ID A0A384A2Q4_BALAS Unreviewed; 2304 AA.
AC A0A384A2Q4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=CREBBP {ECO:0000313|RefSeq:XP_007181608.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007181608.1};
RN [1] {ECO:0000313|RefSeq:XP_007181608.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007181608.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_007181608.1; XM_007181546.1.
DR GeneID; 103016523; -.
DR CTD; 1387; -.
DR OrthoDB; 5490807at2759; -.
DR Proteomes; UP000261681; 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; cd15557; PHD_CBP_p300; 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:UP000261681};
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 347..433
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 587..666
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 967..1039
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1187..1564
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1566..1614
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1629..1710
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 347..433
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1629..1710
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1738..1823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1974..2113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2156..2278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..929
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..945
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1466
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1747..1780
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1818
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1974..2009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2026..2050
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2057..2083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2091..2113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2156..2212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2213..2240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2257..2278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2304 AA; 251496 MW; 1574E5FA29F37E74 CRC64;
MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGGE LGLLNSGNLV
PDAASKHKQL SELLRGGSSS SINPGIGNVS ASSPVQQGLG GQAQGQPNSA NMASLGAMGK
SPLNQGDSSA PSLPKQAAST SGPTPPASQA LNPQAQKQVG LVTSSPATSQ TGPGICMNAN
FNQTHPGLLN SNSGHSLMNP AQQGQAQVMN GSLGAAGRGR GAGMPYATPA MQGAASSVLA
ETLTQVSPQM ASHAGLNTAQ AGGMSKMGMT GNTSPFGQPF SQTGGQQMGA PGVNPQLPSK
QSMVNSLPPF AADIKNASVT NVPNMSQMQT SVGIGPTQAI ATGPTADPEK RKLIQQQLVL
LLHAHKCQRR EQANGEVRAC SLPHCRTMKN VLNHMTHCQA GKACQVAHCA SSRQIISHWK
NCTRHDCPVC LPLKNASDKR NQQTILGSPA SGIQNTIGSV GTGQQNATSL SNPNPIDPSS
MQRAYAALGL PYLNQPQTQL QPQVPGQQPA QPQTHQQMRT LNPLGNNPMN IPSGGITTDQ
QPPNLISESA LPTSLGAANP LISDGSNSGN IGTLSTIPTA APPSSTGVRK GWHEHVTQDL
RSHLVHKLVQ AIFPTPDPAA LKDRRMENLV AYAKKVEGDM YESANSRDEY YHLLAEKIYK
IQKELEEKRR SRLHKQGILG NQPALPAPGT QPPGIPQAQP VRPPNGPMPL PVNRMQVSQG
MNSFNPISLG NVQLPQAPMG PRASSPMNHS VPMNSMGSVP GMAISPSRMP QPPNMMGTHA
NNMMAQAPAQ NQFLPQNQFP SSSGALNVNS VGMGQPAAQA SVSQLSQAAA SIDNRVPTPS
SVASAETNSQ QPGPDVPMLE MKAEVKTEDT EPDASEPKAE PGAAMMEEDL QGSSQVKEET
DTTEQKSEPM EVDEKKPEVK VEAKEEEESS TNGTASQSTS PSQPRKKIFK PEELRQALMP
TLEALYRQDP ESLPFRQPVD PQLLGIPDYF DIVKNPMDLS TIKRKLDTGQ YQEPWQYVDD
VWLMFNNAWL YNRKTSRVYK FCSKLAEVFE QEIDPVMQSL GYCCGRKYEF SPQTLCCYGK
QLCTIPRDAA YYSYQNRYHF CEKCFTEIQG ENVTLGDDPS QPQTTISKDQ FEKKKNDTLD
PEPFVDCKEC GRKMHQICVL HYDIIWPSGF VCDNCLKKTG RTRKENKFSA KRLQTTRLGN
HLEDRVNKFL RRQNHPEAGE VFVRVVASSD KTVEVKPGMK SRFVDSGEMS ESFPYRTKAL
FAFEEIDGVD VCFFGMHVQE YGSDCPPPNT RRVYISYLDS IHFFRPRCLR TAVYHEILIG
YLEYVKKLGY VTGHIWACPP SEGDDYIFHC HPPDQKIPKP KRLQEWYKKM LDKAFAERII
HDYKDIFKQA TEDRLTSAKE LPYFEGDFWP NVLEESIKEL EQEEEERKKE ESTAASETPE
GSQGDSKNAK KKNNKKTNKN KSSISRANKK KPSMPNVSND LSQKLYATME KHKEVFFVIH
LHAGPVINTL PPIVDPDPLL SCDLMDGRDA FLTLARDKHW EFSSLRRSKW STLCMLVELH
TQGQDRFVYT CNECKHHVET RWHCTVCEDY DLCINCYNTK SHTHKMVKWG LGLDDEGSSQ
GEPQSKSPQE SRRLSIQRCI QSLVHACQCR NANCSLPSCQ KMKRVVQHTK GCKRKTNGGC
PVCKQLIALC CYHAKHCQEN KCPVPFCLNI KHKLRQQQIQ HRLQQAQLMR RRMATMNTRN
VPQQSLPSPT SAPPGTPTQQ PSPPQTPQPP AQPQPSPVNM SPAGFPSVAR TQPPTTVSTG
KPTNQVPAPP PPAQPPPAAV EAARQIEREA QQQQHLYRVN INNGMPPGRT GMVTPVSQMA
PVGLNVPRPN QVSGPVVPSL PPGQWQQAPI PQQQPMPGMP RPVMSMQAQP AVAGPRMPSV
QPPRSISPGA LQDLLRTLKS PSSPQQQQQV LNILKSNPQL MAAFIKQRTA KYVASQPGLQ
PQPGLQPQPG LQSQPGLHQQ PSLQNLNAMQ AGGPRPGVPP QQPAMGGLNP QGQALNIMNP
GHNPSMASMN PQYREMLRRQ LLQQQQQQQQ QQQQQQQQQG SAGMAGGMAG HSQFQQPQGP
GGYPAAMQQQ RMQQHLPIQG SSMGQMAAQM GQLSQMGQPG LGADSTPNIQ QALQQRILQQ
QQMKQQIGSP GQPNPMSPQQ HMLSGQPQAS HLPGQQMATS LSSQVRSPAP VQSPRPQSQP
PHSSPSPRIQ PQPSPHHVSP QTGSPHPGLA VTMASSIDQG HLGNPEQSAM LPQLNTPNRS
ALSNELSLVG DTTGDTLEKF VEGL
//
