dbPTM

EP300_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EP300_MOUSE
UniProt AC	B2RWS6
Protein Name	Histone acetyltransferase p300
Gene Name	Ep300
Organism	Mus musculus (Mouse).
Sequence Length	2412
Subcellular Localization	Cytoplasm . Nucleus . In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus.
Protein Description	Functions as histone acetyltransferase and regulates transcription via chromatin remodeling (By similarity). Acetylates all four core histones in nucleosomes (By similarity). Histone acetylation gives an epigenetic tag for transcriptional activation (By similarity). Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. [PubMed: 18486321]
Protein Sequence	MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDISQLQTSLGIVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQAMASQAQQNSPGLSLINSMVKSPMAQTGLTSPNMGIGSSGPNQGPTQSPAGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRPNMQYPNAGMGNAGSLLTEPLQQGSPQMGGQPGLRGPQPLKMGMMNNPSPYGSPYTQNSGQQIGASGLGLQIQTKTVLPNNLSPFAMDKKAVPGGGMPSMGQQPTPSVQQPGLVTPVAAGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQSILTGAPVGLGNPSSLGVGQQSTPSLSTVSQIDPSSIERAYAALGLPYQVNQIPPQPQVQAKNQQSQPSGQSPQGMRSVNNMSASPMGVNGGVGVQTPNLLSDSMLHSTINSQNPMMSENAGVASLGPLPTAAQPSSTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAPGMGPVPMNTGSNMGQQPTGMTTNGPVPDPSMIRGSVPNHMMPRMTPQPGLNQFGQMNMPQPPIGPRQPSPLQHHGQLAQSGSLNPPMGYGPRMQQASGQNQFLSQTQFTSQGMNVTNMPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPTLPQQAHQNSPSPVPSRTPTPHHTPPSIGNQPPPATAIPTPVPTPPAIPPGPQPPSLHPSSRQTPTPPTHLPPQVQPSLPAAPSADQSQQQPRSQQSTAVSVPTPTAPLLPPQPSTPLSQPAVSIEGQVSNPPSTSSTEVNSQTIPEKQPSQEVKMESKMEVDKPEPADAQPEDTKEAKGEDVKVEPTEMEERGPELKTDGKEEEEQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPSGFVCDGCLKKTARTRKENKLSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDILKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIACPAPNSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVAGQQQGLPSPTPATPTTPTGQQPATPQTPQPQPTSQPQPTPPNNMTPYLPRTQTTGPVSQGKAPGQVTPPTPPQTAQAPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPQMSPMAPMGMNPPPMARGPGGHLDPGIGPAGMQQQPPWAQGGMPQPQQMQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGVSPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANPNPQPLPGQPGMTQGQPGLQPPTMPGQQGVHSNPALQNMNPLQAGVQRAGLPQQQPQQQLQPPMGAMSPQAQQMNMNHNTMPSQFRDILRRQMMQQQGAGPGIGPGMANQFQQPQGIGYPPQQQQQQRMQHHMQQMQQGNMGQMGQLPQALGAEAGASLQAYQQRLLQQQMGSPAQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQAANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSSDNADLNSNLSQSTLDIH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAENVVEPG ------CCCCCCCCC	28.51	-
12	Phosphorylation	VVEPGPPSAKRPKLS CCCCCCCCCCCCCCC	49.94	25619855
14	Acetylation	EPGPPSAKRPKLSSP CCCCCCCCCCCCCCC	73.83	23236377
79	Acetylation	QDAASKHKQLSELLR HHHHHHHHHHHHHHH	57.58	23806337
82	Phosphorylation	ASKHKQLSELLRSGS HHHHHHHHHHHHHCC	24.57	26643407
87	Phosphorylation	QLSELLRSGSSPNLN HHHHHHHHCCCCCCC	42.89	26643407
89	Phosphorylation	SELLRSGSSPNLNMG HHHHHHCCCCCCCCC	43.82	26643407
90	Phosphorylation	ELLRSGSSPNLNMGV HHHHHCCCCCCCCCC	22.72	26643407
112	Phosphorylation	ASQAQQNSPGLSLIN HHHHHHHCCCHHHHH	18.92	22802335
116	Phosphorylation	QQNSPGLSLINSMVK HHHCCCHHHHHHHHC	32.87	22802335
120	Phosphorylation	PGLSLINSMVKSPMA CCHHHHHHHHCCCCC	20.26	22802335
262	Phosphorylation	GSPYTQNSGQQIGAS CCCCCCCCCCCCCCC	28.32	22802335
286	Phosphorylation	TVLPNNLSPFAMDKK EECCCCCCCCCCCCC	21.79	25266776
292	Acetylation	LSPFAMDKKAVPGGG CCCCCCCCCCCCCCC	29.55	23236377
419	Acetylation	CPVCLPLKNAGDKRN CCEEEECCCCCCCCH	42.69	-
424	Acetylation	PLKNAGDKRNQQSIL ECCCCCCCCHHCHHH	52.94	-
494	Phosphorylation	VQAKNQQSQPSGQSP CCCCCCCCCCCCCCC	34.00	24899341
497	Phosphorylation	KNQQSQPSGQSPQGM CCCCCCCCCCCCCCC	41.65	23684622
500	Phosphorylation	QSQPSGQSPQGMRSV CCCCCCCCCCCCCCC	23.79	25521595
581	Methylation	EDITQDLRNHLVHKL HHHHHHHHHHHHHHH	36.49	-
605	Methylation	PAALKDRRMENLVAY HHHHHHHHHHHHHHH	47.07	-
612	Phosphorylation	RMENLVAYARKVEGD HHHHHHHHHHHHCCC	10.24	19854140
637	Acetylation	YYHLLAEKIYKIQKE HHHHHHHHHHHHHHH	45.81	-
833	Phosphorylation	QAHQNSPSPVPSRTP HHCCCCCCCCCCCCC	38.05	23737553
845	Phosphorylation	RTPTPHHTPPSIGNQ CCCCCCCCCCCCCCC	33.58	28973931
885	Phosphorylation	LHPSSRQTPTPPTHL CCCCCCCCCCCCCCC	28.19	25266776
887	Phosphorylation	PSSRQTPTPPTHLPP CCCCCCCCCCCCCCC	45.33	29233185
890	Phosphorylation	RQTPTPPTHLPPQVQ CCCCCCCCCCCCCCC	36.93	25266776
899	Phosphorylation	LPPQVQPSLPAAPSA CCCCCCCCCCCCCCC	29.87	25266776
905	Phosphorylation	PSLPAAPSADQSQQQ CCCCCCCCCCHHHCC	39.49	25777480
909	Phosphorylation	AAPSADQSQQQPRSQ CCCCCCHHHCCCCHH	30.42	25777480
972	Phosphorylation	TIPEKQPSQEVKMES CCCCCCCCCCCCCCC	36.16	28285833
976	Acetylation	KQPSQEVKMESKMEV CCCCCCCCCCCCCCC	35.88	-
980	Acetylation	QEVKMESKMEVDKPE CCCCCCCCCCCCCCC	26.27	23806337
1009	Phosphorylation	EDVKVEPTEMEERGP CCCCCCCCCHHHCCC	34.16	26643407
1019	Acetylation	EERGPELKTDGKEEE HHCCCCCCCCCCCCC	42.80	-
1019	Sumoylation	EERGPELKTDGKEEE HHCCCCCCCCCCCCC	42.80	-
1020	Phosphorylation	ERGPELKTDGKEEEE HCCCCCCCCCCCCCC	63.71	25619855
1023	Acetylation	PELKTDGKEEEEQPS CCCCCCCCCCCCCCC	65.84	-
1023	Sumoylation	PELKTDGKEEEEQPS CCCCCCCCCCCCCCC	65.84	-
1030	Phosphorylation	KEEEEQPSTSATQSS CCCCCCCCCCCCCCC	34.39	25619855
1031	Phosphorylation	EEEEQPSTSATQSSP CCCCCCCCCCCCCCC	29.12	25619855
1032	Phosphorylation	EEEQPSTSATQSSPA CCCCCCCCCCCCCCC	33.39	25619855
1034	Phosphorylation	EQPSTSATQSSPAPG CCCCCCCCCCCCCCC	28.84	25619855
1036	Phosphorylation	PSTSATQSSPAPGQS CCCCCCCCCCCCCCC	33.65	27087446
1037	Phosphorylation	STSATQSSPAPGQSK CCCCCCCCCCCCCCC	18.44	25521595
1043	Phosphorylation	SSPAPGQSKKKIFKP CCCCCCCCCCCCCCH	52.97	25619855
1179	Acetylation	QTLCCYGKQLCTIPR CCEEECCCEEECCCC	17.39	23806337
1321	Phosphorylation	HPESGEVTVRVVHAS CCCCCCEEEEEEECC	9.78	22871156
1328	Phosphorylation	TVRVVHASDKTVEVK EEEEEECCCCEEEEC	25.43	22871156
1331	Phosphorylation	VVHASDKTVEVKPGM EEECCCCEEEECCCC	27.21	22871156
1335	Acetylation	SDKTVEVKPGMKARF CCCEEEECCCCEEEE	23.50	-
1393	Phosphorylation	PPNQRRVYISYLDSV CCCCCEEEEEECCCC	5.15	19854140
1395	Phosphorylation	NQRRVYISYLDSVHF CCCEEEEEECCCCEE	11.27	19854140
1396	Phosphorylation	QRRVYISYLDSVHFF CCEEEEEECCCCEEC	12.64	19854140
1399	Phosphorylation	VYISYLDSVHFFRPK EEEEECCCCEECCHH	18.20	19854140
1413	Phosphorylation	KCLRTAVYHEILIGY HHHHHHHHHHHHHHH	7.41	21183079
1420	Phosphorylation	YHEILIGYLEYVKKL HHHHHHHHHHHHHHH	6.86	22817900
1423	Phosphorylation	ILIGYLEYVKKLGYT HHHHHHHHHHHHCCC	18.25	22817900
1472	Acetylation	WYKKMLDKAVSERIV HHHHHHHHHHHHHHH	46.88	-
1498	Acetylation	EDRLTSAKELPYFEG HHHCCCCHHCCCCCC	60.60	156925
1541	Acetylation	NESTDVTKGDSKNAK CCCCCCCCCCHHCHH	61.64	22733758
1545	Acetylation	DVTKGDSKNAKKKNN CCCCCCHHCHHHHCC	66.71	22826441
1548	Acetylation	KGDSKNAKKKNNKKT CCCHHCHHHHCCCCC	73.92	156931
1549	Acetylation	GDSKNAKKKNNKKTS CCHHCHHHHCCCCCC	59.32	156933
1550	Acetylation	DSKNAKKKNNKKTSK CHHCHHHHCCCCCCC	66.11	22733758
1553	Acetylation	NAKKKNNKKTSKNKS CHHHHCCCCCCCCHH	67.81	22733758
1554	Acetylation	AKKKNNKKTSKNKSS HHHHCCCCCCCCHHH	61.22	22733758
1557	Acetylation	KNNKKTSKNKSSLSR HCCCCCCCCHHHHCC	73.88	23806337
1559	Acetylation	NKKTSKNKSSLSRGN CCCCCCCHHHHCCCC	45.20	23806337
1582	Acetylation	VSNDLSQKLYATMEK CCHHHHHHHHHHHHH	39.84	-
1589	Acetylation	KLYATMEKHKEVFFV HHHHHHHHHHHEEEE	49.51	156953
1642	Phosphorylation	DKHLEFSSLRRAQWS HCCCCHHHHHHHHHH	31.08	23140645
1673	Acetylation	VYTCNECKHHVETRW EEECCCCCCCCCCCE	30.48	-
1698	Acetylation	CITCYNTKNHDHKME EEEEEECCCCCCHHH	48.96	-
1703	Acetylation	NTKNHDHKMEKLGLG ECCCCCCHHHHCCCC	55.61	22902405
1706	Acetylation	NHDHKMEKLGLGLDD CCCCHHHHCCCCCCC	44.34	23806337
1715	Phosphorylation	GLGLDDESNNQQAAA CCCCCCCCCCCHHHH	48.34	28285833
1723	Phosphorylation	NNQQAAATQSPGDSR CCCHHHHHCCCCHHH	25.50	25266776
1725	Phosphorylation	QQAAATQSPGDSRRL CHHHHHCCCCHHHHH	26.88	25266776
1729	Phosphorylation	ATQSPGDSRRLSIQR HHCCCCHHHHHHHHH	25.80	28066266
1733	Phosphorylation	PGDSRRLSIQRCIQS CCHHHHHHHHHHHHH	18.18	25367039
1759	Acetylation	CSLPSCQKMKRVVQH CCCCHHHHHHHHHHH	51.20	156959
1768	Acetylation	KRVVQHTKGCKRKTN HHHHHHCCCCCCCCC	61.25	-
1833	Phosphorylation	MLRRRMASMQRTGVA HHHHHHHHHHHHCCC	13.20	-
1907	Phosphorylation	GKAPGQVTPPTPPQT CCCCCCCCCCCCCCC	18.70	22006019
1910	Phosphorylation	PGQVTPPTPPQTAQA CCCCCCCCCCCCCCC	49.13	25338131
2060	Methylation	QNLLRTLRSPSSPLQ HHHHHHHCCCCCHHH	46.00	97812493
2143	Citrullination	PLQAGVQRAGLPQQQ HHHHHHHHCCCCCCC	28.37	-
2143	Methylation	PLQAGVQRAGLPQQQ HHHHHHHHCCCCCCC	28.37	-
2268	Phosphorylation	LLQQQMGSPAQPNPM HHHHHCCCCCCCCCC	25.83	22802335
2276	Phosphorylation	PAQPNPMSPQQHMLP CCCCCCCCHHHCCCC	32.59	22802335
2288	Phosphorylation	MLPNQAQSPHLQGQQ CCCCCCCCCCCCCCC	38.55	22802335
2301	Phosphorylation	QQIPNSLSNQVRSPQ CCCCCCHHCCCCCCC	58.15	22802335
2306	Phosphorylation	SLSNQVRSPQPVPSP CHHCCCCCCCCCCCC	28.73	26643407
2312	Phosphorylation	RSPQPVPSPRPQSQP CCCCCCCCCCCCCCC	43.29	26160508
2317	Phosphorylation	VPSPRPQSQPPHSSP CCCCCCCCCCCCCCC	46.34	26160508
2322	Phosphorylation	PQSQPPHSSPSPRMQ CCCCCCCCCCCCCCC	33.54	23684622
2323	Phosphorylation	QSQPPHSSPSPRMQP CCCCCCCCCCCCCCC	32.15	23684622
2325	Phosphorylation	QPPHSSPSPRMQPQP CCCCCCCCCCCCCCC	50.12	26824392
2364	Phosphorylation	MEQGHFASPDQNSML CCCCCCCCCCHHHHH	18.13	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
89	S	Phosphorylation	Kinase	AMPK	-	Uniprot
1733	S	Phosphorylation	Kinase	AKT1	P31749	PSP
1733	S	Phosphorylation	Kinase	AKT2	P31751	PSP
1833	S	Phosphorylation	Kinase	AKT1	P31749	PSP
1833	S	Phosphorylation	Kinase	AKT2	P31751	PSP
2276	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
2312	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
2364	S	Phosphorylation	Kinase	MAPK1	P28482	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
89	S	Phosphorylation	-
Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear receptors, such as PPARG (By similarity).
419	K	Acetylation	-
Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706.
424	K	Acetylation	-
Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706.
581	R	Methylation	-
Methylated at Arg-581 and Arg-605 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response.
605	R	Methylation	-
Methylated at Arg-581 and Arg-605 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response.
1019	K	Acetylation	-
Deacetylated in the transcriptional repression domain (CRD1) by SIRT1, preferentially at Lys-1019.
1541	K	Acetylation	-
Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706.
1545	K	Acetylation	-
Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706.
1548	K	Acetylation	-
Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706.
1698	K	Acetylation	-
Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706.
1703	K	Acetylation	-
Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706.
1706	K	Acetylation	-
Deacetylated by SIRT2, preferentially at Lys-419, Lys-424, Lys-1541, Lys-1545, Lys-1548, Lys-1698, Lys-1703 and Lys-1706.
2143	R	Citrullination	-
Citrullinated at Arg-2143 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1.
2143	R	Methylation	-
Also methylated at Arg-2143 by CARM1, which impairs interaction with NCOA2/GRIP1 (By similarity).
2143	R	Methylation	-
Citrullinated at Arg-2143 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of EP300_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NUPR1_MOUSE	Nupr1	physical	19723804
PITX2_MOUSE	Pitx2	physical	12464179
CEBPB_MOUSE	Cebpb	physical	15878863
H4_BOVIN	H4	physical	15485860
H33_BOVIN	H3F3A	physical	15485860
KAT2B_MOUSE	Kat2b	physical	9659901
MYOD1_MOUSE	Myod1	physical	9659901
CCNT1_HUMAN	CCNT1	physical	20081228
GATA4_HUMAN	GATA4	physical	20081228
ACTB_HUMAN	ACTB	physical	20081228
CDK9_HUMAN	CDK9	physical	20081228
EP300_HUMAN	EP300	physical	20081228
RPB1_HUMAN	POLR2A	physical	20081228
ZBT7B_MOUSE	Zbtb7b	physical	20810990
NR1H4_MOUSE	Nr1h4	physical	19883617
MECP2_MOUSE	Mecp2	physical	22677942
CEBPA_MOUSE	Cebpa	physical	22086955
H2A3_MOUSE	Hist3h2a	physical	16704373
CHD4_MOUSE	Chd4	physical	15189737
HTF4_MOUSE	Tcf12	physical	15189737
P85A_MOUSE	Pik3r1	physical	21057544
HIF1A_MOUSE	Hif1a	physical	18268343
FOXO3_MOUSE	Foxo3	physical	18268343
SPI1_MOUSE	Spi1	physical	16702405
ETV4_MOUSE	Etv4	physical	14976201
KAT2B_MOUSE	Kat2b	physical	9742083
KAT2A_MOUSE	Kat2a	physical	9742083
CREB1_MOUSE	Creb1	physical	17525731
SRC_MOUSE	Src	physical	26695438

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EP300_MOUSE

Related Literatures of Post-Translational Modification

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