ID G1SLV2_RABIT Unreviewed; 2403 AA.
AC G1SLV2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 83.
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:ENSOCUP00000003854.4};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000003854.4, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000003854.4, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000003854.4}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000003854.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR SMR; G1SLV2; -.
DR STRING; 9986.ENSOCUP00000003854; -.
DR PaxDb; 9986-ENSOCUP00000003854; -.
DR Ensembl; ENSOCUT00000004463.4; ENSOCUP00000003854.4; ENSOCUG00000004458.4.
DR eggNOG; KOG1778; Eukaryota.
DR GeneTree; ENSGT00940000155364; -.
DR HOGENOM; CLU_000162_2_0_1; -.
DR InParanoid; G1SLV2; -.
DR TreeFam; TF101097; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000004458; Expressed in uterus and 16 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000123; C:histone acetyltransferase complex; IEA:InterPro.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
DR GO; GO:0043993; F:histone H3K18 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0044017; F:histone H3K27 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0043426; F:MRF binding; IEA:Ensembl.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031669; P:cellular response to nutrient levels; IEA:Ensembl.
DR GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
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:UP000001811};
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 323..409
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT DOMAIN 562..641
FT /note="KIX"
FT /evidence="ECO:0000259|PROSITE:PS50952"
FT DOMAIN 1081..1153
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 1301..1678
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51727"
FT DOMAIN 1680..1728
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 1743..1824
FT /note="TAZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50134"
FT ZN_FING 323..409
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT ZN_FING 1743..1824
FT /note="TAZ-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00203"
FT REGION 50..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1534..1592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1852..1936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1955..2011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2168..2226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2255..2290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2302..2389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..865
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1043
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1534..1549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1580
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1861..1894
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1899..1917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1996..2011
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2168..2187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2312..2339
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2356..2389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2403 AA; 260064 MW; 62713B243C2E993C CRC64;
MLKSNFGSLF DLENDLPDEL IPNGGELGLL NSGNLVPDAA SKHKQLSELL RGGSGSSINP
GIGNVSASSP VQQGLGGQAQ GQPNSTNMAS LGAMGKSPLN QGDSNASSLP KQAASTSGPT
PPASQALNPQ AQKQVGLVTS SPATSQTGPG ICMSANFNQT HPGLLNSNSG HSLMNQAQQG
QAQVMNGSLG AAGRGRGAGM PYPAPAMQGA TSSVLAETLT QVSPQMAGHA GLNPAQAGGM
PKMGMTGNTS PFGQPFSQTG GQQMGGAGVN PQLSSKQSMV NSLPTFPTDI KNTSVTNVPN
MSQMQTSVGI VPTQAIATGP TADPEKRKLI QQQLVLLLHA HKCQRREQAN GEVRACSLPH
CRTMKNVLNH MTHCQAGKAC QVAHCASSRQ IISHWKNCTR HDCPVCLPLK NASDKRNQQT
ILGSPASGIQ NTIGSVGTGQ QNATSLSNPN PIDPSSMQRA YAALGLPYMN QPQTQLQPQA
PGQQPAQPPT HQQMRTLTPL GNNPMNIPAG GMTADQQPPN LISESALPAS LGATNPLMND
GSSSNIGTLS TIPAAAPPSS TGVRKGWHEH VTQDLRSHLV HKLVQAIFPT PDPAALKDRR
MENLVAYAKK VEGDMYESAN SRDEYYHLLA EKIYKIQKEL EEKRRSRLHK QGILGNQPAL
PAPGAQPPGM PPTQPVRPPN GPLSLPVTRM QVSQGMNSFN PMSLGNVQLP QAPMGPRAAS
PMNHSVQMNS MGSVPGMAIS PSRMPQPPNM MGAHANNMMA QTPTQNQFLA QNQFPSSSGA
MSVNSVSMGQ PTAQAGVAQG QVPGAALPNP LNMLGPQTSQ LPCPPVTQSP LHPTPPPASA
AAGLPSLQHP PPPGMTPPQP AAPAQPSTPV SSSGQTPTPT PGSVPSAAQA QSTPTVQAAS
QAQVTPQPQT PVQPPSVATP QSSQQQPTPV HVQPPSTPLS QAAASIDNRV PTPSSVASAE
TSSQQPGPDV PVLEMKAEVQ AEDAEPDPGE PKGEPRSEVM EEDLQGSSQI KEETDSTEQK
PEPMEVDEKK PEVKVEAKEE EESSTNGTAS QSTSPSQPRK KIFKPEELRQ ALMPTLEALY
RQDPESLPFR QPVDPQLLGI PDYFDIVKNP MDLSTIKRKL DTGQYQEPWQ YVDDVWLMFN
NAWLYNRKTS RVYKFCSKLA EVFEQEIDPV MQSLGYCCGR KYEFSPQTLC CYGKQLCTIP
RDAAYYSYQN RYHFCEKCFT EIQGENVTLG DDPSQPQTTI SKDQFEKKKN DTLDPEPFVD
CKECGRKMHQ ICVLHYDIIW PSGFVCDNCL KKTGRPRKEN KFSAKRLQTT RLGNHLEDRV
NKFLRRQNHP EAGEVFVRVV ASSDKTVEVK PGMKSRFVDS GEMSESFPYR TKALFAFEEI
DGVDVCFFGM HVQEYGSDCP PPNTRRVYIS YLDSIHFFRP RCLRTAVYHE ILIGYLEYVK
KLGYVTGHIW ACPPSEGDDY IFHCHPPDQK IPKPKRLQEW YKKMLDKAFA ERIIHDYKDI
LKQATEDRLT SAKELPYFEG DFWPNVLEES IKELEQEEEE RKKEESTAAS ETTEGSQGDS
KNAKKKNNKK TNKNKSSISR ANKKKPSVPS VSNDLSQKLY ATMEKHKEVF FVIHLHAGPV
INTLPPIVDP DPLLSCDLMD GRDAFLTLAR DKHWEFSSLR RSKWSTLCML VELHTQGQDR
FVYTCNECKH HVETRWHCTV CEDYDLCINC YNTKSHTHKM VKWGLGLDDE GSSQGEPQSK
SPQESRRLSI QRCIQSLVHA CQCRNANCSL PSCQKMKRVV QHTKGCKRKT NGGCPVCKQL
IALCCYHAKH CQENKCPVPF CLNIKHKLRQ QQIQHRLQQA QLMRRRMATM NTRNVPQQSL
PSPTSAPPGT PTQQPGTPQT PQPPAQPQPS PVSMSPAGFP SVARTQPPTT VSAGKPTNQV
PAAPPPAQPP PAAVEAARQI EREAQQQQHL YRVNINSGMP PGRTGLGTPG SQMAPVGLNV
PRPSQVSGPG MPGMPPGQWQ QAPLPPQQPM PGMPRPVMSM QAQAAVAGPR MPSVPPPRSI
SPSALQDLLR TLKSPSSPQQ QQQVLNILKS NPQLMAAFIK QRTAKYVANQ PGLQPQPGLQ
AQPGMHQQPG LQNLNAMQAG VPRPGVPPQQ QAMGGLNAPG QALNIMNPGH SPSVASMNPQ
YREMLRRQLL QQQQQQQQQQ QQQQGGGGVA GGVAGGMAGH GQFQQPQGPG GYAPAMQHGS
SMGQMAAQMG QLGQMGQPGL GADGTPSIQQ ALQQRILQQQ QMKQQMGSPG QPNPMSPQQH
LLSGQPQASH LPGQQIATSL SNQVRSPAPV QSPRPQSQPP HSSPSPRIQP QPSPHHVSPQ
TGSPHPGLAV TMASSIDQGH LGNPEQSAML PQLNTPSRST LSSELSLVGD TTGDTLEKFV
EGL
//
