ID A0A1S3S4K4_SALSA Unreviewed; 2712 AA.
AC A0A1S3S4K4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=LOC106607167 {ECO:0000313|RefSeq:XP_014059288.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014059288.1};
RN [1] {ECO:0000313|RefSeq:XP_014059288.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014059288.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_014059288.1; XM_014203813.1.
DR GeneID; 106607167; -.
DR CTD; 565612; -.
DR OrthoDB; 5490807at2759; -.
DR Proteomes; UP000087266; Chromosome ssa06.
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; 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; 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; 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:UP000087266};
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 554..636
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1108..1191
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1349..1729
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1731..1779
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1794..1875
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 1794..1875
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1582..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1888..2080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2093..2226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2307..2336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2359..2409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2443..2482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2498..2546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2558..2712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..888
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1920..1934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1935..1955
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1960..2022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2047..2080
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2151..2165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2168..2182
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2183..2212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2498..2513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2558..2604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2605..2626
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2627..2680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2696..2712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2712 AA; 292022 MW; D4F038DEA0400AC0 CRC64;
MADNVLESGP PSAKRPKLSS PALSVSASDG NDFGSLFDLE HDLPDELINS SELGLVNGGD
LSQLHTSLGG GMGGGQDAAA KHKQLSELLR AGALPPSSQQ GATNSPGGSM GLLGSMNASP
GPQSMAPQGQ HPSPQQAGMM QQAGMVGGLN RAMMGAQKGN GQQQGSTPQG MMGGQVMNGS
PRMGYQVNPG MGSNSNLLAE TLQQQGGQQM GSGGQAGMRP QQPGALNKMN MMANAGPYGG
PYGQSAGQGL GGAGLGPQHQ NKAGLANSLA QFNLDKKTPP IQGMAGMASQ QASAVGPVSV
VGGGAQAGLG TVATGPGAAP PTADPEKRKL IQQQLVLLLH AHKCQRREQA NGEVRQCSLP
HCRTMKNVLN HMTHCQAGKS CQVAHCASSR QIISHWKNCT RHDCPVCLPL KNAGDKRNQQ
SLLSSAGVGL GNSLGAVPGG QPSTPNLTPP SQIDPSSIER AYAALGLTYQ GNQMPQQPPQ
SNLPNQPGMR SLNAMGGNPM GMNGGVGVQP PNQSNLLPDT MLHNNMNVQS LMNDGSGVGS
LGAMPMATPP SAAGMRKNWH EDITQDLRNH LVHKLVSSVQ AIFPTPDPAA LKDRRMENLV
AYARKVEGDM YESANSRAEY YHLLAEKIYK IQKELEEKRR TRLQKQGMMP TQPGMPPSGL
PQGPLGMGQS PLAPGQPSNG SHADPSMIRP TGPNQMVNRM QNPAGMNQFG QMGMQSLGQR
STPPLPLGGP LNQMGMGPTR MGQPNVAQLQ NQYLPPGQFP GSSPGLGAGA VGMNHPGLQG
GVTQQAQMPT PPSLPVSSPA AQPGSVAGSG PSQGSMGPGS VGGGPPSNLQ LPNSNSSQPN
SHPHCPPIRQ NSPSPARSLT PTPHQTPPGQ PGSQTPQPHT PNPPQVAAPL PQLASSQPMG
QGMNSEKPSQ LQQQTNGGGA SGGLPTGQAQ SVPTQNAHVP TQLPQTPLSQ KSSLTADGQA
STPASVSSVD PSSQLTSSDA PAPAEPKMEV KQQDDEDAED QGEGKASGKM GKGQADIKSE
EKPEIKKEKP SGDGCKGEPM DTSSSAATPK MEDRDRKPEV KTEPKDEEER SGASGTHSSP
ASAQNKRKIF KPEELRQALM PTLEALYRQD PESLPFRQPV DPQLLGIPVR IRTSNKTNLD
YFDIVKNPID LSTIKRKLDT GQYQEPWQYV DDIWLMFNNA WLYNRKTSRV YKYCSKLAEV
FEAEIDPVMQ GLGYCCGRKL EFSPQTLCCY GKQLCTIPRD AAYFSYQNSS PQFGLLADRY
HFCEKCFNEI QGECVSLGDD PSQPQTSISK DQFQRKKNDT LDPEWLVECT DCGRKMHQIC
VLHNDTIWPA GFVCDSCLKK ANKTRKENKY AARRLPQTKL GSFLEGRVND YLRRQNHPES
GDVTIRVVHV SDKVVEVKPG MKSRFVDTGE MSESFPYRTK ALFAFEDIDG ADVCFFGMHV
QEYGSDSPPP NQRRVYISYL DSVHFFQPRH LRTGVYHEIL IGYLEYVKKL GFTTGHIWAC
PPSEGDDYIF HCHPVDQKIP KPKRLQEWYK KMLDKAVAER IVHDYKDVFK QATEDRLTSA
NELPYFEGDF WPNVLEESIK ELEQEEEERK REENSTSSES VDVSAPKSDS KNAKKKNSKK
TSKNKNSSLI RANKKKPGMP SVSNDLSQKL YACMEKHKEV FFVIRLIAGP TANSLPPITD
PDPLMACDLM DGRDAFLTLA RDKHLEFSSL RRAKWSSMCM LVELHNQSQD RFVYTCNECK
ASVETRFHCT VCEDYDLCIT CYNTKGHEHK MEKLGLGLDD ESNNAAAAAT QSPGDSRRLS
IQRCIQSLVH ACQCRNANCS LPSCQKMKRV VQHTKGCKRK TNGGCPICKQ LIALCCYHAK
HCQENKCPVP FCLNIKHKLR QQQLQHRLQQ AQMLRRRMAS MQRVGQPACG GGGPPGGLPS
PGNNGTTAPS TPTSGGTQPP TPQTPTQPNI PPGPQPGMGG GGTLQQQQGG MPQQHHQLHH
QFQQMPGGGM MNSPQQQQMV PQVQQQSQAS NPQQLQQHPN SLPPYTNRPP GSSPHPQSQG
KPGLGPATPP QQQPPQQQPN PGQPSMPQQQ QQPPSGPPPA AVEIAMKIQQ VADAQRKMAL
QRQAAQAAGM MPPHPHHQQP QGQMGMAHPG VGMVGAQGLP PHAQAAQAAA RAHMEQQQQQ
QQGPPGMMVG PGPSPMQQQP NPQGQLPPQV QQQRVGPPLQ NPQQQWAGQG MPPQQRQAMM
GHPGMVAPQQ QQPQQMQQRQ QAQGPGGLIG MVQQGGAAGG GNLPQAALQE LLRTLRSPSS
PEQQQQVLNI LRSNPQLMAA FIKQRASKYK GGPGPPGAPG GPGPGRVPGG MGGQQVNVNA
VASQPGMHMG QGVNMPTMTQ LQQVQQQQQP QQQRPMLSSL QQQQVAALQQ HQQQQHQQGG
MPGQQAPNMA NINPQFRELL MRRHLQLQQQ QQQIGNHTQF QQQGYMGQPG MAPQQPGQGQ
SGLQQQPGAQ PGQQQQGYPS TVAQQQAAAV LQQRLQHQHQ LQMQQQQHQN AMVGHQGAEG
GPGTGVGGPP QQPPQGTPQP QSSQALLQQA LHQRLLQQQQ HLGGGSPAQH SSPMSPQQQM
AQSPHLQGQT LSTSLSNQVR SPQPSPRPQS QPSHSSPSPR MQPQPSPHHI SPQTQTGSPH
PGQLTQHHPG MVVPSQQPPQ QQNSMDQFGP DQNAMLSQLS GMSGLHGPGG PDMLSGNSQD
LGQNINHNTL DM
//
