CHD6_HUMAN
ID CHD6_HUMAN Reviewed; 2715 AA.
AC Q8TD26; Q5JYQ0; Q5TGZ9; Q5TH00; Q5TH01; Q8IZR2; Q8WTY0; Q9H4H6; Q9H6D4;
AC Q9NTT7; Q9P2L1;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 6;
DE Short=CHD-6;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase CHD6;
DE AltName: Full=Radiation-induced gene B protein;
GN Name=CHD6; Synonyms=CHD5, KIAA1335, RIGB;
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 1).
RX PubMed=11889561; DOI=10.1007/s00335-001-3042-6;
RA Schuster E.F., Stoeger R.J.;
RT "CHD5 defines a new subfamily of chromodomain-SWI2/SNF2-like helicases.";
RL Mamm. Genome 13:117-119(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2442-2715 (ISOFORM 1).
RC TISSUE=Hippocampus, Lymph, and Retinoblastoma;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 299-2715 (ISOFORM 3).
RA Zhou P.-K., Sui J.-L.;
RT "cDNA cloning and transcriptional controlling of a novel radiation-induced
RT gene and its function analysis.";
RL Zhonghua Fang She Yi Xue Yu Fang Hu Za Zhi 22:73-77(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 675-2715 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 759-1527 (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP FUNCTION IN TRANSCRIPTION, AND INTERACTION WITH NFE2L2.
RX PubMed=16314513; DOI=10.1128/mcb.25.24.10895-10906.2005;
RA Nioi P., Nguyen T., Sherratt P.J., Pickett C.B.;
RT "The carboxy-terminal Neh3 domain of Nrf2 is required for transcriptional
RT activation.";
RL Mol. Cell. Biol. 25:10895-10906(2005).
RN [9]
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND REGION.
RX PubMed=17027977; DOI=10.1016/j.febslet.2006.09.049;
RA Lutz T., Stoger R., Nieto A.;
RT "CHD6 is a DNA-dependent ATPase and localizes at nuclear sites of mRNA
RT synthesis.";
RL FEBS Lett. 580:5851-5857(2006).
RN [10]
RP DISEASE.
RX PubMed=18627065; DOI=10.1002/ajmg.a.32419;
RA Kalscheuer V.M., Feenstra I., Van Ravenswaaij-Arts C.M., Smeets D.F.,
RA Menzel C., Ullmann R., Musante L., Ropers H.H.;
RT "Disruption of the TCF4 gene in a girl with mental retardation but without
RT the classical Pitt-Hopkins syndrome.";
RL Am. J. Med. Genet. A 146A:2053-2059(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN PAPILLOMAVIRUS
RP PROTEIN E8^E2C.
RX PubMed=20631145; DOI=10.1128/jvi.00678-10;
RA Fertey J., Ammermann I., Winkler M., Stoeger R., Iftner T., Stubenrauch F.;
RT "Interaction of the papillomavirus E8--E2C protein with the cellular CHD6
RT protein contributes to transcriptional repression.";
RL J. Virol. 84:9505-9515(2010).
RN [13]
RP SUBCELLULAR LOCATION, INTERACTION WITH INFLUENZA A POLYMERASE COMPLEX
RP (MICROBIAL INFECTION), AND FUNCTION (MICROBIAL INFECTION).
RX PubMed=21899694; DOI=10.1111/j.1462-5822.2011.01679.x;
RA Alfonso R., Lutz T., Rodriguez A., Chavez J.P., Rodriguez P., Gutierrez S.,
RA Nieto A.;
RT "CHD6 chromatin remodeler is a negative modulator of influenza virus
RT replication that relocates to inactive chromatin upon infection.";
RL Cell. Microbiol. 13:1894-1906(2011).
RN [14]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=23408615; DOI=10.1128/jvi.00554-12;
RA Alfonso R., Rodriguez A., Rodriguez P., Lutz T., Nieto A.;
RT "CHD6, a cellular repressor of influenza virus replication, is degraded in
RT human alveolar epithelial cells and mice lungs during infection.";
RL J. Virol. 87:4534-4544(2013).
RN [15]
RP FUNCTION.
RX PubMed=28533432; DOI=10.1074/jbc.m117.779470;
RA Manning B.J., Yusufzai T.;
RT "The ATP-dependent Chromatin Remodeling Enzymes CHD6, CHD7, and CHD8
RT Exhibit Distinct Nucleosome Binding and Remodeling Activities.";
RL J. Biol. Chem. 292:11927-11936(2017).
RN [16]
RP STRUCTURE BY NMR OF 371-431.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of chromo domain 2 in chromodomain-helicase-DNA-binding
RT protein 6.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: DNA-dependent ATPase that plays a role in chromatin
CC remodeling. Regulates transcription by disrupting nucleosomes in a
CC largely non-sliding manner which strongly increases the accessibility
CC of chromatin (PubMed:28533432). Activates transcription of specific
CC genes in response to oxidative stress through interaction with NFE2L2.
CC {ECO:0000269|PubMed:16314513, ECO:0000269|PubMed:28533432}.
CC -!- FUNCTION: (Microbial infection) Acts as a transcriptional repressor of
CC different viruses including influenza virus or papillomavirus. During
CC influenza virus infection, the viral polymerase complex localizes CHD6
CC to inactive chromatin where it gets degraded in a proteasome
CC independent-manner. {ECO:0000269|PubMed:20631145,
CC ECO:0000269|PubMed:21899694, ECO:0000269|PubMed:23408615}.
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:0000269|PubMed:17027977};
CC -!- SUBUNIT: Interacts with NFE2L2; involved in activation of the
CC transcription. {ECO:0000269|PubMed:16314513}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the influenza A
CC polymerase complex composed fo PB1, PB2 and PA.
CC {ECO:0000269|PubMed:21899694}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via N-terminus) with human
CC papillomavirus protein E8^E2C (via C-terminus); this interaction
CC induces transcriptional repression of the viral genome.
CC {ECO:0000269|PubMed:20631145}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:17027977, ECO:0000269|PubMed:21899694}.
CC Note=Enriched at sites of mRNA synthesis (PubMed:17027977). During
CC influenza A virus infection, localizes to inactive chromatin.
CC {ECO:0000269|PubMed:17027977, ECO:0000269|PubMed:21899694}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TD26-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TD26-2; Sequence=VSP_015296, VSP_015297, VSP_015298;
CC Name=3;
CC IsoId=Q8TD26-3; Sequence=VSP_015299, VSP_015300, VSP_015301;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DISEASE: Note=A chromosomal aberration disrupting CHD6 has been found
CC in a patient with mild to moderate intellectual disability and minor
CC facial anomalies. Translocation t(18;20)(q21.1;q11.2) with TCF4
CC producing a CHD6-TCF4 fusion transcript (PubMed:18627065).
CC {ECO:0000269|PubMed:18627065}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK56405.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAN59903.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15325.1; Type=Miscellaneous discrepancy; Note=The sequence differs from position 1528 onward for unknown reasons.; Evidence={ECO:0000305};
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DR EMBL; AY034072; AAK56405.1; ALT_INIT; mRNA.
DR EMBL; AL031667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL031669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021907; AAH21907.1; -; mRNA.
DR EMBL; BC039860; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC040016; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF525085; AAN59903.1; ALT_INIT; mRNA.
DR EMBL; AB037756; BAA92573.2; -; mRNA.
DR EMBL; AK026022; BAB15325.1; ALT_SEQ; mRNA.
DR CCDS; CCDS13317.1; -. [Q8TD26-1]
DR RefSeq; NP_115597.3; NM_032221.4. [Q8TD26-1]
DR PDB; 2EPB; NMR; -; A=371-431.
DR PDBsum; 2EPB; -.
DR BMRB; Q8TD26; -.
DR SMR; Q8TD26; -.
DR BioGRID; 123931; 51.
DR IntAct; Q8TD26; 29.
DR MINT; Q8TD26; -.
DR STRING; 9606.ENSP00000362330; -.
DR CarbonylDB; Q8TD26; -.
DR GlyGen; Q8TD26; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TD26; -.
DR PhosphoSitePlus; Q8TD26; -.
DR BioMuta; CHD6; -.
DR DMDM; 296439466; -.
DR EPD; Q8TD26; -.
DR jPOST; Q8TD26; -.
DR MassIVE; Q8TD26; -.
DR MaxQB; Q8TD26; -.
DR PaxDb; Q8TD26; -.
DR PeptideAtlas; Q8TD26; -.
DR PRIDE; Q8TD26; -.
DR ProteomicsDB; 74223; -. [Q8TD26-1]
DR ProteomicsDB; 74224; -. [Q8TD26-2]
DR ProteomicsDB; 74225; -. [Q8TD26-3]
DR Antibodypedia; 27058; 52 antibodies from 15 providers.
DR DNASU; 84181; -.
DR Ensembl; ENST00000373222.3; ENSP00000362319.3; ENSG00000124177.16. [Q8TD26-2]
DR Ensembl; ENST00000373233.8; ENSP00000362330.3; ENSG00000124177.16. [Q8TD26-1]
DR GeneID; 84181; -.
DR KEGG; hsa:84181; -.
DR MANE-Select; ENST00000373233.8; ENSP00000362330.3; NM_032221.5; NP_115597.3.
DR UCSC; uc002xka.3; human. [Q8TD26-1]
DR CTD; 84181; -.
DR DisGeNET; 84181; -.
DR GeneCards; CHD6; -.
DR HGNC; HGNC:19057; CHD6.
DR HPA; ENSG00000124177; Low tissue specificity.
DR MIM; 616114; gene.
DR neXtProt; NX_Q8TD26; -.
DR OpenTargets; ENSG00000124177; -.
DR PharmGKB; PA134974700; -.
DR VEuPathDB; HostDB:ENSG00000124177; -.
DR eggNOG; KOG0384; Eukaryota.
DR GeneTree; ENSGT00940000158986; -.
DR HOGENOM; CLU_000315_5_1_1; -.
DR InParanoid; Q8TD26; -.
DR OMA; SLENMMY; -.
DR OrthoDB; 7181at2759; -.
DR PhylomeDB; Q8TD26; -.
DR TreeFam; TF313572; -.
DR PathwayCommons; Q8TD26; -.
DR SignaLink; Q8TD26; -.
DR BioGRID-ORCS; 84181; 13 hits in 1096 CRISPR screens.
DR ChiTaRS; CHD6; human.
DR EvolutionaryTrace; Q8TD26; -.
DR GenomeRNAi; 84181; -.
DR Pharos; Q8TD26; Tbio.
DR PRO; PR:Q8TD26; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8TD26; protein.
DR Bgee; ENSG00000124177; Expressed in sural nerve and 187 other tissues.
DR ExpressionAtlas; Q8TD26; baseline and differential.
DR Genevisible; Q8TD26; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:UniProtKB.
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:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF160481; SSF160481; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
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 DNA-binding; Helicase; Host-virus interaction; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..2715
FT /note="Chromodomain-helicase-DNA-binding protein 6"
FT /id="PRO_0000080231"
FT DOMAIN 292..343
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 375..439
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 473..647
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 787..956
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1449..1503
FT /note="Myb-like"
FT REGION 1..747
FT /note="Required for DNA-dependent ATPase activity"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1318..1390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2027..2063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2116..2148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2321..2351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2373..2422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2547..2602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2648..2715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 598..601
FT /note="DEAH box"
FT COMPBIAS 15..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2027..2050
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2116..2146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2547..2564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2565..2584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 486..493
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 1..10
FT /note="MKMKIQKKEK -> MCQSHMIGFCTSSVNEETETQGDQISCPNPTTLVFRTQ
FT ISSLPSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015296"
FT VAR_SEQ 325..338
FT /note="FSYLHCKWATMEEL -> LYVYLKYSLYLGFI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015297"
FT VAR_SEQ 339..2715
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015298"
FT VAR_SEQ 592..1108
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015299"
FT VAR_SEQ 1337..1339
FT /note="GNT -> QHR (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015300"
FT VAR_SEQ 1340..2715
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_015301"
FT VARIANT 780
FT /note="Q -> H (in dbSNP:rs4474937)"
FT /id="VAR_059213"
FT VARIANT 2161
FT /note="H -> Q (in dbSNP:rs3817893)"
FT /id="VAR_023363"
FT CONFLICT 134
FT /note="K -> E (in Ref. 1; AAK56405)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="T -> A (in Ref. 4; AAN59903)"
FT /evidence="ECO:0000305"
FT CONFLICT 1031
FT /note="E -> K (in Ref. 1; AAK56405)"
FT /evidence="ECO:0000305"
FT CONFLICT 2442..2447
FT /note="RGRRPR -> EIVGLE (in Ref. 3; AAH21907)"
FT /evidence="ECO:0000305"
FT CONFLICT 2663
FT /note="D -> G (in Ref. 1; AAK56405)"
FT /evidence="ECO:0000305"
FT STRAND 379..387
FT /evidence="ECO:0007829|PDB:2EPB"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:2EPB"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:2EPB"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:2EPB"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:2EPB"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:2EPB"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:2EPB"
SQ SEQUENCE 2715 AA; 305412 MW; 5B3FEC537340A8B7 CRC64;
MKMKIQKKEK QLSNLKVLNH SPMSDASVNF DYKSPSPFDC STDQEEKIED VASHCLPQKD
LYTAEEEAAT LFPRKMTSHN GMEDSGGGGT GVKKKRKKKE PGDQEGAAKG SKDREPKPKR
KREPKEPKEP RKAKEPKKAK EHKEPKQKDG AKKARKPREA SGTKEAKEKR SCTDSAARTK
SRKASKEQGP TPVEKKKKGK RKSETTVESL ELDQGLTNPS LRSPEESTES TDSQKRRSGR
QVKRRKYNED LDFKVVDDDG ETIAVLGAGR TSALSASTLA WQAEEPPEDD ANIIEKILAS
KTVQEVHPGE PPFDLELFYV KYRNFSYLHC KWATMEELEK DPRIAQKIKR FRNKQAQMKH
IFTEPDEDLF NPDYVEVDRI LEVAHTKDAE TGEEVTHYLV KWCSLPYEES TWELEEDVDP
AKVKEFESLQ VLPEIKHVER PASDSWQKLE KSREYKNSNQ LREYQLEGMN WLLFNWYNRK
NCILADEMGL GKTIQSITFL SEIFLRGIHG PFLIIAPLST ITNWEREFRT WTEMNAIVYH
GSQISRQMIQ QYEMVYRDAQ GNPLSGVFKF HVVITTFEMI LADCPELKKI HWSCVIIDEA
HRLKNRNCKL LEGLKLMALE HKVLLTGTPL QNSVEELFSL LNFLEPSQFP SETAFLEEFG
DLKTEEQVKK LQSILKPMML RRLKDDVEKN LAPKQETIIE VELTNIQKKY YRAILEKNFS
FLTKGANQHN MPNLINTMME LRKCCNHPYL INGAEEKILE DFRKTHSPDA PDFQLQAMIQ
AAGKLVLIDK LLPKLIAGGH KVLIFSQMVR CLDILEDYLI QRRYTYERID GRVRGNLRQA
AIDRFCKPDS DRFVFLLCTR AGGLGINLTA ADTCIIFDSD WNPQNDLQAQ ARCHRIGQSK
AVKVYRLITR NSYEREMFDK ASLKLGLDKA VLQDINRKGG TNGVQQLSKM EVEDLLRKGA
YGALMDEEDE GSKFCEEDID QILQRRTHTI TIQSEGKGST FAKASFVASG NRTDISLDDP
NFWQKWAKIA ELDTEAKNEK ESLVIDRPRV RKQTKHYNSF EEDELMEFSE LDSDSDERPT
RSRRLNDKAR RYLRAECFRV EKNLLIFGWG RWKDILTHGR FKWHLNEKDM EMICRALLVY
CVKHYKGDEK IKSFIWELIT PTKDGQAQTL QNHSGLSAPV PRGRKGKKTK NQLLIPELKD
ADWLATCNPE VVLHDDGYKK HLKQHCNKVL LRVRMLYYLK AEILGEAAEK AFEGSPAREL
DVPLPDIDYM EIPVDWWDAE ADKSLLIGVF KHGYERYNAM RADPALCFLE KVGMPDEKSL
SAEQGVTDGT SDIPERGNTD KEDNAEDKVD GLQKQTESSS DGGDGVFSEK KDDSRAAQDG
SDPDKSPWPV SSALTARLRR LVTVYQRCNR KELCRPEILG PGNQGYWVQE EMFRRTSEMD
LINKEAQKRW TRREQADFYR TVSSFGVVYD QEKKTFDWTQ FRIISRLDKK SDESLEQYFY
SFVAMCRNVC RLPTWKDGGP PDTTIYVEPI TEERAARTLY RIELLRKVRE QVLKCPQLHE
RLQLCRPSLY LPVWWECGKH DRDLLIGTAK HGLNRTDCYI MNDPQLSFLD AYRNYAQHKR
SGTQAPGNLC CLYQTNSKLY ESLTYSQMSR TSESLENEPE NLVRVESRDD HLSLPDVTCE
NFISKVQDVI SINHDESLLP ESLESMMYGK KVLSQEPSSF QESPSTNTES RKDVITISIS
KDGNCQSGGP EAEIASGPTF MGSLEAGGVA QANIKNGKHL LMSISKEGEL CCSEAGQRPE
NIGQLEAKCL ASPSLNPGNE SGFVDMCSLS VCDSKRNLSS DQQLIDLLEN KSLESKLILS
QNHSDEEEEE EENEEENLAM AVGMGERPEV LHLTEPTTNI SREKNQGFQD ETKKGSLEVA
NQTPGLQRAF PAPAACQCHC KHMERWMHGL ENDEFEIEKP KAYIPDLFKS KTNTIAMEGE
PTAIPSQPFK VKHELLKEPW KESAEGQNVF PTYPLEGSEL KSEDMDFENK DDYDRDGNCH
SQDYPGKYSE EESKSSTSGI TGDIGDELQE ARAPTIAQLL QEKTLYSFSE WPKDRVIINR
LDNICHVVLK GKWPSSQQYE PSGTLPTPVL TSSAGSRTSL SEPEAAEHSF SNGAALAAQI
HKESFLAPVF TKDEQKHRRP YEFEVERDAK ARGLEQFSAT HGHTPIILNG WHGESAMDLS
CSSEGSPGAT SPFPVSASTP KIGAISSLQG ALGMDLSGIL QAGLIHPVTG QIVNGSLRRD
DAATRRRRGR RKHVEGGMDL IFLKEQTLQA GILEVHEDPG QATLSTTHPE GPGPATSAPE
PATAASSQAE KSIPSKSLLD WLRQQADYSL EVPGFGANFS DKPKQRRPRC KEPGKLDVSS
LSGEERVPAI PKEPGLRGFL PENKFNHTLA EPILRDTGPR RRGRRPRSEL LKAPSIVADS
PSGMGPLFMN GLIAGMDLVG LQNMRNMPGI PLTGLVGFPA GFATMPTGEE VKSTLSMLPM
MLPGMAAVPQ MFGVGGLLSP PMATTCTSTA PASLSSTTKS GTAVTEKTAE DKPSSHDVKT
DTLAEDKPGP GPFSDQSEPA ITTSSPVAFN PFLIPGVSPG LIYPSMFLSP GMGMALPAMQ
QARHSEIVGL ESQKRKKKKT KGDNPNSHPE PAPSCEREPS GDENCAEPSA PLPAEREHGA
QAGEGALKDS NNDTN
