ID A0A8M3AXY5_DANRE Unreviewed; 2645 AA. AC A0A8M3AXY5; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 22-FEB-2023, entry version 4. 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_009297684.1}; 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_009297684.1}; RN [1] {ECO:0000313|RefSeq:XP_009297684.1} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_009297684.1}; RG RefSeq; RL Submitted (APR-2022) 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_009297684.1; XM_009299409.3. DR GeneID; 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; 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:A0A8M3AXY5}; 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 301..387 FT /note="TAZ-type" FT /evidence="ECO:0000259|PROSITE:PS50134" FT DOMAIN 533..612 FT /note="KIX" FT /evidence="ECO:0000259|PROSITE:PS50952" FT DOMAIN 1039..1122 FT /note="Bromo" FT /evidence="ECO:0000259|PROSITE:PS50014" FT DOMAIN 1280..1657 FT /note="CBP/p300-type HAT" FT /evidence="ECO:0000259|PROSITE:PS51727" FT DOMAIN 1659..1707 FT /note="ZZ-type" FT /evidence="ECO:0000259|PROSITE:PS50135" FT DOMAIN 1722..1803 FT /note="TAZ-type" FT /evidence="ECO:0000259|PROSITE:PS50134" FT ZN_FING 301..387 FT /note="TAZ-type" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203" FT ZN_FING 1722..1803 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 395..433 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 453..476 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 615..634 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 718..1020 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1513..1572 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1826..1988 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2083..2157 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2228..2266 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2328..2348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2371..2472 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2493..2645 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 730..762 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 769..784 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 800..819 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 820..836 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 843..929 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 958..1003 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1513..1528 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1545..1559 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1851..1882 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1913..1936 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1945..1960 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2105..2157 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2328..2346 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2371..2454 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2493..2537 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2538..2559 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2560..2578 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2596..2615 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1391..1393 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01065" FT BINDING 1403..1404 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01065" FT BINDING 1450 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01065" FT BINDING 1455 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01065" FT BINDING 1459 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01065" SQ SEQUENCE 2645 AA; 287470 MW; CD00CC10BCC020A8 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 GPGVVGGVSG PGGTAAPPAA DPEKRKLIQQ QLVLLLHAHK CHRREQANGE VRQCNLPHCR TMKNVLNHMT HCQAGKSCQV AHCASSRQII SHWKNCTRHD CPVCLPLKSA GDKRNQQSLL GGAGMAMGGP LGGSLPGGQP SAPNINPPSQ IDPSSIERAY AALGLTYQGN QASNQNQQTS VPGQPGMRSL NNMAGGNSMG VNGGVGAPMS NQHPGMLPDG MLHRNMTAQS LMNDSSGVGN MGSAATATPP SAGMRKSWHE DITQDLRNHL VHKLVQAIFP TPDPAALKDR RMENLVAYAR KVEGDMYESA NSRAEYYHLL AEKIYKIQKE LEEKRRTRLQ KQDGPHSDPS LVQATGPSQM VNRMQNPAGM PHSLNGMNQF GQVGMQQPMG QRATPPLPMG ANLNQMSMQG TPRMAQPNVP QLQNQYMQNQ FTGTGAGLGQ GAVGLNQPAG QGAMPQNQMP TPPSLSVHSP VAQSQSSVPV SGAAAGPQGP PSNHPPPAPQ PGLHTHCPPL RQNSPSPARS LTPTPAPHQT PPQLPGNQTP QPHTPNSSTT MAPPASQLPP MAQGVASEKS SQLQQQSHGG GATGGPQTGL ASSVPSQNAH GLCTHPHSPL SQKSSATVDG QASTPASVSS ADPSSQLTSS EPTAPLDSKT EVKQQDEEEE NENETEDKAS GKMAAMQTEI KSEEKPEIKK EEPAGDECKT EPMETSTAED KKPEVKTEPK EEEVAGANST PANTQSKKKE FKPDELRQAL MPTLEALYRQ DPESLPFRQP VDPQLLGIPV RIRTSNKTNL DYFDIVKNPI DLSTIKRKLD TGQYQEPWQY VDDVWLMFNN AWLYNRKTSR VYKYCSKLAE VFEQEIDPVM QELGYCCGRK LEFSPQTLCC YGKQLCTIPR DAAYFSYQNS SPKYGLLADR YHFCEKCFNE IQGENVSLGD DPTQPQTSIN KDQFQRKKND TLDPELLLEC GDCGRKMHQI CVLHNETIWP SGFICDGCLK KSNSTRKENK YAAKRLPQTK LGNFLETRVN DYLKRQNHPE SGEVTIRVVH ISDKVVEVKP GMKSRFVDSG EMSESFPYRT KALFAFEEID GTDVCFFGMH VQEYGSDCPP PNQRRVYISY LDSVHFFQPR HLRTGVYHEI LIGYLEYVKK MGFVMGHIWA CPPSEGDDYI FHCHPSDQKI PKPKRLQEWY KKMLDKAVTE RIVHDYKDIF KQATEDRLTS AKELPYFEGD FWPNVLEESI KELEQEEEER KREENNTSSE SIDATNGDSK NAKKKNNKKT SKNKSSLSRA NKKKPGMPNV SNDLSQKLYA TMEKHKEVFF VIRFIAGPAA NSLPPISDPD TLMACDLMDG RDAFLTLARD KHLEFSSLRR AKWSSMCMLV ELHNQTQDRF VYTCNECKHH VETRFHCTVC EDYDLCITCY NVKGHEHKME KLGLGLDDES NNQAAASTQN PGDSRRLSIQ RCIQSLVHAC QCRNANCSLP SCQKMKRVVQ HTKGCKRKTN GGCPICKQLI ALCCYHAKHC QETKCPVPFC LNIKHKLRQQ QLQHRLQQAQ MLRRRMATMQ RVGQPPPCGG GPPGGLPSPG NNGATGPSTP TSVGTQPATP QTPTQLTPNL ISLPQPGAGG VPAGAPQQSP QHPVHHQFQQ MPGAGGMMNS QQQQMVPQQS LGQVPHPHNQ YGPHPTGPSP NTQSQGKPGL GPATPPQLPS NPGTVPMAQQ QQPTGPPAAA VEIAMKIQQV ADAQRKMAQV QLLQRQAAQA GMMPQHHQQP QGQIGVAHPG IGMVGPQGLA SQAQTSANRV QMEQQQGPQG MMGAGPMQQQ QPQQVAVQGQ MPPQMHPQQP RMNPPLQPQQ QQWPGQGMPT QQRPAMMSQQ GMVSMQPQPQ PQQPSQQTQQ QQAPQMPNRN ALMSMVQAGL QSGVASGAAA SNLPQGALQQ LLRTLRSPSS PQQQQQVLNI LRSSPLLMAA FIKQRVHKYK GGTGGPSGPQ GGPGPMGGQP VGVNTGVPQP GMHLGQGVNM QSQLLSQQQS QQQQQMQQRP LLQQQQVAAL QQQQQQQQQQ QQQQQQQQHQ QQQQQQQHQQ QQQQQQGIQG QGTPNMANPH FRELVMRRQQ QLQFQQQQQQ QQQQQQQQMS NHAAFQQQQG YMSQQGNMQV PPGGQPLQGV QPGQQQNFPG NPAQQQAAAA LQQRLAQQQH QLQMQQQQNA ATQGPDMGPG GGPQPTQLGP GLQSPQALLQ QALHQRLFPQ QQHLSGTSPA QQNNPMSPQQ QQISQSPHLQ GQQLPSSLSN QVCSPQPSPR PQSQPPHSSP SPRLQPQPSP HHISPQTQTG SPHPSHLQQH HSGMAPPPPP HQQPQHNSKD PSGFGADQNA MLSQLSGMAG LHGPGANDML PPSGQDLGIN MNLTL //