LOCUS       NP_001020603            2441 aa            linear   ROD 08-APR-2025
DEFINITION  histone lysine acetyltransferase CREBBP [Mus musculus].
ACCESSION   NP_001020603 XP_148699 XP_622591
VERSION     NP_001020603.1
DBSOURCE    REFSEQ: accession NM_001025432.1
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 2441)
  AUTHORS   Gamu,D., Cameron,M.S. and Gibson,W.T.
  TITLE     Maintenance of thermogenic adipose tissues despite loss of the
            H3K27 acetyltransferases p300 or CBP
  JOURNAL   Am J Physiol Endocrinol Metab 327 (4), E459-E468 (2024)
   PUBMED   39140972
REFERENCE   2  (residues 1 to 2441)
  AUTHORS   Li,J., Chin,C.R., Ying,H.Y., Meydan,C., Teater,M.R., Xia,M.,
            Farinha,P., Takata,K., Chu,C.S., Jiang,Y., Eagles,J., Passerini,V.,
            Tang,Z., Rivas,M.A., Weigert,O., Pugh,T.J., Chadburn,A., Steidl,C.,
            Scott,D.W., Roeder,R.G., Mason,C.E., Zappasodi,R., Beguelin,W. and
            Melnick,A.M.
  TITLE     Loss of CREBBP and KMT2D cooperate to accelerate lymphomagenesis
            and shape the lymphoma immune microenvironment
  JOURNAL   Nat Commun 15 (1), 2879 (2024)
   PUBMED   38570506
  REMARK    GeneRIF: Loss of CREBBP and KMT2D cooperate to accelerate
            lymphomagenesis and shape the lymphoma immune microenvironment.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2441)
  AUTHORS   Zhang,L., Zhu,K., Xu,J., Chen,X., Sheng,C., Zhang,D., Yang,Y.,
            Sun,L., Zhao,H., Wang,X., Tao,B., Zhou,L. and Liu,J.
  TITLE     Acetyltransferases CBP/p300 Control Transcriptional Switch of
            beta-Catenin and Stat1 Promoting Osteoblast Differentiation
  JOURNAL   J Bone Miner Res 38 (12), 1885-1899 (2023)
   PUBMED   37850815
  REMARK    GeneRIF: Acetyltransferases CBP/p300 Control Transcriptional Switch
            of beta-Catenin and Stat1 Promoting Osteoblast Differentiation.
REFERENCE   4  (residues 1 to 2441)
  AUTHORS   Louphrasitthiphol,P., Loffreda,A., Pogenberg,V., Picaud,S.,
            Schepsky,A., Friedrichsen,H., Zeng,Z., Lashgari,A., Thomas,B.,
            Patton,E.E., Wilmanns,M., Filippakopoulos,P., Lambert,J.P.,
            Steingrimsson,E., Mazza,D. and Goding,C.R.
  TITLE     Acetylation reprograms MITF target selectivity and residence time
  JOURNAL   Nat Commun 14 (1), 6051 (2023)
   PUBMED   37770430
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2441)
  AUTHORS   Tseng,C., Han,Y., Lv,Z., Song,Q., Wang,K., Shen,H. and Chen,Z.
  TITLE     Glucose-stimulated PGC-1alpha couples with CBP and Runx2 to mediate
            intervertebral disc degeneration through transactivation of
            ADAMTS4/5 in diet-induced obesity mice
  JOURNAL   Bone 167, 116617 (2023)
   PUBMED   36403758
  REMARK    GeneRIF: Glucose-stimulated PGC-1alpha couples with CBP and Runx2
            to mediate intervertebral disc degeneration through transactivation
            of ADAMTS4/5 in diet-induced obesity mice.
REFERENCE   6  (residues 1 to 2441)
  AUTHORS   Parker,D., Ferreri,K., Nakajima,T., LaMorte,V.J., Evans,R.,
            Koerber,S.C., Hoeger,C. and Montminy,M.R.
  TITLE     Phosphorylation of CREB at Ser-133 induces complex formation with
            CREB-binding protein via a direct mechanism
  JOURNAL   Mol Cell Biol 16 (2), 694-703 (1996)
   PUBMED   8552098
REFERENCE   7  (residues 1 to 2441)
  AUTHORS   Chen,X.N. and Korenberg,J.R.
  TITLE     Localization of human CREBBP (CREB binding protein) to 16p13.3 by
            fluorescence in situ hybridization
  JOURNAL   Cytogenet Cell Genet 71 (1), 56-57 (1995)
   PUBMED   7606928
REFERENCE   8  (residues 1 to 2441)
  AUTHORS   Kwok,R.P., Lundblad,J.R., Chrivia,J.C., Richards,J.P.,
            Bachinger,H.P., Brennan,R.G., Roberts,S.G., Green,M.R. and
            Goodman,R.H.
  TITLE     Nuclear protein CBP is a coactivator for the transcription factor
            CREB
  JOURNAL   Nature 370 (6486), 223-226 (1994)
   PUBMED   7913207
REFERENCE   9  (residues 1 to 2441)
  AUTHORS   Chrivia,J.C., Kwok,R.P., Lamb,N., Hagiwara,M., Montminy,M.R. and
            Goodman,R.H.
  TITLE     Phosphorylated CREB binds specifically to the nuclear protein CBP
  JOURNAL   Nature 365 (6449), 855-859 (1993)
   PUBMED   8413673
REFERENCE   10 (residues 1 to 2441)
  AUTHORS   Kozak,L.P., Britton,J.H., Kozak,U.C. and Wells,J.M.
  TITLE     The mitochondrial uncoupling protein gene. Correlation of exon
            structure to transmembrane domains
  JOURNAL   J Biol Chem 263 (25), 12274-12277 (1988)
   PUBMED   3410843
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC010297.1, BC072594.1, BU705617.1 and CAAA01026247.1.
            
            On or before Jul 20, 2005 this sequence version replaced
            XP_148699.5, XP_622591.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            RNAseq introns :: mixed sample support SAMN00849374, SAMN00849375
                              [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2441
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="16"
                     /map="16 2.4 cM"
     Protein         1..2441
                     /product="histone lysine acetyltransferase CREBBP"
                     /EC_number="2.3.1.48"
                     /note="protein-lysine acetyltransferase CREBBP; protein
                     lactyltransferas CREBBP"
                     /calculated_mol_wt=265438
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P45481.3)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Region          73..168
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P45481.3)"
     Site            120
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            219
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Region          226..409
                     /region_name="Interaction with SRCAP.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (P45481.3)"
     Region          261..292
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P45481.3)"
     Region          362..429
                     /region_name="zf-TAZ"
                     /note="TAZ zinc finger; pfam02135"
                     /db_xref="CDD:460457"
     Region          586..666
                     /region_name="KIX"
                     /note="KIX domain; pfam02172"
                     /db_xref="CDD:366953"
     Site            600
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000305|PubMed:11701890; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            624
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000305|PubMed:11701890; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            656
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Region          <687..1037
                     /region_name="PHA03247"
                     /note="large tegument protein UL36; Provisional"
                     /db_xref="CDD:223021"
     Region          792..1088
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P45481.3)"
     Region          942..>1194
                     /region_name="COG5076"
                     /note="Transcription factor involved in chromatin
                     remodeling, contains bromodomain [Chromatin structure and
                     dynamics / Transcription]"
                     /db_xref="CDD:227408"
     Site            1015
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            1031
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            1077
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Region          1088..1195
                     /region_name="Bromo_cbp_like"
                     /note="Bromodomain, cbp_like subfamily. Cbp (CREB binding
                     protein or CREBBP) is an acetyltransferase acting on
                     histone, which gives a specific tag for transcriptional
                     activation and also acetylates non-histone proteins.
                     CREBBP binds specifically to...; cd05495"
                     /db_xref="CDD:99927"
     Site            order(1116,1123,1126,1165,1169,1175)
                     /site_type="active"
                     /note="acetyllysine binding site [active]"
                     /db_xref="CDD:99927"
     Region          1125..1171
                     /region_name="Interaction with histone.
                     /evidence=ECO:0000250|UniProtKB:Q92793"
                     /note="propagated from UniProtKB/Swiss-Prot (P45481.3)"
     Region          1163..1181
                     /region_name="Interaction with ASF1A.
                     /evidence=ECO:0000250|UniProtKB:Q92793"
                     /note="propagated from UniProtKB/Swiss-Prot (P45481.3)"
     Region          1207..1279
                     /region_name="RING_CBP-p300"
                     /note="atypical RING domain found in CREB-binding protein
                     and p300 histone acetyltransferases; cd15802"
                     /db_xref="CDD:276805"
     Site            order(1207,1210..1211,1277,1279)
                     /site_type="other"
                     /note="HAT interface [polypeptide binding]"
                     /db_xref="CDD:276805"
     Site            1217
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Region          1281..1312
                     /region_name="PHD_CBP_p300"
                     /note="PHD finger found in CREB-binding protein (CBP) and
                     histone acetyltransferase p300; cd15557"
                     /db_xref="CDD:277032"
     Site            order(1281..1284,1288,1307)
                     /site_type="other"
                     /note="putative histone H3 binding site [polypeptide
                     binding]"
                     /db_xref="CDD:277032"
     Region          1343..1650
                     /region_name="HAT_KAT11"
                     /note="Histone acetylation protein; pfam08214"
                     /db_xref="CDD:400497"
     Site            1383
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKA.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            1387
                     /site_type="phosphorylation"
                     /note="Phosphoserine, by IKKA.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Region          1434..1436
                     /region_name="Interaction with histone.
                     /evidence=ECO:0000250|UniProtKB:Q09472"
                     /note="propagated from UniProtKB/Swiss-Prot (P45481.3)"
     Region          1557..1616
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P45481.3)"
     Site            1584
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            1592
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            1593
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            1596
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            1598
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Region          1706..1746
                     /region_name="ZZ_CBP"
                     /note="Zinc finger, ZZ type. Zinc finger present in
                     CBP/p300 and related proteins. The ZZ motif coordinates
                     two zinc ions and most likely participates in ligand
                     binding or molecular scaffolding. CREB-binding protein
                     (CBP) is a large multidomain protein that...; cd02337"
                     /db_xref="CDD:239077"
     Site            order(1708,1711,1721,1724,1730,1733,1739,1741)
                     /site_type="other"
                     /note="Zinc-binding sites [ion binding]"
                     /db_xref="CDD:239077"
     Site            order(1708,1711,1730,1733)
                     /site_type="other"
                     /note="zinc cluster 1 [ion binding]"
                     /db_xref="CDD:239077"
     Site            order(1709,1718,1720,1726,1728)
                     /site_type="active"
                     /note="putative charged binding surface [active]"
                     /db_xref="CDD:239077"
     Site            order(1719,1734,1743,1746)
                     /site_type="active"
                     /note="putative hydrophobic binding surface [active]"
                     /db_xref="CDD:239077"
     Site            order(1721,1724,1739,1741)
                     /site_type="other"
                     /note="zinc cluster 2 [ion binding]"
                     /db_xref="CDD:239077"
     Site            1742
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            1745
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            1764
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Region          1773..1841
                     /region_name="zf-TAZ"
                     /note="TAZ zinc finger; pfam02135"
                     /db_xref="CDD:460457"
     Region          1875..1959
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P45481.3)"
     Region          1961..>2351
                     /region_name="Med15"
                     /note="ARC105 or Med15 subunit of Mediator complex
                     non-fungal; pfam09606"
                     /db_xref="CDD:312941"
     Region          2014..2115
                     /region_name="Creb_binding"
                     /note="Creb binding; pfam09030"
                     /db_xref="CDD:462659"
     Site            2064
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            2077
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Site            2080
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q92793; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     Region          2112..2421
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P45481.3)"
     Site            2350
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P45481.3)"
     CDS             1..2441
                     /gene="Crebbp"
                     /gene_synonym="CBP; CBP/p300; KAT3A; p300/CBP"
                     /coded_by="NM_001025432.1:182..7507"
                     /db_xref="CCDS:CCDS27915.1"
                     /db_xref="GeneID:12914"
                     /db_xref="MGI:MGI:1098280"
ORIGIN      
        1 maenlldgpp npkraklssp gfsandntdf gslfdlendl pdelipngel sllnsgnlvp
       61 daaskhkqls ellrggsgss inpgignvsa sspvqqglgg qaqgqpnstn maslgamgks
      121 plnqgdsstp nlpkqaasts gptppasqal npqaqkqvgl vtsspatsqt gpgicmnanf
      181 nqthpgllns nsghslmnqa qqgqaqvmng slgaagrgrg agmpypapam qgatssvlae
      241 tltqvspqma ghaglntaqa ggmtkmgmtg ttspfgqpfs qtggqqmgat gvnpqlaskq
      301 smvnslpafp tdikntsvtt vpnmsqlqts vgivptqaia tgptadpekr kliqqqlvll
      361 lhahkcqrre qangevracs lphcrtmknv lnhmthcqag kacqvahcas srqiishwkn
      421 ctrhdcpvcl plknasdkrn qqtilgspas giqntigsvg agqqnatsls npnpidpssm
      481 qrayaalglp ymnqpqtqlq pqvpgqqpaq ppahqqmrtl nalgnnpmsi paggittdqq
      541 ppnlisesal ptslgatnpl mndgsnsgni gslstiptaa ppsstgvrkg whehvtqdlr
      601 shlvhklvqa ifptpdpaal kdrrmenlva yakkvegdmy esansrdeyy hllaekiyki
      661 qkeleekrrs rlhkqgilgn qpalpasgaq ppvippaqsv rppngplplp vnrmqvsqgm
      721 nsfnpmslgn vqlpqapmgp raaspmnhsv qmnsmasvpg maispsrmpq ppnmmgthan
      781 nimaqaptqn qflpqnqfps ssgamsvnsv gmgqpaaqag vsqgqvpgaa lpnplnmlap
      841 qasqlpcppv tqsplhptpp pastaagmps lqhptapgmt ppqpaaptqp stpvssgqtp
      901 tptpgsvpsa aqtqstptvq aaaqaqvtpq pqtpvqppsv atpqssqqqp tpvhtqppgt
      961 plsqaaasid nrvptpssvt saetssqqpg pdvpmlemkt evqtddaepe pteskgeprs
     1021 emmeedlqgs sqvkeetdtt eqksepmeve ekkpevkvea keeeenssnd tasqstspsq
     1081 prkkifkpee lrqalmptle alyrqdpesl pfrqpvdpql lgipdyfdiv knpmdlstik
     1141 rkldtgqyqe pwqyvddvwl mfnnawlynr ktsrvykfcs klaevfeqei dpvmqslgyc
     1201 cgrkyefspq tlccygkqlc tiprdaayys yqnryhfcek cfteiqgenv tlgddpsqpq
     1261 ttiskdqfek kkndtldpep fvdckecgrk mhqicvlhyd iiwpsgfvcd nclkktgrpr
     1321 kenkfsakrl qttrlgnhle drvnkflrrq nhpeagevfv rvvassdktv evkpgmksrf
     1381 vdsgemsesf pyrtkalfaf eeidgvdvcf fgmhvqeygs dcpppntrrv yisyldsihf
     1441 frprclrtav yheiligyle yvkklgyvtg hiwacppseg ddyifhchpp dqkipkpkrl
     1501 qewykkmldk afaeriindy kdifkqaned rltsakelpy fegdfwpnvl eesikeleqe
     1561 eeerkkeest aasetpegsq gdsknakkkn nkktnknkss isrankkkps mpnvsndlsq
     1621 klyatmekhk evffvihlha gpvistqppi vdpdpllscd lmdgrdaflt lardkhwefs
     1681 slrrskwstl cmlvelhtqg qdrfvytcne ckhhvetrwh ctvcedydlc incyntksht
     1741 hkmvkwglgl ddegssqgep qskspqesrr lsiqrciqsl vhacqcrnan cslpscqkmk
     1801 rvvqhtkgck rktnggcpvc kqlialccyh akhcqenkcp vpfclnikhk lrqqqiqhrl
     1861 qqaqlmrrrm atmntrnvpq qslpsptsap pgtptqqpst pqtpqppaqp qpspvnmspa
     1921 gfpnvartqp ptivsagkpt nqvpappppa qpppaaveaa rqiereaqqq qhlyraninn
     1981 gmppgragmg tpgsqmtpvg lnvprpnqvs gpvmssmppg qwqqapipqq qpmpgmprpv
     2041 msmqaqaava gprmpnvqpp rsispsalqd llrtlkspss pqqqqqvlni lksnpqlmaa
     2101 fikqrtakyv anqpgmqpqp glqsqpgmqp qpgmhqqpsl qnlnamqagv prpgvpppqp
     2161 amgglnpqgq alnimnpghn pnmtnmnpqy remvrrqllq hqqqqqqqqq qqqqqqnsas
     2221 laggmaghsq fqqpqgpggy apamqqqrmq qhlpiqgssm gqmaapmgql gqmgqpglga
     2281 dstpniqqal qqrilqqqqm kqqigspgqp npmspqqhml sgqpqashlp gqqiatslsn
     2341 qvrspapvqs prpqsqpphs spspriqpqp sphhvspqtg sphpglavtm assmdqghlg
     2401 npeqsamlpq lntpnrsals selslvgdtt gdtlekfveg l
//
