CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024655
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Histone acetyltransferase p300 
Protein Synonyms/Alias
 p300 HAT; E1A-associated protein p300 
Gene Name
 Ep300 
Gene Synonyms/Alias
 P300 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
14EPGPPSAKRPKLSSPacetylation[1]
79QDAASKHKQLSELLRacetylation[2]
292LSPFAMDKKAVPGGGacetylation[1]
980QEVKMESKMEVDKPEacetylation[2]
1019EERGPELKTDGKEEEsumoylation[3]
1023PELKTDGKEEEEQPSsumoylation[3]
1179QTLCCYGKQLCTIPRacetylation[1, 2, 4]
1498EDRLTSAKELPYFEGacetylation[1, 2, 5]
1541NESTDVTKGDSKNAKacetylation[4, 5, 6]
1545DVTKGDSKNAKKKNNacetylation[4, 5]
1550DSKNAKKKNNKKTSKacetylation[6]
1553NAKKKNNKKTSKNKSacetylation[4, 6]
1554AKKKNNKKTSKNKSSacetylation[4, 6]
1557KNNKKTSKNKSSLSRacetylation[2, 4, 5, 6]
1559NKKTSKNKSSLSRGNacetylation[2, 4, 5, 6]
1582VSNDLSQKLYATMEKacetylation[1]
1589KLYATMEKHKEVFFVacetylation[1, 2, 4]
1673VYTCNECKHHVETRWacetylation[2, 4]
1703NTKNHDHKMEKLGLGacetylation[5]
1706NHDHKMEKLGLGLDDacetylation[1, 2, 5]
1768KRVVQHTKGCKRKTNacetylation[2]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] P300 transcriptional repression is mediated by SUMO modification.
 Girdwood D, Bumpass D, Vaughan OA, Thain A, Anderson LA, Snowden AW, Garcia-Wilson E, Perkins ND, Hay RT.
 Mol Cell. 2003 Apr;11(4):1043-54. [PMID: 12718889]
 [4] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [5] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758] 
Functional Description
 Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Also functions as acetyltransferase for nonhistone targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator in the presence of CREBBP. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Acetylates FOXO1 and enhances its transcriptional activity (By similarity). 
Sequence Annotation
 DOMAIN 567 646 KIX.
 DOMAIN 1066 1138 Bromo.
 ZN_FING 332 418 TAZ-type 1.
 ZN_FING 1663 1706 ZZ-type.
 ZN_FING 1727 1808 TAZ-type 2.
 REGION 2 139 Interaction with ALX1 (By similarity).
 REGION 1016 1028 CRD1; mediates transcriptional repression
 REGION 2042 2240 Interaction with NCOA2 (By similarity).
 MOTIF 11 17 Nuclear localization signal (Potential).
 METAL 348 348 Zinc 1 (By similarity).
 METAL 352 352 Zinc 1 (By similarity).
 METAL 365 365 Zinc 1 (By similarity).
 METAL 370 370 Zinc 1 (By similarity).
 METAL 379 379 Zinc 2 (By similarity).
 METAL 383 383 Zinc 2 (By similarity).
 METAL 389 389 Zinc 2 (By similarity).
 METAL 394 394 Zinc 2 (By similarity).
 METAL 403 403 Zinc 3 (By similarity).
 METAL 407 407 Zinc 3 (By similarity).
 METAL 412 412 Zinc 3 (By similarity).
 METAL 415 415 Zinc 3 (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 89 89 Phosphoserine; by AMPK (By similarity).
 MOD_RES 286 286 Phosphoserine (By similarity).
 MOD_RES 581 581 Omega-N-methylated arginine; by CARM1 (By
 MOD_RES 605 605 Omega-N-methylated arginine; by CARM1 (By
 MOD_RES 637 637 N6-acetyllysine (By similarity).
 MOD_RES 885 885 Phosphothreonine (By similarity).
 MOD_RES 887 887 Phosphothreonine (By similarity).
 MOD_RES 976 976 N6-acetyllysine (By similarity).
 MOD_RES 980 980 N6-acetyllysine (By similarity).
 MOD_RES 1019 1019 N6-acetyllysine; alternate (By
 MOD_RES 1023 1023 N6-acetyllysine; alternate (By
 MOD_RES 1037 1037 Phosphoserine (By similarity).
 MOD_RES 1102 1102 N6-acetyllysine (By similarity).
 MOD_RES 1335 1335 N6-acetyllysine (By similarity).
 MOD_RES 1472 1472 N6-acetyllysine (By similarity).
 MOD_RES 1498 1498 N6-acetyllysine; by autocatalysis (By
 MOD_RES 1541 1541 N6-acetyllysine (By similarity).
 MOD_RES 1545 1545 N6-acetyllysine (By similarity).
 MOD_RES 1548 1548 N6-acetyllysine; by autocatalysis (By
 MOD_RES 1553 1553 N6-acetyllysine; by autocatalysis (By
 MOD_RES 1554 1554 N6-acetyllysine (By similarity).
 MOD_RES 1557 1557 N6-acetyllysine (By similarity).
 MOD_RES 1559 1559 N6-acetyllysine; by autocatalysis (By
 MOD_RES 1582 1582 N6-acetyllysine (By similarity).
 MOD_RES 1589 1589 N6-acetyllysine (By similarity).
 MOD_RES 1673 1673 N6-acetyllysine (By similarity).
 MOD_RES 1733 1733 Phosphoserine (By similarity).
 MOD_RES 1856 1856 Phosphothreonine (By similarity).
 MOD_RES 1858 1858 Phosphothreonine (By similarity).
 MOD_RES 2143 2143 Asymmetric dimethylarginine; by CARM1;
 MOD_RES 2143 2143 Citrulline; by PADI4; alternate (By
 CROSSLNK 1019 1019 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1023 1023 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Bromodomain; Cell cycle; Citrullination; Coiled coil; Complete proteome; Cytoplasm; Differentiation; Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2415 AA 
Protein Sequence
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD 60
ISQLQTSLGI VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQAMASQAQQ NSPGLSLINS 120
MVKSPMAQTG LTSPNMGIGS SGPNQGPTQS PAGMMNSPVN QPAMGMNTGM NAGMNPGMLA 180
AGNGQGIMPN QVMNGSIGAG RGRPNMQYPN AGMGNAGSLL TEPLQQGSPQ MGGQPGLRGP 240
QPLKMGMMNN PSPYGSPYTQ NSGQQIGASG LGLQIQTKTV LPNNLSPFAM DKKAVPGGGM 300
PSMGQQPTPS VQQPGLVTPV AAGMGSGAHT ADPEKRKLIQ QQLVLLLHAH KCQRREQANG 360
EVRQCNLPHC RTMKNVLNHM THCQSGKSCQ VAHCASSRQI ISHWKNCTRH DCPVCLPLKN 420
AGDKRNQQSI LTGAPVGLGN PSSLGVGQQS TPSLSTVSQI DPSSIERAYA ALGLPYQVNQ 480
IPPQPQVQAK NQQSQPSGQS PQGMRSVNNM SASPMGVNGG VGVQTPNLLS DSMLHSTINS 540
QNPMMSENAG VASLGPLPTA AQPSSTGIRK QWHEDITQDL RNHLVHKLVQ AIFPTPDPAA 600
LKDRRMENLV AYARKVEGDM YESANNRAEY YHLLAEKIYK IQKELEEKRR TRLQKQNMLP 660
NAPGMGPVPM NTGSNMEQQP TGMTTNGPVP DPSMIRGSVP NHMMPRMTPQ PGLNQFGQMN 720
MPQPPIGPRQ PSPLQHHGQL AQSGSLNPPM GYGPRMQQAS GQNQFLSQTQ FTSQGMNVTN 780
MPLAPSSGQA PVSQAQMSSS SCPVNSPIMP PGSQGSHIHC PTLPQQAHQN SPSPVPSRTP 840
TPHHTPPSIG NQPPPATAIP TPVPTPPAIP PGPQPPSLHP SSRQTPTPPT HLPPQVQPSL 900
PAAPSADQSQ QQPRSQQSTA VSVPTPTAPL LPPQPSTPLS QPAVSIEGQV SNPPSTSSTE 960
VNSQTIPEKQ PSQEVKMESK MEVDKPEPAD AQPEDTKEAK GEDVKVEPTE MEERGPELKT 1020
DGKEEEEQPS TSATQSSPAP GQSKKKIFKP EELRQALMPT LEALYRQDPE SLPFRQPVDP 1080
QLLGIPDYFD IVKSPMDLST IKRKLDTGQY QEPWQYIDDI WLMFNNAWLY NRKTSRVYKY 1140
CSKLSEVFEQ EIDPVMQSLG YCCGRKLEFS PQTLCCYGKQ LCTIPRDATY YSYQNRYHFC 1200
EKCFNEIQGE SVSLGDDPSQ PQTTINKEQF SKRKNDTLDP ELFVECTECG RKMHQICVLH 1260
HEIIWPSGFV CDGCLKKTAR TRKENKLSAK RLPSTRLGTF LENRVNDFLR RQNHPESGEV 1320
TVRVVHASDK TVEVKPGMKA RFVDSGEMAE SFPYRTKALF AFEEIDGVDL CFFGMHVQEY 1380
GSDCPPPNQR RVYISYLDSV HFFRPKCLRT AVYHEILIGY LEYVKKLGYT TGHIWACPPS 1440
EGDDYIFHCH PPDQKIPKPK RLQEWYKKML DKAVSERIVH DYKDILKQAT EDRLTSAKEL 1500
PYFEGDFWPN VLEESIKELE QEEEERKREE NTSNESTDVT KGDSKNAKKK NNKKTSKNKS 1560
SLSRGNKKKP GMPNVSNDLS QKLYATMEKH KEVFFVIRLI ACPAPNSLPP IVDPDPLIPC 1620
DLMDGRDAFL TLARDKHLEF SSLRRAQWST MCMLVELHTQ SQDRFVYTCN ECKHHVETRW 1680
HCTVCEDYDL CITCYNTKNH DHKMEKLGLG LDDESNNQQA AATQSPGDSR RLSIQRCIQS 1740
LVHACQCRNA NCSLPSCQKM KRVVQHTKGC KRKTNGGCPI CKQLIALCCY HAKHCQENKC 1800
PVPFCLNIKQ KLRQQQLQHR LQQAQMLRRR MASMQRTGVA GQQQGLPSPT PATPTTPTGQ 1860
QPATPQTPQP QPTSQPQPTP PNNMTPYLPR TQTTGPVSQG KAPGQVTPPT PPQTAQAPLP 1920
GPPPAAVEMA MQIQRAAETQ RQMAHVQIFQ RPIQHQMPQM SPMAPMGMNP PPMARGPGGH 1980
LDPGIGPAGM QQQPPWAQGG MPQPQQMQSG MPRPAMMSVA QHGQPLNMAP QPGLGQVGVS 2040
PLKPGTVSQQ ALQNLLRTLR SPSSPLQQQQ VLSILHANPQ LLAAFIKQRA AKYANPNPQP 2100
LPGQPGMTQG QPGLQPPTMP GQQGVHSNPA LQNMNPLQAG VQRAGLPQQQ PQQQLQPPMG 2160
AMSPQAQQMN MNHNTMPSQF RDILRRQMMQ QQGAGPGIGP GMANQFQQPQ GIGYPPQQQQ 2220
QQQQQRMQHH MQQMQQGNMG QMGQLPQALG AEAGASLQAY QQRLLQQQMG SPAQPNPMSP 2280
QQHMLPNQAQ SPHLQGQQIP NSLSNQVRSP QPVPSPRPQS QPPHSSPSPR MQPQPSPHHV 2340
SPQTSSPHPG LVAAQAANPM EQGHFASPDQ NSMLSQLASN PGMANLHGAS ATDLGLSSDN 2400
ADLNSNLSQS TLDIH 2415 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
 GO:0005667; C:transcription factor complex; IDA:UniProtKB.
 GO:0031490; F:chromatin DNA binding; IDA:MGI.
 GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
 GO:0004468; F:lysine N-acetyltransferase activity; ISS:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; ISS:UniProtKB.
 GO:0051216; P:cartilage development; NAS:UniProtKB.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0007507; P:heart development; IMP:MGI.
 GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
 GO:0030324; P:lung development; IMP:MGI.
 GO:0018076; P:N-terminal peptidyl-lysine acetylation; ISS:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0009887; P:organ morphogenesis; IMP:MGI.
 GO:0032092; P:positive regulation of protein binding; IDA:MGI.
 GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0043627; P:response to estrogen stimulus; ISS:UniProtKB.
 GO:0001666; P:response to hypoxia; ISS:UniProtKB.
 GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
 GO:0001756; P:somitogenesis; IGI:MGI.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR010303; DUF902_CREBbp.
 IPR013178; Histone_H3-K56_AcTrfase_RTT109.
 IPR003101; KIX_dom.
 IPR009110; Nuc_rcpt_coact.
 IPR014744; Nuc_rcpt_coact_CREBbp.
 IPR000197; Znf_TAZ.
 IPR000433; Znf_ZZ. 
Pfam
 PF00439; Bromodomain
 PF09030; Creb_binding
 PF06001; DUF902
 PF08214; KAT11
 PF02172; KIX
 PF02135; zf-TAZ
 PF00569; ZZ 
SMART
 SM00297; BROMO
 SM00551; ZnF_TAZ
 SM00291; ZnF_ZZ 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50952; KIX
 PS50134; ZF_TAZ
 PS01357; ZF_ZZ_1
 PS50135; ZF_ZZ_2 
PRINTS
 PR00503; BROMODOMAIN.