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Chromodomain-helicase-DNA-binding protein 6 (CHD-6) (EC 3.6.4.12) (ATP-dependent helicase CHD6) (Radiation-induced gene B protein)

 CHD6_HUMAN              Reviewed;        2715 AA.
Q8TD26; Q5JYQ0; Q5TGZ9; Q5TH00; Q5TH01; Q8IZR2; Q8WTY0; Q9H4H6;
Q9H6D4; Q9NTT7; Q9P2L1;
19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 4.
20-JUN-2018, entry version 165.
RecName: Full=Chromodomain-helicase-DNA-binding protein 6;
Short=CHD-6;
EC=3.6.4.12;
AltName: Full=ATP-dependent helicase CHD6;
AltName: Full=Radiation-induced gene B protein;
Name=CHD6; Synonyms=CHD5, KIAA1335, RIGB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11889561; DOI=10.1007/s00335-001-3042-6;
Schuster E.F., Stoeger R.J.;
"CHD5 defines a new subfamily of chromodomain-SWI2/SNF2-like
helicases.";
Mamm. Genome 13:117-119(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 2442-2715 (ISOFORM 1).
TISSUE=Hippocampus, Lymph, and Retinoblastoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 299-2715 (ISOFORM 3).
Zhou P.-K., Sui J.-L.;
"cDNA cloning and transcriptional controlling of a novel radiation-
induced gene and its function analysis.";
Zhonghua Fang She Yi Xue Yu Fang Hu Za Zhi 22:73-77(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 675-2715 (ISOFORM 1).
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 7:65-73(2000).
[6]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 759-1527 (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
FUNCTION IN TRANSCRIPTION, AND INTERACTION WITH NFE2L2.
PubMed=16314513; DOI=10.1128/MCB.25.24.10895-10906.2005;
Nioi P., Nguyen T., Sherratt P.J., Pickett C.B.;
"The carboxy-terminal Neh3 domain of Nrf2 is required for
transcriptional activation.";
Mol. Cell. Biol. 25:10895-10906(2005).
[9]
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND REGION.
PubMed=17027977; DOI=10.1016/j.febslet.2006.09.049;
Lutz T., Stoger R., Nieto A.;
"CHD6 is a DNA-dependent ATPase and localizes at nuclear sites of mRNA
synthesis.";
FEBS Lett. 580:5851-5857(2006).
[10]
DISEASE.
PubMed=18627065; DOI=10.1002/ajmg.a.32419;
Kalscheuer V.M., Feenstra I., Van Ravenswaaij-Arts C.M., Smeets D.F.,
Menzel C., Ullmann R., Musante L., Ropers H.H.;
"Disruption of the TCF4 gene in a girl with mental retardation but
without the classical Pitt-Hopkins syndrome.";
Am. J. Med. Genet. A 146A:2053-2059(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HUMAN
PAPILLOMAVIRUS PROTEIN E8^E2C.
PubMed=20631145; DOI=10.1128/JVI.00678-10;
Fertey J., Ammermann I., Winkler M., Stoeger R., Iftner T.,
Stubenrauch F.;
"Interaction of the papillomavirus E8--E2C protein with the cellular
CHD6 protein contributes to transcriptional repression.";
J. Virol. 84:9505-9515(2010).
[13]
SUBCELLULAR LOCATION, INTERACTION WITH INFLUENZA A POLYMERASE COMPLEX,
AND FUNCTION (MICROBIAL INFECTION).
PubMed=21899694; DOI=10.1111/j.1462-5822.2011.01679.x;
Alfonso R., Lutz T., Rodriguez A., Chavez J.P., Rodriguez P.,
Gutierrez S., Nieto A.;
"CHD6 chromatin remodeler is a negative modulator of influenza virus
replication that relocates to inactive chromatin upon infection.";
Cell. Microbiol. 13:1894-1906(2011).
[14]
FUNCTION (MICROBIAL INFECTION).
PubMed=23408615; DOI=10.1128/JVI.00554-12;
Alfonso R., Rodriguez A., Rodriguez P., Lutz T., Nieto A.;
"CHD6, a cellular repressor of influenza virus replication, is
degraded in human alveolar epithelial cells and mice lungs during
infection.";
J. Virol. 87:4534-4544(2013).
[15]
FUNCTION.
PubMed=28533432; DOI=10.1074/jbc.M117.779470;
Manning B.J., Yusufzai T.;
"The ATP-dependent Chromatin Remodeling Enzymes CHD6, CHD7, and CHD8
Exhibit Distinct Nucleosome Binding and Remodeling Activities.";
J. Biol. Chem. 292:11927-11936(2017).
[16]
STRUCTURE BY NMR OF 371-431.
RIKEN structural genomics initiative (RSGI);
"Solution structure of chromo domain 2 in chromodomain-helicase-DNA-
binding protein 6.";
Submitted (OCT-2007) to the PDB data bank.
-!- FUNCTION: DNA-dependent ATPase that plays a role in chromatin
remodeling. Regulates transcription by disrupting nucleosomes in a
largely non-sliding manner which strongly increases the
accessibility of chromatin (PubMed:28533432). Activates
transcription of specific genes in response to oxidative stress
through interaction with NFE2L2. {ECO:0000269|PubMed:16314513,
ECO:0000269|PubMed:28533432}.
-!- FUNCTION: (Microbial infection) Acts as a transcriptional
repressor of different viruses including influenza virus or
papillomavirus. During influenza virus infection, the viral
polymerase complex localizes CHD6 to inactive chromatin where it
gets degraded in a proteasome independent-manner.
{ECO:0000269|PubMed:20631145, ECO:0000269|PubMed:21899694,
ECO:0000269|PubMed:23408615}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:17027977}.
-!- SUBUNIT: Interacts with NFE2L2; involved in activation of the
transcription. {ECO:0000269|PubMed:16314513}.
-!- SUBUNIT: (Microbial infection) Interacts with the influenza A
polymerase complex composed fo PB1, PB2 and PA (PubMed:21899694).
Interacts (via N-terminus) with human papillomavirus protein
E8^E2C (via C-terminus); this interaction induces transcriptional
repression of the viral genome (PubMed:20631145).
{ECO:0000269|PubMed:20631145, ECO:0000269|PubMed:21899694}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:17027977, ECO:0000269|PubMed:21899694}.
Note=Enriched at sites of mRNA synthesis (PubMed:17027977). During
influenza A virus infection, localizes to inactive chromatin.
{ECO:0000269|PubMed:17027977, ECO:0000269|PubMed:21899694}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8TD26-1; Sequence=Displayed;
Name=2;
IsoId=Q8TD26-2; Sequence=VSP_015296, VSP_015297, VSP_015298;
Note=Gene prediction based on EST data.;
Name=3;
IsoId=Q8TD26-3; Sequence=VSP_015299, VSP_015300, VSP_015301;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
-!- DISEASE: Note=A chromosomal aberration disrupting CHD6 has been
found in a patient with mild to moderate mental retardation and
minor facial anomalies. Translocation t(18;20)(q21.1;q11.2) with
TCF4 producing a CHD6-TCF4 fusion transcript (PubMed:18627065).
{ECO:0000269|PubMed:18627065}.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK56405.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAN59903.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB15325.1; Type=Miscellaneous discrepancy; Note=The sequence differs from position 1528 onward for unknown reasons.; Evidence={ECO:0000305};
Sequence=CAI21743.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAI22254.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AY034072; AAK56405.1; ALT_INIT; mRNA.
EMBL; AL121674; CAI21743.1; ALT_SEQ; Genomic_DNA.
EMBL; AL031669; CAI21743.1; JOINED; Genomic_DNA.
EMBL; AL121674; CAI21744.1; -; Genomic_DNA.
EMBL; AL031667; CAI21744.1; JOINED; Genomic_DNA.
EMBL; AL031669; CAI21744.1; JOINED; Genomic_DNA.
EMBL; AL121674; CAI21745.1; -; Genomic_DNA.
EMBL; AL031667; CAI21745.1; JOINED; Genomic_DNA.
EMBL; AL031669; CAI21745.1; JOINED; Genomic_DNA.
EMBL; AL031669; CAI22254.1; ALT_SEQ; Genomic_DNA.
EMBL; AL121674; CAI22254.1; JOINED; Genomic_DNA.
EMBL; AL031669; CAI22255.1; -; Genomic_DNA.
EMBL; AL031667; CAI22255.1; JOINED; Genomic_DNA.
EMBL; AL121674; CAI22255.1; JOINED; Genomic_DNA.
EMBL; AL031669; CAI22256.1; -; Genomic_DNA.
EMBL; AL031667; CAI22256.1; JOINED; Genomic_DNA.
EMBL; AL121674; CAI22256.1; JOINED; Genomic_DNA.
EMBL; AL031667; CAI42977.1; -; Genomic_DNA.
EMBL; AL031669; CAI42977.1; JOINED; Genomic_DNA.
EMBL; AL121674; CAI42977.1; JOINED; Genomic_DNA.
EMBL; AL031667; CAI42981.1; -; Genomic_DNA.
EMBL; AL031669; CAI42981.1; JOINED; Genomic_DNA.
EMBL; AL121674; CAI42981.1; JOINED; Genomic_DNA.
EMBL; AL031667; CAI42983.1; -; Genomic_DNA.
EMBL; BC021907; AAH21907.1; -; mRNA.
EMBL; BC039860; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC040016; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AF525085; AAN59903.1; ALT_INIT; mRNA.
EMBL; AB037756; BAA92573.2; -; mRNA.
EMBL; AK026022; BAB15325.1; ALT_SEQ; mRNA.
CCDS; CCDS13317.1; -. [Q8TD26-1]
RefSeq; NP_115597.3; NM_032221.4. [Q8TD26-1]
UniGene; Hs.740645; -.
PDB; 2EPB; NMR; -; A=371-431.
PDBsum; 2EPB; -.
ProteinModelPortal; Q8TD26; -.
SMR; Q8TD26; -.
BioGrid; 123931; 15.
IntAct; Q8TD26; 13.
MINT; Q8TD26; -.
STRING; 9606.ENSP00000362330; -.
CarbonylDB; Q8TD26; -.
iPTMnet; Q8TD26; -.
PhosphoSitePlus; Q8TD26; -.
BioMuta; CHD6; -.
DMDM; 296439466; -.
EPD; Q8TD26; -.
MaxQB; Q8TD26; -.
PaxDb; Q8TD26; -.
PeptideAtlas; Q8TD26; -.
PRIDE; Q8TD26; -.
ProteomicsDB; 74223; -.
ProteomicsDB; 74224; -. [Q8TD26-2]
ProteomicsDB; 74225; -. [Q8TD26-3]
Ensembl; ENST00000373222; ENSP00000362319; ENSG00000124177. [Q8TD26-2]
Ensembl; ENST00000373233; ENSP00000362330; ENSG00000124177. [Q8TD26-1]
GeneID; 84181; -.
KEGG; hsa:84181; -.
UCSC; uc002xka.3; human. [Q8TD26-1]
CTD; 84181; -.
DisGeNET; 84181; -.
EuPathDB; HostDB:ENSG00000124177.14; -.
GeneCards; CHD6; -.
H-InvDB; HIX0015824; -.
H-InvDB; HIX0027712; -.
HGNC; HGNC:19057; CHD6.
HPA; HPA015543; -.
MIM; 616114; gene.
neXtProt; NX_Q8TD26; -.
OpenTargets; ENSG00000124177; -.
PharmGKB; PA134974700; -.
eggNOG; KOG0383; Eukaryota.
eggNOG; COG0553; LUCA.
GeneTree; ENSGT00760000119067; -.
HOVERGEN; HBG081150; -.
InParanoid; Q8TD26; -.
KO; K14436; -.
OMA; THGRFKW; -.
OrthoDB; EOG091G0022; -.
PhylomeDB; Q8TD26; -.
TreeFam; TF313572; -.
ChiTaRS; CHD6; human.
EvolutionaryTrace; Q8TD26; -.
GenomeRNAi; 84181; -.
PRO; PR:Q8TD26; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000124177; -.
CleanEx; HS_CHD5; -.
CleanEx; HS_CHD6; -.
ExpressionAtlas; Q8TD26; baseline and differential.
Genevisible; Q8TD26; HS.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:UniProtKB.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0001221; F:transcription cofactor binding; IPI:UniProtKB.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0036091; P:positive regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00024; CHROMO; 2.
CDD; cd00079; HELICc; 1.
Gene3D; 3.40.50.10810; -; 1.
InterPro; IPR006576; BRK_domain.
InterPro; IPR037259; BRK_sf.
InterPro; IPR016197; Chromo-like_dom_sf.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR023780; Chromo_domain.
InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR038718; SNF2-like_sf.
InterPro; IPR000330; SNF2_N.
Pfam; PF00385; Chromo; 2.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF00176; SNF2_N; 1.
SMART; SM00592; BRK; 1.
SMART; SM00298; CHROMO; 2.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF160481; SSF160481; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF54160; SSF54160; 2.
PROSITE; PS50013; CHROMO_2; 1.
PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Chromatin regulator;
Complete proteome; DNA-binding; Helicase; Host-virus interaction;
Hydrolase; Nucleotide-binding; Nucleus; Polymorphism;
Reference proteome; Repeat; Transcription; Transcription regulation.
CHAIN 1 2715 Chromodomain-helicase-DNA-binding protein
6.
/FTId=PRO_0000080231.
DOMAIN 292 343 Chromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
DOMAIN 375 439 Chromo 2. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
DOMAIN 473 647 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 787 956 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 1449 1503 Myb-like.
NP_BIND 486 493 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 1 747 Required for DNA-dependent ATPase
activity.
MOTIF 598 601 DEAH box.
COMPBIAS 93 202 Lys-rich.
VAR_SEQ 1 10 MKMKIQKKEK -> MCQSHMIGFCTSSVNEETETQGDQISC
PNPTTLVFRTQISSLPSL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015296.
VAR_SEQ 325 338 FSYLHCKWATMEEL -> LYVYLKYSLYLGFI (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015297.
VAR_SEQ 339 2715 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015298.
VAR_SEQ 592 1108 Missing (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_015299.
VAR_SEQ 1337 1339 GNT -> QHR (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_015300.
VAR_SEQ 1340 2715 Missing (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_015301.
VARIANT 780 780 Q -> H (in dbSNP:rs4474937).
/FTId=VAR_059213.
VARIANT 2161 2161 H -> Q (in dbSNP:rs3817893).
/FTId=VAR_023363.
CONFLICT 134 134 K -> E (in Ref. 1; AAK56405).
{ECO:0000305}.
CONFLICT 575 575 T -> A (in Ref. 4; AAN59903).
{ECO:0000305}.
CONFLICT 1031 1031 E -> K (in Ref. 1; AAK56405).
{ECO:0000305}.
CONFLICT 2442 2447 RGRRPR -> EIVGLE (in Ref. 3; AAH21907).
{ECO:0000305}.
CONFLICT 2663 2663 D -> G (in Ref. 1; AAK56405).
{ECO:0000305}.
STRAND 379 387 {ECO:0000244|PDB:2EPB}.
STRAND 389 391 {ECO:0000244|PDB:2EPB}.
STRAND 394 401 {ECO:0000244|PDB:2EPB}.
HELIX 407 409 {ECO:0000244|PDB:2EPB}.
STRAND 412 414 {ECO:0000244|PDB:2EPB}.
TURN 415 417 {ECO:0000244|PDB:2EPB}.
HELIX 420 429 {ECO:0000244|PDB:2EPB}.
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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