CCDS53885.1; -. [Q9HCK8-1]
DR   RefSeq; NP_001164100.1; NM_001170629.1. [Q9HCK8-1]
DR   RefSeq; NP_065971.2; NM_020920.3. [Q9HCK8-2]
DR   PDB; 2CKA; NMR; -; A=2291-2364.
DR   PDB; 2DL6; NMR; -; A=2303-2372.
DR   PDBsum; 2CKA; -.
DR   PDBsum; 2DL6; -.
DR   AlphaFoldDB; Q9HCK8; -.
DR   SMR; Q9HCK8; -.
DR   BioGRID; 121709; 172.
DR   CORUM; Q9HCK8; -.
DR   DIP; DIP-38021N; -.
DR   ELM; Q9HCK8; -.
DR   IntAct; Q9HCK8; 81.
DR   MINT; Q9HCK8; -.
DR   STRING; 9606.ENSP00000495240; -.
DR   GlyCosmos; Q9HCK8; 3 sites, 2 glycans.
DR   GlyGen; Q9HCK8; 13 sites, 2 O-linked glycans (13 sites).
DR   iPTMnet; Q9HCK8; -.
DR   MetOSite; Q9HCK8; -.
DR   PhosphoSitePlus; Q9HCK8; -.
DR   BioMuta; CHD8; -.
DR   DMDM; 317373586; -.
DR   EPD; Q9HCK8; -.
DR   jPOST; Q9HCK8; -.
DR   MassIVE; Q9HCK8; -.
DR   MaxQB; Q9HCK8; -.
DR   PaxDb; 9606-ENSP00000382863; -.
DR   PeptideAtlas; Q9HCK8; -.
DR   ProteomicsDB; 81748; -. [Q9HCK8-1]
DR   ProteomicsDB; 81749; -. [Q9HCK8-2]
DR   Pumba; Q9HCK8; -.
DR   Antibodypedia; 73; 151 antibodies from 21 providers.
DR   DNASU; 57680; -.
DR   Ensembl; ENST00000430710.8; ENSP00000406288.3; ENSG00000100888.15. [Q9HCK8-2]
DR   Ensembl; ENST00000557364.6; ENSP00000451601.1; ENSG00000100888.15. [Q9HCK8-1]
DR   Ensembl; ENST00000643469.1; ENSP00000495070.1; ENSG00000100888.15. [Q9HCK8-1]
DR   Ensembl; ENST00000645929.1; ENSP00000494402.1; ENSG00000100888.15. [Q9HCK8-2]
DR   Ensembl; ENST00000646647.2; ENSP00000495240.1; ENSG00000100888.15. [Q9HCK8-1]
DR   GeneID; 57680; -.
DR   KEGG; hsa:57680; -.
DR   MANE-Select; ENST00000646647.2; ENSP00000495240.1; NM_001170629.2; NP_001164100.1.
DR   UCSC; uc001war.3; human. [Q9HCK8-1]
DR   AGR; HGNC:20153; -.
DR   CTD; 57680; -.
DR   DisGeNET; 57680; -.
DR   GeneCards; CHD8; -.
DR   GeneReviews; CHD8; -.
DR   HGNC; HGNC:20153; CHD8.
DR   HPA; ENSG00000100888; Low tissue specificity.
DR   MalaCards; CHD8; -.
DR   MIM; 610528; gene.
DR   MIM; 615032; phenotype.
DR   neXtProt; NX_Q9HCK8; -.
DR   OpenTargets; ENSG00000100888; -.
DR   Orphanet; 261229; 14q11.2 microduplication syndrome.
DR   Orphanet; 642675; CHD8 overgrowth syndrome.
DR   Orphanet; 106; NON RARE IN EUROPE: Autism.
DR   PharmGKB; PA134957052; -.
DR   VEuPathDB; HostDB:ENSG00000100888; -.
DR   eggNOG; KOG0384; Eukaryota.
DR   GeneTree; ENSGT00940000153649; -.
DR   HOGENOM; CLU_000315_5_2_1; -.
DR   InParanoid; Q9HCK8; -.
DR   OMA; AYMEDHR; -.
DR   OrthoDB; 22878at2759; -.
DR   PhylomeDB; Q9HCK8; -.
DR   TreeFam; TF313572; -.
DR   PathwayCommons; Q9HCK8; -.
DR   Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR   SignaLink; Q9HCK8; -.
DR   SIGNOR; Q9HCK8; -.
DR   BioGRID-ORCS; 57680; 152 hits in 1185 CRISPR screens.
DR   ChiTaRS; CHD8; human.
DR   EvolutionaryTrace; Q9HCK8; -.
DR   GeneWiki; CHD8; -.
DR   GenomeRNAi; 57680; -.
DR   Pharos; Q9HCK8; Tbio.
DR   PRO; PR:Q9HCK8; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9HCK8; Protein.
DR   Bgee; ENSG00000100888; Expressed in sural nerve and 196 other cell types or tissues.
DR   ExpressionAtlas; Q9HCK8; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:GO_Central.
DR   GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR   GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; IMP:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; IMP:GO_Central.
DR   GO; GO:0048565; P:digestive tract development; IMP:GO_Central.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:UniProtKB.
DR   GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:GO_Central.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR   GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IMP:UniProtKB.
DR   GO; GO:0060134; P:prepulse inhibition; IEA:Ensembl.
DR   GO; GO:0035176; P:social behavior; IEA:Ensembl.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd18668; CD1_tandem_CHD5-9_like; 1.
DR   CDD; cd18663; CD2_tandem_CHD5-9_like; 1.
DR   CDD; cd18060; DEXHc_CHD8; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   Gene3D; 3.40.5.120; -; 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   HAMAP; MF_03071; CHD8; 1.
DR   InterPro; IPR006576; BRK_domain.
DR   InterPro; IPR037259; BRK_sf.
DR   InterPro; IPR034724; CHD8.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
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; PTHR46850; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR   PANTHER; PTHR46850:SF3; DNA HELICASE; 1.
DR   Pfam; PF07533; BRK; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00592; BRK; 2.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF160481; BRK domain-like; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   Genevisible; Q9HCK8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; ATP-binding; Autism;
KW   Autism spectrum disorder; Chromatin regulator; Disease variant;
KW   DNA-binding; Helicase; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation;
KW   Wnt signaling pathway.
FT   CHAIN           1..2581
FT                   /note="Chromodomain-helicase-DNA-binding protein 8"
FT                   /id="PRO_0000080233"
FT   DOMAIN          642..709
FT                   /note="Chromo 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT   DOMAIN          724..790
FT                   /note="Chromo 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT   DOMAIN          823..997
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT   DOMAIN          1137..1288
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT   REGION          22..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          253..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          429..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1692..1712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1789..2302
FT                   /note="Interaction with FAM124B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03071,
FT                   ECO:0000269|PubMed:23285124"
FT   REGION          1991..2116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2189..2229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2481..2581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           948..951
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT   COMPBIAS        43..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..389
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..466
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        488..521
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..582
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1692..1710
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2041..2055
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2075..2094
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2095..2115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2213..2229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2491..2511
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2536..2553
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         836..843
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT   MOD_RES         432
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         553
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         562
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1420
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         1424
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         1976
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1978
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1993
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         1995
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIX5"
FT   MOD_RES         2008
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT   MOD_RES         2046
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         2051
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16964243"
FT   MOD_RES         2069
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         2071
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         2182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336"
FT   MOD_RES         2200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         2202
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q09XV5"
FT   MOD_RES         2204
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q09XV5"
FT   MOD_RES         2211
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336"
FT   MOD_RES         2215
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q09XV5"
FT   MOD_RES         2223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIX5"
FT   MOD_RES         2519
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   CROSSLNK        609
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT   CROSSLNK        2025
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        2256
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447"
FT   VAR_SEQ         1..281
FT                   /note="MADPIMDLFDDPNLFGLDSLTDDSFNQVTQDPIEEALGLPSSLDSLDQMNQD
FT                   GGGGDVGNSSASELVPPPEETAPTELSKESTAPAPESITLHDYTTQPASQEQPAQPVLQ
FT                   TSTPTSGLLQVSKSQEILSQGNPFMGVSATAVSSSSAGGQPPQSAPKIVILKAPPSSSV
FT                   TGAHVAQIQAQGITSTAQPLVAGTANGGKVTFTKVLTGTPLRPGVSIVSGNTVLAAKVP
FT                   GNQAAVQRIVQPSRPVKQLVLQPVKGSAPAGNPGATGPPLKPAVTLTSTPTQ -> MK
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_017270"
FT   VARIANT         744
FT                   /note="V -> I (in IDDAM; uncertain significance;
FT                   dbSNP:rs996150988)"
FT                   /evidence="ECO:0000269|PubMed:26637798"
FT                   /id="VAR_078704"
FT   VARIANT         2498
FT                   /note="Missing (in IDDAM)"
FT                   /evidence="ECO:0000269|PubMed:23160955"
FT                   /id="VAR_069573"
FT   MUTAGEN         842
FT                   /note="K->R: Abolishes ATPase activity."
FT                   /evidence="ECO:0000269|PubMed:18378692"
FT   CONFLICT        594
FT                   /note="T -> A (in Ref. 1; CAH18170)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1008
FT                   /note="D -> N (in Ref. 1; CAH18170)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2481
FT                   /note="P -> Q (in Ref. 1; CAH18170)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2568
FT                   /note="M -> I (in Ref. 8; AAH36920)"
FT                   /evidence="ECO:0000305"
FT   STRAND          2311..2314
FT                   /evidence="ECO:0007829|PDB:2CKA"
FT   STRAND          2317..2319
FT                   /evidence="ECO:0007829|PDB:2CKA"
FT   TURN            2320..2322
FT                   /evidence="ECO:0007829|PDB:2CKA"
FT   HELIX           2328..2330
FT                   /evidence="ECO:0007829|PDB:2DL6"
FT   HELIX           2334..2343
FT                   /evidence="ECO:0007829|PDB:2CKA"
FT   STRAND          2347..2349
FT                   /evidence="ECO:0007829|PDB:2CKA"
FT   HELIX           2351..2359
FT                   /evidence="ECO:0007829|PDB:2CKA"
SQ   SEQUENCE   2581 AA;  290519 MW;  379F09DC6F814851 CRC64;
     MADPIMDLFD DPNLFGLDSL TDDSFNQVTQ DPIEEALGLP SSLDSLDQMN QDGGGGDVGN
     SSASELVPPP EETAPTELSK ESTAPAPESI TLHDYTTQPA SQEQPAQPVL QTSTPTSGLL
     QVSKSQEILS QGNPFMGVSA TAVSSSSAGG QPPQSAPKIV ILKAPPSSSV TGAHVAQIQA
     QGITSTAQPL VAGTANGGKV TFTKVLTGTP LRPGVSIVSG NTVLAAKVPG NQAAVQRIVQ
     PSRPVKQLVL QPVKGSAPAG NPGATGPPLK PAVTLTSTPT QGESKRITLV LQQPQSGGPQ
     GHRHVVLGSL PGKIVLQGNQ LAALTQAKNA QGQPAKVVTI QLQVQQPQQK IQIVPQPPSS
     QPQPQQPPST QPVTLSSVQQ AQIMGPGQSP GQRLSVPVKV VLQPQAGSSQ GASSGLSVVK
     VLSASEVAAL SSPASSAPHS GGKTGMEENR RLEHQKKQEK ANRIVAEAIA RARARGEQNI
     PRVLNEDELP SVRPEEEGEK KRRKKSAGER LKEEKPKKSK TSGASKTKGK SKLNTITPVV
     GKKRKRNTSS DNSDVEVMPA QSPREDEESS IQKRRSNRQV KRKKYTEDLD IKITDDEEEE
     EVDVTGPIKP EPILPEPVQE PDGETLPSMQ FFVENPSEED AAIVDKVLSM RIVKKELPSG
     QYTEAEEFFV KYKNYSYLHC EWATISQLEK DKRIHQKLKR FKTKMAQMRH FFHEDEEPFN
     PDYVEVDRIL DESHSIDKDN GEPVIYYLVK WCSLPYEDST WELKEDVDEG KIREFKRIQS
     RHPELKRVNR PQASAWKKLE LSHEYKNRNQ LREYQLEGVN WLLFNWYNRQ NCILADEMGL
     GKTIQSIAFL QEVYNVGIHG PFLVIAPLST ITNWEREFNT WTEMNTIVYH GSLASRQMIQ
     QYEMYCKDSR GRLIPGAYKF DALITTFEMI LSDCPELREI EWRCVIIDEA HRLKNRNCKL
     LDSLKHMDLE HKVLLTGTPL QNTVEELFSL LHFLEPSQFP SESEFLKDFG DLKTEEQVQK
     LQAILKPMML RRLKEDVEKN LAPKQETIIE VELTNIQKKY YRAILEKNFS FLSKGAGHTN
     MPNLLNTMME LRKCCNHPYL INGAEEKILT EFREACHIIP HDFHLQAMVR SAGKLVLIDK
     LLPKLKAGGH KVLIFSQMVR CLDILEDYLI QRRYLYERID GRVRGNLRQA AIDRFSKPDS
     DRFVFLLCTR AGGLGINLTA ADTCIIFDSD WNPQNDLQAQ ARCHRIGQSK AVKVYRLITR
     NSYEREMFDK ASLKLGLDKA VLQSMSGRDG NITGIQQFSK KEIEDLLRKG AYAAIMEEDD
     EGSKFCEEDI DQILLRRTTT ITIESEGKGS TFAKASFVAS ENRTDISLDD PNFWQKWAKK
     ADLDMDLLNS KNNLVIDTPR VRKQTRHFST LKDDDLVEFS DLESEDDERP RSRRHDRHHA
     YGRTDCFRVE KHLLVYGWGR WRDILSHGRF KRRMTERDVE TICRAILVYC LLHYRGDENI
     KGFIWDLISP AENGKTKELQ NHSGLSIPVP RGRKGKKVKS QSTFDIHKAD WIRKYNPDTL
     FQDESYKKHL KHQCNKVLLR VRMLYYLRQE VIGDQAEKVL GGAIASEIDI WFPVVDQLEV
     PTTWWDSEAD KSLLIGVFKH GYEKYNTMRA DPALCFLEKA GRPDDKAIAA EHRVLDNFSD
     IVEGVDFDKD CEDPEYKPLQ GPPKDQDDEG DPLMMMDEEI SVIDGDEAQV TQQPGHLFWP
     PGSALTARLR RLVTAYQRSY KREQMKIEAA ERGDRRRRRC EAAFKLKEIA RREKQQRWTR
     REQTDFYRVV STFGVEYDPD TMQFHWDRFR TFARLDKKTD ESLTKYFHGF VAMCRQVCRL
     PPAAGDEPPD PNLFIEPITE ERASRTLYRI ELLRRLREQV LCHPLLEDRL ALCQPPGPEL
     PKWWEPVRHD GELLRGAARH GVSQTDCNIM QDPDFSFLAA RMNYMQNHQA GAPAPSLSRC
     STPLLHQQYT SRTASPLPLR PDAPVEKSPE ETATQVPSLE SLTLKLEHEV VARSRPTPQD
     YEMRVSPSDT TPLVSRSVPP VKLEDEDDSD SELDLSKLSP SSSSSSSSSS SSSSTDESED
     EKEEKLTDQS RSKLYDEESL LSLTMSQDGF PNEDGEQMTP ELLLLQERQR ASEWPKDRVL
     INRIDLVCQA VLSGKWPSSR RSQEMVTGGI LGPGNHLLDS PSLTPGEYGD SPVPTPRSSS
     AASMAEEEAS AVSTAAAQFT KLRRGMDEKE FTVQIKDEEG LKLTFQKHKL MANGVMGDGH
     PLFHKKKGNR KKLVELEVEC MEEPNHLDVD LETRIPVINK VDGTLLVGED APRRAELEMW
     LQGHPEFAVD PRFLAYMEDR RKQKWQRCKK NNKAELNCLG MEPVQTANSR NGKKGHHTET
     VFNRVLPGPI APESSKKRAR RMRPDLSKMM ALMQGGSTGS LSLHNTFQHS SSGLQSVSSL
     GHSSATSASL PFMPFVMGGA PSSPHVDSST MLHHHHHHPH PHHHHHHHPG LRAPGYPSSP
     VTTASGTTLR LPPLQPEEDD DEDEEDDDDL SQGYDSSERD FSLIDDPMMP ANSDSSEDAD
     D
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