ID A0A452SHB6_URSAM Unreviewed; 2184 AA.
AC A0A452SHB6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=EP300 {ECO:0000313|Ensembl:ENSUAMP00000031897.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000031897.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000031897.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR Ensembl; ENSUAMT00000035566.1; ENSUAMP00000031897.1; ENSUAMG00000023761.1.
DR GeneTree; ENSGT00940000155497; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
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; cd15646; PHD_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: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; 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:UP000291022};
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 315..401
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 539..618
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 828..900
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1048..1424
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1426..1474
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1489..1570
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 315..401
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1489..1570
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 73..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1585..1692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1721..1779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1857..2020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2032..2184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..717
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..777
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..794
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1326
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1649
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1672..1687
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1750..1767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1921..1939
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 1979..1994
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1995..2012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2032..2080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2081..2112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2132..2151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2168..2184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2184 AA; 239575 MW; AD9BEE6A4508B241 CRC64;
LILQCTGQSP LPLQQRLFNF GSLFDLEHDL PDELINSTEL GLTNGGDISQ LQTSLGIVQD
AASKHKQLSE LLRSGSSPNL NMGVGGPGQG MASQPQQNSP GLGLINSMVK SPMAQAGLTS
PNMGMGTSGP NQGPTPSAAG MMNSPVNQPA MGMNTGMNAG MNPGMLNAGN GQGMMPNQVM
NGSIGAGRGR PNMQYPNPGM GNAGNLMTEP LQQGSPQMGG QTGLRGPQPL KMGMMNNPNP
YGSPYTQNSG QQIGAGGLGL QIQTKSVLPN NLSPFAMDKK AVPGGGMPNM APQVQQPGLV
TPVAQGMGSG AHTADPEKRK LIQQQLVLLL HAHKCQRREQ ANGEVRQCNL PHCRTMKNVL
NHMTHCQSGK SCQVAHCASS RQIISHWKNC TRHDCPVCLP LKNAGDKRNQ QFALYLKSXG
QQSTPSLSTV SQIDPSSIER AYAALGLPYQ VNQMPTQPQV QAKNQQNQQS GQSPQGMRPM
SNMSNPMGVN GGVGVQTSNL LSDSMLHSAI NSQNPMMSEN ASVASLGPMP TAAQPSNTGI
RKQWHEDITQ DLRNHLVHKL VQAIFPTPDP AALKDRRMEN LVAYARKVEG DMYESANNRA
EYYHLLAEKI YKIQKELEEK RRTRLQKQNM LPSAAGMVPV SMNPGPNMGQ PQPGMTSSKC
FLLQLLRGEI VNSPIMPPGS QGSHIHCPPL PQSALHQNSP SPVPSRTPTP HHTPPSIGAQ
QPPATAIPAP VPTPPAMPPG PQTQALHPPP RQTPTPPPTQ LPPQVQPSLP AAPSADQPPQ
QPLSQQSTAA SVPTPTAPLL PPQPATPVIF KPEELRQALM PTLEALYRQD PESLPFRQPV
DPQLLGIPDY FDIVKSPMDL STIKRKLDTG QYQEPWQYVD DIWLMFNNAW LYNRKTSRVY
KYCSKLSEVF EQEIDPVMQS LGYCCGRKLE FSPQTLCCYG KQLCTIPRDA TYYSYQNRYH
FCEKCFNEIQ GESVSLGDDP SQPQTTINKE QFSKRKNDTL DPELFVECTE CGRKMHQICV
LHHEIIWPSG FVCDGCLKKS ARTRKENKFS AKRLPSTRLG TFLENRVNDF LRRQNHPESG
EVTVRVVHAS DKTVEVKPGM KARFVDSGEM AESFPYRTKA LFAFEEIDGV DLCFFGMHVQ
EYGSDCPPPN QRRVYISYLD SVHFFRPKCL RTAVYHEILI GYLEYVKKLG YTTGHIWACP
PSEGDDYIFH CHPPDQKIPK PKRLQEWYKK MLDKAVSERI VHDYKDIFKQ ATEDRLTSAK
ELPYFEGDFW PNVLEESIKE LEQEEEERKR EENTSNESTD VTKGDSKNAK KKNNKKTSKN
KSSLSRGNKK KPGMPNVSND LSQKLYATME KHKEVFFVIR LIAGPAANSL PPIVDPDPLI
PCDLMDGRDA FLTLARDKHL EFSSLRRAQW STMCMLVELH TQSQDRFVYT CNECKHHVET
RWHCTVCEDY DLCITCYNTK NHDHKMEKLG LGLDDESNSQ QAAATQSPGD SRRLSIQRCI
QSLVHACQCR NANCSLPSCQ KMKRVVQHTK GCKRKTNGGC PICKQLIALC CYHAKHCQEN
KCPVPFCLNI KQKLRQQQLQ HRLQQAQMLR RRMASMQRTG VVGQQQGLPS PTPATPTTPT
GQQPATPQTP QPQPPSQPQP TPPNSMPPYL PRTQAAGPVS QGKAAGQVTP PTPPQTAQPP
LPGPPPAAVE MAMQIQRAAE TQRQMAHVQI FQRPIQHQMP QMTPMAPMGM NPPPMTRGPS
GHLEPGMGPT GMQQQPQWVQ GGLPQPQQLQ PGMPRPAMMS VAQHGQPLNI APQPGLGQVG
VSPLKPGTVS QQALQNLLRT LRSPSSPLQQ QQVLSILHAN PQLLAAFIKQ RAAKYASSNP
QPLAGQPGMP QGQPGLQPPA MPGQQGVHSS PAMPNMSPMQ AGVQRAGLPQ QQPQQPLQPP
MGGMSPQAQQ MNMNHNAMPS QFRDILRRQQ MMQQQQQQGA GPGIGPGMAN HNQFQQPQGV
GYPPPPPPPP QPQQQRMQHH LQQMQPGSMG QMGQLPQALG AEAGAGLQAY QQRLLQQQMG
SPAQPNPMSP QQHMLPSQAQ SPHLQGQQIP SSLSNQVRSP QPVPSPRPQS QPPHSSPSPR
MQPQPSPHHV SPQTSSPHPG LVAAQANPME QGHFASPDQS SMLSQLASNP GMANLHGAGA
TDLGLGPDNA DLNSNLSQST LDIH
//
