ID A0A1S3R8T6_SALSA Unreviewed; 2182 AA.
AC A0A1S3R8T6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=LOC106601244 {ECO:0000313|RefSeq:XP_014048770.1};
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_014048770.1};
RN [1] {ECO:0000313|RefSeq:XP_014048770.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014048770.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_014048770.1; XM_014193295.1.
DR GeneID; 106601244; -.
DR OrthoDB; 5490807at2759; -.
DR Proteomes; UP000087266; Chromosome ssa03.
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; 1.
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; 1.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 1.
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; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS50952; KIX; 1.
DR PROSITE; PS50134; ZF_TAZ; 1.
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 23..105
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 576..659
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 817..1197
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1199..1247
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1262..1343
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 1262..1343
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1772..1802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1837..1875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1912..2015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2028..2182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..354
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1403..1423
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1515..1530
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1692..1709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1912..1982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2028..2074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2075..2096
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2097..2112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2123..2149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2166..2182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2182 AA; 238269 MW; 09D2604819BFD978 CRC64;
MNDGSGVGSL GSMPMATPPS AAGMRKNWHE DITQDLRNHL VHKLVSSVQA IFPTPDPAAL
KDRRMENLVA YARKVEGDMY ESANSRAEYY HLLAEKIYKI QKELEEKRRT RLQKQGMMPT
QPDMPPSGLP QGTLSMGQSP LAPGPPSNGS HADPSMVRPT GPNQMVNRMQ NPAGINQFGQ
MGMQSLGQRS TPPLPLGGPL NQMGMGPTRM GQPNVAQLQN QYLPPGQFPG SSPGLGAGPV
GMNHPGPQGG VVQQAQMPTP PSLPVSSPAA QPGSVAGSGH SQGSMGPGSV GGPPSNLQLP
NSSQANSHPH CPPIRQNSPS PARSLTPTPH HTPPGLPGSQ TPQPHTPNPP QVAAPLPQQQ
LASSQPMGQG MNSEKPSQLQ QQTNGGGASG ALQTGQAQPV PTQNAHVPTQ LPRTPLSQKS
SLTADGQAST PASVSSVDPS SQLTSSDAPA PAEPKMEVKQ QDDEDAEDQG EGKASGKMGK
GQADIKSEEK PEIKKEKPSG DGCKGEPMDT SSSAATPKME DRDRKPEVKT EPKDEEERSG
ALGTHNSPAS AQNKRKIFKP EELRQALMPT LEALYRQDPE SLPFRQPVDP QLLGIPVRIR
TSNKTNLDYF DIVKNPIDLS TIKRKLDTGQ YQEPWQYVDD IWLMFNNAWL YNRKTSRVYK
YCSKLAEVFE AEIDPVMQGL GYCCGRKLEF SPQTLCCYGK QLCTIPRDAA YFSYQNSSPQ
FGLLADRYHF CEKCFNEIQG ECVSLGDDPS QPQTSISKDQ FQRKKNDTLD PEWLVECTDC
GRKMHQICVL HNDTIWPAGF VCDSCLKKAN KTRKENKYAA RRLPQTKLGS FLEGRVNDYL
RRQNHPESGD VTIRVVHVSD KVVEVKPGMK SRFVDTGEMS ESFPYRTKAL FAFEDIDGAD
VCFFGMHVQE YGSDSPPPNQ RRVYISYLDS VHFFQPRHLR TGVYHEILIG YLEYVKKLGF
TTGHIWACPP SEGDDYIFHC HPVDQKIPKP KRLQEWYKKM LDKAVAERIV HDYKDVFKQA
TEDRLTSANE LPYFEGDFWP NVLEESIKEL EQEEEERKRE ENSTSCESVD VSAPKSDSKN
AKKKNSKKTS KNKNSSLIRA NKKKPGMPNV SNDLSQKLYA CMEKHKEVFF VIRLIAGPTA
NSLPPITDPD PLMACDLMDG RDAFLTLARD KHLEFSSLRR AKWSSMCMLV ELHNQSQDRF
VYTCNECKAS VETRFHCTVC EDYDLCITCY NTKGHEHKME KLGLGLDDES NNAAAAATQS
PGDSRRLSIQ RCIQSLVHAC QCRNANCSLP SCQKMKRVVQ HTKGCKRKTN GGCPICKQLI
ALCCYHAKHC QENKCPVPFC LNIKHKLRQQ QLQHRLQQAQ MLRRRMASMQ RVGQPACGGG
GPPGGLPSPG NNGTTAPSTP TSGGTQPPTP QTPTQPNMPP GPQPGMGGGG TLQQQQGGMP
QQHHQLHHQF QQMPGGGMIN SPQQQQMVPQ VQQQSQASNP QQLQQHPNSL PPYTNRPPGS
SPHPQSQGKP GLGPATPPQQ QPPQQQPNPG QPSMPQQQQQ QPPSGPPPAA VEIAMKIQQV
ADAQRKMSLQ RQAAQAAGMM PPHPHHQQPQ GQMGMAHPGV GMVGAQGLPP QAQAAARAHM
EQQQQQQQQG PPGMMVGPGP MQQQPNPQSQ LPPQVQQQRV GPPLQNPQQQ WAGQGMPPQQ
RQAMMGHPGM VAPQQQQPQQ MQQRQQAQGP GGLIGMVQQG GAAGGGNLPQ AALQELLRTL
RSPSSPEQQQ QVLNILRSNP QLMAAFIKQR ASKYKGGPGP PGAPGGPGPG RVSGGMGGQQ
VNVNAVAGQP GMHMGQGVNM PTMTQLQQVQ QLQQQQQQQQ PQQQRPMLSS LQQQQVAALQ
QHQQGGMPGQ QAPNMANINP QFRELLMRRH LQLQQQQQQQ QIGNHAQFQQ QGYMGQPGMA
PQQPGQGQSG LQQQPGAQPG QQQQGYPSTV AQQQAAAVLQ QRLQHQHQLQ MQQQQHQNAM
SGHQGAEGGP GTGVGGPPQQ PQPPQGAPQP QSSQALLQQA LHQRLLQQQQ HLGGGSPAQH
SSPMSPQQQM AQSPHLQGQT LSTSLSNQVR SPQPSPRPQS QPPHSSPSPR MQPQPSPHHI
SPQTQTGSPH PGQLPQHHPG MVVPSQQPPQ QQNSMDHFGS DQNAMLSQLS GMGGLHGPGG
PDMLSGNSQD LGQNINHNTL DM
//
