EP300 (E1A binding protein p300)

2014-11-01   Gloria Negri , Cristina Gervasini 

Department of Health Science, Medical Genetics, Universita degli Studi di Milano, Milano, Italy




Atlas Image
Schematic representation of EP300 gene. Black boxes represent exons and gray ones 5 and 3 UTRs. Thin black lines represent introns. (Modified from Zimmerman et al., 2007).


p300 was first discovered on the basis of its interaction with the adenoviral protein E1A and EP300 locus was subsequently mapped to the long arm of chromosome 22, spanning about 88 kb (Whyte et al., 1989; Eckner et al., 1994).


EP300 has only one splice variant derived from the splicing of its 31 exons with an mRNA of 9585 bp which includes 1219 and 1121 bp of 5UTR and 3UTR, respectively.


No pseudogenes are known.


Atlas Image
Schematic structure of p300 protein including its functional and structural domains and their localization. NLS (nuclear localization signal), CH1 (cysteine/histidine-rich region 1, also known as transcriptional-adaptor zinc-finger domain 1 or TAZ1), KIX (kinase inducible domain of CREB interacting domain), BROMO (bromodomain), PHD (plant homeodomain finger), KAT11 (lysine acetyltransferase domain), ZZ (ZZ-type zinc finger domain), TAZ2 (transcriptional-adaptor zinc-finger domain 2; ZZ and TAZ2 together are sometimes referred to as CH3 or cysteine/histidine-rich region 3), and IBiD (IRF3-binding domain). Aminoacid positions are from UniGene NP_001420.2.


p300 is a large size protein of about 264 kDa belonging to the KAT3 (lysine or K-acetyltransferase) family (Valor et al., 2013).
p300 shares a modular organization consisting in several conserved domains including a central chromatin association and modification region which includes the bromodomain/PHD finger module and the KAT11 domain (Rack et al., 2014) which is flanked by four transactivation domains (TADs): i) the CH1 that encompasses the TAZ1 domain, ii) the KIX domain, iii) another CH3 containing the TAZ2 domain and a ZZ domain, and iv) the IBiD (Bedford et al., 2012; Wang et al., 2013).
The Bromodomain mediates p300 binding to acetylated histones, nucleosomes and transcriptional factors and could therefore play a role in tethering p300 to specific chromosomal sites (Kalkhoven et al., 2004; Rack et al., 2014) moreover, the associated PHD finger is an integral part of the enzymatic core of the protein influencing its ability to recognize and acetylate both itself as well as histones and non-histone substrates (Kalkhoven et al., 2004; Wang et al., 2013; Rack et al., 2014). The KAT11 catalytic domain can acetylate p300 itself and a variety of histonic and non-histonic proteins and the CH rich regions are able to bind zinc and are involved in protein-protein interaction (Valor et al., 2013; Wang et al., 2013).
p300 has also multiple specific interaction domains for different transcriptional factors such as the KIX domain that mediates CREB-p300 interaction and CREB phosphorylation at serine 133 residue but also for the Retinoic Acid Receptor-related orphan receptor A (RORA) and for ALX1 at the N-term end of the protein and for Interferons at C-term end.


p300 is ubiquitously expressed in human tissues (Kalkhoven et al., 2004; Valor et al., 2013). p300 is highly evolutionary conserved and present in many multicellular organisms including flies, worms and plants but not in lower eukaryotes such as yeasts (Kalkhoven et al., 2004).


p300 is a nuclear protein which resides in a specific nuclear structure called nuclear body (Chan and La Thangue, 2001).


p300 is a transcriptional coactivator with intrinsic lysine acetyltransferase activity able to regulate transcription and gene expression in different ways.
1) Acetylation of histones tails: p300 can enable transcription through the catalytic activity of its KAT domain which is able to acetylate promoter nucleosomal histones resulting in chromatin remodelling and relaxation and in increased accessibility of the DNA to other essential regulators (Kalhoven et al., 2004; Wang et al., 2013). Thanks to its ability in modifying chromatin structure by histone acetylation, p300 can be defined as "writer" of the epigenetic code (Berdasco et al., 2013).
2) Acetylation of other target proteins: p300 can also acetylate other kinds of proteins, such as transcriptional factors, modulating their activity positively or negatively, or coactivators.
Acetylation of non-histone substrates can result in either positive or negative effects on transcription by affecting protein-protein interactions (activator of thyroid and retinoid receptors ACTR), protein-DNA interactions (the high mobility group protein HMGI), nuclear retention (the hepatocyte nuclear factor HNF4) or protein half-life (E2F).
For example some acetylated p300 targets regulate the expression of histone methyltransferase leading to chromatin condensation and gene silencing.
3) RNA Polymerase II stabilization: p300 functions as a "bridge" linking the DNA-bound transcription factors (activators) to the basal transcription machinery through direct interaction with TFIID, including TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs) and TFIIB promoting the pre-initiation complex (PIC) assembly (Wang et al., 2013).

p300 has also some more indirect chromatin-related roles:
4) DNA replication and repair: p300 interacts with various replication and repair proteins, including proliferating cell nuclear antigen (PCNA), the Recq4 helicase, Flap endonuclease 1 (Fen1), DNA polymerase b and thymine DNA glycosylase, with the latter three also serving as acetylation substrates.
5) Cell cycle regulation: p300 associates with the complex formed between cyclin E and cyclin-dependent kinase 2 (cdk2) regulating proper progression of the cell cycle.
6) p53 activity regulation: p300 is involved in p53 degradation, which depends on the murine double minute 2 protein (MDM2). Degradation and ubiquitination of p53 is dependent on MDM2, and a ternary complex between these two proteins and p300 regulates the turnover of p53 itself in cycling cells. Furthermore, the CH-1 region of p300 displays polyubiquitin ligase activity towards p53, and could therefore play a key role in controlling p53 levels.
7) Nuclear import: p300 can acetylate two proteins involved in regulating nuclear import, the importin-α1 isoform Rch1 and importin-α7, and could therefore play a role in this process.
Because of its ability of interacting with more than 400 partner proteins, p300 can be considered a "hub" (Bedford et al., 2014). Its interactome includes pro-proliferative proteins and oncoproteins: c-Myc, c-Myb, CREB, c-Jun and c-Fos; transforming viral proteins: E1A, and E6; as well as tumor suppressors and pro-apoptotic proteins: Forkhead box class O (FoxO) transcription factors FoxO1, FoxO3a, and FoxO4, signal transducers and activators of transcription (STAT) 1 and STAT 2, Hypoxia-inducible factor 1α (HIF-1α), breast cancer 1 (BRCA1), SMA/MAD homology (Smad) proteins, the Runt-related transcription factor (RUNX), E2 Transcription Factor (E2F), and E-proteins (Wang et al., 2013).

Atlas Image
Comparison of p300 and CBP amino acidic sequences. The blue regions indicate the areas of highest homology with the percentage of amino acid identity specified in between. Position of the corresponding domains are taken from UniGene (NP_001420.2 for EP300 and NP_004371.2 for CREBBP). (Modified from Chan and La Thangue, 2001).


p300 is highly homologous to the cyclic AMP response element-binding (CREB) binding protein (CBP) with 63% identity and 75% similarity at amino-acid level (Narayanan et al., 2004; Wang et al., 20113). CREBBP/CBP locus was mapped on 16p13.3, a region of extensive homology to the one on chromosome 22 where EP300/p300 resides (Chan and La Thangue, 2001; Gervasini, 2010).



Rubinstein-Taybi Syndrome (RSTS; OMIM #180849, #613684).


Cancers derived from almost all tissues and organs, such as those of hematopoietic and lymphoid organs, cancers of eye, skin, bones, thyroid, salivary and adrenal glands, central nervous system (CNS) including meninges, and nervous system (NS) including automatic ganglia, esophagus, upper aerodigestive tract, lung and pleura, stomach, liver, pancreas, biliary tract, large and small intestine, kidney, urinary tract and breast, endometrium, cervix, ovary and prostate.


The identification of mutations in epigenetic genes, classified as writers, readers and erasers based on their function (Berdasco and Esteller, 2013), represents a link between the cancer epigenome and genetic alterations acting as "driver" or "passenger" mutations in cancer development. Actually, many genetic alterations in cancer epigenetic regulators cause cancer-associated phenotype via epigenetic dysfunction (Roy et al., 2014).

Implicated in

Entity name
Rubinstein-taybi syndrome (RSTS; OMIM #180849, #613684)
Germinal mutations leading to loss of function/haploinsufficiency.
Rubinstein-Taybi syndrome is a rare (1:125000 live birth) autosomal dominant neurodevelopmental disorder. It is characterized by postnatal growth retardation, intellectual disability (ID), skeletal anomalies (broad and/or duplicated distal phalanges of thumbs and halluces are a landmark sign) and distinctive facial dysmorphisms including down-slanting palpebral fissures, broad nasal bridge, beaked nose and micrognathia (Hennekam, 2006).
All EP300-mutated RSTS patients described in literature are alive (Roelfsema et al., 2005; Bartholdi et al., 2007; Zimmermann et al., 2007; Foley et al., 2009; Bartsh et al., 2010; Tsai et al., 2011; Negri et al., 2014).
Hybrid gene
The identification of EP300 as the second RSTS causative gene in 2005 (Roelfsema et al., 2005) disclosed the heterogeneous nature of the syndrome. EP300 heterozygous point mutations and intragenic deletions have been detected in about 8% of RSTS CREBBP-negative cases (Negri et al., 2014). Fourteen patients are clinically and genetically described (Roelfsema et al., 2005; Bartholdi et al., 2007; Zimmermann et al., 2007; Foley et al., 2009; Bartsh et al., 2010; Tsai et al., 2011; Negri et al., 2014), while 12 additional alterations are reported in the LOVD database .
Atlas Image
EP300 germline mutations in Rubinstein-Taybi patients (2014 update). A) Point mutations, B) intragenic deletions and C) schematic of the gene with type and localization of all 26 mutations reported so far. (Modified from Negri et al., 2014).
RSTS patients (estimated incidence 5%) have an increased predisposition to malignancies like leukemia, neuroblastoma, meningioma and pilomatrixoma, developed either in the first years of life or in mid-adulthood (30-40 years) (Siraganin et al., 1989; van de Kar, 2014). Glaucomas and keloids are reported too; in particular, EP300-mutated RSTS patients show a slight increase in developing skin anomalies such as keloids (Van Genderen et al., 2000; van de Kar, 2014; Negri et al., 2014).
Entity name
Various cancers
All data are taken from COSMIC database (Catalogue of Somatic Mutations In Cancer) ( Release v70 August 2014).
EP300 point mutations, copy number variations (CNVs) but also gene expression profile alterations have been detected in almost all human cancers independently of the embryonic origin. Out of >14.000 tumor samples tested, those derived from hematopoietic and lymphoid organs, lung, central nervous system (CNS), breast, intestine and ovary show the highest prevalence of EP300 mutations.
Hybrid gene
The majority of EP300 point mutations detected in tumoral samples are heterozygous (Aumann et al., 2014).
Atlas Image
EP300 somatic point mutations load. A) Pie chart of the main kinds of point mutations and relative numbers, B) bar chart of the distribution of the mutations within the gene domains and C) recurrent mutations and localization. Data are reworked from COSMIC database.
The oncogenic mechanism by which EP300 mutations act is not yet clear, but as the most frequently mutated region is the lysine acetyltransferase domain, which catalyzes acetylation of histones and other essential proteins, aberrant acetyltransferase activity may be a key feature. In vitro studies demonstrated reduced H3K18 acetylation, as well as decreased ability to acetylate p53 and BCL6, in p300- mutated cells (Peifer et al., 2012). Because of p300 multiple functions and diverse interactions, many intertwisted mechanisms could play a role in the different mutations effects.
Entity name
t(11;22)(q23;q13) --> resulting in KMT2A -EP300 fusion gene
Somatic mutations.
Therapy-related leukemias and myeloid neoplasms.
Ida et al., described the first patient presenting the karyotype 48,XY,+8,+8,(11;22)(q23;q13); the same group (Ohnishi et al.) described a second patient with 46,XX,t(1;22;11)(q44;q13;q23), t(10;17)(q22,q21), while a third patient, with 46;XY,t(11;22)(q23;q13)[15]/47,idem,+8[2], was reported by Duhoux et al.
Hybrid gene
Rearrangements of the mixed lineage leukemia (MLL1 or KMT2A; gene ID: 4297) locus are frequently encountered in acute leukemias and at least 104 different chromosomal rearrangements involving MLL1 itself with more than 64 translocation partner genes have been described (Meyer et al., 2009) while rearrangements of EP300 gene locus seem to be rare events.
Only three cases of MLL1-EP300 fusion genes have been described, all in therapy-related leukemia patients following chemoterapy with topoisomerase II inhibitors. The first patient was initially diagnosed as having non-Hodgkin lymphoma and, after conventional chemotherapy, he developed secondary AML which was cytogenetically characterized as t(11;22)(q23;q13) producing a chimeric MLL1-EP300 gene in which the exon 9 of MLL1 was juxtaposed to EP300 exon 15 (Ida et al., 1997). The second case is a girl who developed AML after chemotherapy for neuroblastoma. She presented a complex karyotype 46,XX,t(1;22;11)(q44;q13;q23),t(10;17)(q22,q21) with the fusion of MLL1 exon 8 to EP300 exon 15 and also a less expressed clone in which exon 7 of MLL1 is fused with exon 15 of EP300, which was considered to be generated by alternative splicing (Ohnishi et al., 2008). The third patient presented AML with myelodysplasia-related changes evolving after chemotherapy in acute myelomonocytic leukaemia (AMML). Leukemic cells were cytologically characterised as 46;XY,t(11;22)(q23;q13)[15]/47,idem,+8[2] including the fusion of exon 10, or exon 11 resulting from alternative splicing, of MLL1 with exon 13 of EP300 (Duhoux et al., 2011).
All chimeric proteins retain almost the same part of both MLL1, including the AT-hook, the DNA methyltransferase and the transcriptional repression domains and p300, i.e. the bromodomain, the catalytic KAT and TADs
Atlas Image
t(11;22)(q23;q13) leads to fusion of MLL1 gene to EP300. A) Schematic representation of MLL1, p300 and the predicted MLL1-p300 fusion proteins of all reported cases (Ida et al., 1997; Ohnishi et al. 2008; Duhoux et al., 2011). B) Nucleotide sequences of the hybrid junctions of the chimeric MLL1-EP300 genes and relative references. Breakpoints are indicated by arrows; AT: AT hooks, NLS: nuclear localization signals, CxxC: motif recognizing unmethylated CpG dinucleotides, PHD: plant homeodomain fingers, TAD: transactivation domain, SET: histone methyltransferase active sites; CH: cystidine/histidine-rich; KIX: kinase inhibitory domain, Bromo: bromodomain, KAT: Lysine acetyltransferase domain. (Modified from Duhoux et al., 2011).
The fusion of MLL1 with the lysine-acetyltransferase p300 supposedly leads to hyperacetylation of chromatin which contributes to increase the transcriptional output conferring a significant oncogenic advantage to the cells. Furthermore, nuclear factors, such as p300, have transcriptional activity and their function might be deregulated by the fusion with MLL1 (Ohnishi et al., 2008; Duhoux et al., 2011).
The translocation t(11;22)(q23;q13) involving MLL1-EP300 is characteristic of therapy related leukemias where it is likely driven by topoisomerase II inhibitors, rather than of de novo leukaemias.
Entity name
t(8;22)(p11;q13) resulting in KAT6A - EP300 fusion gene
Somatic mutations.
de novo, progression or therapy-related AML.
The t(8;22)(p11;q13) is a rare translocation found in acute myeloid leukaemia (AML) described in only three patients (Lai et al., 1992; Soenen et al., 1996; Chaffanet et al., 2000; Kitabayashi et al., 2000; Tasaka et al., 2002). The first patient was diagnosed as having a de novo AML with karyotype 47, XY,+8,t(8;22)(p11;q13), while the second patient suffered from a chronic myelomonocytic leukaemia (CMML) which evolved in AML with the abnormal karyotype: 46,XY,t(8;22)(p11;q13)/idem,+der(8)t(8;22)(p11;q13)del(17)(p11) (Lai et al., 1992; Soenen et al., 1996; Chaffanet et al., 2000). The third case is a man with primary macroglobulinemia who developed a secondary AML during chemotherapy, with the karyotype: 47, XY, t(8;22)(p11.2;q13.1),+der(8)t(8;22)(22qter→22q13.1::8p11.2→8q13::8q22→8qter),add(19)(p13.3) (Kitabayashi et al., 2001; Tasaka et al., 2002).
Hybrid gene
Monocytic leukemia zinc finger gene (MOZ, Gene ID: 7994) codifies for a Myst (MOZ, Ybf2 (Sas3), Sas2, Tip60)-type lysine acetyltransferase (KAT) also named KAT6A (lysine acetyltransferase 6A).
The gene underlies chromosomal translocation with different partners, generating fusion genes, such as MOZ-TIF2, MOZ-CBP and MOZ-EP300 in acute myeloid leukemia (AML). All MOZ fusion partner genes are involved in histone modification and transcriptional regulation (Katsumoto et al., 2008).
To date, only three cases of t(8;22)(p11;q13) involving MOZ and EP300 have been reported and investigated at DNA and RNA levels in two of them (Lai et al., 1992; Soenen et al., 1996; Chaffanet et al., 2000; Kitabayashi et al., 2001; Tasaka et al., 2002).
In Chaffanet et al., and in Kitabayashi et al., MOZ-EP300 fusion genes result from the hybrid junction between exon 16 and exon 15 of MOZ with exons 2 and 3 of EP300, respectively.
In both cases, the MOZ breakpoints are located in or around its acidic domain resulting in the retention of its N-terminal region and the replacement of the C-terminal end with the p300 fusion partner. The N-terminal region of MOZ contains a H15 (histone H1/H5) domain related to nuclear localization, a PHD (plant homeobox-like domain) zinc finger involved in binding to methylated histones, a basic domain and a Myst-type KAT domain. The KAT domain contains C2HC zinc finger and helix-turn-helix motifs that bind to nucleosomes and DNA. Because of the early truncation of EP300 , almost all its functional domains are conserved, including the KAT, the bromodomain and the CH1-3, resulting in a fusion protein with both MOZ and p300 KAT domains.
In the reciprocal fusion genes, EP300-MOZ, exon 1 or 2 of EP300 are juxtaposed to exons 17 and 16 of MOZ, respectively. In both cases, the N-terminal region including only the nuclear receptor interaction domain (NID) of p300 and the C-terminal of MOZ encompassing its serine, proline-glutammine and methionine-rich regions are conserved (Chaffanet et al., 2000; Kitabayashi et al., 2001).
Atlas Image
Schematic representation of the p300, MOZ, MOZ-p300 and p300-MOZ proteins. A) p300, MOZ, p300-MOZ and MOZ-p300 diagram of the first case and B) p300, MOZ, p300-MOZ and MOZ-p300 diagram of the third one.
Red arrows indicate the breakpoints of the translocations and nucleotide sequences of WT and hybrid junctions are reported. The functional domains of MOZ and p300 as well as those of fusion proteins are indicated above and beneath the diagrams.
NID: nuclear receptor interaction domain, CH1-3: cysteine/histidine-rich domain, CID: CREB-interaction domain, B: bromodomain, KAT: lysine acetyltransferase domain, Q: glutamine-rich region, PH: PHD class zinc finger, MYST: MOZ, YB1, SAS, TIP homology domain, S: serine-rich region, PQ: proline/glutamine region, M: methionine-rich region. (Modified from Kitabayashi et al., 2001).
The conservation of MOZ and p300 KAT catalytic domains in the hybrid proteins MOZ-p300 may result in abnormal acetylation of histonic and non histonic proteins with a consequent alteration in gene expression regulation, leading to leukaemogenesis; furthermore, MOZ-p300 fusion proteins retain the domains required for the interaction with AML1 thus affecting AML1-dependent transcription whose deregulation may be implicated in leukaemogenesis too (Kitabayashi et al., 2001).


Pubmed IDLast YearTitleAuthors
251118212014Somatic alterations and dysregulation of epigenetic modifiers in cancers.Aumann S et al
172202152007Genetic heterogeneity in Rubinstein-Taybi syndrome: delineation of the phenotype of the first patients carrying mutations in EP300.Bartholdi D et al
200142642010Two patients with EP300 mutations and facial dysmorphism different from the classic Rubinstein-Taybi syndrome.Bartsch O et al
225116392012Is histone acetylation the most important physiological function for CBP and p300?Bedford DC et al
233705042013Genetic syndromes caused by mutations in epigenetic genes.Berdasco M et al
108249982000MOZ is fused to p300 in an acute monocytic leukemia with t(8;22).Chaffanet M et al
115597452001p300/CBP proteins: HATs for transcriptional bridges and scaffolds.Chan HM et al
209800532011Novel variant form of t(11;22)(q23;q13)/MLL-EP300 fusion transcript in the evolution of an acute myeloid leukemia with myelodysplasia-related changes.Duhoux FP et al
75871351994The adenovirus E1A-associated 300-kD protein exhibits properties of a transcriptional coactivator and belongs to an evolutionarily conserved family.Eckner R et al
193536452009Further case of Rubinstein-Taybi syndrome due to a deletion in EP300.Foley P et al
168685632006Rubinstein-Taybi syndrome.Hennekam RC et al
93896841997Adenoviral E1A-associated protein p300 is involved in acute myeloid leukemia with t(11;22)(q23;q13).Ida K et al
153134122004CBP and p300: HATs for different occasions.Kalkhoven E et al
187548622008Roles of the histone acetyltransferase monocytic leukemia zinc finger protein in normal and malignant hematopoiesis.Katsumoto T et al
112434052001Fusion of MOZ and p300 histone acetyltransferases in acute monocytic leukemia with a t(8;22)(p11;q13) chromosome translocation.Kitabayashi I et al
16065611992Acute monocytic leukemia with (8;22)(p11;q13) translocation. Involvement of 8p11 as in classical t(8;16)(p11;p13).Lai JL et al
192625982009New insights to the MLL recombinome of acute leukemias.Meyer C et al
244764202015Clinical and molecular characterization of Rubinstein-Taybi syndrome patients carrying distinct novel mutations of the EP300 gene.Negri G et al
187783672008A complex t(1;22;11)(q44;q13;q23) translocation causing MLL-p300 fusion gene in therapy-related acute myeloid leukemia.Ohnishi H et al
229411882012Integrative genome analyses identify key somatic driver mutations of small-cell lung cancer.Peifer M et al
251580952014The PHD finger of p300 influences its ability to acetylate histone and non-histone targets.Rack JGM et al
157064852005Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease.Roelfsema JH et al
246228422014Driver mutations of cancer epigenomes.Roy DM et al
25863631989Keloids and neoplasms in the Rubinstein-Taybi syndrome.Siraganian PA et al
87216861996Identification of a YAC spanning the translocation breakpoint t(8;22) associated with acute monocytic leukemia.Soenen V et al
120106822002Secondary acute monocytic leukemia with a translocation t(8;22)(p11;q13).Tasaka T et al
207171662011Exon deletions of the EP300 and CREBBP genes in two children with Rubinstein-Taybi syndrome detected by aCGH.Tsai AC et al
234484612013Lysine acetyltransferases CBP and p300 as therapeutic targets in cognitive and neurodegenerative disorders.Valor LM et al
233070742013Transcriptional/epigenetic regulator CBP/p300 in tumorigenesis: structural and functional versatility in target recognition.Wang F et al
25213011989Cellular targets for transformation by the adenovirus E1A proteins.Whyte P et al
172994362007Confirmation of EP300 gene mutations as a rare cause of Rubinstein-Taybi syndrome.Zimmermann N et al
110041072000Ocular features in Rubinstein-Taybi syndrome: investigation of 24 patients and review of the literature.van Genderen MM et al
251320002014Keloids in Rubinstein-Taybi syndrome: a clinical study.van de Kar AL et al

Other Information

Locus ID:

NCBI: 2033
MIM: 602700
HGNC: 3373
Ensembl: ENSG00000100393


dbSNP: 2033
ClinVar: 2033
TCGA: ENSG00000100393


Gene IDTranscript IDUniprot

Expression (GTEx)



PathwaySourceExternal ID
Cell cycleKEGGko04110
Wnt signaling pathwayKEGGko04310
Notch signaling pathwayKEGGko04330
TGF-beta signaling pathwayKEGGko04350
Adherens junctionKEGGko04520
Jak-STAT signaling pathwayKEGGko04630
Long-term potentiationKEGGko04720
Huntington's diseaseKEGGko05016
Renal cell carcinomaKEGGko05211
Prostate cancerKEGGko05215
Cell cycleKEGGhsa04110
Wnt signaling pathwayKEGGhsa04310
Notch signaling pathwayKEGGhsa04330
TGF-beta signaling pathwayKEGGhsa04350
Adherens junctionKEGGhsa04520
Jak-STAT signaling pathwayKEGGhsa04630
Long-term potentiationKEGGhsa04720
Huntington's diseaseKEGGhsa05016
Pathways in cancerKEGGhsa05200
Renal cell carcinomaKEGGhsa05211
Prostate cancerKEGGhsa05215
Influenza AKEGGko05164
Influenza AKEGGhsa05164
HTLV-I infectionKEGGko05166
HTLV-I infectionKEGGhsa05166
Herpes simplex infectionKEGGko05168
Herpes simplex infectionKEGGhsa05168
Epstein-Barr virus infectionKEGGhsa05169
Epstein-Barr virus infectionKEGGko05169
Viral carcinogenesisKEGGhsa05203
Viral carcinogenesisKEGGko05203
Hepatitis BKEGGhsa05161
HIF-1 signaling pathwayKEGGhsa04066
MicroRNAs in cancerKEGGhsa05206
MicroRNAs in cancerKEGGko05206
FoxO signaling pathwayKEGGhsa04068
Thyroid hormone signaling pathwayKEGGhsa04919
cAMP signaling pathwayKEGGhsa04024
cAMP signaling pathwayKEGGko04024
Glucagon signaling pathwayKEGGhsa04922
Glucagon signaling pathwayKEGGko04922
Metabolism of proteinsREACTOMER-HSA-392499
Post-translational protein modificationREACTOMER-HSA-597592
Diseases of signal transductionREACTOMER-HSA-5663202
Signaling by NOTCH1 in CancerREACTOMER-HSA-2644603
Signaling by NOTCH1 PEST Domain Mutants in CancerREACTOMER-HSA-2644602
Constitutive Signaling by NOTCH1 PEST Domain MutantsREACTOMER-HSA-2644606
Signaling by NOTCH1 HD+PEST Domain Mutants in CancerREACTOMER-HSA-2894858
Constitutive Signaling by NOTCH1 HD+PEST Domain MutantsREACTOMER-HSA-2894862
Immune SystemREACTOMER-HSA-168256
Innate Immune SystemREACTOMER-HSA-168249
RIG-I/MDA5 mediated induction of IFN-alpha/beta pathwaysREACTOMER-HSA-168928
TRAF3-dependent IRF activation pathwayREACTOMER-HSA-918233
TRAF6 mediated IRF7 activationREACTOMER-HSA-933541
Cytosolic sensors of pathogen-associated DNAREACTOMER-HSA-1834949
LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN productionREACTOMER-HSA-3134973
C-type lectin receptors (CLRs)REACTOMER-HSA-5621481
CD209 (DC-SIGN) signalingREACTOMER-HSA-5621575
Factors involved in megakaryocyte development and platelet productionREACTOMER-HSA-983231
Signal TransductionREACTOMER-HSA-162582
Signaling by NOTCHREACTOMER-HSA-157118
Pre-NOTCH Expression and ProcessingREACTOMER-HSA-1912422
Pre-NOTCH Transcription and TranslationREACTOMER-HSA-1912408
Signaling by NOTCH1REACTOMER-HSA-1980143
NOTCH1 Intracellular Domain Regulates TranscriptionREACTOMER-HSA-2122947
Signaling by NOTCH2REACTOMER-HSA-1980145
NOTCH2 intracellular domain regulates transcriptionREACTOMER-HSA-2197563
Signaling by WntREACTOMER-HSA-195721
TCF dependent signaling in response to WNTREACTOMER-HSA-201681
Formation of the beta-catenin:TCF transactivating complexREACTOMER-HSA-201722
Gene ExpressionREACTOMER-HSA-74160
Generic Transcription PathwayREACTOMER-HSA-212436
Transcriptional Regulation by TP53REACTOMER-HSA-3700989
Epigenetic regulation of gene expressionREACTOMER-HSA-212165
Cell CycleREACTOMER-HSA-1640170
Cell Cycle, MitoticREACTOMER-HSA-69278
Mitotic G2-G2/M phasesREACTOMER-HSA-453274
G2/M TransitionREACTOMER-HSA-69275
Polo-like kinase mediated eventsREACTOMER-HSA-156711
Circadian ClockREACTOMER-HSA-400253
BMAL1:CLOCK,NPAS2 activates circadian gene expressionREACTOMER-HSA-1368108
RORA activates gene expressionREACTOMER-HSA-1368082
Metabolism of lipids and lipoproteinsREACTOMER-HSA-556833
Fatty acid, triacylglycerol, and ketone body metabolismREACTOMER-HSA-535734
Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha)REACTOMER-HSA-400206
PPARA activates gene expressionREACTOMER-HSA-1989781
Developmental BiologyREACTOMER-HSA-1266738
Transcriptional regulation of white adipocyte differentiationREACTOMER-HSA-381340
Cellular responses to stressREACTOMER-HSA-2262752
Cellular response to hypoxiaREACTOMER-HSA-2262749
Regulation of Hypoxia-inducible Factor (HIF) by oxygenREACTOMER-HSA-1234174
Regulation of gene expression by Hypoxia-inducible FactorREACTOMER-HSA-1234158
Cellular response to heat stressREACTOMER-HSA-3371556
HSF1-dependent transactivationREACTOMER-HSA-3371571
Attenuation phaseREACTOMER-HSA-3371568
Chromatin organizationREACTOMER-HSA-4839726
Chromatin modifying enzymesREACTOMER-HSA-3247509
HATs acetylate histonesREACTOMER-HSA-3214847
Nucleotide Excision RepairREACTOMER-HSA-5696398
Transcription-Coupled Nucleotide Excision Repair (TC-NER)REACTOMER-HSA-6781827
Formation of TC-NER Pre-Incision ComplexREACTOMER-HSA-6781823
Dual incision in TC-NERREACTOMER-HSA-6782135
Gap-filling DNA repair synthesis and ligation in TC-NERREACTOMER-HSA-6782210
Positive epigenetic regulation of rRNA expressionREACTOMER-HSA-5250913
B-WICH complex positively regulates rRNA expressionREACTOMER-HSA-5250924
Activation of HOX genes during differentiationREACTOMER-HSA-5619507
Activation of anterior HOX genes in hindbrain development during early embryogenesisREACTOMER-HSA-5617472
TP53 Regulates Transcription of Cell Cycle GenesREACTOMER-HSA-6791312
TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle ArrestREACTOMER-HSA-6804114
Regulation of TP53 ActivityREACTOMER-HSA-5633007
Regulation of TP53 Activity through MethylationREACTOMER-HSA-6804760
Regulation of TP53 Activity through AcetylationREACTOMER-HSA-6804758
Transcriptional regulation by the AP-2 (TFAP2) family of transcription factorsREACTOMER-HSA-8864260
Activation of the TFAP2 (AP-2) family of transcription factorsREACTOMER-HSA-8866907
Metalloprotease DUBsREACTOMER-HSA-5689901
PI5P Regulates TP53 AcetylationREACTOMER-HSA-6811555

Protein levels (Protein atlas)

Not detected


Pubmed IDYearTitleCitations
119317692002The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1.311
213901262011Inactivating mutations of acetyltransferase genes in B-cell lymphoma.301
192706802009CBP/p300-mediated acetylation of histone H3 on lysine 56.286
211319052011Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated H3K18/27ac in nuclear receptor transactivation.286
204188692010miR-132 regulates antiviral innate immunity through suppression of the p300 transcriptional co-activator.153
126902032003Polyubiquitination of p53 by a ubiquitin ligase activity of p300.140
156321932005SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1.132
157064852005Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease.114
192736022009Acetylation of Nrf2 by p300/CBP augments promoter-specific DNA binding of Nrf2 during the antioxidant response.114
258186472015Intracellular crotonyl-CoA stimulates transcription through p300-catalyzed histone crotonylation.106


Gloria Negri ; Cristina Gervasini

EP300 (E1A binding protein p300)

Atlas Genet Cytogenet Oncol Haematol. 2014-11-01

Online version: http://atlasgeneticsoncology.org/gene/97/ep300-(e1a-binding-protein-p300)

Historical Card

2000-01-01 EP300 (E1A binding protein p300) by  Jean-Loup Huret 

Genetics, Dept Medical Information, University of Poitiers, CHU Poitiers Hospital, F-86021 Poitiers, France