ID H3CR68_TETNG Unreviewed; 2320 AA.
AC H3CR68;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 8 {ECO:0000256|HAMAP-Rule:MF_03071};
DE Short=CHD-8 {ECO:0000256|HAMAP-Rule:MF_03071};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_03071};
DE AltName: Full=ATP-dependent helicase CHD8 {ECO:0000256|HAMAP-Rule:MF_03071};
GN Name=CHD8 {ECO:0000256|HAMAP-Rule:MF_03071};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000010752.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000010752.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. May also act as a transcription activator by
CC participating in efficient U6 RNA polymerase III transcription.
CC {ECO:0000256|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:0000256|ARBA:ARBA00001665, ECO:0000256|HAMAP-
CC Rule:MF_03071};
CC -!- SUBUNIT: Component of some MLL1/MLL complex. {ECO:0000256|HAMAP-
CC Rule:MF_03071}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03071}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. CHD8 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03071}.
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DR STRING; 99883.ENSTNIP00000010752; -.
DR Ensembl; ENSTNIT00000010933.1; ENSTNIP00000010752.1; ENSTNIG00000007932.1.
DR GeneTree; ENSGT00940000153649; -.
DR HOGENOM; CLU_000315_5_2_1; -.
DR InParanoid; H3CR68; -.
DR OMA; AYMEDHR; -.
DR TreeFam; TF313572; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0071339; C:MLL1 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
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:0043066; P:negative regulation of apoptotic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; 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 DNA-templated transcription; IEA:UniProtKB-UniRule.
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; 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:SF2; -; 1.
DR PANTHER; PTHR46850; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 9; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|HAMAP-Rule:MF_03071};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03071}; Chromatin regulator {ECO:0000256|HAMAP-Rule:MF_03071};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_03071}; Helicase {ECO:0000256|HAMAP-Rule:MF_03071};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03071};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03071}; Nucleus {ECO:0000256|HAMAP-Rule:MF_03071};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_03071};
KW Repressor {ECO:0000256|HAMAP-Rule:MF_03071};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_03071};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_03071};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687, ECO:0000256|HAMAP-
KW Rule:MF_03071}.
FT DOMAIN 616..683
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 698..764
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 797..971
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1115..1266
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 389..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1384..1426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1657..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1961..1995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2007..2073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2198..2227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2240..2264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1712..1726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2020..2045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2046..2062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2242..2264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2320 AA; 260131 MW; 0A146DC12E251CDB CRC64;
MADPIMDLFE DTPLFNLDAL PDDSFTPGSS DPVEEALKLA LGQVDPPTDS ELVPTGLSDP
LVACAMPDPV PVPTPQPVPV MASQTVSIAS APSVTPAPVD GLQQIQVQTS IPVVSNTSVA
TSSTVLLTPQ QLAAITQQAG GKIVILKGPQ GQAQVLQTVS GATSQAGGKV IRVLSGTPLK
PGMSILQGGT VLNQTSPGQA QRVQRVLQSP NGPVKQVLLT SVPQQAQGQA VQVQIPAQAT
IDQGQTQGGE AKRITLVLQP PSQPGSVAGQ AAKLVLGQLP GGKLVLQGSQ LAALTQARAA
GQAGGQPKVL TIQLQVQQQP NQQGGVKVRK KYQLVSGAGN TGSPQVLQIS QGQGGQRVAI
PLKMLLQPQT SSASTAGGTV SVMKVTNASA AGPSATTTPS TQTIRITKAP QGESASVRRV
EILCKQEKAN RIVAEAIARA KARGEKNLPR VLNQDELPNT QSSPESGGTL TVVSAAKKNK
KKSPMSGGLT PKTAGGANKN STITLVGAKK RKRNASSDHS DGEISPASPV PLDDDLIMKR
RSNRVVKRKK YTEDLDIKIT DDEDEQEDVD VITTSAAVAS ISGGTAAQLK QELELDVDGH
PSMQFFVENP SEEDAAIVDK ILAVRVTKKE LTPGQYANAE EFFVKYKNYS YLHCEWASLE
QLEKDKRIHQ KIKRFKTKHA QMSRLFQEDE EPFNPDYVEV DRILDVSHSV DKDNGENVIY
YLVKWCSLPY EDATWELNED VDEGKVEEFK KIQNRQPRLK RTPRPSPGSW KKLEESREYK
NANTLREYQL EGVNWLLFNW YNRQNCILAD EMGLGKTIQS ITLLSEIYAA GVQGPFLVIA
PLSTITNWER EFSTWTNMNA IVYHGSLASR QMIQQYEMYC KDEKDHLIPG AYKFDALITT
FEMILSDCPE LREISWRCVI IDEAHRLKNR NCKLLDSLKM MDLEHKVLLT GTPLQNTVEE
LFSLLHFLEP AQFPSEIEFL REFGDLKTEE QVQKLQSILK PMMLRRLKED VEKNLAPKQE
TIIEVELTDV QKKYYRAILE RNFSFLSLGA NSNSNVPNLL NTMMELRKCC NHPYLINECP
GAEEKIVAEL REVYDPSAPD FHLQALIRSA GKLVLLDKLL PRLKAGGHKV LIFSQMVRCL
DILEDYLINK RYLYERIDGR VRGNLRQAAI DRFSKPDSDR FVFLLCTRAG GLGINLTAAD
TCVIFDSDWN PQNDLQAQAR CHRIGQSKAV KVYRLITRNS YEREMLDKAS LKLGLDRAVL
QSMSGNKDSN VNGIQQFSKK EIEDLLRKGA YAAIMDENDE GSRFCEEDID QILQRRATTI
TIESEGKGST FSKASFVASE NRTDIALDDP EFWQKWAKKA DIDVDSMNRK NTLVIDTPRV
RKQTRQYSSL RGEGGELSDL DSDDEYPPAN SRQSRASRRA DRHSGGGYGR TDCFRVEKHL
LVYGWGRWRD ILSHARCKRR LSERDVETIC RVILVFCLLH YRGDENIKSF IWELITPPEN
GREPQTLLNH SGLSIPVPRG RKGKRVKAQS TFDVQKVEWI RKYNPDTLLL DDSYRKHLKH
QCNKVLLRVR MLYYLKQEVI GEHADSILKG ADIRDVDIWM PDMEQQEVPA LWWDGEADRS
LLAGVFKHGY EMYTTMRADS CLCFLERVGR PDDKAIDAEQ HTGDAELGDD AEYDKYSEDP
EFKPATRHSK DIFEESDSMN VEEEISVEDK VKQPITESTS SQSGVCDWPS SSSLTARLRR
LITAYQRSYR QEQLKIEAEA KGDRRRRRCE QASKLKEIAR QERQQRWTRR EECDFYRVVS
TFGVETIKKE PDTLEGAQQE FDWNRFRTFA RLDKKTDESL SRYFRSFVAM CRRVCHLRPG
REDTSELPQT VAPITEERAS RTLYRISLLR RLRERVLPHP SLEERLLLAP HGSELPTWWK
LPDHDRQLML GAALHGVSRT ELSIFSDPQF TFSQARDEFI QNQQAPPPPP PAVSLIQPKS
EDIPSMNAEG TEEESPLLAG TQALADLPDT PLSHRDGKAA VQEWSMKRSK VRVEKTRDGT
KVEGGSDSDS DSGSSSSERS GSSDESGDSE EEKKWIPQIN LFSMCFLDVD NGLIPMMPSQ
DGIPPPDPLR LDWPKDRVLI NRLDSLCTLV VSGQWPSGRR YVSEAQLNPS SEFPGDDMAY
ARMVRKPLGM PGGPGADGED GEFTVKLLKE EGLKLTFSKQ ALMPNGSSGE SSRKRHKDQE
VCDRVPPSFS FPFSSKLSYS DGLHDPLERT PRRRDPPTWL KENPDYEVEG DMLELLVNRS
KRKRRRRADK ALTGTEKVKI INMRTGKKGF LPETLFHRLL
//
