ID A0A3Q1CQ65_AMPOC Unreviewed; 2374 AA.
AC A0A3Q1CQ65;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=CREBBP {ECO:0000313|Ensembl:ENSAOCP00000027918.1};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000027918.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000027918.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSAOCT00000020479.1; ENSAOCP00000027918.1; ENSAOCG00000017268.1.
DR GeneTree; ENSGT00940000155364; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:UniProt.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:UniProt.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:UniProt.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd05495; Bromo_cbp_like; 1.
DR CDD; cd20910; NCBD_CREBBP-p300_like; 1.
DR CDD; cd15647; PHD_CBP; 1.
DR CDD; cd15802; RING_CBP-p300; 1.
DR CDD; cd02337; ZZ_CBP; 1.
DR Gene3D; 2.10.110.40; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.246.20; Coactivator CBP, KIX domain; 1.
DR Gene3D; 1.10.1630.10; Nuclear receptor coactivator, CREB-bp-like, interlocking domain; 1.
DR Gene3D; 1.20.1020.10; TAZ domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR003101; KIX_dom.
DR InterPro; IPR036529; KIX_dom_sf.
DR InterPro; IPR009110; Nuc_rcpt_coact.
DR InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR InterPro; IPR037073; Nuc_rcpt_coact_CREBbp_sf.
DR InterPro; IPR010303; RING_CBP-p300.
DR InterPro; IPR038547; RING_CBP-p300_sf.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; CBP/P300-RELATED; 1.
DR PANTHER; PTHR13808:SF34; CREB-BINDING PROTEIN; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF09030; Creb_binding; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02172; KIX; 1.
DR Pfam; PF06001; RING_CBP-p300; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF47040; Kix domain of CBP (creb binding protein); 1.
DR SUPFAM; SSF69125; Nuclear receptor coactivator interlocking domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF57933; TAZ domain; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00203}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00203};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 365..451
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 609..688
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 996..1068
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1216..1593
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1595..1643
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1658..1739
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 365..451
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1658..1739
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1449..1507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1767..1867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1961..1994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2037..2068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2122..2362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1495
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1781..1845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1846..1863
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2038..2065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2122..2170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2193..2245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2273..2317
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2330..2350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2374 AA; 258233 MW; 112DDFEC120E002B CRC64;
MAENLLDIGP PNSKRPKLNS PALSTSDGQD LGSLSWDDLE NDLPDELIPN GGDLSLMGAM
PSNGGAAPGG GGTGGAPAGL GGGGGAGVPD AAAKHKQLSE LLRAGSTSSI TGTGLNSASP
QPGGMGPQLG TPLGKSPLGQ GSPNNHPSPQ AQKAGTPTGV AGQNNNNNTA AMGLNATGFN
QAMINNSQGH AGLLAQGGQP QPGQVMNGGL VPGAGRGRGA GVAGMQYKGP TMQGTATGPG
GSGSALAETL TQGGQQMGAH TTLNAAQQAG NMNKMGMNNN GGPFGAQPYG QGAAGPGQQL
NPQQQLQNKA ALANSLPPFP NELKGAAVTS VPNMQLQQQP QQQAAMLPLP GGGGVAVPSA
GPTADPEKRK LIQQQLVLLL HAHKCQRREQ ANGEVRACAL PHCRTMKNVL NHMTHCQAGK
SCQVAHCASS RQIISHWKNC TRHDCPVCLP LKNASDKRTQ QPMLSSPSTG LQNPMSSVGV
GQPSAPTINT SAPIDPSSMQ RAYAALGLPY SSQATGQAQA QQAPGQTAGA QNAQAQQQQL
PQQMRPINTL GNQMALGGAT MGVTTSEQTN LHTDSLPNSL NTNNQLLSDG SAVGSMGSLP
TAAPISATGS RKAWHEHVTQ DLRNHLVHKL VQAIFPTPDP AALKDRRMEN LVAYARKVEG
DMYESANSRD EYYHFLAEKI YKIQKELEEK RRSRLQKQII NQAPMTAQGT QQPGLSQPNA
LGPRPQNGPV PLPNMPNQIM NRMQVSQGIN QFNHMALPNA QMSQAPMGAR AASPMNHPQQ
MNMSSVPAMG MSPSRMPQAQ GMMTGHSGGN MVGQTASQGQ FMSQTQFPPG SAAVAATGAM
NVTVGPGMGQ PPAQAAVTQL SQPGASLDNR VPTPASAASA DLHSQHVGAD LPVQEVKAEA
HHDQQEFEAA GGKTEPKMET EDDSASVMVK KEEPDEKPEP MEVEEKKPEM KTEPKEEEEG
GANGTTSSSP SQSRRKIFKP EELRQALMPT LESLYRQDPE SLPFRQPVDP MLLGIPDYFD
IVKNPIDLST IKRKLDTGQY QEPWQYVDDV WLMFNNAWLY NRKTSRVYKY CSKLAEVFES
EIDPVMEGLG YCCGRKYEFS PQTLCCYGKQ LCTIPTGGTY YSYQNRYHFC EKCFNEIQGE
SVTLGDDPAQ PQTMISKDQF ERKKNDVLDP EPFVECKDCG RKMHQICVLH YEVIWPSGFI
CDNCLKKSGK TRKENKFSAK RLQSTRLGMY IEDRVNKYLK RQNHPEAGEV FVRVVASSDK
TVEVKPGMKT RFVDTGEMPE TFPYRTKALF AFEEIDGVDV CFFGMHVQEY GSECPFPNTR
RVYISYLDSI HFFRPRILRT AVYHEILIGY LEYVKKLGYA QGHIWACPPS EGDDYIFHCH
PPDQKIPKPK RLQEWYRKML DKAFAERILH DYKDIFKQAT EDRLTSANEL PYFEGDFWPN
VLEESIKELE QEEEERKKEE NTAASETPEG TPGDSKNAKK KNNKKTNKNK SSMSRANKKK
PGMPNVANDL SQKLYATMEK HKEVFFVIHL HSGPMANTLP PIVDPDPLLS CDLMDGRDAF
LTLARDKHWE FSSLRRCKWS TMCMLVELHN QGQDRFVYTC NECKHHVETR WHCTVCEDFD
LCINCYNTKG HEHQMVKWGL GLDDDNNSQS GEASKSPQES RRLSIQRCIQ SLVHACQCRN
ANCSLPSCQK MKRVVQHTKG CKRKTNGGCP VCKQLIALCC YHAKHCQENK CPVPFCLNIK
HKLRQQQLQH RLQQAQLMRR RMATMQGRTM PLPSPPASAA PSTPTSHAQP NTPQTPQQPL
SNQPQTPNSA GVMSPSFPNA PRTGQPQTPV SQGKPGPQAS PLHQQQSPLP QPPQPPQQLP
QQPPPAAVKM ARHIEMMAQA QQNQQNYRLS VNGLPMNPQQ PQPRMTGPMQ MVPGPRGQQV
MPAGMAPGQW PGAAASMQTN QQPGLVPGQT AQQTINMQRA MMPPGQQPQP NQRMLIPQQP
GARPQTPQRS GAIPPNALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA FIKQRTAKYH
ANQPQQQQQQ QPQAGQQQQP GMPTMQTMAM PGGAVQRPGM PPQQPQQAPV QGMAQLGPQG
QLMNAAHNTN PQIQELYRRQ LLRQQQQQQQ QQQGVMPQGH PGQFPAQAQG TTTTYSQLRM
QQQQQQIAMQ AGAGAAGGSM GQLPPMAQMA QPGMGMDSQN MLHQRLLQQQ QQQQQQLPQQ
QAVLKQQMGS PAQPSPMSPQ THLLAGQPQG GAHLPGQPAL ANALSNQVRS PAPVQSPCPP
SQQQQPQPPH SSPSPQVQSQ PQPSPQHPPP PHSGSPHPGL GGPLQSMEQG HLGTPEQSAM
LPQLNTPNRG GLSGDLGMVG DATGDTLEKF VEGL
//
