Gene Report

Basic Information

Approved Symbol	EP300
Approved Name	E1A binding protein p300
Symbol Alias	p300, KAT3B
Name Alias	histone acetyltransferase p300
Location	22q13.2
Position	chr22:41488614-41576081 (+)
External Links	Entrez Gene: 2033 Ensembl: ENSG00000100393 UCSC: uc003azl.4 HGNC ID: 3373
No. of Studies (Positive/Negative)	1(1/0)
Type	Literature-origin

Positive relationships between EP300 and MDD (count: 1)

Name in Literature	Reference	Research Type	Statistical Result	Relation Description
EP300	Aston, 2005	patients and normal controls		Genes altered in major depressive disorder Genes altered in major depressive disorder

Positive relationships between EP300 and other components at different levels (count: 0)

Positive relationship network of EP300 in MK4MDD

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Note:
1. The different color of the nodes denotes the level of the nodes.

Genetic/Epigenetic Locus	Protein and Other Molecule	Cell and Molecular Pathway	Neural System	Cognition and Behavior	Symptoms and Signs	Environment	MDD

2. Besides the component related relationships from literature, gene mapped protein and protein mapped gene are also shown in the network. If the mapped gene or protein is not from literature, square node would be used instead of Circle node. Accordingly, the relationship is marked with dot line.
2. User can drag the nodes to rearrange the layout of the network. Click the node will enter the report page of the node. Right-click will show also the menus to link to the report page of the node and remove the node and related edges. Hover the node will show the level of the node and hover the edge will show the evidence/description of the edge.
3. The network is generated using Cytoscape Web

Negative relationships between EP300 and MDD (count: 0)

Negative relationships between EP300 and other components at different levels (count: 0)

EP300 related SNPs in MK4MDD (count: 0)

EP300 related proteins in MK4MDD (count: 1)

Approved Name	UniportKB	No. of Studies (Positive/Negative)	Source
Histone acetyltransferase p300	Q09472	0(0/0)	Gene mapped

EP300 related GO terms (count: 51)

ID	Name	Type	Evidence
Literature-origin GO terms
GO:0006915	apoptotic process	biological process	IMP[9194565]

ID	Name	Type	Evidence
Gene mapped GO terms
GO:0009887	organ morphogenesis	biological process	IEA
GO:0005737	cytoplasm	cellular component	IDA
GO:0007399	nervous system development	biological process	TAS[10205054]
GO:0032092	positive regulation of protein binding	biological process	IEA
GO:0008134	transcription factor binding	molecular function	IPI[15261140]
GO:0030324	lung development	biological process	IEA
GO:0016746	transferase activity, transferring acyl groups	molecular function	IDA[17403783]
GO:0007507	heart development	biological process	IEA
GO:0004468	lysine N-acetyltransferase activity	molecular function	IDA
GO:0018076	N-terminal peptidyl-lysine acetylation	biological process	IDA[12435739]
GO:0003677	DNA binding	molecular function	IDA[9194565]
GO:0005730	nucleolus	cellular component	IDA
GO:0000122	negative regulation of transcription from RNA polymerase II promoter	biological process	IDA[10733570]
GO:0003682	chromatin binding	molecular function	IMP[17641689]
GO:0033613	activating transcription factor binding	molecular function	IPI
GO:0002039	p53 binding	molecular function	IEA
GO:0008013	beta-catenin binding	molecular function	IPI[12408825]
GO:0001666	response to hypoxia	biological process	IDA[9887100]
GO:0006351	transcription, DNA-dependent	biological process	IEA
GO:0050681	androgen receptor binding	molecular function	IPI[18487222]
GO:0045087	innate immune response	biological process	TAS
GO:0001047	core promoter binding	molecular function	IDA[17641689]
GO:0061418	regulation of transcription from RNA polymerase II promoter in response to hypoxia	biological process	TAS
GO:0071456	cellular response to hypoxia	biological process	TAS
GO:0007049	cell cycle	biological process	IEA
GO:0001756	somitogenesis	biological process	IEA
GO:0045944	positive regulation of transcription from RNA polymerase II promoter	biological process	IDA[12586840]; IMP[16325578]
GO:0007519	skeletal muscle tissue development	biological process	IEA
GO:0042771	intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator	biological process	IDA[17403783]
GO:0051091	positive regulation of sequence-specific DNA binding transcription factor activity	biological process	IDA[10518217]
GO:0033554	cellular response to stress	biological process	TAS
GO:0005667	transcription factor complex	cellular component	IEA
GO:0007219	Notch signaling pathway	biological process	TAS
GO:0018393	internal peptidyl-lysine acetylation	biological process	IDA[17403783]
GO:0003713	transcription coactivator activity	molecular function	IDA[16687403]; IDA[12929931]
GO:0043923	positive regulation by host of viral transcription	biological process	IDA[16687403]
GO:0031490	chromatin DNA binding	molecular function	IEA
GO:0000123	histone acetyltransferase complex	cellular component	IEA
GO:0001102	RNA polymerase II activating transcription factor binding	molecular function	IPI
GO:0043627	response to estrogen stimulus	biological process	IDA[11581164]
GO:0006355	regulation of transcription, DNA-dependent	biological process	IDA[15261140]
GO:0005515	protein binding	molecular function	IPI
GO:0016407	acetyltransferase activity	molecular function	IMP[12435739]
GO:0005634	nucleus	cellular component	IDA
GO:0008270	zinc ion binding	molecular function	IEA
GO:0005654	nucleoplasm	cellular component	TAS
GO:0004402	histone acetyltransferase activity	molecular function	IDA[12040021]
GO:0060765	regulation of androgen receptor signaling pathway	biological process	IDA[18487222]
GO:0043967	histone H4 acetylation	biological process	IMP[16325578]
GO:0019048	virus-host interaction	biological process	IEA

EP300 related KEGG pathways (count: 12)

ID	Name	Brief Description	Full Description
Gene mapped KEGG pathways
hsa05215	prostate cancer	Prostate cancer	The identification of key molecular alterations in prostate-...... The identification of key molecular alterations in prostate-cancer cells implicates carcinogen defenses (GSTP1), growth-factor-signaling pathways (NKX3.1, PTEN, and p27), and androgens (AR) as critical determinants of the phenotype of prostate-cancer cells. Glutathione S-transferases (GSTP1) are detoxifying enzymes that catalyze conjunction of glutathione with harmful, electrophilic molecules, thereby protecting cells from carcinogenic factors. Cells of prostatic intraepithelial neoplasia, devoid of GSTP1, undergo genomic damage mediated by such carcinogens. NKX3.1, PTEN, and p27 regulate the growth and survival of prostate cells in the normal prostate. Inadequate levels of PTEN and NKX3.1 lead to a reduction in p27 levels and to increased proliferation and decreased apoptosis. After therapeutic reduction in the levels of testosterone and dihydrotestosterone, the emergence of androgen-independent prostate cancer has been associated with mutations in the androgen receptor (AR) that permit receptor activation by other ligands, increased expression of androgen receptors accompanying AR amplification, and ligand-independent androgen-receptor activation. More...
hsa04110	cell cycle	Cell cycle	Mitotic cell cycle progression is accomplished through a rep...... Mitotic cell cycle progression is accomplished through a reproducible sequence of events, DNA replication (S phase) and mitosis (M phase) separated temporally by gaps known as G1 and G2 phases. Cyclin-dependent kinases (CDKs) are key regulatory enzymes, each consisting of a catalytic CDK subunit and an activating cyclin subunit. CDKs regulate the cell's progression through the phases of the cell cycle by modulating the activity of key substrates. Downstream targets of CDKs include transcription factor E2F and its regulator Rb. Precise activation and inactivation of CDKs at specific points in the cell cycle are required for orderly cell division. Cyclin-CDK inhibitors (CKIs), such as p16Ink4a, p15Ink4b, p27Kip1, and p21Cip1, are involved in the negative regulation of CDK activities, thus providing a pathway through which the cell cycle is negatively regulated. Eukaryotic cells respond to DNA damage by activating signaling pathways that promote cell cycle arrest and DNA repair. In response to DNA damage, the checkpoint kinase ATM phosphorylates and activates Chk2, which in turn directly phosphorylates and activates p53 tumor suppressor protein. p53 and its transcriptional targets play an important role in both G1 and G2 checkpoints. ATR-Chk1-mediated protein degradation of Cdc25A protein phosphatase is also a mechanism conferring intra-S-phase checkpoint activation. More...
hsa04630	jak stat_signaling_pathway	Jak-STAT signaling pathway	The Janus kinase/signal transducers and activators of transc...... The Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway is one of a handful of pleiotropic cascades used to transduce a multitude of signals for development and homeostasis in animals, from humans to flies. In mammals, the JAK/STAT pathway is the principal signaling mechanism for a wide array of cytokines and growth factors. Following the binding of cytokines to their cognate receptor, STATs are activated by members of the JAK family of tyrosine kinases. Once activated, they dimerize and translocate to the nucleus and modulate the expression of target genes. In addition to the activation of STATs, JAKs mediate the recruitment of other molecules such as the MAP kinases, PI3 kinase etc. These molecules process downstream signals via the Ras-Raf-MAP kinase and PI3 kinase pathways which results in the activation of additional transcription factors. More...
hsa05211	renal cell_carcinoma	Renal cell carcinoma	Renal cell carcinoma (RCC) is a heterogenous term comprising...... Renal cell carcinoma (RCC) is a heterogenous term comprising a group of neoplasms of renal origin. There are 4 major histologic subtypes of RCC: conventional (clear cell RCC, 75%), papillary (15%), chromophobic (5%), and collecting duct (2%). Multiple genes are involved in the molecular pathogenesis of RCC. VHL is a tumor suppressor gene responsible for hereditary (von Hippel-Lindau) and sporadic variants of conventional (clear cell) RCC. In the absence of VHL, hypoxia-inducible factor alpha (HIF-alpha) accumulates, leading to production of several growth factors, including vascular endothelial growth factor and platelet-derived growth factor. An oncogene, MET has been found to be mutant in cases of hereditary papillary renal cancer (HPRC), although the incidence of c-MET mutations is low in sporadic papillary RCC. Once activated, MET mediates a number of biological effects including motility, invasion of extracellular matrix, cellular transformation, prevention of apoptosis and metastasis formation. Mutations in the fumarate hydratase (FH) gene cause hereditary leiomyomatosis and renal cancer syndrome (HLRCC) papillary renal tumors, although the incidence of FH mutations in sporadic tumors is unknown. Loss of functional FH leads to accumulation of fumarate in the cell, triggering inhibition of HPH and preventing targeted pVHL-mediated degradation of HIF-alpha. BHD mutations cause the Birt-Hogg-Dube syndrome and its associated chromophobe, hybrid oncocytic, and conventional (clear cell) RCC. The incidence of BHD mutations in sporadic renal tumors is not known. More...
hsa04330	notch signaling_pathway	Notch signaling pathway	The Notch signaling pathway is an evolutionarily conserved, ...... The Notch signaling pathway is an evolutionarily conserved, intercellular signaling mechanism essential for proper embryonic development in all metazoan organisms in the Animal kingdom. The Notch proteins (Notch1-Notch4 in vertebrates) are single-pass receptors that are activated by the Delta (or Delta-like) and Jagged/Serrate families of membrane-bound ligands. They are transported to the plasma membrane as cleaved, but otherwise intact polypeptides. Interaction with ligand leads to two additional proteolytic cleavages that liberate the Notch intracellular domain (NICD) from the plasma membrane. The NICD translocates to the nucleus, where it forms a complex with the DNA binding protein CSL, displacing a histone deacetylase (HDAc)-co-repressor (CoR) complex from CSL. Components of an activation complex, such as MAML1 and histone acetyltransferases (HATs), are recruited to the NICD-CSL complex, leading to the transcriptional activation of Notch target genes. More...
hsa04720	long term_potentiation	Long-term potentiation	Hippocampal long-term potentiation (LTP), a long-lasting inc...... Hippocampal long-term potentiation (LTP), a long-lasting increase in synaptic efficacy, is the molecular basis for learning and memory. Tetanic stimulation of afferents in the CA1 region of the hippocampus induces glutamate release and activation of glutamate receptors in dendritic spines. A large increase in i resulting from influx through NMDA receptors leads to constitutive activation of CaM kinase II (CaM KII). Constitutively active CaM kinase II phosphorylates AMPA receptors, resulting in potentiation of the ionic conductance of AMPA receptors. Early-phase LTP (E-LTP) expression is due, in part, to this phosphorylation of the AMPA receptor. It is hypothesized that postsynaptic Ca2+ increases generated through NMDA receptors activate several signal transduction pathways including the Erk/MAP kinase and cAMP regulatory pathways. The convergence of these pathways at the level of the CREB/CRE transcriptional pathway may increase expression of a family of genes required for late-phase LTP (L-LTP). More...
hsa04310	wnt signaling_pathway	Wnt signaling pathway	Wnt proteins are secreted morphogens that are required for b...... Wnt proteins are secreted morphogens that are required for basic developmental processes, such as cell-fate specification, progenitor-cell proliferation and the control of asymmetric cell division, in many different species and organs. There are at least three different Wnt pathways: the canonical pathway, the planar cell polarity (PCP) pathway and the Wnt/Ca2+ pathway. In the canonical Wnt pathway, the major effect of Wnt ligand binding to its receptor is the stabilization of cytoplasmic beta-catenin through inhibition of the bea-catenin degradation complex. Beta-catenin is then free to enter the nucleus and activate Wnt-regulated genes through its interaction with TCF (T-cell factor) family transcription factors and concomitant recruitment of coactivators. Planar cell polarity (PCP) signaling leads to the activation of the small GTPases RHOA (RAS homologue gene-family member A) and RAC1, which activate the stress kinase JNK (Jun N-terminal kinase) and ROCK (RHO-associated coiled-coil-containing protein kinase 1) and leads to remodelling of the cytoskeleton and changes in cell adhesion and motility. WNT-Ca2+ signalling is mediated through G proteins and phospholipases and leads to transient increases in cytoplasmic free calcium that subsequently activate the kinase PKC (protein kinase C) and CAMKII (calcium calmodulin mediated kinase II) and the phosphatase calcineurin. More...
hsa05200	pathways in_cancer	Pathways in cancer
hsa04520	adherens junction	Adherens junction	Cell-cell adherens junctions (AJs), the most common type of ...... Cell-cell adherens junctions (AJs), the most common type of intercellular adhesions, are important for maintaining tissue architecture and cell polarity and can limit cell movement and proliferation. At AJs, E-cadherin serves as an essential cell adhesion molecules (CAMs). The cytoplasmic tail binds beta-catenin, which in turn binds alpha-catenin. Alpha-catenin is associated with F-actin bundles directly and indirectly. The integrity of the cadherin-catenin complex is negatively regulated by phosphorylation of beta-catenin by receptor tyrosine kinases (RTKs) and cytoplasmic tyrosine kinases (Fer, Fyn, Yes, and Src), which leads to dissociation of the cadherin-catenin complex. Integrity of this complex is positively regulated by beta -catenin phosphorylation by casein kinase II, and dephosphorylation by protein tyrosine phosphatases. Changes in the phosphorylation state of beta-catenin affect cell-cell adhesion, cell migration and the level of signaling beta-catenin. Wnt signaling acts as a positive regulator of beta-catenin by inhibiting beta-catenin degradation, which stabilizes beta-catenin, and causes its accumulation. Cadherin may acts as a negative regulator of signaling beta-catenin as it binds beta-catenin at the cell surface and thereby sequesters it from the nucleus. Nectins also function as CAMs at AJs, but are more highly concentrated at AJs than E-cadherin. Nectins transduce signals through Cdc42 and Rac, which reorganize the actin cytoskeleton, regulate the formation of AJs, and strengthen cell-cell adhesion. More...
hsa04350	tgf beta_signaling_pathway	TGF-beta signaling pathway	The transforming growth factor-beta (TGF-beta) family member...... The transforming growth factor-beta (TGF-beta) family members, which include TGF-betas, activins and bone morphogenetic proteins (BMPs), are structurally related secreted cytokines found in species ranging from worms and insects to mammals. A wide spectrum of cellular functions such as proliferation, apoptosis, differentiation and migration are regulated by TGF-beta family members. TGF-beta family member binds to the Type II receptor and recruits Type I, whereby Type II receptor phosphorylates and activates Type I. The Type I receptor, in turn, phosphorylates receptor-activated Smads ( R-Smads: Smad1, Smad2, Smad3, Smad5, and Smad8). Once phosphorylated, R-Smads associate with the co-mediator Smad, Smad4, and the heteromeric complex then translocates into the nucleus. In the nucleus, Smad complexes activate specific genes through cooperative interactions with other DNA-binding and coactivator (or co-repressor) proteins. More...
hsa04916	melanogenesis	Melanogenesis	Cutaneous melanin pigment plays a critical role in camouflag...... Cutaneous melanin pigment plays a critical role in camouflage, mimicry, social communication, and protection against harmful effects of solar radiation. Melanogenesis is under complex regulatory control by multiple agents. The most important positive regulator of melanogenesis is the MC1 receptor with its ligands melanocortic peptides. MC1R activates the cyclic AMP (cAMP) response-element binding protein (CREB). Increased expression of MITF and its activation by phosphorylation (P) stimulate the transcription of tyrosinase (TYR), tyrosinase-related protein 1 (TYRP1), and dopachrome tautomerase (DCT), which produce melanin. Melanin synthesis takes place within specialized intracellular organelles named melanosomes. Melanin-containing melanosomes then move from the perinuclear region to the dendrite tips and are transferred to keratinocytes by a still not well-characterized mechanism. More...
hsa05016	huntingtons disease	Huntington's disease	Huntington disease (HD) is an autosomal-dominant neurodegene...... Huntington disease (HD) is an autosomal-dominant neurodegenerative disorder that primarily affects medium spiny striatal neurons (MSN). HD is caused by a CAG repeat expansion in the IT15 gene, which results in a long stretch of polyglutamine close to the amino-terminus of the HD protein huntingtin (Htt). Mutant Htt (mHtt) has effects both in the cytoplasm and in the nucleus. In the cytoplasm, full-length mHtt can interfere with BDNF vesicular transport on microtubules. This mutant protein also may lead to abnormal endocytosis and secretion in neurons, because normal Htt form a complex with the proteins Hip1, clathrin and AP2 that are involved in endocytosis. In addition, mHtt affects Ca2+ signaling by sensitizing InsP3R1 to activation by InsP3, stimulating NR2B/NR1 NMDAR activity, and destabilizing mitochondrial Ca2+ handling. As a result, stimulation of glutamate receptors leads to supranormal Ca2+ responses in HD MSN and mitochondrial Ca2+ overload. The mHtt translocates to the nucleus, where it forms intranuclear inclusions, though they are not primarily responsible for toxicity. Nuclear toxicity is believed to be caused by interference with gene transcription, leading to loss of transcription of neuroprotective molecules such as BDNF. While mHtt binds to p53 and upregulates levels of nuclear p53 as well as p53 transcriptional activity. Augmented p53 mediates mitochondrial dysfunction. More...

EP300 related BioCarta pathways (count: 14)

ID	Name	Brief Description	Full Description
Literature-origin BioCarta pathway
NTHI_PATHWAY	nthi pathway	NFkB activation by Nontypeable Hemophilus influenzae	The role of Hemophilus influenzae in ear infections and chro...... The role of Hemophilus influenzae in ear infections and chronic obstructive pulmonary disease includes the induction of an inflammatory response through activation of the transcription factor NF-kB. In addition to activation of inflammatory cytokine genes like IL-1 and TNF, H. influenzae activates TLR2 expression and genes involved in mucus production. Hemophilus influenzae activates NF-kB by multiple mechanisms, starting with activation of the Toll-like receptor 2 (TLR2) by the p16 protein in the H. influenzae outer membrane. TLR2 plays a key role in innate immune responses and is expressed in high levels in lymphoid cells as well as low levels in epithelial cells. The role of TLR2 was supported by blocking NF-kB activation with a dominant negative TLR2 and increasing it with transfection of a normal TLR2 gene. TLR2 in turn activates TAK1, which activates two divergent signaling pathways. One of these pathways leads to IkB kinase activation, IkB phosphorylation and degradation, releasing the NF-kB heterodimer to translocate into the nucleus and activate transcription of target genes. In the alternate pathway, TAK1 also activates NF-kB through a Map kinase pathway, activating p38 and NF-kB in a nuclear translocation independent manner. Investigation of the mechanisms of H. influenzae signaling involved in NF-kB activation may provide the information needed to develop better treatments for inflammatory conditions caused by this pathogen. Other pathways modulate the role of NF-kB in H. influenzae pathogenesis. Glucocorticoids widely used as anti-inflammatory drugs increase TLR2 activation by H. influenzae through the NIK/I-kB kinase pathway, while they repress the p38 dependent activation of NF-kB. The repression of the p38 pathway by glucocorticoids occurs through activation of the MAP kinase phosphatase-1 (MKP-1) which dephosphorylates and deactivates p38. Another aspect of the inflammatory response to H. influenzae infection is the production of excessive mucus, contributing to the overall symptoms of infection. NF-kB activation of the Muc2 gene contributes to mucus overproduction, in addition to H. influenzae activation of the TGF-beta receptor, activating SMAD transcription factors SMAD3 and SMAD4. Understanding mechanisms that modify H. influenzae signaling will contribute to further understanding the pathogenesis and treatment of ear infections and chronic obstructive pulmonary disease. More...

ID	Name	Brief Description	Full Description
Gene mapped BioCarta pathways
P53HYPOXIA_PATHWAY	p53hypoxia pathway	Hypoxia and p53 in the Cardiovascular system	Hypoxic stress, like DNA damage, induces p53 protein accumul...... Hypoxic stress, like DNA damage, induces p53 protein accumulation and p53-dependent apoptosis in oncogenically transformed cells. Unlike DNA damage, hypoxia does not induce p53-dependent cell cycle arrest, suggesting that p53 activity is differentially regulated by these two stresses. Hypoxia induces p53 protein accumulation, but in contrast to DNA damage, hypoxia fails to induce endogenous downstream p53 effector mRNAs and proteins, such as p21, Bax, CIP1, WAF1 etc. Hypoxia does not inhibit the induction of p53 target genes by ionizing radiation, indicating that p53-dependent transactivation requires a DNA damage-inducible signal that is lacking under hypoxic treatment alone. The phosphatidylinositol 3-OH-kinase-Akt pathway inhibits p53-mediated transcription and apoptosis. Mdm2, a ubiquitin ligase for p53, plays a central role in regulation of the stability of p53 and serves as a good substrate for Akt. Mdm-2 targets the p53 tumor suppressor for ubiquitin-dependent degradation by the proteasome, but, in addition, the p53 transcription factor induces Mdm-2, thus, establishing a feedback loop. Hypoxia or DNA damage by abrogating binding of HIF-1 with VHL and p53 with Mdm-2, respectively, leads to stabilization and accumulation transcriptionally active HIF-1 and p53. At the molecular level, DNA damage induces the interaction of p53 with the transcriptional activator p300 as well as with the transcriptional corepressor mSin3A. In contrast, hypoxia primarily induces an interaction of p53 with mSin3A, but not with p300. More...
HIF_PATHWAY	hif pathway	Hypoxia-Inducible Factor in the Cardiovascular System	Hypoxia (or low O2 levels) affects various pathologies. Firs...... Hypoxia (or low O2 levels) affects various pathologies. First, tissue ischemia, a variation in O2 tension caused by hypoxia/reoxygenation, can lead to endothelial cell changes. For example, long periods of ischemia result in endothelial changes, such as vascular leakage, resulting in varicose veins. In more severe situations, ischemia can lead to myocardial or cerebral infarction and retinal vessel occlusion. Of interest, HIF-1 is stabilized prior to induction of vascular endothelial growth factor (VEGF) expression during acute ischemia in the human heart. Second, pulmonary hypertension associated with chronic respiratory disorders results from persistent vasoconstriction and vascular remodeling. Third, hypoxic gradients created in enlarging solid tumors trigger expression of genes containing hypoxia response element (HRE)s such as those involved in angiogenesis. This allows subsequent delivery of O2, nutrients, and further tumor growth. Vascular remodeling is an important component to tumorigenesis; without proper blood supply, delivery of oxygen may occur by diffusion, but becomes inefficient in tumors greater than 1 mm in diameter. Short-term hypoxia can also elevate platelet numbers, while prolonged exposure may cause some degree of thrombocytopenia in response to increased levels of erythropoetin (EPO). Another disorder involving inadequate responses to hypoxia is preeclampsia, a pathology of pregnancy thought to be caused by improper differentiation of placental trophoblast cells due to poorly controlled O2 tension or improper hypoxia-inducible factor (HIF)-mediated responses. The primary molecular mechanism of gene activation during hypoxia is through HIF-1. Several genes involved in cellular differentiation are directly or indirectly regulated by hypoxia. These include EPO, LDH-A, ET-1, transferrin, transferrin receptor, VEGF, Flk-1, Flt-1, platelet-derived growth factor- (PDGF-), basic fibroblast growth factor (bFGF), and others genes affecting glycolysis. HIF-1 is a member of the basic helix-loop-helix (bHLH)-PAS family of transcription factors known to induce gene expression by binding to a ~50-bp HRE containing a core 5'-ACGTG-3' sequence. bHLH-PAS proteins heterodimerize to form transcription complexes that regulate O2 homeostasis, circadian rhythms, neurogenesis, and toxin metabolism. Three bHLH-PAS proteins in vertebrates respond to hypoxia: HIF-1 , EPAS (HIF-2 ), and HIF-3. These dimerize with ARNT (aryl hydrocarbon receptor nuclear translocator protein), ARNT-2, or ARNT-3. HIF-1 is ubiquitinated and subsequently degraded in less than 5 minutes under normoxic conditions. Although several candidate O2-sensing molecules have emerged in the literature, the molecular basis of how cells sense O2 levels is poorly characterized. pVHL, the protein product of a tumor-suppressor gene responsible for von Hippel Lindau disease, is implicated in this O2-sensing system by its association with HIF-1 , targeting it for ubiquitin-mediated degradation. Similarly, F-box-containing proteins recognize substrates of the ubiquitin ligases, targeting them for phosphorylation-dependent ubiquitination and proteosomal degradation. In addition to F-boxes, most of these proteins also contain a WD40 or a leucine-rich repeat (LLR) domain that presumably functions as a Ser/Thr binding module. A second family of proteins assisting the ubiquitin ligases share a region designated SOCS-box (originally from the suppressor of cytokine signaling proteins SOCS). Under low O2 (<5% O2) HIF-1 is stabilized leading to the formation of a functional transcription factor complex with ARNT. This complex is the master regulator of O2 homeostasis and induces a network of genes involved in angiogenesis, erythropoiesis, and glucose metabolism. More...
IL7_PATHWAY	il7 pathway	IL-7 Signal Transduction	IL-7 is a key cytokine in the immune system, essential for n...... IL-7 is a key cytokine in the immune system, essential for normal development of B cells and T cells. Mice with the IL-7 receptor deleted lack B and T cells. Some humans with SCID (severe combined immunodeficiency disease) also have mutation of their IL-7 receptor gene leading to an absence of T cells and greatly impaired B cell production. The IL-7 receptor includes two polypeptides, a gamma chain and an alpha chain. The alpha-chain is unique to the IL-7 receptor while several other cytokines use the same gamma receptor chain as IL-7, including IL-2, IL-4, IL-9, IL-15 and IL-21. Binding of IL-7 to the alpha chain leads to dimerization of the alpha and gamma chains. JAK3 associated with the gamma chain tyrosine phosphorylates the alpha chain after dimerization. The importance of JAK3 in IL-7 signaling is supported by the similarity of the immune defects in JAK3 knockout mice and IL-7 knockout mice. The phosphorylated alpha chain serves as the site for recruiting other signaling molecules to the complex to be phosphorylated and activated, including STAT5, src kinases, PI3 kinase, Pyk2 and Bcl2 proteins. Some targets of IL-7 signaling contribute to cellular survival, including Bcl2 and Pyk2. Other targets contribute to cellular proliferation, including PI3 kinase, src family kinases (lck and fyn) and STAT5. The transcription factor STAT5 contributes to activation of multiple different downstream genes in B and T cells and may contribute to VDJ recombination through alteration of chromatin structure. The cell survival and cell proliferation signals induced by IL-7 combine to induce normal B and T cell development. More...
PITX2_PATHWAY	pitx2 pathway	Multi-step Regulation of Transcription by Pitx2	Many transcription factors play essential roles in normal de...... Many transcription factors play essential roles in normal development by determining the proliferation and differentiation of cells. The coordinated transcriptional control of proliferation in specific developmental cell types is crucial in multiple developmental settings. One of a family of three bicoid-related transcription factors, Pitx2 acts downstream of the extracellular signaling protein Wnt to drive proliferation of cells with specific developmental fates, including cells in the pituitary, cardiac outflow region, and muscle. Wnt binds to Frizzled, a G-protein coupled receptor, activating homologs of the Drosophila Disheveled protein. Activation of Frizzled and Disheveled inhibits the kinase GSK-3 beta, part of a protein complex in the absence of Wnt signaling, causing beta-catenin protein to accumulate in the cytoplasm. Beta-catenin is known to alter the function of transcription factors like TCF/Lef. One result of Wnt signaling is activation of the transcription factor Lef by beta-catenin, inducing Pitx2 expression. Wnt activation also changes Pitx2 from a repressor to an activator by causing transcriptional corepressors like histone deacetylase 1 (HDAC1) bound to Pitx2 to be exchanged for coactivators. With coactivators bound, Pitx2 activates transcription of genes that regulate the cell cycle like Cyclin D2. Different coactivators are recruited by Pitx2 and other transcription factors like Myc to the Cyclin D2 promoter, with CBP/p300 recruited first, followed by NLI/Ldb/CLIM, Tip60/TRRAP, and PBP coactivators. Many of these coactivators help to alter histone acetylation and chromatin structure as part of transcriptional activation. The activation of cell cycle genes by Pitx2 ultimately stimulates the proliferation of specific cell types with the confluence of tissue-specific gene expression, growth factor signaling and coactivator recruitment. More...
G2_PATHWAY	g2 pathway	Cell Cycle: G2/M Checkpoint	The G2/M DNA damage checkpoint prevents the cell from enteri...... The G2/M DNA damage checkpoint prevents the cell from entering mitosis (M phase) if the genome is damaged. The Cdc2-cyclin B kinase is pivotal in regulating this transition. During G2 phase, Cdc2 is maintained in an inactive state by the kinases Wee1 and Mt1. As cells approach M phase, the phosphatase Cdc25 is activated, perhaps by the polo-kinase Pik1. Cdc25 then activates Cdc2, establishing a feedback amplification loop that efficiently drives the cell into mitosis. DNA damage activates the DNA-PK/ATM/ATR kinases, initiating two parallel cascades that inactivate Cdc2-cyclin B. The first cascade rapidly inhibits progression into mitosis: the CHK kinases phosphorylate and inactivate Cdc25, which can no longer activate Cdc2. The second cascade is slower. Phosphorylation of p53 dissociates it from MDM2, activating its DNA binding activity. Acetylation by p300/PCAF further activates its transcriptional activity. The genes that are turned on by p53 constitute effectors of this second cascade. They include 14-3-3s, which binds to the phosphorylated Cdc2-cyclin B kinase and exports it from the nucleus; GADD45, which apparently binds to and dissociates the Cdc2-cyclin B kinase; and p21Cip1, an inhibitor of a subset of the cyclin-dependent kinases including Cdc2 (CDK1). More...
HER2_PATHWAY	her2 pathway	Role of ERBB2 in Signal Transduction and Oncology	Her2 or ERBB2 belongs to a class of proteins having high hom...... Her2 or ERBB2 belongs to a class of proteins having high homology with epidermal growth factor receptor (EGFR or ERBB1). It encodes a protein with the molecular weight of 185 KDa. Unlike other members of EGFR family, no ligand for Her2 has been found and it usually associates with members of ERBB1 family to form functional heterodimers. It has been shown that it can form dimers with ERBB (EGFR), ERBB3 and ERBB4 as well as gp130 subunits of IL-6 receptor. In at least some cell types, the association between gp130 and HRBB2 is essential for HRBB2-ERBB3 phosphorylation and subsequent MAP kinase signaling. Although ERBB1 can form homodimers, the signaling for ERBB1 is usually transient and the receptor undergoes internalization after ligand binding and activation. EGFR-HER2 complex increases the signaling capacity of EGFR by increasing the ligand affinity as well as the recycling of the heterodimer. Of all the ERBB heterodimers, ERBB2-ERBB3 heterodimers perhaps elicit the strongest signal. Removing ERBB3 from the cell has a drastic effect on ERBB2 mediated signaling and downstream effectors. The clinical importance of HER2 cannot be overstated. In addition, monoclonal antibody (Herceptin) against this receptor has been shown to be an effective treatment of breast cancer patients who have a high level of HER2 over expression. More...
TGFB_PATHWAY	tgfb pathway	TGF beta signaling pathway	TGF-beta regulates growth and proliferation of cells, blocki...... TGF-beta regulates growth and proliferation of cells, blocking growth of many cell types. The TGF-beta receptor includes type 1 and type 2 subunits that are serine-threonine kinases and that signal through the SMAD family of transcriptional regulators. Defects in TGF-beta signaling, includes mutation in SMADs, have been associated with cancer in humans. Prior to activation, receptor regulated SMADs are anchored to the cell membrane by factors like SARA (SMAD Anchor for Receptor Activation) that brings the SMADs into proximity of the TGF receptor kinases. Binding of TGF induces phosphorylation and activation of the TGF-beta R1 receptor by the TGF-beta R2 receptor. The activated TGF-beta R1 phosphorylates SMAD2 and SMAD3, which bind to the SMAD4 mediator to move into the nucleus and form complexes that regulate transcription. SMADs regulate transcription in several ways, including binding to DNA, interacting with other transcription factors, and interacting with transcription corepressors and coactivators like p300 and CBP. SMAD-7 represses signaling by other SMADs to down-regulate the system. Other signaling pathways like the MAP kinase-ERK cascade are activated by TGF-beta signaling, modulate SMAD activation. SnoN also regulates TGF-beta signaling, by binding to SMADs to block transcriptional activation. TGF-beta signaling causes degradation of SnoN, releasing SMADs to regulate transcription, and also activates expression of SnoN, to down-regulate SMAD signaling at later times. More...
VDR_PATHWAY	vdr pathway	Control of Gene Expression by Vitamin D Receptor	The vitamin D receptor, VDR is the mediator of all genomic a...... The vitamin D receptor, VDR is the mediator of all genomic actions of vitamin D3 and its analogs. It belongs to a family of ligand induced transcription factors, nuclear receptors (NRs). Vitamin D3 is the main regulator of calcium homeostasis and is critical in bone formation. It is also involved in controlling cellular growth, differentiation and apoptosis, which makes synthetic vitamin D3 analogues interesting for therapy of such diseases as cancer and psoriasis. NRs are comprised of: an amino-terminal activation function domain AF-1; the DNA-binding domain; a hinge region; and a carboxy-terminal ligand-binding domain containing a second activation function, AF-2. VDR acts primarily as a heterodimer with the retinoid X receptor (RXR) on vitamin D response elements (VDREs). It interacts with the transcription machinery and nuclear receptor coactivators or corepressors to regulate target gene activity. NRs coregulators can be divided into 3 major classes: 1)ATP-dependent chromatin remodeling complexes that are involved in the location and association of nucleosomes with DNA; 2) Enzymes that catalyze modifications of histone tails to regulate histone-histone and histone-DNA interactions 3) General transcription factors adaptors that bridge the functions between regulators and basal transcription factors. A novel multifunctional ATP-dependent chromatin remodeling complex c WINAC directly interacts with the vitamin D receptor. It contains BRG1 or hBRM as ATPase subunits as all SWI/SNF complexes do, but it also has subunits associated with DNA replication (TopoII_ and CAF-1p150) and transcript elongation through nucleosomes (FACTP140) not found before in SWI/SNF complexes. WINAC also contains the Williams syndrome transcription factor (WSTF). WSTF appears to function as a platform protein for the assembly of components in WINAC, and it interacts directly with the vitamin D receptor in a ligand-independent manner. WINAC and vitamin Dreceptor are targeted to vitamin D responsive promoters in the absence of ligand to both positively and negatively regulated genes. WINAC may rearrange the nucleosome array around the positive and negative VDREs, thereby facilitating the coregulatory complexes access for further transcription control. Upon ligand binding, two HAT complexes, p160/CBP and TRRAP/PCAF, coactivate the NR function. The p160 proteins (SRC protein family) interact directly with an NR activation surface AF2 and serve as platforms for the recruitment of histone-modifying enzymes, including CBP/p300 and methyltransferases. The SRC/p160 family members SRC-1 and p/CIP, as well as CBP and p300 contain intrinsic histone acetyltransferase activity(HAT). Both the HAT activity and the histone methyltransferase activity may cooperate in histone modification and facilitate nucleosome remodeling and recruitment of transcriptional machinery. A third group of coactivators is represented by thyroid receptor-associated proteins (TRAP)/vitamin D receptor-interacting proteins (DRIP). This complex may play a role by directly contacting the basal transcriptional machinery. As the VDR/RXR heterodimer also represses transcription in a ligand-dependent manner through negative VDRE (nVDRE), a number of corepressor proteins such as NCoR and ALIEN may also be recruited to the surface of the receptor. They, too function as platforms but serve to recruit enzymes such as histone deacetylases. WINAC association with VDR facilitates targeting of a putative corepressor complex to the nVDRE More...
PPARA_PATHWAY	ppara pathway	Mechanism of Gene Regulation by Peroxisome Proliferators via PPARa(alpha)	The most recognized mechanism by which peroxisome proliferat...... The most recognized mechanism by which peroxisome proliferators regulated gene expresssion is through a PPAR/RXR heterodimeric complex binding to a peroxisome proliferator-response element (PPRE) (classical mechanism). However, there are the possibility of several variations on this theme: 1). The peroxisome proliferator interacts with PPAR that preexists as a DNA complex with associated corepressors proteins. The interaction with ligand causes release of the corepressor and association with a coactivator, resulting in the classical mechanism. 2). The peroxisome proliferator interacts with PPAR as a soluble member of the nucleus. The binding of ligand results in RXR heterodimerization, DNA binding and coactivator recruitment. 3). In this scenario, PPAR exists in the cytosol, perhaps complexed to heat shock protein 90 and/or other chaperones. Binding of peroxisome proliferator causes a conformational change and translocation into the nucleus. Scenarios 4 and 5 require regulation of gene expression via non-classical mechanisms: 4). PPAR is capable of interacting with, and forming DNA binding heterodimers with, several nuclear receptors including the thyroid hormone receptor. The binding site for this non-RXR heterodimer need not be the classic DR-1 motif found in the PPRE. 5). PPAR may participate in the regulation of gene expression witout binding to DNA. By association with transcription factors such as c-jun or p65, PPAR diminishes the ability of AP1 or NFB to bind to their cognate DNA sequences, respectively. Also shown in this scheme are two means to modify the peroxisome proliferator response. Most importantly, growth factor signaling has a pronounced affect on PPAR via post-translational modification. PPAR is a phosphoprotein and its activity is affected by insulin. Several kinase pathways affects PPARa's activity, although the specific kinases and phosphorylation sites have not been conclusively determined. More...
RELA_PATHWAY	rela pathway	Acetylation and Deacetylation of RelA in The Nucleus
MEF2D_PATHWAY	mef2d pathway	Role of MEF2D in T-cell Apoptosis	Mef2 pathway. Mef2 pathway.
CARM1_PATHWAY	carm1 pathway	Transcription Regulation by Methyltransferase of CARM1	Several forms of post-translational modification regulate pr...... Several forms of post-translational modification regulate protein activities. Recently, protein methylation by CARM1 (coactivator-associated arginine methyltransferase 1) has been observed to play a key role in transcriptional regulation. CARM1 associates with the p160 class of transcriptional coactivators involved in gene activation by steroid hormone family receptors. CARM1 also interacts with CBP/p300 transcriptional coactivators involved in gene activation by a large variety of transcription factors, including steroid hormone receptors and CEBP. One target of CARM1 is the core histones H3 and H4, which are also targets of the histone acetylase activity of CBP/p300 coactivators. Recruitment of CARM1 to the promoter region by binding to coactivators increases histone methylation and makes promoter regions more accessible for transcription. Another target of CARM1 methylation is a coactivator it interacts with, CBP. Methylation of CBP by CARM1 blocks CBP from acting as a coactivator for CREB and redirects the limited CBP pool in the cell to be available for steroid hormone receptors. Other forms of post-translational protein modification such as phosphorylation are reversible in nature, but as of yet a protein demethylase is not known. More...
CARM_ER_PATHWAY	carm er_pathway	CARM1 and Regulation of the Estrogen Receptor	Several forms of post-translational modification regulate pr...... Several forms of post-translational modification regulate protein activities. Recently, protein methylation by CARM1 (coactivator-associated arginine methyltransferase 1) has been observed to play a key role in transcriptional regulation. CARM1 associates with the p160 class of transcriptional coactivators involved in gene activation by steroid hormone family receptors. CARM1 also interacts with CBP/p300 transcriptional coactivators involved in gene activation by a large variety of transcription factors, including steroid hormone receptors and CEBP. One target of CARM1 is the core histones H3 and H4, which are also targets of the histone acetylase activity of CBP/p300 coactivators. Recruitment of CARM1 to the promoter region by binding to coactivators increases histone methylation and makes promoter regions more accessible for transcription. Another target of CARM1 methylation is a coactivator it interacts with, CBP. Methylation of CBP by CARM1 blocks CBP from acting as a coactivator for CREB and redirects the limited CBP pool in the cell to be available for steroid hormone receptors. Other forms of post-translational protein modification such as phosphorylation are reversible in nature, but as of yet a protein demethylase is not known. The methylation activity of CARM1 modulates the activity of specific transcriptional regulators. CARM1 acts as a coactivator for the myogenic transcription factor Mef2c, and is necessary for normal muscle cell differentiation. The estrogen receptor is another transcription factor that uses CARM1 as one of several coactivators, acting synergistically with CBP through the Grip1 member of the p160 family of coactivators. The interaction of estrogen receptor with various ligand-dependent coactivators may produce the tissue selective response of some estrogen receptor ligands like tamoxifen. More...

EP300 related Reactome pathways (count: 0)

EP300 related interactors from protein-protein interaction data in HPRD (count: 210)

Gene	Interactor	Interactor in MK4MDD?	Experiment Type	PMID
EP300	KAT5	Yes	in vivo	16001085
EP300	CEBPB	No	in vitro;in vivo	9343424
EP300	KLF5	No	in vitro;in vivo	14612398
EP300	ETV1	No	in vitro;in vivo	12917345
EP300	NCOA1	No	in vitro;yeast 2-hybrid	11113179
EP300	KAT2B	No	in vitro;in vivo	9267036 , 8684459
EP300	PCNA	No	in vitro;in vivo	11268218
EP300	SNIP1	No	in vitro;in vivo	10887155
EP300	CALCOCO1	No	in vitro	16931570
EP300	NUP98	No	in vitro;in vivo	9858599
EP300	SIRT1	Yes	in vitro;in vivo	15632193
EP300	NEUROD1	No	in vitro	10545951
EP300	NCOA6	No	in vitro	10823961
EP300	TP73	No	in vivo	10648616 , 11804596
EP300	ING4	No	in vivo	12750254
EP300	FEN1	No	in vitro;in vivo	11430825
EP300	HAND2	No	in vitro;in vivo	11994297
EP300	E2F5	No	in vitro;in vivo;yeast 2-hybrid	7760804 , 12789259
EP300	CDK2	No	in vivo	10330164
EP300	JMY	No	in vitro;in vivo;yeast 2-hybrid	10518217
EP300	SUB1	No	in vitro	11279157
EP300	TGFB1I1	No	in vitro	14755691
EP300	AHR	No	in vivo	10999956
EP300	PAX6	No	in vitro;in vivo	10506141
EP300	MYB	No	in vitro;in vivo	10656693
EP300	USF2	No	in vivo	10434034
EP300	MRE11A	No	in vitro;in vivo	16051665
EP300	RORA	No	in vitro;in vivo	9862959
EP300	MSH6	No	in vitro;in vivo	16051665
EP300	MITF	No	in vitro;in vivo	9660747
EP300	NPAS2	Yes	in vitro;in vivo	14645221
EP300	TFAP2A	No	in vivo;yeast 2-hybrid	12586840
EP300	BAT3	No	in vivo	17403783
EP300	HOXA10	No	in vitro;in vivo	11585930
EP300	TACC2	No	in vivo	14767476
EP300	PPARD	No	in vitro	10567538
EP300	CTBP1	No	in vitro;in vivo	15834423
EP300	SMAD1	No	in vitro;in vivo	10673036
EP300	SNW1	No	in vitro	14985122
EP300	MEF2D	No	in vitro;in vivo	11096067
EP300	PPARA	No	in vitro;yeast 2-hybrid	9407140
EP300	ZNF76	No	in vitro;in vivo	16337145
EP300	CEBPA	No	in vitro	11340085
EP300	ZFPM2	No	in vitro;in vivo	15220332
EP300	NFATC1	No	in vitro;in vivo	15117818
EP300	BRCA1	No	in vitro;in vivo	10655477
EP300	HOXB3	No	in vitro;in vivo	11585930
EP300	CHD4	No	in vitro	15189737
EP300	STAT5B	No	in vitro;in vivo	9989503 , 14726487
EP300	MDM2	No	in vitro	9809062
EP300	ING2	No	in vitro;in vivo	16024799 , 16782091
EP300	CDX2	No	in vitro;in vivo	10506141
EP300	NBN	No	in vitro;in vivo	16051665
EP300	RUNX3	No	in vivo	15138260
EP300	HOXD4	No	in vitro;in vivo	11585930
EP300	HDAC6	No	in vitro	15102857
EP300	HOXB1	No	in vitro;in vivo	11585930
EP300	ACTA2	No	in vivo	16051665
EP300	UBE2I	No	in vitro	8824223
EP300	PROX1	No	in vivo;yeast 2-hybrid	11943779
EP300	RPS6KA5	No	in vitro	12569367
EP300	HOXB2	No	in vitro;in vivo	11585930
EP300	GATA5	No	in vitro;in vivo	10567378
EP300	CEBPD	No	in vitro;in vivo	16397300
EP300	TGS1	No	in vitro;in vivo	11912212
EP300	CITED1	No	in vitro;in vivo	10722728
EP300	RELA	No	in vitro;in vivo;yeast 2-hybrid	9096323 , 12419806 , 12456660 , 15171256
EP300	HOXB4	No	in vitro;in vivo	11585930
EP300	PTMA	No	in vitro;in vivo	11967287
EP300	MYOD1	No	in vitro;in vivo	9001254 , 10944526
EP300	CITED4	No	in vitro;in vivo	11744733
EP300	HOXB9	No	in vitro;in vivo	11585930
EP300	NEIL2	No	in vitro;in vivo	15175427
EP300	CTBP2	No	in vivo	16356938
EP300	CITED2	No	in vitro;in vivo;yeast 2-hybrid	9887100 , 12586840 , 12778114
EP300	APEX1	No	in vitro;in vivo	14633989
EP300	HOXB6	No	in vitro;in vivo	11585930
EP300	STAT1	No	in vivo	15824515 , 8986769 , 9843502
EP300	NR2F2	No	in vitro;in vivo	9826778
EP300	SMAD3	No	in vivo;yeast 2-hybrid	10497242
EP300	SS18	No	in vivo	11030627
EP300	KPNA2	No	in vivo	10801418
EP300	STAT6	No	in vitro	10454341
EP300	BCL6	Yes	in vitro;in vivo	12402037
EP300	STAT5A	No	in vitro;in vivo	9989503 , 14726487
EP300	SUV39H1	No	in vitro	11252719
EP300	CCND1	Yes	in vitro	11788592
EP300	EP300	Yes	in vitro	15004546 , 10779504 , 12384515 , 9812974
EP300	ZRANB2	No	in vivo	11448987
EP300	RAN	No	in vitro;in vivo;yeast 2-hybrid	12649209
EP300	RB1	No	in vitro;in vivo	11433299
EP300	SREBF2	No	in vitro;in vivo	8918891
EP300	IRF3	No	in vitro	9488451
EP300	ASCL1	No	in vivo	11564735
EP300	DDX24	No	in vivo	16051665
EP300	SATB1	No	in vitro;in vivo	14605447
EP300	MAP2K1	No	in vitro;in vivo	11278389
EP300	STAT3	No	in vitro;in vivo	10205054 , 15649887
EP300	TCF4	No	in vitro	17410209
EP300	HERC1	No	in vivo	16051665
EP300	TSG101	No	in vitro;in vivo	10440698
EP300	MN1	Yes	in vitro	12569362
EP300	ING5	No	in vivo	12750254
EP300	EMB	No	in vitro	15024082
EP300	TWIST1	No	in vitro;in vivo	10025406
EP300	TP53BP1	No	in vivo	16051665
EP300	PAX8	No	in vitro	10924503
EP300	NEDD1	No	in vivo	16051665
EP300	HIF1A	No	in vitro;in vivo	11823643 , 11959990 , 17382325 , 12778114 , 18519678
EP300	ELK1	No	in vitro;in vivo	12514134
EP300	HMGN2	No	in vitro;in vivo	10207070 , 10753971
EP300	HMGN1	No	in vitro;in vivo	10753971
EP300	SMAD2	No	in vivo	11264182 , 11371641
EP300	GTF2B	No	in vitro	10330164
EP300	SP1	No	in vitro;in vivo	10362258
EP300	EID1	No	in vivo	11073989 , 11073990
EP300	SENP3	No	in vitro;in vivo	15632193
EP300	TCF12	No	in vitro	11755530
EP300	RAD50	No	in vivo	16051665
EP300	HOXB7	No	in vitro;in vivo	11585930
EP300	ZBTB17	No	in vitro	12840021
EP300	MPG	No	in vitro	14761960
EP300	ABL1	No	in vivo	16648821
EP300	MAML1	No	in vitro	12050117 , 12391150
EP300	ETV4	No	in vitro	14976201
EP300	NFYB	No	in vitro;in vivo	10075648
EP300	GATA6	No	in vivo	10851229
EP300	CRX	No	in vitro;in vivo	10708567
EP300	GATA4	No	in vivo	11481322
EP300	PDHX	No	in vitro;in vivo	11756538
EP300	JDP2	No	in vitro;in vivo	12101239
EP300	GPBP1	No	in vitro;in vivo	14612417
EP300	PML	No	in vitro	11940591
EP300	AR	Yes	in vitro	10779504
EP300	N4BP2	No	in vivo	12730195
EP300	COPS6	No	yeast 2-hybrid	16169070
EP300	EGR1	Yes	in vivo;yeast 2-hybrid	9806899
EP300	NAP1L1	No	in vitro;in vivo;yeast 2-hybrid	11940655
EP300	HNF1A	No	in vitro;in vivo	11978637
EP300	RAD23A	No	in vitro;yeast 2-hybrid	11196199
EP300	NUPR1	Yes	in vitro	11940591
EP300	MAF	No	in vivo;yeast 2-hybrid	11943779
EP300	GPS2	No	in vitro;in vivo	10846067
EP300	ETS2	No	in vitro	10942770
EP300	IRF2	Yes	in vitro;in vivo	11304541
EP300	CTNNB1	No	in vitro;in vivo	15060161
EP300	ZEB1	No	in vitro	12743039
EP300	PIAS3	No	in vitro;yeast 2-hybrid	14691252
EP300	TADA3	No	in vivo;yeast 2-hybrid	11707411
EP300	MYBL2	No	in vivo	11733503
EP300	ESR1	Yes	in vitro;in vivo	11782371
EP300	PRKCD	No	in vitro;in vivo	12379484 , 11020388
EP300	TCF3	No	in vitro;in vivo	12435739
EP300	PPP2R5C	No	in vitro;in vivo	15632055
EP300	ZNF148	No	in vitro;in vivo	10899165
EP300	AKT1	No	in vitro	11116148
EP300	HNRNPU	No	in vitro;in vivo	11909954
EP300	KLF2	No	in vitro	15136591
EP300	SMAD4	No	in vitro	9843571
EP300	YY1	No	in vivo	7758944
EP300	ING1	No	in vivo	12015309
EP300	CREBBP	Yes	in vitro	9267036
EP300	POU3F2	No	in vitro;yeast 2-hybrid	11029584
EP300	IRF1	No	in vitro	10438822
EP300	TRIP4	No	in vitro;in vivo;yeast 2-hybrid	10454579
EP300	ELF3	No	in vitro;in vivo	15075319
EP300	RUNX2	No	in vitro;in vivo	12697832
EP300	TAL1	No	in vitro;in vivo	10490830
EP300	TRERF1	No	in vitro;in vivo	11349124
EP300	MEF2A	No	in vivo	12371907
EP300	OLIG2	Yes	in vitro	14576772
EP300	RUNX1	No	in vitro;in vivo	14752096
EP300	TP53	No	in vitro;in vivo	16438982 , 12724314 , 9288740 , 9744860 , 9809062 , 10942770 , 9194564 , 11907332
EP300	MEF2C	No	in vitro	9001254
EP300	DTX1	No	in vivo	11564735
EP300	DBP	No	in vitro;in vivo	10364202
EP300	ALX1	No	in vitro;in vivo;yeast 2-hybrid	12929931
EP300	ZBTB16	Yes	in vitro;in vivo	15964811
EP300	PELP1	No	in vivo	11481323
EP300	FHL2	No	in vitro;in vivo	15572674
EP300	GABPA	No	in vitro	9990060
EP300	MDC1	No	in vitro;in vivo	16051665
EP300	NAP1L4	No	in vitro;in vivo	11073993
EP300	FOXO3	No	in vitro	11896584
EP300	NOTCH1	No	in vitro;in vivo	11604511
EP300	JUN	Yes	in vitro;in vivo	11689449
EP300	LEF1	No	in vitro;in vivo	12446687
EP300	SET	No	in vitro;in vivo	11073993
EP300	SS18L1	No	in vitro	14716005
EP300	NR4A1	No	in vitro	12082103
EP300	SMAD7	No	in vitro;in vivo	12408818
EP300	MGMT	No	in vivo	11564893
EP300	NFATC2	No	in vitro;in vivo	9625762
EP300	MDM4	No	in vitro;in vivo	12483531
EP300	RBM14	No	in vitro	11443112
EP300	TP63	No	in vitro;in vivo	15965232
EP300	SP3	No	in vitro	12071960
EP300	TDG	No	in vitro;in vivo	11864601
EP300	NCOA2	No	in vitro;in vivo	15731352
EP300	CARM1	No	in vivo	15616592
EP300	KAT2A	No	in vitro	9742083
EP300	SOX9	No	in vitro;in vivo	12732631
EP300	IRF7	No	in vitro	12604599
EP300	EPAS1	No	in vitro;in vivo	15261140
EP300	NCOA3	No	in vitro	9267036
EP300	ARNT	No	in vivo	10999956
EP300	TCF7L2	No	in vitro;in vivo	12861022
EP300	EID2	No	in vitro;in vivo	14585496
EP300	MYC	No	in vivo	12776737 , 17157259
EP300	ETS1	No	in vitro	10942770

Gene Report

Literature-origin GO terms

Gene mapped GO terms

Gene mapped KEGG pathways

Literature-origin BioCarta pathway

Gene mapped BioCarta pathways