ID A0A8M3AQU5_DANRE Unreviewed; 2646 AA. AC A0A8M3AQU5; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 28-JUN-2023, entry version 6. DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184}; DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184}; GN Name=ep300b {ECO:0000313|RefSeq:XP_009297682.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Proteomes:UP000000437, ECO:0000313|RefSeq:XP_009297682.1}; RN [1] {ECO:0000313|RefSeq:XP_009297682.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_009297682.1}; RG RefSeq; RL Submitted (MAR-2023) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_009297682.1; XM_009299407.3. DR GeneID; 565612; -. DR KEGG; dre:565612; -. DR CTD; 565612; -. DR Proteomes; UP000000437; Chromosome 3. 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-UniRule. DR GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0016573; P:histone acetylation; 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; 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; 1.20.1020.10; 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; 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; 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:SF29; HISTONE ACETYLTRANSFERASE P300; 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; 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 1: Evidence at protein level; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315, ECO:0000256|PROSITE- KW ProRule:PRU01065}; 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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A8M3AQU5}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; 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, ECO:0000256|PROSITE- KW ProRule:PRU01065}; 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 302..388 FT /note="TAZ-type" FT /evidence="ECO:0000259|PROSITE:PS50134" FT DOMAIN 534..613 FT /note="KIX" FT /evidence="ECO:0000259|PROSITE:PS50952" FT DOMAIN 1040..1123 FT /note="Bromo" FT /evidence="ECO:0000259|PROSITE:PS50014" FT DOMAIN 1281..1658 FT /note="CBP/p300-type HAT" FT /evidence="ECO:0000259|PROSITE:PS51727" FT DOMAIN 1660..1708 FT /note="ZZ-type" FT /evidence="ECO:0000259|PROSITE:PS50135" FT DOMAIN 1723..1804 FT /note="TAZ-type" FT /evidence="ECO:0000259|PROSITE:PS50134" FT ZN_FING 302..388 FT /note="TAZ-type" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203" FT ZN_FING 1723..1804 FT /note="TAZ-type" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 49..139 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 396..434 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 454..477 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 616..635 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 719..1021 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1514..1573 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1827..1989 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2084..2158 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2229..2267 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2329..2349 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2372..2473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2494..2646 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 55..69 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 731..763 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 770..785 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 801..820 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 821..837 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 844..930 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 959..1004 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1514..1529 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1546..1560 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1852..1883 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1914..1937 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1946..1961 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2106..2158 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2329..2347 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2372..2455 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2494..2538 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2539..2560 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2561..2579 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2597..2616 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1392..1394 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01065" FT BINDING 1404..1405 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01065" FT BINDING 1451 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01065" FT BINDING 1456 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01065" FT BINDING 1460 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01065" SQ SEQUENCE 2646 AA; 287599 MW; 18D9B3C9B336159C CRC64; MADNVLDSGP PTAKRPKLSS PALSVSASDG NDFGSLFDLE HDLPDELINS SDLGLPNGMD PSQLHTSLGG GGMSGPLGVS GQDTAAKHKH LSELLRPGAP PSASTATGSP GNAASLGMMG GLSGGPVTQG MGGPQQQPSM MPQPGMVGGL NRAMMGTQKG NGQPQSMMGG QMMNGAPRMG YANVNMNAGM AGNGNMLPDS LQQPNAGQQM AQAAMRPQQP GAVNKMGMMG APGPYGGSYG QCGGQSQLGP QLQNKAGQPN SINQFNMDKK PQLGQNMGGM QGPGVVGGVS GPGGTAAPPA ADPEKRKLIQ QQLVLLLHAH KCHRREQANG EVRQCNLPHC RTMKNVLNHM THCQAGKSCQ VAHCASSRQI ISHWKNCTRH DCPVCLPLKS AGDKRNQQSL LGGAGMAMGG PLGGSLPGGQ PSAPNINPPS QIDPSSIERA YAALGLTYQG NQASNQNQQT SVPGQPGMRS LNNMAGGNSM GVNGGVGAPM SNQHPGMLPD GMLHRNMTAQ SLMNDSSGVG NMGSAATATP PSAGMRKSWH EDITQDLRNH LVHKLVQAIF PTPDPAALKD RRMENLVAYA RKVEGDMYES ANSRAEYYHL LAEKIYKIQK ELEEKRRTRL QKQDGPHSDP SLVQATGPSQ MVNRMQNPAG MPHSLNGMNQ FGQVGMQQPM GQRATPPLPM GANLNQMSMQ GTPRMAQPNV PQLQNQYMQN QFTGTGAGLG QGAVGLNQPA GQGAMPQNQM PTPPSLSVHS PVAQSQSSVP VSGAAAGPQG PPSNHPPPAP QPGLHTHCPP LRQNSPSPAR SLTPTPAPHQ TPPQLPGNQT PQPHTPNSST TMAPPASQLP PMAQGVASEK SSQLQQQSHG GGATGGPQTG LASSVPSQNA HGLCTHPHSP LSQKSSATVD GQASTPASVS SADPSSQLTS SEPTAPLDSK TEVKQQDEEE ENENETEDKA SGKMAAMQTE IKSEEKPEIK KEEPAGDECK TEPMETSTAE DKKPEVKTEP KEEEVAGANS TPANTQSKKK EFKPDELRQA LMPTLEALYR QDPESLPFRQ PVDPQLLGIP VRIRTSNKTN LDYFDIVKNP IDLSTIKRKL DTGQYQEPWQ YVDDVWLMFN NAWLYNRKTS RVYKYCSKLA EVFEQEIDPV MQELGYCCGR KLEFSPQTLC CYGKQLCTIP RDAAYFSYQN SSPKYGLLAD RYHFCEKCFN EIQGENVSLG DDPTQPQTSI NKDQFQRKKN DTLDPELLLE CGDCGRKMHQ ICVLHNETIW PSGFICDGCL KKSNSTRKEN KYAAKRLPQT KLGNFLETRV NDYLKRQNHP ESGEVTIRVV HISDKVVEVK PGMKSRFVDS GEMSESFPYR TKALFAFEEI DGTDVCFFGM HVQEYGSDCP PPNQRRVYIS YLDSVHFFQP RHLRTGVYHE ILIGYLEYVK KMGFVMGHIW ACPPSEGDDY IFHCHPSDQK IPKPKRLQEW YKKMLDKAVT ERIVHDYKDI FKQATEDRLT SAKELPYFEG DFWPNVLEES IKELEQEEEE RKREENNTSS ESIDATNGDS KNAKKKNNKK TSKNKSSLSR ANKKKPGMPN VSNDLSQKLY ATMEKHKEVF FVIRFIAGPA ANSLPPISDP DTLMACDLMD GRDAFLTLAR DKHLEFSSLR RAKWSSMCML VELHNQTQDR FVYTCNECKH HVETRFHCTV CEDYDLCITC YNVKGHEHKM EKLGLGLDDE SNNQAAASTQ NPGDSRRLSI QRCIQSLVHA CQCRNANCSL PSCQKMKRVV QHTKGCKRKT NGGCPICKQL IALCCYHAKH CQETKCPVPF CLNIKHKLRQ QQLQHRLQQA QMLRRRMATM QRVGQPPPCG GGPPGGLPSP GNNGATGPST PTSVGTQPAT PQTPTQLTPN LISLPQPGAG GVPAGAPQQS PQHPVHHQFQ QMPGAGGMMN SQQQQMVPQQ SLGQVPHPHN QYGPHPTGPS PNTQSQGKPG LGPATPPQLP SNPGTVPMAQ QQQPTGPPAA AVEIAMKIQQ VADAQRKMAQ VQLLQRQAAQ AGMMPQHHQQ PQGQIGVAHP GIGMVGPQGL ASQAQTSANR VQMEQQQGPQ GMMGAGPMQQ QQPQQVAVQG QMPPQMHPQQ PRMNPPLQPQ QQQWPGQGMP TQQRPAMMSQ QGMVSMQPQP QPQQPSQQTQ QQQAPQMPNR NALMSMVQAG LQSGVASGAA ASNLPQGALQ QLLRTLRSPS SPQQQQQVLN ILRSSPLLMA AFIKQRVHKY KGGTGGPSGP QGGPGPMGGQ PVGVNTGVPQ PGMHLGQGVN MQSQLLSQQQ SQQQQQMQQR PLLQQQQVAA LQQQQQQQQQ QQQQQQQQQH QQQQQQQQHQ QQQQQQQGIQ GQGTPNMANP HFRELVMRRQ QQLQFQQQQQ QQQQQQQQQM SNHAAFQQQQ GYMSQQGNMQ VPPGGQPLQG VQPGQQQNFP GNPAQQQAAA ALQQRLAQQQ HQLQMQQQQN AATQGPDMGP GGGPQPTQLG PGLQSPQALL QQALHQRLFP QQQHLSGTSP AQQNNPMSPQ QQQISQSPHL QGQQLPSSLS NQVCSPQPSP RPQSQPPHSS PSPRLQPQPS PHHISPQTQT GSPHPSHLQQ HHSGMAPPPP PHQQPQHNSK DPSGFGADQN AMLSQLSGMA GLHGPGANDM LPPSGQDLGI NMNLTL //