EP300

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EP300
Protein EP300 PDB 1f81.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases EP300 , KAT3B, RSTS2, p300, E1A binding protein p300, MKHK2
External IDs OMIM: 602700; MGI: 1276116; HomoloGene: 1094; GeneCards: EP300; OMA:EP300 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

2033

328572

Ensembl

ENSG00000100393

ENSMUSG00000055024

UniProt

Q09472

B2RWS6

RefSeq (mRNA)

NM_001429
NM_001362843

NM_177821

RefSeq (protein)

NP_001420
NP_001349772

NP_808489

Location (UCSC) Chr 22: 41.09 – 41.18 Mb Chr 15: 81.47 – 81.54 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Histone acetyltransferase p300 also known as p300 HAT or E1A-associated protein p300 (where E1A = adenovirus early region 1A) also known as EP300 or p300 is an enzyme that, in humans, is encoded by the EP300 gene. [5] It functions as histone acetyltransferase that regulates transcription of genes via chromatin remodeling by allowing histone proteins to wrap DNA less tightly. This enzyme plays an essential role in regulating cell growth and division, prompting cells to mature and assume specialized functions (differentiate), and preventing the growth of cancerous tumors. The p300 protein appears to be critical for normal development before and after birth.

The EP300 gene is located on the long (q) arm of the human chromosome 22 at position 13.2. This gene encodes the adenovirus E1A-associated cellular p300 transcriptional co-activator protein.

EP300 is closely related to another gene, CREB binding protein, which is found on human chromosome 16.

Function

p300 HAT functions as histone acetyltransferase [6] that regulates transcription via chromatin remodeling, and is important in the processes of cell proliferation and differentiation. It mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein.

p300 HAT contains a bromodomain which is involved in IL6 signaling. [7] : 3.1 

This gene has also been identified as a co-activator of HIF1A (hypoxia-inducible factor 1 alpha), and, thus, plays a role in the stimulation of hypoxia-induced genes such as VEGF. [8]

Mechanism

The p300 protein carries out its function of activating transcription by binding to transcription factors, and the transcription machinery. On the basis of this function, p300 is called a transcriptional coactivator. The p300 interaction with transcription factors is managed by one or more of p300 domains: the nuclear receptor interaction domain (RID), the KIX domain (CREB and MYB interaction domain), the cysteine/histidine regions (TAZ1/CH1 and TAZ2/CH3) and the interferon response binding domain (IBiD). The last four domains, KIX, TAZ1, TAZ2 and IBiD of p300, each bind tightly to a sequence spanning both transactivation domains 9aaTADs of transcription factor p53. [9]

Clinical significance

Mutations in the EP300 gene are responsible for a small percentage of cases of Rubinstein-Taybi syndrome. These mutations result in the loss of one copy of the gene in each cell, which reduces the amount of p300 protein by half. Some mutations lead to the production of a very short, nonfunctional version of the p300 protein, while others prevent one copy of the gene from making any protein at all. Although researchers do not know how a reduction in the amount of p300 protein leads to the specific features of Rubinstein-Taybi syndrome, it is clear that the loss of one copy of the EP300 gene disrupts normal development.[ citation needed ]

Chromosomal rearrangements involving chromosome 22 have rarely been associated with certain types of cancer. These rearrangements, called translocations, disrupt the region of chromosome 22 that contains the EP300 gene. For example, researchers have found a translocation between chromosomes 8 and 22 in several people with a cancer of blood cells called acute myeloid leukemia (AML). Another translocation, involving chromosomes 11 and 22, has been found in a small number of people who have undergone cancer treatment. This chromosomal change is associated with the development of AML following chemotherapy for other forms of cancer.[ citation needed ]

Mutations in the EP300 gene have been identified in several other types of cancer. These mutations are somatic, which means they are acquired during a person's lifetime and are present only in certain cells. Somatic mutations in the EP300 gene have been found in a small number of solid tumors, including cancers of the colon and rectum, stomach, breast, and pancreas. Studies suggest that EP300 mutations may also play a role in the development of some prostate cancers, and could help predict whether these tumors will increase in size or spread to other parts of the body. In cancer cells, EP300 mutations prevent the gene from producing any functional protein. Without p300, cells cannot effectively restrain growth and division, which can allow cancerous tumors to form.[ citation needed ]

Interactions

EP300 has been shown to interact with:

Related Research Articles

p300-CBP coactivator family Protein family

The p300-CBP coactivator family in humans is composed of two closely related transcriptional co-activating proteins :

  1. p300
  2. CBP
<span class="mw-page-title-main">PCAF</span> Protein-coding gene in humans

P300/CBP-associated factor (PCAF), also known as K(lysine) acetyltransferase 2B (KAT2B), is a human gene and transcriptional coactivator associated with p53.

<span class="mw-page-title-main">CREB-binding protein</span> Nuclear protein that binds to CREB

CREB-binding protein, also known as CREBBP or CBP or KAT3A, is a coactivator encoded by the CREBBP gene in humans, located on chromosome 16p13.3. CBP has intrinsic acetyltransferase functions; it is able to add acetyl groups to both transcription factors as well as histone lysines, the latter of which has been shown to alter chromatin structure making genes more accessible for transcription. This relatively unique acetyltransferase activity is also seen in another transcription enzyme, EP300 (p300). Together, they are known as the p300-CBP coactivator family and are known to associate with more than 16,000 genes in humans; however, while these proteins share many structural features, emerging evidence suggests that these two co-activators may promote transcription of genes with different biological functions.

<span class="mw-page-title-main">IRF3</span> Protein-coding gene in the species Homo sapiens

Interferon regulatory factor 3, also known as IRF3, is an interferon regulatory factor.

<span class="mw-page-title-main">Nuclear receptor coactivator 2</span> Protein-coding gene in the species Homo sapiens

The nuclear receptor coactivator 2 also known as NCoA-2 is a protein that in humans is encoded by the NCOA2 gene. NCoA-2 is also frequently called glucocorticoid receptor-interacting protein 1 (GRIP1), steroid receptor coactivator-2 (SRC-2), or transcriptional mediators/intermediary factor 2 (TIF2).

<span class="mw-page-title-main">Nuclear receptor coactivator 3</span> Protein found in humans

The nuclear receptor coactivator 3 also known as NCOA3 is a protein that, in humans, is encoded by the NCOA3 gene. NCOA3 is also frequently called 'amplified in breast 1' (AIB1), steroid receptor coactivator-3 (SRC-3), or thyroid hormone receptor activator molecule 1 (TRAM-1).

<span class="mw-page-title-main">Retinoid X receptor alpha</span> Protein-coding gene in the species Homo sapiens

Retinoid X receptor alpha (RXR-alpha), also known as NR2B1 is a nuclear receptor that in humans is encoded by the RXRA gene.

<span class="mw-page-title-main">KAT2A</span> Protein-coding gene in the species Homo sapiens

Histone acetyltransferase KAT2A is an enzyme that in humans is encoded by the KAT2A gene.

<span class="mw-page-title-main">CTBP1</span> Protein-coding gene in the species Homo sapiens

C-terminal-binding protein 1 also known as CtBP1 is a protein that in humans is encoded by the CTBP1 gene. CtBP1 is one of two CtBP proteins, the other protein being CtBP2.

<span class="mw-page-title-main">Myocyte-specific enhancer factor 2A</span> Protein-coding gene in the species Homo sapiens

Myocyte-specific enhancer factor 2A is a protein that in humans is encoded by the MEF2A gene. MEF2A is a transcription factor in the Mef2 family. In humans it is located on chromosome 15q26. Certain mutations in MEF2A cause an autosomal dominant form of coronary artery disease and myocardial infarction.

<span class="mw-page-title-main">CUTL1</span> Protein-coding gene in the species Homo sapiens

Cux1 is a homeodomain protein that in humans is encoded by the CUX1 gene.

<span class="mw-page-title-main">TAF9</span> Protein-coding gene in the species Homo sapiens

TAF9 RNA polymerase II, TATA box binding protein (TBP)-associated factor, 32kDa, also known as TAF9, is a protein that in humans is encoded by the TAF9 gene.

<span class="mw-page-title-main">TAF4</span> Protein-coding gene in the species Homo sapiens

Transcription initiation factor TFIID subunit 4 is a protein that in humans is encoded by the TAF4 gene.

<span class="mw-page-title-main">NCOA6</span> Protein-coding gene in the species Homo sapiens

Nuclear receptor coactivator 6 is a protein that in humans is encoded by the NCOA6 gene.

<span class="mw-page-title-main">CITED2</span> Protein-coding gene in humans

Cbp/p300-interacting transactivator 2 is a protein that in humans is encoded by the CITED2 gene.

<span class="mw-page-title-main">CITED1</span> Protein-coding gene in humans

Cbp/p300-interacting transactivator 1 is a protein that in humans is encoded by the CITED1 gene.

<span class="mw-page-title-main">TAF5L</span> Protein-coding gene in the species Homo sapiens

TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L is an enzyme that in humans is encoded by the TAF5L gene.

<span class="mw-page-title-main">TAZ zinc finger</span>

In molecular biology, TAZ zinc finger domains are zinc-containing domains found in the homologous transcriptional co-activators CREB-binding protein (CBP) and the P300. CBP and P300 are histone acetyltransferases that catalyse the reversible acetylation of all four histones in nucleosomes, acting to regulate transcription via chromatin remodelling. These large nuclear proteins interact with numerous transcription factors and viral oncoproteins, including p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1, and are involved in cell growth, differentiation and apoptosis. Both CBP and P300 have two copies of the TAZ domain, one in the N-terminal region, the other in the C-terminal region. The TAZ1 domain of CBP and P300 forms a complex with CITED2, inhibiting the activity of the hypoxia inducible factor (HIF-1alpha) and thereby attenuating the cellular response to low tissue oxygen concentration. Adaptation to hypoxia is mediated by transactivation of hypoxia-responsive genes by hypoxia-inducible factor-1 (HIF-1) in complex with the CBP and p300 transcriptional coactivators.

<span class="mw-page-title-main">KIX domain</span>

In biochemistry, the KIX domain (kinase-inducible domain (KID) interacting domain) or CREB binding domain is a protein domain of the eukaryotic transcriptional coactivators CBP and P300. It serves as a docking site for the formation of heterodimers between the coactivator and specific transcription factors. Structurally, the KIX domain is a globular domain consisting of three α-helices and two short 310-helices.

The transactivation domain or trans-activating domain (TAD) is a transcription factor scaffold domain which contains binding sites for other proteins such as transcription coregulators. These binding sites are frequently referred to as activation functions (AFs). TADs are named after their amino acid composition. These amino acids are either essential for the activity or simply the most abundant in the TAD. Transactivation by the Gal4 transcription factor is mediated by acidic amino acids, whereas hydrophobic residues in Gcn4 play a similar role. Hence, the TADs in Gal4 and Gcn4 are referred to as acidic or hydrophobic, respectively.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000100393 – Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000055024 – Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Eckner R, Ewen ME, Newsome D, Gerdes M, DeCaprio JA, Lawrence JB, Livingston DM (April 1994). "Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor". Genes Dev. 8 (8): 869–84. doi: 10.1101/gad.8.8.869 . PMID   7523245.
  6. ↑ Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y (1996). "The transcriptional coactivators p300 and CBP are histone acetyltransferases". Cell. 87 (5): 953–9. doi: 10.1016/S0092-8674(00)82001-2 . PMID   8945521.
  7. ↑ Ntranos A, Casaccia P (June 2016). "Bromodomains: Translating the words of lysine acetylation into myelin injury and repair". Neuroscience Letters. 625: 4–10. doi:10.1016/j.neulet.2015.10.015. PMC   4841751 . PMID   26472704.
  8. ↑ "Entrez Gene: EP300".
  9. ↑ Teufel DP, Freund SM, Bycroft M, Fersht AR (April 2007). "Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53". PNAS. 104 (17): 7009–7014. Bibcode:2007PNAS..104.7009T. doi: 10.1073/pnas.0702010104 . PMC   1855428 . PMID   17438265.; Piskacek S, Gregor M, Nemethova M, Grabner M, Kovarik P, Piskacek M (June 2007). "Nine-amino-acid transactivation domain: establishment and prediction utilities". Genomics. 89 (6): 756–68. doi: 10.1016/j.ygeno.2007.02.003 . PMID   17467953.
  10. ↑ Na SY, Choi JE, Kim HJ, Jhun BH, Lee YC, Lee JW (October 1999). "Bcl3, an IkappaB protein, stimulates activating protein-1 transactivation and cellular proliferation". J. Biol. Chem. 274 (40): 28491–6. doi: 10.1074/jbc.274.40.28491 . PMID   10497212.
  11. 1 2 Fan S, Ma YX, Wang C, Yuan RQ, Meng Q, Wang JA, Erdos M, Goldberg ID, Webb P, Kushner PJ, Pestell RG, Rosen EM (January 2002). "p300 Modulates the BRCA1 inhibition of estrogen receptor activity". Cancer Res. 62 (1): 141–51. PMID   11782371.
  12. ↑ Pao GM, Janknecht R, Ruffner H, Hunter T, Verma IM (February 2000). "CBP/p300 interact with and function as transcriptional coactivators of BRCA1". Proc. Natl. Acad. Sci. U.S.A. 97 (3): 1020–5. Bibcode:2000PNAS...97.1020P. doi: 10.1073/pnas.97.3.1020 . PMC   15508 . PMID   10655477.
  13. 1 2 Hussain MA, Habener JF (October 1999). "Glucagon gene transcription activation mediated by synergistic interactions of pax-6 and cdx-2 with the p300 co-activator". J. Biol. Chem. 274 (41): 28950–7. doi: 10.1074/jbc.274.41.28950 . PMID   10506141.
  14. ↑ Mink S, Haenig B, Klempnauer KH (November 1997). "Interaction and functional collaboration of p300 and C/EBPbeta". Mol. Cell. Biol. 17 (11): 6609–17. doi:10.1128/mcb.17.11.6609. PMC   232514 . PMID   9343424.
  15. ↑ Yahata T, de Caestecker MP, Lechleider RJ, Andriole S, Roberts AB, Isselbacher KJ, Shioda T (March 2000). "The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors". J. Biol. Chem. 275 (12): 8825–34. doi: 10.1074/jbc.275.12.8825 . PMID   10722728.
  16. ↑ Bhattacharya S, Michels CL, Leung MK, Arany ZP, Kung AL, Livingston DM (January 1999). "Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1". Genes Dev. 13 (1): 64–75. doi:10.1101/gad.13.1.64. PMC   316375 . PMID   9887100.
  17. 1 2 Bragança J, Eloranta JJ, Bamforth SD, Ibbitt JC, Hurst HC, Bhattacharya S (May 2003). "Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2". J. Biol. Chem. 278 (18): 16021–9. doi: 10.1074/jbc.M208144200 . PMID   12586840.
  18. ↑ Bragança J, Swingler T, Marques FI, Jones T, Eloranta JJ, Hurst HC, Shioda T, Bhattacharya S (March 2002). "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". J. Biol. Chem. 277 (10): 8559–65. doi: 10.1074/jbc.M110850200 . PMID   11744733.
  19. ↑ Glenn DJ, Maurer RA (December 1999). "MRG1 binds to the LIM domain of Lhx2 and may function as a coactivator to stimulate glycoprotein hormone alpha-subunit gene expression". J. Biol. Chem. 274 (51): 36159–67. doi: 10.1074/jbc.274.51.36159 . PMID   10593900.
  20. ↑ Rossow KL, Janknecht R (January 2003). "Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300". Oncogene. 22 (1): 151–6. doi: 10.1038/sj.onc.1206067 . PMID   12527917.
  21. ↑ Yamamoto N, Yamamoto S, Inagaki F, Kawaichi M, Fukamizu A, Kishi N, Matsuno K, Nakamura K, Weinmaster G, Okano H, Nakafuku M (November 2001). "Role of Deltex-1 as a transcriptional regulator downstream of the Notch receptor". J. Biol. Chem. 276 (48): 45031–40. doi: 10.1074/jbc.M105245200 . PMID   11564735.
  22. ↑ Miyake S, Sellers WR, Safran M, Li X, Zhao W, Grossman SR, Gan J, DeCaprio JA, Adams PD, Kaelin WG (December 2000). "Cells degrade a novel inhibitor of differentiation with E1A-like properties upon exiting the cell cycle". Mol. Cell. Biol. 20 (23): 8889–902. doi:10.1128/mcb.20.23.8889-8902.2000. PMC   86544 . PMID   11073989.
  23. ↑ MacLellan WR, Xiao G, Abdellatif M, Schneider MD (December 2000). "A novel Rb- and p300-binding protein inhibits transactivation by MyoD". Mol. Cell. Biol. 20 (23): 8903–15. doi:10.1128/mcb.20.23.8903-8915.2000. PMC   86545 . PMID   11073990.
  24. ↑ Li QJ, Yang SH, Maeda Y, Sladek FM, Sharrocks AD, Martins-Green M (January 2003). "MAP kinase phosphorylation-dependent activation of Elk-1 leads to activation of the co-activator p300". EMBO J. 22 (2): 281–91. doi:10.1093/emboj/cdg028. PMC   140103 . PMID   12514134.
  25. 1 2 Fajas L, Egler V, Reiter R, Hansen J, Kristiansen K, Debril MB, Miard S, Auwerx J (December 2002). "The retinoblastoma-histone deacetylase 3 complex inhibits PPARgamma and adipocyte differentiation". Dev. Cell. 3 (6): 903–10. doi: 10.1016/s1534-5807(02)00360-x . PMID   12479814.
  26. ↑ Kang YK, Guermah M, Yuan CX, Roeder RG (March 2002). "The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro". Proc. Natl. Acad. Sci. U.S.A. 99 (5): 2642–7. Bibcode:2002PNAS...99.2642K. doi: 10.1073/pnas.261715899 . PMC   122401 . PMID   11867769.
  27. ↑ Hasan S, Stucki M, Hassa PO, Imhof R, Gehrig P, Hunziker P, Hübscher U, Hottiger MO (June 2001). "Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300". Mol. Cell. 7 (6): 1221–31. doi: 10.1016/s1097-2765(01)00272-6 . PMID   11430825.
  28. ↑ Peng YC, Breiding DE, Sverdrup F, Richard J, Androphy EJ (July 2000). "AMF-1/Gps2 binds p300 and enhances its interaction with papillomavirus E2 proteins". J. Virol. 74 (13): 5872–9. doi:10.1128/jvi.74.13.5872-5879.2000. PMC   112082 . PMID   10846067.
  29. ↑ Lando D, Peet DJ, Whelan DA, Gorman JJ, Whitelaw ML (February 2002). "Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch". Science. 295 (5556): 858–61. Bibcode:2002Sci...295..858L. doi:10.1126/science.1068592. PMID   11823643. S2CID   24045310.
  30. ↑ Freedman SJ, Sun ZY, Poy F, Kung AL, Livingston DM, Wagner G, Eck MJ (April 2002). "Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha". Proc. Natl. Acad. Sci. U.S.A. 99 (8): 5367–72. Bibcode:2002PNAS...99.5367F. doi: 10.1073/pnas.082117899 . PMC   122775 . PMID   11959990.
  31. ↑ Ban N, Yamada Y, Someya Y, Miyawaki K, Ihara Y, Hosokawa M, Toyokuni S, Tsuda K, Seino Y (May 2002). "Hepatocyte nuclear factor-1alpha recruits the transcriptional co-activator p300 on the GLUT2 gene promoter". Diabetes. 51 (5): 1409–18. doi: 10.2337/diabetes.51.5.1409 . PMID   11978637.
  32. ↑ Martens JH, Verlaan M, Kalkhoven E, Dorsman JC, Zantema A (April 2002). "Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes". Mol. Cell. Biol. 22 (8): 2598–606. doi:10.1128/mcb.22.8.2598-2606.2002. PMC   133732 . PMID   11909954.
  33. 1 2 Shiseki M, Nagashima M, Pedeux RM, Kitahama-Shiseki M, Miura K, Okamura S, Onogi H, Higashimoto Y, Appella E, Yokota J, Harris CC (May 2003). "p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity". Cancer Res. 63 (10): 2373–8. PMID   12750254.
  34. ↑ Masumi A, Ozato K (June 2001). "Coactivator p300 acetylates the interferon regulatory factor-2 in U937 cells following phorbol ester treatment". J. Biol. Chem. 276 (24): 20973–80. doi: 10.1074/jbc.M101707200 . PMID   11304541.
  35. ↑ Hecht A, Stemmler MP (February 2003). "Identification of a promoter-specific transcriptional activation domain at the C terminus of the Wnt effector protein T-cell factor 4". J. Biol. Chem. 278 (6): 3776–85. doi: 10.1074/jbc.M210081200 . PMID   12446687.
  36. 1 2 Chen Q, Dowhan DH, Liang D, Moore DD, Overbeek PA (July 2002). "CREB-binding protein/p300 co-activation of crystallin gene expression". J. Biol. Chem. 277 (27): 24081–9. doi: 10.1074/jbc.M201821200 . PMID   11943779.
  37. ↑ Wallberg AE, Pedersen K, Lendahl U, Roeder RG (November 2002). "p300 and PCAF act cooperatively to mediate transcriptional activation from chromatin templates by notch intracellular domains in vitro". Mol. Cell. Biol. 22 (22): 7812–9. doi:10.1128/mcb.22.22.7812-7819.2002. PMC   134732 . PMID   12391150.
  38. ↑ Fryer CJ, Lamar E, Turbachova I, Kintner C, Jones KA (June 2002). "Mastermind mediates chromatin-specific transcription and turnover of the Notch enhancer complex". Genes Dev. 16 (11): 1397–411. doi:10.1101/gad.991602. PMC   186317 . PMID   12050117.
  39. 1 2 Sartorelli V, Huang J, Hamamori Y, Kedes L (February 1997). "Molecular mechanisms of myogenic coactivation by p300: direct interaction with the activation domain of MyoD and with the MADS box of MEF2C". Mol. Cell. Biol. 17 (2): 1010–26. doi:10.1128/mcb.17.2.1010. PMC   231826 . PMID   9001254.
  40. ↑ Youn HD, Grozinger CM, Liu JO (July 2000). "Calcium regulates transcriptional repression of myocyte enhancer factor 2 by histone deacetylase 4". J. Biol. Chem. 275 (29): 22563–7. doi: 10.1074/jbc.C000304200 . PMID   10825153.
  41. ↑ Youn HD, Liu JO (July 2000). "Cabin1 represses MEF2-dependent Nur77 expression and T cell apoptosis by controlling association of histone deacetylases and acetylases with MEF2". Immunity. 13 (1): 85–94. doi: 10.1016/s1074-7613(00)00010-8 . PMID   10933397.
  42. ↑ Johnson LR, Johnson TK, Desler M, Luster TA, Nowling T, Lewis RE, Rizzino A (February 2002). "Effects of B-Myb on gene transcription: phosphorylation-dependent activity and acetylation by p300". J. Biol. Chem. 277 (6): 4088–97. doi: 10.1074/jbc.M105112200 . PMID   11733503.
  43. 1 2 Grossman SR, Perez M, Kung AL, Joseph M, Mansur C, Xiao ZX, Kumar S, Howley PM, Livingston DM (October 1998). "p300/MDM2 complexes participate in MDM2-mediated p53 degradation". Mol. Cell. 2 (4): 405–15. doi: 10.1016/s1097-2765(00)80140-9 . PMID   9809062.
  44. 1 2 Lau P, Bailey P, Dowhan DH, Muscat GE (January 1999). "Exogenous expression of a dominant negative RORalpha1 vector in muscle cells impairs differentiation: RORalpha1 directly interacts with p300 and myoD". Nucleic Acids Res. 27 (2): 411–20. doi:10.1093/nar/27.2.411. PMC   148194 . PMID   9862959.
  45. 1 2 De Luca A, Severino A, De Paolis P, Cottone G, De Luca L, De Falco M, Porcellini A, Volpe M, Condorelli G (February 2003). "p300/cAMP-response-element-binding-protein ('CREB')-binding protein (CBP) modulates co-operation between myocyte enhancer factor 2A (MEF2A) and thyroid hormone receptor-retinoid X receptor". Biochem. J. 369 (Pt 3): 477–84. doi:10.1042/BJ20020057. PMC   1223100 . PMID   12371907.
  46. ↑ Ko L, Cardona GR, Chin WW (May 2000). "Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator". Proc. Natl. Acad. Sci. U.S.A. 97 (11): 6212–7. Bibcode:2000PNAS...97.6212K. doi: 10.1073/pnas.97.11.6212 . PMC   18584 . PMID   10823961.
  47. ↑ García-Rodríguez C, Rao A (June 1998). "Nuclear factor of activated T cells (NFAT)-dependent transactivation regulated by the coactivators p300/CREB-binding protein (CBP)". J. Exp. Med. 187 (12): 2031–6. doi:10.1084/jem.187.12.2031. PMC   2212364 . PMID   9625762.
  48. ↑ Curtis AM, Seo SB, Westgate EJ, Rudic RD, Smyth EM, Chakravarti D, FitzGerald GA, McNamara P (February 2004). "Histone acetyltransferase-dependent chromatin remodeling and the vascular clock". J. Biol. Chem. 279 (8): 7091–7. doi: 10.1074/jbc.M311973200 . PMID   14645221.
  49. ↑ Avantaggiati ML, Ogryzko V, Gardner K, Giordano A, Levine AS, Kelly K (1997). "Recruitment of p300/CBP in p53-dependent signal pathways". Cell. 89 (7): 1175–84. doi: 10.1016/s0092-8674(00)80304-9 . PMID   9215639. S2CID   14375605.
  50. ↑ An W, Kim J, Roeder RG (June 2004). "Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53". Cell. 117 (6): 735–48. doi: 10.1016/j.cell.2004.05.009 . PMID   15186775.
  51. ↑ Pastorcic M, Das HK (November 2000). "Regulation of transcription of the human presenilin-1 gene by ets transcription factors and the p53 protooncogene". J. Biol. Chem. 275 (45): 34938–45. doi: 10.1074/jbc.M005411200 . PMID   10942770.
  52. ↑ Livengood JA, Scoggin KE, Van Orden K, McBryant SJ, Edayathumangalam RS, Laybourn PJ, Nyborg JK (March 2002). "p53 Transcriptional activity is mediated through the SRC1-interacting domain of CBP/p300". J. Biol. Chem. 277 (11): 9054–61. doi: 10.1074/jbc.M108870200 . PMID   11782467.
  53. ↑ Hasan S, Hassa PO, Imhof R, Hottiger MO (March 2001). "Transcription coactivator p300 binds PCNA and may have a role in DNA repair synthesis". Nature. 410 (6826): 387–91. Bibcode:2001Natur.410..387H. doi:10.1038/35066610. PMID   11268218. S2CID   2129847.
  54. ↑ Subramanian C, Hasan S, Rowe M, Hottiger M, Orre R, Robertson ES (May 2002). "Epstein-Barr virus nuclear antigen 3C and prothymosin alpha interact with the p300 transcriptional coactivator at the CH1 and CH3/HAT domains and cooperate in regulation of transcription and histone acetylation". J. Virol. 76 (10): 4699–708. doi:10.1128/jvi.76.10.4699-4708.2002. PMC   136123 . PMID   11967287.
  55. ↑ Dowell P, Ishmael JE, Avram D, Peterson VJ, Nevrivy DJ, Leid M (December 1997). "p300 functions as a coactivator for the peroxisome proliferator-activated receptor alpha". J. Biol. Chem. 272 (52): 33435–43. doi: 10.1074/jbc.272.52.33435 . PMID   9407140.
  56. ↑ Dowell P, Ishmael JE, Avram D, Peterson VJ, Nevrivy DJ, Leid M (May 1999). "Identification of nuclear receptor corepressor as a peroxisome proliferator-activated receptor alpha interacting protein". J. Biol. Chem. 274 (22): 15901–7. doi: 10.1074/jbc.274.22.15901 . PMID   10336495.
  57. ↑ Kiernan R, Brès V, Ng RW, Coudart MP, El Messaoudi S, Sardet C, Jin DY, Emiliani S, Benkirane M (January 2003). "Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65". J. Biol. Chem. 278 (4): 2758–66. doi: 10.1074/jbc.M209572200 . PMID   12419806.
  58. ↑ Gerritsen ME, Williams AJ, Neish AS, Moore S, Shi Y, Collins T (April 1997). "CREB-binding protein/p300 are transcriptional coactivators of p65". Proc. Natl. Acad. Sci. U.S.A. 94 (7): 2927–32. Bibcode:1997PNAS...94.2927G. doi: 10.1073/pnas.94.7.2927 . PMC   20299 . PMID   9096323.
  59. ↑ Pearson KL, Hunter T, Janknecht R (December 1999). "Activation of Smad1-mediated transcription by p300/CBP". Biochim. Biophys. Acta. 1489 (2–3): 354–64. doi:10.1016/S0167-4781(99)00166-9. PMID   10673036.
  60. 1 2 Nakashima K, Yanagisawa M, Arakawa H, Kimura N, Hisatsune T, Kawabata M, Miyazono K, Taga T (April 1999). "Synergistic signaling in fetal brain by STAT3-Smad1 complex bridged by p300". Science. 284 (5413): 479–82. Bibcode:1999Sci...284..479N. doi:10.1126/science.284.5413.479. PMID   10205054.
  61. ↑ Wotton D, Lo RS, Lee S, Massagué J (April 1999). "A Smad transcriptional corepressor". Cell. 97 (1): 29–39. doi: 10.1016/S0092-8674(00)80712-6 . PMID   10199400.
  62. ↑ Pessah M, Prunier C, Marais J, Ferrand N, Mazars A, Lallemand F, Gauthier JM, Atfi A (May 2001). "c-Jun interacts with the corepressor TG-interacting factor (TGIF) to suppress Smad2 transcriptional activity". Proc. Natl. Acad. Sci. U.S.A. 98 (11): 6198–203. Bibcode:2001PNAS...98.6198P. doi: 10.1073/pnas.101579798 . PMC   33445 . PMID   11371641.
  63. ↑ Grönroos E, Hellman U, Heldin CH, Ericsson J (September 2002). "Control of Smad7 stability by competition between acetylation and ubiquitination". Mol. Cell. 10 (3): 483–93. doi: 10.1016/s1097-2765(02)00639-1 . PMID   12408818.
  64. ↑ Kim RH, Wang D, Tsang M, Martin J, Huff C, de Caestecker MP, Parks WT, Meng X, Lechleider RJ, Wang T, Roberts AB (July 2000). "A novel smad nuclear interacting protein, SNIP1, suppresses p300-dependent TGF-beta signal transduction". Genes Dev. 14 (13): 1605–16. doi:10.1101/gad.14.13.1605. PMC   316742 . PMID   10887155.
  65. ↑ Eid JE, Kung AL, Scully R, Livingston DM (September 2000). "p300 interacts with the nuclear proto-oncoprotein SYT as part of the active control of cell adhesion". Cell. 102 (6): 839–48. doi: 10.1016/s0092-8674(00)00072-6 . PMID   11030627.
  66. ↑ McDonald C, Reich NC (July 1999). "Cooperation of the transcriptional coactivators CBP and p300 with Stat6". J. Interferon Cytokine Res. 19 (7): 711–22. doi:10.1089/107999099313550. PMID   10454341.
  67. ↑ Huang S, Qiu Y, Stein RW, Brandt SJ (September 1999). "p300 functions as a transcriptional coactivator for the TAL1/SCL oncoprotein". Oncogene. 18 (35): 4958–67. doi: 10.1038/sj.onc.1202889 . PMID   10490830.
  68. ↑ Bradney C, Hjelmeland M, Komatsu Y, Yoshida M, Yao TP, Zhuang Y (January 2003). "Regulation of E2A activities by histone acetyltransferases in B lymphocyte development". J. Biol. Chem. 278 (4): 2370–6. doi: 10.1074/jbc.M211464200 . PMID   12435739.
  69. ↑ Misra P, Qi C, Yu S, Shah SH, Cao WQ, Rao MS, Thimmapaya B, Zhu Y, Reddy JK (May 2002). "Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation". J. Biol. Chem. 277 (22): 20011–9. doi: 10.1074/jbc.M201739200 . PMID   11912212.
  70. ↑ Gizard F, Lavallée B, DeWitte F, Hum DW (September 2001). "A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression". J. Biol. Chem. 276 (36): 33881–92. doi: 10.1074/jbc.M100113200 . PMID   11349124.
  71. ↑ Sun Z, Pan J, Hope WX, Cohen SN, Balk SP (August 1999). "Tumor susceptibility gene 101 protein represses androgen receptor transactivation and interacts with p300". Cancer. 86 (4): 689–96. doi: 10.1002/(sici)1097-0142(19990815)86:4<689::aid-cncr19>3.0.co;2-p . PMID   10440698. S2CID   26971556.
  72. ↑ Hamamori Y, Sartorelli V, Ogryzko V, Puri PL, Wu HY, Wang JY, Nakatani Y, Kedes L (February 1999). "Regulation of histone acetyltransferases p300 and PCAF by the bHLH protein twist and adenoviral oncoprotein E1A". Cell. 96 (3): 405–13. doi: 10.1016/S0092-8674(00)80553-X . PMID   10025406.
  73. ↑ Yao YL, Yang WM, Seto E (September 2001). "Regulation of transcription factor YY1 by acetylation and deacetylation". Mol. Cell. Biol. 21 (17): 5979–91. doi:10.1128/mcb.21.17.5979-5991.2001. PMC   87316 . PMID   11486036.
  74. ↑ Lee JS, Galvin KM, See RH, Eckner R, Livingston D, Moran E, Shi Y (May 1995). "Relief of YY1 transcriptional repression by adenovirus E1A is mediated by E1A-associated protein p300". Genes Dev. 9 (10): 1188–98. doi: 10.1101/gad.9.10.1188 . PMID   7758944.
  75. ↑ Silverman ES, Du J, Williams AJ, Wadgaonkar R, Drazen JM, Collins T (November 1998). "cAMP-response-element-binding-protein-binding protein (CBP) and p300 are transcriptional co-activators of early growth response factor-1 (Egr-1)". Biochem. J. 336 (1): 183–9. doi:10.1042/bj3360183. PMC   1219856 . PMID   9806899.

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