ID EP300_MOUSE Reviewed; 2412 AA. AC B2RWS6; E9PYJ8; DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2014, sequence version 2. DT 27-MAR-2024, entry version 141. DE RecName: Full=Histone acetyltransferase p300; DE Short=p300 HAT; DE EC=2.3.1.48 {ECO:0000269|PubMed:27105113}; DE AltName: Full=E1A-associated protein p300; DE AltName: Full=Histone butyryltransferase p300; DE EC=2.3.1.- {ECO:0000269|PubMed:27105113}; DE AltName: Full=Histone crotonyltransferase p300; DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q09472}; DE AltName: Full=Protein 2-hydroxyisobutyryltransferase p300 {ECO:0000250|UniProtKB:Q09472}; DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q09472}; DE AltName: Full=Protein lactyltransferas p300; DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q09472}; DE AltName: Full=Protein propionyltransferase p300; DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q09472}; GN Name=Ep300; Synonyms=P300; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION, AND INTERACTION WITH NEUROD1. RX PubMed=9512516; DOI=10.1101/gad.12.6.820; RA Mutoh H., Naya F.J., Tsai M.J., Leiter A.B.; RT "The basic helix-loop-helix protein BETA2 interacts with p300 to coordinate RT differentiation of secretin-expressing enteroendocrine cells."; RL Genes Dev. 12:820-830(1998). RN [4] RP INTERACTION WITH CITED2. RX PubMed=10593900; DOI=10.1074/jbc.274.51.36159; RA Glenn D.J., Maurer R.A.; RT "MRG1 binds to the LIM domain of Lhx2 and may function as a coactivator to RT stimulate glycoprotein hormone alpha-subunit gene expression."; RL J. Biol. Chem. 274:36159-36167(1999). RN [5] RP INTERACTION WITH CITED1. RX PubMed=10722728; DOI=10.1074/jbc.275.12.8825; RA Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., RA Isselbacher K.J., Shioda T.; RT "The MSG1 non-DNA-binding transactivator binds to the p300/CBP RT coactivators, enhancing their functional link to the Smad transcription RT factors."; RL J. Biol. Chem. 275:8825-8834(2000). RN [6] RP IDENTIFICATION IN A COMPLEX WITH MSX3 AND CREBBP. RX PubMed=11115394; RA Mehra-Chaudhary R., Matsui H., Raghow R.; RT "Msx3 protein recruits histone deacetylase to down-regulate the Msx1 RT promoter."; RL Biochem. J. 353:13-22(2001). RN [7] RP INTERACTION WITH NR4A3. RX PubMed=12709428; DOI=10.1074/jbc.m300088200; RA Wansa K.D., Harris J.M., Yan G., Ordentlich P., Muscat G.E.; RT "The AF-1 domain of the orphan nuclear receptor NOR-1 mediates trans- RT activation, coactivator recruitment, and activation by the purine anti- RT metabolite 6-mercaptopurine."; RL J. Biol. Chem. 278:24776-24790(2003). RN [8] RP FUNCTION, AND INTERACTION WITH NPAS2. RX PubMed=14645221; DOI=10.1074/jbc.m311973200; RA Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., RA Chakravarti D., FitzGerald G.A., McNamara P.; RT "Histone acetyltransferase-dependent chromatin remodeling and the vascular RT clock."; RL J. Biol. Chem. 279:7091-7097(2004). RN [9] RP INTERACTION WITH MYOCD. RX PubMed=15601857; DOI=10.1128/mcb.25.1.364-376.2005; RA Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A., RA Wang D.Z., Olson E.N.; RT "Modulation of smooth muscle gene expression by association of histone RT acetyltransferases and deacetylases with myocardin."; RL Mol. Cell. Biol. 25:364-376(2005). RN [10] RP INTERACTION WITH HIPK2, AND PHOSPHORYLATION BY HIPK2. RX PubMed=16917507; DOI=10.1038/sj.emboj.7601273; RA Aikawa Y., Nguyen L.A., Isono K., Takakura N., Tagata Y., Schmitz M.L., RA Koseki H., Kitabayashi I.; RT "Roles of HIPK1 and HIPK2 in AML1- and p300-dependent transcription, RT hematopoiesis and blood vessel formation."; RL EMBO J. 25:3955-3965(2006). RN [11] RP FUNCTION, AND INTERACTION WITH CREBBP. RX PubMed=18486321; DOI=10.1016/j.mce.2008.03.009; RA Cesena T.I., Cui T.X., Subramanian L., Fulton C.T., Iniguez-Lluhi J.A., RA Kwok R.P., Schwartz J.; RT "Acetylation and deacetylation regulate CCAAT/enhancer binding protein beta RT at K39 in mediating gene transcription."; RL Mol. Cell. Endocrinol. 289:94-101(2008). RN [12] RP INTERACTION WITH CEBPB, AND SUBCELLULAR LOCATION. RX PubMed=19324970; DOI=10.1210/me.2008-0277; RA Ohoka N., Kato S., Takahashi Y., Hayashi H., Sato R.; RT "The orphan nuclear receptor RORalpha restrains adipocyte differentiation RT through a reduction of C/EBPbeta activity and perilipin gene expression."; RL Mol. Endocrinol. 23:759-771(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Lung, Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [14] RP INTERACTION WITH RB1. RX PubMed=20940255; DOI=10.1242/jcs.068924; RA Pickard A., Wong P.P., McCance D.J.; RT "Acetylation of Rb by PCAF is required for nuclear localization and RT keratinocyte differentiation."; RL J. Cell Sci. 123:3718-3726(2010). RN [15] RP FUNCTION IN ACETYLATION OF ZBTB7B. RX PubMed=20810990; DOI=10.4049/jimmunol.1001462; RA Zhang M., Zhang J., Rui J., Liu X.; RT "p300-mediated acetylation stabilizes the Th-inducing POK factor."; RL J. Immunol. 185:3960-3969(2010). RN [16] RP FUNCTION IN ACETYLATION OF XBP1. RX PubMed=20955178; DOI=10.1042/bj20101293; RA Wang F.M., Chen Y.J., Ouyang H.J.; RT "Regulation of unfolded protein response modulator XBP1s by acetylation and RT deacetylation."; RL Biochem. J. 433:245-252(2011). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1179; LYS-1557 AND LYS-1559, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [18] RP FUNCTION. RX PubMed=25200183; DOI=10.1016/j.cmet.2014.08.001; RA Ryu D., Jo Y.S., Lo Sasso G., Stein S., Zhang H., Perino A., Lee J.U., RA Zeviani M., Romand R., Hottiger M.O., Schoonjans K., Auwerx J.; RT "A SIRT7-dependent acetylation switch of GABPbeta1 controls mitochondrial RT function."; RL Cell Metab. 20:856-869(2014). RN [19] RP FUNCTION, AND INTERACTION WITH ATF5 AND CREBBP. RX PubMed=24216764; DOI=10.1128/mcb.00956-13; RA Zhao Y., Zhang Y.D., Zhang Y.Y., Qian S.W., Zhang Z.C., Li S.F., Guo L., RA Liu Y., Wen B., Lei Q.Y., Tang Q.Q., Li X.; RT "p300-dependent acetylation of activating transcription factor 5 enhances RT C/EBPbeta transactivation of C/EBPalpha during 3T3-L1 differentiation."; RL Mol. Cell. Biol. 34:315-324(2014). RN [20] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014; RA Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z., RA Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J., RA Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C., Panne D., RA Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.; RT "Dynamic competing histone H4 K5K8 acetylation and butyrylation are RT hallmarks of highly active gene promoters."; RL Mol. Cell 62:169-180(2016). RN [21] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=28576496; DOI=10.1016/j.bbrc.2017.05.170; RA Noritsugu K., Ito A., Nakao Y., Yoshida M.; RT "Identification of zinc finger transcription factor EGR2 as a novel RT acetylated protein."; RL Biochem. Biophys. Res. Commun. 489:455-459(2017). RN [22] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=28883095; DOI=10.1242/jcs.206904; RA Lai Y., Li J., Li X., Zou C.; RT "Lipopolysaccharide modulates p300 and Sirt1 to promote PRMT1 stability via RT an SCFFbxl17-recognized acetyldegron."; RL J. Cell Sci. 130:3578-3587(2017). CC -!- FUNCTION: Functions as a histone acetyltransferase and regulates CC transcription via chromatin remodeling (By similarity). Acetylates all CC four core histones in nucleosomes (By similarity). Histone acetylation CC gives an epigenetic tag for transcriptional activation (By similarity). CC Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a CC modification that localizes at the surface of the histone octamer and CC stimulates transcription, possibly by promoting nucleosome instability CC (By similarity). Mediates acetylation of histone H3 at 'Lys-18' and CC 'Lys-27' (H3K18ac and H3K27ac, respectively) (By similarity). Also able CC to acetylate histone lysine residues that are already monomethylated on CC the same side chain to form N6-acetyl-N6-methyllysine (Kacme), an CC epigenetic mark of active chromatin associated with increased CC transcriptional initiation (By similarity). Catalyzes formation of CC histone H4 acetyl-methylated at 'Lys-5' and 'Lys-12' (H4K5acme and CC H4K12acme, respectively) (By similarity). Also functions as CC acetyltransferase for non-histone targets, such as ALX1, HDAC1, PRMT1, CC SIRT2 or STAT3 (PubMed:28883095, PubMed:28576496). Acetylates 'Lys-131' CC of ALX1 and acts as its coactivator (By similarity). Acetylates SIRT2 CC and is proposed to indirectly increase the transcriptional activity of CC TP53 through acetylation and subsequent attenuation of SIRT2 CC deacetylase function (By similarity). Following DNA damage, forms a CC stress-responsive p53/TP53 coactivator complex with JMY which mediates CC p53/TP53 acetylation, thereby increasing p53/TP53-dependent CC transcription and apoptosis (By similarity). Promotes chromatin CC acetylation in heat shock responsive HSP genes during the heat shock CC response (HSR), thereby stimulating HSR transcription (By similarity). CC Acetylates HDAC1 leading to its inactivation and modulation of CC transcription (By similarity). Acetylates 'Lys-247' of EGR2 CC (PubMed:28576496). Acts as a TFAP2A-mediated transcriptional CC coactivator in presence of CITED2 (By similarity). Plays a role as a CC coactivator of NEUROD1-dependent transcription of the secretin and p21 CC genes and controls terminal differentiation of cells in the intestinal CC epithelium (By similarity). Promotes cardiac myocyte enlargement (By CC similarity). Can also mediate transcriptional repression (By CC similarity). Acetylates FOXO1 and enhances its transcriptional activity CC (By similarity). Acetylates STAT3 at different sites, promoting both CC STAT3 dimerization and activation and recruitment to chromatin (By CC similarity). Acetylates BCL6 wich disrupts its ability to recruit CC histone deacetylases and hinders its transcriptional repressor activity CC (By similarity). Participates in CLOCK or NPAS2-regulated rhythmic gene CC transcription; exhibits a circadian association with CLOCK or NPAS2, CC correlating with increase in PER1/2 mRNA and histone H3 acetylation on CC the PER1/2 promoter (By similarity). Acetylates MTA1 at 'Lys-626' which CC is essential for its transcriptional coactivator activity CC (PubMed:14645221, PubMed:9512516). Acetylates XBP1 isoform 2; CC acetylation increases protein stability of XBP1 isoform 2 and enhances CC its transcriptional activity (PubMed:20955178). Acetylates PCNA; CC acetylation promotes removal of chromatin-bound PCNA and its CC degradation during nucleotide excision repair (NER) (By similarity). CC Acetylates MEF2D (By similarity). Acetylates and stabilizes ZBTB7B CC protein by antagonizing ubiquitin conjugation and degradation, this CC mechanism may be involved in CD4/CD8 lineage differentiation CC (PubMed:20810990). Acetylates GABPB1, impairing GABPB1 CC heterotetramerization and activity (PubMed:25200183). Acetylates PCK1 CC and promotes PCK1 anaplerotic activity (By similarity). Acetylates RXRA CC and RXRG (By similarity). Acetylates isoform M2 of PKM (PKM2), CC promoting its homodimerization and conversion into a protein kinase (By CC similarity). Acetylates RPTOR in response to leucine, leading to CC activation of the mTORC1 complex (By similarity). Mediates cAMP-gene CC regulation by binding specifically to phosphorylated CREBBP CC (PubMed:18486321, PubMed:24216764). In addition to protein CC acetyltransferase, can use different acyl-CoA substrates, such as (2E)- CC butenoyl-CoA (crotonyl-CoA), butanoyl-CoA (butyryl-CoA), 2- CC hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), lactoyl-CoA or CC propanoyl-CoA (propionyl-CoA), and is able to mediate protein CC crotonylation, butyrylation, 2-hydroxyisobutyrylation, lactylation or CC propionylation, respectively (PubMed:27105113). Acts as a histone CC crotonyltransferase; crotonylation marks active promoters and enhancers CC and confers resistance to transcriptional repressors. Histone CC crotonyltransferase activity is dependent on the concentration of (2E)- CC butenoyl-CoA (crotonyl-CoA) substrate and such activity is weak when CC (2E)-butenoyl-CoA (crotonyl-CoA) concentration is low (By similarity). CC Also acts as a histone butyryltransferase; butyrylation marks active CC promoters (PubMed:27105113). Catalyzes histone lactylation in CC macrophages by using lactoyl-CoA directly derived from endogenous or CC exogenous lactate, leading to stimulates gene transcription (By CC similarity). Acts as a protein-lysine 2-hydroxyisobutyryltransferase; CC regulates glycolysis by mediating 2-hydroxyisobutyrylation of CC glycolytic enzymes. Functions as a transcriptional coactivator for CC SMAD4 in the TGF-beta signaling pathway (By similarity). CC {ECO:0000250|UniProtKB:Q09472, ECO:0000269|PubMed:14645221, CC ECO:0000269|PubMed:18486321, ECO:0000269|PubMed:20810990, CC ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:25200183, CC ECO:0000269|PubMed:27105113, ECO:0000269|PubMed:28576496, CC ECO:0000269|PubMed:28883095, ECO:0000269|PubMed:9512516, CC ECO:0000305|PubMed:20955178}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC Evidence={ECO:0000269|PubMed:27105113}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; CC Evidence={ECO:0000269|PubMed:27105113}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; CC Evidence={ECO:0000269|PubMed:28576496, ECO:0000305|PubMed:28883095}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949; CC Evidence={ECO:0000269|PubMed:28576496, ECO:0000305|PubMed:28883095}; CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + N(6)-methyl-L-lysyl-[histone] = CoA + H(+) + CC N(6)-acetyl-N(6)-methyl-L-lysyl-[histone]; Xref=Rhea:RHEA:77775, CC Rhea:RHEA-COMP:9846, Rhea:RHEA-COMP:18984, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61929, CC ChEBI:CHEBI:197459; Evidence={ECO:0000250|UniProtKB:Q09472}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77776; CC Evidence={ECO:0000250|UniProtKB:Q09472}; CC -!- CATALYTIC ACTIVITY: CC Reaction=butanoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-butanoyl- CC L-lysyl-[protein]; Xref=Rhea:RHEA:53912, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:13708, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:137955; CC Evidence={ECO:0000269|PubMed:27105113}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)- CC (2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA- CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332, CC ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q09472}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[protein] + propanoyl-CoA = CoA + H(+) + N(6)- CC propanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54020, Rhea:RHEA- CC COMP:9752, Rhea:RHEA-COMP:13758, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, CC ChEBI:CHEBI:138019; Evidence={ECO:0000250|UniProtKB:Q09472}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) + CC N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180, CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780, CC ChEBI:CHEBI:144968; Evidence={ECO:0000250|UniProtKB:Q09472}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181; CC Evidence={ECO:0000250|UniProtKB:Q09472}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[protein] + lactoyl-CoA = CoA + H(+) + N(6)-lactoyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:61996, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:16001, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57382, ChEBI:CHEBI:145324; CC Evidence={ECO:0000250|UniProtKB:Q09472}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61997; CC Evidence={ECO:0000250|UniProtKB:Q09472}; CC -!- SUBUNIT: Part of a complex composed of MSX3, CREBBP/CBP AND EP300/p300; CC the interaction with MSX3 decreases histone acetylation activity CC (PubMed:11115394). Interacts with HIF1A; the interaction is stimulated CC in response to hypoxia and inhibited by CITED2. Probably part of a CC complex with HIF1A and CREBBP. Interacts (via N-terminus) with TFAP2A CC (via N-terminus); the interaction requires CITED2 (By similarity). CC Interacts (via CH1 domain) with CITED2 (via C-terminus) CC (PubMed:10593900). Interacts with CITED1 (unphosphorylated form CC preferentially and via C-terminus) (PubMed:10722728). Interacts with CC ESR1; the interaction is estrogen-dependent and enhanced by CITED1 (By CC similarity). Interacts with HIPK2 (PubMed:16917507). Interacts with CC DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, CC SP1, SP3, SPIB, SRY, TCF7L2, DDX5, DDX17, SATB1, SRCAP and TRERF1 (By CC similarity). Interacts with JMY, the complex activates p53/TP53 CC transcriptional activity. Interacts with TTC5/STRAP; the interaction CC facilitates the association between JMY and p300/EP300 cofactors. CC Interacts with p53/TP53; the interaction is facilitated by TTC5/STRAP. CC Forms a complex with TTC5/STRAP and HSF1; these interactions augment CC chromatin-bound HSF1 and p300/EP300 histone acetyltransferase activity CC (By similarity). Part of a complex containing CARM1 and NCOA2/GRIP1. CC Interacts with ING4 and this interaction may be indirect. Interacts CC with ING5. Interacts with the C-terminal region of CITED4. Non- CC sumoylated EP300 preferentially interacts with SENP3. Interacts with CC SS18L1/CREST. Interacts with ALX1 (via homeobox domain) (By CC similarity). Interacts with NEUROD1; the interaction is inhibited by CC NR0B2 (PubMed:9512516). Interacts with TCF3 (By similarity). Interacts CC (via CREB-binding domain) with MYOCD (via C-terminus) CC (PubMed:15601857). Interacts with ROCK2 and PPARG. Forms a complex made CC of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy CC in cardiomyocytes. Interacts with IRF1 and this interaction enhances CC acetylation of p53/TP53 and stimulation of its activity. Interacts with CC ALKBH4 and DDIT3/CHOP. Interacts with KLF15 (By similarity). Interacts CC with CEBPB and RORA (PubMed:18486321, PubMed:24216764). Interacts with CC NPAS2, BMAL1 and CLOCK. Interacts with SIRT2 isoform 1, isoform 2 and CC isoform 5. Interacts with MTA1. Interacts with HDAC4 and HDAC5 in the CC presence of TFAP2C. Interacts with TRIP4 (By similarity). Interacts CC with NPAS2 (PubMed:14645221). Directly interacts with ZBTB49; this CC interaction leads to synergistic transactivation of CDKN1A (By CC similarity). Interacts with NR4A3 (PubMed:12709428). Interacts with CC ZNF451 (By similarity). Interacts with ATF5; EP300 is required for ATF5 CC and CEBPB interaction and DNA binding (PubMed:24216764). Interacts with CC HSF1. Interacts with ZBTB48/TZAP. Interacts with STAT1; the interaction CC is enhanced upon IFN-gamma stimulation. Interacts with HNRNPU (via C- CC terminus); this interaction enhances DNA-binding of HNRNPU to nuclear CC scaffold/matrix attachment region (S/MAR) elements. Interacts with CC BCL11B. Interacts with SMAD4; negatively regulated by ZBTB7A. Interacts CC with DUX4 (via C-terminus). Interacts with NUPR1; this interaction CC enhances the effect of EP300 on PAX2 transcription factor activity. CC Interacts with RXRA; the interaction is decreased by 9-cis retinoic CC acid. NR4A1 competes with EP300 for interaction with RXRA and thereby CC attenuates EP300 mediated acetylation of RXRA (By similarity). CC Interacts with RB1 (PubMed:20940255). Interacts with DDX3X; this CC interaction may facilitate HNF4A acetylation. Interacts with SOX9. CC Interacts with ATF4; EP300/p300 stabilizes ATF4 and increases its CC transcriptional activity independently of its catalytic activity by CC preventing its ubiquitination (By similarity). Interacts with KAT5; CC promoting KAT5 autoacetylation (By similarity). Interacts (via bromo CC domain) with (acetylated) STAT3; interaction takes place following CC STAT3 acetylation by EP300 and promotes enhanceosome assembly (By CC similarity). {ECO:0000250|UniProtKB:Q09472, CC ECO:0000269|PubMed:10593900, ECO:0000269|PubMed:10722728, CC ECO:0000269|PubMed:11115394, ECO:0000269|PubMed:12709428, CC ECO:0000269|PubMed:14645221, ECO:0000269|PubMed:15601857, CC ECO:0000269|PubMed:16917507, ECO:0000269|PubMed:18486321, CC ECO:0000269|PubMed:19324970, ECO:0000269|PubMed:20940255, CC ECO:0000269|PubMed:24216764, ECO:0000269|PubMed:9512516}. CC -!- INTERACTION: CC B2RWS6; A0A087WPF7: Auts2; NbExp=3; IntAct=EBI-3953360, EBI-27122375; CC B2RWS6; P02340: Tp53; NbExp=3; IntAct=EBI-3953360, EBI-474016; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q09472}. Nucleus CC {ECO:0000255|PROSITE-ProRule:PRU00311, ECO:0000269|PubMed:19324970}. CC Note=In the presence of ALX1 relocalizes from the cytoplasm to the CC nucleus. Colocalizes with ROCK2 in the nucleus. Localizes to sites of CC DNA damage. {ECO:0000250|UniProtKB:Q09472}. CC -!- DOMAIN: The CRD1 domain (cell cycle regulatory domain 1) mediates CC transcriptional repression of a subset of p300 responsive genes; it can CC be de-repressed by CDKN1A/p21WAF1 at least at some promoters. It CC contains sumoylation and acetylation sites and the same lysine residues CC may be targeted for the respective modifications. It is proposed that CC deacetylation by SIRT1 allows sumoylation leading to suppressed CC activity (By similarity). {ECO:0000250|UniProtKB:Q09472}. CC -!- PTM: Acetylated on Lys at up to 17 positions by intermolecular CC autocatalysis. Deacetylated in the transcriptional repression domain CC (CRD1) by SIRT1, preferentially at Lys-1019. Deacetylated by SIRT2, CC preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys- CC 1698, Lys-1703 and Lys-1706. {ECO:0000250|UniProtKB:Q09472}. CC -!- PTM: Citrullinated at Arg-2143 by PADI4, which impairs methylation by CC CARM1 and promotes interaction with NCOA2/GRIP1. CC {ECO:0000250|UniProtKB:Q09472}. CC -!- PTM: Methylated at Arg-581 and Arg-605 in the KIX domain by CARM1, CC which blocks association with CREB, inhibits CREB signaling and CC activates apoptotic response. Also methylated at Arg-2143 by CARM1, CC which impairs interaction with NCOA2/GRIP1 (By similarity). CC {ECO:0000250|UniProtKB:Q09472}. CC -!- PTM: Sumoylated; sumoylation in the transcriptional repression domain CC (CRD1) mediates transcriptional repression. Desumoylated by SENP3 CC through the removal of SUMO2 and SUMO3 (By similarity). CC {ECO:0000250|UniProtKB:Q09472}. CC -!- PTM: Probable target of ubiquitination by FBXO3, leading to rapid CC proteasome-dependent degradation. {ECO:0000250|UniProtKB:Q09472}. CC -!- PTM: Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear CC receptors, such as PPARG (By similarity). Phosphorylated by HIPK2 in a CC RUNX1-dependent manner. This phosphorylation that activates EP300 CC happens when RUNX1 is associated with DNA and CBFB. Phosphorylated by CC ROCK2 and this enhances its activity (By similarity). CC {ECO:0000250|UniProtKB:Q09472}. 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 EMBL; AC102262; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC160528; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC144976; AAI44977.1; -; mRNA. DR EMBL; BC150681; AAI50682.1; -; mRNA. DR CCDS; CCDS37149.1; -. DR RefSeq; NP_808489.4; NM_177821.6. DR AlphaFoldDB; B2RWS6; -. DR BMRB; B2RWS6; -. DR SMR; B2RWS6; -. DR BioGRID; 236625; 92. DR CORUM; B2RWS6; -. DR DIP; DIP-60610N; -. DR IntAct; B2RWS6; 10. DR MINT; B2RWS6; -. DR STRING; 10090.ENSMUSP00000066789; -. DR GlyGen; B2RWS6; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; B2RWS6; -. DR PhosphoSitePlus; B2RWS6; -. DR SwissPalm; B2RWS6; -. DR EPD; B2RWS6; -. DR PaxDb; 10090-ENSMUSP00000066789; -. DR PeptideAtlas; B2RWS6; -. DR ProteomicsDB; 275928; -. DR Pumba; B2RWS6; -. DR Antibodypedia; 296; 1177 antibodies from 40 providers. DR DNASU; 328572; -. DR Ensembl; ENSMUST00000068387.11; ENSMUSP00000066789.5; ENSMUSG00000055024.13. DR GeneID; 328572; -. DR KEGG; mmu:328572; -. DR UCSC; uc007wws.1; mouse. DR AGR; MGI:1276116; -. DR CTD; 2033; -. DR MGI; MGI:1276116; Ep300. DR VEuPathDB; HostDB:ENSMUSG00000055024; -. DR eggNOG; KOG1778; Eukaryota. DR GeneTree; ENSGT00940000155497; -. DR HOGENOM; CLU_000162_2_0_1; -. DR InParanoid; B2RWS6; -. DR OMA; NMNASPM; -. DR OrthoDB; 5490807at2759; -. DR PhylomeDB; B2RWS6; -. DR TreeFam; TF101097; -. DR BRENDA; 2.3.1.48; 3474. DR Reactome; R-MMU-1234158; Regulation of gene expression by Hypoxia-inducible Factor. DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription. DR Reactome; R-MMU-3134973; LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production. DR Reactome; R-MMU-3371568; Attenuation phase. DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors. DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling. DR Reactome; R-MMU-5689901; Metalloprotease DUBs. DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex. DR Reactome; R-MMU-6782135; Dual incision in TC-NER. DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation. DR Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation. DR Reactome; R-MMU-6811555; PI5P Regulates TP53 Acetylation. DR Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors. DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function. DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known. DR Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling. DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity. DR Reactome; R-MMU-8951936; RUNX3 regulates p14-ARF. DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression. DR Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux. DR Reactome; R-MMU-933541; TRAF6 mediated IRF7 activation. DR Reactome; R-MMU-9617629; Regulation of FOXO transcriptional activity by acetylation. DR Reactome; R-MMU-9701898; STAT3 nuclear events downstream of ALK signaling. DR Reactome; R-MMU-9759194; Nuclear events mediated by NFE2L2. DR BioGRID-ORCS; 328572; 19 hits in 88 CRISPR screens. DR ChiTaRS; Ep300; mouse. DR PRO; PR:B2RWS6; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; B2RWS6; Protein. DR Bgee; ENSMUSG00000055024; Expressed in embryonic post-anal tail and 224 other cell types or tissues. DR ExpressionAtlas; B2RWS6; baseline and differential. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI. DR GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB. DR GO; GO:0140033; F:acetylation-dependent protein binding; IEA:Ensembl. DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0016746; F:acyltransferase activity; ISO:MGI. DR GO; GO:0003823; F:antigen binding; ISO:MGI. DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI. DR GO; GO:0043425; F:bHLH transcription factor binding; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0140069; F:histone butyryltransferase activity; IDA:UniProtKB. DR GO; GO:0140068; F:histone crotonyltransferase activity; ISS:UniProtKB. DR GO; GO:0044013; F:histone H2B acetyltransferase activity; ISO:MGI. DR GO; GO:0010484; F:histone H3 acetyltransferase activity; ISO:MGI. DR GO; GO:0140908; F:histone H3K122 acetyltransferase activity; ISS:UniProtKB. DR GO; GO:0043993; F:histone H3K18 acetyltransferase activity; ISS:UniProtKB. DR GO; GO:0044017; F:histone H3K27 acetyltransferase activity; ISS:UniProtKB. DR GO; GO:0010485; F:histone H4 acetyltransferase activity; ISS:UniProtKB. DR GO; GO:0120301; F:histone lactyltransferase activity; ISS:UniProtKB. DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; ISS:UniProtKB. DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI. DR GO; GO:0051059; F:NF-kappaB binding; ISO:MGI. DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI. DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:MGI. DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI. DR GO; GO:0002039; F:p53 binding; IPI:MGI. DR GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA. DR GO; GO:0140065; F:peptide butyryltransferase activity; ISO:MGI. DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI. DR GO; GO:0097157; F:pre-mRNA intronic binding; IDA:MGI. DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI. DR GO; GO:1990405; F:protein antigen binding; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0061920; F:protein propionyltransferase activity; ISS:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:MGI. DR GO; GO:0046332; F:SMAD binding; ISO:MGI. DR GO; GO:0097677; F:STAT family protein binding; ISO:MGI. DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI. DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB. DR GO; GO:0001221; F:transcription coregulator binding; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI. DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB. DR GO; GO:0030183; P:B cell differentiation; IMP:MGI. DR GO; GO:0002209; P:behavioral defense response; IMP:ARUK-UCL. DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; ISO:MGI. DR GO; GO:0051216; P:cartilage development; NAS:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI. DR GO; GO:0071233; P:cellular response to leucine; ISS:UniProtKB. DR GO; GO:0031669; P:cellular response to nutrient levels; ISO:MGI. DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB. DR GO; GO:0007623; P:circadian rhythm; IDA:UniProtKB. DR GO; GO:0060325; P:face morphogenesis; IMP:ARUK-UCL. DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0006475; P:internal protein amino acid acetylation; ISS:UniProtKB. DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:MGI. DR GO; GO:0007611; P:learning or memory; IMP:ARUK-UCL. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0010742; P:macrophage derived foam cell differentiation; ISS:UniProtKB. DR GO; GO:0035855; P:megakaryocyte development; IMP:MGI. DR GO; GO:0035264; P:multicellular organism growth; IMP:ARUK-UCL. DR GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; ISS:UniProtKB. DR GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI. DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISO:MGI. DR GO; GO:2000629; P:negative regulation of miRNA metabolic process; ISO:MGI. DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0140067; P:peptidyl-lysine butyrylation; IDA:UniProtKB. DR GO; GO:0140066; P:peptidyl-lysine crotonylation; ISS:UniProtKB. DR GO; GO:0061921; P:peptidyl-lysine propionylation; ISS:UniProtKB. DR GO; GO:0030220; P:platelet formation; IMP:MGI. DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI. DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI. DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI. DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:MGI. DR GO; GO:0045793; P:positive regulation of cell size; ISO:MGI. DR GO; GO:1900039; P:positive regulation of cellular response to hypoxia; ISO:MGI. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI. DR GO; GO:0010560; P:positive regulation of glycoprotein biosynthetic process; ISO:MGI. DR GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; ISO:MGI. DR GO; GO:0014737; P:positive regulation of muscle atrophy; ISO:MGI. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI. DR GO; GO:1901985; P:positive regulation of protein acetylation; ISO:MGI. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI. DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI. DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI. DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI. DR GO; GO:0060298; P:positive regulation of sarcomere organization; ISO:MGI. DR GO; GO:1904263; P:positive regulation of TORC1 signaling; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI. DR GO; GO:0045727; P:positive regulation of translation; ISO:MGI. DR GO; GO:0006473; P:protein acetylation; IDA:UniProtKB. DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB. DR GO; GO:0036211; P:protein modification process; ISO:MGI. DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB. DR GO; GO:0065004; P:protein-DNA complex assembly; ISO:MGI. DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISO:MGI. DR GO; GO:0060177; P:regulation of angiotensin metabolic process; ISO:MGI. DR GO; GO:0006110; P:regulation of glycolytic process; ISS:UniProtKB. DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISS:UniProtKB. DR GO; GO:0051592; P:response to calcium ion; ISO:MGI. DR GO; GO:0071548; P:response to dexamethasone; ISO:MGI. DR GO; GO:0043627; P:response to estrogen; ISS:UniProtKB. DR GO; GO:0009749; P:response to glucose; ISO:MGI. DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB. DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI. DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI. DR GO; GO:0001756; P:somitogenesis; IGI:MGI. DR GO; GO:0036268; P:swimming; IMP:ARUK-UCL. DR GO; GO:0001966; P:thigmotaxis; IMP:ARUK-UCL. DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; ISS:UniProtKB. DR CDD; cd05495; Bromo_cbp_like; 1. DR CDD; cd20910; NCBD_CREBBP-p300_like; 1. DR CDD; cd15646; PHD_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: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 PRINTS; PR01217; PRICHEXTENSN. 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. DR Genevisible; B2RWS6; MM. PE 1: Evidence at protein level; KW Acetylation; Acyltransferase; Biological rhythms; Bromodomain; Cell cycle; KW Citrullination; Coiled coil; Cytoplasm; Differentiation; Isopeptide bond; KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Transcription; Transcription regulation; Transferase; KW Ubl conjugation; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT CHAIN 2..2412 FT /note="Histone acetyltransferase p300" FT /id="PRO_0000409386" FT DOMAIN 567..646 FT /note="KIX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00311" FT DOMAIN 1066..1138 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 1286..1662 FT /note="CBP/p300-type HAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065" FT ZN_FING 332..418 FT /note="TAZ-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203" FT ZN_FING 1664..1712 FT /note="ZZ-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT ZN_FING 1727..1808 FT /note="TAZ-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..149 FT /note="Interaction with RORA" FT REGION 2..139 FT /note="Interaction with ALX1" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT REGION 130..156 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 484..517 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 719..762 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 776..1049 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1016..1028 FT /note="CRD1; mediates transcriptional repression" FT /evidence="ECO:0000250" FT REGION 1396..1398 FT /note="Interaction with histone" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT REGION 1519..1577 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1830..1925 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1991..2011 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2042..2237 FT /note="Interaction with NCOA2" FT /evidence="ECO:0000250" FT REGION 2094..2133 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2192..2236 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2263..2348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 1510..1539 FT /evidence="ECO:0000255" FT MOTIF 11..17 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 776..834 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 835..900 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 901..925 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 940..972 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 973..1028 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1519..1546 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1547..1564 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1850..1885 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1886..1904 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1905..1925 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1996..2011 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2106..2133 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2203..2236 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2263..2307 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2308..2339 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 348 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 352 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 365 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 370 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 379 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 383 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 389 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 394 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 403 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 407 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 412 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 415 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1397..1399 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1409..1410 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1456 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1461 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1465 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1669 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1672 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1682 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1685 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1691 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1694 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1700 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1702 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT SITE 2089 FT /note="Interaction with NCOA2" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT SITE 2143 FT /note="Interaction with NCOA2" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 89 FT /note="Phosphoserine; by AMPK" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 419 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 424 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 500 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 581 FT /note="Asymmetric dimethylarginine; by CARM1" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 605 FT /note="Asymmetric dimethylarginine; by CARM1" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 637 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 976 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1019 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1023 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1037 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1179 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1335 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1472 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1498 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1541 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1545 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1548 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1553 FT /note="N6-acetyllysine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1554 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1557 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1559 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1582 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1698 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1703 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1706 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 1725 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 2143 FT /note="Asymmetric dimethylarginine; by CARM1; alternate" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT MOD_RES 2143 FT /note="Citrulline; by PADI4; alternate" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT CROSSLNK 1019 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT CROSSLNK 1023 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT CONFLICT 677 FT /note="G -> E (in Ref. 2; AAI44977/AAI50682)" FT /evidence="ECO:0000305" FT CONFLICT 2217 FT /note="Q -> QQQQ (in Ref. 2; AAI44977/AAI50682)" FT /evidence="ECO:0000305" SQ SEQUENCE 2412 AA; 263305 MW; 0E9B2D9508237671 CRC64; MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD ISQLQTSLGI VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQAMASQAQQ NSPGLSLINS MVKSPMAQTG LTSPNMGIGS SGPNQGPTQS PAGMMNSPVN QPAMGMNTGM NAGMNPGMLA AGNGQGIMPN QVMNGSIGAG RGRPNMQYPN AGMGNAGSLL TEPLQQGSPQ MGGQPGLRGP QPLKMGMMNN PSPYGSPYTQ NSGQQIGASG LGLQIQTKTV LPNNLSPFAM DKKAVPGGGM PSMGQQPTPS VQQPGLVTPV AAGMGSGAHT ADPEKRKLIQ QQLVLLLHAH KCQRREQANG EVRQCNLPHC RTMKNVLNHM THCQSGKSCQ VAHCASSRQI ISHWKNCTRH DCPVCLPLKN AGDKRNQQSI LTGAPVGLGN PSSLGVGQQS TPSLSTVSQI DPSSIERAYA ALGLPYQVNQ IPPQPQVQAK NQQSQPSGQS PQGMRSVNNM SASPMGVNGG VGVQTPNLLS DSMLHSTINS QNPMMSENAG VASLGPLPTA AQPSSTGIRK QWHEDITQDL RNHLVHKLVQ AIFPTPDPAA LKDRRMENLV AYARKVEGDM YESANNRAEY YHLLAEKIYK IQKELEEKRR TRLQKQNMLP NAPGMGPVPM NTGSNMGQQP TGMTTNGPVP DPSMIRGSVP NHMMPRMTPQ PGLNQFGQMN MPQPPIGPRQ PSPLQHHGQL AQSGSLNPPM GYGPRMQQAS GQNQFLSQTQ FTSQGMNVTN MPLAPSSGQA PVSQAQMSSS SCPVNSPIMP PGSQGSHIHC PTLPQQAHQN SPSPVPSRTP TPHHTPPSIG NQPPPATAIP TPVPTPPAIP PGPQPPSLHP SSRQTPTPPT HLPPQVQPSL PAAPSADQSQ QQPRSQQSTA VSVPTPTAPL LPPQPSTPLS QPAVSIEGQV SNPPSTSSTE VNSQTIPEKQ PSQEVKMESK MEVDKPEPAD AQPEDTKEAK GEDVKVEPTE MEERGPELKT DGKEEEEQPS TSATQSSPAP GQSKKKIFKP EELRQALMPT LEALYRQDPE SLPFRQPVDP QLLGIPDYFD IVKSPMDLST IKRKLDTGQY QEPWQYIDDI WLMFNNAWLY NRKTSRVYKY CSKLSEVFEQ EIDPVMQSLG YCCGRKLEFS PQTLCCYGKQ LCTIPRDATY YSYQNRYHFC EKCFNEIQGE SVSLGDDPSQ PQTTINKEQF SKRKNDTLDP ELFVECTECG RKMHQICVLH HEIIWPSGFV CDGCLKKTAR TRKENKLSAK RLPSTRLGTF LENRVNDFLR RQNHPESGEV TVRVVHASDK TVEVKPGMKA RFVDSGEMAE SFPYRTKALF AFEEIDGVDL CFFGMHVQEY GSDCPPPNQR RVYISYLDSV HFFRPKCLRT AVYHEILIGY LEYVKKLGYT TGHIWACPPS EGDDYIFHCH PPDQKIPKPK RLQEWYKKML DKAVSERIVH DYKDILKQAT EDRLTSAKEL PYFEGDFWPN VLEESIKELE QEEEERKREE NTSNESTDVT KGDSKNAKKK NNKKTSKNKS SLSRGNKKKP GMPNVSNDLS QKLYATMEKH KEVFFVIRLI ACPAPNSLPP IVDPDPLIPC DLMDGRDAFL TLARDKHLEF SSLRRAQWST MCMLVELHTQ SQDRFVYTCN ECKHHVETRW HCTVCEDYDL CITCYNTKNH DHKMEKLGLG LDDESNNQQA AATQSPGDSR RLSIQRCIQS LVHACQCRNA NCSLPSCQKM KRVVQHTKGC KRKTNGGCPI CKQLIALCCY HAKHCQENKC PVPFCLNIKQ KLRQQQLQHR LQQAQMLRRR MASMQRTGVA GQQQGLPSPT PATPTTPTGQ QPATPQTPQP QPTSQPQPTP PNNMTPYLPR TQTTGPVSQG KAPGQVTPPT PPQTAQAPLP GPPPAAVEMA MQIQRAAETQ RQMAHVQIFQ RPIQHQMPQM SPMAPMGMNP PPMARGPGGH LDPGIGPAGM QQQPPWAQGG MPQPQQMQSG MPRPAMMSVA QHGQPLNMAP QPGLGQVGVS PLKPGTVSQQ ALQNLLRTLR SPSSPLQQQQ VLSILHANPQ LLAAFIKQRA AKYANPNPQP LPGQPGMTQG QPGLQPPTMP GQQGVHSNPA LQNMNPLQAG VQRAGLPQQQ PQQQLQPPMG AMSPQAQQMN MNHNTMPSQF RDILRRQMMQ QQGAGPGIGP GMANQFQQPQ GIGYPPQQQQ QQRMQHHMQQ MQQGNMGQMG QLPQALGAEA GASLQAYQQR LLQQQMGSPA QPNPMSPQQH MLPNQAQSPH LQGQQIPNSL SNQVRSPQPV PSPRPQSQPP HSSPSPRMQP QPSPHHVSPQ TSSPHPGLVA AQAANPMEQG HFASPDQNSM LSQLASNPGM ANLHGASATD LGLSSDNADL NSNLSQSTLD IH //