Details for: EP300

Gene ID: 2033

Symbol: EP300

Ensembl ID: ENSG00000100393

Description: E1A binding protein p300

Associated with

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: polychromatophilic erythroblast (CL0000550)
    Fold Change: 389.8705
    Cell Significance Index: -60.6400
  • Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
    Fold Change: 242.7818
    Cell Significance Index: -61.5800
  • Cell Name: smooth muscle fiber of ileum (CL1000278)
    Fold Change: 137.5914
    Cell Significance Index: -64.9600
  • Cell Name: mucosal type mast cell (CL0000485)
    Fold Change: 132.5515
    Cell Significance Index: -53.8500
  • Cell Name: peripheral blood mononuclear cell (CL2000001)
    Fold Change: 119.1519
    Cell Significance Index: -61.2900
  • Cell Name: ciliated cell of the bronchus (CL0002332)
    Fold Change: 56.5807
    Cell Significance Index: -54.0200
  • Cell Name: orthochromatic erythroblast (CL0000552)
    Fold Change: 50.1235
    Cell Significance Index: -61.8000
  • Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
    Fold Change: 23.3346
    Cell Significance Index: -62.5100
  • Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
    Fold Change: 17.4478
    Cell Significance Index: -53.5900
  • Cell Name: stromal cell of bone marrow (CL0010001)
    Fold Change: 16.1731
    Cell Significance Index: -63.8200
  • Cell Name: epidermal Langerhans cell (CL0002457)
    Fold Change: 12.5378
    Cell Significance Index: -27.4400
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 1.9843
    Cell Significance Index: 398.0500
  • Cell Name: neoplastic cell (CL0001063)
    Fold Change: 1.8926
    Cell Significance Index: 375.5900
  • Cell Name: retinal progenitor cell (CL0002672)
    Fold Change: 1.4606
    Cell Significance Index: 81.9600
  • Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 1.4108
    Cell Significance Index: 506.0200
  • Cell Name: intestinal crypt stem cell of colon (CL0009043)
    Fold Change: 1.3193
    Cell Significance Index: 143.5000
  • Cell Name: enteroendocrine cell of small intestine (CL0009006)
    Fold Change: 1.2645
    Cell Significance Index: 31.6100
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: 1.0620
    Cell Significance Index: 29.6800
  • Cell Name: basal cell of urothelium (CL1000486)
    Fold Change: 1.0510
    Cell Significance Index: 129.2300
  • Cell Name: cardiac muscle myoblast (CL0000513)
    Fold Change: 0.9820
    Cell Significance Index: 75.3600
  • Cell Name: tuft cell of colon (CL0009041)
    Fold Change: 0.9498
    Cell Significance Index: 857.6300
  • Cell Name: intermediate cell of urothelium (CL4030055)
    Fold Change: 0.9437
    Cell Significance Index: 170.1200
  • Cell Name: GABAergic interneuron (CL0011005)
    Fold Change: 0.8030
    Cell Significance Index: 555.3600
  • Cell Name: enterocyte of epithelium of large intestine (CL0002071)
    Fold Change: 0.7907
    Cell Significance Index: 35.8400
  • Cell Name: skeletal muscle fiber (CL0008002)
    Fold Change: 0.6880
    Cell Significance Index: 17.6900
  • Cell Name: forebrain neuroblast (CL1000042)
    Fold Change: 0.6175
    Cell Significance Index: 37.9600
  • Cell Name: placental villous trophoblast (CL2000060)
    Fold Change: 0.6022
    Cell Significance Index: 16.0800
  • Cell Name: enterocyte of epithelium of small intestine (CL1000334)
    Fold Change: 0.5902
    Cell Significance Index: 17.0100
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 0.5750
    Cell Significance Index: 29.9500
  • Cell Name: early pro-B cell (CL0002046)
    Fold Change: 0.5748
    Cell Significance Index: 37.0900
  • Cell Name: preadipocyte (CL0002334)
    Fold Change: 0.5616
    Cell Significance Index: 10.9600
  • Cell Name: cell in vitro (CL0001034)
    Fold Change: 0.5537
    Cell Significance Index: 302.3900
  • Cell Name: stromal cell of ovary (CL0002132)
    Fold Change: 0.5240
    Cell Significance Index: 71.9600
  • Cell Name: hair follicular keratinocyte (CL2000092)
    Fold Change: 0.4055
    Cell Significance Index: 179.2800
  • Cell Name: indirect pathway medium spiny neuron (CL4023029)
    Fold Change: 0.3963
    Cell Significance Index: 17.5300
  • Cell Name: direct pathway medium spiny neuron (CL4023026)
    Fold Change: 0.3209
    Cell Significance Index: 12.1500
  • Cell Name: hippocampal granule cell (CL0001033)
    Fold Change: 0.2469
    Cell Significance Index: 16.6000
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: 0.2353
    Cell Significance Index: 443.1300
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: 0.1732
    Cell Significance Index: 110.0000
  • Cell Name: small intestine goblet cell (CL1000495)
    Fold Change: 0.1429
    Cell Significance Index: 5.0200
  • Cell Name: cerebellar granule cell (CL0001031)
    Fold Change: 0.1418
    Cell Significance Index: 2.4300
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: 0.1387
    Cell Significance Index: 62.9600
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: 0.1263
    Cell Significance Index: 194.4200
  • Cell Name: bladder urothelial cell (CL1001428)
    Fold Change: 0.1140
    Cell Significance Index: 5.9200
  • Cell Name: pancreatic acinar cell (CL0002064)
    Fold Change: 0.1137
    Cell Significance Index: 19.4200
  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: 0.1118
    Cell Significance Index: 206.2300
  • Cell Name: tonsil germinal center B cell (CL2000006)
    Fold Change: 0.0691
    Cell Significance Index: 8.1500
  • Cell Name: odontoblast (CL0000060)
    Fold Change: 0.0520
    Cell Significance Index: 6.6700
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: 0.0369
    Cell Significance Index: 50.1900
  • Cell Name: enteroendocrine cell of colon (CL0009042)
    Fold Change: 0.0087
    Cell Significance Index: 1.6600
  • Cell Name: colon goblet cell (CL0009039)
    Fold Change: 0.0073
    Cell Significance Index: 0.7200
  • Cell Name: cortical cell of adrenal gland (CL0002097)
    Fold Change: -0.0045
    Cell Significance Index: -0.1200
  • Cell Name: pancreatic A cell (CL0000171)
    Fold Change: -0.0198
    Cell Significance Index: -14.6300
  • Cell Name: pancreatic PP cell (CL0002275)
    Fold Change: -0.0235
    Cell Significance Index: -14.6800
  • Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
    Fold Change: -0.0348
    Cell Significance Index: -25.5300
  • Cell Name: acinar cell of salivary gland (CL0002623)
    Fold Change: -0.0650
    Cell Significance Index: -3.0300
  • Cell Name: pulmonary alveolar epithelial cell (CL0000322)
    Fold Change: -0.0676
    Cell Significance Index: -51.1600
  • Cell Name: type B pancreatic cell (CL0000169)
    Fold Change: -0.0798
    Cell Significance Index: -45.0200
  • Cell Name: epithelial cell of small intestine (CL0002254)
    Fold Change: -0.1016
    Cell Significance Index: -16.5300
  • Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
    Fold Change: -0.1504
    Cell Significance Index: -7.0700
  • Cell Name: eye photoreceptor cell (CL0000287)
    Fold Change: -0.1536
    Cell Significance Index: -9.6800
  • Cell Name: pancreatic endocrine cell (CL0008024)
    Fold Change: -0.1600
    Cell Significance Index: -18.2600
  • Cell Name: sebum secreting cell (CL0000317)
    Fold Change: -0.1719
    Cell Significance Index: -12.1600
  • Cell Name: pancreatic D cell (CL0000173)
    Fold Change: -0.1812
    Cell Significance Index: -38.1700
  • Cell Name: abnormal cell (CL0001061)
    Fold Change: -0.1892
    Cell Significance Index: -19.3300
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: -0.1955
    Cell Significance Index: -56.2600
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: -0.1984
    Cell Significance Index: -28.8400
  • Cell Name: cortical interneuron (CL0008031)
    Fold Change: -0.2264
    Cell Significance Index: -5.4300
  • Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
    Fold Change: -0.2997
    Cell Significance Index: -5.5400
  • Cell Name: epithelial cell of stomach (CL0002178)
    Fold Change: -0.3031
    Cell Significance Index: -35.3200
  • Cell Name: lactocyte (CL0002325)
    Fold Change: -0.3150
    Cell Significance Index: -40.7000
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: -0.3540
    Cell Significance Index: -4.8300
  • Cell Name: pancreatic ductal cell (CL0002079)
    Fold Change: -0.3713
    Cell Significance Index: -42.5400
  • Cell Name: basal cell of prostate epithelium (CL0002341)
    Fold Change: -0.4357
    Cell Significance Index: -11.8600
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: -0.4596
    Cell Significance Index: -47.8600
  • Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
    Fold Change: -0.4993
    Cell Significance Index: -37.2100
  • Cell Name: transit amplifying cell of small intestine (CL0009012)
    Fold Change: -0.5122
    Cell Significance Index: -10.6300
  • Cell Name: hippocampal pyramidal neuron (CL1001571)
    Fold Change: -0.5565
    Cell Significance Index: -15.8800
  • Cell Name: paneth cell of epithelium of small intestine (CL1000343)
    Fold Change: -0.5701
    Cell Significance Index: -12.3500
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: -0.6482
    Cell Significance Index: -18.5800
  • Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
    Fold Change: -0.6751
    Cell Significance Index: -53.4700
  • Cell Name: umbrella cell of urothelium (CL4030056)
    Fold Change: -0.7091
    Cell Significance Index: -6.5300
  • Cell Name: endothelial cell of placenta (CL0009092)
    Fold Change: -0.7249
    Cell Significance Index: -4.3800
  • Cell Name: leptomeningeal cell (CL0000708)
    Fold Change: -0.7380
    Cell Significance Index: -15.7800
  • Cell Name: glycinergic neuron (CL1001509)
    Fold Change: -0.8743
    Cell Significance Index: -45.9100
  • Cell Name: fibroblast of cardiac tissue (CL0002548)
    Fold Change: -0.8795
    Cell Significance Index: -12.6300
  • Cell Name: intestinal tuft cell (CL0019032)
    Fold Change: -0.9246
    Cell Significance Index: -56.6900
  • Cell Name: retinal rod cell (CL0000604)
    Fold Change: -1.0318
    Cell Significance Index: -12.3000
  • Cell Name: peg cell (CL4033014)
    Fold Change: -1.0323
    Cell Significance Index: -23.8500
  • Cell Name: granulosa cell (CL0000501)
    Fold Change: -1.0523
    Cell Significance Index: -27.6700
  • Cell Name: centrilobular region hepatocyte (CL0019029)
    Fold Change: -1.1027
    Cell Significance Index: -18.5800
  • Cell Name: cardiac muscle cell (CL0000746)
    Fold Change: -1.1054
    Cell Significance Index: -16.3200
  • Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
    Fold Change: -1.1095
    Cell Significance Index: -23.6300
  • Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
    Fold Change: -1.1299
    Cell Significance Index: -23.9800
  • Cell Name: Purkinje cell (CL0000121)
    Fold Change: -1.1317
    Cell Significance Index: -24.7800
  • Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
    Fold Change: -1.2057
    Cell Significance Index: -38.4000
  • Cell Name: L6b glutamatergic cortical neuron (CL4023038)
    Fold Change: -1.2104
    Cell Significance Index: -39.6300
  • Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
    Fold Change: -1.2711
    Cell Significance Index: -44.1700
  • Cell Name: neutrophil progenitor cell (CL0000834)
    Fold Change: -1.3081
    Cell Significance Index: -34.9900
  • Cell Name: mesenchymal cell (CL0008019)
    Fold Change: -1.3386
    Cell Significance Index: -22.4000

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.

Other Information

**Key Characteristics:** 1. **Histone Acetyltransferase (HAT) Activity:** EP300 possesses HAT activity, which enables it to acetylate histones, leading to chromatin relaxation and increased gene transcription. 2. **Broad Interactions:** EP300 interacts with numerous transcription factors, signaling pathways, and proteins, including Notch, Wnt, and NF-κB, to regulate gene expression and cellular processes. 3. **Cell Cycle Regulation:** EP300 is involved in regulating the cell cycle, particularly during G2/M transition, ensuring proper cell division and proliferation. 4. **Stress Response:** EP300 is activated in response to various forms of cellular stress, including heat, hypoxia, and chemical stress, to regulate cellular responses and maintain homeostasis. 5. **Epigenetic Regulation:** EP300 modulates epigenetic marks, such as histone modifications and DNA methylation, to regulate gene expression and cellular processes. **Pathways and Functions:** 1. **Cellular Signaling:** EP300 is involved in various signaling pathways, including Notch, Wnt, and NF-κB, to regulate gene expression and cellular processes. 2. **Gene Expression:** EP300 regulates gene expression by acetylating histones, interacting with transcription factors, and modulating epigenetic marks. 3. **Cell Cycle Regulation:** EP300 ensures proper cell division and proliferation by regulating the cell cycle, particularly during G2/M transition. 4. **Stress Response:** EP300 responds to various forms of cellular stress, activating cellular responses and maintaining homeostasis. 5. **Immune Response:** EP300 is involved in regulating the immune response, particularly in the context of viral infections and cancer. **Clinical Significance:** 1. **Cancer:** EP300 is often overexpressed in various types of cancer, contributing to tumorigenesis and cancer progression. 2. **Neurological Disorders:** EP300 is involved in regulating gene expression in the brain, making it a potential target for treating neurological disorders, such as Alzheimer's disease and Parkinson's disease. 3. **Infectious Diseases:** EP300 is activated in response to viral infections, making it a potential target for treating infectious diseases. 4. ** Metabolic Disorders:** EP300 regulates lipid metabolism, making it a potential target for treating metabolic disorders, such as obesity and diabetes. In conclusion, EP300 is a multifunctional protein that plays a crucial role in regulating gene expression, cell cycle, and various cellular processes. Its involvement in various diseases highlights its importance in maintaining cellular balance. Further research is necessary to fully elucidate the mechanisms by which EP300 regulates cellular processes and to identify potential therapeutic targets for various diseases.

Genular Protein ID: 2324620225

Symbol: EP300_HUMAN

Name: E1A-associated protein p300

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 7523245

Title: Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor.

PubMed ID: 7523245

DOI: 10.1101/gad.8.8.869

PubMed ID: 10591208

Title: The DNA sequence of human chromosome 22.

PubMed ID: 10591208

DOI: 10.1038/990031

PubMed ID: 10824998

Title: MOZ is fused to p300 in an acute monocytic leukemia with t(8;22).

PubMed ID: 10824998

DOI: 10.1002/(sici)1098-2264(200006)28:2<138::aid-gcc2>3.0.co;2-2

PubMed ID: 7870179

Title: Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP.

PubMed ID: 7870179

DOI: 10.1038/374085a0

PubMed ID: 11701890

Title: A transcriptional switch mediated by cofactor methylation.

PubMed ID: 11701890

DOI: 10.1126/science.1065961

PubMed ID: 10518217

Title: A novel cofactor for p300 that regulates the p53 response.

PubMed ID: 10518217

DOI: 10.1016/s1097-2765(00)80338-x

PubMed ID: 8945521

Title: The transcriptional coactivators p300 and CBP are histone acetyltransferases.

PubMed ID: 8945521

DOI: 10.1016/s0092-8674(00)82001-2

PubMed ID: 8684459

Title: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A.

PubMed ID: 8684459

DOI: 10.1038/382319a0

PubMed ID: 8917528

Title: An essential role for p300/CBP in the cellular response to hypoxia.

PubMed ID: 8917528

DOI: 10.1073/pnas.93.23.12969

PubMed ID: 9528808

Title: Differential transcriptional activation by human T-cell leukemia virus type 1 Tax mutants is mediated by distinct interactions with CREB binding protein and p300.

PubMed ID: 9528808

DOI: 10.1128/mcb.18.4.2392

PubMed ID: 9590696

Title: Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex.

PubMed ID: 9590696

DOI: 10.1038/30032

PubMed ID: 10545121

Title: HIV-1 tat transcriptional activity is regulated by acetylation.

PubMed ID: 10545121

DOI: 10.1093/emboj/18.21.6106

PubMed ID: 9887100

Title: Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1.

PubMed ID: 9887100

DOI: 10.1101/gad.13.1.64

PubMed ID: 9862959

Title: Exogenous expression of a dominant negative RORalpha1 vector in muscle cells impairs differentiation: RORalpha1 directly interacts with p300 and myoD.

PubMed ID: 9862959

DOI: 10.1093/nar/27.2.411

PubMed ID: 10722728

Title: The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors.

PubMed ID: 10722728

DOI: 10.1074/jbc.275.12.8825

PubMed ID: 10733570

Title: A novel transcriptional repression domain mediates p21(WAF1/CIP1) induction of p300 transactivation.

PubMed ID: 10733570

DOI: 10.1128/mcb.20.8.2676-2686.2000

PubMed ID: 11073989

Title: Cells degrade a novel inhibitor of differentiation with E1A-like properties upon exiting the cell cycle.

PubMed ID: 11073989

DOI: 10.1128/mcb.20.23.8889-8902.2000

PubMed ID: 11073990

Title: A novel Rb- and p300-binding protein inhibits transactivation by MyoD.

PubMed ID: 11073990

DOI: 10.1128/mcb.20.23.8903-8915.2000

PubMed ID: 10823961

Title: Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator.

PubMed ID: 10823961

DOI: 10.1073/pnas.97.11.6212

PubMed ID: 11080476

Title: Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones.

PubMed ID: 11080476

DOI: 10.1006/viro.2000.0593

PubMed ID: 11581164

Title: Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein.

PubMed ID: 11581164

DOI: 10.1101/gad.906301

PubMed ID: 11518699

Title: Regulation of transcription by AMP-activated protein kinase: phosphorylation of p300 blocks its interaction with nuclear receptors.

PubMed ID: 11518699

DOI: 10.1074/jbc.c100316200

PubMed ID: 11581372

Title: Adenovirus DNA binding protein interacts with the SNF2-related CBP activator protein (SrCap) and inhibits SrCap-mediated transcription.

PubMed ID: 11581372

DOI: 10.1128/jvi.75.21.10033-10040.2001

PubMed ID: 11511361

Title: A TPR motif cofactor contributes to p300 activity in the p53 response.

PubMed ID: 11511361

DOI: 10.1016/s1097-2765(01)00277-5

PubMed ID: 11463834

Title: The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to mediate transcriptional activation.

PubMed ID: 11463834

DOI: 10.1128/mcb.21.16.5520-5530.2001

PubMed ID: 11559821

Title: Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by binding CREB binding protein/p300.

PubMed ID: 11559821

DOI: 10.1128/jvi.75.20.9885-9895.2001

PubMed ID: 11349124

Title: A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression.

PubMed ID: 11349124

DOI: 10.1074/jbc.m100113200

PubMed ID: 11481323

Title: Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha.

PubMed ID: 11481323

DOI: 10.1074/jbc.m103783200

PubMed ID: 11564735

Title: Role of Deltex-1 as a transcriptional regulator downstream of the Notch receptor.

PubMed ID: 11564735

DOI: 10.1074/jbc.m105245200

PubMed ID: 11430825

Title: Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300.

PubMed ID: 11430825

DOI: 10.1016/s1097-2765(01)00272-6

PubMed ID: 11433299

Title: Acetylation control of the retinoblastoma tumour-suppressor protein.

PubMed ID: 11433299

DOI: 10.1038/35083062

PubMed ID: 11864910

Title: Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with negative cross-talk with c-Myb.

PubMed ID: 11864910

PubMed ID: 11744733

Title: 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.

PubMed ID: 11744733

DOI: 10.1074/jbc.m110850200

PubMed ID: 11940591

Title: The HMG-I/Y-related protein p8 binds to p300 and Pax2 trans-activation domain-interacting protein to regulate the trans-activation activity of the Pax2A and Pax2B transcription factors on the glucagon gene promoter.

PubMed ID: 11940591

DOI: 10.1074/jbc.m201657200

PubMed ID: 11909954

Title: Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes.

PubMed ID: 11909954

DOI: 10.1128/mcb.22.8.2598-2606.2002

PubMed ID: 11997499

Title: Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities.

PubMed ID: 11997499

DOI: 10.1128/mcb.22.11.3621-3632.2002

PubMed ID: 12402037

Title: Acetylation inactivates the transcriptional repressor BCL6.

PubMed ID: 12402037

DOI: 10.1038/ng1018

PubMed ID: 12750254

Title: p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity.

PubMed ID: 12750254

PubMed ID: 12446687

Title: Identification of a promoter-specific transcriptional activation domain at the C-terminus of the Wnt effector protein T-cell factor 4.

PubMed ID: 12446687

DOI: 10.1074/jbc.m210081200

PubMed ID: 12586840

Title: Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2.

PubMed ID: 12586840

DOI: 10.1074/jbc.m208144200

PubMed ID: 12732631

Title: Transcriptional co-activators CREB-binding protein and p300 regulate chondrocyte-specific gene expression via association with Sox9.

PubMed ID: 12732631

DOI: 10.1074/jbc.m303471200

PubMed ID: 12837748

Title: Acetylated SP3 is a transcriptional activator.

PubMed ID: 12837748

DOI: 10.1074/jbc.m305961200

PubMed ID: 12929931

Title: P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1), paired-like homeoprotein, through acetylation of the conserved lysine residue adjacent to the homeodomain.

PubMed ID: 12929931

DOI: 10.1359/jbmr.2003.18.8.1419

PubMed ID: 14605447

Title: SATB1 makes a complex with p300 and represses gp91(phox) promoter activity.

PubMed ID: 14605447

DOI: 10.1111/j.1348-0421.2003.tb03438.x

PubMed ID: 12718889

Title: P300 transcriptional repression is mediated by SUMO modification.

PubMed ID: 12718889

DOI: 10.1016/s1097-2765(03)00141-2

PubMed ID: 12527917

Title: Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300.

PubMed ID: 12527917

DOI: 10.1038/sj.onc.1206067

PubMed ID: 15186775

Title: Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53.

PubMed ID: 15186775

DOI: 10.1016/j.cell.2004.05.009

PubMed ID: 15297880

Title: Regulation of human SRY subcellular distribution by its acetylation/deacetylation.

PubMed ID: 15297880

DOI: 10.1038/sj.emboj.7600352

PubMed ID: 14645221

Title: Histone acetyltransferase-dependent chromatin remodeling and the vascular clock.

PubMed ID: 14645221

DOI: 10.1074/jbc.m311973200

PubMed ID: 15075319

Title: 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.

PubMed ID: 15075319

DOI: 10.1074/jbc.m401356200

PubMed ID: 15509808

Title: Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent acetylation of p53.

PubMed ID: 15509808

DOI: 10.1128/mcb.24.22.10083-10098.2004

PubMed ID: 15448695

Title: A new effector pathway links ATM kinase with the DNA damage response.

PubMed ID: 15448695

DOI: 10.1038/ncb1170

PubMed ID: 15004546

Title: Regulation of the p300 HAT domain via a novel activation loop.

PubMed ID: 15004546

DOI: 10.1038/nsmb740

PubMed ID: 14752053

Title: Orphan nuclear receptor small heterodimer partner, a novel corepressor for a basic helix-loop-helix transcription factor BETA2/neuroD.

PubMed ID: 14752053

DOI: 10.1210/me.2003-0311

PubMed ID: 14716005

Title: Dendrite development regulated by CREST, a calcium-regulated transcriptional activator.

PubMed ID: 14716005

DOI: 10.1126/science.1089845

PubMed ID: 15706485

Title: Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease.

PubMed ID: 15706485

DOI: 10.1086/429130

PubMed ID: 16285960

Title: STAT3 NH2-terminal acetylation is activated by the hepatic acute-phase response and required for IL-6 induction of angiotensinogen.

PubMed ID: 16285960

DOI: 10.1053/j.gastro.2005.07.055

PubMed ID: 15632193

Title: SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1.

PubMed ID: 15632193

DOI: 10.1074/jbc.m408748200

PubMed ID: 16219772

Title: p300 modulates ATF4 stability and transcriptional activity independently of its acetyltransferase domain.

PubMed ID: 16219772

DOI: 10.1074/jbc.m505294200

PubMed ID: 15890677

Title: The coactivator p300 directly acetylates the forkhead transcription factor Foxo1 and stimulates Foxo1-induced transcription.

PubMed ID: 15890677

DOI: 10.1210/me.2004-0292

PubMed ID: 15731352

Title: Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination.

PubMed ID: 15731352

DOI: 10.1073/pnas.0407159102

PubMed ID: 15653507

Title: Stat3 dimerization regulated by reversible acetylation of a single lysine residue.

PubMed ID: 15653507

DOI: 10.1126/science.1105166

PubMed ID: 16809611

Title: BCL11B participates in the activation of IL2 gene expression in CD4+ T lymphocytes.

PubMed ID: 16809611

DOI: 10.1182/blood-2006-05-021790

PubMed ID: 16574662

Title: Nuclear Rho kinase, ROCK2, targets p300 acetyltransferase.

PubMed ID: 16574662

DOI: 10.1074/jbc.m510954200

PubMed ID: 16864582

Title: The transcriptional activity of CITED1 is regulated by phosphorylation in a cell cycle-dependent manner.

PubMed ID: 16864582

DOI: 10.1074/jbc.m602631200

PubMed ID: 17065153

Title: Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation.

PubMed ID: 17065153

DOI: 10.1074/jbc.m608813200

PubMed ID: 16762839

Title: HDAC1 acetylation is linked to progressive modulation of steroid receptor-induced gene transcription.

PubMed ID: 16762839

DOI: 10.1016/j.molcel.2006.04.019

PubMed ID: 16478997

Title: Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription.

PubMed ID: 16478997

DOI: 10.1128/mcb.26.5.1770-1785.2006

PubMed ID: 16617102

Title: MTA1, a transcriptional activator of breast cancer amplified sequence 3.

PubMed ID: 16617102

DOI: 10.1073/pnas.0601989103

PubMed ID: 17872950

Title: Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portion.

PubMed ID: 17872950

DOI: 10.1074/jbc.m703735200

PubMed ID: 17226766

Title: Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF.

PubMed ID: 17226766

DOI: 10.1002/jcb.21250

PubMed ID: 17267393

Title: Lysine propionylation and butyrylation are novel post-translational modifications in histones.

PubMed ID: 17267393

DOI: 10.1074/mcp.m700021-mcp200

PubMed ID: 17761950

Title: Orphan receptor TR3 attenuates the p300-induced acetylation of retinoid X receptor-alpha.

PubMed ID: 17761950

DOI: 10.1210/me.2007-0107

PubMed ID: 18722353

Title: Acetylation of Sirt2 by p300 attenuates its deacetylase activity.

PubMed ID: 18722353

DOI: 10.1016/j.bbrc.2008.08.042

PubMed ID: 18695000

Title: PEBP2-beta/CBF-beta-dependent phosphorylation of RUNX1 and p300 by HIPK2: implications for leukemogenesis.

PubMed ID: 18695000

DOI: 10.1182/blood-2008-01-134122

PubMed ID: 18451878

Title: A transcription cofactor required for the heat-shock response.

PubMed ID: 18451878

DOI: 10.1038/embor.2008.70

PubMed ID: 18599479

Title: An interaction between the human T cell leukemia virus type 1 basic leucine zipper factor (HBZ) and the KIX domain of p300/CBP contributes to the down-regulation of tax-dependent viral transcription by HBZ.

PubMed ID: 18599479

DOI: 10.1074/jbc.m803116200

PubMed ID: 18782771

Title: The STAT3 NH2-terminal domain stabilizes enhanceosome assembly by interacting with the p300 bromodomain.

PubMed ID: 18782771

DOI: 10.1074/jbc.m805941200

PubMed ID: 18809579

Title: PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-mediated degradation.

PubMed ID: 18809579

DOI: 10.1128/mcb.00897-08

PubMed ID: 18995842

Title: The SIRT2 deacetylase regulates autoacetylation of p300.

PubMed ID: 18995842

DOI: 10.1016/j.molcel.2008.09.018

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19680224

Title: SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation.

PubMed ID: 19680224

DOI: 10.1038/emboj.2009.210

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20940255

Title: Acetylation of Rb by PCAF is required for nuclear localization and keratinocyte differentiation.

PubMed ID: 20940255

DOI: 10.1242/jcs.068924

PubMed ID: 20810990

Title: p300-mediated acetylation stabilizes the Th-inducing POK factor.

PubMed ID: 20810990

DOI: 10.4049/jimmunol.1001462

PubMed ID: 20081228

Title: Cyclin-dependent kinase-9 is a component of the p300/GATA4 complex required for phenylephrine-induced hypertrophy in cardiomyocytes.

PubMed ID: 20081228

DOI: 10.1074/jbc.m109.070458

PubMed ID: 21030595

Title: HDAC3 is negatively regulated by the nuclear protein DBC1.

PubMed ID: 21030595

DOI: 10.1074/jbc.m110.153270

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 20955178

Title: Regulation of unfolded protein response modulator XBP1s by acetylation and deacetylation.

PubMed ID: 20955178

DOI: 10.1042/bj20101293

PubMed ID: 21131905

Title: Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated H3K18/27ac in nuclear receptor transactivation.

PubMed ID: 21131905

DOI: 10.1038/emboj.2010.318

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 23145062

Title: Human ALKBH4 interacts with proteins associated with transcription.

PubMed ID: 23145062

DOI: 10.1371/journal.pone.0049045

PubMed ID: 23415232

Title: Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer.

PubMed ID: 23415232

DOI: 10.1016/j.cell.2013.01.032

PubMed ID: 23911289

Title: A hybrid mechanism of action for BCL6 in B cells defined by formation of functionally distinct complexes at enhancers and promoters.

PubMed ID: 23911289

DOI: 10.1016/j.celrep.2013.06.016

PubMed ID: 23999430

Title: Kruppel-like factor 15 is critical for vascular inflammation.

PubMed ID: 23999430

DOI: 10.1172/jci68552

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24120661

Title: Mitogenic and oncogenic stimulation of K433 acetylation promotes PKM2 protein kinase activity and nuclear localization.

PubMed ID: 24120661

DOI: 10.1016/j.molcel.2013.09.004

Sequence Information:

  • Length: 2414
  • Mass: 264161
  • Checksum: 8E869E1F174A6FEB
  • Sequence:
  • MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD 
    INQLQTSLGM VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQVMASQAQQ SSPGLGLINS 
    MVKSPMTQAG LTSPNMGMGT SGPNQGPTQS TGMMNSPVNQ PAMGMNTGMN AGMNPGMLAA 
    GNGQGIMPNQ VMNGSIGAGR GRQNMQYPNP GMGSAGNLLT EPLQQGSPQM GGQTGLRGPQ 
    PLKMGMMNNP NPYGSPYTQN PGQQIGASGL GLQIQTKTVL SNNLSPFAMD KKAVPGGGMP 
    NMGQQPAPQV QQPGLVTPVA QGMGSGAHTA DPEKRKLIQQ QLVLLLHAHK CQRREQANGE 
    VRQCNLPHCR TMKNVLNHMT HCQSGKSCQV AHCASSRQII SHWKNCTRHD CPVCLPLKNA 
    GDKRNQQPIL TGAPVGLGNP SSLGVGQQSA PNLSTVSQID PSSIERAYAA LGLPYQVNQM 
    PTQPQVQAKN QQNQQPGQSP QGMRPMSNMS ASPMGVNGGV GVQTPSLLSD SMLHSAINSQ 
    NPMMSENASV PSLGPMPTAA QPSTTGIRKQ WHEDITQDLR NHLVHKLVQA IFPTPDPAAL 
    KDRRMENLVA YARKVEGDMY ESANNRAEYY HLLAEKIYKI QKELEEKRRT RLQKQNMLPN 
    AAGMVPVSMN PGPNMGQPQP GMTSNGPLPD PSMIRGSVPN QMMPRITPQS GLNQFGQMSM 
    AQPPIVPRQT PPLQHHGQLA QPGALNPPMG YGPRMQQPSN QGQFLPQTQF PSQGMNVTNI 
    PLAPSSGQAP VSQAQMSSSS CPVNSPIMPP GSQGSHIHCP QLPQPALHQN SPSPVPSRTP 
    TPHHTPPSIG AQQPPATTIP APVPTPPAMP PGPQSQALHP PPRQTPTPPT TQLPQQVQPS 
    LPAAPSADQP QQQPRSQQST AASVPTPTAP LLPPQPATPL SQPAVSIEGQ VSNPPSTSST 
    EVNSQAIAEK QPSQEVKMEA KMEVDQPEPA DTQPEDISES KVEDCKMEST ETEERSTELK 
    TEIKEEEDQP STSATQSSPA PGQSKKKIFK PEELRQALMP TLEALYRQDP ESLPFRQPVD 
    PQLLGIPDYF DIVKSPMDLS TIKRKLDTGQ YQEPWQYVDD IWLMFNNAWL YNRKTSRVYK 
    YCSKLSEVFE QEIDPVMQSL GYCCGRKLEF SPQTLCCYGK QLCTIPRDAT YYSYQNRYHF 
    CEKCFNEIQG ESVSLGDDPS QPQTTINKEQ FSKRKNDTLD PELFVECTEC GRKMHQICVL 
    HHEIIWPAGF VCDGCLKKSA RTRKENKFSA KRLPSTRLGT FLENRVNDFL RRQNHPESGE 
    VTVRVVHASD KTVEVKPGMK ARFVDSGEMA ESFPYRTKAL FAFEEIDGVD LCFFGMHVQE 
    YGSDCPPPNQ RRVYISYLDS VHFFRPKCLR TAVYHEILIG YLEYVKKLGY TTGHIWACPP 
    SEGDDYIFHC HPPDQKIPKP KRLQEWYKKM LDKAVSERIV HDYKDIFKQA TEDRLTSAKE 
    LPYFEGDFWP NVLEESIKEL EQEEEERKRE ENTSNESTDV TKGDSKNAKK KNNKKTSKNK 
    SSLSRGNKKK PGMPNVSNDL SQKLYATMEK HKEVFFVIRL IAGPAANSLP PIVDPDPLIP 
    CDLMDGRDAF LTLARDKHLE FSSLRRAQWS TMCMLVELHT QSQDRFVYTC NECKHHVETR 
    WHCTVCEDYD LCITCYNTKN HDHKMEKLGL GLDDESNNQQ AAATQSPGDS RRLSIQRCIQ 
    SLVHACQCRN ANCSLPSCQK MKRVVQHTKG CKRKTNGGCP ICKQLIALCC YHAKHCQENK 
    CPVPFCLNIK QKLRQQQLQH RLQQAQMLRR RMASMQRTGV VGQQQGLPSP TPATPTTPTG 
    QQPTTPQTPQ PTSQPQPTPP NSMPPYLPRT QAAGPVSQGK AAGQVTPPTP PQTAQPPLPG 
    PPPAAVEMAM QIQRAAETQR QMAHVQIFQR PIQHQMPPMT PMAPMGMNPP PMTRGPSGHL 
    EPGMGPTGMQ QQPPWSQGGL PQPQQLQSGM PRPAMMSVAQ HGQPLNMAPQ PGLGQVGISP 
    LKPGTVSQQA LQNLLRTLRS PSSPLQQQQV LSILHANPQL LAAFIKQRAA KYANSNPQPI 
    PGQPGMPQGQ PGLQPPTMPG QQGVHSNPAM QNMNPMQAGV QRAGLPQQQP QQQLQPPMGG 
    MSPQAQQMNM NHNTMPSQFR DILRRQQMMQ QQQQQGAGPG IGPGMANHNQ FQQPQGVGYP 
    PQQQQRMQHH MQQMQQGNMG QIGQLPQALG AEAGASLQAY QQRLLQQQMG SPVQPNPMSP 
    QQHMLPNQAQ SPHLQGQQIP NSLSNQVRSP QPVPSPRPQS QPPHSSPSPR MQPQPSPHHV 
    SPQTSSPHPG LVAAQANPME QGHFASPDQN SMLSQLASNP GMANLHGASA TDLGLSTDNS 
    DLNSNLSQST LDIH

Genular Protein ID: 2362155451

Symbol: Q7Z6C1_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

Sequence Information:

  • Length: 1553
  • Mass: 170081
  • Checksum: BEFFB9C8206AD891
  • Sequence:
  • MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD 
    INQLQTSLGM VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQVMASQAQQ SSPGLGLINS 
    MVKSPMTQAG LTSPNMGMGT SGPNQGPTQS TGMMNSPVNQ PAMGMNTGMN AGMNPGMLAA 
    GNGQGIMPNQ VMNGSIGAGR GRQNMQYPNP GMGSAGNLLT EPLQQGSPQM GGQTGLRGPQ 
    PLKMGMMNNP NPYGSPYTQN PGQQIGASGL GLQIQTKTVL SNNLSPFAMD KKAVPGGGMP 
    NMGQQPAPQV QQPGLVTPVA QGMGSGAHTA DPEKRKLIQQ QLVLLLHAHK CQRREQANGE 
    VRQCNLPHCR TMKNVLNHMT HCQSGKSCQV AHCASSRQII SHWKNCTRHD CPVCLPLKNA 
    GDKRNQQPIL TGAPVGLGNP SSLGVGQQSA PNLSTVSQID PSSIERAYAA LGLPYQVNQM 
    PTQPQVQAKN QQNQQPGQSP QGMRPMSNMS ASPMGVNGGV GVQTPSLLSD SMLHSAINSQ 
    NPMMSENASV PSLGPMPTAA QPSTTGIRKQ WHEDITQDLR NHLVHKLVQA IFPTPDPAAL 
    KDRRMENLVA YARKVEGDMY ESANNRAEYY HLLAEKIYKI QKELEEKRRT RLQKQNMLPN 
    AAGMVPVSMN PGPNMGQPQP GMTSNGPLPD PSMIRGSVPN QMMPRITPQS GLNQFGQMSM 
    AQPPIVPRQT PPLQHHGQLA QPGALNPPMG YGPRMQQPSN QGQFLPQTQF PSQGMNVTNI 
    PLAPSSGQAP VSQAQMSSSS CPVNSPIMPP GSQGSHIHCP QLPQPALHQN SPSPVPSRTP 
    TPHHTPPSIG AQQPPATTIP APVPTPPAMP PGPQSQALHP PPRQTPTPPT TQLPQQVQPS 
    LPAAPSADQP QQQPRSQQST AASVPTPTAP LLPPQPATPL SQPAVSIEGQ VSNPPSTSST 
    EVNSQAIAEK QPSQEVKMEA KMEVDQPEPA DTQPEDISES KVEDCKMEST ETEERSTELK 
    TEIKEEEDQP STSATQSSPA PGQSKKKIFK PEELRQALMP TLEALYRQDP ESLPFRQPVD 
    PQLLGIPDYF DIVKSPMDLS TIKRKLDTGQ YQEPWQYVDD IWLMFNNAWL YNRKTSRVYK 
    YCSKLSEVFE QEIDPVMQSL GYCCGRKLEF SPQTLCCYGK QLCTIPRDAT YYSYQNRYHF 
    CEKCFNEIQG ESVSLGDDPS QPQTTINKEQ FSKRKNDTLD PELFVECTEC GRKMHQICVL 
    HHEIIWPAGF VCDGCLKKSA RTRKENKFSA KRLPSTRLGT FLENRVNDFL RRQNHPESGE 
    VTVRVVHASD KTVEVKPGMK ARFVDSGEMA ESFPYRTKAL FAFEEIDGVD LCFFGMHVQE 
    YGSDCPPPNQ RRVYISYLDS VHFFRPKCLR TAVYHEILIG YLEYVKKLGY TTGHIWACPP 
    SEGDDYIFHC HPPDQKIPKP KRLQEWYKKM LDKAVSERIV HDYKDIFKQA TEDRLTSAKE 
    LPYFEGDFWP NVLEESIKEL EQEEEERKRE ENTSNESTDV TKGDSKNAKK KKK

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.