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CHD8_MOUSE
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   03-AUG-2022, entry version 137.
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).
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. {ECO:0000255|HAMAP-Rule:MF_03071,
CC       ECO:0000269|PubMed:16949368, ECO:0000269|PubMed:19151705}.
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       {ECO:0000255|HAMAP-Rule:MF_03071, ECO:0000269|PubMed:16949368,
CC       ECO:0000269|PubMed:19151705}.
CC   -!- INTERACTION:
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}. Note=Localizes to the promoter regions of
CC       several CTNNB1-responsive genes. Also present at known CTCF target
CC       sites. {ECO:0000255|HAMAP-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; 4.
DR   MINT; Q09XV5; -.
DR   STRING; 10090.ENSMUSP00000087184; -.
DR   iPTMnet; Q09XV5; -.
DR   PhosphoSitePlus; Q09XV5; -.
DR   EPD; Q09XV5; -.
DR   jPOST; Q09XV5; -.
DR   MaxQB; Q09XV5; -.
DR   PaxDb; Q09XV5; -.
DR   PeptideAtlas; Q09XV5; -.
DR   PRIDE; Q09XV5; -.
DR   ProteomicsDB; 281607; -. [Q09XV5-1]
DR   ProteomicsDB; 281608; -. [Q09XV5-2]
DR   Antibodypedia; 73; 131 antibodies from 21 providers.
DR   Ensembl; ENSMUST00000089752; ENSMUSP00000087184; ENSMUSG00000053754. [Q09XV5-1]
DR   Ensembl; ENSMUST00000200169; ENSMUSP00000142890; ENSMUSG00000053754. [Q09XV5-1]
DR   GeneID; 67772; -.
DR   KEGG; mmu:67772; -.
DR   UCSC; uc007tot.1; mouse. [Q09XV5-1]
DR   UCSC; uc007tov.1; mouse. [Q09XV5-2]
DR   CTD; 57680; -.
DR   MGI; MGI:1915022; Chd8.
DR   VEuPathDB; HostDB:ENSMUSG00000053754; -.
DR   eggNOG; KOG0384; Eukaryota.
DR   GeneTree; ENSGT00940000153649; -.
DR   InParanoid; Q09XV5; -.
DR   OMA; IFSDPQF; -.
DR   OrthoDB; 7181at2759; -.
DR   PhylomeDB; Q09XV5; -.
DR   TreeFam; TF313572; -.
DR   Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR   BioGRID-ORCS; 67772; 18 hits in 79 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 277 other 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: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: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:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; 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:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
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   Gene3D; 3.40.5.120; -; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; IPR000330; SNF2_N.
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; SSF160481; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54160; SSF54160; 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
 
 
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