Difference between revisions of "Histone acetyltransferase p300"

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{{#invoke:InfoboxforTarget|run|EP300, p300 HAT|[https://www.uniprot.org/uniprot/Q09472 Q09472]|Homo sapiens|Cys1438|[http://pfam.xfam.org/family/PF08214 Histone acetylation protein]|[[:Category:Histone acetyltransferase p300|Ligand list]]|Post-translational Modification}}
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{{#invoke:InfoboxforTarget|run|EP300, p300 HAT|[https://www.uniprot.org/uniprot/Q09472 Q09472]|Homo sapiens|Cys1438|[http://pfam.xfam.org/family/PF08214 Histone acetylation protein]|[[:Category:Histone acetyltransferase p300|Ligand list]]|Post-translational Modification, Transcription Related}}
  
 
==Summary==
 
==Summary==
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==Reference==
 
==Reference==
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# Pereira S R, Vasconcelos V M, Antunes A. '''Computational study of the covalent bonding of microcystins to cysteine residues–a reaction involved in the inhibition of the PPP family of protein phosphatases[J].''' The FEBS journal, 2013, 280(2): 674-680. [https://www.ncbi.nlm.nih.gov/pubmed/?term=22177231 22177231]<br/>  
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# Ravindra K C, Narayan V, Lushington G H, et al. '''Targeting of Histone Acetyltransferase p300 by Cyclopentenone Prostaglandin Δ<sup>12</sup>-PGJ<sub>2</sub> through Covalent Binding to Cys1438[J].''' Chemical research in toxicology, 2011, 25(2): 337-347. [https://www.ncbi.nlm.nih.gov/pubmed/?term=22141352 22141352]<br/>
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# MacKintosh R W, Dalby K N, Campbell D G, et al. '''The cyanobacterial toxin microcystin binds covalently to cysteine-273 on protein phosphatase 1[J].''' Febs Letters, 1995, 371(3): 236-240. [https://www.ncbi.nlm.nih.gov/pubmed/?term=7556599 7556599]<br/>
 
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# Hastie C J, Borthwick E B, Morrison L F, et al. '''Inhibition of several protein phosphatases by a non-covalently interacting microcystin and a novel cyanobacterial peptide, nostocyclin[J].''' Biochimica et Biophysica Acta (BBA)-General Subjects, 2005, 1726(2): 187-193. [https://www.ncbi.nlm.nih.gov/pubmed/?term=16046071 16046071]<br/>
 
  
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[[Category:Targets|Targets]]
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[[Category:Targets]]
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[[Category:Homo sapiens|Homo sapiens]]
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[[Category:Homo sapiens]]
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[[Category:Post-translational Modification|Post-translational Modification]]
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[[Category:Post-translational Modification]]
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[[Category:Histone acetylation protein|Histone acetylation protein]]
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[[Category:Transcription Related]]
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[[Category:cAMP signaling pathway|cAMP signaling pathway]]
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[[Category:Histone acetylation protein]]
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[[Category:HIF-1 signaling pathway|HIF-1 signaling pathway]]
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Latest revision as of 23:01, 19 August 2019

Basic Information
Short Name EP300, p300 HAT
UNP ID Q09472
Organism Homo sapiens
Cys Site Cys1438
Family/Domain Histone acetylation protein
Known Ligand Ligand list
Function Type Post-translational Modification, Transcription Related

Summary

Protein Function

p300 HAT functions as histone acetyltransferase 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.
This protein 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. (From Wikipedia)
acetyl-CoA + L-lysyl-[protein] = CoA + H+ + N6-acetyl-L-lysyl-[protein]

Cys Function & Property

Cys1438 is close to the cofactor Acetyl-CoA binding site in space.

  • Hydrophobic property:
538-hydro.png
  • SASA：
Cys1438: 39.714 A^2

Protein 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

Structural Information

  • Known structures with covalent ligands:
Unknown
  • Protein structure:
538.png

Related Pathway

Experimental Evidence

Cys-directed Mutation

Reference

  1. Ravindra K C, Narayan V, Lushington G H, et al. Targeting of Histone Acetyltransferase p300 by Cyclopentenone Prostaglandin Δ12-PGJ2 through Covalent Binding to Cys1438[J]. Chemical research in toxicology, 2011, 25(2): 337-347. 22141352
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