ID CBP_MOUSE Reviewed; 2441 AA. AC P45481; E9QPH4; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 27-MAR-2024, entry version 235. DE RecName: Full=Histone lysine acetyltransferase CREBBP; DE EC=2.3.1.48 {ECO:0000269|PubMed:11115394}; DE AltName: Full=Protein-lysine acetyltransferase CREBBP; DE EC=2.3.1.- {ECO:0000269|PubMed:15220471}; GN Name=Crebbp; Synonyms=Cbp; 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 [MRNA]. RC TISSUE=Brain; RX PubMed=8413673; DOI=10.1038/365855a0; RA Chrivia J.C., Kwok R.P.S., Lamb N., Hagiwara M., Montminy M.R., RA Goodman R.H.; RT "Phosphorylated CREB binds specifically to the nuclear protein CBP."; RL Nature 365:855-859(1993). RN [2] 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 [3] RP INTERACTION WITH NCOA1. RX PubMed=8616895; DOI=10.1016/s0092-8674(00)81118-6; RA Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B., Lin S.-C., RA Heyman R.A., Rose D.W., Glass C.K., Rosenfeld M.G.; RT "A CBP integrator complex mediates transcriptional activation and AP-1 RT inhibition by nuclear receptors."; RL Cell 85:403-414(1996). RN [4] RP INTERACTION WITH CREB1, AND MUTAGENESIS OF ARG-600. RX PubMed=8552098; DOI=10.1128/mcb.16.2.694; RA Parker D., Ferreri K., Nakajima T., LaMorte V.J., Evans R., Koerber S.C., RA Hoeger C., Montminy M.R.; RT "Phosphorylation of CREB at Ser-133 induces complex formation with CREB- RT binding protein via a direct mechanism."; RL Mol. Cell. Biol. 16:694-703(1996). RN [5] RP INTERACTION WITH NCOA3. RX PubMed=9192892; DOI=10.1038/42652; RA Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., RA Rosenfeld M.G.; RT "The transcriptional co-activator p/CIP binds CBP and mediates nuclear- RT receptor function."; RL Nature 387:677-684(1997). RN [6] RP INTERACTION WITH MSX1 AND MSX3. RX PubMed=10215616; DOI=10.1042/bj3390751; RA Shetty S., Takahashi T., Matsui H., Ayengar R., Raghow R.; RT "Transcriptional autorepression of Msx1 gene is mediated by interactions of RT Msx1 protein with a multi-protein transcriptional complex containing TATA- RT binding protein, Sp1 and cAMP-response-element-binding protein-binding RT protein (CBP/p300)."; RL Biochem. J. 339:751-758(1999). RN [7] RP FUNCTION, INTERACTION WITH GATA1, AND MUTAGENESIS OF 1690-LYS-CYS-1691. RX PubMed=10207073; DOI=10.1128/mcb.19.5.3496; RA Hung H.L., Lau J., Kim A.Y., Weiss M.J., Blobel G.A.; RT "CREB-Binding protein acetylates hematopoietic transcription factor GATA-1 RT at functionally important sites."; RL Mol. Cell. Biol. 19:3496-3505(1999). RN [8] 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 [9] RP FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION IN A COMPLEX WITH MSX3 AND RP EP300. RC TISSUE=Muscle; 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 [10] RP INTERACTION WITH CARM1, METHYLATION AT ARG-600 AND ARG-624, AND FUNCTION. RX PubMed=11701890; DOI=10.1126/science.1065961; RA Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M., RA Evans R.M.; RT "A transcriptional switch mediated by cofactor methylation."; RL Science 294:2507-2511(2001). RN [11] RP INTERACTION WITH CITED4. RX PubMed=12504852; DOI=10.1006/geno.2002.7005; RA Yahata T., Takedatsu H., Dunwoodie S.L., Braganca J., Swingler T., RA Withington S.L., Hur J., Coser K.R., Isselbacher K.J., Bhattacharya S., RA Shioda T.; RT "Cloning of mouse Cited4, a member of the CITED family p300/CBP-binding RT transcriptional coactivators: induced expression in mammary epithelial RT cells."; RL Genomics 80:601-613(2002). RN [12] RP INTERACTION WITH MAF. RX PubMed=11943779; DOI=10.1074/jbc.m201821200; RA Chen Q., Dowhan D.H., Liang D., Moore D.D., Overbeek P.A.; RT "CREB-binding protein/p300 co-activation of crystallin gene expression."; RL J. Biol. Chem. 277:24081-24089(2002). RN [13] RP INTERACTION WITH DDX5. RX PubMed=12527917; DOI=10.1038/sj.onc.1206067; RA Rossow K.L., Janknecht R.; RT "Synergism between p68 RNA helicase and the transcriptional coactivators RT CBP and p300."; RL Oncogene 22:151-156(2003). RN [14] RP FUNCTION IN ACETYLATION OF FOXO1, AND CATALYTIC ACTIVITY. RX PubMed=15220471; DOI=10.1073/pnas.0400593101; RA Daitoku H., Hatta M., Matsuzaki H., Aratani S., Ohshima T., Miyagishi M., RA Nakajima T., Fukamizu A.; RT "Silent information regulator 2 potentiates Foxo1-mediated transcription RT through its deacetylase activity."; RL Proc. Natl. Acad. Sci. U.S.A. 101:10042-10047(2004). RN [15] RP SUMOYLATION AT LYS-999; LYS-1015; LYS-1034 AND LYS-1057, INTERACTION WITH RP DAXX, FUNCTION, AND MUTAGENESIS OF LYS-999; LYS-1015; LYS-1034; LYS-1043; RP LYS-1053; LYS-1057; LYS-1061 AND LYS-1087. RX PubMed=16287980; DOI=10.1073/pnas.0504460102; RA Kuo H.-Y., Chang C.-C., Jeng J.-C., Hu H.-M., Lin D.-Y., Maul G.G., RA Kwok R.P.S., Shih H.-M.; RT "SUMO modification negatively modulates the transcriptional activity of RT CREB-binding protein via the recruitment of Daxx."; RL Proc. Natl. Acad. Sci. U.S.A. 102:16973-16978(2005). RN [16] RP INTERACTION WITH DDX17. RX PubMed=17226766; DOI=10.1002/jcb.21250; RA Shin S., Janknecht R.; RT "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the RT coactivators p300 and P/CAF."; RL J. Cell. Biochem. 101:1252-1265(2007). RN [17] RP INTERACTION WITH ZCCHC12. RX PubMed=18160706; DOI=10.1128/mcb.01038-07; RA Cho G., Lim Y., Zand D., Golden J.A.; RT "Sizn1 is a novel protein that functions as a transcriptional coactivator RT of bone morphogenic protein signaling."; RL Mol. Cell. Biol. 28:1565-1572(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-2064 AND SER-2350, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and RC 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 [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-656; LYS-1217; LYS-1596; LYS-1598 RP AND LYS-1745, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [20] RP FUNCTION, AND INTERACTION WITH BMAL1. RX PubMed=24737000; DOI=10.1371/journal.pbio.1001840; RA Anafi R.C., Lee Y., Sato T.K., Venkataraman A., Ramanathan C., RA Kavakli I.H., Hughes M.E., Baggs J.E., Growe J., Liu A.C., Kim J., RA Hogenesch J.B.; RT "Machine learning helps identify CHRONO as a circadian clock component."; RL PLoS Biol. 12:E1001840-E1001840(2014). RN [21] RP INTERACTION WITH ACSS2. RX PubMed=28552616; DOI=10.1016/j.molcel.2017.04.026; RA Li X., Yu W., Qian X., Xia Y., Zheng Y., Lee J.H., Li W., Lyu J., Rao G., RA Zhang X., Qian C.N., Rozen S.G., Jiang T., Lu Z.; RT "Nucleus-Translocated ACSS2 Promotes Gene Transcription for Lysosomal RT Biogenesis and Autophagy."; RL Mol. Cell 66:684-697(2017). RN [22] RP STRUCTURE BY NMR OF 340-439 IN COMPLEX WITH 220-269 OF CITED2 AND ZINC RP IONS. RX PubMed=14594809; DOI=10.1074/jbc.m310348200; RA De Guzman R.N., Martinez-Yamout M.A., Dyson H.J., Wright P.E.; RT "Interaction of the TAZ1 domain of the CREB-binding protein with the RT activation domain of CITED2: regulation by competition between RT intrinsically unstructured ligands for non-identical binding sites."; RL J. Biol. Chem. 279:3042-3049(2004). CC -!- FUNCTION: Acetylates histones, giving a specific tag for CC transcriptional activation (PubMed:11115394). Mediates acetylation of CC histone H3 at 'Lys-18' and 'Lys-27' (H3K18ac and H3K27ac, respectively) CC (By similarity). Also acetylates non-histone proteins, like DDX21, FBL, CC IRF2, MAFG, NCOA3, POLR1E/PAF53 and FOXO1 (PubMed:10207073, CC PubMed:11701890, PubMed:16287980, PubMed:15220471). Binds specifically CC to phosphorylated CREB and enhances its transcriptional activity toward CC cAMP-responsive genes (By similarity). Acts as a coactivator of ALX1 CC (By similarity). Acts as a circadian transcriptional coactivator which CC enhances the activity of the circadian transcriptional activators: CC NPAS2-BMAL1 and CLOCK-BMAL1 heterodimers (By similarity). Acetylates CC PCNA; acetylation promotes removal of chromatin-bound PCNA and its CC degradation during nucleotide excision repair (NER) (PubMed:24737000). CC Acetylates POLR1E/PAF53, leading to decreased association of RNA CC polymerase I with the rDNA promoter region and coding region (By CC similarity). Acetylates DDX21, thereby inhibiting DDX21 helicase CC activity (By similarity). Acetylates FBL, preventing methylation of CC 'Gln-105' of histone H2A (H2AQ104me) (By similarity). Functions as a CC transcriptional coactivator for SMAD4 in the TGF-beta signaling pathway CC (By similarity). {ECO:0000250|UniProtKB:Q92793, CC ECO:0000269|PubMed:10207073, ECO:0000269|PubMed:11115394, CC ECO:0000269|PubMed:11701890, ECO:0000269|PubMed:15220471, CC ECO:0000269|PubMed:16287980, ECO:0000269|PubMed:24737000}. 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:11115394}; 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:15220471}; 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 DHX9 (via N-terminus); this CC interaction mediates association with RNA polymerase II holoenzyme and CC stimulates CREB-dependent transcriptional activation (By similarity). CC Interacts (via transactivation domain and C-terminus) with PCNA; the CC interaction occurs on chromatin in UV-irradiated damaged cells (By CC similarity). Found in a complex containing NCOA2; NCOA3; IKKA; IKKB and CC IKBKG. Probably part of a complex with HIF1A and EP300. The TAZ-type 1 CC domain interacts with HIF1A. Interacts with SRCAP, ELF3, MLLT7/FOXO4, CC N4BP2, NCOA6, PCAF, PELP1, PML, SMAD1, SMAD2, SMAD3, SPIB and TRERF1. CC Interacts with KLF1; the interaction results in acetylation and CC enhancement of transcriptional activity of KLF1. Interacts with MAFG; CC the interaction acetylates MAFG in the basic region and stimulates NFE2 CC transcriptional activity through increasing its DNA-binding activity. CC Interacts with IRF2; the interaction acetylates IRF2 and regulates its CC activity on the H4 promoter. Interacts with IRF3 (when phosphorylated); CC forming the dsRNA-activated factor 1 (DRAF1), a complex which activates CC the transcription of the type I interferon genes (By similarity). CC Interacts (via N-terminus) with SS18L1/CREST (via C-terminus). CC Interacts with FOXO1; the interaction acetylates FOXO1 and inhibits its CC transcriptional activity. Interacts with MECOM and MTDH. Interacts with CC ASF1A and ASF1B; this promotes histone acetylation. Interacts with CC acetylated TP53/p53 and with the acetylated histones H3 and H4 (By CC similarity). Interacts with CITED1 (via C-terminus). Interacts with CC GATA1; the interaction results in acetylation and enhancement of CC transcriptional activity of GATA1. Interacts with MAF, CARM1. NCOA3, CC ZCCHC12, DDX17, DDX5 and CITED4 (C-terminal region). Interacts with CC phosphorylated CREB1. Interacts with DAXX; the interaction is dependent CC on CBP sumoylation and results in suppression of the transcriptional CC activity via recruitment of HDAC2 to DAXX. Interacts with NPAS2, CLOCK CC and BMAL1. Interacts with SMAD4; negatively regulated by ZBTB7A (By CC similarity). Forms a complex with KMT2A and CREB1 (By similarity). CC Interacts with DDX3X; this interaction may facilitate HNF4A acetylation CC (By similarity). Interacts with MSX1; the interaction may inhibit MSX1 CC autoinactivation (PubMed:10215616). Interacts with MSX3 CC (PubMed:10215616). Interacts with ACSS2 (PubMed:28552616). CC {ECO:0000250|UniProtKB:Q92793, ECO:0000269|PubMed:10207073, CC ECO:0000269|PubMed:10215616, ECO:0000269|PubMed:10722728, CC ECO:0000269|PubMed:11115394, ECO:0000269|PubMed:11701890, CC ECO:0000269|PubMed:11943779, ECO:0000269|PubMed:12504852, CC ECO:0000269|PubMed:12527917, ECO:0000269|PubMed:14594809, CC ECO:0000269|PubMed:16287980, ECO:0000269|PubMed:17226766, CC ECO:0000269|PubMed:18160706, ECO:0000269|PubMed:24737000, CC ECO:0000269|PubMed:28552616, ECO:0000269|PubMed:8552098, CC ECO:0000269|PubMed:8616895, ECO:0000269|PubMed:9192892}. CC -!- INTERACTION: CC P45481; Q9WTL8-4: Bmal1; NbExp=2; IntAct=EBI-296306, EBI-644568; CC P45481; Q02248: Ctnnb1; NbExp=3; IntAct=EBI-296306, EBI-397872; CC P45481; P27577: Ets1; NbExp=3; IntAct=EBI-296306, EBI-4289053; CC P45481; Q60749: Khdrbs1; NbExp=7; IntAct=EBI-296306, EBI-519077; CC P45481; Q04207: Rela; NbExp=9; IntAct=EBI-296306, EBI-644400; CC P45481; Q62318-1: Trim28; NbExp=2; IntAct=EBI-296306, EBI-6876996; CC P45481; P41182: BCL6; Xeno; NbExp=2; IntAct=EBI-296306, EBI-765407; CC P45481; O60566: BUB1B; Xeno; NbExp=3; IntAct=EBI-296306, EBI-1001438; CC P45481; P61201: COPS2; Xeno; NbExp=2; IntAct=EBI-296306, EBI-1050386; CC P45481; P17844: DDX5; Xeno; NbExp=3; IntAct=EBI-296306, EBI-351962; CC P45481; P35637: FUS; Xeno; NbExp=4; IntAct=EBI-296306, EBI-400434; CC P45481; P62805: H4C9; Xeno; NbExp=2; IntAct=EBI-296306, EBI-302023; CC P45481; Q03164: KMT2A; Xeno; NbExp=7; IntAct=EBI-296306, EBI-591370; CC P45481; O95863: SNAI1; Xeno; NbExp=7; IntAct=EBI-296306, EBI-1045459; CC P45481; P04637: TP53; Xeno; NbExp=10; IntAct=EBI-296306, EBI-366083; CC P45481; P03254; Xeno; NbExp=3; IntAct=EBI-296306, EBI-8599077; CC P45481; P03255; Xeno; NbExp=2; IntAct=EBI-296306, EBI-2603114; CC P45481; P88946; Xeno; NbExp=6; IntAct=EBI-296306, EBI-936023; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92793}. CC Nucleus. Note=Recruited to nuclear bodies by SS18L1/CREST. In the CC presence of ALX1 relocalizes from the cytoplasm to the nucleus. CC {ECO:0000250|UniProtKB:Q92793}. CC -!- PTM: Methylation of the KIX domain by CARM1 blocks association with CC CREB. This results in the blockade of CREB signaling, and in activation CC of apoptotic response. {ECO:0000269|PubMed:11701890}. CC -!- PTM: Phosphorylated by CHUK/IKKA at Ser-1383 and Ser-1387; these CC phosphorylations promote cell growth by switching the binding CC preference of CREBBP from TP53 to NF-kappa-B. CC {ECO:0000250|UniProtKB:Q92793}. CC -!- PTM: Sumoylation negatively regulates transcriptional activity via the CC recruitment of DAAX. {ECO:0000269|PubMed:16287980}. CC -!- PTM: Autoacetylation is required for binding to protein substrates, CC such as acetylated histones and acetylated TP53/p53. Autoacetylation is CC induced by glucose and fatty acids. {ECO:0000250|UniProtKB:Q92793}. 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; S66385; AAB28651.1; -; mRNA. DR EMBL; AC132380; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS27915.1; -. DR PIR; S39161; S39161. DR PDB; 1F81; NMR; -; A=1764-1850. DR PDB; 1JJS; NMR; -; A=2067-2112. DR PDB; 1KBH; NMR; -; B=2059-2117. DR PDB; 1KDX; NMR; -; A=586-666. DR PDB; 1L8C; NMR; -; A=345-439. DR PDB; 1R8U; NMR; -; B=340-439. DR PDB; 1SB0; NMR; -; A=586-672. DR PDB; 1TOT; NMR; -; A=1700-1751. DR PDB; 1U2N; NMR; -; A=340-439. DR PDB; 2AGH; NMR; -; B=586-672. DR PDB; 2C52; NMR; -; A=2059-2117. DR PDB; 2KA4; NMR; -; A=340-439. DR PDB; 2KA6; NMR; -; A=1764-1855. DR PDB; 2KKJ; NMR; -; A=2059-2117. DR PDB; 2L14; NMR; -; A=2059-2117. DR PDB; 2LQH; NMR; -; A=586-672. DR PDB; 2LQI; NMR; -; A=586-672. DR PDB; 2LWW; NMR; -; A=340-439. DR PDB; 4I9O; X-ray; 2.00 A; A=586-672. DR PDB; 5HOU; NMR; -; A=340-439. DR PDB; 5HP0; NMR; -; A=1764-1857. DR PDB; 5HPD; NMR; -; A=1764-1855. DR PDB; 5U4K; NMR; -; A=586-672. DR PDB; 5U7G; X-ray; 2.40 A; A/B=1079-1556. DR PDB; 5W0I; X-ray; 1.43 A; A=1083-1198. DR PDB; 6DMX; X-ray; 2.80 A; B/D/G/I=586-672. DR PDB; 6DNQ; X-ray; 2.35 A; B/D=586-672. DR PDB; 7LVS; X-ray; 2.02 A; B=340-439. DR PDBsum; 1F81; -. DR PDBsum; 1JJS; -. DR PDBsum; 1KBH; -. DR PDBsum; 1KDX; -. DR PDBsum; 1L8C; -. DR PDBsum; 1R8U; -. DR PDBsum; 1SB0; -. DR PDBsum; 1TOT; -. DR PDBsum; 1U2N; -. DR PDBsum; 2AGH; -. DR PDBsum; 2C52; -. DR PDBsum; 2KA4; -. DR PDBsum; 2KA6; -. DR PDBsum; 2KKJ; -. DR PDBsum; 2L14; -. DR PDBsum; 2LQH; -. DR PDBsum; 2LQI; -. DR PDBsum; 2LWW; -. DR PDBsum; 4I9O; -. DR PDBsum; 5HOU; -. DR PDBsum; 5HP0; -. DR PDBsum; 5HPD; -. DR PDBsum; 5U4K; -. DR PDBsum; 5U7G; -. DR PDBsum; 5W0I; -. DR PDBsum; 6DMX; -. DR PDBsum; 6DNQ; -. DR PDBsum; 7LVS; -. DR AlphaFoldDB; P45481; -. DR BMRB; P45481; -. DR SASBDB; P45481; -. DR SMR; P45481; -. DR CORUM; P45481; -. DR DIP; DIP-5974N; -. DR IntAct; P45481; 39. DR MINT; P45481; -. DR STRING; 10090.ENSMUSP00000023165; -. DR GlyGen; P45481; 7 sites, 1 O-linked glycan (7 sites). DR iPTMnet; P45481; -. DR PhosphoSitePlus; P45481; -. DR SwissPalm; P45481; -. DR EPD; P45481; -. DR jPOST; P45481; -. DR MaxQB; P45481; -. DR PaxDb; 10090-ENSMUSP00000023165; -. DR ProteomicsDB; 281475; -. DR Pumba; P45481; -. DR AGR; MGI:1098280; -. DR MGI; MGI:1098280; Crebbp. DR eggNOG; KOG1778; Eukaryota. DR InParanoid; P45481; -. 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-350054; Notch-HLH transcription pathway. DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha. DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling. DR Reactome; R-MMU-8866907; Activation of the TFAP2 (AP-2) family of transcription factors. DR Reactome; R-MMU-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells. DR Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling. DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression. 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-9707564; Cytoprotection by HMOX1. DR Reactome; R-MMU-9759194; Nuclear events mediated by NFE2L2. DR ChiTaRS; Crebbp; mouse. DR EvolutionaryTrace; P45481; -. DR PRO; PR:P45481; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P45481; Protein. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI. DR GO; GO:0016604; C:nuclear body; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0000940; C:outer kinetochore; IDA:MGI. DR GO; GO:0016605; C:PML body; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA. DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:MGI. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0016407; F:acetyltransferase activity; ISS:UniProtKB. DR GO; GO:0008140; F:cAMP response element binding protein binding; IPI:CAFA. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central. DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB. DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB. DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:MGI. 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:0060090; F:molecular adaptor activity; EXP:DisProt. DR GO; GO:0043426; F:MRF binding; ISS:UniProtKB. DR GO; GO:0002039; F:p53 binding; ISO:MGI. DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISO:MGI. DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI. DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB. DR GO; GO:0046332; F:SMAD binding; ISO:MGI. DR GO; GO:0001093; F:TFIIB-class transcription factor binding; IPI:MGI. DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI. DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI. DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI. DR GO; GO:0008270; F:zinc ion binding; IMP:CAFA. DR GO; GO:0048148; P:behavioral response to cocaine; ISO:MGI. DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:MGI. 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:0098586; P:cellular response to virus; IMP:CAFA. DR GO; GO:0060325; P:face morphogenesis; IMP:ARUK-UCL. DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:MGI. DR GO; GO:0007616; P:long-term memory; ISO:MGI. DR GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; ISS:UniProtKB. DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:CAFA. DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0048525; P:negative regulation of viral process; IMP:CAFA. DR GO; GO:0038061; P:non-canonical NF-kappaB signal transduction; ISO:MGI. DR GO; GO:0060355; P:positive regulation of cell adhesion molecule production; ISO:MGI. DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI. DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; TAS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI. DR GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; ISO:MGI. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI. DR GO; GO:0031648; P:protein destabilization; ISS:UniProtKB. DR GO; GO:0036211; P:protein modification process; ISO:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI. 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 DisProt; DP00348; -. 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 IDEAL; IID50008; -. 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 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Acyltransferase; Biological rhythms; KW Bromodomain; Cytoplasm; Isopeptide bond; Metal-binding; Methylation; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT CHAIN 2..2441 FT /note="Histone lysine acetyltransferase CREBBP" FT /id="PRO_0000211191" FT DOMAIN 586..665 FT /note="KIX" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00311" FT DOMAIN 1104..1176 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 1324..1701 FT /note="CBP/p300-type HAT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065" FT ZN_FING 346..432 FT /note="TAZ-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203" FT ZN_FING 1703..1751 FT /note="ZZ-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT ZN_FING 1766..1847 FT /note="TAZ-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203" FT REGION 1..29 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 73..168 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 226..409 FT /note="Interaction with SRCAP" FT /evidence="ECO:0000250" FT REGION 261..292 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 792..1088 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1125..1171 FT /note="Interaction with histone" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT REGION 1163..1181 FT /note="Interaction with ASF1A" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT REGION 1434..1436 FT /note="Interaction with histone" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT REGION 1557..1616 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1875..1959 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2112..2421 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 262..292 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 792..821 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 850..864 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 875..889 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 890..930 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 939..991 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 999..1068 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1557..1572 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1589..1603 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1884..1917 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1922..1939 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1941..1955 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2112..2146 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2169..2265 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2276..2349 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2350..2377 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2394..2421 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 362 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 366 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 379 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 384 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 393 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 397 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 403 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 408 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 417 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT BINDING 421 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT BINDING 426 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT BINDING 429 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT BINDING 1435..1437 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1447..1448 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1494 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1499 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1503 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000250|UniProtKB:Q09472" FT BINDING 1708 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1711 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1721 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1724 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1730 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1733 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1739 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 1741 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 120 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 219 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 600 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000305|PubMed:11701890" FT MOD_RES 624 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000305|PubMed:11701890" FT MOD_RES 656 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1015 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1031 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1077 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1217 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1383 FT /note="Phosphoserine; by IKKA" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1387 FT /note="Phosphoserine; by IKKA" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1584 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1592 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1593 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1596 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1598 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1742 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 1745 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 1764 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 2064 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2077 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 2080 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92793" FT MOD_RES 2350 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT CROSSLNK 999 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:16287980" FT CROSSLNK 1034 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:16287980" FT CROSSLNK 1057 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:16287980" FT MUTAGEN 600 FT /note="R->N: Abolishes binding to CREB." FT /evidence="ECO:0000269|PubMed:8552098" FT MUTAGEN 999 FT /note="K->R: Enhanced transcriptional activity. No FT sumoylation, loss of recruitment of HDAC2 to DAAX and FT greatly enhanced transcriptional activity; when associated FT with R-1034 and R-1057." FT /evidence="ECO:0000269|PubMed:16287980" FT MUTAGEN 1015 FT /note="K->R: No change in sumoylation." FT /evidence="ECO:0000269|PubMed:16287980" FT MUTAGEN 1034 FT /note="K->R: Enhanced transcriptional activity. No FT sumoylation, loss of recruitment of HDAC2 to DAAX and FT greatly enhanced transcriptional activity; when associated FT with R-999 and R-1057." FT /evidence="ECO:0000269|PubMed:16287980" FT MUTAGEN 1043 FT /note="K->R: No change in sumoylation." FT /evidence="ECO:0000269|PubMed:16287980" FT MUTAGEN 1053 FT /note="K->R: No change in sumoylation." FT /evidence="ECO:0000269|PubMed:16287980" FT MUTAGEN 1057 FT /note="K->R: Enhanced transcriptional activity. No FT sumoylation, loss of recruitment of HDAC2 to DAAX and FT greatly enhanced transcriptional activity; when associated FT with R-999 and R-1034." FT /evidence="ECO:0000269|PubMed:16287980" FT MUTAGEN 1061 FT /note="K->R: No change in sumoylation." FT /evidence="ECO:0000269|PubMed:16287980" FT MUTAGEN 1087 FT /note="K->R: No change in sumoylation." FT /evidence="ECO:0000269|PubMed:16287980" FT MUTAGEN 1690..1691 FT /note="LC->KL: Abolishes histone acetyltransferase FT activity." FT /evidence="ECO:0000269|PubMed:10207073" FT CONFLICT 400 FT /note="G -> P (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 530 FT /note="I -> V (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 670 FT /note="S -> T (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 826 FT /note="V -> E (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 978 FT /note="S -> T (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 1159 FT /note="W -> R (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 1239 FT /note="E -> G (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 1417 FT /note="N -> D (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 1429 FT /note="R -> C (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 1466 FT /note="G -> V (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 1470 FT /note="G -> A (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 1850..1851 FT /note="KL -> NV (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 1859 FT /note="R -> C (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 1987 FT /note="A -> D (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 2060 FT /note="P -> N (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT CONFLICT 2381 FT /note="S -> T (in Ref. 1; AAB28651)" FT /evidence="ECO:0000305" FT TURN 343..345 FT /evidence="ECO:0007829|PDB:2KA4" FT HELIX 347..373 FT /evidence="ECO:0007829|PDB:7LVS" FT STRAND 374..376 FT /evidence="ECO:0007829|PDB:1U2N" FT HELIX 384..394 FT /evidence="ECO:0007829|PDB:7LVS" FT HELIX 400..402 FT /evidence="ECO:0007829|PDB:7LVS" FT HELIX 408..420 FT /evidence="ECO:0007829|PDB:7LVS" FT TURN 423..425 FT /evidence="ECO:0007829|PDB:2LWW" FT TURN 427..429 FT /evidence="ECO:0007829|PDB:7LVS" FT HELIX 430..433 FT /evidence="ECO:0007829|PDB:7LVS" FT HELIX 436..438 FT /evidence="ECO:0007829|PDB:1R8U" FT HELIX 590..594 FT /evidence="ECO:0007829|PDB:4I9O" FT HELIX 597..611 FT /evidence="ECO:0007829|PDB:4I9O" FT TURN 617..619 FT /evidence="ECO:0007829|PDB:4I9O" FT HELIX 622..642 FT /evidence="ECO:0007829|PDB:4I9O" FT HELIX 646..664 FT /evidence="ECO:0007829|PDB:4I9O" FT TURN 667..671 FT /evidence="ECO:0007829|PDB:1SB0" FT HELIX 1088..1103 FT /evidence="ECO:0007829|PDB:5W0I" FT TURN 1106..1109 FT /evidence="ECO:0007829|PDB:5W0I" FT HELIX 1110..1112 FT /evidence="ECO:0007829|PDB:5W0I" FT HELIX 1118..1121 FT /evidence="ECO:0007829|PDB:5W0I" FT HELIX 1126..1129 FT /evidence="ECO:0007829|PDB:5W0I" FT HELIX 1136..1144 FT /evidence="ECO:0007829|PDB:5W0I" FT HELIX 1151..1168 FT /evidence="ECO:0007829|PDB:5W0I" FT HELIX 1174..1197 FT /evidence="ECO:0007829|PDB:5W0I" FT STRAND 1281..1283 FT /evidence="ECO:0007829|PDB:5U7G" FT TURN 1285..1287 FT /evidence="ECO:0007829|PDB:5U7G" FT STRAND 1290..1292 FT /evidence="ECO:0007829|PDB:5U7G" FT HELIX 1293..1296 FT /evidence="ECO:0007829|PDB:5U7G" FT TURN 1300..1302 FT /evidence="ECO:0007829|PDB:5U7G" FT HELIX 1310..1314 FT /evidence="ECO:0007829|PDB:5U7G" FT HELIX 1334..1350 FT /evidence="ECO:0007829|PDB:5U7G" FT STRAND 1358..1371 FT /evidence="ECO:0007829|PDB:5U7G" FT HELIX 1374..1380 FT /evidence="ECO:0007829|PDB:5U7G" FT TURN 1381..1384 FT /evidence="ECO:0007829|PDB:5U7G" FT STRAND 1388..1403 FT /evidence="ECO:0007829|PDB:5U7G" FT STRAND 1406..1418 FT /evidence="ECO:0007829|PDB:5U7G" FT STRAND 1429..1437 FT /evidence="ECO:0007829|PDB:5U7G" FT HELIX 1444..1446 FT /evidence="ECO:0007829|PDB:5U7G" FT HELIX 1447..1465 FT /evidence="ECO:0007829|PDB:5U7G" FT STRAND 1469..1473 FT /evidence="ECO:0007829|PDB:5U7G" FT STRAND 1483..1487 FT /evidence="ECO:0007829|PDB:5U7G" FT HELIX 1497..1513 FT /evidence="ECO:0007829|PDB:5U7G" FT STRAND 1518..1522 FT /evidence="ECO:0007829|PDB:5U7G" FT HELIX 1523..1530 FT /evidence="ECO:0007829|PDB:5U7G" FT HELIX 1535..1537 FT /evidence="ECO:0007829|PDB:5U7G" FT HELIX 1545..1555 FT /evidence="ECO:0007829|PDB:5U7G" FT TURN 1709..1711 FT /evidence="ECO:0007829|PDB:1TOT" FT STRAND 1713..1726 FT /evidence="ECO:0007829|PDB:1TOT" FT HELIX 1731..1737 FT /evidence="ECO:0007829|PDB:1TOT" FT STRAND 1741..1746 FT /evidence="ECO:0007829|PDB:1TOT" FT HELIX 1765..1785 FT /evidence="ECO:0007829|PDB:1F81" FT HELIX 1794..1808 FT /evidence="ECO:0007829|PDB:1F81" FT HELIX 1812..1815 FT /evidence="ECO:0007829|PDB:1F81" FT HELIX 1818..1833 FT /evidence="ECO:0007829|PDB:1F81" FT STRAND 1840..1843 FT /evidence="ECO:0007829|PDB:5HPD" FT HELIX 1844..1849 FT /evidence="ECO:0007829|PDB:1F81" FT STRAND 2061..2064 FT /evidence="ECO:0007829|PDB:1KBH" FT HELIX 2068..2075 FT /evidence="ECO:0007829|PDB:1JJS" FT STRAND 2076..2079 FT /evidence="ECO:0007829|PDB:1JJS" FT HELIX 2088..2091 FT /evidence="ECO:0007829|PDB:1JJS" FT HELIX 2097..2100 FT /evidence="ECO:0007829|PDB:1JJS" FT HELIX 2102..2104 FT /evidence="ECO:0007829|PDB:1JJS" FT STRAND 2106..2108 FT /evidence="ECO:0007829|PDB:1JJS" SQ SEQUENCE 2441 AA; 265494 MW; D89AF52B7BD33347 CRC64; MAENLLDGPP NPKRAKLSSP GFSANDNTDF GSLFDLENDL PDELIPNGEL SLLNSGNLVP DAASKHKQLS ELLRGGSGSS INPGIGNVSA SSPVQQGLGG QAQGQPNSTN MASLGAMGKS PLNQGDSSTP NLPKQAASTS GPTPPASQAL NPQAQKQVGL VTSSPATSQT GPGICMNANF NQTHPGLLNS NSGHSLMNQA QQGQAQVMNG SLGAAGRGRG AGMPYPAPAM QGATSSVLAE TLTQVSPQMA GHAGLNTAQA GGMTKMGMTG TTSPFGQPFS QTGGQQMGAT GVNPQLASKQ SMVNSLPAFP TDIKNTSVTT VPNMSQLQTS VGIVPTQAIA TGPTADPEKR KLIQQQLVLL LHAHKCQRRE QANGEVRACS LPHCRTMKNV LNHMTHCQAG KACQVAHCAS SRQIISHWKN CTRHDCPVCL PLKNASDKRN QQTILGSPAS GIQNTIGSVG AGQQNATSLS NPNPIDPSSM QRAYAALGLP YMNQPQTQLQ PQVPGQQPAQ PPAHQQMRTL NALGNNPMSI PAGGITTDQQ PPNLISESAL PTSLGATNPL MNDGSNSGNI GSLSTIPTAA PPSSTGVRKG WHEHVTQDLR SHLVHKLVQA IFPTPDPAAL KDRRMENLVA YAKKVEGDMY ESANSRDEYY HLLAEKIYKI QKELEEKRRS RLHKQGILGN QPALPASGAQ PPVIPPAQSV RPPNGPLPLP VNRMQVSQGM NSFNPMSLGN VQLPQAPMGP RAASPMNHSV QMNSMASVPG MAISPSRMPQ PPNMMGTHAN NIMAQAPTQN QFLPQNQFPS SSGAMSVNSV GMGQPAAQAG VSQGQVPGAA LPNPLNMLAP QASQLPCPPV TQSPLHPTPP PASTAAGMPS LQHPTAPGMT PPQPAAPTQP STPVSSGQTP TPTPGSVPSA AQTQSTPTVQ AAAQAQVTPQ PQTPVQPPSV ATPQSSQQQP TPVHTQPPGT PLSQAAASID NRVPTPSSVT SAETSSQQPG PDVPMLEMKT EVQTDDAEPE PTESKGEPRS EMMEEDLQGS SQVKEETDTT EQKSEPMEVE EKKPEVKVEA KEEEENSSND TASQSTSPSQ PRKKIFKPEE LRQALMPTLE ALYRQDPESL PFRQPVDPQL LGIPDYFDIV KNPMDLSTIK RKLDTGQYQE PWQYVDDVWL MFNNAWLYNR KTSRVYKFCS KLAEVFEQEI DPVMQSLGYC CGRKYEFSPQ TLCCYGKQLC TIPRDAAYYS YQNRYHFCEK CFTEIQGENV TLGDDPSQPQ TTISKDQFEK KKNDTLDPEP FVDCKECGRK MHQICVLHYD IIWPSGFVCD NCLKKTGRPR KENKFSAKRL QTTRLGNHLE DRVNKFLRRQ NHPEAGEVFV RVVASSDKTV EVKPGMKSRF VDSGEMSESF PYRTKALFAF EEIDGVDVCF FGMHVQNTAL IAPHQIQGRV YISYLDSIHF FRPRCLRTAV YHEILIGYLE YVKKLGYVTG HIWACPPSEG DDYIFHCHPP DQKIPKPKRL QEWYKKMLDK AFAERIINDY KDIFKQANED RLTSAKELPY FEGDFWPNVL EESIKELEQE EEERKKEEST AASETPEGSQ GDSKNAKKKN NKKTNKNKSS ISRANKKKPS MPNVSNDLSQ KLYATMEKHK EVFFVIHLHA GPVISTQPPI VDPDPLLSCD LMDGRDAFLT LARDKHWEFS SLRRSKWSTL CMLVELHTQG QDRFVYTCNE CKHHVETRWH CTVCEDYDLC INCYNTKSHT HKMVKWGLGL DDEGSSQGEP QSKSPQESRR LSIQRCIQSL VHACQCRNAN CSLPSCQKMK RVVQHTKGCK RKTNGGCPVC KQLIALCCYH AKHCQENKCP VPFCLNIKHK LRQQQIQHRL QQAQLMRRRM ATMNTRNVPQ QSLPSPTSAP PGTPTQQPST PQTPQPPAQP QPSPVNMSPA GFPNVARTQP PTIVSAGKPT NQVPAPPPPA QPPPAAVEAA RQIEREAQQQ QHLYRANINN GMPPGRAGMG TPGSQMTPVG LNVPRPNQVS GPVMSSMPPG QWQQAPIPQQ QPMPGMPRPV MSMQAQAAVA GPRMPNVQPP RSISPSALQD LLRTLKSPSS PQQQQQVLNI LKSNPQLMAA FIKQRTAKYV ANQPGMQPQP GLQSQPGMQP QPGMHQQPSL QNLNAMQAGV PRPGVPPPQP AMGGLNPQGQ ALNIMNPGHN PNMTNMNPQY REMVRRQLLQ HQQQQQQQQQ QQQQQQNSAS LAGGMAGHSQ FQQPQGPGGY APAMQQQRMQ QHLPIQGSSM GQMAAPMGQL GQMGQPGLGA DSTPNIQQAL QQRILQQQQM KQQIGSPGQP NPMSPQQHML SGQPQASHLP GQQIATSLSN QVRSPAPVQS PRPQSQPPHS SPSPRIQPQP SPHHVSPQTG SPHPGLAVTM ASSMDQGHLG NPEQSAMLPQ LNTPNRSALS SELSLVGDTT GDTLEKFVEG L //