General information | DisProt: | DP00633 | Name: | Histone acetyltransferase p300 | Synonym(s): | EP300_HUMAN
EC=2.3.1.48
p300 HAT
E1A-associated protein p300
| First appeared in release: | Release 5.2 (08/07/2010) | UniProt: | Q09472 | UniGene: | Hs.517517 | SwissProt: | EP300_HUMAN | TrEMBL: | | NCBI (GI): | 223590203 | Source organism: | Homo sapiens (Human) | Sequence length: | 2414 | Percent disordered: | 7% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD - 60 INQLQTSLGM VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQVMASQAQQ SSPGLGLINS - 120 MVKSPMTQAG LTSPNMGMGT SGPNQGPTQS TGMMNSPVNQ PAMGMNTGMN AGMNPGMLAA - 180 GNGQGIMPNQ VMNGSIGAGR GRQNMQYPNP GMGSAGNLLT EPLQQGSPQM GGQTGLRGPQ - 240 PLKMGMMNNP NPYGSPYTQN PGQQIGASGL GLQIQTKTVL SNNLSPFAMD KKAVPGGGMP - 300 NMGQQPAPQV QQPGLVTPVA QGMGSGAHTA DPEKRKLIQQ QLVLLLHAHK CQRREQANGE - 360 VRQCNLPHCR TMKNVLNHMT HCQSGKSCQV AHCASSRQII SHWKNCTRHD CPVCLPLKNA - 420 GDKRNQQPIL TGAPVGLGNP SSLGVGQQSA PNLSTVSQID PSSIERAYAA LGLPYQVNQM - 480 PTQPQVQAKN QQNQQPGQSP QGMRPMSNMS ASPMGVNGGV GVQTPSLLSD SMLHSAINSQ - 540 NPMMSENASV PSLGPMPTAA QPSTTGIRKQ WHEDITQDLR NHLVHKLVQA IFPTPDPAAL - 600 KDRRMENLVA YARKVEGDMY ESANNRAEYY HLLAEKIYKI QKELEEKRRT RLQKQNMLPN - 660 AAGMVPVSMN PGPNMGQPQP GMTSNGPLPD PSMIRGSVPN QMMPRITPQS GLNQFGQMSM - 720 AQPPIVPRQT PPLQHHGQLA QPGALNPPMG YGPRMQQPSN QGQFLPQTQF PSQGMNVTNI - 780 PLAPSSGQAP VSQAQMSSSS CPVNSPIMPP GSQGSHIHCP QLPQPALHQN SPSPVPSRTP - 840 TPHHTPPSIG AQQPPATTIP APVPTPPAMP PGPQSQALHP PPRQTPTPPT TQLPQQVQPS - 900 LPAAPSADQP QQQPRSQQST AASVPTPTAP LLPPQPATPL SQPAVSIEGQ VSNPPSTSST - 960 EVNSQAIAEK QPSQEVKMEA KMEVDQPEPA DTQPEDISES KVEDCKMEST ETEERSTELK - 1020 TEIKEEEDQP STSATQSSPA PGQSKKKIFK PEELRQALMP TLEALYRQDP ESLPFRQPVD - 1080 PQLLGIPDYF DIVKSPMDLS TIKRKLDTGQ YQEPWQYVDD IWLMFNNAWL YNRKTSRVYK - 1140 YCSKLSEVFE QEIDPVMQSL GYCCGRKLEF SPQTLCCYGK QLCTIPRDAT YYSYQNRYHF - 1200 CEKCFNEIQG ESVSLGDDPS QPQTTINKEQ FSKRKNDTLD PELFVECTEC GRKMHQICVL - 1260 HHEIIWPAGF VCDGCLKKSA RTRKENKFSA KRLPSTRLGT FLENRVNDFL RRQNHPESGE - 1320 VTVRVVHASD KTVEVKPGMK ARFVDSGEMA ESFPYRTKAL FAFEEIDGVD LCFFGMHVQE - 1380 YGSDCPPPNQ RRVYISYLDS VHFFRPKCLR TAVYHEILIG YLEYVKKLGY TTGHIWACPP - 1440 SEGDDYIFHC HPPDQKIPKP KRLQEWYKKM LDKAVSERIV HDYKDIFKQA TEDRLTSAKE - 1500 LPYFEGDFWP NVLEESIKEL EQEEEERKRE ENTSNESTDV TKGDSKNAKK KNNKKTSKNK - 1560 SSLSRGNKKK PGMPNVSNDL SQKLYATMEK HKEVFFVIRL IAGPAANSLP PIVDPDPLIP - 1620 CDLMDGRDAF LTLARDKHLE FSSLRRAQWS TMCMLVELHT QSQDRFVYTC NECKHHVETR - 1680 WHCTVCEDYD LCITCYNTKN HDHKMEKLGL GLDDESNNQQ AAATQSPGDS RRLSIQRCIQ - 1740 SLVHACQCRN ANCSLPSCQK MKRVVQHTKG CKRKTNGGCP ICKQLIALCC YHAKHCQENK - 1800 CPVPFCLNIK QKLRQQQLQH RLQQAQMLRR RMASMQRTGV VGQQQGLPSP TPATPTTPTG - 1860 QQPTTPQTPQ PTSQPQPTPP NSMPPYLPRT QAAGPVSQGK AAGQVTPPTP PQTAQPPLPG - 1920 PPPAAVEMAM QIQRAAETQR QMAHVQIFQR PIQHQMPPMT PMAPMGMNPP PMTRGPSGHL - 1980 EPGMGPTGMQ QQPPWSQGGL PQPQQLQSGM PRPAMMSVAQ HGQPLNMAPQ PGLGQVGISP - 2040 LKPGTVSQQA LQNLLRTLRS PSSPLQQQQV LSILHANPQL LAAFIKQRAA KYANSNPQPI - 2100 PGQPGMPQGQ PGLQPPTMPG QQGVHSNPAM QNMNPMQAGV QRAGLPQQQP QQQLQPPMGG - 2160 MSPQAQQMNM NHNTMPSQFR DILRRQQMMQ QQQQQGAGPG IGPGMANHNQ FQQPQGVGYP - 2220 PQQQQRMQHH MQQMQQGNMG QIGQLPQALG AEAGASLQAY QQRLLQQQMG SPVQPNPMSP - 2280 QQHMLPNQAQ SPHLQGQQIP NSLSNQVRSP QPVPSPRPQS QPPHSSPSPR MQPQPSPHHV - 2340 SPQTSSPHPG LVAAQANPME QGHFASPDQN SMLSQLASNP GMANLHGASA TDLGLSTDNS - 2400 DLNSNLSQST LDIH
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Functional narrative |
Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes.
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Map of ordered and disordered regions |
![](regions/DP00633.gif)
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Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | IBiD Homology Domain (IHD) | Location: | 401 - 566 | Length: | 166 | Region sequence: |
SHWKNCTRHDCPVCLPLKNAGDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQID PSSIERAYAALGLPYQVNQMPTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGV GVQTPSLLSDSMLHSAINSQNPMMSENASVPSLGPMPTAAQPSTTG | Modification type: | Engineered
Fragment
| PDB: | | Structural/functional type: | Relationship to function unknown | Functional classes: | Unknown
| Functional subclasses: | Transactivation (transcriptional activation)
| Detection methods:
- Nuclear magnetic resonance (NMR) (293 K; 2H20 (buffer) 10 %; DTT (buffer, at pH 6.8) 5 mM; Mes (buffer) 50 mM; NaCl (buffer) 100 mM; p300 IHD (bound to p53 peptide (aa 1-93)) 180 uM)
- Fluorescence polarization/anisotropy (296 K; DTT (titration buffer, at pH 6.8) 5 mM; Mes (titration buffer) 50 mM; NaCl (titration buffer) 100 mM; p300 IHD (varying concentrations of 10-600uM); p53 peptide (aa 1-93) 0.5 uM)
| References:
- Teufel DP, Freund SM, Bycroft M, Fersht AR. "Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53." Proc Natl Acad Sci U S A. 2007; 104(17): 7009-14. PubMed: 17438265
| Comments:
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References |
- Teufel DP, Freund SM, Bycroft M, Fersht AR. "Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53." Proc Natl Acad Sci U S A. 2007; 104(17): 7009-14. PubMed: 17438265
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Comments |
Av (7-28-2010) PubMed: 17438265
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