GenomeNet

Database: UniProt
Entry: B5DE69
LinkDB: B5DE69
Original site: B5DE69 
ID   CHD8_XENTR              Reviewed;        2184 AA.
AC   B5DE69;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   31-JUL-2019, entry version 62.
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};
GN   Name=chd8 {ECO:0000255|HAMAP-Rule:MF_03071};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA helicase that acts as a chromatin remodeling factor
CC       and 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
CC       histone H1 and preventing p53/tp53 transactivation activity. Acts
CC       as a negative regulator of Wnt signaling pathway by regulating
CC       beta-catenin (ctnnb1) activity. Negatively regulates ctnnb1-
CC       targeted gene expression by being recruited specifically to the
CC       promoter regions of several ctnnb1 responsive genes. May also act
CC       as a transcription activator by participating in efficient U6 RNA
CC       polymerase III transcription. {ECO:0000255|HAMAP-Rule:MF_03071}.
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: Component of some MLL1/MLL complex. {ECO:0000255|HAMAP-
CC       Rule:MF_03071}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03071}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. CHD8
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03071}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI68549.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; BC168549; AAI68549.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001131089.2; NM_001137617.2.
DR   SMR; B5DE69; -.
DR   STRING; 8364.ENSXETP00000037477; -.
DR   GeneID; 100192376; -.
DR   KEGG; xtr:100192376; -.
DR   CTD; 57680; -.
DR   Xenbase; XB-GENE-966847; chd8.
DR   InParanoid; B5DE69; -.
DR   KO; K04494; -.
DR   OrthoDB; 7181at2759; -.
DR   Reactome; R-XTR-3769402; Deactivation of the beta-catenin transactivating complex.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008013; F:beta-catenin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042393; F:histone binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0002039; F:p53 binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; IEA:UniProtKB-UniRule.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   Gene3D; 2.20.28.130; -; 1.
DR   Gene3D; 3.40.50.10810; -; 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_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; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   Activator; ATP-binding; Chromatin regulator; Complete proteome;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Wnt signaling pathway.
FT   CHAIN         1   2184       Chromodomain-helicase-DNA-binding protein
FT                                8.
FT                                /FTId=PRO_0000367313.
FT   DOMAIN      586    653       Chromo 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_03071}.
FT   DOMAIN      668    734       Chromo 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_03071}.
FT   DOMAIN      767    941       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03071}.
FT   DOMAIN     1081   1252       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_03071}.
FT   NP_BIND     780    787       ATP. {ECO:0000255|HAMAP-Rule:MF_03071}.
FT   MOTIF       892    895       DEAH box. {ECO:0000255|HAMAP-
FT                                Rule:MF_03071}.
FT   COMPBIAS    225    356       Gln-rich. {ECO:0000255|HAMAP-
FT                                Rule:MF_03071}.
FT   COMPBIAS   1901   1967       Ser-rich. {ECO:0000255|HAMAP-
FT                                Rule:MF_03071}.
SQ   SEQUENCE   2184 AA;  246687 MW;  08867A829AD6919D CRC64;
     MADPIMDLFD DPNLFGLDSL TGDSFGRDGP DTIDDALGLG NVLGPLEPIT DRVGLPGADV
     GNNEVKQQTE SQVLPDNPAL MSATEIMQPI QLPTNQETLN QGNPFMGASN AGAPKIMILK
     APAGMTVGAC PVTQIQTLTP HQAANGGKVA FAKVLTGTPL RPGVSIVSGN TVLAKMPSTG
     VAGQVGAVRP VRQLLLQPVR ASAAPGSSES NTGIKPAITL TSAPQQGDPK RITLVLQQPS
     QVGATAQQGQ RHVVLGGLPG KIVLQGNQLA ALTQAKTPQG QPAKVVTIQL QVQQQPGAAG
     QTPQKFQIVQ QAPGGVAIAP SGQHTHMLNQ QGVQRLSVPL KVVLQPQAGS SQGTAQGLSV
     VKVLNASEVA NLTASQTVVK TSTGGGESRK LDSQKKQEKA NRIVAEAIAR ARARGEQNIP
     RVLNEDELPS VNPEDDDGSR RKRKKKKGET SDRSKDEKPK KVKGSGSLRS RSKGKPSTIT
     PIVGKKRKRN PSSDNSDAEI MASQASPAED EDSVQKRRSN RQVKRKKYTE DLDIKITDDE
     DDEEVDVTGP VKTEPVLLPE PMPLPDSEAV PSMQFFVENP SEEDAAIVDK ILSMRLAKKE
     LPTGEYVEVE EYFVKYKNYS YLHCEWATIE QLERDKRIHQ KLKRFKTKMT QMQHFLQEDE
     ESFNPDYVEV DRILDESHST DKDNGEPVVY YLVKWCSLPY EDSTWELKED VDDGKIEEFK
     RIEARQPNLK RVARPAATSW KKLELSREYQ NGNQLREYQL EGVNWLLFNW YNRQNCILAD
     EMGLGKTIQS ITFLQEVYNV GIRGPFLVIA PLSTITNWER EFGSWTQMNT IVYHGSLASR
     QMIQQYEMYC KDSKGRLIPG AYKFDALITT FEMVLSDCPE LREIEWRCVI IDEAHRLKNR
     NCKLLDSLKH MDLEHKVLLT GTPLQNTVEE LFSLLHFLEP TQFSSEAEFL KDFGDLKTEE
     QVQKLQAILK PMMLRRLKED VEKNLAPKQE TIIEVELTNI QKKYYRAILE KNFSFLTKGA
     SQSNTPNLLN TMMELRKCCN HPYLITGAEE KIISEFREAT PVVPPDFHVQ AMVRSSGKLV
     LIDKLLPKLR AGGHKVLIFS QMVRCLDILE DYLIQRRYLY ERIDGRVRGN MRQAAIDRFS
     RPDSDRFVFL LCTRAGGLGI NLTAADTCII FDSDWNPQND LQAQARCHRI GQSKAVKIYR
     LITRNSYERE MFDKASLKLG LDKAVLQSMS GRDNHLSGPI QQFTKKEIED LLRKGAYAAI
     MDEDDEGSKF CEEDIDQILL RRTTTITIES EGKGSTFSKA SFVASENRTD ISLDDPNFWQ
     KWAKKADLDL DLLSSKNTLV IDTPRIRKQT RHFTNKDDDM VEFSDLESDD DDRPKARRQD
     RKHGYGRTDC FRVEKHLLVY GWGRWRDILT HGRFKRGMNE RDVEKICRAI LVYCLLHYRG
     DENIKSFIWD LITPAENGKT KQLQNHSGLS IPVPRGRKGK KVKSQSSFDI HKADWIHKYN
     PDTLFQDEGY KKHLKHQCNK VLLRVRMLYF LRQEVIGNQA MKVLSGVEAR QIDIWFPQVD
     QVEVPSRWWD READKSLLIG VFKHGYEKYN TMRADPALCF LEKVGGPDEQ AIAAEHHAQD
     FSELPDGGDF DRDIEDPEYK PLHAQKDPED EIDSLMMDEE ISVVDGEEAT AMPSGMLWPP
     GSALTARLRR LITAYQRSYK REQLKLEAEE RGDKRRKRCE AAFKLKEIAR REKQQRWTRR
     EACDFFRVLS SFGVEYDPDT QLYDWQRFRG LARLDKKTDE SLLKYFHGFV AMCRQVCRLP
     PAAGDEPPDP SLFIEPISEE RASRALFRLD LLRRVREQVL CHPLLIPRLS LCRPDPELPE
     WWESGRHDNE LLQGAARYGL SRTDLTILQD HAFSFLRCQI SYFQSRGISG HSRPSTPTTA
     PSVPTERQPS HLASLSSSVS CSPAPRRSSS CSSSSHSSNS EDSSDESNGV KVKPNAGLSH
     ARLYDEESRL SLTASPADLT TEDSIQTALE TPHSTDWPKD RVLICRIEQV CSAVLTGKWS
     SPRRLSDPPS DSPDSLPPTP EQQSPAHFTQ IRPAPDPKEF TIQIKSEEGL KIKFQKHKFM
     GNGALDSAPH TQKKKSKKKM DLDMDTRIPV VNQKDGTLLL GEEAPLRCQL PEWLHRNPDF
     MVDPRFIAVS GYWIPYINRG KHFL
//
DBGET integrated database retrieval system