ID A0A3Q3AS16_KRYMA Unreviewed; 2428 AA.
AC A0A3Q3AS16;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, 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|Ensembl:ENSKMAP00000019200.1};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000019200.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000019200.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_017291429.1; XM_017435940.1.
DR STRING; 37003.ENSKMAP00000019200; -.
DR Ensembl; ENSKMAT00000019463.1; ENSKMAP00000019200.1; ENSKMAG00000014238.1.
DR GeneID; 108247643; -.
DR KEGG; kmr:108247643; -.
DR CTD; 567111; -.
DR GeneTree; ENSGT00940000155364; -.
DR OMA; MEYTCNK; -.
DR OrthoDB; 5490807at2759; -.
DR Proteomes; UP000264800; 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:UP000264800};
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 324..410
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 559..638
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 324..410
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..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..1042
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 2052..2074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2214..2273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2286..2419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..678
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..869
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..894
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..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 1841..1890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1898..1936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2286..2333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2342..2376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2384..2415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2428 AA; 265738 MW; 5301A0C6807B9A95 CRC64;
MNPNIMADNL LDAGPPTAKR PKLNSPLSGS DGPDFVSLFD LENDLPDELI PNGDLGMGLS
SNSGPGAGVP GLNSVGADAA AKHKQLSELL QPGSSSLLGG GLNSTNPQQG GTVGSQLSAV
LGKGPLGQGS PNHQSPQGQK GGASTGQGNG GVGIGYNPML NSGQGHGVMG QAGQVMNGAM
GPAGRGRPGP GMQYQGQGMQ GPQVGAGPGV GGSVLAETLT QGGPSMGGQH VLNAQQAGNM
NKMTMSGAPF GQQYGPAGVQ QMGTAGVNAQ QLQNKTPLSN NLPPFPTELK GPGNVPNMSQ
MQQQVASMGM APGVGGVSGG PTADPEKRKL IQQQLVLLLH AHKCQRREQA NGEVRACTLP
HCRTMKNVLN HMTHCQAGKS CQVAHCASSR QIISHWKNCT RHDCPVCLPL KNASDKRNQQ
PMLGSPGTGL QNAINTVGPG QPSATTINSA ASHFDPSSMQ RAYAALGLPY GNQSPAQVQG
QGPAQQNSQG HQQLRNMNSL GTNQMNQMRG GMGTSSSDQT GCHSDSSLPS TLNNQLMPDG
SVVGGMGNLP TATPLSASGI RKAWHEHVTQ DLRTHLVHKL VQAIFPTPDP AALKDRRMEN
LVAYARKVEG DMYESANSRD EYYHFLAEKI YKIQKELEEK RRSRQEKQPG IVGPGGPQQP
VMVQPNPMGP GQPVRPQNGP APMPNIPNQI MNRMQVDQGI NQFNPIAMQN AQMPQAPMGA
RAPSPMSHPP QINMNPVPTM GMSPSRMPQT PGMLGTHTSN VSQPANQGQF LPQGQFPGAA
GGAMNVNMGL GHIMSQAPVA QQTQNSNLPL NALGSQLPSG PPAQPTLRST PPPNVSQQQQ
QQHALMQAQV PPQPSTPSST AGPSSTPTHM PSSIPRPPAA MSTPPDPSQP LTPLQPHSEP
SSQMQQPTSV QAQHPATPLS QAGAGIDNRV PTPGSVAELS SQQALPDMSG IEIKSEVKKE
DDDSNSGKKQ NDVKMEQDDE TKPVLVKKED PDAAEPKQEK METEEKKPEV KAEPKEEEDS
GANSTSSTST AQNRRKIFKP EELRQALMPT LEALYRQDPE SLPFRQPVDP MLLGIPDYFD
IVKNPIDLST IKRKLDTGQY REPWQYVDDV WLMFNNAWLY NRKTSRVYKY CTKLAEVFEA
EIDPVMQSLG YCCGRKYEFS PQTLCCYGKQ LCTISRDSTY YSYQNRYHYC EKCFNEIQGN
SVTLGDDPSQ PPTLISKDQF EKKKNDMLDP EPFVECKDCG RKMHQICVLH YDVIWPSGFI
CDNCVRKSGK TRKENKFSAR RLQSTRLGTY IEDRVNKYLK RQTHPEAGEV FVRVVASSDK
TVDVKSGMKS RFVESGEMVE SFPYRTKALF AFEEIDGVDV CFFGMHVQEY GSECPFPNTR
RVYISYLDSI HFFRPRLLRT AVYHEILIGY LEYVKKLGYV MGHIWACPPS EGDDYIFHCH
PPDQKIPKPK RLVEWYRKML DKAFAERIIH DYKDIFKQAT EDRLTSANEL PYFEGDFWPN
VLEESIKELE QEEEERKKEE NTASSETTEG AQADSKNAKK KNNKKTNKNK SSVSRANKKK
PGMPNVANDL SQKLYATMEK HKEVFFIIHL HAGPVINTLP PIMDPDPLLT CDLMDGRDAF
LTLARDKHWE FSSLRRCKWS TMCMLVELHN QGQDRFVYTC NECKHHVETR WHCTVCEDYD
LCINCYNSKG HEHQMVKWGL GIDDDSNSQG GEASKSPQES RRLSIQRCIQ SLVHACQCRN
ANCALPSCQK MKRVVQHTKG CKRKTNGGCP VCKQLIALCC YHAKHCQENK CPVPFCLNIK
QKLRQQQLQH RVQQAHMMRR RMATMAGRGM PMPSPPTSAA PDTPNSVQQP NTPQTPQPMS
NQPQQQQPPN PASIAQGFLS NGRISQPTTP VPQGKPGPQS SPLHQQLSPM PNMSHQQQPQ
PPQQQPQQQQ QQQQQQQQRL TALKVAQQIE MVAKAKQQQP NYANNGMPLS QVRVMGSMPN
QMQMVQGPRG PQVMQGQWGA GMQNPQGHQS QVPLQQGPMV SQHAQVTPMS QQGQLMQRPM
MPQQHGLQMP SVMPPQGPSQ QSMTPQQQNM PQRMSGNITS SALQELLRTL KSPSSPQQQQ
QVLTILKSNP HLMAAFIKQR TAKYQASQVP QQQQQAQQQN PQAMMGSQAG MQAMAVMANQ
VQRPVMAPQQ QPPQPVGPQG MAPMGPQGQM MNPAQNGNPQ QYHRQQLLRM QQMQQMQQQG
GLPQGHGQFP PQQPGPPNFS QLRAQPQMAM QGGGGPMGQL PPTSQMGQPG MGLEGLQNHV
KQRILQHQMK QQMGSAAQAN SMSPQPHLLQ GQGQGGPHLP GQTIANTLVR SPAPVQSPRP
PSQQAPHSSS SPRIQPQPSP QHGALHSSSP HPSLGPMSGS MEQGHMGTPE QSAMLPQLNT
PNRGGLNNDM SMVGDTTGDT LEKFVEGL
//
