ID A0A3B3TZL7_9TELE Unreviewed; 2435 AA.
AC A0A3B3TZL7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSPLAP00000005927.1};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000005927.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000005927.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_014881447.1; XM_015025961.1.
DR STRING; 48699.ENSPLAP00000005927; -.
DR Ensembl; ENSPLAT00000007118.1; ENSPLAP00000005927.1; ENSPLAG00000007956.1.
DR GeneID; 106942609; -.
DR CTD; 567111; -.
DR GeneTree; ENSGT00940000155364; -.
DR OrthoDB; 5490807at2759; -.
DR Proteomes; UP000261500; 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 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 317..403
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 552..631
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1056..1128
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1276..1653
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1655..1703
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1718..1799
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 317..403
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1718..1799
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1826..1936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2012..2072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2169..2278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2292..2415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..898
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 963..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1555
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1851..1867
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1868..1890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1898..1913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1922..1936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2012..2049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2053..2070
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2169..2184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2194..2256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2292..2340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2349..2415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2435 AA; 266449 MW; D53DC055656DF9E3 CRC64;
MADNLLDAGP PTAKRPKINS PISGSDGPDL VSLLDLENDL PDELILNGES GNGPSANCGP
SGVPPGLNSA IPDAASKHKQ LSELLRPGSS SILGGALNSG SPQQGGMVAS QLGAVLGKGP
LGQGSPNHQS PQGQKVVSTG QGNGVMGFNQ TMLNSGQGHG VMGQVGQVMN GAMGPAGRGR
PGPGMQYQGQ AMQGTQGGAG PGVGGSVLAE TLTQGGPQMG APHTMNAQQA GNMNKMVMSG
APFGQQYGQA GVQQMGTAGV NAQQLQNKTA LSNNLPPFPA DLKGAGNVPN MAQMQQQVAS
MGMVSGAGGV SGGPTADPEK RKLIQQQLVL LLHAHKCQRR EQANGEVRAC TLPHCRTMKN
VLNHMTHCQA GKSCQVAHCA SSRQIISHWK NCTRHDCPVC LPLKNASDKR NQQPMLSSPG
ASLQNAISTV GPGQPSATAI NSAPTHIDPS SMQRAYAALG LPYGNHSPAQ VQGQGPAQQN
PQAHQQLRNM NPLGTNQMNQ MAGGLGSHSS DQTGLLSDSP LPSSLNKQLL PDGSEVEGMG
NLPAATPLSA TGVRKAWHEH VTQGLRSHLV HKLVQAIFPT PDPAALKDRR MENLVAYARK
VEGDMYESAN SRDEYYHFLA EKIYKIQKEL EEKRRSRLQK QPIMVGAPGP QQPGMAQPNS
MGPAQAVRPP NGPATMPNMP NQMMNRMQVD QGISQFNPMA MQNAQMPQAP MGARAPSPMS
HPQQMNMNSV MGMSPSRMPP NQGMMGNHAN SMSQPAAQGQ YLQQGQYPGA AGGAMNVNIS
MGQTMPQAAV AQQQQTSNLP LNALGSQLPS GPTTQPARGT PPPPSISQQQ QQQQQQQHAP
TQAQVPPQPS TPGSAVGPPS TPTHIPSSLP RPPAAMSTPP DPSQPLTPLQ PPSEPPSQMQ
QPTSVQPQHP STPLSQAAAG IDNRVPTPGS VAELSSQQAL PDMSISEVKS EVKEEEEEEE
EEDSKSGKKQ NDVKMEQDDE TKPSLVKKEE TDAAEPKQEP METDEKKPEV KVEPKEEEDG
ASNSTSAAST AQNRKKIFKP EELRQALMPT LEALYRQDPE SLPFRQPVDP MVLGIPDYFD
IVKNPIDLST IKRKLDTGQY QEPWQYVDDI WLMFNNAWLY NRKTSRVYKY CTKLAEVFEA
EIDPVMQGLG YCCGRKYEFS PQTLCCYGKQ LCTISRDSTY YSYQNRYHYC EKCFNEIQGN
SVNLGDDPAQ PQTKISKDQF EKKKNDTLDP EPFVECKDCG RKMHQICVLH YDVIWPSGFV
CDNCLRKSGK TRKENKFSAK RLQTTRLGTY IEDRVNKYLK RQNHPEAGEV FVRVVASSDK
TVDIKPGMKS RFVDSGEMVA SFPYRTKALF AFEEIDGVDV CFFGMHVQEY GSDCPFPNTR
RVYISYLDSV HFFKPRVLRT AVYHEILIGY LEYVRKLGYV MGHIWACPPS EGDDYIFHCH
PPDQKIPKPK RLQEWYRKML DKAFAERIIH DYKDIFKQAT EDRLTSANEL PYFEGDFWPN
VLEESIKELE QEEEERKKEE NTASSETTEG VQADSKNAKK KNNKKTNKNK SSVSRSNKKK
PGMPNVANDL SQKLYATMEK HKEVFFVIHL HSGPVINTLP PIMDPDPLLT CDLMDGRDAF
LTLARDKHWE FSSLRRCKWS SMCMLVELHN QGQDRFVYTC NECKHHVETR WHCTVCEDYD
MCINCYNTKG HEHQMVKWGL GIDDDSNSQS GEASKSPQES RRLSIQRCIQ SLVHACQCRN
ANCSLASCQK MKRVVQHTKG CKRKTNGGCP VCKQLIALCC YHAKHCQENK CPVPFCLNIK
QKLRQQQLQH RLQQAQMMRR RMATMAGRGM PMPSPPTSSA PETPTSVQQP NTPQTPQPMP
NHPQQQQPPN PGNLGQGFPS NGRSSQPSTP GPQGKPGPQS SPLHQQLSPM PNMPHQQQAP
PPQQPQQQQQ QQQQQLLAAM KVAQQIEMAA KAKQQQQQQQ PGYAMNGMPM NQTRMMSPIQ
NQMQMMQGHR GPQVMQAVSQ GQWGVGMQNA QGHQSLVPPQ QGPTASQQAQ GNPMSQQSPL
MQRPMMPQQS GPQMPGVMPP QGPPQQGMTP QQPNMPRVMP GNITPSAVQE LLHTLKSPSS
PQQQQQVLTI LKSNPHLMAA FIKQRAAKYQ ASQAAPQQQQ QQQQVQQQNP QVLLGSQPGM
QAMAAMNQMQ RTGMAPQQQP PQLVGPQGMA PMGPQGQMMN TAQNGSPQYH RQLLRMQQMQ
QQTGMPQGHS QFPPQQQGPP GFSQLRTHQQ LVMQGGSGPM GSVPPMSQMG QPGMGMEGIS
NHLKQRMLQN QMMKQQMGSP GQANPMSPQP HLLQGQGQPG AHLPGQTMAN TLGNQVRSPA
PVQSPRPPSQ QAPHSGSSPR IQPQPSPQHG ALHSSSPHPS LGPMSGSMDQ GHMGTSEQSA
MLPQLNTPNR GGLSNDMNMV GDTTGDTLER FVEGL
//
