ID   CHD5_HUMAN              Reviewed;        1954 AA.
AC   Q8TDI0; O75032; Q5TG89; Q7LGH2; Q9UFR9;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 5;
DE            Short=CHD-5;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase CHD5;
GN   Name=CHD5 {ECO:0000312|EMBL:AAL98962.1}; Synonyms=KIAA0444;
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] {ECO:0000305, ECO:0000312|EMBL:AAL98962.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=12592387; DOI=10.1038/sj.onc.1206211;
RA   Thompson P.M., Gotoh T., Kok M., White P.S., Brodeur G.M.;
RT   "CHD5, a new member of the chromodomain gene family, is preferentially
RT   expressed in the nervous system.";
RL   Oncogene 22:1002-1011(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 567-1954, AND VARIANT PRO-1539.
RC   TISSUE=Testis;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 977-1954, AND VARIANT PRO-1539.
RC   TISSUE=Brain;
RX   PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA   Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA   Nomura N., Ohara O.;
RT   "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT   human brain.";
RL   DNA Res. 4:345-349(1997).
RN   [5]
RP   DISEASE.
RX   PubMed=17289567; DOI=10.1016/j.cell.2006.11.052;
RA   Bagchi A., Papazoglu C., Wu Y., Capurso D., Brodt M., Francis D.,
RA   Bredel M., Vogel H., Mills A.A.;
RT   "CHD5 is a tumor suppressor at human 1p36.";
RL   Cell 128:459-475(2007).
RN   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=21931736; DOI=10.1371/journal.pone.0024515;
RA   Potts R.C., Zhang P., Wurster A.L., Precht P., Mughal M.R., Wood W.H.,
RA   Zhang Y., Becker K.G., Mattson M.P., Pazin M.J.;
RT   "CHD5, a brain-specific paralog of Mi2 chromatin remodeling enzymes,
RT   regulates expression of neuronal genes.";
RL   PLoS ONE 6:E24515-E24515(2011).
RN   [7]
RP   FUNCTION AS A TRANSCRIPTIONAL REGULATOR, FUNCTION IN NEURON
RP   DIFFERENTIATION, INTERACTION WITH HISTONE H3K27ME3, SUBCELLULAR LOCATION,
RP   CHROMO DOMAINS, AND MUTAGENESIS OF LEU-518 AND TYR-619.
RX   PubMed=23948251; DOI=10.1016/j.devcel.2013.07.008;
RA   Egan C.M., Nyman U., Skotte J., Streubel G., Turner S., O'Connell D.J.,
RA   Rraklli V., Dolan M.J., Chadderton N., Hansen K., Farrar G.J., Helin K.,
RA   Holmberg J., Bracken A.P.;
RT   "CHD5 is required for neurogenesis and has a dual role in facilitating gene
RT   expression and polycomb gene repression.";
RL   Dev. Cell 26:223-236(2013).
RN   [8]
RP   METHYLATION AT GLN-1390, AND MUTAGENESIS OF GLN-1390.
RX   PubMed=26797129; DOI=10.1074/jbc.m115.711952;
RA   Kusevic D., Kudithipudi S., Jeltsch A.;
RT   "Substrate specificity of the HEMK2 protein glutamine methyltransferase and
RT   identification of novel substrates.";
RL   J. Biol. Chem. 291:6124-6133(2016).
RN   [9]
RP   VARIANTS [LARGE SCALE ANALYSIS] MET-45; ASN-119 AND GLY-667.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [10]
RP   VARIANTS PMNDS GLN-193; TRP-193; VAL-272; 314-GLU--ILE-1954 DEL; LYS-427;
RP   596-ARG--ILE-1954 DEL; PHE-912; ASN-1084; LEU-1124; HIS-1136; ILE-1140;
RP   MET-1419; VAL-1488 AND GLY-1714, AND INVOLVEMENT IN PMNDS.
RX   PubMed=33944996; DOI=10.1007/s00439-021-02283-2;
RG   Undiagnosed Diseases Network;
RA   Parenti I., Lehalle D., Nava C., Torti E., Leitao E., Person R.,
RA   Mizuguchi T., Matsumoto N., Kato M., Nakamura K., de Man S.A., Cope H.,
RA   Shashi V., Friedman J., Joset P., Steindl K., Rauch A., Muffels I.,
RA   van Hasselt P.M., Petit F., Smol T., Le Guyader G., Bilan F., Sorlin A.,
RA   Vitobello A., Philippe C., van de Laar I.M.B.H., van Slegtenhorst M.A.,
RA   Campeau P.M., Au P.Y.B., Nakashima M., Saitsu H., Yamamoto T., Nomura Y.,
RA   Louie R.J., Lyons M.J., Dobson A., Plomp A.S., Motazacker M.M.,
RA   Kaiser F.J., Timberlake A.T., Fuchs S.A., Depienne C., Mignot C.;
RT   "Missense and truncating variants in CHD5 in a dominant neurodevelopmental
RT   disorder with intellectual disability, behavioral disturbances, and
RT   epilepsy.";
RL   Hum. Genet. 140:1109-1120(2021).
CC   -!- FUNCTION: Chromatin-remodeling protein that binds DNA through histones
CC       and regulates gene transcription. May specifically recognize and bind
CC       trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone
CC       H3. Acts as a component of the histone deacetylase NuRD complex which
CC       participates in the remodeling of chromatin. Plays a role in the
CC       development of the nervous system by activating the expression of genes
CC       promoting neuron terminal differentiation. In parallel, it may also
CC       positively regulate the trimethylation of histone H3 at 'Lys-27'
CC       thereby specifically repressing genes that promote the differentiation
CC       into non-neuronal cell lineages. Regulates the expression of genes
CC       involved in cell proliferation and differentiation. Downstream
CC       activated genes may include CDKN2A that positively regulates the
CC       p53/TP53 pathway, which in turn, prevents cell proliferation. In
CC       spermatogenesis, it probably regulates histone hyperacetylation and the
CC       replacement of histones by transition proteins in chromatin, a crucial
CC       step in the condensation of spermatid chromatin and the production of
CC       functional spermatozoa. {ECO:0000250|UniProtKB:A2A8L1,
CC       ECO:0000269|PubMed:23948251}.
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 nucleosome remodeling and deacetylase (NuRD)
CC       repressor complex, composed of core proteins MTA1, MTA2, MTA3, RBBP4,
CC       RBBP7, HDAC1, HDAC2, MBD2, MBD3, and peripherally associated proteins
CC       CDK2AP1, CDK2AP2, GATAD2A, GATAD2B, CHD3, CHD4 and CHD5. The exact
CC       stoichiometry of the NuRD complex is unknown, and some subunits such as
CC       MBD2 and MBD3, GATAD2A and GATAD2B, and CHD3, CHD4 and CHD5 define
CC       mutually exclusive NuRD complexes. Interacts with HDAC2.
CC       {ECO:0000250|UniProtKB:A2A8L1}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21931736,
CC       ECO:0000269|PubMed:23948251}. Chromosome
CC       {ECO:0000250|UniProtKB:A2A8L1}.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in total brain, fetal
CC       brain, and cerebellum. It is also moderately expressed in the adrenal
CC       gland and detected in testis. {ECO:0000269|PubMed:12592387,
CC       ECO:0000269|PubMed:21931736}.
CC   -!- DOMAIN: The PHD domains mediate specific binding to histone H3
CC       unmethylated at 'Lys-4' and may preferentially recruit the protein to
CC       transcriptionally inactive genes. {ECO:0000250|UniProtKB:A2A8L1}.
CC   -!- DOMAIN: The chromo domains mediate specific binding to histone H3
CC       trimethylated at 'Lys-27' (H3K27me3) and may be required in neuron
CC       differentiation for proper gene regulation.
CC       {ECO:0000269|PubMed:23948251}.
CC   -!- PTM: Methylated at Gln-1390 by N6AMT1. {ECO:0000269|PubMed:26797129}.
CC   -!- DISEASE: Note=Defects in CHD5 may be a cause of the development of
CC       cancers from epithelial, neural and hematopoietic origin. CHD5 is one
CC       of the missing genes in the del(1p36), a deletion which is extremely
CC       common in this type of cancers. A decrease of its expression, results
CC       in increased susceptibility of cells to Ras-mediated transformation in
CC       vitro and in vivo (PubMed:17289567). {ECO:0000269|PubMed:17289567}.
CC   -!- DISEASE: Parenti-Mignot neurodevelopmental syndrome (PMNDS)
CC       [MIM:619873]: An autosomal dominant neurodevelopmental disorder
CC       characterized by intellectual disability, speech delay, motor delay,
CC       behavioral problems, and epilepsy. {ECO:0000269|PubMed:33944996}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000255}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/44521/CHD5";
CC   ---------------------------------------------------------------------------
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DR   EMBL; AF425231; AAL98962.1; -; mRNA.
DR   EMBL; AL031847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL035406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL117491; CAB55959.1; -; mRNA.
DR   EMBL; AB007913; BAA32289.1; -; mRNA.
DR   CCDS; CCDS57.1; -.
DR   PIR; T17269; T17269.
DR   RefSeq; NP_056372.1; NM_015557.2.
DR   PDB; 6GUU; X-ray; 2.95 A; A/B=412-649.
DR   PDBsum; 6GUU; -.
DR   AlphaFoldDB; Q8TDI0; -.
DR   SMR; Q8TDI0; -.
DR   BioGRID; 117504; 64.
DR   IntAct; Q8TDI0; 16.
DR   MINT; Q8TDI0; -.
DR   STRING; 9606.ENSP00000262450; -.
DR   iPTMnet; Q8TDI0; -.
DR   PhosphoSitePlus; Q8TDI0; -.
DR   BioMuta; CHD5; -.
DR   DMDM; 51701343; -.
DR   EPD; Q8TDI0; -.
DR   jPOST; Q8TDI0; -.
DR   MassIVE; Q8TDI0; -.
DR   MaxQB; Q8TDI0; -.
DR   PaxDb; 9606-ENSP00000262450; -.
DR   PeptideAtlas; Q8TDI0; -.
DR   ProteomicsDB; 74289; -.
DR   Antibodypedia; 27125; 155 antibodies from 29 providers.
DR   DNASU; 26038; -.
DR   Ensembl; ENST00000262450.8; ENSP00000262450.3; ENSG00000116254.18.
DR   GeneID; 26038; -.
DR   KEGG; hsa:26038; -.
DR   MANE-Select; ENST00000262450.8; ENSP00000262450.3; NM_015557.3; NP_056372.1.
DR   UCSC; uc001amb.3; human.
DR   AGR; HGNC:16816; -.
DR   CTD; 26038; -.
DR   DisGeNET; 26038; -.
DR   GeneCards; CHD5; -.
DR   HGNC; HGNC:16816; CHD5.
DR   HPA; ENSG00000116254; Group enriched (brain, pituitary gland, testis).
DR   MalaCards; CHD5; -.
DR   MIM; 610771; gene.
DR   MIM; 619873; phenotype.
DR   neXtProt; NX_Q8TDI0; -.
DR   OpenTargets; ENSG00000116254; -.
DR   Orphanet; 528084; Non-specific syndromic intellectual disability.
DR   PharmGKB; PA134969178; -.
DR   VEuPathDB; HostDB:ENSG00000116254; -.
DR   eggNOG; KOG0383; Eukaryota.
DR   GeneTree; ENSGT00940000159249; -.
DR   HOGENOM; CLU_000315_22_1_1; -.
DR   InParanoid; Q8TDI0; -.
DR   OMA; KVQKIMH; -.
DR   OrthoDB; 2910821at2759; -.
DR   PhylomeDB; Q8TDI0; -.
DR   TreeFam; TF106448; -.
DR   PathwayCommons; Q8TDI0; -.
DR   SignaLink; Q8TDI0; -.
DR   BioGRID-ORCS; 26038; 15 hits in 1161 CRISPR screens.
DR   ChiTaRS; CHD5; human.
DR   GeneWiki; CHD5; -.
DR   GenomeRNAi; 26038; -.
DR   Pharos; Q8TDI0; Tbio.
DR   PRO; PR:Q8TDI0; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q8TDI0; Protein.
DR   Bgee; ENSG00000116254; Expressed in sperm and 135 other cell types or tissues.
DR   ExpressionAtlas; Q8TDI0; baseline and differential.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016581; C:NuRD complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0061628; F:H3K27me3 modified histone binding; IDA:UniProtKB.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0021895; P:cerebral cortex neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:GO_Central.
DR   GO; GO:0035092; P:sperm DNA condensation; ISS:UniProtKB.
DR   CDD; cd18667; CD1_tandem_CHD3-4_like; 1.
DR   CDD; cd18662; CD2_tandem_CHD3-4_like; 1.
DR   CDD; cd18057; DEXHc_CHD5; 1.
DR   CDD; cd15531; PHD1_CHD_II; 1.
DR   CDD; cd15532; PHD2_CHD_II; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 2.40.50.40; -; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR012957; CHD_C2.
DR   InterPro; IPR009462; CHD_II_SANT-like.
DR   InterPro; IPR012958; CHD_N.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR028727; DEXHc_CHD5.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR009463; DUF1087.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF6; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 5; 1.
DR   Pfam; PF08074; CHDCT2; 1.
DR   Pfam; PF06461; CHDII_SANT-like; 1.
DR   Pfam; PF08073; CHDNT; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF06465; DUF1087; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM01146; DUF1086; 1.
DR   SMART; SM01147; DUF1087; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
DR   Genevisible; Q8TDI0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chromatin regulator; Chromosome;
KW   Differentiation; Disease variant; DNA-binding; Epilepsy; Helicase;
KW   Hydrolase; Intellectual disability; Metal-binding; Methylation;
KW   Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Spermatogenesis; Transcription;
KW   Transcription regulation; Tumor suppressor; Zinc; Zinc-finger.
FT   CHAIN           1..1954
FT                   /note="Chromodomain-helicase-DNA-binding protein 5"
FT                   /id="PRO_0000080230"
FT   DOMAIN          497..554
FT                   /note="Chromo 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          592..653
FT                   /note="Chromo 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   DOMAIN          712..896
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1028..1193
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   ZN_FING         343..390
FT                   /note="PHD-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         416..463
FT                   /note="PHD-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          1..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          343..653
FT                   /note="Histone-binding"
FT   REGION          549..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1351..1411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1524..1564
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1597..1640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1658..1696
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           847..850
FT                   /note="DEAH box"
FT   COMPBIAS        15..36
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..64
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        112..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        241..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..272
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1216..1230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1386..1408
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1600..1640
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         725..732
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q14839,
FT                   ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         1390
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000269|PubMed:26797129"
FT   MOD_RES         1554
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A2A8L1"
FT   VARIANT         45
FT                   /note="V -> M (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs1470692239)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035475"
FT   VARIANT         119
FT                   /note="D -> N (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035476"
FT   VARIANT         193
FT                   /note="R -> Q (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087312"
FT   VARIANT         193
FT                   /note="R -> W (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087313"
FT   VARIANT         272
FT                   /note="A -> V (in PMNDS; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087314"
FT   VARIANT         314..1954
FT                   /note="Missing (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087315"
FT   VARIANT         427
FT                   /note="E -> K (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087316"
FT   VARIANT         596..1954
FT                   /note="Missing (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087317"
FT   VARIANT         667
FT                   /note="R -> G (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035477"
FT   VARIANT         912
FT                   /note="S -> F (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087318"
FT   VARIANT         1084
FT                   /note="D -> N (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087319"
FT   VARIANT         1124
FT                   /note="P -> L (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087320"
FT   VARIANT         1136
FT                   /note="R -> H (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087321"
FT   VARIANT         1140
FT                   /note="N -> I (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087322"
FT   VARIANT         1253
FT                   /note="S -> I (in dbSNP:rs6657997)"
FT                   /id="VAR_048729"
FT   VARIANT         1419
FT                   /note="I -> M (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087323"
FT   VARIANT         1488
FT                   /note="D -> V (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087324"
FT   VARIANT         1539
FT                   /note="S -> P (in dbSNP:rs2843493)"
FT                   /evidence="ECO:0000269|PubMed:17974005,
FT                   ECO:0000269|PubMed:9455484"
FT                   /id="VAR_048730"
FT   VARIANT         1714
FT                   /note="E -> G (in PMNDS)"
FT                   /evidence="ECO:0000269|PubMed:33944996"
FT                   /id="VAR_087325"
FT   MUTAGEN         518
FT                   /note="L->A: Reduced affinity for trimethylated histone
FT                   H3K27me3."
FT                   /evidence="ECO:0000269|PubMed:23948251"
FT   MUTAGEN         619
FT                   /note="Y->E: Reduced affinity for trimethylated histone
FT                   H3K27me3."
FT                   /evidence="ECO:0000269|PubMed:23948251"
FT   MUTAGEN         1390
FT                   /note="Q->R: Abolishes methylation by N6AMT1."
FT                   /evidence="ECO:0000269|PubMed:26797129"
FT   TURN            420..422
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   STRAND          432..435
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   TURN            440..442
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   STRAND          443..445
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   HELIX           458..461
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   STRAND          469..477
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   STRAND          509..515
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   HELIX           520..522
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   STRAND          524..527
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   HELIX           528..534
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   HELIX           536..545
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   STRAND          548..550
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   HELIX           575..581
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   HELIX           583..585
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   HELIX           589..592
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   STRAND          593..602
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   STRAND          608..614
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   HELIX           619..621
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   STRAND          623..628
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   HELIX           634..642
FT                   /evidence="ECO:0007829|PDB:6GUU"
FT   HELIX           644..647
FT                   /evidence="ECO:0007829|PDB:6GUU"
SQ   SEQUENCE   1954 AA;  223050 MW;  E333062B5B55E71F CRC64;
     MRGPVGTEEE LPRLFAEEME NEDEMSEEED GGLEAFDDFF PVEPVSLPKK KKPKKLKENK
     CKGKRKKKEG SNDELSENEE DLEEKSESEG SDYSPNKKKK KKLKDKKEKK AKRKKKDEDE
     DDNDDGCLKE PKSSGQLMAE WGLDDVDYLF SEEDYHTLTN YKAFSQFLRP LIAKKNPKIP
     MSKMMTVLGA KWREFSANNP FKGSSAAAAA AAVAAAVETV TISPPLAVSP PQVPQPVPIR
     KAKTKEGKGP GVRKKIKGSK DGKKKGKGKK TAGLKFRFGG ISNKRKKGSS SEEDEREESD
     FDSASIHSAS VRSECSAALG KKSKRRRKKK RIDDGDGYET DHQDYCEVCQ QGGEIILCDT
     CPRAYHLVCL DPELEKAPEG KWSCPHCEKE GIQWEPKDDD DEEEEGGCEE EEDDHMEFCR
     VCKDGGELLC CDACPSSYHL HCLNPPLPEI PNGEWLCPRC TCPPLKGKVQ RILHWRWTEP
     PAPFMVGLPG PDVEPSLPPP KPLEGIPERE FFVKWAGLSY WHCSWVKELQ LELYHTVMYR
     NYQRKNDMDE PPPFDYGSGD EDGKSEKRKN KDPLYAKMEE RFYRYGIKPE WMMIHRILNH
     SFDKKGDVHY LIKWKDLPYD QCTWEIDDID IPYYDNLKQA YWGHRELMLG EDTRLPKRLL
     KKGKKLRDDK QEKPPDTPIV DPTVKFDKQP WYIDSTGGTL HPYQLEGLNW LRFSWAQGTD
     TILADEMGLG KTVQTIVFLY SLYKEGHSKG PYLVSAPLST IINWEREFEM WAPDFYVVTY
     TGDKESRSVI RENEFSFEDN AIRSGKKVFR MKKEVQIKFH VLLTSYELIT IDQAILGSIE
     WACLVVDEAH RLKNNQSKFF RVLNSYKIDY KLLLTGTPLQ NNLEELFHLL NFLTPERFNN
     LEGFLEEFAD ISKEDQIKKL HDLLGPHMLR RLKADVFKNM PAKTELIVRV ELSQMQKKYY
     KFILTRNFEA LNSKGGGNQV SLLNIMMDLK KCCNHPYLFP VAAVEAPVLP NGSYDGSSLV
     KSSGKLMLLQ KMLKKLRDEG HRVLIFSQMT KMLDLLEDFL EYEGYKYERI DGGITGGLRQ
     EAIDRFNAPG AQQFCFLLST RAGGLGINLA TADTVIIYDS DWNPHNDIQA FSRAHRIGQN
     KKVMIYRFVT RASVEERITQ VAKRKMMLTH LVVRPGLGSK SGSMTKQELD DILKFGTEEL
     FKDDVEGMMS QGQRPVTPIP DVQSSKGGNL AASAKKKHGS TPPGDNKDVE DSSVIHYDDA
     AISKLLDRNQ DATDDTELQN MNEYLSSFKV AQYVVREEDG VEEVEREIIK QEENVDPDYW
     EKLLRHHYEQ QQEDLARNLG KGKRIRKQVN YNDASQEDQE WQDELSDNQS EYSIGSEDED
     EDFEERPEGQ SGRRQSRRQL KSDRDKPLPP LLARVGGNIE VLGFNARQRK AFLNAIMRWG
     MPPQDAFNSH WLVRDLRGKS EKEFRAYVSL FMRHLCEPGA DGAETFADGV PREGLSRQHV
     LTRIGVMSLV RKKVQEFEHV NGKYSTPDLI PEGPEGKKSG EVISSDPNTP VPASPAHLLP
     APLGLPDKME AQLGYMDEKD PGAQKPRQPL EVQALPAALD RVESEDKHES PASKERAREE
     RPEETEKAPP SPEQLPREEV LPEKEKILDK LELSLIHSRG DSSELRPDDT KAEEKEPIET
     QQNGDKEEDD EGKKEDKKGK FKFMFNIADG GFTELHTLWQ NEERAAVSSG KIYDIWHRRH
     DYWLLAGIVT HGYARWQDIQ NDPRYMILNE PFKSEVHKGN YLEMKNKFLA RRFKLLEQAL
     VIEEQLRRAA YLNMTQDPNH PAMALNARLA EVECLAESHQ HLSKESLAGN KPANAVLHKV
     LNQLEELLSD MKADVTRLPS MLSRIPPVAA RLQMSERSIL SRLTNRAGDP TIQQGAFGSS
     QMYSNNFGPN FRGPGPGGIV NYNQMPLGPY VTDI
//