Histone acetyltransferase p300 - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Histone acetyltransferase p300
      Short name=p300 HAT
    EC=2.3.1.48
Alternative name(s):
    E1A-associated protein p300

Gene names

Name:	EP300
Synonyms:	P300

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	2414 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Ref.6 Ref.23 Ref.31
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Interacts with phosphorylated CREB1 By similarity. Interacts with DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, SP1, SP3, SPIB, SRY, TCF7L2, TP53, SATB1, SRCAP, TTC5, JMY and TRERF1. The TAZ-type 1 domain interacts with HIF1A. Probably part of a complex with HIF1A and CREBBP. Part of a complex containing CARM1 and NCOA2/GRIP1. Interacts with ING4 and this interaction may be indirect. Interacts with ING5. Interacts with the C-terminal region of CITED4. Interacts with HTLV-1 Tax and p30II. Interacts with and acetylates HIV-1 Tat. Non-sumoylated EP300 preferentially interacts with SENP3. Interacts with SS18L1/CREST. Ref.6 Ref.23 Ref.31 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.27 Ref.28 Ref.29 Ref.30 Ref.32 Ref.33 Ref.37 Ref.40 Ref.43 Ref.48
Subcellular location	Nucleus.
Post-translational modification	Acetylated on Lys at up to 17 positions by intermolecular autocatalysis. Citrullinated at Arg-2142 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1. Methylated at Arg-580 and Arg-604 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2142 by CARM1, which impairs interaction with NCOA2/GRIP1. Ref.6 Ref.37 Sumoylated; Desumoylated by SENP3 through the removal of SUMO2 and SUMO3. Ref.43
Involvement in disease	Defects in EP300 may play a role in epithelial cancer. Chromosomal aberrations involving EP300 may be a cause of acute myeloid leukemias. Translocation t(8;22)(p11;q13) with MYST3. Defects in EP300 are a cause of Rubinstein-Taybi syndrome (RSTS) [MIM:180849]. RSTS is an autosomal dominant disorder characterized by craniofacial abnormalities, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. Ref.36
Sequence similarities	Contains 1 bromo domain. Contains 1 KIX domain. Contains 2 TAZ-type zinc fingers. Contains 1 ZZ-type zinc finger.

Ontologies

Keywords
Biological process	Cell cycle Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Disease mutation
Domain	Bromodomain Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Transferase
PTM	Acetylation Citrullination Methylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	N-terminal peptidyl-lysine acetylation Inferred from direct assay. Source: UniProtKB apoptosis Inferred from mutant phenotype. Source: UniProtKB cell cycle Inferred from electronic annotation. Source: UniProtKB-KW histone acetylation Inferred from electronic annotation. Source: InterPro interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW nervous system development Traceable author statement. Source: ProtInc positive regulation of transcription factor activity Inferred from direct assay. Source: UniProtKB response to hypoxia Inferred from direct assay. Source: UniProtKB transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: HPA
Molecular function	histone acetyltransferase activity Inferred from direct assay. Source: UniProtKB transcription coactivator activity Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CITED2	Q99967	1	EBI-447295,EBI-937732
EPAS1	Q99814	1	EBI-447295,EBI-447470
HIF1A	Q16665	2	EBI-447295,EBI-447269
His2A	P84051	1	EBI-447295,EBI-182580	From a different organism.
His3	P02299	1	EBI-447295,EBI-522090	From a different organism.
His4	P84040	1	EBI-447295,EBI-185028	From a different organism.
IFNAR1	P17181	1	EBI-447295,EBI-1547250
IFNAR2	P48551	1	EBI-447295,EBI-958408
Jmy	Q9QXM1	6	EBI-447295,EBI-866001	From a different organism.
KAT2B	Q92831	2	EBI-447295,EBI-477430
MYC	P01106	1	EBI-447295,EBI-447544
NAP1L1	P55209	2	EBI-447295,EBI-356392
NCOA3	Q9Y6Q9	1	EBI-447295,EBI-81196
POU3F2	P20265	2	EBI-447295,EBI-1167176
PPARG	P37231	1	EBI-447295,EBI-781384
TFAP2A	P05549	1	EBI-447295,EBI-347351
TP53	P04637	3	EBI-447295,EBI-366083
Tp53	P02340	1	EBI-447295,EBI-474016	From a different organism.
ZBTB17	Q13105	1	EBI-447295,EBI-372156

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 2414

2413

Histone acetyltransferase p300

PRO_0000211193

Regions

Domain

566 – 645

KIX

Domain

1067 – 1139

Bromo

Zinc finger

331 – 417

TAZ-type 1

Zinc finger

1664 – 1707

ZZ-type

Zinc finger

1728 – 1809

TAZ-type 2

Region

1572 – 1818

247

Binding region for E1A adenovirus

Region

2003 – 2212

210

Interaction with HTLV-1 Tax

Region

2041 – 2240

200

Interaction with NCOA2

Motif

11 – 17

Nuclear localization signal Potential

Compositional bias

797 – 800

Poly-Ser

Compositional bias

1519 – 1526

Poly-Glu

Compositional bias

2066 – 2069

Poly-Gln

Compositional bias

2190 – 2195

Poly-Gln

Sites

Site

31 – 32

Breakpoint for translocation to form MYST3-EP300 and EP300-MYST3

Site

2088

Interaction with NCOA2

Site

Interaction with NCOA2

Amino acid modifications

Modified residue

N-acetylalanine Ref.42

Modified residue

285

Phosphoserine Ref.42

Modified residue

580

Omega-N-methylated arginine; by CARM1 Ref.6

Modified residue

604

Omega-N-methylated arginine; by CARM1 Ref.6

Modified residue

636

N6-acetyllysine Ref.45

Modified residue

885

Phosphothreonine Ref.42

Modified residue

887

Phosphothreonine Ref.42

Modified residue

977

N6-acetyllysine Ref.45

Modified residue

981

N6-acetyllysine Ref.45

Modified residue

1038

Phosphoserine Ref.42

Modified residue

1103

N6-acetyllysine Ref.45

Modified residue

1336

N6-acetyllysine; by autocatalysis Ref.38

Modified residue

1473

N6-acetyllysine; by autocatalysis Ref.38

Modified residue

1499

N6-acetyllysine; by autocatalysis Ref.45

Modified residue

1542

N6-acetyllysine; by autocatalysis Ref.45

Modified residue

1546

N6-acetyllysine; by autocatalysis Ref.45

Modified residue

1549

N6-acetyllysine; by autocatalysis Ref.45

Modified residue

1550

N6-acetyllysine; by autocatalysis

Modified residue

1551

N6-acetyllysine; by autocatalysis

Modified residue

1554

N6-acetyllysine; by autocatalysis Ref.45 Ref.39

Modified residue

1555

N6-acetyllysine; by autocatalysis Ref.45 Ref.39

Modified residue

1558

N6-acetyllysine; by autocatalysis Ref.45 Ref.39

Modified residue

1560

N6-acetyllysine; by autocatalysis Ref.45 Ref.39

Modified residue

1568

N6-acetyllysine; by autocatalysis

Modified residue

1569

N6-acetyllysine; by autocatalysis

Modified residue

1583

N6-acetyllysine Ref.45

Modified residue

1590

N6-acetyllysine Ref.45

Modified residue

1637

N6-acetyllysine; by autocatalysis

Modified residue

1674

N6-acetyllysine Ref.45

Modified residue

1734

Phosphoserine

Modified residue

1857

Phosphothreonine Ref.42

Modified residue

1859

Phosphothreonine Ref.42

Modified residue

Asymmetric dimethylarginine; by CARM1; alternate Ref.37

Modified residue

Citrulline; by PADI4; alternate

Natural variations

Natural variant

289

M → V: dbSNP rs2230111.

VAR_055554

Natural variant

827

L → P in breast cancer. Ref.49

VAR_014428

Natural variant

997

I → V: dbSNP rs20551.

VAR_020425

Natural variant

1013

E → G in breast cancer. Ref.49

VAR_014429

Natural variant

1650

S → Y in pancreatic cancer. Ref.49

VAR_014430

Natural variant

2174

T → S: dbSNP rs5758252.

VAR_038376

Natural variant

2221

P → Q in colorectal cancer. dbSNP rs28937578. Ref.49

VAR_014431

Natural variant

2223

Q → P: dbSNP rs1046088. Ref.1

VAR_038377

Experimental info

Mutagenesis

1357

T → L: 40% decrease in activity. Ref.47

Mutagenesis

1357

T → R: 40% decrease in activity. 90% decrease in activity; when associated with R-1505; R-1625 and R-1628. Ref.47

Mutagenesis

1396

S → R: Loss of activity; when associated with R-1397. Ref.47

Mutagenesis

1396

S → W: Loss of activity; when associated with W-1397. Ref.47

Mutagenesis

1397

Y → R: Loss of activity; when associated with R-1396. Ref.47

Mutagenesis

1397

Y → W: Loss of activity; when associated with W-1397. Ref.47

Mutagenesis

1505

E → R: 90% decrease in activity; when associated with R-1625 and R-1628. 90% decrease in activity; when associated with R-1357; R-1625 and R-1628. Ref.47

Mutagenesis

1625

D → R: 70% decrease in activity; when associated with R-1628. 90% decrease in activity; when associated with R-1505 and R-1628. 90% decrease in activity; when associated with R-1357; R-1505 and R-1628. Ref.47

Mutagenesis

1628

D → R: 70% decrease in activity; when associated with R-1625. 90% decrease in activity; when associated with E-1505 and R-1625. 90% decrease in activity; when associated with R-1357; R-1505 and R-1625. Ref.47

Mutagenesis

2056

R → K: No effect on interaction with NCOA2. Ref.37

Mutagenesis

2088

R → K: Abolishes interaction with NCOA2. Ref.37

Mutagenesis

R → K: Strongly reduces interaction with NCOA2. Ref.37

Sequence conflict

169

M → T in AAA18639. Ref.1

Sequence conflict

204

N → D in AAA18639. Ref.1

Sequence conflict

928

T → N in AAA18639. Ref.1

Sequence conflict

1924

A → T in AAA18639. Ref.1

Secondary structure

2414

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q09472-1 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: 8E869E1F174A6FEB
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FASTA

2,414

264,161

        10         20         30         40         50         60 
MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD 

        70         80         90        100        110        120 
INQLQTSLGM VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQVMASQAQQ SSPGLGLINS 

       130        140        150        160        170        180 
MVKSPMTQAG LTSPNMGMGT SGPNQGPTQS TGMMNSPVNQ PAMGMNTGMN AGMNPGMLAA 

       190        200        210        220        230        240 
GNGQGIMPNQ VMNGSIGAGR GRQNMQYPNP GMGSAGNLLT EPLQQGSPQM GGQTGLRGPQ 

       250        260        270        280        290        300 
PLKMGMMNNP NPYGSPYTQN PGQQIGASGL GLQIQTKTVL SNNLSPFAMD KKAVPGGGMP 

       310        320        330        340        350        360 
NMGQQPAPQV QQPGLVTPVA QGMGSGAHTA DPEKRKLIQQ QLVLLLHAHK CQRREQANGE 

       370        380        390        400        410        420 
VRQCNLPHCR TMKNVLNHMT HCQSGKSCQV AHCASSRQII SHWKNCTRHD CPVCLPLKNA 

       430        440        450        460        470        480 
GDKRNQQPIL TGAPVGLGNP SSLGVGQQSA PNLSTVSQID PSSIERAYAA LGLPYQVNQM 

       490        500        510        520        530        540 
PTQPQVQAKN QQNQQPGQSP QGMRPMSNMS ASPMGVNGGV GVQTPSLLSD SMLHSAINSQ 

       550        560        570        580        590        600 
NPMMSENASV PSLGPMPTAA QPSTTGIRKQ WHEDITQDLR NHLVHKLVQA IFPTPDPAAL 

       610        620        630        640        650        660 
KDRRMENLVA YARKVEGDMY ESANNRAEYY HLLAEKIYKI QKELEEKRRT RLQKQNMLPN 

       670        680        690        700        710        720 
AAGMVPVSMN PGPNMGQPQP GMTSNGPLPD PSMIRGSVPN QMMPRITPQS GLNQFGQMSM 

       730        740        750        760        770        780 
AQPPIVPRQT PPLQHHGQLA QPGALNPPMG YGPRMQQPSN QGQFLPQTQF PSQGMNVTNI 

       790        800        810        820        830        840 
PLAPSSGQAP VSQAQMSSSS CPVNSPIMPP GSQGSHIHCP QLPQPALHQN SPSPVPSRTP 

       850        860        870        880        890        900 
TPHHTPPSIG AQQPPATTIP APVPTPPAMP PGPQSQALHP PPRQTPTPPT TQLPQQVQPS 

       910        920        930        940        950        960 
LPAAPSADQP QQQPRSQQST AASVPTPTAP LLPPQPATPL SQPAVSIEGQ VSNPPSTSST 

       970        980        990       1000       1010       1020 
EVNSQAIAEK QPSQEVKMEA KMEVDQPEPA DTQPEDISES KVEDCKMEST ETEERSTELK 

      1030       1040       1050       1060       1070       1080 
TEIKEEEDQP STSATQSSPA PGQSKKKIFK PEELRQALMP TLEALYRQDP ESLPFRQPVD 

      1090       1100       1110       1120       1130       1140 
PQLLGIPDYF DIVKSPMDLS TIKRKLDTGQ YQEPWQYVDD IWLMFNNAWL YNRKTSRVYK 

      1150       1160       1170       1180       1190       1200 
YCSKLSEVFE QEIDPVMQSL GYCCGRKLEF SPQTLCCYGK QLCTIPRDAT YYSYQNRYHF 

      1210       1220       1230       1240       1250       1260 
CEKCFNEIQG ESVSLGDDPS QPQTTINKEQ FSKRKNDTLD PELFVECTEC GRKMHQICVL 

      1270       1280       1290       1300       1310       1320 
HHEIIWPAGF VCDGCLKKSA RTRKENKFSA KRLPSTRLGT FLENRVNDFL RRQNHPESGE 

      1330       1340       1350       1360       1370       1380 
VTVRVVHASD KTVEVKPGMK ARFVDSGEMA ESFPYRTKAL FAFEEIDGVD LCFFGMHVQE 

      1390       1400       1410       1420       1430       1440 
YGSDCPPPNQ RRVYISYLDS VHFFRPKCLR TAVYHEILIG YLEYVKKLGY TTGHIWACPP 

      1450       1460       1470       1480       1490       1500 
SEGDDYIFHC HPPDQKIPKP KRLQEWYKKM LDKAVSERIV HDYKDIFKQA TEDRLTSAKE 

      1510       1520       1530       1540       1550       1560 
LPYFEGDFWP NVLEESIKEL EQEEEERKRE ENTSNESTDV TKGDSKNAKK KNNKKTSKNK 

      1570       1580       1590       1600       1610       1620 
SSLSRGNKKK PGMPNVSNDL SQKLYATMEK HKEVFFVIRL IAGPAANSLP PIVDPDPLIP 

      1630       1640       1650       1660       1670       1680 
CDLMDGRDAF LTLARDKHLE FSSLRRAQWS TMCMLVELHT QSQDRFVYTC NECKHHVETR 

      1690       1700       1710       1720       1730       1740 
WHCTVCEDYD LCITCYNTKN HDHKMEKLGL GLDDESNNQQ AAATQSPGDS RRLSIQRCIQ 

      1750       1760       1770       1780       1790       1800 
SLVHACQCRN ANCSLPSCQK MKRVVQHTKG CKRKTNGGCP ICKQLIALCC YHAKHCQENK 

      1810       1820       1830       1840       1850       1860 
CPVPFCLNIK QKLRQQQLQH RLQQAQMLRR RMASMQRTGV VGQQQGLPSP TPATPTTPTG 

      1870       1880       1890       1900       1910       1920 
QQPTTPQTPQ PTSQPQPTPP NSMPPYLPRT QAAGPVSQGK AAGQVTPPTP PQTAQPPLPG 

      1930       1940       1950       1960       1970       1980 
PPPAAVEMAM QIQRAAETQR QMAHVQIFQR PIQHQMPPMT PMAPMGMNPP PMTRGPSGHL 

      1990       2000       2010       2020       2030       2040 
EPGMGPTGMQ QQPPWSQGGL PQPQQLQSGM PRPAMMSVAQ HGQPLNMAPQ PGLGQVGISP 

      2050       2060       2070       2080       2090       2100 
LKPGTVSQQA LQNLLRTLRS PSSPLQQQQV LSILHANPQL LAAFIKQRAA KYANSNPQPI 

      2110       2120       2130       2140       2150       2160 
PGQPGMPQGQ PGLQPPTMPG QQGVHSNPAM QNMNPMQAGV QRAGLPQQQP QQQLQPPMGG 

      2170       2180       2190       2200       2210       2220 
MSPQAQQMNM NHNTMPSQFR DILRRQQMMQ QQQQQGAGPG IGPGMANHNQ FQQPQGVGYP 

      2230       2240       2250       2260       2270       2280 
PQQQQRMQHH MQQMQQGNMG QIGQLPQALG AEAGASLQAY QQRLLQQQMG SPVQPNPMSP 

      2290       2300       2310       2320       2330       2340 
QQHMLPNQAQ SPHLQGQQIP NSLSNQVRSP QPVPSPRPQS QPPHSSPSPR MQPQPSPHHV 

      2350       2360       2370       2380       2390       2400 
SPQTSSPHPG LVAAQANPME QGHFASPDQN SMLSQLASNP GMANLHGASA TDLGLSTDNS 

      2410 
DLNSNLSQST LDIH

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor." Eckner R., Ewen M.E., Newsome D., Gerdes M., Decaprio J.A., Lawrence J.B., Livingston D.M. Genes Dev. 8:869-884(1994) [PubMed: 7523245] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-2223.
[2]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"MOZ is fused to p300 in an acute monocytic leukemia with t(8;22)." Chaffanet M., Gressin L., Preudhomme C., Soenen-Cornu V., Birnbaum D., Pebusque M.-J. Genes Chromosomes Cancer 28:138-144(2000) [PubMed: 10824998] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-42, CHROMOSOMAL TRANSLOCATION WITH MYST3.
[5]	"Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP." Lundblad J.R., Kwok R.P.S., Laurance M.E., Harter M.L., Goodman R.H. Nature 374:85-88(1995) [PubMed: 7870179] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-660.
[6]	"A transcriptional switch mediated by cofactor methylation." Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M., Evans R.M. Science 294:2507-2511(2001) [PubMed: 11701890] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH CARM1, METHYLATION AT ARG-580 AND ARG-604, FUNCTION.
[7]	"The transcriptional coactivators p300 and CBP are histone acetyltransferases." Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y. Cell 87:953-959(1996) [PubMed: 8945521] [Abstract] Cited for: ENZYME ACTIVITY.
[8]	"A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A." Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y. Nature 382:319-324(1996) [PubMed: 8684459] [Abstract] Cited for: INTERACTION WITH PCAF.
[9]	"An essential role for p300/CBP in the cellular response to hypoxia." Arany Z., Huang L.E., Eckner R., Bhattacharya S., Jiang C., Goldberg M.A., Bunn H.F., Livingston D.M. Proc. Natl. Acad. Sci. U.S.A. 93:12969-12973(1996) [PubMed: 8917528] [Abstract] Cited for: INTERACTION WITH HIF1A AND CREBBP.
[10]	"Differential transcriptional activation by human T-cell leukemia virus type 1 Tax mutants is mediated by distinct interactions with CREB binding protein and p300." Bex F., Yin M.-J., Burny A., Gaynor R.B. Mol. Cell. Biol. 18:2392-2405(1998) [PubMed: 9528808] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX.
[11]	"Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex." Fryer C.J., Archer T.K. Nature 393:88-91(1998) [PubMed: 9590696] [Abstract] Cited for: INTERACTION WITH NR3C1.
[12]	"HIV-1 tat transcriptional activity is regulated by acetylation." Kiernan R.E., Vanhulle C., Schiltz L., Adam E., Xiao H., Maudoux F., Calomme C., Burny A., Nakatani Y., Jeang K.-T., Benkirane M., Van Lint C. EMBO J. 18:6106-6118(1999) [PubMed: 10545121] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[13]	"Cells degrade a novel inhibitor of differentiation with E1A-like properties upon exiting the cell cycle." Miyake S., Sellers W.R., Safran M., Li X., Zhao W., Grossman S.R., Gan J., DeCaprio J.A., Adams P.D., Kaelin W.G. Jr. Mol. Cell. Biol. 20:8889-8902(2000) [PubMed: 11073989] [Abstract] Cited for: INTERACTION WITH EID1.
[14]	"A novel Rb- and p300-binding protein inhibits transactivation by MyoD." MacLellan W.R., Xiao G., Abdellatif M., Schneider M.D. Mol. Cell. Biol. 20:8903-8915(2000) [PubMed: 11073990] [Abstract] Cited for: INTERACTION WITH EID1.
[15]	"Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator." Ko L., Cardona G.R., Chin W.W. Proc. Natl. Acad. Sci. U.S.A. 97:6212-6217(2000) [PubMed: 10823961] [Abstract] Cited for: INTERACTION WITH NCOA6.
[16]	"Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones." Deng L., de la Fuente C., Fu P., Wang L., Donnelly R., Wade J.D., Lambert P., Li H., Lee C.-G., Kashanchi F. Virology 277:278-295(2000) [PubMed: 11080476] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[17]	"Adenovirus DNA binding protein interacts with the SNF2-related CBP activator protein (SrCap) and inhibits SrCap-mediated transcription." Xu X., Chackalaparampil I., Monroy M.A., Cannella M.T., Pesek E., Chrivia J., Yaciuk P. J. Virol. 75:10033-10040(2001) [PubMed: 11581372] [Abstract] Cited for: INTERACTION WITH SRCAP.
[18]	"The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to mediate transcriptional activation." Scoggin K.E.S., Ulloa A., Nyborg J.K. Mol. Cell. Biol. 21:5520-5530(2001) [PubMed: 11463834] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX.
[19]	"Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by binding CREB binding protein/p300." Zhang W., Nisbet J.W., Albrecht B., Ding W., Kashanchi F., Bartoe J.T., Lairmore M.D. J. Virol. 75:9885-9895(2001) [PubMed: 11559821] [Abstract] Cited for: INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P30II.
[20]	"A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression." Gizard F., Lavallee B., DeWitte F., Hum D.W. J. Biol. Chem. 276:33881-33892(2001) [PubMed: 11349124] [Abstract] Cited for: INTERACTION WITH TRERF1.
[21]	"Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha." Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A., Kumar R. J. Biol. Chem. 276:38272-38279(2001) [PubMed: 11481323] [Abstract] Cited for: INTERACTION WITH PELP1.
[22]	"Role of Deltex-1 as a transcriptional regulator downstream of the Notch receptor." Yamamoto N., Yamamoto S., Inagaki F., Kawaichi M., Fukamizu A., Kishi N., Matsuno K., Nakamura K., Weinmaster G., Okano H., Nakafuku M. J. Biol. Chem. 276:45031-45040(2001) [PubMed: 11564735] [Abstract] Cited for: INTERACTION WITH DTX1.
[23]	"Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300." Hasan S., Stucki M., Hassa P.O., Imhof R., Gehrig P., Hunziker P., Hubscher U., Hottiger M.O. Mol. Cell 7:1221-1231(2001) [PubMed: 11430825] [Abstract] Cited for: FUNCTION, INTERACTION WITH FEN1.
[24]	"Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with negative cross-talk with c-Myb." Yamamoto H., Kihara-Negishi F., Yamada T., Suzuki M., Nakano T., Oikawa T. Cell Growth Differ. 13:69-75(2002) [PubMed: 11864910] [Abstract] Cited for: INTERACTION WITH SPIB.
[25]	"Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2." Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J., Hurst H.C., Shioda T., Bhattacharya S. J. Biol. Chem. 277:8559-8565(2002) [PubMed: 11744733] [Abstract] Cited for: INTERACTION WITH CITED4.
[26]	"Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities." Lee Y.-H., Koh S.S., Zhang X., Cheng X., Stallcup M.R. Mol. Cell. Biol. 22:3621-3632(2002) [PubMed: 11997499] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH CARM1 AND NCOA2.
[27]	"p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity." Shiseki M., Nagashima M., Pedeux R.M., Kitahama-Shiseki M., Miura K., Okamura S., Onogi H., Higashimoto Y., Appella E., Yokota J., Harris C.C. Cancer Res. 63:2373-2378(2003) [PubMed: 12750254] [Abstract] Cited for: INTERACTION WITH ING4 AND ING5.
[28]	"Identification of a promoter-specific transcriptional activation domain at the C-terminus of the Wnt effector protein T-cell factor 4." Hecht A., Stemmler M.P. J. Biol. Chem. 278:3776-3785(2003) [PubMed: 12446687] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH TCF7L2 AND LEF1.
[29]	"Acetylated SP3 is a transcriptional activator." Ammanamanchi S., Freeman J.W., Brattain M.G. J. Biol. Chem. 278:35775-35780(2003) [PubMed: 12837748] [Abstract] Cited for: INTERACTION WITH SP3.
[30]	"SATB1 makes a complex with p300 and represses gp91(phox) promoter activity." Fujii Y., Kumatori A., Nakamura M. Microbiol. Immunol. 47:803-811(2003) [PubMed: 14605447] [Abstract] Cited for: INTERACTION WITH SATB1.
[31]	"Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53." An W., Kim J., Roeder R.G. Cell 117:735-748(2004) [PubMed: 15186775] [Abstract] Cited for: INTERACTION WITH TP53, FUNCTION.
[32]	"Regulation of human SRY subcellular distribution by its acetylation/deacetylation." Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N., Aldrian-Herrada G., Poulat F., Berta P., Benkirane M., Boizet-Bonhoure B. EMBO J. 23:3336-3345(2004) [PubMed: 15297880] [Abstract] Cited for: INTERACTION WITH SRY.
[33]	"Positive and negative modulation of the transcriptional activity of the ETS factor ESE-1 through interaction with p300, CREB-binding protein, and Ku 70/86." Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P. J. Biol. Chem. 279:25241-25250(2004) [PubMed: 15075319] [Abstract] Cited for: INTERACTION WITH ELF3.
[34]	"Regulation of the p300 HAT domain via a novel activation loop." Thompson P.R., Wang D., Wang L., Fulco M., Pediconi N., Zhang D., An W., Ge Q., Roeder R.G., Wong J., Levrero M., Sartorelli V., Cotter R.J., Cole P.A. Nat. Struct. Mol. Biol. 11:308-315(2004) [PubMed: 15004546] [Abstract] Cited for: ACETYLATION.
[35]	"Dendrite development regulated by CREST, a calcium-regulated transcriptional activator." Aizawa H., Hu S.-C., Bobb K., Balakrishnan K., Ince G., Gurevich I., Cowan M., Ghosh A. Science 303:197-202(2004) [PubMed: 14716005] [Abstract] Cited for: INTERACTION WITH SS18L1/CREST.
[36]	"Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease." Roelfsema J.H., White S.J., Ariyuerek Y., Bartholdi D., Niedrist D., Papadia F., Bacino C.A., den Dunnen J.T., van Ommen G.-J.B., Breuning M.H., Hennekam R.C., Peters D.J.M. Am. J. Hum. Genet. 76:572-580(2005) [PubMed: 15706485] [Abstract] Cited for: INVOLVEMENT IN RSTS.
[37]	"Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination." Lee Y.-H., Coonrod S.A., Kraus W.L., Jelinek M.A., Stallcup M.R. Proc. Natl. Acad. Sci. U.S.A. 102:3611-3616(2005) [PubMed: 15731352] [Abstract] Cited for: METHYLATION AT ARG-2142, CITRULLINATION AT ARG-2142, INTERACTION WITH NCOA2, MUTAGENESIS OF ARG-2056; ARG-2088 AND ARG-2142.
[38]	"Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation." Karanam B., Jiang L., Wang L., Kelleher N.L., Cole P.A. J. Biol. Chem. 281:40292-40301(2006) [PubMed: 17065153] [Abstract] Cited for: ACETYLATION AT LYS-1336 AND LYS-1473, MASS SPECTROMETRY.
[39]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1554; LYS-1555; LYS-1558 AND LYS-1560, MASS SPECTROMETRY. Tissue: Epithelium.
[40]	"Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription." Hung J.J., Wang Y.T., Chang W.C. Mol. Cell. Biol. 26:1770-1785(2006) [PubMed: 16478997] [Abstract] Cited for: INTERACTION WITH SP1.
[41]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[42]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285; THR-885; THR-887; SER-1038; THR-1857 AND THR-1859, MASS SPECTROMETRY.
[43]	"SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation." Huang C., Han Y., Wang Y., Sun X., Yan S., Yeh E.T.H., Chen Y., Cang H., Li H., Shi G., Cheng J., Tang X., Yi J. EMBO J. 28:2748-2762(2009) [PubMed: 19680224] [Abstract] Cited for: INTERACTION WITH SENP3, SUMOYLATION.
[44]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1734, MASS SPECTROMETRY.
[45]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-636; LYS-977; LYS-981; LYS-1103; LYS-1499; LYS-1542; LYS-1546; LYS-1549; LYS-1554; LYS-1555; LYS-1558; LYS-1560; LYS-1583; LYS-1590 AND LYS-1674, MASS SPECTROMETRY.
[46]	"Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha." Freedman S.J., Sun Z.-Y.J., Poy F., Kung A.L., Livingston D.M., Wagner G., Eck M.J. Proc. Natl. Acad. Sci. U.S.A. 99:5367-5372(2002) [PubMed: 11959990] [Abstract] Cited for: STRUCTURE BY NMR OF 302-418 IN COMPLEX WITH 786-826 OF HIF1A.
[47]	"The structural basis of protein acetylation by the p300/CBP transcriptional coactivator." Liu X., Wang L., Zhao K., Thompson P.R., Hwang Y., Marmorstein R., Cole P.A. Nature 451:846-850(2008) [PubMed: 18273021] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1287-1666 IN COMPLEX WITH LYS-COA, MUTAGENESIS OF THR-1357; SER-1396; TYR-1397; GLU-1505; ASP-1625 AND ASP-1628.
[48]	"Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation." Feng H., Jenkins L.M.M., Durell S.R., Hayashi R., Mazur S.J., Cherry S., Tropea J.E., Miller M., Wlodawer A., Appella E., Bai Y. Structure 17:202-210(2009) [PubMed: 19217391] [Abstract] Cited for: STRUCTURE BY NMR OF 1723-1812, INTERACTION WITH TP53.
[49]	"Mutations truncating the EP300 acetylase in human cancers." Gayther S.A., Batley S.J., Linger L., Bannister A., Thorpe K., Chin S.-F., Daigo Y., Russell P., Wilson A., Sowter H.M., Delhanty J.D.A., Ponder B.A.J., Kouzarides T., Caldas C. Nat. Genet. 24:300-303(2000) [PubMed: 10700188] [Abstract] Cited for: VARIANTS BREAST CANCER PRO-827 AND GLY-1013, VARIANT PANCREATIC CANCER TYR-1650, VARIANT COLORECTAL CANCER GLN-2221.
+	Additional computationally mapped references.

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Web resources

GeneReviews

Wikipedia

P300/CBP entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U01877 mRNA. Translation: AAA18639.1.
AL080243, AL035658, AL096765 Genomic DNA. Translation: CAH70384.1.
AL096765, AL035658, AL080243 Genomic DNA. Translation: CAH73688.1.
AL035658, AL080243, AL096765 Genomic DNA. Translation: CAI23037.1.
CH471095 Genomic DNA. Translation: EAW60408.1.

IPI

IPI00020985.

PIR

A54277.

RefSeq

NP_001420.2.

UniGene

Hs.517517

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L3E	NMR	-	B	323-423	[»]
1P4Q	NMR	-	B	323-423	[»]
2K8F	NMR	-	A	1723-1812	[»]
3BIY	X-ray	1.70	A	1287-1666	[»]
3I3J	X-ray	2.33	A/B/C/D/E/F/G/H/I/J/K/L	1040-1161	[»]
3IO2	X-ray	2.50	A	1723-1836	[»]

SMR

Q09472. Positions 566-652, 1663-1713, 2050-2092.

ModBase

Protein-protein interaction databases

DIP

DIP-257N.

IntAct

Q09472. 23 interactions.

STRING

Q09472.

PTM databases

PhosphoSite

Q09472.

Proteomic databases

PRIDE

Q09472.

Genome annotation databases

Ensembl

ENST00000263253; ENSP00000263253; ENSG00000100393; Homo sapiens. [Genome view]

GeneID

2033.

KEGG

hsa:2033.

Organism-specific databases

CTD

2033.

GeneCards

GC22P039812.

H-InvDB

HIX0027847.

HGNC

HGNC:3373. EP300.

HPA

CAB000146.
HPA003128.
HPA004112.

MIM

180849. phenotype.
602700. gene.

Orphanet

783. Rubinstein-Taybi syndrome.

PharmGKB

PA27807.

GenAtlas

Phylogenomic databases

eggNOG

prNOG11621.

HOGENOM

HBG402903.

HOVERGEN

Q09472.

InParanoid

Q09472.

OMA

RRQQMMQ.

OrthoDB

EOG9WWV3Q.

PhylomeDB

Q09472.

Enzyme and pathway databases

BRENDA

2.3.1.48. 247.

Pathway_Interaction_DB

pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
hnf3apathway. FOXA1 transcription factor network.
foxm1pathway. FOXM1 transcription factor network.
foxopathway. FoxO family signaling.
hif1_tfpathway. HIF-1-alpha transcription factor network.
ifngpathway. IFN-gamma pathway.
ar_tf_pathway. Regulation of Androgen receptor activity.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classiii_pathway. Signaling events mediated by HDAC Class III.

Gene expression databases

ArrayExpress

Q09472.

Bgee

Q09472.

CleanEx

HS_EP300.

Genevestigator

Q09472.

GermOnline

ENSG00000100393. Homo sapiens.

Family and domain databases

InterPro

IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR010303. DUF902_CREBbp.
IPR003101. KIX.
IPR009110. Nuc_rcpt_coact.
IPR014744. Nuc_rcpt_coact_CREBbp.
IPR000197. Znf_TAZ.
IPR000433. Znf_ZZ.
[Graphical view]

Gene3D

G3DSA:1.20.920.10. Bromodomain. 1 hit.
G3DSA:1.10.246.20. KIX. 1 hit.
G3DSA:1.10.1630.10. Nuc_rcpt_coact_CREBbp. 1 hit.
G3DSA:1.20.1020.10. Znf_TAZ. 2 hits.

Pfam

PF00439. Bromodomain. 1 hit.
PF09030. Creb_binding. 1 hit.
PF06001. DUF902. 1 hit.
PF02172. KIX. 1 hit.
PF02135. zf-TAZ. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 1 hit.
SM00551. ZnF_TAZ. 2 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]

PROSITE

PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS50952. KIX. 1 hit.
PS50134. ZF_TAZ. 2 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

ProtoNet

Other Resources

SOURCE

Entry information

Entry name

EP300_HUMAN

Accession

Primary (citable) accession number: Q09472
Secondary accession number(s): B1AKC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 10, 2009
Last modified:	February 9, 2010
This is version 137 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.