ID CHD8_MOUSE Reviewed; 2582 AA.
AC Q09XV5; Q3TV89; Q5I1Z2; Q6ZPM8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 146.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 8 {ECO:0000255|HAMAP-Rule:MF_03071};
DE Short=CHD-8 {ECO:0000255|HAMAP-Rule:MF_03071};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_03071};
DE AltName: Full=ATP-dependent helicase CHD8 {ECO:0000255|HAMAP-Rule:MF_03071};
DE AltName: Full=Axis duplication inhibitor;
DE Short=Duplin;
GN Name=Chd8 {ECO:0000255|HAMAP-Rule:MF_03071}; Synonyms=Kiaa1564;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CTCF,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo;
RX PubMed=16949368; DOI=10.1016/j.molcel.2006.08.008;
RA Ishihara K., Oshimura M., Nakao M.;
RT "CTCF-dependent chromatin insulator is linked to epigenetic remodeling.";
RL Mol. Cell 23:733-742(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DISRUPTION PHENOTYPE, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=15367660; DOI=10.1128/mcb.24.19.8386-8394.2004;
RA Nishiyama M., Nakayama K., Tsunematsu R., Tsukiyama T., Kikuchi A.,
RA Nakayama K.I.;
RT "Early embryonic death in mice lacking the beta-catenin-binding protein
RT Duplin.";
RL Mol. Cell. Biol. 24:8386-8394(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1730-2582.
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2020-2582.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH TP53 AND HISTONE H1.
RX PubMed=19151705; DOI=10.1038/ncb1831;
RA Nishiyama M., Oshikawa K., Tsukada Y.I., Nakagawa T., Iemura S.,
RA Natsume T., Fan Y., Kikuchi A., Skoultchi A.I., Nakayama K.I.;
RT "CHD8 suppresses p53-mediated apoptosis through histone H1 recruitment
RT during early embryogenesis.";
RL Nat. Cell Biol. 11:172-182(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555; SER-1422; SER-1426;
RP SER-1999; SER-2202; SER-2204; THR-2206; SER-2213 AND THR-2217, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HNRNPL.
RX PubMed=36537238; DOI=10.1093/nar/gkac1134;
RA Kerschbamer E., Arnoldi M., Tripathi T., Pellegrini M., Maturi S.,
RA Erdin S., Salviato E., Di Leva F., Sebestyen E., Dassi E., Zarantonello G.,
RA Benelli M., Campos E., Basson M.A., Gusella J.F., Gustincich S., Piazza S.,
RA Demichelis F., Talkowski M.E., Ferrari F., Biagioli M.;
RT "CHD8 suppression impacts on histone H3 lysine 36 trimethylation and alters
RT RNA alternative splicing.";
RL Nucleic Acids Res. 50:12809-12828(2022).
CC -!- FUNCTION: DNA helicase that acts as a chromatin remodeling factor and
CC regulates transcription. Acts as a transcription repressor by
CC remodeling chromatin structure and recruiting histone H1 to target
CC genes. Suppresses p53/TP53-mediated apoptosis by recruiting histone H1
CC and preventing p53/TP53 transactivation activity. Acts as a negative
CC regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1)
CC activity. Negatively regulates CTNNB1-targeted gene expression by being
CC recruited specifically to the promoter regions of several CTNNB1
CC responsive genes. Involved in both enhancer blocking and epigenetic
CC remodeling at chromatin boundary via its interaction with CTCF. Acts as
CC a suppressor of STAT3 activity by suppressing the LIF-induced STAT3
CC transcriptional activity. Also acts as a transcription activator via
CC its interaction with ZNF143 by participating in efficient U6 RNA
CC polymerase III transcription. Regulates alternative splicing of a core
CC group of genes involved in neuronal differentiation, cell cycle and DNA
CC repair. Enables H3K36me3-coupled transcription elongation and co-
CC transcriptional RNA processing likely via interaction with HNRNPL.
CC {ECO:0000255|HAMAP-Rule:MF_03071, ECO:0000269|PubMed:16949368,
CC ECO:0000269|PubMed:19151705, ECO:0000269|PubMed:36537238}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03071};
CC -!- SUBUNIT: Interacts with CTNNB1 and PIAS3. Component of some MLL1/MLL
CC complex, at least composed of the core components KMT2A/MLL1, ASH2L,
CC HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components
CC BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA,
CC KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with CHD7.
CC Interacts with FAM124B (By similarity). Interacts with p53/TP53 and
CC histone H1 (PubMed:19151705). Interacts with CTCF (PubMed:16949368).
CC Interacts with TLK2 (By similarity). Interacts with HNRNPL in an RNA-
CC dependent manner. {ECO:0000250|UniProtKB:Q9HCK8, ECO:0000255|HAMAP-
CC Rule:MF_03071, ECO:0000269|PubMed:16949368,
CC ECO:0000269|PubMed:19151705, ECO:0000269|PubMed:36537238}.
CC -!- INTERACTION:
CC Q09XV5; P28033: Cebpb; NbExp=2; IntAct=EBI-1169080, EBI-1029979;
CC Q09XV5; Q61164: Ctcf; NbExp=3; IntAct=EBI-1169080, EBI-932785;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03071,
CC ECO:0000269|PubMed:16949368, ECO:0000269|PubMed:36537238}.
CC Note=Localizes to the promoter regions of several CTNNB1-responsive
CC genes. Also present at known CTCF target sites. {ECO:0000255|HAMAP-
CC Rule:MF_03071}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q09XV5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q09XV5-2; Sequence=VSP_036676, VSP_036677;
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly from early- to mid-stage
CC mouse embryogenesis. Detected throughout embryos from 7.5 to 9.5 dpc
CC but localizes predominantly in the brain, faces, branchial arches, limb
CC buds, and tail buds of embryos at 10.5 dpc.
CC {ECO:0000269|PubMed:15367660}.
CC -!- PTM: Sumoylated. {ECO:0000255|HAMAP-Rule:MF_03071}.
CC -!- DISRUPTION PHENOTYPE: Death during early embryogenesis due to
CC widespread apoptosis. Embryos manifest growth retardation from 5.5 dpc
CC and developmental arrest accompanied by massive apoptosis at 7.5 dpc.
CC They develop into an egg cylinder but do not form a primitive streak or
CC mesoderm. Mice lacking both Tp53 and Chd8 ameliorate this developmental
CC arrest. {ECO:0000269|PubMed:15367660, ECO:0000269|PubMed:19151705}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. CHD8 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03071}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98203.2; Type=Miscellaneous discrepancy; Note=Partially unspliced pre-RNA.; Evidence={ECO:0000305};
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DR EMBL; DQ190419; ABB02259.1; -; mRNA.
DR EMBL; AY863219; AAW56421.1; -; mRNA.
DR EMBL; AK129393; BAC98203.2; ALT_SEQ; Transcribed_RNA.
DR EMBL; AK160299; BAE35730.1; -; mRNA.
DR CCDS; CCDS36919.1; -. [Q09XV5-1]
DR RefSeq; NP_963999.2; NM_201637.2. [Q09XV5-1]
DR RefSeq; XP_006519539.1; XM_006519476.3.
DR AlphaFoldDB; Q09XV5; -.
DR SMR; Q09XV5; -.
DR BioGRID; 212432; 20.
DR IntAct; Q09XV5; 6.
DR MINT; Q09XV5; -.
DR STRING; 10090.ENSMUSP00000142890; -.
DR GlyGen; Q09XV5; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; Q09XV5; -.
DR PhosphoSitePlus; Q09XV5; -.
DR EPD; Q09XV5; -.
DR jPOST; Q09XV5; -.
DR MaxQB; Q09XV5; -.
DR PaxDb; 10090-ENSMUSP00000087184; -.
DR PeptideAtlas; Q09XV5; -.
DR ProteomicsDB; 281607; -. [Q09XV5-1]
DR ProteomicsDB; 281608; -. [Q09XV5-2]
DR Pumba; Q09XV5; -.
DR Antibodypedia; 73; 151 antibodies from 21 providers.
DR Ensembl; ENSMUST00000089752.11; ENSMUSP00000087184.5; ENSMUSG00000053754.15. [Q09XV5-1]
DR Ensembl; ENSMUST00000200169.6; ENSMUSP00000142890.2; ENSMUSG00000053754.15. [Q09XV5-1]
DR GeneID; 67772; -.
DR KEGG; mmu:67772; -.
DR UCSC; uc007tot.1; mouse. [Q09XV5-1]
DR UCSC; uc007tov.1; mouse. [Q09XV5-2]
DR AGR; MGI:1915022; -.
DR CTD; 57680; -.
DR MGI; MGI:1915022; Chd8.
DR VEuPathDB; HostDB:ENSMUSG00000053754; -.
DR eggNOG; KOG0384; Eukaryota.
DR GeneTree; ENSGT00940000153649; -.
DR InParanoid; Q09XV5; -.
DR OMA; AYMEDHR; -.
DR OrthoDB; 22878at2759; -.
DR PhylomeDB; Q09XV5; -.
DR TreeFam; TF313572; -.
DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR BioGRID-ORCS; 67772; 20 hits in 85 CRISPR screens.
DR ChiTaRS; Chd8; mouse.
DR PRO; PR:Q09XV5; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q09XV5; Protein.
DR Bgee; ENSMUSG00000053754; Expressed in embryonic post-anal tail and 281 other cell types or tissues.
DR ExpressionAtlas; Q09XV5; baseline and differential.
DR Genevisible; Q09XV5; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0070016; F:armadillo repeat domain binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0048565; P:digestive tract development; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0006397; P:mRNA processing; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
DR GO; GO:0035176; P:social behavior; IMP:MGI.
DR GO; GO:0001964; P:startle response; IMP:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd18668; CD1_tandem_CHD5-9_like; 1.
DR CDD; cd18663; CD2_tandem_CHD5-9_like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR HAMAP; MF_03071; CHD8; 1.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR034724; CHD8.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR46850; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR PANTHER; PTHR46850:SF3; DNA HELICASE; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00592; BRK; 2.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF160481; BRK domain-like; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ATP-binding; Chromatin regulator;
KW DNA-binding; Helicase; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation;
KW Wnt signaling pathway.
FT CHAIN 1..2582
FT /note="Chromodomain-helicase-DNA-binding protein 8"
FT /id="PRO_0000367310"
FT DOMAIN 644..711
FT /note="Chromo 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT DOMAIN 726..792
FT /note="Chromo 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT DOMAIN 825..999
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT DOMAIN 1139..1290
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT REGION 22..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1694..1715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1791..2304
FT /note="Interaction with FAM124B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT REGION 1990..2019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2045..2120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2187..2233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2486..2582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 950..953
FT /note="DEAH box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT COMPBIAS 43..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..373
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2076..2095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2096..2118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2492..2512
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2516..2532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2537..2554
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 838..845
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCK8"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCK8"
FT MOD_RES 1422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCK8"
FT MOD_RES 1980
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCK8"
FT MOD_RES 1995
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCK8"
FT MOD_RES 1997
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIX5"
FT MOD_RES 1999
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2010
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCK8"
FT MOD_RES 2040
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 2070
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCK8"
FT MOD_RES 2072
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCK8"
FT MOD_RES 2184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCK8"
FT MOD_RES 2202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2206
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2217
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIX5"
FT MOD_RES 2520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HCK8"
FT CROSSLNK 611
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03071"
FT CROSSLNK 2027
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HCK8"
FT CROSSLNK 2258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HCK8"
FT VAR_SEQ 745..751
FT /note="PVIYYLV -> VSWARRT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15367660"
FT /id="VSP_036676"
FT VAR_SEQ 752..2582
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15367660"
FT /id="VSP_036677"
FT CONFLICT 21
FT /note="T -> A (in Ref. 2; AAW56421)"
FT /evidence="ECO:0000305"
FT CONFLICT 2020
FT /note="N -> S (in Ref. 3; BAC98203)"
FT /evidence="ECO:0000305"
FT CONFLICT 2298
FT /note="L -> V (in Ref. 3; BAC98203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2582 AA; 290847 MW; D9432500F6A8C329 CRC64;
MADPIMDLFD DPNLFGLDSL TDDSFNQVTQ DPIEEALGLP SSLDSLDQMN QDGGGGDVGN
SSASDLVPPP EETASTELPK ESTAPAPESL TLHDYTTQPT SQEQPAQPVL QTSTPTAGLL
QVSKSQEILS QGNPFMGVSA TGVSPSNTGG QPSQSAPKIV ILKAPPNSSV TGTHVAQIQA
QGITSTAQPL VAGTANGGKV TFTKVLTGTP LRPGVSIVSG NTVLATKVPG NQAAVQRIVQ
PSRPVKQLVL QPVKGSAPAG NPGAAGPPLK PAVTLTSTPT QGESKRITLV LQQPQSGGPQ
GHRHVVLGSL PGKIVLQGNQ LAALTQAKNA QGQPAKVVTI QLQVQQPQQK IQIVPQPPSS
QPQPQPQPPP SAQPLTLSSV QQAQIMGPGQ NPGQRLSVPL KMVLQPQAGS SQGASSGLSV
VKVLSASEVA ALSSPASCAP HTAGKTGMEE NRRLEHQKKQ EKANRIVAEA IARARARGEQ
NIPRVLNEDE LPSVRPEEEG EKKRRKKSSG ERLKEEKPKK SKTAAASKTK GKSKLNTITP
VVGKKRKRNT SSDNSDVEVM PAQSPREDEE SSIQKRRSNR QVKRKKYTED LDIKITDDEE
EEEVDVTGPI KPEPILPEPV QEPDGETLPS MQFFVENPSE EDAAIVDKVL SMRVVKKELP
SGQYTEAEEF FVKYKNYSYL HCEWATISQL EKDKRIHQKL KRFKTKMAQM RHFFHEDEEP
FNPDYVEVDR ILDESHSVDK DNGEPVIYYL VKWCSLPYED STWELKEDVD EGKIREFKRI
QSRHPELRRV NRPQANAWKK LELSHEYKNR NQLREYQLEG VNWLLFNWYN RQNCILADEM
GLGKTIQSIA FLQEVYNVGI HGPFLVIAPL STITNWEREF NTWTEMNTIV YHGSLASRQM
IQQYEMYCKD SRGRLIPGAY KFDALITTFE MILSDCPELR EIEWRCVIID EAHRLKNRNC
KLLDSLKHMD LEHKVLLTGT PLQNTVEELF SLLHFLEPSQ FPSESEFLKD FGDLKTEEQV
QKLQAILKPM MLRRLKEDVE KNLAPKQETI IEVELTNIQK KYYRAILEKN FSFLSKGAGH
TNMPNLLNTM MELRKCCNHP YLINGAEEKI LMEFREACHI IPQDFHLQAM VRSAGKLVLI
DKLLPKLKAG GHKVLIFSQM VRCLDILEDY LIQRRYLYER IDGRVRGNLR QAAIDRFSKP
DSDRFVFLLC TRAGGLGINL TAADTCIIFD SDWNPQNDLQ AQARCHRIGQ SKAVKVYRLI
TRNSYEREMF DKASLKLGLD KAVLQSMSGR DGNITGIQQF SKKEIEDLLR KGAYAAIMEE
DDEGSKFCEE DIDQILLRRT TTITIESEGK GSTFAKASFV ASENRTDISL DDPNFWQKWA
KKADLDMDLL NSKNNLVIDT PRVRKQTRHF STLKDDDLVE FSDLESEDDE RPRSRRHDRH
HTYGRTDCFR VEKHLLVYGW GRWRDILSHG RFKRRMTERD VETICRAILV YCLLHYRGDE
NIKSFIWDLI SPAENGKTKE LQNHSGLSIP VPRGRKGKKV KSQSTFDIHK ADWIRKYNPD
TLFQDESYKK HLKHQCNKVL LRVRMLYYLR QEVIGDQAEK VLGGAIASEI DIWFPVVDQL
EVPTTWWDSE ADKSLLIGVF KHGYEKYNTM RADPALCFLE KAGRPDDKAI AAEHRVLDNF
SDLVEGIDFD KDCEDPEYKP LQGPPKDPDD EGDPLMMMDE EISVIDGEEA QVTQQPGHLF
WPPGSALTAR LRRLVTAYQR SYKREQMKME AAERGDRRRR RCEAAFKLKE IARREKQQRW
TRREQTDFYR VVSTFGVEYD PDNMQFHWDR FRTFARLDKK TDESLTKYFH GFVAMCRQVC
RLPPAAGDEP PDPNLFIEPI TEERASRTLY RIELLRRLRE QVLCHPLLED RLALCQPPGL
ELPKWWEPVR HDGELLRGAA RHGVSQTDCN IMQDPDFSFL AARMNYMQNH QAGASAASLS
RCSTPLLHQQ CTSRTASPSP LRPDAPVEKS PEESTVQVPN LESLTLKLED EVVARSRLTS
QDYEVRVGSS DTAPLSRSVP PVKLEDEDDS DSELDLSKLS PSSSSSSSSS SSSSSTDESE
DEKEEKLTAD RSRPKLYDEE SLLSLTMSQD GFPNEDGEQM TPELLLLQER QRASEWPKDR
VLINRIDLVC QAVLSGKWPS NRRSQEVTAG GILGPGNHLL DSPSLTPGED GDSPVPTPRS
GSAASMAEEE ASAVTTAAAQ FTKLRRGMDE KEFTVQIKDE EGLKLTFQKH RLMANGVMGD
GHPLFHKKKG NRKKLVELEV ECMEEPNHLD LDLETRIPVI NKVDGTLLVG DEAPRRAELE
MWLQGHPEFA VDPRFLAYME ERRKQKWQRC KKNNKAELNC LGMEPVQPAN SRNGKKGHYA
ETAFNRVLPG PVAPENSKKR VRRTRPDLSK MMALMQGGST GSLSLHNTFQ HSSSNLQSVS
SLGHSSTTSA SLPFMPFVMG AAAPPHVDSS TMLHHHHHHP HPHHHHHHHP GLRTTGYPSS
PATTTSGTAL RLPTLQPEDD DEEEDEEDDD LSQGYDSSER DFSLIDDPMM PANSDSSEDA
DD
//
