ID H2U5B8_TAKRU Unreviewed; 2423 AA.
AC H2U5B8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 74.
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:ENSTRUP00000032131.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000032131.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000032131.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000032131.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR STRING; 31033.ENSTRUP00000033022; -.
DR Ensembl; ENSTRUT00000032254.3; ENSTRUP00000032131.3; ENSTRUG00000012692.3.
DR GeneTree; ENSGT00940000155364; -.
DR HOGENOM; CLU_000162_2_0_1; -.
DR Proteomes; UP000005226; Chromosome 17.
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:UP000005226};
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 343..429
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 555..634
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1042..1114
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1262..1639
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1641..1689
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1704..1785
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 343..429
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1704..1785
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1495..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1813..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2087..2136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2163..2203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2265..2393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..883
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1495..1510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1527..1541
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1850..1891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1892..1906
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2087..2108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2265..2351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2376..2393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2423 AA; 263516 MW; 6F74FC296FAD2B0B CRC64;
MAENLLEMGP PSSKRPKLNS PALSASDGPD LGSLTWDDLE NDLPDELIPN GGDLSLMSGM
PSNGGAASGP GGTPTGLGGG GSGVPDAAAK HKQLSELLRG GNSSSIASTG LNSANSQAGS
MGPQLGTPLG KSPLGQGSPN NHHSPQAQKA GTPSGVAGQN TNGNTAAMGL NSAGFNQTMI
NNGPSHGGLL PQGGQPQPGQ MMNGGLGADA GRYQGASMQA AAAGAGGAAS ALAETLTQGG
QQMGAHTNLN GAQQAGSLNK MGLSSNGGPF GAQPYGQGAT GPGQQLNQQQ QLQNKVTLAN
SLPPFHNELK GAAVTNQPQQ QAPMLPMAGS GSVAVTSAGP TADPEKRKLI QQQLVLLLHA
HKCQRREQAN GEVRACALPH CRTMKNVLNH MTHCQAGKSC QVAHCASSRQ IISHWKNCTR
HDCPVCLPLK NASDKRTQQP KLGSPNAGLQ NSISSVGVGQ PSPTINTSTP IDPSSMQRAY
AALGLPYSSQ TTGQSQQGPG QQAGNQMALG GTAMGVTTSD QTNLHTDSVP NLLSDGSAVG
SMGNLPTAAP MSATGTRKAW HEHVTQDLRS HLVHKLVQAI FPTPDPAALK DRRMENLVAY
ARKVEGDMYE SANSRDEYYH FLAEKIYKIQ KELEEKRRSR LQKQIMNQAP LAVQGTQQPS
LPQPNAFGAR PQNGPVPLPN MPNQIMNRMQ VSQGMNQFNH MALPNAQISQ APMGARAASP
MNHPQQMNLS AVPALGMSPS RMPQAQGMMA GHGAGNMVGQ TNSQGQFLAQ SQFPTGAAVN
AAATMNVTVG SGMGQSPAQA AVTQQQQQSA NLPMNALGPS LGPQLVSSQT PLQSTPPAAA
SSAPTVGGAT NLPHPQPSSR SSTPTLPAPA PGATPPRPTQ PQPQVELPTA AQMQPPPQPP
TTPVRLRSFR MPSTMTPHLE NRVPTPASAS SADLHTQHVG ADLPTQEVKT DANHDQQEYE
AACGKIEPKM EAEEDMVSVK KEEPEEKTES MEVEEKKPEP KEEDDAGANG TTSSSPSQSR
RKIFKPEELR QALMPTLESL YRQDPESLPF RQPVDPLLLG IPDYFDIVKN PIDLSTIKRK
LDTSQYQEPW QYVDDVWLMF NNAWLYNRKT SRVYKYCSKL AEVFESEIDP VMQGLGYCCG
RKYEFSPQTL CCYGKQLCTI PTGGTYYSYQ NRYHFCEKCF NEIQGDSVTL GDDPAQPQTL
TQLLYNIELF TQYFPLNRFV ECKDCGRKMH QICVLHYEVI WPSGFICKSC LKKSGKTRKE
NKFTAKRLQT TRLGMYIEDR VNKYLKRQNH PEAGEVFVRV VASSDKTVEV KPGMKARFVD
TGEMPETFPY RTKALFAFEE IDGVDVCFFG MHVQEYGSEC AFPNTRRVYI SYLDSIHFFR
PRILRTAVYH EILIGYLEYV KKLGYTQGHI WACPPSEGDD YIFHCHPPEQ KIPKPKRLQE
WYRKMLDKAF AERILHDYKD IFKQATEDRL TSANELPYFE GDFWPNVLEE SIKELEQEEE
ERKKEENTAA SETPEGAQGD SKNAKKKNNK KTNKNKSSLS RANKKKPGMP NVANDLSQKL
YATMEKHKEV FFVIHLHSGP MANTLPPIVD PDPLLSCDLM DGRDAFLTLA RDKHWEFSSL
RRCKWSTMCM LVELHNQGQD RFVYTCNECK HHVETRWHCT VCEDFDLCIS CYNTKGHEHQ
MVKWGLGLDD DNNSQSGEAS KSPQESRRLS IQRCIQSLVH ACQCRNANCS LPSCQKMKRV
VQHTKGCKRK TNGGCPVCKQ LIALCCYHAK HCQENKCPVP FCLNIKHKLR QQQMQHRLQQ
AQLMKRRMAT MQGRTMPLPS PPATAAPSTP TSHTQPNTPQ TPQPPLSNQP QTPNSARVMS
PTFANAPRNG QPQAPVSQGK PGPQASPLHQ QQSPLPQPPQ APQQLQQQPP PLAAVKMARH
IEMMAQAQQN YRANMNGLPM NPPQQQQRMP GPVQPSMQMV PGPRGAQVMQ PGMTPGQWPG
AAGPIQAVQN PQGLVPGQTP QQPMTMQRAM MTPGQQPQQP ARMLIPQQPG ARPQTPQRPG
TIAPNALQDL LRTLKSPSSP QQQQQVLNIL KSNPQLMAAF IKQRTAKYQA NQPQQPGGQQ
QQPGMPTIQP MTMAGAVQRP GMPPQQPQQP SAQGMASLGA QTQLMNPAHN TGPQVQEMYR
RQLLRQQQQQ QQQQQGVMPQ GHPGQFPPQA QGTAATYSQL RMQQQQQQQQ LALQAGAGTA
GGGLGQLPPM SQMAQAGLGM DSTQNLLHQR MLQQQQQQQQ QQLPQQQQVV LKQQMGSPAQ
PSPMSPQTHL LAGQSQTGGH LPGQPSLASA LNNQVRSPAA VQSPCPSSQQ QSQQQRPHSS
PSPQVSNQAQ PSPQHPHPPH SASPHPGLGG TLSGSIEQGH LGTPEQSAML PQLNTPNRGV
LNSDLGMVGD TTGDTLESFV AQL
//
