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EP300

Histon-acetiltransferaza p300, znana i kao p300 HAT ili E1A-vezani protein p300 (gdje je E1A = adenovirusna rana regija 1A) također poznat kao i kao EP300 ili p300, jest enzim koji je kod ljudi kodiran genom EP300 sa hromosoma 22.[5] Funkcioniše kao histon-acetiltransferaza koja reguliše transkripciju gena putem remodeliranja hromatina, dozvoljavajući histonskim proteinima da manje čvrsto omotaju DNK. Ovaj enzim ima esencijalnu ulogu u regulaciji ćelijskog rasta i diobe, podstičući ćelije da sazrijevaju i preuzmu specijalizirane funkcije (diferencijacije), te sprječavaju rast kancerogenih tumora. Čini se da je protein p300 kritičan za normalan razvoj prije i nakon rođenja.

EP300
Dostupne strukture
PDBPretraga ortologa: PDBe RCSB
Spisak PDB ID kodova

1L3E, 1P4Q, 2K8F, 2MH0, 2MZD, 3BIY, 3I3J, 3IO2, 3P57, 3T92, 4BHW, 4PZR, 4PZS, 4PZT, 5BT3

Identifikatori
AliasiEP300
Vanjski ID-jeviOMIM: 602700 MGI: 1276116 HomoloGene: 1094 GeneCards: EP300
Lokacija gena (čovjek)
Hromosom 22 (čovjek)
Hrom.Hromosom 22 (čovjek)[1]
Hromosom 22 (čovjek)
Genomska lokacija za EP300
Genomska lokacija za EP300
Bend22q13.2Početak41,092,592 bp[1]
Kraj41,180,077 bp[1]
Lokacija gena (miš)
Hromosom 15 (miš)
Hrom.Hromosom 15 (miš)[2]
Hromosom 15 (miš)
Genomska lokacija za EP300
Genomska lokacija za EP300
Bend15|15 E1Početak81,469,552 bp[2]
Kraj81,536,278 bp[2]
Obrazac RNK ekspresije


Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija• protein C-terminus binding
• transcription factor binding
• GO:0001104 transcription coregulator activity
• vezivanje iona metala
• acyltransferase activity
• aktivnost sa transferazom
• beta-catenin binding
• pre-mRNA intronic binding
• vezivanje iona cinka
• chromatin binding
• oštećeno vezivanje sa DNK
• GO:0001948, GO:0016582 vezivanje za proteine
• acetyltransferase activity
• vezivanje sa DNK
• GO:0001077, GO:0001212, GO:0001213, GO:0001211, GO:0001205 DNA-binding transcription activator activity, RNA polymerase II-specific
• GO:0001105 transcription coactivator activity
• p53 binding
• androgen receptor binding
• chromatin DNA binding
• histone acetyltransferase activity
• lysine N-acetyltransferase activity, acting on acetyl phosphate as donor
• peptide N-acetyltransferase activity
• peptide-lysine-N-acetyltransferase activity
• protein propionyltransferase activity
• STAT family protein binding
• peptide butyryltransferase activity
• histone crotonyltransferase activity
• histone butyryltransferase activity
• GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding
Ćelijska komponenta• jedro
• histone acetyltransferase complex
• transcription regulator complex
• nukleoplazma
• citoplazma
• citosol
• hromosom
Biološki proces• somitogenesis
• rhythmic process
• transcription by RNA polymerase II
• histone H2B acetylation
• animal organ morphogenesis
• ćelijski ciklus
• B cell differentiation
• GO:0097285 apoptoza
• GO:0009373 regulation of transcription, DNA-templated
• lung development
• N-terminal peptidyl-lysine acetylation
• platelet formation
• stimulatory C-type lectin receptor signaling pathway
• transcription, DNA-templated
• GO:0060469, GO:0009371 positive regulation of transcription, DNA-templated
• heart development
• regulation of transcription from RNA polymerase II promoter in response to hypoxia
• GO:0022415 viral process
• protein acetylation
• Notch signaling pathway
• cellular response to UV
• protein stabilization
• positive regulation of DNA-binding transcription factor activity
• GO:1901227 negative regulation of transcription by RNA polymerase II
• nervous system development
• regulation of autophagy
• regulation of androgen receptor signaling pathway
• positive regulation of protein binding
• positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response
• fat cell differentiation
• positive regulation by host of viral transcription
• megakaryocyte development
• intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator
• internal protein amino acid acetylation
• regulation of cell cycle
• regulation of tubulin deacetylation
• GO:1901313 positive regulation of gene expression
• histone H4 acetylation
• regulation of cellular response to heat
• transcription-coupled nucleotide-excision repair
• skeletal muscle tissue development
• positive regulation of type I interferon production
• response to estrogen
• response to hypoxia
• regulation of signal transduction by p53 class mediator
• internal peptidyl-lysine acetylation
• beta-catenin-TCF complex assembly
• DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest
• macrophage derived foam cell differentiation
• Jednodnevni biološki ritam
• protein deubiquitination
• GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II
• protein destabilization
• regulation of megakaryocyte differentiation
• histone acetylation
• epigenetic maintenance of chromatin in transcription-competent conformation
• peptidyl-lysine propionylation
• peptidyl-lysine crotonylation
• peptidyl-lysine butyrylation
Izvori:Amigo / QuickGO
Ortolozi
VrsteČovjekMiš
Entrez

2033

328572

Ensembl

ENSG00000100393

ENSMUSG00000055024

UniProt

Q09472

B2RWS6

RefSeq (mRNK)

NM_001429
NM_001362843

NM_177821

RefSeq (bjelančevina)

NP_001420
NP_001349772

NP_808489

Lokacija (UCSC)Chr 22: 41.09 – 41.18 MbChr 15: 81.47 – 81.54 Mb
PubMed pretraga[3][4]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/uredi – miš

Gen EP300 se nalazi na dugom (q) kraku ljudskog hromosoma 22 na poziciji 13.2. Ovaj gen kodira adenovirusni E1A povezan sa ćelijskim p300 transkripcijskim koaktivatorskim proteinom.

EP300 je blisko povezan sa drugim genom, CREB vezujući protein, koji se nalazi na ljudskom hromosomu 16.

Aminokiselinska sekvenca

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Dužina polipeptidnog lanca je 2.414 aminokiselina, a molekulska težina 264.161 Da.

1020304050
MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINS
TELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGP
GQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTSGPNQGPTQS
TGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGR
GRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGMMNNP
NPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMP
NMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHK
CQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQII
SHWKNCTRHDCPVCLPLKNAGDKRNQQPILTGAPVGLGNPSSLGVGQQSA
PNLSTVSQIDPSSIERAYAALGLPYQVNQMPTQPQVQAKNQQNQQPGQSP
QGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQNPMMSENASV
PSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAAL
KDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRT
RLQKQNMLPNAAGMVPVSMNPGPNMGQPQPGMTSNGPLPDPSMIRGSVPN
QMMPRITPQSGLNQFGQMSMAQPPIVPRQTPPLQHHGQLAQPGALNPPMG
YGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSS
CPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPHHTPPSIG
AQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPS
LPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQ
VSNPPSTSSTEVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISES
KVEDCKMESTETEERSTELKTEIKEEEDQPSTSATQSSPAPGQSKKKIFK
PEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLS
TIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFE
QEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHF
CEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTEC
GRKMHQICVLHHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGT
FLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMA
ESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDS
VHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHC
HPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKE
LPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKK
KNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRL
IAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWS
TMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKN
HDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRN
ANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENK
CPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSP
TPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGK
AAGQVTPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQR
PIQHQMPPMTPMAPMGMNPPPMTRGPSGHLEPGMGPTGMQQQPPWSQGGL
PQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISPLKPGTVSQQA
LQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPI
PGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQP
QQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPG
IGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMGQIGQLPQALG
AEAGASLQAYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIP
NSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPG
LVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNS
DLNSNLSQSTLDIH

Funkcija

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p300 HAT funkcionira kao histon-acetiltransferaza[6] koji regulira transkripciju putem remodeliranja hromatina i važan je u procesima proliferacije i diferencijacije ćelija. Posreduje u regulaciji cAMP-gena, tako što se specifično vezuje za fosforilizirani CREB protein.

p300 HAT sadrži bromodomain koji je uključen u IL6 signalizaciju.[7]:3.1

Ovaj gen je također identificiran kao koaktivator HIF1A (faktor 1 alfa induciran hipoksijom), te stoga ima ulogu u stimulaciji gena izazvanih hipoksijom, kao što je VEGF.[8]

Mehanizam

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Protein p300 obavlja svoju funkciju aktivacije transkripcije vezivanjem za transkripcijski faktor i transkripcijski mehanizam. Na osnovu ove funkcije, p300 se naziva transkripcijski koaktivator. Interakcijom p300 sa faktorima transkripcije upravlja jedan ili više p300 domena: jedarni receptorski domen interakcije (RID), KIX domen (CREB i MYB domen interakcije), cistein/histidin regije (TAZ1/CH1 i TAZ2/CH3) i interferonski domen za vezivanje odgovora (IBiD). Posljednja četiri domena, KIX, TAZ1, TAZ2 i IBiD od p300, svaki se čvrsto vezuje za sekvencu koja obuhvata oba trasaltivacijska domena 9aaTAD faktora transkripcije p53.[9]

Klinički značaj

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Mutacije u genu EP300 odgovorne su za mali procent slučajeva Rubinstein-Taybijevog sindroma. Ove mutacije rezultiraju gubitkom jedne kopije gena u svakoj ćeliji, što smanjuje količinu p300 proteina za polovinu. Neke mutacije dovode do proizvodnje vrlo kratke, nefunkcionalne verzije proteina p300, dok druge sprječavaju da jedna kopija gena uopće napravi bilo koji protein. Iako se ne zna kako smanjenje količine p300 proteina dovodi do specifičnih karakteristika Rubinstein-Taybijevog sindroma, jasno je da gubitak jedne kopije gena EP300 remeti normalan razvoj.

Preuređenje hromosoma koji uključuje hromosom 22 rijetko je povezano s određenim tipovima raka. Ova preuređivanja, zvana translokacije, remete regiju hromosoma 22 koji sadrži gen EP300. Naprimjer, nađena je translokaciju između hromosoma 8 i 22 kod nekoliko ljudi s rakom krvnih ćelija pod nazivom akutna mijeloidna leukemija (AML). Još jedna translokacija, koja uključuje hromosome 11 i 22, pronađena je kod malog broja ljudi koji su bili podvrgnuti liječenju raka. Ova hromosomska promjena povezana je s razvojem AML-a nakon hemoterapija za druge oblike raka.

Mutacije u genu EP300 identificirane su u nekoliko drugih tipova raka. Ove mutacije su somatske, što znači da se stiču tokom života osobe i prisutne su samo u određenim ćelijama. Somatske mutacije u genu EP300 pronađene su u malom broju solidnih tumora, uključujući karcinom debelog crijeva i rektuma, želuca, dojke i [ [rak gušterače|gušterače]]. Studije sugeriraju da mutacije EP300 također mogu imati ulogu u razvoju nekih karcinoma prostate i mogu pomoći u predviđanju da li će se ovi tumori povećati dimenzije ili proširiti na druge dijelove tijela. U ćelijama raka, mutacije EP300 sprečavaju gen da proizvodi bilo koji funkcionalni protein. Bez p300, ćelije ne mogu efikasno obuzdati rast i podjelu, što može omogućiti nastanak kanceroznih tumora.

Interakcije

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Pokazalo se da EP300 reaguje sa:

Reference

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000100393 - Ensembl, maj 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000055024 - Ensembl, maj 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. ^ a b 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. ^ a b 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. ^ a b 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. ^ a b 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. ^ a b 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. ^ a b 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. ^ a b 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. ^ a b 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. ^ a b 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. ^ a b 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. ^ Kodera Y, Takeyama K, Murayama A, Suzawa M, Masuhiro Y, Kato S (October 2000). "Ligand type-specific interactions of peroxisome proliferator-activated receptor gamma with transcriptional coactivators". J. Biol. Chem. 275 (43): 33201–4. doi:10.1074/jbc.C000517200. PMID 10944516.
  58. ^ 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.
  59. ^ 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.
  60. ^ 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.
  61. ^ a b 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.
  62. ^ 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.
  63. ^ 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.
  64. ^ 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.
  65. ^ 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.
  66. ^ 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.
  67. ^ 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.
  68. ^ 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.
  69. ^ 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.
  70. ^ 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.
  71. ^ 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.
  72. ^ 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.
  73. ^ 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.
  74. ^ 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.
  75. ^ 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.
  76. ^ 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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Ovaj članak uključuje tekst iz Nacionalne medicinske biblioteke Sjedinjenih Država, koji je u javnom vlasništvu.

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