GenomeNet

Database: UniProt
Entry: Q8TD26
LinkDB: Q8TD26
Original site: Q8TD26 
ID   CHD6_HUMAN              Reviewed;        2715 AA.
AC   Q8TD26; Q5JYQ0; Q5TGZ9; Q5TH00; Q5TH01; Q8IZR2; Q8WTY0; Q9H4H6;
AC   Q9H6D4; Q9NTT7; Q9P2L1;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 4.
DT   16-OCT-2019, entry version 175.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   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.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   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.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   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
RP   SEQUENCE [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
RT   project: 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-
RT   induced 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.
RT   The complete sequences of 150 new cDNA clones from brain which code
RT   for large 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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
RT   transcriptional 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
RT   without 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
RP   PAPILLOMAVIRUS PROTEIN E8^E2C.
RX   PubMed=20631145; DOI=10.1128/jvi.00678-10;
RA   Fertey J., Ammermann I., Winkler M., Stoeger R., Iftner T.,
RA   Stubenrauch F.;
RT   "Interaction of the papillomavirus E8--E2C protein with the cellular
RT   CHD6 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.,
RA   Gutierrez S., 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
RT   degraded in human alveolar epithelial cells and mice lungs during
RT   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-
RT   binding 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
CC       accessibility of chromatin (PubMed:28533432). Activates
CC       transcription of specific genes in response to oxidative stress
CC       through interaction with NFE2L2. {ECO:0000269|PubMed:16314513,
CC       ECO:0000269|PubMed:28533432}.
CC   -!- FUNCTION: (Microbial infection) Acts as a transcriptional
CC       repressor of different viruses including influenza virus or
CC       papillomavirus. During influenza virus infection, the viral
CC       polymerase complex localizes CHD6 to inactive chromatin where it
CC       gets degraded in a proteasome independent-manner.
CC       {ECO:0000269|PubMed:20631145, ECO:0000269|PubMed:21899694,
CC       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
CC       human papillomavirus protein E8^E2C (via C-terminus); this
CC       interaction induces transcriptional repression of the viral
CC       genome. {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         Note=Gene prediction based on EST data.;
CC       Name=3;
CC         IsoId=Q8TD26-3; Sequence=VSP_015299, VSP_015300, VSP_015301;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DISEASE: Note=A chromosomal aberration disrupting CHD6 has been
CC       found in a patient with mild to moderate mental retardation and
CC       minor facial anomalies. Translocation t(18;20)(q21.1;q11.2) with
CC       TCF4 producing a CHD6-TCF4 fusion transcript (PubMed:18627065).
CC       {ECO:0000269|PubMed:18627065}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {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};
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   SMR; Q8TD26; -.
DR   BioGrid; 123931; 21.
DR   IntAct; Q8TD26; 15.
DR   MINT; Q8TD26; -.
DR   STRING; 9606.ENSP00000362330; -.
DR   CarbonylDB; Q8TD26; -.
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   Ensembl; ENST00000373222; ENSP00000362319; ENSG00000124177. [Q8TD26-2]
DR   Ensembl; ENST00000373233; ENSP00000362330; ENSG00000124177. [Q8TD26-1]
DR   GeneID; 84181; -.
DR   KEGG; hsa:84181; -.
DR   UCSC; uc002xka.3; human. [Q8TD26-1]
DR   CTD; 84181; -.
DR   DisGeNET; 84181; -.
DR   GeneCards; CHD6; -.
DR   HGNC; HGNC:19057; CHD6.
DR   HPA; HPA015543; -.
DR   MIM; 616114; gene.
DR   neXtProt; NX_Q8TD26; -.
DR   OpenTargets; ENSG00000124177; -.
DR   PharmGKB; PA134974700; -.
DR   eggNOG; KOG0383; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   GeneTree; ENSGT00940000158986; -.
DR   InParanoid; Q8TD26; -.
DR   KO; K14436; -.
DR   OMA; AKDERKH; -.
DR   OrthoDB; 7181at2759; -.
DR   PhylomeDB; Q8TD26; -.
DR   TreeFam; TF313572; -.
DR   ChiTaRS; CHD6; human.
DR   EvolutionaryTrace; Q8TD26; -.
DR   GenomeRNAi; 84181; -.
DR   Pharos; Q8TD26; -.
DR   PRO; PR:Q8TD26; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   Bgee; ENSG00000124177; Expressed in 197 organ(s), highest expression level in lung.
DR   ExpressionAtlas; Q8TD26; baseline and differential.
DR   Genevisible; Q8TD26; HS.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:UniProtKB.
DR   GO; GO:0001221; F:transcription cofactor binding; IPI:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:UniProtKB.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.10810; -; 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_N; 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   Complete proteome; DNA-binding; Helicase; Host-virus interaction;
KW   Hydrolase; Nucleotide-binding; Nucleus; Polymorphism;
KW   Reference proteome; Repeat; Transcription; Transcription regulation.
FT   CHAIN         1   2715       Chromodomain-helicase-DNA-binding protein
FT                                6.
FT                                /FTId=PRO_0000080231.
FT   DOMAIN      292    343       Chromo 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      375    439       Chromo 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      473    647       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      787    956       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     1449   1503       Myb-like.
FT   NP_BIND     486    493       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        1    747       Required for DNA-dependent ATPase
FT                                activity.
FT   MOTIF       598    601       DEAH box.
FT   COMPBIAS     93    202       Lys-rich.
FT   VAR_SEQ       1     10       MKMKIQKKEK -> MCQSHMIGFCTSSVNEETETQGDQISC
FT                                PNPTTLVFRTQISSLPSL (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_015296.
FT   VAR_SEQ     325    338       FSYLHCKWATMEEL -> LYVYLKYSLYLGFI (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_015297.
FT   VAR_SEQ     339   2715       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_015298.
FT   VAR_SEQ     592   1108       Missing (in isoform 3).
FT                                {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_015299.
FT   VAR_SEQ    1337   1339       GNT -> QHR (in isoform 3).
FT                                {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_015300.
FT   VAR_SEQ    1340   2715       Missing (in isoform 3).
FT                                {ECO:0000303|Ref.4}.
FT                                /FTId=VSP_015301.
FT   VARIANT     780    780       Q -> H (in dbSNP:rs4474937).
FT                                /FTId=VAR_059213.
FT   VARIANT    2161   2161       H -> Q (in dbSNP:rs3817893).
FT                                /FTId=VAR_023363.
FT   CONFLICT    134    134       K -> E (in Ref. 1; AAK56405).
FT                                {ECO:0000305}.
FT   CONFLICT    575    575       T -> A (in Ref. 4; AAN59903).
FT                                {ECO:0000305}.
FT   CONFLICT   1031   1031       E -> K (in Ref. 1; AAK56405).
FT                                {ECO:0000305}.
FT   CONFLICT   2442   2447       RGRRPR -> EIVGLE (in Ref. 3; AAH21907).
FT                                {ECO:0000305}.
FT   CONFLICT   2663   2663       D -> G (in Ref. 1; AAK56405).
FT                                {ECO:0000305}.
FT   STRAND      379    387       {ECO:0000244|PDB:2EPB}.
FT   STRAND      389    391       {ECO:0000244|PDB:2EPB}.
FT   STRAND      394    401       {ECO:0000244|PDB:2EPB}.
FT   HELIX       407    409       {ECO:0000244|PDB:2EPB}.
FT   STRAND      412    414       {ECO:0000244|PDB:2EPB}.
FT   TURN        415    417       {ECO:0000244|PDB:2EPB}.
FT   HELIX       420    429       {ECO:0000244|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
//
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