CINXE.COM

<!DOCTYPE html> <html class="client-nojs vector-feature-language-in-header-enabled vector-feature-language-in-main-page-header-disabled vector-feature-sticky-header-disabled vector-feature-page-tools-pinned-disabled vector-feature-toc-pinned-clientpref-1 vector-feature-main-menu-pinned-disabled vector-feature-limited-width-clientpref-1 vector-feature-limited-width-content-enabled vector-feature-custom-font-size-clientpref-1 vector-feature-appearance-pinned-clientpref-1 vector-feature-night-mode-enabled skin-theme-clientpref-day vector-toc-available" lang="en" dir="ltr"> <head> <meta charset="UTF-8"> <title>Histone acetyltransferase - Wikipedia</title> <script>(function(){var className="client-js vector-feature-language-in-header-enabled vector-feature-language-in-main-page-header-disabled vector-feature-sticky-header-disabled vector-feature-page-tools-pinned-disabled vector-feature-toc-pinned-clientpref-1 vector-feature-main-menu-pinned-disabled vector-feature-limited-width-clientpref-1 vector-feature-limited-width-content-enabled vector-feature-custom-font-size-clientpref-1 vector-feature-appearance-pinned-clientpref-1 vector-feature-night-mode-enabled skin-theme-clientpref-day vector-toc-available";var cookie=document.cookie.match(/(?:^|; )enwikimwclientpreferences=([^;]+)/);if(cookie){cookie[1].split('%2C').forEach(function(pref){className=className.replace(new RegExp('(^| )'+pref.replace(/-clientpref-\w+$|[^\w-]+/g,'')+'-clientpref-\\w+( |$)'),'$1'+pref+'$2');});}document.documentElement.className=className;}());RLCONF={"wgBreakFrames":false,"wgSeparatorTransformTable":["",""],"wgDigitTransformTable":["",""],"wgDefaultDateFormat":"dmy", "wgMonthNames":["","January","February","March","April","May","June","July","August","September","October","November","December"],"wgRequestId":"7c641a9d-6985-45be-95df-43083bd76bf9","wgCanonicalNamespace":"","wgCanonicalSpecialPageName":false,"wgNamespaceNumber":0,"wgPageName":"Histone_acetyltransferase","wgTitle":"Histone acetyltransferase","wgCurRevisionId":1242313011,"wgRevisionId":1242313011,"wgArticleId":553612,"wgIsArticle":true,"wgIsRedirect":false,"wgAction":"view","wgUserName":null,"wgUserGroups":["*"],"wgCategories":["Articles with short description","Short description matches Wikidata","All articles with unsourced statements","Articles with unsourced statements from April 2021","Transferases","EC 2.3.1","Epigenetics"],"wgPageViewLanguage":"en","wgPageContentLanguage":"en","wgPageContentModel":"wikitext","wgRelevantPageName":"Histone_acetyltransferase","wgRelevantArticleId":553612,"wgIsProbablyEditable":true,"wgRelevantPageIsProbablyEditable":true,"wgRestrictionEdit":[], "wgRestrictionMove":[],"wgNoticeProject":"wikipedia","wgCiteReferencePreviewsActive":false,"wgFlaggedRevsParams":{"tags":{"status":{"levels":1}}},"wgMediaViewerOnClick":true,"wgMediaViewerEnabledByDefault":true,"wgPopupsFlags":0,"wgVisualEditor":{"pageLanguageCode":"en","pageLanguageDir":"ltr","pageVariantFallbacks":"en"},"wgMFDisplayWikibaseDescriptions":{"search":true,"watchlist":true,"tagline":false,"nearby":true},"wgWMESchemaEditAttemptStepOversample":false,"wgWMEPageLength":50000,"wgRelatedArticlesCompat":[],"wgCentralAuthMobileDomain":false,"wgEditSubmitButtonLabelPublish":true,"wgULSPosition":"interlanguage","wgULSisCompactLinksEnabled":false,"wgVector2022LanguageInHeader":true,"wgULSisLanguageSelectorEmpty":false,"wgWikibaseItemId":"Q1036906","wgCheckUserClientHintsHeadersJsApi":["brands","architecture","bitness","fullVersionList","mobile","model","platform","platformVersion"],"GEHomepageSuggestedEditsEnableTopics":true,"wgGETopicsMatchModeEnabled":false, "wgGEStructuredTaskRejectionReasonTextInputEnabled":false,"wgGELevelingUpEnabledForUser":false};RLSTATE={"ext.globalCssJs.user.styles":"ready","site.styles":"ready","user.styles":"ready","ext.globalCssJs.user":"ready","user":"ready","user.options":"loading","ext.cite.styles":"ready","skins.vector.search.codex.styles":"ready","skins.vector.styles":"ready","skins.vector.icons":"ready","jquery.makeCollapsible.styles":"ready","ext.wikimediamessages.styles":"ready","ext.visualEditor.desktopArticleTarget.noscript":"ready","ext.uls.interlanguage":"ready","wikibase.client.init":"ready","ext.wikimediaBadges":"ready"};RLPAGEMODULES=["ext.cite.ux-enhancements","mediawiki.page.media","site","mediawiki.page.ready","jquery.makeCollapsible","mediawiki.toc","skins.vector.js","ext.centralNotice.geoIP","ext.centralNotice.startUp","ext.gadget.ReferenceTooltips","ext.gadget.switcher","ext.urlShortener.toolbar","ext.centralauth.centralautologin","mmv.bootstrap","ext.popups", "ext.visualEditor.desktopArticleTarget.init","ext.visualEditor.targetLoader","ext.echo.centralauth","ext.eventLogging","ext.wikimediaEvents","ext.navigationTiming","ext.uls.interface","ext.cx.eventlogging.campaigns","ext.cx.uls.quick.actions","wikibase.client.vector-2022","ext.checkUser.clientHints","ext.growthExperiments.SuggestedEditSession","wikibase.sidebar.tracking"];</script> <script>(RLQ=window.RLQ||[]).push(function(){mw.loader.impl(function(){return["user.options@12s5i",function($,jQuery,require,module){mw.user.tokens.set({"patrolToken":"+\\","watchToken":"+\\","csrfToken":"+\\"}); }];});});</script> <link rel="stylesheet" href="/w/load.php?lang=en&modules=ext.cite.styles%7Cext.uls.interlanguage%7Cext.visualEditor.desktopArticleTarget.noscript%7Cext.wikimediaBadges%7Cext.wikimediamessages.styles%7Cjquery.makeCollapsible.styles%7Cskins.vector.icons%2Cstyles%7Cskins.vector.search.codex.styles%7Cwikibase.client.init&only=styles&skin=vector-2022"> <script async="" src="/w/load.php?lang=en&modules=startup&only=scripts&raw=1&skin=vector-2022"></script> <meta name="ResourceLoaderDynamicStyles" content=""> <link rel="stylesheet" href="/w/load.php?lang=en&modules=site.styles&only=styles&skin=vector-2022"> <meta name="generator" content="MediaWiki 1.44.0-wmf.4"> <meta name="referrer" content="origin"> <meta name="referrer" content="origin-when-cross-origin"> <meta name="robots" content="max-image-preview:standard"> <meta name="format-detection" content="telephone=no"> <meta property="og:image" content="https://upload.wikimedia.org/wikipedia/commons/f/fb/5trm.jpg"> <meta property="og:image:width" content="1200"> <meta property="og:image:height" content="956"> <meta property="og:image" content="https://upload.wikimedia.org/wikipedia/commons/thumb/f/fb/5trm.jpg/800px-5trm.jpg"> <meta property="og:image:width" content="800"> <meta property="og:image:height" content="638"> <meta property="og:image" content="https://upload.wikimedia.org/wikipedia/commons/thumb/f/fb/5trm.jpg/640px-5trm.jpg"> <meta property="og:image:width" content="640"> <meta property="og:image:height" content="510"> <meta name="viewport" content="width=1120"> <meta property="og:title" content="Histone acetyltransferase - Wikipedia"> <meta property="og:type" content="website"> <link rel="preconnect" href="//upload.wikimedia.org"> <link rel="alternate" media="only screen and (max-width: 640px)" href="//en.m.wikipedia.org/wiki/Histone_acetyltransferase"> <link rel="alternate" type="application/x-wiki" title="Edit this page" href="/w/index.php?title=Histone_acetyltransferase&action=edit"> <link rel="apple-touch-icon" href="/static/apple-touch/wikipedia.png"> <link rel="icon" href="/static/favicon/wikipedia.ico"> <link rel="search" type="application/opensearchdescription+xml" href="/w/rest.php/v1/search" title="Wikipedia (en)"> <link rel="EditURI" type="application/rsd+xml" href="//en.wikipedia.org/w/api.php?action=rsd"> <link rel="canonical" href="https://en.wikipedia.org/wiki/Histone_acetyltransferase"> <link rel="license" href="https://creativecommons.org/licenses/by-sa/4.0/deed.en"> <link rel="alternate" type="application/atom+xml" title="Wikipedia Atom feed" href="/w/index.php?title=Special:RecentChanges&feed=atom"> <link rel="dns-prefetch" href="//meta.wikimedia.org" /> <link rel="dns-prefetch" href="//login.wikimedia.org"> </head> <body class="skin--responsive skin-vector skin-vector-search-vue mediawiki ltr sitedir-ltr mw-hide-empty-elt ns-0 ns-subject mw-editable page-Histone_acetyltransferase rootpage-Histone_acetyltransferase skin-vector-2022 action-view"><a class="mw-jump-link" href="#bodyContent">Jump to content</a> <div class="vector-header-container"> <header class="vector-header mw-header"> <div class="vector-header-start"> <nav class="vector-main-menu-landmark" aria-label="Site"> <div id="vector-main-menu-dropdown" class="vector-dropdown vector-main-menu-dropdown vector-button-flush-left vector-button-flush-right" > <input type="checkbox" id="vector-main-menu-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-main-menu-dropdown" class="vector-dropdown-checkbox " aria-label="Main menu" > <label id="vector-main-menu-dropdown-label" for="vector-main-menu-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" ><span class="vector-icon mw-ui-icon-menu mw-ui-icon-wikimedia-menu"></span> <span class="vector-dropdown-label-text">Main menu</span> </label> <div class="vector-dropdown-content"> <div id="vector-main-menu-unpinned-container" class="vector-unpinned-container"> <div id="vector-main-menu" class="vector-main-menu vector-pinnable-element"> <div class="vector-pinnable-header vector-main-menu-pinnable-header vector-pinnable-header-unpinned" data-feature-name="main-menu-pinned" data-pinnable-element-id="vector-main-menu" data-pinned-container-id="vector-main-menu-pinned-container" data-unpinned-container-id="vector-main-menu-unpinned-container" > <div class="vector-pinnable-header-label">Main menu</div> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-main-menu.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-main-menu.unpin">hide</button> </div> <div id="p-navigation" class="vector-menu mw-portlet mw-portlet-navigation" > <div class="vector-menu-heading"> Navigation </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="n-mainpage-description" class="mw-list-item"><a href="/wiki/Main_Page" title="Visit the main page [z]" accesskey="z"><span>Main page</span></a></li><li id="n-contents" class="mw-list-item"><a href="/wiki/Wikipedia:Contents" title="Guides to browsing Wikipedia"><span>Contents</span></a></li><li id="n-currentevents" class="mw-list-item"><a href="/wiki/Portal:Current_events" title="Articles related to current events"><span>Current events</span></a></li><li id="n-randompage" class="mw-list-item"><a href="/wiki/Special:Random" title="Visit a randomly selected article [x]" accesskey="x"><span>Random article</span></a></li><li id="n-aboutsite" class="mw-list-item"><a href="/wiki/Wikipedia:About" title="Learn about Wikipedia and how it works"><span>About Wikipedia</span></a></li><li id="n-contactpage" class="mw-list-item"><a href="//en.wikipedia.org/wiki/Wikipedia:Contact_us" title="How to contact Wikipedia"><span>Contact us</span></a></li> </ul> </div> </div> <div id="p-interaction" class="vector-menu mw-portlet mw-portlet-interaction" > <div class="vector-menu-heading"> Contribute </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="n-help" class="mw-list-item"><a href="/wiki/Help:Contents" title="Guidance on how to use and edit Wikipedia"><span>Help</span></a></li><li id="n-introduction" class="mw-list-item"><a href="/wiki/Help:Introduction" title="Learn how to edit Wikipedia"><span>Learn to edit</span></a></li><li id="n-portal" class="mw-list-item"><a href="/wiki/Wikipedia:Community_portal" title="The hub for editors"><span>Community portal</span></a></li><li id="n-recentchanges" class="mw-list-item"><a href="/wiki/Special:RecentChanges" title="A list of recent changes to Wikipedia [r]" accesskey="r"><span>Recent changes</span></a></li><li id="n-upload" class="mw-list-item"><a href="/wiki/Wikipedia:File_upload_wizard" title="Add images or other media for use on Wikipedia"><span>Upload file</span></a></li> </ul> </div> </div> </div> </div> </div> </div> </nav> <a href="/wiki/Main_Page" class="mw-logo"> <img class="mw-logo-icon" src="/static/images/icons/wikipedia.png" alt="" aria-hidden="true" height="50" width="50"> <span class="mw-logo-container skin-invert"> <img class="mw-logo-wordmark" alt="Wikipedia" src="/static/images/mobile/copyright/wikipedia-wordmark-en.svg" style="width: 7.5em; height: 1.125em;"> <img class="mw-logo-tagline" alt="The Free Encyclopedia" src="/static/images/mobile/copyright/wikipedia-tagline-en.svg" width="117" height="13" style="width: 7.3125em; height: 0.8125em;"> </span> </a> </div> <div class="vector-header-end"> <div id="p-search" role="search" class="vector-search-box-vue vector-search-box-collapses vector-search-box-show-thumbnail vector-search-box-auto-expand-width vector-search-box"> <a href="/wiki/Special:Search" class="cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only search-toggle" title="Search Wikipedia [f]" accesskey="f"><span class="vector-icon mw-ui-icon-search mw-ui-icon-wikimedia-search"></span> <span>Search</span> </a> <div class="vector-typeahead-search-container"> <div class="cdx-typeahead-search cdx-typeahead-search--show-thumbnail cdx-typeahead-search--auto-expand-width"> <form action="/w/index.php" id="searchform" class="cdx-search-input cdx-search-input--has-end-button"> <div id="simpleSearch" class="cdx-search-input__input-wrapper" data-search-loc="header-moved"> <div class="cdx-text-input cdx-text-input--has-start-icon"> <input class="cdx-text-input__input" type="search" name="search" placeholder="Search Wikipedia" aria-label="Search Wikipedia" autocapitalize="sentences" title="Search Wikipedia [f]" accesskey="f" id="searchInput" > <span class="cdx-text-input__icon cdx-text-input__start-icon"></span> </div> <input type="hidden" name="title" value="Special:Search"> </div> <button class="cdx-button cdx-search-input__end-button">Search</button> </form> </div> </div> </div> <nav class="vector-user-links vector-user-links-wide" aria-label="Personal tools"> <div class="vector-user-links-main"> <div id="p-vector-user-menu-preferences" class="vector-menu mw-portlet emptyPortlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> </ul> </div> </div> <div id="p-vector-user-menu-userpage" class="vector-menu mw-portlet emptyPortlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> </ul> </div> </div> <nav class="vector-appearance-landmark" aria-label="Appearance"> <div id="vector-appearance-dropdown" class="vector-dropdown " title="Change the appearance of the page's font size, width, and color" > <input type="checkbox" id="vector-appearance-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-appearance-dropdown" class="vector-dropdown-checkbox " aria-label="Appearance" > <label id="vector-appearance-dropdown-label" for="vector-appearance-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" ><span class="vector-icon mw-ui-icon-appearance mw-ui-icon-wikimedia-appearance"></span> <span class="vector-dropdown-label-text">Appearance</span> </label> <div class="vector-dropdown-content"> <div id="vector-appearance-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <div id="p-vector-user-menu-notifications" class="vector-menu mw-portlet emptyPortlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> </ul> </div> </div> <div id="p-vector-user-menu-overflow" class="vector-menu mw-portlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="pt-sitesupport-2" class="user-links-collapsible-item mw-list-item user-links-collapsible-item"><a data-mw="interface" href="https://donate.wikimedia.org/wiki/Special:FundraiserRedirector?utm_source=donate&utm_medium=sidebar&utm_campaign=C13_en.wikipedia.org&uselang=en" class=""><span>Donate</span></a> </li> <li id="pt-createaccount-2" class="user-links-collapsible-item mw-list-item user-links-collapsible-item"><a data-mw="interface" href="/w/index.php?title=Special:CreateAccount&returnto=Histone+acetyltransferase" title="You are encouraged to create an account and log in; however, it is not mandatory" class=""><span>Create account</span></a> </li> <li id="pt-login-2" class="user-links-collapsible-item mw-list-item user-links-collapsible-item"><a data-mw="interface" href="/w/index.php?title=Special:UserLogin&returnto=Histone+acetyltransferase" title="You're encouraged to log in; however, it's not mandatory. [o]" accesskey="o" class=""><span>Log in</span></a> </li> </ul> </div> </div> </div> <div id="vector-user-links-dropdown" class="vector-dropdown vector-user-menu vector-button-flush-right vector-user-menu-logged-out" title="Log in and more options" > <input type="checkbox" id="vector-user-links-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-user-links-dropdown" class="vector-dropdown-checkbox " aria-label="Personal tools" > <label id="vector-user-links-dropdown-label" for="vector-user-links-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" ><span class="vector-icon mw-ui-icon-ellipsis mw-ui-icon-wikimedia-ellipsis"></span> <span class="vector-dropdown-label-text">Personal tools</span> </label> <div class="vector-dropdown-content"> <div id="p-personal" class="vector-menu mw-portlet mw-portlet-personal user-links-collapsible-item" title="User menu" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="pt-sitesupport" class="user-links-collapsible-item mw-list-item"><a href="https://donate.wikimedia.org/wiki/Special:FundraiserRedirector?utm_source=donate&utm_medium=sidebar&utm_campaign=C13_en.wikipedia.org&uselang=en"><span>Donate</span></a></li><li id="pt-createaccount" class="user-links-collapsible-item mw-list-item"><a href="/w/index.php?title=Special:CreateAccount&returnto=Histone+acetyltransferase" title="You are encouraged to create an account and log in; however, it is not mandatory"><span class="vector-icon mw-ui-icon-userAdd mw-ui-icon-wikimedia-userAdd"></span> <span>Create account</span></a></li><li id="pt-login" class="user-links-collapsible-item mw-list-item"><a href="/w/index.php?title=Special:UserLogin&returnto=Histone+acetyltransferase" title="You're encouraged to log in; however, it's not mandatory. [o]" accesskey="o"><span class="vector-icon mw-ui-icon-logIn mw-ui-icon-wikimedia-logIn"></span> <span>Log in</span></a></li> </ul> </div> </div> <div id="p-user-menu-anon-editor" class="vector-menu mw-portlet mw-portlet-user-menu-anon-editor" > <div class="vector-menu-heading"> Pages for logged out editors <a href="/wiki/Help:Introduction" aria-label="Learn more about editing"><span>learn more</span></a> </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="pt-anoncontribs" class="mw-list-item"><a href="/wiki/Special:MyContributions" title="A list of edits made from this IP address [y]" accesskey="y"><span>Contributions</span></a></li><li id="pt-anontalk" class="mw-list-item"><a href="/wiki/Special:MyTalk" title="Discussion about edits from this IP address [n]" accesskey="n"><span>Talk</span></a></li> </ul> </div> </div> </div> </div> </nav> </div> </header> </div> <div class="mw-page-container"> <div class="mw-page-container-inner"> <div class="vector-sitenotice-container"> <div id="siteNotice"></div> </div> <div class="vector-column-start"> <div class="vector-main-menu-container"> <div id="mw-navigation"> <nav id="mw-panel" class="vector-main-menu-landmark" aria-label="Site"> <div id="vector-main-menu-pinned-container" class="vector-pinned-container"> </div> </nav> </div> </div> <div class="vector-sticky-pinned-container"> <nav id="mw-panel-toc" aria-label="Contents" data-event-name="ui.sidebar-toc" class="mw-table-of-contents-container vector-toc-landmark"> <div id="vector-toc-pinned-container" class="vector-pinned-container"> <div id="vector-toc" class="vector-toc vector-pinnable-element"> <div class="vector-pinnable-header vector-toc-pinnable-header vector-pinnable-header-pinned" data-feature-name="toc-pinned" data-pinnable-element-id="vector-toc" > <h2 class="vector-pinnable-header-label">Contents</h2> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-toc.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-toc.unpin">hide</button> </div> <ul class="vector-toc-contents" id="mw-panel-toc-list"> <li id="toc-mw-content-text" class="vector-toc-list-item vector-toc-level-1"> <a href="#" class="vector-toc-link"> <div class="vector-toc-text">(Top)</div> </a> </li> <li id="toc-HAT_families" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#HAT_families"> <div class="vector-toc-text"> <span class="vector-toc-numb">1</span> <span>HAT families</span> </div> </a> <button aria-controls="toc-HAT_families-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle HAT families subsection</span> </button> <ul id="toc-HAT_families-sublist" class="vector-toc-list"> <li id="toc-Gcn5-related_N-acetyltransferases_(GNATs)" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Gcn5-related_N-acetyltransferases_(GNATs)"> <div class="vector-toc-text"> <span class="vector-toc-numb">1.1</span> <span>Gcn5-related <i>N</i>-acetyltransferases (GNATs)</span> </div> </a> <ul id="toc-Gcn5-related_N-acetyltransferases_(GNATs)-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-MYST_HATs" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#MYST_HATs"> <div class="vector-toc-text"> <span class="vector-toc-numb">1.2</span> <span>MYST HATs</span> </div> </a> <ul id="toc-MYST_HATs-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Others" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Others"> <div class="vector-toc-text"> <span class="vector-toc-numb">1.3</span> <span>Others</span> </div> </a> <ul id="toc-Others-sublist" class="vector-toc-list"> <li id="toc-Nuclear_receptor_coactivators" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Nuclear_receptor_coactivators"> <div class="vector-toc-text"> <span class="vector-toc-numb">1.3.1</span> <span>Nuclear receptor coactivators</span> </div> </a> <ul id="toc-Nuclear_receptor_coactivators-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> </ul> </li> <li id="toc-Overall_structure" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Overall_structure"> <div class="vector-toc-text"> <span class="vector-toc-numb">2</span> <span>Overall structure</span> </div> </a> <button aria-controls="toc-Overall_structure-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Overall structure subsection</span> </button> <ul id="toc-Overall_structure-sublist" class="vector-toc-list"> <li id="toc-GNAT_and_MYST_families" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#GNAT_and_MYST_families"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.1</span> <span>GNAT and MYST families</span> </div> </a> <ul id="toc-GNAT_and_MYST_families-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-p300/CBP_family" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#p300/CBP_family"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.2</span> <span>p300/CBP family</span> </div> </a> <ul id="toc-p300/CBP_family-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Rtt109" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Rtt109"> <div class="vector-toc-text"> <span class="vector-toc-numb">2.3</span> <span>Rtt109</span> </div> </a> <ul id="toc-Rtt109-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Catalytic_mechanisms" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Catalytic_mechanisms"> <div class="vector-toc-text"> <span class="vector-toc-numb">3</span> <span>Catalytic mechanisms</span> </div> </a> <button aria-controls="toc-Catalytic_mechanisms-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Catalytic mechanisms subsection</span> </button> <ul id="toc-Catalytic_mechanisms-sublist" class="vector-toc-list"> <li id="toc-GNAT_family" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#GNAT_family"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.1</span> <span>GNAT family</span> </div> </a> <ul id="toc-GNAT_family-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-MYST_family" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#MYST_family"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.2</span> <span>MYST family</span> </div> </a> <ul id="toc-MYST_family-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-p300/CBP_family_2" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#p300/CBP_family_2"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.3</span> <span>p300/CBP family</span> </div> </a> <ul id="toc-p300/CBP_family_2-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Rtt109_2" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Rtt109_2"> <div class="vector-toc-text"> <span class="vector-toc-numb">3.4</span> <span>Rtt109</span> </div> </a> <ul id="toc-Rtt109_2-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Substrate_binding_and_specificity" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Substrate_binding_and_specificity"> <div class="vector-toc-text"> <span class="vector-toc-numb">4</span> <span>Substrate binding and specificity</span> </div> </a> <button aria-controls="toc-Substrate_binding_and_specificity-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Substrate binding and specificity subsection</span> </button> <ul id="toc-Substrate_binding_and_specificity-sublist" class="vector-toc-list"> <li id="toc-Lysine_selectivity" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Lysine_selectivity"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.1</span> <span>Lysine selectivity</span> </div> </a> <ul id="toc-Lysine_selectivity-sublist" class="vector-toc-list"> <li id="toc-GNAT_family_2" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#GNAT_family_2"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.1.1</span> <span>GNAT family</span> </div> </a> <ul id="toc-GNAT_family_2-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-MYST_family_2" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#MYST_family_2"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.1.2</span> <span>MYST family</span> </div> </a> <ul id="toc-MYST_family_2-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Others_2" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#Others_2"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.1.3</span> <span>Others</span> </div> </a> <ul id="toc-Others_2-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Non-histone_substrates_(in_vitro)" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Non-histone_substrates_(in_vitro)"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.2</span> <span>Non-histone substrates (<i>in vitro</i>)</span> </div> </a> <ul id="toc-Non-histone_substrates_(in_vitro)-sublist" class="vector-toc-list"> <li id="toc-PCAF" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#PCAF"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.2.1</span> <span>PCAF</span> </div> </a> <ul id="toc-PCAF-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-p300/CBP" class="vector-toc-list-item vector-toc-level-3"> <a class="vector-toc-link" href="#p300/CBP"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.2.2</span> <span>p300/CBP</span> </div> </a> <ul id="toc-p300/CBP-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Multisubunit_HAT_complexes" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Multisubunit_HAT_complexes"> <div class="vector-toc-text"> <span class="vector-toc-numb">4.3</span> <span>Multisubunit HAT complexes</span> </div> </a> <ul id="toc-Multisubunit_HAT_complexes-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Regulation_of_HAT_activity" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Regulation_of_HAT_activity"> <div class="vector-toc-text"> <span class="vector-toc-numb">5</span> <span>Regulation of HAT activity</span> </div> </a> <ul id="toc-Regulation_of_HAT_activity-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Interaction_with_HDACs" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Interaction_with_HDACs"> <div class="vector-toc-text"> <span class="vector-toc-numb">6</span> <span>Interaction with HDACs</span> </div> </a> <ul id="toc-Interaction_with_HDACs-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Biological_role" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Biological_role"> <div class="vector-toc-text"> <span class="vector-toc-numb">7</span> <span>Biological role</span> </div> </a> <button aria-controls="toc-Biological_role-sublist" class="cdx-button cdx-button--weight-quiet cdx-button--icon-only vector-toc-toggle"> <span class="vector-icon mw-ui-icon-wikimedia-expand"></span> <span>Toggle Biological role subsection</span> </button> <ul id="toc-Biological_role-sublist" class="vector-toc-list"> <li id="toc-Chromatin_remodeling" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Chromatin_remodeling"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.1</span> <span>Chromatin remodeling</span> </div> </a> <ul id="toc-Chromatin_remodeling-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-Gene_expression" class="vector-toc-list-item vector-toc-level-2"> <a class="vector-toc-link" href="#Gene_expression"> <div class="vector-toc-text"> <span class="vector-toc-numb">7.2</span> <span>Gene expression</span> </div> </a> <ul id="toc-Gene_expression-sublist" class="vector-toc-list"> </ul> </li> </ul> </li> <li id="toc-Clinical_significance" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#Clinical_significance"> <div class="vector-toc-text"> <span class="vector-toc-numb">8</span> <span>Clinical significance</span> </div> </a> <ul id="toc-Clinical_significance-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-See_also" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#See_also"> <div class="vector-toc-text"> <span class="vector-toc-numb">9</span> <span>See also</span> </div> </a> <ul id="toc-See_also-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-References" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#References"> <div class="vector-toc-text"> <span class="vector-toc-numb">10</span> <span>References</span> </div> </a> <ul id="toc-References-sublist" class="vector-toc-list"> </ul> </li> <li id="toc-External_links" class="vector-toc-list-item vector-toc-level-1"> <a class="vector-toc-link" href="#External_links"> <div class="vector-toc-text"> <span class="vector-toc-numb">11</span> <span>External links</span> </div> </a> <ul id="toc-External_links-sublist" class="vector-toc-list"> </ul> </li> </ul> </div> </div> </nav> </div> </div> <div class="mw-content-container"> <main id="content" class="mw-body"> <header class="mw-body-header vector-page-titlebar"> <nav aria-label="Contents" class="vector-toc-landmark"> <div id="vector-page-titlebar-toc" class="vector-dropdown vector-page-titlebar-toc vector-button-flush-left" > <input type="checkbox" id="vector-page-titlebar-toc-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-titlebar-toc" class="vector-dropdown-checkbox " aria-label="Toggle the table of contents" > <label id="vector-page-titlebar-toc-label" for="vector-page-titlebar-toc-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--icon-only " aria-hidden="true" ><span class="vector-icon mw-ui-icon-listBullet mw-ui-icon-wikimedia-listBullet"></span> <span class="vector-dropdown-label-text">Toggle the table of contents</span> </label> <div class="vector-dropdown-content"> <div id="vector-page-titlebar-toc-unpinned-container" class="vector-unpinned-container"> </div> </div> </div> </nav> <h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Histone acetyltransferase</span></h1> <div id="p-lang-btn" class="vector-dropdown mw-portlet mw-portlet-lang" > <input type="checkbox" id="p-lang-btn-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-p-lang-btn" class="vector-dropdown-checkbox mw-interlanguage-selector" aria-label="Go to an article in another language. Available in 16 languages" > <label id="p-lang-btn-label" for="p-lang-btn-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet cdx-button--action-progressive mw-portlet-lang-heading-16" aria-hidden="true" ><span class="vector-icon mw-ui-icon-language-progressive mw-ui-icon-wikimedia-language-progressive"></span> <span class="vector-dropdown-label-text">16 languages</span> </label> <div class="vector-dropdown-content"> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li class="interlanguage-link interwiki-ar mw-list-item"><a href="https://ar.wikipedia.org/wiki/%D9%87%D9%8A%D8%B3%D8%AA%D9%88%D9%86_%D8%A3%D8%B3%D9%8A%D8%AA%D9%8A%D9%84_%D8%AA%D8%B1%D8%A7%D9%86%D8%B3%D9%81%D9%8A%D8%B1%D8%A7%D8%B2" title="هيستون أسيتيل ترانسفيراز – Arabic" lang="ar" hreflang="ar" data-title="هيستون أسيتيل ترانسفيراز" data-language-autonym="العربية" data-language-local-name="Arabic" class="interlanguage-link-target"><span>العربية</span></a></li><li class="interlanguage-link interwiki-bs mw-list-item"><a href="https://bs.wikipedia.org/wiki/Histon-acetiltransferaza" title="Histon-acetiltransferaza – Bosnian" lang="bs" hreflang="bs" data-title="Histon-acetiltransferaza" data-language-autonym="Bosanski" data-language-local-name="Bosnian" class="interlanguage-link-target"><span>Bosanski</span></a></li><li class="interlanguage-link interwiki-es mw-list-item"><a href="https://es.wikipedia.org/wiki/Histona_acetiltransferasa" title="Histona acetiltransferasa – Spanish" lang="es" hreflang="es" data-title="Histona acetiltransferasa" data-language-autonym="Español" data-language-local-name="Spanish" class="interlanguage-link-target"><span>Español</span></a></li><li class="interlanguage-link interwiki-fr mw-list-item"><a href="https://fr.wikipedia.org/wiki/Histone_ac%C3%A9tyltransf%C3%A9rase" title="Histone acétyltransférase – French" lang="fr" hreflang="fr" data-title="Histone acétyltransférase" data-language-autonym="Français" data-language-local-name="French" class="interlanguage-link-target"><span>Français</span></a></li><li class="interlanguage-link interwiki-it mw-list-item"><a href="https://it.wikipedia.org/wiki/Istone_acetiltransferasi" title="Istone acetiltransferasi – Italian" lang="it" hreflang="it" data-title="Istone acetiltransferasi" data-language-autonym="Italiano" data-language-local-name="Italian" class="interlanguage-link-target"><span>Italiano</span></a></li><li class="interlanguage-link interwiki-hu mw-list-item"><a href="https://hu.wikipedia.org/wiki/Hiszton-acetiltranszfer%C3%A1z" title="Hiszton-acetiltranszferáz – Hungarian" lang="hu" hreflang="hu" data-title="Hiszton-acetiltranszferáz" data-language-autonym="Magyar" data-language-local-name="Hungarian" class="interlanguage-link-target"><span>Magyar</span></a></li><li class="interlanguage-link interwiki-nl mw-list-item"><a href="https://nl.wikipedia.org/wiki/Histon-acetyltransferase" title="Histon-acetyltransferase – Dutch" lang="nl" hreflang="nl" data-title="Histon-acetyltransferase" data-language-autonym="Nederlands" data-language-local-name="Dutch" class="interlanguage-link-target"><span>Nederlands</span></a></li><li class="interlanguage-link interwiki-ja mw-list-item"><a href="https://ja.wikipedia.org/wiki/%E3%83%92%E3%82%B9%E3%83%88%E3%83%B3%E3%82%A2%E3%82%BB%E3%83%81%E3%83%AB%E3%83%88%E3%83%A9%E3%83%B3%E3%82%B9%E3%83%95%E3%82%A7%E3%83%A9%E3%83%BC%E3%82%BC" title="ヒストンアセチルトランスフェラーゼ – Japanese" lang="ja" hreflang="ja" data-title="ヒストンアセチルトランスフェラーゼ" data-language-autonym="日本語" data-language-local-name="Japanese" class="interlanguage-link-target"><span>日本語</span></a></li><li class="interlanguage-link interwiki-pt mw-list-item"><a href="https://pt.wikipedia.org/wiki/Histona_acetiltransferase" title="Histona acetiltransferase – Portuguese" lang="pt" hreflang="pt" data-title="Histona acetiltransferase" data-language-autonym="Português" data-language-local-name="Portuguese" class="interlanguage-link-target"><span>Português</span></a></li><li class="interlanguage-link interwiki-ru mw-list-item"><a href="https://ru.wikipedia.org/wiki/%D0%93%D0%B8%D1%81%D1%82%D0%BE%D0%BD%D0%B0%D1%86%D0%B5%D1%82%D0%B8%D0%BB%D1%82%D1%80%D0%B0%D0%BD%D1%81%D1%84%D0%B5%D1%80%D0%B0%D0%B7%D0%B0" title="Гистонацетилтрансфераза – Russian" lang="ru" hreflang="ru" data-title="Гистонацетилтрансфераза" data-language-autonym="Русский" data-language-local-name="Russian" class="interlanguage-link-target"><span>Русский</span></a></li><li class="interlanguage-link interwiki-sr mw-list-item"><a href="https://sr.wikipedia.org/wiki/Histon_acetiltransferaza" title="Histon acetiltransferaza – Serbian" lang="sr" hreflang="sr" data-title="Histon acetiltransferaza" data-language-autonym="Српски / srpski" data-language-local-name="Serbian" class="interlanguage-link-target"><span>Српски / srpski</span></a></li><li class="interlanguage-link interwiki-sh mw-list-item"><a href="https://sh.wikipedia.org/wiki/Histon_acetiltransferaza" title="Histon acetiltransferaza – Serbo-Croatian" lang="sh" hreflang="sh" data-title="Histon acetiltransferaza" data-language-autonym="Srpskohrvatski / српскохрватски" data-language-local-name="Serbo-Croatian" class="interlanguage-link-target"><span>Srpskohrvatski / српскохрватски</span></a></li><li class="interlanguage-link interwiki-sv mw-list-item"><a href="https://sv.wikipedia.org/wiki/Histonacetyltransferas" title="Histonacetyltransferas – Swedish" lang="sv" hreflang="sv" data-title="Histonacetyltransferas" data-language-autonym="Svenska" data-language-local-name="Swedish" class="interlanguage-link-target"><span>Svenska</span></a></li><li class="interlanguage-link interwiki-tr mw-list-item"><a href="https://tr.wikipedia.org/wiki/Histon_asetiltransferaz" title="Histon asetiltransferaz – Turkish" lang="tr" hreflang="tr" data-title="Histon asetiltransferaz" data-language-autonym="Türkçe" data-language-local-name="Turkish" class="interlanguage-link-target"><span>Türkçe</span></a></li><li class="interlanguage-link interwiki-uk mw-list-item"><a href="https://uk.wikipedia.org/wiki/%D0%93%D1%96%D1%81%D1%82%D0%BE%D0%BD%D0%B0%D1%86%D0%B5%D1%82%D0%B8%D0%BB%D1%82%D1%80%D0%B0%D0%BD%D1%81%D1%84%D0%B5%D1%80%D0%B0%D0%B7%D0%B8" title="Гістонацетилтрансферази – Ukrainian" lang="uk" hreflang="uk" data-title="Гістонацетилтрансферази" data-language-autonym="Українська" data-language-local-name="Ukrainian" class="interlanguage-link-target"><span>Українська</span></a></li><li class="interlanguage-link interwiki-zh mw-list-item"><a href="https://zh.wikipedia.org/wiki/%E7%B5%84%E8%9B%8B%E7%99%BD%E4%B9%99%E9%86%AF%E8%BD%89%E7%A7%BB%E9%85%B6" title="組蛋白乙醯轉移酶 – Chinese" lang="zh" hreflang="zh" data-title="組蛋白乙醯轉移酶" data-language-autonym="中文" data-language-local-name="Chinese" class="interlanguage-link-target"><span>中文</span></a></li> </ul> <div class="after-portlet after-portlet-lang"><span class="wb-langlinks-edit wb-langlinks-link"><a href="https://www.wikidata.org/wiki/Special:EntityPage/Q1036906#sitelinks-wikipedia" title="Edit interlanguage links" class="wbc-editpage">Edit links</a></span></div> </div> </div> </div> </header> <div class="vector-page-toolbar"> <div class="vector-page-toolbar-container"> <div id="left-navigation"> <nav aria-label="Namespaces"> <div id="p-associated-pages" class="vector-menu vector-menu-tabs mw-portlet mw-portlet-associated-pages" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="ca-nstab-main" class="selected vector-tab-noicon mw-list-item"><a href="/wiki/Histone_acetyltransferase" title="View the content page [c]" accesskey="c"><span>Article</span></a></li><li id="ca-talk" class="vector-tab-noicon mw-list-item"><a href="/wiki/Talk:Histone_acetyltransferase" rel="discussion" title="Discuss improvements to the content page [t]" accesskey="t"><span>Talk</span></a></li> </ul> </div> </div> <div id="vector-variants-dropdown" class="vector-dropdown emptyPortlet" > <input type="checkbox" id="vector-variants-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-variants-dropdown" class="vector-dropdown-checkbox " aria-label="Change language variant" > <label id="vector-variants-dropdown-label" for="vector-variants-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet" aria-hidden="true" ><span class="vector-dropdown-label-text">English</span> </label> <div class="vector-dropdown-content"> <div id="p-variants" class="vector-menu mw-portlet mw-portlet-variants emptyPortlet" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> </ul> </div> </div> </div> </div> </nav> </div> <div id="right-navigation" class="vector-collapsible"> <nav aria-label="Views"> <div id="p-views" class="vector-menu vector-menu-tabs mw-portlet mw-portlet-views" > <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="ca-view" class="selected vector-tab-noicon mw-list-item"><a href="/wiki/Histone_acetyltransferase"><span>Read</span></a></li><li id="ca-edit" class="vector-tab-noicon mw-list-item"><a href="/w/index.php?title=Histone_acetyltransferase&action=edit" title="Edit this page [e]" accesskey="e"><span>Edit</span></a></li><li id="ca-history" class="vector-tab-noicon mw-list-item"><a href="/w/index.php?title=Histone_acetyltransferase&action=history" title="Past revisions of this page [h]" accesskey="h"><span>View history</span></a></li> </ul> </div> </div> </nav> <nav class="vector-page-tools-landmark" aria-label="Page tools"> <div id="vector-page-tools-dropdown" class="vector-dropdown vector-page-tools-dropdown" > <input type="checkbox" id="vector-page-tools-dropdown-checkbox" role="button" aria-haspopup="true" data-event-name="ui.dropdown-vector-page-tools-dropdown" class="vector-dropdown-checkbox " aria-label="Tools" > <label id="vector-page-tools-dropdown-label" for="vector-page-tools-dropdown-checkbox" class="vector-dropdown-label cdx-button cdx-button--fake-button cdx-button--fake-button--enabled cdx-button--weight-quiet" aria-hidden="true" ><span class="vector-dropdown-label-text">Tools</span> </label> <div class="vector-dropdown-content"> <div id="vector-page-tools-unpinned-container" class="vector-unpinned-container"> <div id="vector-page-tools" class="vector-page-tools vector-pinnable-element"> <div class="vector-pinnable-header vector-page-tools-pinnable-header vector-pinnable-header-unpinned" data-feature-name="page-tools-pinned" data-pinnable-element-id="vector-page-tools" data-pinned-container-id="vector-page-tools-pinned-container" data-unpinned-container-id="vector-page-tools-unpinned-container" > <div class="vector-pinnable-header-label">Tools</div> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-page-tools.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-page-tools.unpin">hide</button> </div> <div id="p-cactions" class="vector-menu mw-portlet mw-portlet-cactions emptyPortlet vector-has-collapsible-items" title="More options" > <div class="vector-menu-heading"> Actions </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="ca-more-view" class="selected vector-more-collapsible-item mw-list-item"><a href="/wiki/Histone_acetyltransferase"><span>Read</span></a></li><li id="ca-more-edit" class="vector-more-collapsible-item mw-list-item"><a href="/w/index.php?title=Histone_acetyltransferase&action=edit" title="Edit this page [e]" accesskey="e"><span>Edit</span></a></li><li id="ca-more-history" class="vector-more-collapsible-item mw-list-item"><a href="/w/index.php?title=Histone_acetyltransferase&action=history"><span>View history</span></a></li> </ul> </div> </div> <div id="p-tb" class="vector-menu mw-portlet mw-portlet-tb" > <div class="vector-menu-heading"> General </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="t-whatlinkshere" class="mw-list-item"><a href="/wiki/Special:WhatLinksHere/Histone_acetyltransferase" title="List of all English Wikipedia pages containing links to this page [j]" accesskey="j"><span>What links here</span></a></li><li id="t-recentchangeslinked" class="mw-list-item"><a href="/wiki/Special:RecentChangesLinked/Histone_acetyltransferase" rel="nofollow" title="Recent changes in pages linked from this page [k]" accesskey="k"><span>Related changes</span></a></li><li id="t-upload" class="mw-list-item"><a href="/wiki/Wikipedia:File_Upload_Wizard" title="Upload files [u]" accesskey="u"><span>Upload file</span></a></li><li id="t-specialpages" class="mw-list-item"><a href="/wiki/Special:SpecialPages" title="A list of all special pages [q]" accesskey="q"><span>Special pages</span></a></li><li id="t-permalink" class="mw-list-item"><a href="/w/index.php?title=Histone_acetyltransferase&oldid=1242313011" title="Permanent link to this revision of this page"><span>Permanent link</span></a></li><li id="t-info" class="mw-list-item"><a href="/w/index.php?title=Histone_acetyltransferase&action=info" title="More information about this page"><span>Page information</span></a></li><li id="t-cite" class="mw-list-item"><a href="/w/index.php?title=Special:CiteThisPage&page=Histone_acetyltransferase&id=1242313011&wpFormIdentifier=titleform" title="Information on how to cite this page"><span>Cite this page</span></a></li><li id="t-urlshortener" class="mw-list-item"><a href="/w/index.php?title=Special:UrlShortener&url=https%3A%2F%2Fen.wikipedia.org%2Fwiki%2FHistone_acetyltransferase"><span>Get shortened URL</span></a></li><li id="t-urlshortener-qrcode" class="mw-list-item"><a href="/w/index.php?title=Special:QrCode&url=https%3A%2F%2Fen.wikipedia.org%2Fwiki%2FHistone_acetyltransferase"><span>Download QR code</span></a></li> </ul> </div> </div> <div id="p-coll-print_export" class="vector-menu mw-portlet mw-portlet-coll-print_export" > <div class="vector-menu-heading"> Print/export </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="coll-download-as-rl" class="mw-list-item"><a href="/w/index.php?title=Special:DownloadAsPdf&page=Histone_acetyltransferase&action=show-download-screen" title="Download this page as a PDF file"><span>Download as PDF</span></a></li><li id="t-print" class="mw-list-item"><a href="/w/index.php?title=Histone_acetyltransferase&printable=yes" title="Printable version of this page [p]" accesskey="p"><span>Printable version</span></a></li> </ul> </div> </div> <div id="p-wikibase-otherprojects" class="vector-menu mw-portlet mw-portlet-wikibase-otherprojects" > <div class="vector-menu-heading"> In other projects </div> <div class="vector-menu-content"> <ul class="vector-menu-content-list"> <li id="t-wikibase" class="wb-otherproject-link wb-otherproject-wikibase-dataitem mw-list-item"><a href="https://www.wikidata.org/wiki/Special:EntityPage/Q1036906" title="Structured data on this page hosted by Wikidata [g]" accesskey="g"><span>Wikidata item</span></a></li> </ul> </div> </div> </div> </div> </div> </div> </nav> </div> </div> </div> <div class="vector-column-end"> <div class="vector-sticky-pinned-container"> <nav class="vector-page-tools-landmark" aria-label="Page tools"> <div id="vector-page-tools-pinned-container" class="vector-pinned-container"> </div> </nav> <nav class="vector-appearance-landmark" aria-label="Appearance"> <div id="vector-appearance-pinned-container" class="vector-pinned-container"> <div id="vector-appearance" class="vector-appearance vector-pinnable-element"> <div class="vector-pinnable-header vector-appearance-pinnable-header vector-pinnable-header-pinned" data-feature-name="appearance-pinned" data-pinnable-element-id="vector-appearance" data-pinned-container-id="vector-appearance-pinned-container" data-unpinned-container-id="vector-appearance-unpinned-container" > <div class="vector-pinnable-header-label">Appearance</div> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-pin-button" data-event-name="pinnable-header.vector-appearance.pin">move to sidebar</button> <button class="vector-pinnable-header-toggle-button vector-pinnable-header-unpin-button" data-event-name="pinnable-header.vector-appearance.unpin">hide</button> </div> </div> </div> </nav> </div> </div> <div id="bodyContent" class="vector-body" aria-labelledby="firstHeading" data-mw-ve-target-container> <div class="vector-body-before-content"> <div class="mw-indicators"> </div> <div id="siteSub" class="noprint">From Wikipedia, the free encyclopedia</div> </div> <div id="contentSub"><div id="mw-content-subtitle"></div></div> <div id="mw-content-text" class="mw-body-content"><div class="mw-content-ltr mw-parser-output" lang="en" dir="ltr"><div class="shortdescription nomobile noexcerpt noprint searchaux" style="display:none">Enzymes that catalyze acyl group transfer from acetyl-CoA to histones</div> <style data-mw-deduplicate="TemplateStyles:r1236090951">.mw-parser-output .hatnote{font-style:italic}.mw-parser-output div.hatnote{padding-left:1.6em;margin-bottom:0.5em}.mw-parser-output .hatnote i{font-style:normal}.mw-parser-output .hatnote+link+.hatnote{margin-top:-0.5em}@media print{body.ns-0 .mw-parser-output .hatnote{display:none!important}}</style><div role="note" class="hatnote navigation-not-searchable">For other uses, see <a href="/wiki/Hat_(disambiguation)" class="mw-disambig" title="Hat (disambiguation)">Hat (disambiguation)</a>.</div> <style data-mw-deduplicate="TemplateStyles:r1257001546">.mw-parser-output .infobox-subbox{padding:0;border:none;margin:-3px;width:auto;min-width:100%;font-size:100%;clear:none;float:none;background-color:transparent}.mw-parser-output .infobox-3cols-child{margin:auto}.mw-parser-output .infobox .navbar{font-size:100%}@media screen{html.skin-theme-clientpref-night .mw-parser-output .infobox-full-data:not(.notheme)>div:not(.notheme)[style]{background:#1f1f23!important;color:#f8f9fa}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .infobox-full-data:not(.notheme) div:not(.notheme){background:#1f1f23!important;color:#f8f9fa}}@media(min-width:640px){body.skin--responsive .mw-parser-output .infobox-table{display:table!important}body.skin--responsive .mw-parser-output .infobox-table>caption{display:table-caption!important}body.skin--responsive .mw-parser-output .infobox-table>tbody{display:table-row-group}body.skin--responsive .mw-parser-output .infobox-table tr{display:table-row!important}body.skin--responsive .mw-parser-output .infobox-table th,body.skin--responsive .mw-parser-output .infobox-table td{padding-left:inherit;padding-right:inherit}}</style><table class="infobox"><tbody><tr><th colspan="2" class="infobox-above">GCN5 Histone acetyltransferase</th></tr><tr><td colspan="2" class="infobox-image"><span typeof="mw:File"><a href="/wiki/File:5trm.jpg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/f/fb/5trm.jpg/270px-5trm.jpg" decoding="async" width="270" height="215" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/f/fb/5trm.jpg/405px-5trm.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/f/fb/5trm.jpg/540px-5trm.jpg 2x" data-file-width="1000" data-file-height="797" /></a></span><div class="infobox-caption">GCN5 histone acetyltransferase domain homo24-mer, Human. Based on <a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a> structure: <span class="plainlinks"><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/pdbe/entry/pdb/5trm">5trm</a></span><sup id="cite_ref-1" class="reference"><a href="#cite_note-1"><span class="cite-bracket">[</span>1<span class="cite-bracket">]</span></a></sup></div></td></tr><tr><th colspan="2" class="infobox-header" style="background-color: #ddd">Identifiers</th></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC no.</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.enzyme-database.org/query.php?ec=2.3.1.48">2.3.1.48</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/CAS_registry_number" class="mw-redirect" title="CAS registry number">CAS no.</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://commonchemistry.cas.org/detail?cas_rn=9054-51-7&title=">9054-51-7 </a></td></tr><tr><th colspan="2" class="infobox-header" style="background-color: #ddd">Databases</th></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/IntEnz" title="IntEnz">IntEnz</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/intenz/query?cmd=SearchEC&ec=2.3.1.48">IntEnz view</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/BRENDA" title="BRENDA">BRENDA</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="http://www.brenda-enzymes.org/enzyme.php?ecno=2.3.1.48">BRENDA entry</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/ExPASy" class="mw-redirect" title="ExPASy">ExPASy</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://enzyme.expasy.org/EC/2.3.1.48">NiceZyme view</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/KEGG" title="KEGG">KEGG</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.genome.jp/dbget-bin/www_bget?enzyme+2.3.1.48">KEGG entry</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/MetaCyc" title="MetaCyc">MetaCyc</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://biocyc.org/META/substring-search?type=NIL&object=2.3.1.48">metabolic pathway</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/PRIAM_enzyme-specific_profiles" title="PRIAM enzyme-specific profiles">PRIAM</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="http://priam.prabi.fr/cgi-bin/PRIAM_profiles_CurrentRelease.pl?EC=2.3.1.48">profile</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/Protein_Data_Bank" title="Protein Data Bank">PDB</a> structures</th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="https://www.rcsb.org/search?q=rcsb_polymer_entity.rcsb_ec_lineage.id:2.3.1.48">RCSB PDB</a> <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/pdbe/entry/search/index?ec_number:2.3.1.48">PDBe</a> <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/enzymes/GetPage.pl?ec_number=2.3.1.48">PDBsum</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3"><a href="/wiki/Gene_Ontology" title="Gene Ontology">Gene Ontology</a></th><td class="infobox-data" style="background-color: #eee"><a rel="nofollow" class="external text" href="http://amigo.geneontology.org/amigo/term/GO:0004402">AmiGO </a> / <a rel="nofollow" class="external text" href="https://www.ebi.ac.uk/QuickGO/term/GO:0004402">QuickGO</a></td></tr><tr><td colspan="2" class="infobox-full-data" style="background-color: #eee"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1257001546"><table class="infobox mw-collapsible mw-collapsed" style="float:none; clear:none; margin:0; border-width:0; border-collapse:collapse; text-align:left; width:100%"><tbody><tr><th colspan="2" class="infobox-header" style="background-color: #ddd">Search</th></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;"><a href="/wiki/PubMed_Central" title="PubMed Central">PMC</a></th><td class="infobox-data" style="background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&term=2.3.1.48%5BEC/RN%20Number%5D%20AND%20pubmed%20pmc%20local%5Bsb%5D">articles</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;"><a href="/wiki/PubMed" title="PubMed">PubMed</a></th><td class="infobox-data" style="background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&term=2.3.1.48%5BEC/RN%20Number%5D">articles</a></td></tr><tr><th scope="row" class="infobox-label" style="background-color: #e7dcc3; border:#fafafa 2px solid; border-width:3px 2px 0 0;"><a href="/wiki/National_Center_for_Biotechnology_Information" title="National Center for Biotechnology Information">NCBI</a></th><td class="infobox-data" style="background-color: #eee; border:#fafafa 2px solid; border-width:3px 0 0 2px;"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/protein?term=2.3.1.48%5BEC/RN%20Number%5D">proteins</a></td></tr></tbody></table></td></tr></tbody></table> <p><b>Histone acetyltransferases</b> (<b>HATs</b>) are <a href="/wiki/Enzyme" title="Enzyme">enzymes</a> that <a href="/wiki/Acetylation" title="Acetylation">acetylate</a> conserved <a href="/wiki/Lysine" title="Lysine">lysine</a> <a href="/wiki/Amino_acid" title="Amino acid">amino acids</a> on <a href="/wiki/Histone" title="Histone">histone</a> proteins by transferring an <a href="/wiki/Acetyl_group" title="Acetyl group">acetyl group</a> from <a href="/wiki/Acetyl-CoA" title="Acetyl-CoA">acetyl-CoA</a> to form ε-<i>N</i>-acetyllysine. DNA is wrapped around histones, and, by transferring an acetyl group to the histones, genes can be turned on and off. In general, histone acetylation increases gene expression. </p><p>In general, histone acetylation is linked to <a href="/wiki/DNA_transcription" class="mw-redirect" title="DNA transcription">transcriptional</a> activation and associated with <a href="/wiki/Euchromatin" title="Euchromatin">euchromatin</a>. Euchromatin, which is less densely compact, allows transcription factors to bind more easily to regulatory sites on DNA, causing transcriptional activation. When it was first discovered, it was thought that <a href="/wiki/Acetylation" title="Acetylation">acetylation</a> of lysine neutralizes the positive <a href="/wiki/Electric_charge" title="Electric charge">charge</a> normally present, thus reducing affinity between histone and (negatively charged) DNA, which renders DNA more accessible to <a href="/wiki/Transcription_factors" class="mw-redirect" title="Transcription factors">transcription factors</a>. Research has emerged, since, to show that lysine acetylation and other <a href="/wiki/Posttranslational_modification" class="mw-redirect" title="Posttranslational modification">posttranslational modifications</a> of histones generate binding sites for specific protein–protein interaction domains, such as the acetyllysine-binding <a href="/wiki/Bromodomain" title="Bromodomain">bromodomain</a><sup class="noprint Inline-Template Template-Fact" style="white-space:nowrap;">[<i><a href="/wiki/Wikipedia:Citation_needed" title="Wikipedia:Citation needed"><span title="This sentence implies a change in the prevailing opinion in the field on the traditional view of how chromatin remodeling works. I could find no evidence to support such a change has happened. (April 2021)">citation needed</span></a></i>]</sup>. Histone acetyltransferases can also acetylate non-histone proteins, such as nuclear receptors and other transcription factors to facilitate gene expression. </p> <meta property="mw:PageProp/toc" /> <div class="mw-heading mw-heading2"><h2 id="HAT_families">HAT families</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=1" title="Edit section: HAT families"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>HATs are traditionally divided into two different classes based on their subcellular localization.<sup id="cite_ref-Lee_2-0" class="reference"><a href="#cite_note-Lee-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> Type A HATs are located in the <a href="/wiki/Cell_nucleus" title="Cell nucleus">nucleus</a> and are involved in the regulation of gene expression through <a href="/wiki/Histone_acetylation_and_deacetylation" title="Histone acetylation and deacetylation">acetylation of nucleosomal histones</a> in the context of chromatin.<sup id="cite_ref-Weaver_3-0" class="reference"><a href="#cite_note-Weaver-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup> They contain a <a href="/wiki/Bromodomain" title="Bromodomain">bromodomain</a>, which helps them recognize and bind to acetylated lysine residues on histone substrates. Gcn5, <a href="/wiki/P300-CBP_coactivator_family" title="P300-CBP coactivator family">p300/CBP</a>, and <a href="/wiki/TAF1" title="TAF1">TAF<sub>II</sub>250</a> are some examples of type A HATs that cooperate with activators to enhance transcription. Type B HATs are located in the <a href="/wiki/Cytoplasm" title="Cytoplasm">cytoplasm</a> and are responsible for acetylating newly synthesized histones prior to their assembly into <a href="/wiki/Nucleosome" title="Nucleosome">nucleosomes</a>. These HATs lack a bromodomain, as their targets are unacetylated. The acetyl groups added by type B HATs to the histones are removed by <a href="/wiki/Histone_deacetylase" title="Histone deacetylase">HDACs</a> once they enter the nucleus and are incorporated into <a href="/wiki/Chromatin" title="Chromatin">chromatin</a>. <a href="/wiki/HAT1" title="HAT1">Hat1</a> is one of the few known examples of a type B HAT.<sup id="cite_ref-Roth_4-0" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Despite this historical classification of HATs, some HAT proteins function in multiple complexes or locations and would thus not easily fit into a particular class.<sup id="cite_ref-Lee0_5-0" class="reference"><a href="#cite_note-Lee0-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Relative_sizes_and_locations_of_important_domains_for_representative_HATs.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/2/2f/Relative_sizes_and_locations_of_important_domains_for_representative_HATs.png/220px-Relative_sizes_and_locations_of_important_domains_for_representative_HATs.png" decoding="async" width="220" height="116" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/2/2f/Relative_sizes_and_locations_of_important_domains_for_representative_HATs.png/330px-Relative_sizes_and_locations_of_important_domains_for_representative_HATs.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/2/2f/Relative_sizes_and_locations_of_important_domains_for_representative_HATs.png/440px-Relative_sizes_and_locations_of_important_domains_for_representative_HATs.png 2x" data-file-width="971" data-file-height="514" /></a><figcaption>Relative sizes and locations of important domains for representative HATs (HAT = catalytic acetyltransferase domain; Bromo = bromodomain; Chromo = chromodomain; Zn = zinc finger domain). The number of amino acid residues in each HAT is indicated at the right in each example.</figcaption></figure> <div class="mw-heading mw-heading3"><h3 id="Gcn5-related_N-acetyltransferases_(GNATs)"><span id="Gcn5-related_N-acetyltransferases_.28GNATs.29"></span>Gcn5-related <i>N</i>-acetyltransferases (GNATs)</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=2" title="Edit section: Gcn5-related N-acetyltransferases (GNATs)"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>HATs can be grouped into several different families based on sequence homology as well as shared structural features and functional roles. The Gcn5-related <i>N</i>-acetyltransferase (GNAT) family includes Gcn5, <a href="/wiki/PCAF" title="PCAF">PCAF</a>, Hat1, <a href="/wiki/ELP3" title="ELP3">Elp3</a>, Hpa2, Hpa3, <a href="/wiki/Activating_transcription_factor_2" title="Activating transcription factor 2">ATF-2</a>, and Nut1. These HATs are generally characterized by the presence of a bromodomain, and they are found to acetylate lysine residues on histones <a href="/wiki/Histone_H2B" title="Histone H2B">H2B</a>, <a href="/wiki/Histone_H3" title="Histone H3">H3</a>,<sup id="cite_ref-6" class="reference"><a href="#cite_note-6"><span class="cite-bracket">[</span>6<span class="cite-bracket">]</span></a></sup> and <a href="/wiki/Histone_H4" title="Histone H4">H4</a>.<sup id="cite_ref-Lee_2-1" class="reference"><a href="#cite_note-Lee-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> All members of the GNAT family are characterized by up to four conserved motifs (A-D) found within the catalytic HAT domain. This includes the most highly conserved motif A, which contains an Arg/Gln-X-X-Gly-X-Gly/Ala sequence that is important for <a href="/wiki/Acetyl-CoA" title="Acetyl-CoA">acetyl-CoA</a> recognition and binding.<sup id="cite_ref-Roth_4-1" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> The C motif is found in most GNATs, but it is not present in the majority of other known HATs.<sup id="cite_ref-Lee0_5-1" class="reference"><a href="#cite_note-Lee0-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> The yeast Gcn5 (general control nonderepressible-5) HAT is one of the best-characterized members of this family. It has four functional domains, including an N-terminal domain, a highly conserved catalytic (HAT) domain, an Ada2 interaction domain, and a C-terminal bromodomain. PCAF (p300/CBP-associated factor) and GCN5 are mammalian GNATs that share a high degree of homology throughout their sequences. These proteins have a 400-residue N-terminal region that is absent in yeast Gcn5, but their HAT functions are evolutionarily conserved with respect to the latter. Hat1 was the first HAT protein to be identified. It is responsible for most of the cytoplasmic HAT activity in yeast, and it binds strongly to histone H4 by virtue of its association with an additional subunit, Hat2. Elp3 is an example of a type A HAT found in yeast. It is part of the <a href="/wiki/RNA_polymerase_II_holoenzyme" title="RNA polymerase II holoenzyme">RNA polymerase II holoenzyme</a> and plays a role in <a href="/wiki/Transcriptional_elongation" class="mw-redirect" title="Transcriptional elongation">transcriptional elongation</a>. </p> <div class="mw-heading mw-heading3"><h3 id="MYST_HATs">MYST HATs</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=3" title="Edit section: MYST HATs"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The MYST family of HATs is named after its four founding members <a href="/wiki/MYST3" class="mw-redirect" title="MYST3">MOZ</a>, Ybf2 (Sas3), Sas2, and <a href="/wiki/KAT5" title="KAT5">Tip60</a>.<sup id="cite_ref-Lee_2-2" class="reference"><a href="#cite_note-Lee-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> Other important members include <a href="/wiki/KAT5" title="KAT5">Esa1</a>, <a href="/wiki/MYST1" class="mw-redirect" title="MYST1">MOF</a>, <a href="/wiki/MYST4" class="mw-redirect" title="MYST4">MORF</a>, and <a href="/wiki/MYST2" class="mw-redirect" title="MYST2">HBO1</a>. These HATs are typically characterized by the presence of <a href="/wiki/Zinc_finger" title="Zinc finger">zinc fingers</a> and <a href="/wiki/Chromodomain" title="Chromodomain">chromodomains</a>, and they are found to acetylate lysine residues on histones <a href="/wiki/Histone_H2A" title="Histone H2A">H2A</a>, H3, and H4. Several MYST family proteins contain zinc fingers as well as the highly conserved motif A found among GNATs that facilitates acetyl-CoA binding.<sup id="cite_ref-Roth_4-2" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> A cysteine-rich region located in the N terminus of the HAT domain of MYST proteins is involved in zinc binding, which is essential for HAT activity.<sup id="cite_ref-Citation9_7-0" class="reference"><a href="#cite_note-Citation9-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> Tip60 (Tat-interactive protein, 60 kDa) was the first human MYST family member to exhibit HAT activity. Sas3 found in yeast is a homolog of MOZ (monocytic leukemia zinc finger protein), which is an <a href="/wiki/Oncogene" title="Oncogene">oncogene</a> found in humans. Esa1 was the first essential HAT to be found in yeast, and MOF is its homolog in fruit flies. The HAT activity of the latter is required for the twofold increased transcription of the male X chromosome (<a href="/wiki/Dosage_compensation" class="mw-redirect" title="Dosage compensation">dosage compensation</a>) in flies. Human HBO1 (HAT bound to ORC1) was the first HAT shown to associate with components of the <a href="/wiki/Origin_recognition_complex" title="Origin recognition complex">origin of replication complex</a>. MORF (MOZ-related factor) exhibits very close homology to MOZ throughout its entire length.<sup id="cite_ref-Lee0_5-2" class="reference"><a href="#cite_note-Lee0-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> It contains an N-terminal repression region that decreases its HAT activity <i>in vitro</i> as well as a C-terminal activation domain that is functional in the absence of the HAT domain. </p> <div class="mw-heading mw-heading3"><h3 id="Others">Others</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=4" title="Edit section: Others"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>In addition to those that are members of the GNAT and MYST families, there are several other proteins found typically in higher eukaryotes that exhibit HAT activity. These include p300/CBP, nuclear receptor coactivators (e.g., ACTR/SRC-1), TAF<sub>II</sub>250, TFIIIC, Rtt109, and <a href="/wiki/CLOCK" title="CLOCK">CLOCK</a>. p300/CBP are <a href="/wiki/Animal" title="Animal">metazoan</a>-specific<sup id="cite_ref-Citation5_8-0" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> and contain several zinc finger regions, a bromodomain, a catalytic (HAT) domain, and regions that interact with other transcription factors.<sup id="cite_ref-Roth_4-3" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Importantly, the HAT domain shows no sequence homology to other known HATs,<sup id="cite_ref-Biochimica_et_Biophysica_Acta_(2009)_9-0" class="reference"><a href="#cite_note-Biochimica_et_Biophysica_Acta_(2009)-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> and it is required for p300/CBP to function in transcriptional activation.<sup id="cite_ref-Roth_4-4" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> In addition, these proteins contain several HAT domain motifs (A, B, and D) that are similar to those of the GNATs. They also possess a novel motif E that is homologous to sequences in the HAT domains of GNATs. TFIIIC is one of the general transcription factors involved in <a href="/wiki/RNA_polymerase_III" title="RNA polymerase III">RNA polymerase III</a>-mediated transcription. Three components in the human protein have been shown to possess independent HAT activity (<a href="/wiki/GTF3C1" title="GTF3C1">hTFIIIC220</a>, <a href="/wiki/GTF3C2" title="GTF3C2">hTFIIIC110</a>, and <a href="/wiki/GTF3C4" title="GTF3C4">hTFIIIC90</a>).<sup id="cite_ref-Citation6_10-0" class="reference"><a href="#cite_note-Citation6-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup> Rtt109 is a <a href="/wiki/Fungus" title="Fungus">fungal</a>-specific HAT that requires association with histone chaperone proteins for activity.<sup id="cite_ref-Citation5_8-1" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> The HAT activities of the human TAF<sub>II</sub>250 and CLOCK coactivators have not been studied as extensively. TAF<sub>II</sub>250 is one of the TBP-associated factor subunits of <a href="/wiki/Transcription_factor_II_D" title="Transcription factor II D">TFIID</a>, and it shares a Gly-X-Gly pattern with Gcn5 that is important for HAT activity.<sup id="cite_ref-Lee0_5-3" class="reference"><a href="#cite_note-Lee0-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> CLOCK is a circadian rhythm master regulator that functions with <a href="/wiki/ARNTL" class="mw-redirect" title="ARNTL">BMAL1</a> to carry out its HAT activity.<sup id="cite_ref-Other1_11-0" class="reference"><a href="#cite_note-Other1-11"><span class="cite-bracket">[</span>11<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading4"><h4 id="Nuclear_receptor_coactivators">Nuclear receptor coactivators</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=5" title="Edit section: Nuclear receptor coactivators"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Three important nuclear receptor coactivators that display HAT activity are <a href="/wiki/Nuclear_receptor_coactivator_1" title="Nuclear receptor coactivator 1">SRC-1</a>, <a href="/wiki/Nuclear_receptor_coactivator_3" title="Nuclear receptor coactivator 3">ACTR</a>, and <a href="/wiki/Nuclear_receptor_coactivator_2" title="Nuclear receptor coactivator 2">TIF-2</a>. Human SRC-1 (steroid receptor coactivator-1) is known to interact with p300/CBP and PCAF, and its HAT domain is located in its C-terminal region. ACTR (also known as RAC3, AIB1, and TRAM-1 in humans) shares significant sequence homology with SRC-1, in particular in the N-terminal and C-terminal (HAT) regions as well as in the receptor and coactivator interaction domains.<sup id="cite_ref-Lee0_5-4" class="reference"><a href="#cite_note-Lee0-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> ACTR also interacts with p300/CBP and PCAF. The former can prevent ACTR from binding to and activating its receptor by acetylating it in its receptor interaction domain. TIF-2 (transcriptional intermediary factor 2; also known as GRIP1) is another nuclear receptor coactivator with HAT activity, and it also interacts with p300/CBP. </p><p>A table summarizing the different families of HATs along with their associated members, parent organisms, multisubunit complexes, histone substrates, and structural features is presented below.<sup id="cite_ref-Lee_2-3" class="reference"><a href="#cite_note-Lee-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Lee0_5-5" class="reference"><a href="#cite_note-Lee0-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Citation5_8-2" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Citation6_10-1" class="reference"><a href="#cite_note-Citation6-10"><span class="cite-bracket">[</span>10<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Citation2_12-0" class="reference"><a href="#cite_note-Citation2-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Citation7_13-0" class="reference"><a href="#cite_note-Citation7-13"><span class="cite-bracket">[</span>13<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Citation8_14-0" class="reference"><a href="#cite_note-Citation8-14"><span class="cite-bracket">[</span>14<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Lee1_15-0" class="reference"><a href="#cite_note-Lee1-15"><span class="cite-bracket">[</span>15<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Lee2_16-0" class="reference"><a href="#cite_note-Lee2-16"><span class="cite-bracket">[</span>16<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Lee3_17-0" class="reference"><a href="#cite_note-Lee3-17"><span class="cite-bracket">[</span>17<span class="cite-bracket">]</span></a></sup> </p> <table class="wikitable" border="3" style="text-align: center;"> <tbody><tr> <th>Family </th> <th>Members</th> <th>Organism</th> <th>Associated complexes</th> <th>Substrate specificity</th> <th>Structural features </th></tr> <tr> <td rowspan="10"><b>GNAT</b> </td> <td>Gcn5</td> <td><i><a href="/wiki/Saccharomyces_cerevisiae" title="Saccharomyces cerevisiae">S. cerevisiae</a></i></td> <td>SAGA, SLIK (SALSA), ADA, <p>HAT-A2 </p> </td> <td>H2B, H3, (H4)</td> <td>Bromodomain </td></tr> <tr> <td>GCN5</td> <td><i><a href="/wiki/Drosophila_melanogaster" title="Drosophila melanogaster">D. melanogaster</a></i></td> <td>SAGA, ATAC</td> <td>H3, H4</td> <td>Bromodomain </td></tr> <tr> <td>GCN5</td> <td><i><a href="/wiki/Human" title="Human">H. sapiens</a></i></td> <td>STAGA, TFTC</td> <td>H3, (H4, H2B)</td> <td>Bromodomain </td></tr> <tr> <td>PCAF</td> <td><i>H. sapiens</i></td> <td>PCAF</td> <td>H3, H4</td> <td>Bromodomain </td></tr> <tr> <td>Hat1</td> <td><i>S. cerevisiae<br />H. sapiens</i></td> <td>HAT-B, NuB4, HAT-A3</td> <td>H4, (H2A)</td> <td> </td></tr> <tr> <td>Elp3</td> <td><i>S. cerevisiae</i></td> <td>Elongator</td> <td>H3, H4, (H2A, H2B)</td> <td> </td></tr> <tr> <td>Hpa2</td> <td><i>S. cerevisiae</i></td> <td>HAT-B</td> <td>H3, H4</td> <td> </td></tr> <tr> <td>Hpa3</td> <td><i>S. cerevisiae</i></td> <td></td> <td>H3, H4</td> <td> </td></tr> <tr> <td>ATF-2</td> <td><i>S. cerevisiae<br />H. sapiens</i></td> <td></td> <td>H2B, H4</td> <td> </td></tr> <tr> <td>Nut1</td> <td><i>S. cerevisiae</i></td> <td><a href="/wiki/Mediator_(coactivator)" title="Mediator (coactivator)">Mediator</a></td> <td>H3, H4</td> <td> </td></tr> <tr> <td rowspan="8"><b>MYST</b> </td> <td>Esa1</td> <td><i>S. cerevisiae</i></td> <td>NuA4, piccolo <a href="/wiki/NuA4_histone_acetyltransferase_complex" title="NuA4 histone acetyltransferase complex">NuA4</a></td> <td>H2A, H4, (H2B, H3)</td> <td>Chromodomain </td></tr> <tr> <td>Sas2</td> <td><i>S. cerevisiae</i></td> <td>SAS, <a href="/wiki/NuA4_histone_acetyltransferase_complex" title="NuA4 histone acetyltransferase complex">NuA4</a></td> <td>H4, (H2A, H3)</td> <td> </td></tr> <tr> <td>Sas3 (Ybf2)</td> <td><i>S. cerevisiae</i></td> <td>NuA3</td> <td>H3, (H4, H2A)</td> <td> </td></tr> <tr> <td>Tip60</td> <td><i>H. sapiens</i></td> <td>Tip60, <a href="/wiki/NuA4_histone_acetyltransferase_complex" title="NuA4 histone acetyltransferase complex">NuA4</a></td> <td>H2A, H4, (H3)</td> <td>Chromodomain </td></tr> <tr> <td>MOF</td> <td><i>D. melanogaster</i></td> <td>MSL</td> <td>H4, (H2A, H3)</td> <td>Chromodomain </td></tr> <tr> <td>MOZ</td> <td><i>H. sapiens</i></td> <td>MSL</td> <td>H3, H4</td> <td> </td></tr> <tr> <td>MORF</td> <td><i>H. sapiens</i></td> <td>MSL</td> <td>H3, H4</td> <td> </td></tr> <tr> <td>HBO1</td> <td><i>H. sapiens</i></td> <td>ORC</td> <td>H3, H4</td> <td> </td></tr> <tr> <td rowspan="2"><b>p300/CBP</b> </td> <td>p300</td> <td><i>H. sapiens</i></td> <td></td> <td>H2A, H2B, H3, H4</td> <td>Bromodomain </td></tr> <tr> <td>CBP</td> <td><i>H. sapiens</i></td> <td></td> <td>H2A, H2B, H3, H4</td> <td>Bromodomain </td></tr> <tr> <td rowspan="3"><b>SRC</b> <p><b>(nuclear receptor coactivators)</b> </p> </td> <td>SRC-1</td> <td><i>H. sapiens</i></td> <td>ACTR/SRC-1</td> <td>H3, H4</td> <td> </td></tr> <tr> <td>ACTR (RAC3, AIB1, TRAM-1, SRC-3)</td> <td><i>H. sapiens</i></td> <td>ACTR/SRC-1</td> <td>H3, H4</td> <td> </td></tr> <tr> <td>TIF-2 (GRIP1)</td> <td><i>H. sapiens</i></td> <td></td> <td>H3, H4</td> <td> </td></tr> <tr> <td rowspan="4"><b>Other</b> </td> <td>TAF<sub>II</sub>250 (TAF1)</td> <td><i>S. cerevisiae<br />H. sapiens</i></td> <td>TFIID</td> <td>H3, H4, (H2A)</td> <td>Bromodomain </td></tr> <tr> <td>TFIIIC (p220, p110, p90)</td> <td><i>H. sapiens</i></td> <td>TFIIIC</td> <td>H2A, H3, H4</td> <td> </td></tr> <tr> <td>Rtt109</td> <td><i>S. cerevisiae</i></td> <td>Histone chaperones</td> <td>H3</td> <td> </td></tr> <tr> <td>CLOCK</td> <td><i>H. sapiens</i></td> <td></td> <td>H3, H4</td> <td> </td></tr></tbody></table> <div class="mw-heading mw-heading2"><h2 id="Overall_structure">Overall structure</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=6" title="Edit section: Overall structure"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Crystal_structure_of_Tetrahymena_Gcn5_with_bound_coenzyme_A_and_histone_H3_peptide.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/1/19/Crystal_structure_of_Tetrahymena_Gcn5_with_bound_coenzyme_A_and_histone_H3_peptide.png/220px-Crystal_structure_of_Tetrahymena_Gcn5_with_bound_coenzyme_A_and_histone_H3_peptide.png" decoding="async" width="220" height="177" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/1/19/Crystal_structure_of_Tetrahymena_Gcn5_with_bound_coenzyme_A_and_histone_H3_peptide.png/330px-Crystal_structure_of_Tetrahymena_Gcn5_with_bound_coenzyme_A_and_histone_H3_peptide.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/1/19/Crystal_structure_of_Tetrahymena_Gcn5_with_bound_coenzyme_A_and_histone_H3_peptide.png/440px-Crystal_structure_of_Tetrahymena_Gcn5_with_bound_coenzyme_A_and_histone_H3_peptide.png 2x" data-file-width="571" data-file-height="460" /></a><figcaption>Crystal structure of Tetrahymena Gcn5 with bound coenzyme A and histone H3 peptide (PDB 1QSN). The central core (green), flanking N- and C-terminal segments (blue), coenzyme A (orange), and histone peptide (red) are shown.</figcaption></figure> <p>In general, HATs are characterized by a structurally conserved core region made up of a three-stranded <a href="/wiki/Beta_sheet" title="Beta sheet">β-sheet</a> followed by a long <a href="/wiki/Alpha_helix" title="Alpha helix">α-helix</a> parallel to and spanning one side of it.<sup id="cite_ref-Citation9_7-1" class="reference"><a href="#cite_note-Citation9-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Citation5_8-3" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> The core region, which corresponds to motifs A, B, and D of the GNAT proteins,<sup id="cite_ref-Roth_4-5" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> is flanked on opposite sides by N- and C-terminal α/β segments that are structurally unique for a given HAT family.<sup id="cite_ref-Citation9_7-2" class="reference"><a href="#cite_note-Citation9-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Citation5_8-4" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> The central core and the flanking segments together form a cleft over the former, which is where histone substrates can bind prior to catalysis.<sup id="cite_ref-Citation5_8-5" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> While the central core domain (motif A in GNATs) is involved in acetyl-CoA binding and catalysis, the N- and C-terminal segments assist in binding histone substrates.<sup id="cite_ref-Citation9_7-3" class="reference"><a href="#cite_note-Citation9-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> Unique features related to the sequence and/or structure of the N- and C-terminal regions for different HAT families may help to explain some observed differences among HATs in histone substrate specificity. CoA binding has been observed to widen the histone binding groove in the central core by moving the C-terminal segment of Gcn5 outward. In addition, since contacts between CoA and protein facilitate the formation of favorable histone-protein contacts, it is likely that CoA binding precedes histone binding <i>in vivo</i>. </p> <div class="mw-heading mw-heading3"><h3 id="GNAT_and_MYST_families">GNAT and MYST families</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=7" title="Edit section: GNAT and MYST families"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>HATs in the GNAT family are most notably characterized by an approximately 160-residue HAT domain and a C-terminal bromodomain, which binds to acetylated lysine residues.<sup id="cite_ref-Citation9_7-4" class="reference"><a href="#cite_note-Citation9-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> Those in the MYST family have HAT domains that are about 250 residues in length. Many MYST proteins also contain a cysteine-rich, zinc-binding domain within the HAT region in addition to an N-terminal chromodomain, which binds to <a href="/wiki/Methyllysine" title="Methyllysine">methylated lysine residues</a>. </p><p>On a broader scale, the structures of the catalytic domains of GNAT proteins (Gcn5, PCAF) exhibit a mixed α/β globular fold with a total of five α-helices and six β-strands.<sup id="cite_ref-Roth_4-6" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> The overall topology resembles a <a href="/wiki/Vise" title="Vise">vise</a>, with the central core of the protein at the base and the N- and C-terminal segments on the sides. </p> <div class="mw-heading mw-heading3"><h3 id="p300/CBP_family"><span id="p300.2FCBP_family"></span>p300/CBP family</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=8" title="Edit section: p300/CBP family"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The p300/CBP HATs have larger HAT domains (about 500 residues) than those present in the GNAT and MYST families.<sup id="cite_ref-Citation9_7-5" class="reference"><a href="#cite_note-Citation9-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> They also contain a bromodomain as well as three cysteine/histidine-rich domains that are thought to mediate interactions with other proteins. The structure of p300/CBP is characterized by an elongated globular domain, which contains a seven-stranded β-sheet in the center that is surrounded by nine α-helices and several loops.<sup id="cite_ref-Biochimica_et_Biophysica_Acta_(2009)_9-1" class="reference"><a href="#cite_note-Biochimica_et_Biophysica_Acta_(2009)-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> The structure of the central core region associated with acetyl-CoA binding is conserved with respect to GNAT and MYST HATs, but there are many structural differences in the regions flanking this central core. Overall, the structural data is consistent with the fact that p300/CBP HATs are more promiscuous than GNAT and MYST HATs with respect to substrate binding. </p> <div class="mw-heading mw-heading3"><h3 id="Rtt109">Rtt109</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=9" title="Edit section: Rtt109"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The structure of Rtt109 is very similar to that of p300, despite there only being 7% sequence identity between the two proteins.<sup id="cite_ref-Biochimica_et_Biophysica_Acta_(2009)_9-2" class="reference"><a href="#cite_note-Biochimica_et_Biophysica_Acta_(2009)-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> There is a seven-stranded β-sheet that is surrounded by α-helices as well as a loop that is involved in acetyl-CoA substrate binding. Despite the conserved structure, Rtt109 and p300/CBP are functionally unique. For instance, the substrate binding site of the former is more similar to that of the GNAT and MYST HATs. In addition, the residues in the active site of each enzyme are distinct, which suggests that they employ different catalytic mechanisms for acetyl group transfer. </p> <div class="mw-heading mw-heading2"><h2 id="Catalytic_mechanisms">Catalytic mechanisms</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=10" title="Edit section: Catalytic mechanisms"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The basic mechanism catalyzed by HATs involves the transfer of an acetyl group from acetyl-CoA to the ε-amino group of a target lysine side-chain within a histone.<sup id="cite_ref-Citation5_8-6" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> Different families of HATs employ unique strategies in order to effect such a transformation. </p> <figure class="mw-default-size" typeof="mw:File/Thumb"><a href="/wiki/File:Catalytic_mechanisms_of_GNAT_and_MYST_family_HATs..png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/9/9a/Catalytic_mechanisms_of_GNAT_and_MYST_family_HATs..png/220px-Catalytic_mechanisms_of_GNAT_and_MYST_family_HATs..png" decoding="async" width="220" height="141" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/9/9a/Catalytic_mechanisms_of_GNAT_and_MYST_family_HATs..png/330px-Catalytic_mechanisms_of_GNAT_and_MYST_family_HATs..png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/9/9a/Catalytic_mechanisms_of_GNAT_and_MYST_family_HATs..png/440px-Catalytic_mechanisms_of_GNAT_and_MYST_family_HATs..png 2x" data-file-width="1317" data-file-height="845" /></a><figcaption>Catalytic mechanisms of GNAT and MYST family HATs. (A) General mechanism of GNAT HATs. (B) General mechanism of MYST HATs.</figcaption></figure> <div class="mw-heading mw-heading3"><h3 id="GNAT_family">GNAT family</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=11" title="Edit section: GNAT family"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Members of the GNAT family have a conserved glutamate residue that acts as a general base for catalyzing the nucleophilic attack of the lysine amine on the acetyl-CoA thioester bond.<sup id="cite_ref-Citation5_8-7" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> These HATs use an ordered sequential bi-bi mechanism wherein both substrates (acetyl-CoA and histone) must bind to form a <a href="/wiki/Ternary_complex" title="Ternary complex">ternary complex</a> with the enzyme before catalysis can occur. Acetyl-CoA binds first, followed by the histone substrate. A conserved glutamate residue (Glu173 in yeast Gcn5) activates a water molecule for removal of a proton from the amine group on lysine, which activates it for direct nucleophilic attack on the carbonyl carbon of enzyme-bound acetyl-CoA. After the reaction, the acetylated histone is released first followed by CoA.<sup id="cite_ref-Roth_4-7" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Citation5_8-8" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="MYST_family">MYST family</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=12" title="Edit section: MYST family"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Studies of yeast Esa1 from the MYST family of HATs have revealed a <a href="/wiki/Ping-pong_mechanism" class="mw-redirect" title="Ping-pong mechanism">ping-pong mechanism</a> involving conserved glutamate and cysteine residues.<sup id="cite_ref-Other2_18-0" class="reference"><a href="#cite_note-Other2-18"><span class="cite-bracket">[</span>18<span class="cite-bracket">]</span></a></sup> The first part of the reaction involves the formation of a covalent intermediate in which a cysteine residue becomes acetylated following nucleophilic attack of this residue on the carbonyl carbon of acetyl-CoA. Then, a glutamate residue acts as a general base to facilitate transfer of the acetyl group from the cysteine to the histone substrate in a manner analogous to the mechanism used by GNATs. When Esa1 is assembled in the piccolo <a href="/wiki/NuA4_histone_acetyltransferase_complex" title="NuA4 histone acetyltransferase complex">NuA4</a> complex, it loses its dependence on the cysteine residue for catalysis, which suggests that the reaction may proceed via a ternary bi-bi mechanism when the enzyme is part of a physiologically relevant multiprotein complex. </p> <div class="mw-heading mw-heading3"><h3 id="p300/CBP_family_2"><span id="p300.2FCBP_family_2"></span>p300/CBP family</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=13" title="Edit section: p300/CBP family"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>In human p300, Tyr1467 acts as a general acid and Trp1436 helps orient the target lysine residue of the histone substrate into the active site.<sup id="cite_ref-Citation5_8-9" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> These two residues are highly conserved within the p300/CBP HAT family and, unlike enzymes in the GNAT and MYST families, p300 does not employ a general base for catalysis. Rather, it is likely that members of the p300/CBP family use a Theorell-Chance (i.e., “hit-and-run”) acetyl transfer mechanism. </p> <div class="mw-heading mw-heading3"><h3 id="Rtt109_2">Rtt109</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=14" title="Edit section: Rtt109"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Rtt109 is likely to employ a mechanism that is different from that of the other HATs.<sup id="cite_ref-Biochimica_et_Biophysica_Acta_(2009)_9-3" class="reference"><a href="#cite_note-Biochimica_et_Biophysica_Acta_(2009)-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> The yeast enzyme has very low catalytic activity in the absence of the histone chaperone proteins <a href="/wiki/ASF1_like_histone_chaperone" title="ASF1 like histone chaperone">Asf1</a> and Vps75, which may be involved in delivering histone substrates to the enzyme for acetylation.<sup id="cite_ref-Citation5_8-10" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> Moreover, a general acid or base have not yet been identified for this HAT. </p> <div class="mw-heading mw-heading2"><h2 id="Substrate_binding_and_specificity">Substrate binding and specificity</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=15" title="Edit section: Substrate binding and specificity"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The structures of several HAT domains bound to acetyl-CoA and histone substrate peptides reveal that the latter bind across a groove on the protein that is formed by the central core region at the base and is flanked on opposite sides by the variable N- and C-terminal segments that mediate the majority of the interactions with the substrate peptide.<sup id="cite_ref-Citation5_8-11" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> It is likely that these variable regions are at least in part responsible for the observed specificity of different HATs for various histone substrates. </p><p>Members of the GNAT and MYST families as well as Rtt109 exhibit greater substrate selectivity than p300/CBP, which is rather promiscuous with regard to substrate binding.<sup id="cite_ref-Citation5_8-12" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> Whereas it appears that only three to five residues on either side of the lysine to be acetylated are necessary for effective substrate binding and catalysis by members of the GNAT and p300/CBP families, more distal regions of the substrate may be important for efficient acetylation by MYST family HATs.<sup id="cite_ref-Current_Opinion_in_Structural_Biology_(2008)_19-0" class="reference"><a href="#cite_note-Current_Opinion_in_Structural_Biology_(2008)-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Lysine_selectivity">Lysine selectivity</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=16" title="Edit section: Lysine selectivity"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Different HATs, usually in the context of multisubunit complexes, have been shown to acetylate specific lysine residues in histones. </p> <div class="mw-heading mw-heading4"><h4 id="GNAT_family_2">GNAT family</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=17" title="Edit section: GNAT family"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Gcn5 cannot acetylate nucleosomal histones in the absence of other protein factors.<sup id="cite_ref-Lee0_5-6" class="reference"><a href="#cite_note-Lee0-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> In the context of complexes like SAGA and ADA, however, Gcn5 is able to acetylate H3K14 among other sites within histones H2B, H3, and H4 (e.g., H3K9, H3K36, H4K8, H4K16).<sup id="cite_ref-Weaver_3-1" class="reference"><a href="#cite_note-Weaver-3"><span class="cite-bracket">[</span>3<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Roth_4-8" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Citation9_7-6" class="reference"><a href="#cite_note-Citation9-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Current_Opinion_in_Structural_Biology_(2008)_19-1" class="reference"><a href="#cite_note-Current_Opinion_in_Structural_Biology_(2008)-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> Both Gcn5 and PCAF have the strongest site preference for H3K14, either as a free histone or within a nucleosome.<sup id="cite_ref-Roth_4-9" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Citation9_7-7" class="reference"><a href="#cite_note-Citation9-7"><span class="cite-bracket">[</span>7<span class="cite-bracket">]</span></a></sup> Hat1 acetylates H4K5 and H4K12, and Hpa2 acetylates H3K14 <i>in vitro</i>.<sup id="cite_ref-Roth_4-10" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Lee0_5-7" class="reference"><a href="#cite_note-Lee0-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading4"><h4 id="MYST_family_2">MYST family</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=18" title="Edit section: MYST family"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>In flies, acetylation of H4K16 on the male X chromosome by MOF in the context of the MSL complex is correlated with transcriptional upregulation as a mechanism for dosage compensation in these organisms.<sup id="cite_ref-Lee_2-4" class="reference"><a href="#cite_note-Lee-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> In humans, the MSL complex carries out the majority of genome-wide H4K16 acetylation. In the context of their cognate complexes, Sas2 (SAS) and Esa1 (NuA4) also carry out acetylation of H4K16, in particular in the <a href="/wiki/Telomere" title="Telomere">telomere</a> regions of chromosomes. Sas2 is also observed to acetylate H3K14 <i>in vitro</i> on free histones.<sup id="cite_ref-Citation2_12-1" class="reference"><a href="#cite_note-Citation2-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> Esa1 can also acetylate H3K14 <i>in vitro</i> on free histones as well as H2AK5, H4K5, H4K8, and H4K12 either <i>in vitro</i> or <i>in vivo</i> on nucleosomal histones. H2AK7 and H2BK16 are also observed to be acetylated by Esa1 <i>in vivo</i>. Notably, neither Sas2 nor Esa1 can acetylate nucleosomal histones <i>in vitro</i> as a free enzyme. This happens to be the case as well for Sas3, which is observed to acetylate H3K9 and H3K14 <i>in vivo</i> as well as lysine residues on H2A and H4. MOZ can also acetylate H3K14.<sup id="cite_ref-Current_Opinion_in_Structural_Biology_(2008)_19-2" class="reference"><a href="#cite_note-Current_Opinion_in_Structural_Biology_(2008)-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading4"><h4 id="Others_2">Others</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=19" title="Edit section: Others"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>p300/CBP acetylate all four nucleosomal core histones equally well.<sup id="cite_ref-Roth_4-11" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> <i>In vitro</i>, they have been observed to acetylate H2AK5, H2BK12, H2BK15, H3K14, H3K18, H4K5, and H4K8.<sup id="cite_ref-Lee0_5-8" class="reference"><a href="#cite_note-Lee0-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> SRC-1 acetylates H3K9 and H3K14, TAF<sub>II</sub>230 (Drosophila homolog of human TAF<sub>II</sub>250) acetylates H3K14, and Rtt109 acetylates H3K9, H3K23,<sup id="cite_ref-Current_Opinion_in_Structural_Biology_(2008)_19-3" class="reference"><a href="#cite_note-Current_Opinion_in_Structural_Biology_(2008)-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> and H3K56 in the presence of either Asf1 or Vps75.<sup id="cite_ref-Biochimica_et_Biophysica_Acta_(2009)_9-4" class="reference"><a href="#cite_note-Biochimica_et_Biophysica_Acta_(2009)-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Non-histone_substrates_(in_vitro)"><span id="Non-histone_substrates_.28in_vitro.29"></span>Non-histone substrates (<i>in vitro</i>)</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=20" title="Edit section: Non-histone substrates (in vitro)"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>In addition to the core histones, certain HATs acetylate a number of other cellular proteins including <a href="/wiki/Activator_(genetics)" title="Activator (genetics)">transcriptional activators</a>, <a href="/wiki/General_transcription_factor" title="General transcription factor">basal transcription factors</a>, structural proteins, <a href="/wiki/Polyamine" title="Polyamine">polyamines</a>, and proteins involved in nuclear import.<sup id="cite_ref-Roth_4-12" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Acetylation of these proteins can alter their ability to interact with their cognate DNA and/or protein substrates. The idea that acetylation can affect protein function in this manner has led to inquiry regarding the role of acetyltransferases in signal transduction pathways and whether an appropriate analogy to <a href="/wiki/Protein_kinase" title="Protein kinase">kinases</a> and phosphorylation events can be made in this respect. </p> <div class="mw-heading mw-heading4"><h4 id="PCAF">PCAF</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=21" title="Edit section: PCAF"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>PCAF and p300/CBP are the main HATs that have been observed to acetylate a number of non-histone proteins. For PCAF, these include the non-histone chromatin (<a href="/wiki/High-mobility_group" title="High-mobility group">high-mobility group (HMG)</a>) proteins <a href="/wiki/HMGN2" title="HMGN2">HMG-N2/HMG17</a> and <a href="/wiki/HMGA1" title="HMGA1">HMG-I(Y)</a>, the transcriptional activators <a href="/wiki/P53" title="P53">p53</a>, <a href="/wiki/MyoD" title="MyoD">MyoD</a>, <a href="/wiki/E2F" title="E2F">E2F(1-3)</a>, and <a href="/wiki/Tat_(HIV)" title="Tat (HIV)">HIV Tat</a>, and the general transcription factors <a href="/wiki/Transcription_factor_II_E" title="Transcription factor II E">TFIIE</a> and <a href="/wiki/Transcription_factor_II_F" title="Transcription factor II F">TFIIF</a>.<sup id="cite_ref-Lee0_5-9" class="reference"><a href="#cite_note-Lee0-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> Other proteins include <a href="/wiki/CIITA" title="CIITA">CIITA</a>, Brm (chromatin remodeler), <a href="/wiki/NF-%CE%BAB" title="NF-κB">NF-κB</a> (p65), <a href="/wiki/TAL1" title="TAL1">TAL1/SCL</a>, <a href="/wiki/NeuroD" title="NeuroD">Beta2/NeuroD</a>, <a href="/wiki/Ccaat-enhancer-binding_proteins" class="mw-redirect" title="Ccaat-enhancer-binding proteins">C/EBPβ</a>, <a href="/wiki/IRF2" title="IRF2">IRF2</a>, <a href="/wiki/IRF7" title="IRF7">IRF7</a>, <a href="/wiki/YY1" title="YY1">YY1</a>, <a href="/wiki/KLF13" title="KLF13">KLF13</a>, <a href="/wiki/EVI1" class="mw-redirect" title="EVI1">EVI1</a>, AME, <a href="/wiki/ETV1" title="ETV1">ER81</a>, and the <a href="/wiki/Androgen_receptor" title="Androgen receptor">androgen receptor (AR)</a>.<sup id="cite_ref-BioEssays_(2004)_20-0" class="reference"><a href="#cite_note-BioEssays_(2004)-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> PCAF has also been observed to acetylate <a href="/wiki/C-myc" class="mw-redirect" title="C-myc">c-MYC</a>, <a href="/wiki/GATA2" title="GATA2">GATA-2</a>, <a href="/wiki/Retinoblastoma_protein" title="Retinoblastoma protein">retinoblastoma (Rb)</a>, <a href="/wiki/Ku70" title="Ku70">Ku70</a>, and <a href="/wiki/Adenovirus_early_region_1A" title="Adenovirus early region 1A">E1A</a> adenovirus protein.<sup id="cite_ref-Gene_(2005)_21-0" class="reference"><a href="#cite_note-Gene_(2005)-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> It can also autoacetylate, which facilitates intramolecular interactions with its bromodomain that may be involved in the regulation of its HAT activity.<sup id="cite_ref-Roth_4-13" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading4"><h4 id="p300/CBP"><span id="p300.2FCBP"></span>p300/CBP</h4><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=22" title="Edit section: p300/CBP"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>p300/CBP have many non-histone substrates, including the non-histone chromatin proteins <a href="/wiki/HMGB1" title="HMGB1">HMG1</a>, <a href="/wiki/HMGN1" title="HMGN1">HMG-N1/HMG14</a>, and HMG-I(Y), the transcriptional activators p53, <a href="/wiki/MYB_(gene)" title="MYB (gene)">c-Myb</a>, <a href="/wiki/GATA1" title="GATA1">GATA-1</a>, <a href="/wiki/KLF1" title="KLF1">EKLF</a>, <a href="/wiki/TCF/LEF_family" title="TCF/LEF family">TCF</a>, and HIV Tat, the nuclear receptor coactivators ACTR, SRC-1, and TIF-2, and the general transcription factors TFIIE and TFIIF.<sup id="cite_ref-Lee0_5-10" class="reference"><a href="#cite_note-Lee0-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> Other substrates include the transcription factors Sp1, <a href="/wiki/KLF5" title="KLF5">KLF5</a>, <a href="/wiki/FOXO1" class="mw-redirect" title="FOXO1">FOXO1</a>, <a href="/wiki/MEF2C" title="MEF2C">MEF2C</a>, <a href="/wiki/SRY" class="mw-redirect" title="SRY">SRY</a>, <a href="/wiki/GATA4" title="GATA4">GATA-4</a>, and <a href="/wiki/Hepatocyte_nuclear_factors" title="Hepatocyte nuclear factors">HNF-6</a>,<sup id="cite_ref-Citation2_12-2" class="reference"><a href="#cite_note-Citation2-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> <a href="/wiki/HMGB2" title="HMGB2">HMG-B2</a>,<sup id="cite_ref-Gene_(2005)_21-1" class="reference"><a href="#cite_note-Gene_(2005)-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> <a href="/wiki/STAT3" title="STAT3">STAT3</a>, the androgen and <a href="/wiki/Estrogen_receptor_alpha" title="Estrogen receptor alpha">estrogen (α)</a> receptors, GATA-2, <a href="/wiki/GATA3" title="GATA3">GATA-3</a>, MyoD, E2F(1-3), <a href="/wiki/P73" title="P73">p73</a>α, retinoblastoma (Rb), NF-κB (p50, p65), <a href="/wiki/Mothers_against_decapentaplegic_homolog_7" title="Mothers against decapentaplegic homolog 7">Smad7</a>, <a href="/wiki/Importin_%CE%B1" title="Importin α">importin-α</a>, Ku70, <a href="/wiki/YAP1" title="YAP1">YAP1</a>,<sup id="cite_ref-22" class="reference"><a href="#cite_note-22"><span class="cite-bracket">[</span>22<span class="cite-bracket">]</span></a></sup> E1A adenovirus protein, and S-HDAg (<a href="/wiki/Hepatitis_D" title="Hepatitis D">hepatitis delta virus</a> small delta antigen).<sup id="cite_ref-Gene_(2005)_21-2" class="reference"><a href="#cite_note-Gene_(2005)-21"><span class="cite-bracket">[</span>21<span class="cite-bracket">]</span></a></sup> p300/CBP have also been observed to acetylate <a href="/wiki/Beta-catenin" class="mw-redirect" title="Beta-catenin">β-catenin</a>, <a href="/wiki/NRIP1" title="NRIP1">RIP140</a>, <a href="/wiki/Proliferating_cell_nuclear_antigen" title="Proliferating cell nuclear antigen">PCNA</a>, the DNA metabolic enzymes <a href="/wiki/Flap_structure-specific_endonuclease_1" title="Flap structure-specific endonuclease 1">flap endonuclease-1</a>, <a href="/wiki/Thymine-DNA_glycosylase" title="Thymine-DNA glycosylase">thymine DNA glycosylase</a>, and <a href="/wiki/Werner_syndrome_ATP-dependent_helicase" class="mw-redirect" title="Werner syndrome ATP-dependent helicase">Werner syndrome DNA helicase</a>, <a href="/wiki/STAT6" title="STAT6">STAT6</a>, <a href="/wiki/RUNX1" title="RUNX1">Runx1 (AML1)</a>, UBF, Beta2/NeuroD, <a href="/wiki/CREB" title="CREB">CREB</a>, <a href="/wiki/C-jun" class="mw-redirect" title="C-jun">c-Jun</a>, C/EBPβ, <a href="/wiki/NFE2" title="NFE2">NF-E2</a>, <a href="/wiki/Sterol_regulatory_element-binding_protein" title="Sterol regulatory element-binding protein">SREBP</a>, IRF2, <a href="/wiki/Sp3_transcription_factor" title="Sp3 transcription factor">Sp3</a>, YY1, KLF13, EVI1, <a href="/wiki/BCL6" title="BCL6">BCL6</a>, <a href="/wiki/Hepatocyte_nuclear_factors" title="Hepatocyte nuclear factors">HNF-4</a>, ER81 and <a href="/wiki/FOXO4" title="FOXO4">FOXO4 (AFX)</a>.<sup id="cite_ref-BioEssays_(2004)_20-1" class="reference"><a href="#cite_note-BioEssays_(2004)-20"><span class="cite-bracket">[</span>20<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Multisubunit_HAT_complexes">Multisubunit HAT complexes</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=23" title="Edit section: Multisubunit HAT complexes"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The formation of multisubunit complexes has been observed to modulate the substrate specificity of HATs.<sup id="cite_ref-Citation2_12-3" class="reference"><a href="#cite_note-Citation2-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> In general, while recombinant HATs are able to acetylate free histones, HATs can acetylate nucleosomal histones only when they are in their respective <i>in vivo</i> HAT complexes.<sup id="cite_ref-Lee0_5-11" class="reference"><a href="#cite_note-Lee0-5"><span class="cite-bracket">[</span>5<span class="cite-bracket">]</span></a></sup> Some of the proteins that associate with HATs in these complexes function by targeting the HAT complex to nucleosomes at specific regions in the <a href="/wiki/Genome" title="Genome">genome</a>.<sup id="cite_ref-Lee_2-5" class="reference"><a href="#cite_note-Lee-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Citation2_12-4" class="reference"><a href="#cite_note-Citation2-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> For instance, it has been observed that HAT complexes (e.g. SAGA, NuA3) often use <a href="/wiki/Histone_methylation" title="Histone methylation">methylated histones</a> as docking sites so that the catalytic HAT subunit can carry out histone acetylation more effectively.<sup id="cite_ref-Lee_2-6" class="reference"><a href="#cite_note-Lee-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup> </p><p>In addition, the formation of multisubunit HAT complexes influences the lysine specificity of HATs.<sup id="cite_ref-Citation2_12-5" class="reference"><a href="#cite_note-Citation2-12"><span class="cite-bracket">[</span>12<span class="cite-bracket">]</span></a></sup> The specific lysine residues that a given HAT acetylates may become either broader or more restricted in scope upon association with its respective complex. For example, the lysine specificity of MYST family HATs toward their histone substrates becomes more restricted when they associate with their complexes. In contrast, Gcn5 acquires the ability to acetylate multiple sites in both histones H2B and H3 when it joins other subunits to form the SAGA and ADA complexes.<sup id="cite_ref-Roth_4-14" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Moreover, the acetylation site specificity of Rtt109 is dictated by its association with either Vps75 or Asf1.<sup id="cite_ref-Current_Opinion_in_Structural_Biology_(2008)_19-4" class="reference"><a href="#cite_note-Current_Opinion_in_Structural_Biology_(2008)-19"><span class="cite-bracket">[</span>19<span class="cite-bracket">]</span></a></sup> When in complex with the former, Rtt109 acetylates H3K9 and H3K27, but, when in complex with the latter, it preferentially acetylates H3K56.<sup id="cite_ref-Citation5_8-13" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Regulation_of_HAT_activity">Regulation of HAT activity</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=24" title="Edit section: Regulation of HAT activity"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The catalytic activity of HATs is regulated by two types of mechanisms: (1) interaction with regulatory protein subunits and (2) autoacetylation.<sup id="cite_ref-Citation5_8-14" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> A given HAT may be regulated in multiple ways, and the same effector may actually lead to different outcomes under different conditions.<sup id="cite_ref-Roth_4-15" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Although it is clear that the association of HATs with multiprotein complexes provides a mechanism for the regulation of both HAT activity and substrate specificity <i>in vivo</i>, the molecular basis for how this actually occurs is still largely unknown.<sup id="cite_ref-Citation5_8-15" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> However, data suggests that associated subunits may contribute to catalysis at least in part by facilitating productive binding of the HAT complex to its native histone substrates. </p><p>The MYST family of HATs, p300/CBP, and Rtt109 have all been shown to be regulated by autoacetylation.<sup id="cite_ref-Citation5_8-16" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup> Human MOF as well as yeast Esa1 and Sas2 are autoacetylated at a conserved active site lysine residue, and this modification is required for their function <i>in vivo</i>. Human p300 contains a highly basic loop embedded in the middle of its HAT domain that is hyperacetylated in the active form of the enzyme.<sup id="cite_ref-Citation5_8-17" class="reference"><a href="#cite_note-Citation5-8"><span class="cite-bracket">[</span>8<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Biochimica_et_Biophysica_Acta_(2009)_9-5" class="reference"><a href="#cite_note-Biochimica_et_Biophysica_Acta_(2009)-9"><span class="cite-bracket">[</span>9<span class="cite-bracket">]</span></a></sup> It has been proposed that, upon autoacetylation, this loop is released from the electronegative substrate binding site where it sits in the inactive HAT.<sup id="cite_ref-Other3_23-0" class="reference"><a href="#cite_note-Other3-23"><span class="cite-bracket">[</span>23<span class="cite-bracket">]</span></a></sup> Acetylation of yeast Rtt109 at Lys290 is also required for it to exhibit full catalytic activity.<sup id="cite_ref-Other4_24-0" class="reference"><a href="#cite_note-Other4-24"><span class="cite-bracket">[</span>24<span class="cite-bracket">]</span></a></sup> Some HATs are also inhibited by acetylation. For example, the HAT activity of the nuclear receptor coactivator ACTR is inhibited upon acetylation by p300/CBP.<sup id="cite_ref-Roth_4-16" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Interaction_with_HDACs">Interaction with HDACs</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=25" title="Edit section: Interaction with HDACs"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>Histone acetyltransferases (HATs) and histone deacetylases (HDACs) are recruited to their target promoters through physical interactions with sequence-specific transcription factors. They usually function within a multisubunit complex in which the other subunits are necessary for them to modify histone residues around the binding site. These enzymes can also modify non-histone proteins. </p> <div class="mw-heading mw-heading2"><h2 id="Biological_role">Biological role</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=26" title="Edit section: Biological role"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <div class="mw-heading mw-heading3"><h3 id="Chromatin_remodeling">Chromatin remodeling</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=27" title="Edit section: Chromatin remodeling"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-default-size mw-halign-left" typeof="mw:File/Thumb"><a href="/wiki/File:Histone_tails_and_their_function_in_chromatin_formation.svg" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/f/f4/Histone_tails_and_their_function_in_chromatin_formation.svg/220px-Histone_tails_and_their_function_in_chromatin_formation.svg.png" decoding="async" width="220" height="484" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/f/f4/Histone_tails_and_their_function_in_chromatin_formation.svg/330px-Histone_tails_and_their_function_in_chromatin_formation.svg.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/f/f4/Histone_tails_and_their_function_in_chromatin_formation.svg/440px-Histone_tails_and_their_function_in_chromatin_formation.svg.png 2x" data-file-width="512" data-file-height="1126" /></a><figcaption>Histone tails and their function in chromatin formation</figcaption></figure> <p>Histone acetyltransferases serve many biological roles inside the cell. <a href="/wiki/Chromatin" title="Chromatin">Chromatin</a> is a combination of proteins and <a href="/wiki/DNA" title="DNA">DNA</a> found in the <a href="/wiki/Cell_nucleus" title="Cell nucleus">nucleus</a>, and it undergoes many structural changes as different cellular events such as <a href="/wiki/DNA_replication" title="DNA replication">DNA replication</a>, <a href="/wiki/DNA_repair" title="DNA repair">DNA repair</a>, and <a href="/wiki/Transcription_(genetics)" class="mw-redirect" title="Transcription (genetics)">transcription</a> occur.<sup id="cite_ref-Voet_25-0" class="reference"><a href="#cite_note-Voet-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> Chromatin in the cell can be found in two states: condensed and uncondensed. The latter, known as <a href="/wiki/Euchromatin" title="Euchromatin">euchromatin</a>, is transcriptionally active, whereas the former, known as <a href="/wiki/Heterochromatin" title="Heterochromatin">heterochromatin</a>, is transcriptionally inactive.<sup id="cite_ref-Voet_25-1" class="reference"><a href="#cite_note-Voet-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Tropp_26-0" class="reference"><a href="#cite_note-Tropp-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> Histones comprise the protein portion of chromatin. There are five different <a href="/wiki/Histone" title="Histone">histone</a> proteins: H1, H2A, H2B, H3, and H4. A core histone is formed when two of each histone subtype, excluding H1, form a quaternary complex. This octameric complex, in association with the 147 base pairs of DNA coiled around it, forms the <a href="/wiki/Nucleosome" title="Nucleosome">nucleosome</a>.<sup id="cite_ref-Roth_4-17" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Histone H1 locks the nucleosome complex together, and it is the last protein to bind in the complex. </p><p>Histones tend to be positively charged proteins with N-terminal tails that stem from the core. The phosphodiester backbone of DNA is negative, which allows for strong ionic interactions between histone proteins and DNA. Histone acetyltransferases transfer an <a href="/wiki/Acetyl" class="mw-redirect" title="Acetyl">acetyl</a> group to specific <a href="/wiki/Lysine" title="Lysine">lysine</a> residues on histones, which neutralizes their positive charge and thus reduces the strong interactions between the histone and DNA.<sup id="cite_ref-Voet_25-2" class="reference"><a href="#cite_note-Voet-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> Acetylation is also thought to perturb interactions between individual nucleosomes and act as interaction sites for other DNA-associated proteins.<sup id="cite_ref-Roth_4-18" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> </p><p>There can be different levels of histone acetylation as well as other types of modifications, allowing the cell to have control over the level of chromatin packing during different cellular events such as replication, transcription, recombination, and repair. Acetylation is not the only regulatory <a href="/wiki/Post-translational_modification" title="Post-translational modification">post-translational modification</a> to histones that dictates chromatin structure; methylation, phosphorylation, ADP-ribosylation, and ubiquitination have also been reported.<sup id="cite_ref-Roth_4-19" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Voet_25-3" class="reference"><a href="#cite_note-Voet-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> These combinations of different covalent modifications on the N-terminal tails of histones have been referred to as the <a href="/wiki/Histone_code" title="Histone code">histone code</a>, and it is thought that this code may be heritable and preserved in the next cell generation.<sup id="cite_ref-Tropp_26-1" class="reference"><a href="#cite_note-Tropp-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> </p><p>H3 and H4 histone proteins are the primary targets of HATs, but H2A and H2B are also acetylated <i>in vivo</i>. Lysines 9, 14, 18, and 23 of H3 and lysines 5, 8, 12, and 16 of H4 are all targeted for acetylation.<sup id="cite_ref-Roth_4-20" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Voet_25-4" class="reference"><a href="#cite_note-Voet-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> Lysines 5, 12, 15, and 20 are acetylated on histone H2B, while only lysines 5 and 9 have been observed to be acetylated on histone H2A.<sup id="cite_ref-Roth_4-21" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Voet_25-5" class="reference"><a href="#cite_note-Voet-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Tropp_26-2" class="reference"><a href="#cite_note-Tropp-26"><span class="cite-bracket">[</span>26<span class="cite-bracket">]</span></a></sup> With so many different sites for acetylation, a high level of specificity can be achieved in triggering specific responses. An example of this specificity is when histone H4 is acetylated at lysines 5 and 12. This acetylation pattern has been seen during histone synthesis. Another example is acetylation of H4K16, which has been associated with dosage compensation of the male X chromosome in <i>Drosophila melanogaster</i>.<sup id="cite_ref-Lee_2-7" class="reference"><a href="#cite_note-Lee-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Roth_4-22" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading3"><h3 id="Gene_expression">Gene expression</h3><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=28" title="Edit section: Gene expression"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <figure class="mw-default-size mw-halign-right" typeof="mw:File/Thumb"><a href="/wiki/File:HAT_transcription.png" class="mw-file-description"><img src="//upload.wikimedia.org/wikipedia/commons/thumb/c/cb/HAT_transcription.png/220px-HAT_transcription.png" decoding="async" width="220" height="169" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/c/cb/HAT_transcription.png/330px-HAT_transcription.png 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/c/cb/HAT_transcription.png/440px-HAT_transcription.png 2x" data-file-width="870" data-file-height="669" /></a><figcaption>Schematic showing the role of HATs in gene transcription.</figcaption></figure> <p>Histone modifications modulate the packing of chromatin. The level of packing of the DNA is important for gene transcription, since the transcriptional machinery must have access to the promoter in order for transcription to occur.<sup id="cite_ref-Roth_4-23" class="reference"><a href="#cite_note-Roth-4"><span class="cite-bracket">[</span>4<span class="cite-bracket">]</span></a></sup> Neutralization of charged lysine residues by HATs allows for the chromatin to decondense so that this machinery has access to the gene to be transcribed. However, acetylation is not always associated with enhanced transcriptional activity. For instance, acetylation of H4K12 has been associated with condensed and transcriptionally inactive chromatin.<sup id="cite_ref-Grunstein_27-0" class="reference"><a href="#cite_note-Grunstein-27"><span class="cite-bracket">[</span>27<span class="cite-bracket">]</span></a></sup> In addition, some histone modifications are associated with both enhanced and repressed activity, in a context-dependent manner.<sup id="cite_ref-pmid26941319_28-0" class="reference"><a href="#cite_note-pmid26941319-28"><span class="cite-bracket">[</span>28<span class="cite-bracket">]</span></a></sup> </p><p>HATs act as transcriptional co-activators or gene silencers and are most often found in large complexes made up of 10 to 20 subunits, some of which shared among different HAT complexes.<sup id="cite_ref-Voet_25-6" class="reference"><a href="#cite_note-Voet-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> These complexes include SAGA (Spt/Ada/Gcn5L acetyltransferase), PCAF, ADA (transcriptional adaptor), TFIID (transcription factor II D), TFTC (TBP-free TAF-containing complex), and NuA3/NuA4 (nucleosomal acetyltransferases of H3 and H4).<sup id="cite_ref-Lee_2-8" class="reference"><a href="#cite_note-Lee-2"><span class="cite-bracket">[</span>2<span class="cite-bracket">]</span></a></sup><sup id="cite_ref-Voet_25-7" class="reference"><a href="#cite_note-Voet-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> These complexes modulate HAT specificity by bringing HATs to their target genes where they can then acetylate nucleosomal histones.<sup id="cite_ref-Voet_25-8" class="reference"><a href="#cite_note-Voet-25"><span class="cite-bracket">[</span>25<span class="cite-bracket">]</span></a></sup> Some HAT transcriptional co-activators contain a <a href="/wiki/Bromodomain" title="Bromodomain">bromodomain</a>, a 110-amino acid module that recognizes acetylated lysine residues and is functionally linked to the co-activators in the regulation of transcription.<sup id="cite_ref-Zhou_29-0" class="reference"><a href="#cite_note-Zhou-29"><span class="cite-bracket">[</span>29<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="Clinical_significance">Clinical significance</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=29" title="Edit section: Clinical significance"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <p>The ability of histone acetyltransferases to manipulate chromatin structure and lay an <a href="/wiki/Epigenetic" class="mw-redirect" title="Epigenetic">epigenetic</a> framework makes them essential in cell maintenance and survival. The process of chromatin remodeling involves several enzymes, including HATs, that assist in the reformation of nucleosomes and are required for DNA damage repair systems to function.<sup id="cite_ref-Rossetto_30-0" class="reference"><a href="#cite_note-Rossetto-30"><span class="cite-bracket">[</span>30<span class="cite-bracket">]</span></a></sup> HATs have been implicated as accessories to disease progression, specifically in neurodegenerative disorders. For instance, <a href="/wiki/Huntington%27s_disease" title="Huntington's disease">Huntington's disease</a> is a disease that affects motor skills and mental abilities. The only known mutation that has been implicated in the disease is in the N-terminal region of the protein <a href="/wiki/Huntingtin" title="Huntingtin">huntingtin (htt)</a>.<sup id="cite_ref-editors_31-0" class="reference"><a href="#cite_note-editors-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> It has been reported that htt directly interacts with HATs and represses the catalytic activity of p300/CBP and PCAF <i>in vitro</i>. </p><p>The human premature aging syndrome Hutchinson Gilford <a href="/wiki/Progeria" title="Progeria">progeria</a> is caused by a mutational defect in the processing of <a href="/wiki/LMNA" class="mw-redirect" title="LMNA">lamin A</a>, a <a href="/wiki/Nuclear_matrix" title="Nuclear matrix">nuclear matrix</a> protein. In a mouse model of this condition, recruitment of <a href="/wiki/DNA_repair" title="DNA repair">repair</a> proteins to sites of <a href="/wiki/DNA_damage_(naturally_occurring)" title="DNA damage (naturally occurring)">DNA damage</a> is delayed. The molecular mechanism underlying this delayed repair response involves a histone acetylation defect.<sup id="cite_ref-pmid21746928_32-0" class="reference"><a href="#cite_note-pmid21746928-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> Specifically, <a href="/wiki/Histone_H4" title="Histone H4">histone H4</a> is hypoacetylated at a lysine 16 residue (H4K16) and this defect is due to reduced association of histone acetyltransferase, Mof, to the nuclear matrix<sup id="cite_ref-pmid21746928_32-1" class="reference"><a href="#cite_note-pmid21746928-32"><span class="cite-bracket">[</span>32<span class="cite-bracket">]</span></a></sup> </p><p><a href="/wiki/Spinocerebellar_ataxia_type_1" title="Spinocerebellar ataxia type 1">Spinocerebellar ataxia type 1</a> is a neurodegenerative disease that arises as a result of a defective mutant <a href="/wiki/Ataxin-1" class="mw-redirect" title="Ataxin-1">Ataxin-1</a> protein. Mutant <a href="/wiki/Ataxin-1" class="mw-redirect" title="Ataxin-1">Ataxin-1</a> reduces histone acetylation resulting in repressed histone acetyltransferase-mediated <a href="/wiki/Transcription_(biology)" title="Transcription (biology)">transcription</a>.<sup id="cite_ref-pmid22884877_33-0" class="reference"><a href="#cite_note-pmid22884877-33"><span class="cite-bracket">[</span>33<span class="cite-bracket">]</span></a></sup> </p><p>HATs have also been associated with control of learning and memory functions. Studies have shown that mice without PCAF or CBP display evidence of <a href="/wiki/Neurodegeneration" class="mw-redirect" title="Neurodegeneration">neurodegeneration</a>.<sup id="cite_ref-editors_31-1" class="reference"><a href="#cite_note-editors-31"><span class="cite-bracket">[</span>31<span class="cite-bracket">]</span></a></sup> Mice with PCAF deletion are incompetent with respect to learning, and those with CBP deletion seem to suffer from long-term memory loss.<sup id="cite_ref-Furdas_34-0" class="reference"><a href="#cite_note-Furdas-34"><span class="cite-bracket">[</span>34<span class="cite-bracket">]</span></a></sup> </p><p>The misregulation of the equilibrium between acetylation and deacetylation has also been associated with the manifestation of certain cancers. If histone acetyltransferases are inhibited, then damaged DNA may not be repaired, eventually leading to cell death. Controlling the <a href="/wiki/Chromatin_remodeling" title="Chromatin remodeling">chromatin remodeling</a> process within cancer cells may provide a novel drug target for cancer research.<sup id="cite_ref-Oike_35-0" class="reference"><a href="#cite_note-Oike-35"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup> Attacking these enzymes within cancer cells could lead to increased <a href="/wiki/Apoptosis" title="Apoptosis">apoptosis</a> due to high accumulation of DNA damage. One such inhibitor of histone acetyltransferases is called garcinol. This compound is found within the rinds of the <a href="/wiki/Garcinia_indica" title="Garcinia indica">garcinia indica</a> fruit, otherwise known as <a href="/wiki/Mangosteen" title="Mangosteen">mangosteen</a>. To explore the effects of garcinol on histone acetyltransferases, researchers used <a href="/wiki/HeLa" title="HeLa">HeLa</a> cells. The cells underwent irradiation, creating double-strand breaks within the DNA, and garcinol was introduced into the cells to see if it influenced the DNA damage response. If garcinol is successful at inhibiting the process of <a href="/wiki/Non-homologous_end_joining" title="Non-homologous end joining">non-homologous end joining</a>, a DNA repair mechanism that shows preference in fixing double-strand breaks,<sup id="cite_ref-Burma_36-0" class="reference"><a href="#cite_note-Burma-36"><span class="cite-bracket">[</span>36<span class="cite-bracket">]</span></a></sup> then it may serve as a <a href="/wiki/Radiosensitizer" title="Radiosensitizer">radiosensitizer</a>, a molecule that increases the sensitivity of cells to radiation damage. Increases in radiosensitivity may increase the effectiveness of radiotherapy.<sup id="cite_ref-Oike_35-1" class="reference"><a href="#cite_note-Oike-35"><span class="cite-bracket">[</span>35<span class="cite-bracket">]</span></a></sup> </p> <div class="mw-heading mw-heading2"><h2 id="See_also">See also</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=30" title="Edit section: See also"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a href="/wiki/Histone-modifying_enzymes" title="Histone-modifying enzymes">Histone-modifying enzymes</a></li> <li><a href="/wiki/Histone_deacetylase" title="Histone deacetylase">Histone deacetylase (HDAC)</a></li> <li><a href="/wiki/Histone_methyltransferase" title="Histone methyltransferase">Histone methyltransferase (HMT)</a></li> <li><a href="/wiki/RNA_polymerase_control_by_chromatin_structure" class="mw-redirect" title="RNA polymerase control by chromatin structure">RNA polymerase control by chromatin structure</a></li> <li><a href="/wiki/Acetyltransferase" title="Acetyltransferase">Acetyltransferase</a></li></ul> <div class="mw-heading mw-heading2"><h2 id="References">References</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=31" title="Edit section: References"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <style data-mw-deduplicate="TemplateStyles:r1239543626">.mw-parser-output .reflist{margin-bottom:0.5em;list-style-type:decimal}@media screen{.mw-parser-output .reflist{font-size:90%}}.mw-parser-output .reflist .references{font-size:100%;margin-bottom:0;list-style-type:inherit}.mw-parser-output .reflist-columns-2{column-width:30em}.mw-parser-output .reflist-columns-3{column-width:25em}.mw-parser-output .reflist-columns{margin-top:0.3em}.mw-parser-output .reflist-columns ol{margin-top:0}.mw-parser-output .reflist-columns li{page-break-inside:avoid;break-inside:avoid-column}.mw-parser-output .reflist-upper-alpha{list-style-type:upper-alpha}.mw-parser-output .reflist-upper-roman{list-style-type:upper-roman}.mw-parser-output .reflist-lower-alpha{list-style-type:lower-alpha}.mw-parser-output .reflist-lower-greek{list-style-type:lower-greek}.mw-parser-output .reflist-lower-roman{list-style-type:lower-roman}</style><div class="reflist reflist-columns references-column-width" style="column-width: 32em;"> <ol class="references"> <li id="cite_note-1"><span class="mw-cite-backlink"><b><a href="#cite_ref-1">^</a></b></span> <span class="reference-text"><style data-mw-deduplicate="TemplateStyles:r1238218222">.mw-parser-output cite.citation{font-style:inherit;word-wrap:break-word}.mw-parser-output .citation q{quotes:"\"""\"""'""'"}.mw-parser-output .citation:target{background-color:rgba(0,127,255,0.133)}.mw-parser-output .id-lock-free.id-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/6/65/Lock-green.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-limited.id-lock-limited a,.mw-parser-output .id-lock-registration.id-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/d/d6/Lock-gray-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .id-lock-subscription.id-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/a/aa/Lock-red-alt-2.svg")right 0.1em center/9px no-repeat}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/4/4c/Wikisource-logo.svg")right 0.1em center/12px no-repeat}body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-free a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-limited a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-registration a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .id-lock-subscription a,body:not(.skin-timeless):not(.skin-minerva) .mw-parser-output .cs1-ws-icon a{background-size:contain;padding:0 1em 0 0}.mw-parser-output .cs1-code{color:inherit;background:inherit;border:none;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;color:var(--color-error,#d33)}.mw-parser-output .cs1-visible-error{color:var(--color-error,#d33)}.mw-parser-output .cs1-maint{display:none;color:#085;margin-left:0.3em}.mw-parser-output .cs1-kern-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right{padding-right:0.2em}.mw-parser-output .citation .mw-selflink{font-weight:inherit}@media screen{.mw-parser-output .cs1-format{font-size:95%}html.skin-theme-clientpref-night .mw-parser-output .cs1-maint{color:#18911f}}@media screen and (prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .cs1-maint{color:#18911f}}</style><cite id="CITEREFWangGuoLiuYin2017" class="citation journal cs1">Wang Y, Guo Y, Liu K, Yin Z, Liu R, Xia Y, Tan L, Yang P, Lee J, et al. (December 6, 2017). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5841452">"KAT2A coupled with the α-KGDH complex acts as a histone H3 succinyltransferase"</a>. <i>Nature</i>. <b>552</b> (7684): 273–277. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2017Natur.552..273W">2017Natur.552..273W</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnature25003">10.1038/nature25003</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5841452">5841452</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/29211711">29211711</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature&rft.atitle=KAT2A+coupled+with+the+%CE%B1-KGDH+complex+acts+as+a+histone+H3+succinyltransferase&rft.volume=552&rft.issue=7684&rft.pages=273-277&rft.date=2017-12-06&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5841452%23id-name%3DPMC&rft_id=info%3Apmid%2F29211711&rft_id=info%3Adoi%2F10.1038%2Fnature25003&rft_id=info%3Abibcode%2F2017Natur.552..273W&rft.aulast=Wang&rft.aufirst=Y&rft.au=Guo%2C+Y&rft.au=Liu%2C+K&rft.au=Yin%2C+Z&rft.au=Liu%2C+R&rft.au=Xia%2C+Y&rft.au=Tan%2C+L&rft.au=Yang%2C+P&rft.au=Lee%2C+J&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC5841452&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Lee-2"><span class="mw-cite-backlink">^ <a href="#cite_ref-Lee_2-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Lee_2-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Lee_2-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Lee_2-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Lee_2-4"><sup><i><b>e</b></i></sup></a> <a href="#cite_ref-Lee_2-5"><sup><i><b>f</b></i></sup></a> <a href="#cite_ref-Lee_2-6"><sup><i><b>g</b></i></sup></a> <a href="#cite_ref-Lee_2-7"><sup><i><b>h</b></i></sup></a> <a href="#cite_ref-Lee_2-8"><sup><i><b>i</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFLeeWorkman2007" class="citation journal cs1">Lee KK, Workman JL (April 2007). <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17380162/">"Histone acetyltransferase complexes: one size doesn't fit all"</a>. <i>Nature Reviews. Molecular Cell Biology</i>. <b>8</b> (4): 284–95. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnrm2145">10.1038/nrm2145</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17380162">17380162</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:1091590">1091590</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature+Reviews.+Molecular+Cell+Biology&rft.atitle=Histone+acetyltransferase+complexes%3A+one+size+doesn%27t+fit+all&rft.volume=8&rft.issue=4&rft.pages=284-95&rft.date=2007-04&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A1091590%23id-name%3DS2CID&rft_id=info%3Apmid%2F17380162&rft_id=info%3Adoi%2F10.1038%2Fnrm2145&rft.aulast=Lee&rft.aufirst=KK&rft.au=Workman%2C+JL&rft_id=https%3A%2F%2Fpubmed.ncbi.nlm.nih.gov%2F17380162%2F&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Weaver-3"><span class="mw-cite-backlink">^ <a href="#cite_ref-Weaver_3-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Weaver_3-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFWeaver_R2007" class="citation book cs1">Weaver R (2007). <i>Molecular Biology</i>. McGraw-Hill. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0073319940" title="Special:BookSources/978-0073319940"><bdi>978-0073319940</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Molecular+Biology&rft.pub=McGraw-Hill&rft.date=2007&rft.isbn=978-0073319940&rft.au=Weaver+R&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Roth-4"><span class="mw-cite-backlink">^ <a href="#cite_ref-Roth_4-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Roth_4-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Roth_4-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Roth_4-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Roth_4-4"><sup><i><b>e</b></i></sup></a> <a href="#cite_ref-Roth_4-5"><sup><i><b>f</b></i></sup></a> <a href="#cite_ref-Roth_4-6"><sup><i><b>g</b></i></sup></a> <a href="#cite_ref-Roth_4-7"><sup><i><b>h</b></i></sup></a> <a href="#cite_ref-Roth_4-8"><sup><i><b>i</b></i></sup></a> <a href="#cite_ref-Roth_4-9"><sup><i><b>j</b></i></sup></a> <a href="#cite_ref-Roth_4-10"><sup><i><b>k</b></i></sup></a> <a href="#cite_ref-Roth_4-11"><sup><i><b>l</b></i></sup></a> <a href="#cite_ref-Roth_4-12"><sup><i><b>m</b></i></sup></a> <a href="#cite_ref-Roth_4-13"><sup><i><b>n</b></i></sup></a> <a href="#cite_ref-Roth_4-14"><sup><i><b>o</b></i></sup></a> <a href="#cite_ref-Roth_4-15"><sup><i><b>p</b></i></sup></a> <a href="#cite_ref-Roth_4-16"><sup><i><b>q</b></i></sup></a> <a href="#cite_ref-Roth_4-17"><sup><i><b>r</b></i></sup></a> <a href="#cite_ref-Roth_4-18"><sup><i><b>s</b></i></sup></a> <a href="#cite_ref-Roth_4-19"><sup><i><b>t</b></i></sup></a> <a href="#cite_ref-Roth_4-20"><sup><i><b>u</b></i></sup></a> <a href="#cite_ref-Roth_4-21"><sup><i><b>v</b></i></sup></a> <a href="#cite_ref-Roth_4-22"><sup><i><b>w</b></i></sup></a> <a href="#cite_ref-Roth_4-23"><sup><i><b>x</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFRothDenuAllis2001" class="citation journal cs1">Roth SY, Denu JM, Allis CD (2001). <a rel="nofollow" class="external text" href="https://www.annualreviews.org/doi/10.1146/annurev.biochem.70.1.81">"Histone acetyltransferases"</a>. <i>Annual Review of Biochemistry</i>. <b>70</b>: 81–120. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1146%2Fannurev.biochem.70.1.81">10.1146/annurev.biochem.70.1.81</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11395403">11395403</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Annual+Review+of+Biochemistry&rft.atitle=Histone+acetyltransferases&rft.volume=70&rft.pages=81-120&rft.date=2001&rft_id=info%3Adoi%2F10.1146%2Fannurev.biochem.70.1.81&rft_id=info%3Apmid%2F11395403&rft.aulast=Roth&rft.aufirst=SY&rft.au=Denu%2C+JM&rft.au=Allis%2C+CD&rft_id=https%3A%2F%2Fwww.annualreviews.org%2Fdoi%2F10.1146%2Fannurev.biochem.70.1.81&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Lee0-5"><span class="mw-cite-backlink">^ <a href="#cite_ref-Lee0_5-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Lee0_5-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Lee0_5-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Lee0_5-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Lee0_5-4"><sup><i><b>e</b></i></sup></a> <a href="#cite_ref-Lee0_5-5"><sup><i><b>f</b></i></sup></a> <a href="#cite_ref-Lee0_5-6"><sup><i><b>g</b></i></sup></a> <a href="#cite_ref-Lee0_5-7"><sup><i><b>h</b></i></sup></a> <a href="#cite_ref-Lee0_5-8"><sup><i><b>i</b></i></sup></a> <a href="#cite_ref-Lee0_5-9"><sup><i><b>j</b></i></sup></a> <a href="#cite_ref-Lee0_5-10"><sup><i><b>k</b></i></sup></a> <a href="#cite_ref-Lee0_5-11"><sup><i><b>l</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFSternerBerger2000" class="citation journal cs1">Sterner DE, Berger SL (June 2000). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC98999">"Acetylation of histones and transcription-related factors"</a>. <i>Microbiology and Molecular Biology Reviews</i>. <b>64</b> (2): 435–59. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1128%2FMMBR.64.2.435-459.2000">10.1128/MMBR.64.2.435-459.2000</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC98999">98999</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10839822">10839822</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Microbiology+and+Molecular+Biology+Reviews&rft.atitle=Acetylation+of+histones+and+transcription-related+factors&rft.volume=64&rft.issue=2&rft.pages=435-59&rft.date=2000-06&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC98999%23id-name%3DPMC&rft_id=info%3Apmid%2F10839822&rft_id=info%3Adoi%2F10.1128%2FMMBR.64.2.435-459.2000&rft.aulast=Sterner&rft.aufirst=DE&rft.au=Berger%2C+SL&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC98999&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-6"><span class="mw-cite-backlink"><b><a href="#cite_ref-6">^</a></b></span> <span class="reference-text"> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFMüllerMuir2014" class="citation journal cs1">Müller, Manuel M.; Muir, Tom W. (2014-10-20). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4378460">"Histones: At the Crossroads of Peptide and Protein Chemistry"</a>. <i><a href="/wiki/Chemical_Reviews" title="Chemical Reviews">Chemical Reviews</a></i>. <b>115</b> (6). <a href="/wiki/American_Chemical_Society" title="American Chemical Society">American Chemical Society</a>: 2296–2349. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fcr5003529">10.1021/cr5003529</a>. <a href="/wiki/ISSN_(identifier)" class="mw-redirect" title="ISSN (identifier)">ISSN</a> <a rel="nofollow" class="external text" href="https://search.worldcat.org/issn/0009-2665">0009-2665</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4378460">4378460</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/25330018">25330018</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:33098192">33098192</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Chemical+Reviews&rft.atitle=Histones%3A+At+the+Crossroads+of+Peptide+and+Protein+Chemistry&rft.volume=115&rft.issue=6&rft.pages=2296-2349&rft.date=2014-10-20&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4378460%23id-name%3DPMC&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A33098192%23id-name%3DS2CID&rft_id=info%3Adoi%2F10.1021%2Fcr5003529&rft.issn=0009-2665&rft_id=info%3Apmid%2F25330018&rft.aulast=M%C3%BCller&rft.aufirst=Manuel+M.&rft.au=Muir%2C+Tom+W.&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4378460&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span> This review cites this research. <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFMittalBlacketerShogren-Knaak2014" class="citation journal cs1">Mittal, C; Blacketer, M.J; Shogren-Knaak, M.A (2014). <a rel="nofollow" class="external text" href="https://www.sciencedirect.com/science/article/pii/S0003269714001730">"Nucleosome acetylation sequencing to study the establishment of chromatin acetylation"</a>. <i>Analytical Biochemistry</i>. <b>457</b> (457): 51–8. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.ab.2014.04.024">10.1016/j.ab.2014.04.024</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/24769374">24769374</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Analytical+Biochemistry&rft.atitle=Nucleosome+acetylation+sequencing+to+study+the+establishment+of+chromatin+acetylation&rft.volume=457&rft.issue=457&rft.pages=51-8&rft.date=2014&rft_id=info%3Adoi%2F10.1016%2Fj.ab.2014.04.024&rft_id=info%3Apmid%2F24769374&rft.aulast=Mittal&rft.aufirst=C&rft.au=Blacketer%2C+M.J&rft.au=Shogren-Knaak%2C+M.A&rft_id=https%3A%2F%2Fwww.sciencedirect.com%2Fscience%2Farticle%2Fpii%2FS0003269714001730&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Citation9-7"><span class="mw-cite-backlink">^ <a href="#cite_ref-Citation9_7-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Citation9_7-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Citation9_7-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Citation9_7-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Citation9_7-4"><sup><i><b>e</b></i></sup></a> <a href="#cite_ref-Citation9_7-5"><sup><i><b>f</b></i></sup></a> <a href="#cite_ref-Citation9_7-6"><sup><i><b>g</b></i></sup></a> <a href="#cite_ref-Citation9_7-7"><sup><i><b>h</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFMarmorstein2001" class="citation journal cs1">Marmorstein R (August 2001). <a rel="nofollow" class="external text" href="https://www.sciencedirect.com/science/article/abs/pii/S0022283601948594">"Structure of histone acetyltransferases"</a>. <i>Journal of Molecular Biology</i>. <b>311</b> (3): 433–44. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1006%2Fjmbi.2001.4859">10.1006/jmbi.2001.4859</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11492997">11492997</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Molecular+Biology&rft.atitle=Structure+of+histone+acetyltransferases&rft.volume=311&rft.issue=3&rft.pages=433-44&rft.date=2001-08&rft_id=info%3Adoi%2F10.1006%2Fjmbi.2001.4859&rft_id=info%3Apmid%2F11492997&rft.aulast=Marmorstein&rft.aufirst=R&rft_id=https%3A%2F%2Fwww.sciencedirect.com%2Fscience%2Farticle%2Fabs%2Fpii%2FS0022283601948594&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Citation5-8"><span class="mw-cite-backlink">^ <a href="#cite_ref-Citation5_8-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Citation5_8-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Citation5_8-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Citation5_8-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Citation5_8-4"><sup><i><b>e</b></i></sup></a> <a href="#cite_ref-Citation5_8-5"><sup><i><b>f</b></i></sup></a> <a href="#cite_ref-Citation5_8-6"><sup><i><b>g</b></i></sup></a> <a href="#cite_ref-Citation5_8-7"><sup><i><b>h</b></i></sup></a> <a href="#cite_ref-Citation5_8-8"><sup><i><b>i</b></i></sup></a> <a href="#cite_ref-Citation5_8-9"><sup><i><b>j</b></i></sup></a> <a href="#cite_ref-Citation5_8-10"><sup><i><b>k</b></i></sup></a> <a href="#cite_ref-Citation5_8-11"><sup><i><b>l</b></i></sup></a> <a href="#cite_ref-Citation5_8-12"><sup><i><b>m</b></i></sup></a> <a href="#cite_ref-Citation5_8-13"><sup><i><b>n</b></i></sup></a> <a href="#cite_ref-Citation5_8-14"><sup><i><b>o</b></i></sup></a> <a href="#cite_ref-Citation5_8-15"><sup><i><b>p</b></i></sup></a> <a href="#cite_ref-Citation5_8-16"><sup><i><b>q</b></i></sup></a> <a href="#cite_ref-Citation5_8-17"><sup><i><b>r</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFYuanMarmorstein2013" class="citation journal cs1">Yuan H, Marmorstein R (February 2013). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4017165">"Histone acetyltransferases: Rising ancient counterparts to protein kinases"</a>. <i>Biopolymers</i>. <b>99</b> (2): 98–111. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2Fbip.22128">10.1002/bip.22128</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4017165">4017165</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/23175385">23175385</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biopolymers&rft.atitle=Histone+acetyltransferases%3A+Rising+ancient+counterparts+to+protein+kinases&rft.volume=99&rft.issue=2&rft.pages=98-111&rft.date=2013-02&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4017165%23id-name%3DPMC&rft_id=info%3Apmid%2F23175385&rft_id=info%3Adoi%2F10.1002%2Fbip.22128&rft.aulast=Yuan&rft.aufirst=H&rft.au=Marmorstein%2C+R&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4017165&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Biochimica_et_Biophysica_Acta_(2009)-9"><span class="mw-cite-backlink">^ <a href="#cite_ref-Biochimica_et_Biophysica_Acta_(2009)_9-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Biochimica_et_Biophysica_Acta_(2009)_9-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Biochimica_et_Biophysica_Acta_(2009)_9-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Biochimica_et_Biophysica_Acta_(2009)_9-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Biochimica_et_Biophysica_Acta_(2009)_9-4"><sup><i><b>e</b></i></sup></a> <a href="#cite_ref-Biochimica_et_Biophysica_Acta_(2009)_9-5"><sup><i><b>f</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFMarmorsteinTrievel2009" class="citation journal cs1">Marmorstein R, Trievel RC (January 2009). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4059211">"Histone modifying enzymes: structures, mechanisms, and specificities"</a>. <i>Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms</i>. <b>1789</b> (1): 58–68. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.bbagrm.2008.07.009">10.1016/j.bbagrm.2008.07.009</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4059211">4059211</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18722564">18722564</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochimica+et+Biophysica+Acta+%28BBA%29+-+Gene+Regulatory+Mechanisms&rft.atitle=Histone+modifying+enzymes%3A+structures%2C+mechanisms%2C+and+specificities&rft.volume=1789&rft.issue=1&rft.pages=58-68&rft.date=2009-01&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4059211%23id-name%3DPMC&rft_id=info%3Apmid%2F18722564&rft_id=info%3Adoi%2F10.1016%2Fj.bbagrm.2008.07.009&rft.aulast=Marmorstein&rft.aufirst=R&rft.au=Trievel%2C+RC&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC4059211&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Citation6-10"><span class="mw-cite-backlink">^ <a href="#cite_ref-Citation6_10-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Citation6_10-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFOgryzko2001" class="citation journal cs1">Ogryzko VV (May 2001). <a rel="nofollow" class="external text" href="https://link.springer.com/article/10.1007/PL00000892">"Mammalian histone acetyltransferases and their complexes"</a>. <i>Cellular and Molecular Life Sciences</i>. <b>58</b> (5–6): 683–92. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1007%2FPL00000892">10.1007/PL00000892</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11337353">11337353</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11437230">11437230</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:20905209">20905209</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Cellular+and+Molecular+Life+Sciences&rft.atitle=Mammalian+histone+acetyltransferases+and+their+complexes&rft.volume=58&rft.issue=5%E2%80%936&rft.pages=683-92&rft.date=2001-05&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC11337353%23id-name%3DPMC&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A20905209%23id-name%3DS2CID&rft_id=info%3Apmid%2F11437230&rft_id=info%3Adoi%2F10.1007%2FPL00000892&rft.aulast=Ogryzko&rft.aufirst=VV&rft_id=https%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2FPL00000892&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Other1-11"><span class="mw-cite-backlink"><b><a href="#cite_ref-Other1_11-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFDoiHirayamaSassone-Corsi2006" class="citation journal cs1">Doi M, Hirayama J, Sassone-Corsi P (May 2006). <a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.cell.2006.03.033">"Circadian regulator CLOCK is a histone acetyltransferase"</a>. <i>Cell</i>. <b>125</b> (3): 497–508. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.cell.2006.03.033">10.1016/j.cell.2006.03.033</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16678094">16678094</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:5968161">5968161</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Cell&rft.atitle=Circadian+regulator+CLOCK+is+a+histone+acetyltransferase&rft.volume=125&rft.issue=3&rft.pages=497-508&rft.date=2006-05&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A5968161%23id-name%3DS2CID&rft_id=info%3Apmid%2F16678094&rft_id=info%3Adoi%2F10.1016%2Fj.cell.2006.03.033&rft.aulast=Doi&rft.aufirst=M&rft.au=Hirayama%2C+J&rft.au=Sassone-Corsi%2C+P&rft_id=https%3A%2F%2Fdoi.org%2F10.1016%252Fj.cell.2006.03.033&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Citation2-12"><span class="mw-cite-backlink">^ <a href="#cite_ref-Citation2_12-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Citation2_12-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Citation2_12-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Citation2_12-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Citation2_12-4"><sup><i><b>e</b></i></sup></a> <a href="#cite_ref-Citation2_12-5"><sup><i><b>f</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFKimuraMatsubaraHorikoshi2005" class="citation journal cs1">Kimura A, Matsubara K, Horikoshi M (December 2005). <a rel="nofollow" class="external text" href="https://academic.oup.com/jb/article/138/6/647/829266?login=false">"A decade of histone acetylation: marking eukaryotic chromosomes with specific codes"</a>. <i>Journal of Biochemistry</i>. <b>138</b> (6): 647–62. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1093%2Fjb%2Fmvi184">10.1093/jb/mvi184</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16428293">16428293</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Journal+of+Biochemistry&rft.atitle=A+decade+of+histone+acetylation%3A+marking+eukaryotic+chromosomes+with+specific+codes&rft.volume=138&rft.issue=6&rft.pages=647-62&rft.date=2005-12&rft_id=info%3Adoi%2F10.1093%2Fjb%2Fmvi184&rft_id=info%3Apmid%2F16428293&rft.aulast=Kimura&rft.aufirst=A&rft.au=Matsubara%2C+K&rft.au=Horikoshi%2C+M&rft_id=https%3A%2F%2Facademic.oup.com%2Fjb%2Farticle%2F138%2F6%2F647%2F829266%3Flogin%3Dfalse&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Citation7-13"><span class="mw-cite-backlink"><b><a href="#cite_ref-Citation7_13-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFMarmorsteinRoth2001" class="citation journal cs1">Marmorstein R, Roth SY (April 2001). <a rel="nofollow" class="external text" href="https://www.sciencedirect.com/science/article/abs/pii/S0959437X00001738">"Histone acetyltransferases: function, structure, and catalysis"</a>. <i>Current Opinion in Genetics & Development</i>. <b>11</b> (2): 155–61. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0959-437X%2800%2900173-8">10.1016/S0959-437X(00)00173-8</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/11250138">11250138</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Opinion+in+Genetics+%26+Development&rft.atitle=Histone+acetyltransferases%3A+function%2C+structure%2C+and+catalysis&rft.volume=11&rft.issue=2&rft.pages=155-61&rft.date=2001-04&rft_id=info%3Adoi%2F10.1016%2FS0959-437X%2800%2900173-8&rft_id=info%3Apmid%2F11250138&rft.aulast=Marmorstein&rft.aufirst=R&rft.au=Roth%2C+SY&rft_id=https%3A%2F%2Fwww.sciencedirect.com%2Fscience%2Farticle%2Fabs%2Fpii%2FS0959437X00001738&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Citation8-14"><span class="mw-cite-backlink"><b><a href="#cite_ref-Citation8_14-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFAnamikaKrebsThompsonPoch2010" class="citation journal cs1">Anamika K, Krebs AR, Thompson J, Poch O, Devys D, Tora L (October 2010). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2972259">"Lessons from genome-wide studies: an integrated definition of the coactivator function of histone acetyl transferases"</a>. <i>Epigenetics & Chromatin</i>. <b>3</b> (1): 18. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1186%2F1756-8935-3-18">10.1186/1756-8935-3-18</a></span>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2972259">2972259</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/20961410">20961410</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Epigenetics+%26+Chromatin&rft.atitle=Lessons+from+genome-wide+studies%3A+an+integrated+definition+of+the+coactivator+function+of+histone+acetyl+transferases&rft.volume=3&rft.issue=1&rft.pages=18&rft.date=2010-10&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2972259%23id-name%3DPMC&rft_id=info%3Apmid%2F20961410&rft_id=info%3Adoi%2F10.1186%2F1756-8935-3-18&rft.aulast=Anamika&rft.aufirst=K&rft.au=Krebs%2C+AR&rft.au=Thompson%2C+J&rft.au=Poch%2C+O&rft.au=Devys%2C+D&rft.au=Tora%2C+L&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2972259&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Lee1-15"><span class="mw-cite-backlink"><b><a href="#cite_ref-Lee1_15-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFCarrozzaUtleyWorkmanCôté2003" class="citation journal cs1">Carrozza MJ, Utley RT, Workman JL, Côté J (June 2003). <a rel="nofollow" class="external text" href="https://www.cell.com/trends/genetics/fulltext/S0168-9525(03)00115-X?_returnURL=https%3A%2F%2Flinkinghub.elsevier.com%2Fretrieve%2Fpii%2FS016895250300115X%3Fshowall%3Dtrue">"The diverse functions of histone acetyltransferase complexes"</a>. <i>Trends in Genetics</i>. <b>19</b> (6): 321–9. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0168-9525%2803%2900115-X">10.1016/S0168-9525(03)00115-X</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/12801725">12801725</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Trends+in+Genetics&rft.atitle=The+diverse+functions+of+histone+acetyltransferase+complexes&rft.volume=19&rft.issue=6&rft.pages=321-9&rft.date=2003-06&rft_id=info%3Adoi%2F10.1016%2FS0168-9525%2803%2900115-X&rft_id=info%3Apmid%2F12801725&rft.aulast=Carrozza&rft.aufirst=MJ&rft.au=Utley%2C+RT&rft.au=Workman%2C+JL&rft.au=C%C3%B4t%C3%A9%2C+J&rft_id=https%3A%2F%2Fwww.cell.com%2Ftrends%2Fgenetics%2Ffulltext%2FS0168-9525%2803%2900115-X%3F_returnURL%3Dhttps%253A%252F%252Flinkinghub.elsevier.com%252Fretrieve%252Fpii%252FS016895250300115X%253Fshowall%253Dtrue&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Lee2-16"><span class="mw-cite-backlink"><b><a href="#cite_ref-Lee2_16-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFTorokGrant2004" class="citation book cs1">Torok MS, Grant PA (2004). <a rel="nofollow" class="external text" href="https://www.sciencedirect.com/science/article/abs/pii/S0065323304670070">"Histone acetyltransferase proteins contribute to transcriptional processes at multiple levels"</a>. <i>Proteins in Eukaryotic Transcription</i>. Advances in Protein Chemistry. Vol. 67. Academic Press. pp. 181–99. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2FS0065-3233%2804%2967007-0">10.1016/S0065-3233(04)67007-0</a>. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/9780120342679" title="Special:BookSources/9780120342679"><bdi>9780120342679</bdi></a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/14969728">14969728</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=bookitem&rft.atitle=Histone+acetyltransferase+proteins+contribute+to+transcriptional+processes+at+multiple+levels&rft.btitle=Proteins+in+Eukaryotic+Transcription&rft.series=Advances+in+Protein+Chemistry&rft.pages=181-99&rft.pub=Academic+Press&rft.date=2004&rft_id=info%3Apmid%2F14969728&rft_id=info%3Adoi%2F10.1016%2FS0065-3233%2804%2967007-0&rft.isbn=9780120342679&rft.aulast=Torok&rft.aufirst=MS&rft.au=Grant%2C+PA&rft_id=https%3A%2F%2Fwww.sciencedirect.com%2Fscience%2Farticle%2Fabs%2Fpii%2FS0065323304670070&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Lee3-17"><span class="mw-cite-backlink"><b><a href="#cite_ref-Lee3_17-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFVernarecciTosiFiletici2010" class="citation journal cs1">Vernarecci S, Tosi F, Filetici P (February 2010). "Tuning acetylated chromatin with HAT inhibitors: a novel tool for therapy". <i>Epigenetics</i>. <b>5</b> (2): 105–11. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.4161%2Fepi.5.2.10942">10.4161/epi.5.2.10942</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/20160510">20160510</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Epigenetics&rft.atitle=Tuning+acetylated+chromatin+with+HAT+inhibitors%3A+a+novel+tool+for+therapy&rft.volume=5&rft.issue=2&rft.pages=105-11&rft.date=2010-02&rft_id=info%3Adoi%2F10.4161%2Fepi.5.2.10942&rft_id=info%3Apmid%2F20160510&rft.aulast=Vernarecci&rft.aufirst=S&rft.au=Tosi%2C+F&rft.au=Filetici%2C+P&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Other2-18"><span class="mw-cite-backlink"><b><a href="#cite_ref-Other2_18-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFBerndsenAlbaughTanDenu2007" class="citation journal cs1">Berndsen CE, Albaugh BN, Tan S, Denu JM (January 2007). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2752042">"Catalytic mechanism of a MYST family histone acetyltransferase"</a>. <i>Biochemistry</i>. <b>46</b> (3): 623–9. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1021%2Fbi602513x">10.1021/bi602513x</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2752042">2752042</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/17223684">17223684</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Biochemistry&rft.atitle=Catalytic+mechanism+of+a+MYST+family+histone+acetyltransferase&rft.volume=46&rft.issue=3&rft.pages=623-9&rft.date=2007-01&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2752042%23id-name%3DPMC&rft_id=info%3Apmid%2F17223684&rft_id=info%3Adoi%2F10.1021%2Fbi602513x&rft.aulast=Berndsen&rft.aufirst=CE&rft.au=Albaugh%2C+BN&rft.au=Tan%2C+S&rft.au=Denu%2C+JM&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2752042&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Current_Opinion_in_Structural_Biology_(2008)-19"><span class="mw-cite-backlink">^ <a href="#cite_ref-Current_Opinion_in_Structural_Biology_(2008)_19-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Current_Opinion_in_Structural_Biology_(2008)_19-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Current_Opinion_in_Structural_Biology_(2008)_19-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Current_Opinion_in_Structural_Biology_(2008)_19-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Current_Opinion_in_Structural_Biology_(2008)_19-4"><sup><i><b>e</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFBerndsenDenu2008" class="citation journal cs1">Berndsen CE, Denu JM (December 2008). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2723715">"Catalysis and substrate selection by histone/protein lysine acetyltransferases"</a>. <i>Current Opinion in Structural Biology</i>. <b>18</b> (6): 682–9. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.sbi.2008.11.004">10.1016/j.sbi.2008.11.004</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2723715">2723715</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/19056256">19056256</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Current+Opinion+in+Structural+Biology&rft.atitle=Catalysis+and+substrate+selection+by+histone%2Fprotein+lysine+acetyltransferases&rft.volume=18&rft.issue=6&rft.pages=682-9&rft.date=2008-12&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2723715%23id-name%3DPMC&rft_id=info%3Apmid%2F19056256&rft_id=info%3Adoi%2F10.1016%2Fj.sbi.2008.11.004&rft.aulast=Berndsen&rft.aufirst=CE&rft.au=Denu%2C+JM&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2723715&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-BioEssays_(2004)-20"><span class="mw-cite-backlink">^ <a href="#cite_ref-BioEssays_(2004)_20-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-BioEssays_(2004)_20-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFYang2004" class="citation journal cs1">Yang XJ (October 2004). "Lysine acetylation and the bromodomain: a new partnership for signaling". <i>BioEssays</i>. <b>26</b> (10): 1076–87. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2Fbies.20104">10.1002/bies.20104</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/15382140">15382140</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:36755688">36755688</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=BioEssays&rft.atitle=Lysine+acetylation+and+the+bromodomain%3A+a+new+partnership+for+signaling&rft.volume=26&rft.issue=10&rft.pages=1076-87&rft.date=2004-10&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A36755688%23id-name%3DS2CID&rft_id=info%3Apmid%2F15382140&rft_id=info%3Adoi%2F10.1002%2Fbies.20104&rft.aulast=Yang&rft.aufirst=XJ&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Gene_(2005)-21"><span class="mw-cite-backlink">^ <a href="#cite_ref-Gene_(2005)_21-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Gene_(2005)_21-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Gene_(2005)_21-2"><sup><i><b>c</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFGlozakSenguptaZhangSeto2005" class="citation journal cs1">Glozak MA, Sengupta N, Zhang X, Seto E (December 2005). <a rel="nofollow" class="external text" href="https://www.sciencedirect.com/science/article/abs/pii/S037811190500572X">"Acetylation and deacetylation of non-histone proteins"</a>. <i>Gene</i>. <b>363</b>: 15–23. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.gene.2005.09.010">10.1016/j.gene.2005.09.010</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16289629">16289629</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Gene&rft.atitle=Acetylation+and+deacetylation+of+non-histone+proteins&rft.volume=363&rft.pages=15-23&rft.date=2005-12&rft_id=info%3Adoi%2F10.1016%2Fj.gene.2005.09.010&rft_id=info%3Apmid%2F16289629&rft.aulast=Glozak&rft.aufirst=MA&rft.au=Sengupta%2C+N&rft.au=Zhang%2C+X&rft.au=Seto%2C+E&rft_id=https%3A%2F%2Fwww.sciencedirect.com%2Fscience%2Farticle%2Fabs%2Fpii%2FS037811190500572X&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-22"><span class="mw-cite-backlink"><b><a href="#cite_ref-22">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFHataHirayamaKajihoNakagawa2012" class="citation journal cs1">Hata S, Hirayama J, Kajiho H, Nakagawa K, Hata Y, Katada T, Furutani-Seiki M, Nishina H (June 2012). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3381167">"A novel acetylation cycle of transcription co-activator Yes-associated protein that is downstream of Hippo pathway is triggered in response to SN2 alkylating agents"</a>. <i>The Journal of Biological Chemistry</i>. <b>287</b> (26): 22089–98. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M111.334714">10.1074/jbc.M111.334714</a></span>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3381167">3381167</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22544757">22544757</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Journal+of+Biological+Chemistry&rft.atitle=A+novel+acetylation+cycle+of+transcription+co-activator+Yes-associated+protein+that+is+downstream+of+Hippo+pathway+is+triggered+in+response+to+SN2+alkylating+agents&rft.volume=287&rft.issue=26&rft.pages=22089-98&rft.date=2012-06&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3381167%23id-name%3DPMC&rft_id=info%3Apmid%2F22544757&rft_id=info%3Adoi%2F10.1074%2Fjbc.M111.334714&rft.aulast=Hata&rft.aufirst=S&rft.au=Hirayama%2C+J&rft.au=Kajiho%2C+H&rft.au=Nakagawa%2C+K&rft.au=Hata%2C+Y&rft.au=Katada%2C+T&rft.au=Furutani-Seiki%2C+M&rft.au=Nishina%2C+H&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3381167&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Other3-23"><span class="mw-cite-backlink"><b><a href="#cite_ref-Other3_23-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFLiuWangZhaoThompson2008" class="citation journal cs1">Liu X, Wang L, Zhao K, Thompson PR, Hwang Y, Marmorstein R, Cole PA (February 2008). <a rel="nofollow" class="external text" href="https://www.nature.com/articles/nature06546">"The structural basis of protein acetylation by the p300/CBP transcriptional coactivator"</a>. <i>Nature</i>. <b>451</b> (7180): 846–50. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2008Natur.451..846L">2008Natur.451..846L</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2Fnature06546">10.1038/nature06546</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/18273021">18273021</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:4426988">4426988</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature&rft.atitle=The+structural+basis+of+protein+acetylation+by+the+p300%2FCBP+transcriptional+coactivator&rft.volume=451&rft.issue=7180&rft.pages=846-50&rft.date=2008-02&rft_id=info%3Adoi%2F10.1038%2Fnature06546&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A4426988%23id-name%3DS2CID&rft_id=info%3Apmid%2F18273021&rft_id=info%3Abibcode%2F2008Natur.451..846L&rft.aulast=Liu&rft.aufirst=X&rft.au=Wang%2C+L&rft.au=Zhao%2C+K&rft.au=Thompson%2C+PR&rft.au=Hwang%2C+Y&rft.au=Marmorstein%2C+R&rft.au=Cole%2C+PA&rft_id=https%3A%2F%2Fwww.nature.com%2Farticles%2Fnature06546&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Other4-24"><span class="mw-cite-backlink"><b><a href="#cite_ref-Other4_24-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFAlbaughArnoldLeeDenu2011" class="citation journal cs1">Albaugh BN, Arnold KM, Lee S, Denu JM (July 2011). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3137045">"Autoacetylation of the histone acetyltransferase Rtt109"</a>. <i>The Journal of Biological Chemistry</i>. <b>286</b> (28): 24694–701. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1074%2Fjbc.M111.251579">10.1074/jbc.M111.251579</a></span>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3137045">3137045</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/21606491">21606491</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=The+Journal+of+Biological+Chemistry&rft.atitle=Autoacetylation+of+the+histone+acetyltransferase+Rtt109&rft.volume=286&rft.issue=28&rft.pages=24694-701&rft.date=2011-07&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3137045%23id-name%3DPMC&rft_id=info%3Apmid%2F21606491&rft_id=info%3Adoi%2F10.1074%2Fjbc.M111.251579&rft.aulast=Albaugh&rft.aufirst=BN&rft.au=Arnold%2C+KM&rft.au=Lee%2C+S&rft.au=Denu%2C+JM&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3137045&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Voet-25"><span class="mw-cite-backlink">^ <a href="#cite_ref-Voet_25-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Voet_25-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Voet_25-2"><sup><i><b>c</b></i></sup></a> <a href="#cite_ref-Voet_25-3"><sup><i><b>d</b></i></sup></a> <a href="#cite_ref-Voet_25-4"><sup><i><b>e</b></i></sup></a> <a href="#cite_ref-Voet_25-5"><sup><i><b>f</b></i></sup></a> <a href="#cite_ref-Voet_25-6"><sup><i><b>g</b></i></sup></a> <a href="#cite_ref-Voet_25-7"><sup><i><b>h</b></i></sup></a> <a href="#cite_ref-Voet_25-8"><sup><i><b>i</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFVoetVoet2004" class="citation book cs1">Voet D, Voet JG (2004). <span class="id-lock-registration" title="Free registration required"><a rel="nofollow" class="external text" href="https://archive.org/details/biochemistry00voet_1"><i>Biochemistry</i></a></span> (3rd ed.). Hoboken, N.J.: John Wiley & Sons. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-471-19350-0" title="Special:BookSources/978-0-471-19350-0"><bdi>978-0-471-19350-0</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Biochemistry&rft.place=Hoboken%2C+N.J.&rft.edition=3rd&rft.pub=John+Wiley+%26+Sons&rft.date=2004&rft.isbn=978-0-471-19350-0&rft.aulast=Voet&rft.aufirst=Donald&rft.au=Voet%2C+Judith+G&rft_id=https%3A%2F%2Farchive.org%2Fdetails%2Fbiochemistry00voet_1&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Tropp-26"><span class="mw-cite-backlink">^ <a href="#cite_ref-Tropp_26-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Tropp_26-1"><sup><i><b>b</b></i></sup></a> <a href="#cite_ref-Tropp_26-2"><sup><i><b>c</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFTropp2008" class="citation book cs1">Tropp BE (2008). <span class="id-lock-registration" title="Free registration required"><a rel="nofollow" class="external text" href="https://archive.org/details/molecularbiology0000trop"><i>Molecular biology : genes to proteins</i></a></span> (3rd ed.). Sudbury, Mass.: Jones and Bartlett Publishers. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/9780763709167" title="Special:BookSources/9780763709167"><bdi>9780763709167</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Molecular+biology+%3A+genes+to+proteins&rft.place=Sudbury%2C+Mass.&rft.edition=3rd&rft.pub=Jones+and+Bartlett+Publishers&rft.date=2008&rft.isbn=9780763709167&rft.aulast=Tropp&rft.aufirst=Burton+E.&rft_id=https%3A%2F%2Farchive.org%2Fdetails%2Fmolecularbiology0000trop&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Grunstein-27"><span class="mw-cite-backlink"><b><a href="#cite_ref-Grunstein_27-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFGrunstein1997" class="citation journal cs1">Grunstein M (September 1997). <a rel="nofollow" class="external text" href="https://www.nature.com/articles/38664">"Histone acetylation in chromatin structure and transcription"</a>. <i>Nature</i>. <b>389</b> (6649): 349–52. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/1997Natur.389..349G">1997Natur.389..349G</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2F38664">10.1038/38664</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/9311776">9311776</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:4419816">4419816</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature&rft.atitle=Histone+acetylation+in+chromatin+structure+and+transcription&rft.volume=389&rft.issue=6649&rft.pages=349-52&rft.date=1997-09&rft_id=info%3Adoi%2F10.1038%2F38664&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A4419816%23id-name%3DS2CID&rft_id=info%3Apmid%2F9311776&rft_id=info%3Abibcode%2F1997Natur.389..349G&rft.aulast=Grunstein&rft.aufirst=M&rft_id=https%3A%2F%2Fwww.nature.com%2Farticles%2F38664&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-pmid26941319-28"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid26941319_28-0">^</a></b></span> <span class="reference-text"> <link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFVoichekBar-ZivBarkai2016" class="citation journal cs1">Voichek Y, Bar-Ziv R, Barkai N (March 2016). <a rel="nofollow" class="external text" href="https://www.science.org/doi/10.1126/science.aad1162">"Expression homeostasis during DNA replication"</a>. <i>Science</i>. <b>351</b> (6277): 1087–90. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2016Sci...351.1087V">2016Sci...351.1087V</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1126%2Fscience.aad1162">10.1126/science.aad1162</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/26941319">26941319</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:32751800">32751800</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Science&rft.atitle=Expression+homeostasis+during+DNA+replication&rft.volume=351&rft.issue=6277&rft.pages=1087-90&rft.date=2016-03&rft_id=info%3Adoi%2F10.1126%2Fscience.aad1162&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A32751800%23id-name%3DS2CID&rft_id=info%3Apmid%2F26941319&rft_id=info%3Abibcode%2F2016Sci...351.1087V&rft.aulast=Voichek&rft.aufirst=Y&rft.au=Bar-Ziv%2C+R&rft.au=Barkai%2C+N&rft_id=https%3A%2F%2Fwww.science.org%2Fdoi%2F10.1126%2Fscience.aad1162&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Zhou-29"><span class="mw-cite-backlink"><b><a href="#cite_ref-Zhou_29-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFDhalluinCarlsonZengHe1999" class="citation journal cs1">Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM (June 1999). <a rel="nofollow" class="external text" href="https://www.nature.com/articles/20974">"Structure and ligand of a histone acetyltransferase bromodomain"</a>. <i>Nature</i>. <b>399</b> (6735): 491–6. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/1999Natur.399..491D">1999Natur.399..491D</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1038%2F20974">10.1038/20974</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/10365964">10365964</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:1210925">1210925</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Nature&rft.atitle=Structure+and+ligand+of+a+histone+acetyltransferase+bromodomain&rft.volume=399&rft.issue=6735&rft.pages=491-6&rft.date=1999-06&rft_id=info%3Adoi%2F10.1038%2F20974&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A1210925%23id-name%3DS2CID&rft_id=info%3Apmid%2F10365964&rft_id=info%3Abibcode%2F1999Natur.399..491D&rft.aulast=Dhalluin&rft.aufirst=C&rft.au=Carlson%2C+JE&rft.au=Zeng%2C+L&rft.au=He%2C+C&rft.au=Aggarwal%2C+AK&rft.au=Zhou%2C+MM&rft_id=https%3A%2F%2Fwww.nature.com%2Farticles%2F20974&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Rossetto-30"><span class="mw-cite-backlink"><b><a href="#cite_ref-Rossetto_30-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFRossettoTrumanKronCôté2010" class="citation journal cs1">Rossetto D, Truman AW, Kron SJ, Côté J (September 2010). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2940951">"Epigenetic modifications in double-strand break DNA damage signaling and repair"</a>. <i>Clinical Cancer Research</i>. <b>16</b> (18): 4543–52. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1158%2F1078-0432.CCR-10-0513">10.1158/1078-0432.CCR-10-0513</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2940951">2940951</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/20823147">20823147</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Clinical+Cancer+Research&rft.atitle=Epigenetic+modifications+in+double-strand+break+DNA+damage+signaling+and+repair&rft.volume=16&rft.issue=18&rft.pages=4543-52&rft.date=2010-09&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2940951%23id-name%3DPMC&rft_id=info%3Apmid%2F20823147&rft_id=info%3Adoi%2F10.1158%2F1078-0432.CCR-10-0513&rft.aulast=Rossetto&rft.aufirst=D&rft.au=Truman%2C+AW&rft.au=Kron%2C+SJ&rft.au=C%C3%B4t%C3%A9%2C+J&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC2940951&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-editors-31"><span class="mw-cite-backlink">^ <a href="#cite_ref-editors_31-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-editors_31-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFKleinVande_Woude2002" class="citation book cs1">Klein G, Vande Woude GF (2002). <i>Advances in Cancer Research, Volume 86</i>. Boston: Academic Press. <a href="/wiki/ISBN_(identifier)" class="mw-redirect" title="ISBN (identifier)">ISBN</a> <a href="/wiki/Special:BookSources/978-0-12-006686-5" title="Special:BookSources/978-0-12-006686-5"><bdi>978-0-12-006686-5</bdi></a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rft.genre=book&rft.btitle=Advances+in+Cancer+Research%2C+Volume+86&rft.place=Boston&rft.pub=Academic+Press&rft.date=2002&rft.isbn=978-0-12-006686-5&rft.aulast=Klein&rft.aufirst=G&rft.au=Vande+Woude%2C+GF&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-pmid21746928-32"><span class="mw-cite-backlink">^ <a href="#cite_ref-pmid21746928_32-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-pmid21746928_32-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFKrishnanChowWangZhang2011" class="citation journal cs1">Krishnan V, Chow MZ, Wang Z, Zhang L, Liu B, Liu X, Zhou Z (July 2011). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3145730">"Histone H4 lysine 16 hypoacetylation is associated with defective DNA repair and premature senescence in Zmpste24-deficient mice"</a>. <i>Proc. Natl. Acad. Sci. U.S.A</i>. <b>108</b> (30): 12325–30. <a href="/wiki/Bibcode_(identifier)" class="mw-redirect" title="Bibcode (identifier)">Bibcode</a>:<a rel="nofollow" class="external text" href="https://ui.adsabs.harvard.edu/abs/2011PNAS..10812325K">2011PNAS..10812325K</a>. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://doi.org/10.1073%2Fpnas.1102789108">10.1073/pnas.1102789108</a></span>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3145730">3145730</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/21746928">21746928</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Proc.+Natl.+Acad.+Sci.+U.S.A.&rft.atitle=Histone+H4+lysine+16+hypoacetylation+is+associated+with+defective+DNA+repair+and+premature+senescence+in+Zmpste24-deficient+mice&rft.volume=108&rft.issue=30&rft.pages=12325-30&rft.date=2011-07&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3145730%23id-name%3DPMC&rft_id=info%3Apmid%2F21746928&rft_id=info%3Adoi%2F10.1073%2Fpnas.1102789108&rft_id=info%3Abibcode%2F2011PNAS..10812325K&rft.aulast=Krishnan&rft.aufirst=V&rft.au=Chow%2C+MZ&rft.au=Wang%2C+Z&rft.au=Zhang%2C+L&rft.au=Liu%2C+B&rft.au=Liu%2C+X&rft.au=Zhou%2C+Z&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3145730&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-pmid22884877-33"><span class="mw-cite-backlink"><b><a href="#cite_ref-pmid22884877_33-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFCvetanovicKularOpal2012" class="citation journal cs1">Cvetanovic M, Kular RK, Opal P (December 2012). <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3987943">"LANP mediates neuritic pathology in Spinocerebellar ataxia type 1"</a>. <i>Neurobiol. Dis</i>. <b>48</b> (3): 526–32. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.nbd.2012.07.024">10.1016/j.nbd.2012.07.024</a>. <a href="/wiki/PMC_(identifier)" class="mw-redirect" title="PMC (identifier)">PMC</a> <span class="id-lock-free" title="Freely accessible"><a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3987943">3987943</a></span>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22884877">22884877</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Neurobiol.+Dis.&rft.atitle=LANP+mediates+neuritic+pathology+in+Spinocerebellar+ataxia+type+1&rft.volume=48&rft.issue=3&rft.pages=526-32&rft.date=2012-12&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3987943%23id-name%3DPMC&rft_id=info%3Apmid%2F22884877&rft_id=info%3Adoi%2F10.1016%2Fj.nbd.2012.07.024&rft.aulast=Cvetanovic&rft.aufirst=M&rft.au=Kular%2C+RK&rft.au=Opal%2C+P&rft_id=https%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpmc%2Farticles%2FPMC3987943&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Furdas-34"><span class="mw-cite-backlink"><b><a href="#cite_ref-Furdas_34-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFFurdasKannanSipplJung2012" class="citation journal cs1">Furdas SD, Kannan S, Sippl W, Jung M (January 2012). <a rel="nofollow" class="external text" href="https://onlinelibrary.wiley.com/doi/10.1002/ardp.201100209">"Small molecule inhibitors of histone acetyltransferases as epigenetic tools and drug candidates"</a>. <i>Archiv der Pharmazie</i>. <b>345</b> (1): 7–21. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1002%2Fardp.201100209">10.1002/ardp.201100209</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22234972">22234972</a>. <a href="/wiki/S2CID_(identifier)" class="mw-redirect" title="S2CID (identifier)">S2CID</a> <a rel="nofollow" class="external text" href="https://api.semanticscholar.org/CorpusID:3125138">3125138</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=Archiv+der+Pharmazie&rft.atitle=Small+molecule+inhibitors+of+histone+acetyltransferases+as+epigenetic+tools+and+drug+candidates&rft.volume=345&rft.issue=1&rft.pages=7-21&rft.date=2012-01&rft_id=https%3A%2F%2Fapi.semanticscholar.org%2FCorpusID%3A3125138%23id-name%3DS2CID&rft_id=info%3Apmid%2F22234972&rft_id=info%3Adoi%2F10.1002%2Fardp.201100209&rft.aulast=Furdas&rft.aufirst=SD&rft.au=Kannan%2C+S&rft.au=Sippl%2C+W&rft.au=Jung%2C+M&rft_id=https%3A%2F%2Fonlinelibrary.wiley.com%2Fdoi%2F10.1002%2Fardp.201100209&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Oike-35"><span class="mw-cite-backlink">^ <a href="#cite_ref-Oike_35-0"><sup><i><b>a</b></i></sup></a> <a href="#cite_ref-Oike_35-1"><sup><i><b>b</b></i></sup></a></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFOikeOgiwaraTorikaiNakano2012" class="citation journal cs1">Oike T, Ogiwara H, Torikai K, Nakano T, Yokota J, Kohno T (November 2012). <a rel="nofollow" class="external text" href="https://www.redjournal.org/article/S0360-3016(12)00060-0/fulltext">"Garcinol, a histone acetyltransferase inhibitor, radiosensitizes cancer cells by inhibiting non-homologous end joining"</a>. <i>International Journal of Radiation Oncology, Biology, Physics</i>. <b>84</b> (3): 815–21. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.ijrobp.2012.01.017">10.1016/j.ijrobp.2012.01.017</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/22417805">22417805</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=International+Journal+of+Radiation+Oncology%2C+Biology%2C+Physics&rft.atitle=Garcinol%2C+a+histone+acetyltransferase+inhibitor%2C+radiosensitizes+cancer+cells+by+inhibiting+non-homologous+end+joining&rft.volume=84&rft.issue=3&rft.pages=815-21&rft.date=2012-11&rft_id=info%3Adoi%2F10.1016%2Fj.ijrobp.2012.01.017&rft_id=info%3Apmid%2F22417805&rft.aulast=Oike&rft.aufirst=T&rft.au=Ogiwara%2C+H&rft.au=Torikai%2C+K&rft.au=Nakano%2C+T&rft.au=Yokota%2C+J&rft.au=Kohno%2C+T&rft_id=https%3A%2F%2Fwww.redjournal.org%2Farticle%2FS0360-3016%2812%2900060-0%2Ffulltext&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> <li id="cite_note-Burma-36"><span class="mw-cite-backlink"><b><a href="#cite_ref-Burma_36-0">^</a></b></span> <span class="reference-text"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1238218222"><cite id="CITEREFBurmaChenChen2006" class="citation journal cs1">Burma S, Chen BP, Chen DJ (September 2006). <a rel="nofollow" class="external text" href="https://www.sciencedirect.com/science/article/abs/pii/S1568786406001650">"Role of non-homologous end joining (NHEJ) in maintaining genomic integrity"</a>. <i>DNA Repair</i>. <b>5</b> (9–10): 1042–8. <a href="/wiki/Doi_(identifier)" class="mw-redirect" title="Doi (identifier)">doi</a>:<a rel="nofollow" class="external text" href="https://doi.org/10.1016%2Fj.dnarep.2006.05.026">10.1016/j.dnarep.2006.05.026</a>. <a href="/wiki/PMID_(identifier)" class="mw-redirect" title="PMID (identifier)">PMID</a> <a rel="nofollow" class="external text" href="https://pubmed.ncbi.nlm.nih.gov/16822724">16822724</a>.</cite><span title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.jtitle=DNA+Repair&rft.atitle=Role+of+non-homologous+end+joining+%28NHEJ%29+in+maintaining+genomic+integrity&rft.volume=5&rft.issue=9%E2%80%9310&rft.pages=1042-8&rft.date=2006-09&rft_id=info%3Adoi%2F10.1016%2Fj.dnarep.2006.05.026&rft_id=info%3Apmid%2F16822724&rft.aulast=Burma&rft.aufirst=S&rft.au=Chen%2C+BP&rft.au=Chen%2C+DJ&rft_id=https%3A%2F%2Fwww.sciencedirect.com%2Fscience%2Farticle%2Fabs%2Fpii%2FS1568786406001650&rfr_id=info%3Asid%2Fen.wikipedia.org%3AHistone+acetyltransferase" class="Z3988"></span></span> </li> </ol></div> <div class="mw-heading mw-heading2"><h2 id="External_links">External links</h2><span class="mw-editsection"><span class="mw-editsection-bracket">[</span><a href="/w/index.php?title=Histone_acetyltransferase&action=edit&section=32" title="Edit section: External links"><span>edit</span></a><span class="mw-editsection-bracket">]</span></span></div> <ul><li><a rel="nofollow" class="external text" href="https://meshb.nlm.nih.gov/record/ui?name=Histone+Acetyltransferases">Histone+Acetyltransferases</a> at the U.S. National Library of Medicine <a href="/wiki/Medical_Subject_Headings" title="Medical Subject Headings">Medical Subject Headings</a> (MeSH)</li></ul> <div class="navbox-styles"><style data-mw-deduplicate="TemplateStyles:r1129693374">.mw-parser-output .hlist dl,.mw-parser-output .hlist ol,.mw-parser-output .hlist ul{margin:0;padding:0}.mw-parser-output .hlist dd,.mw-parser-output .hlist dt,.mw-parser-output .hlist li{margin:0;display:inline}.mw-parser-output .hlist.inline,.mw-parser-output .hlist.inline dl,.mw-parser-output .hlist.inline ol,.mw-parser-output .hlist.inline ul,.mw-parser-output .hlist dl dl,.mw-parser-output .hlist dl ol,.mw-parser-output .hlist dl ul,.mw-parser-output .hlist ol dl,.mw-parser-output .hlist ol ol,.mw-parser-output .hlist ol ul,.mw-parser-output .hlist ul dl,.mw-parser-output .hlist ul ol,.mw-parser-output .hlist ul ul{display:inline}.mw-parser-output .hlist .mw-empty-li{display:none}.mw-parser-output .hlist dt::after{content:": "}.mw-parser-output .hlist dd::after,.mw-parser-output .hlist li::after{content:" · ";font-weight:bold}.mw-parser-output .hlist dd:last-child::after,.mw-parser-output .hlist dt:last-child::after,.mw-parser-output .hlist li:last-child::after{content:none}.mw-parser-output .hlist dd dd:first-child::before,.mw-parser-output .hlist dd dt:first-child::before,.mw-parser-output .hlist dd li:first-child::before,.mw-parser-output .hlist dt dd:first-child::before,.mw-parser-output .hlist dt dt:first-child::before,.mw-parser-output .hlist dt li:first-child::before,.mw-parser-output .hlist li dd:first-child::before,.mw-parser-output .hlist li dt:first-child::before,.mw-parser-output .hlist li li:first-child::before{content:" (";font-weight:normal}.mw-parser-output .hlist dd dd:last-child::after,.mw-parser-output .hlist dd dt:last-child::after,.mw-parser-output .hlist dd li:last-child::after,.mw-parser-output .hlist dt dd:last-child::after,.mw-parser-output .hlist dt dt:last-child::after,.mw-parser-output .hlist dt li:last-child::after,.mw-parser-output .hlist li dd:last-child::after,.mw-parser-output .hlist li dt:last-child::after,.mw-parser-output .hlist li li:last-child::after{content:")";font-weight:normal}.mw-parser-output .hlist ol{counter-reset:listitem}.mw-parser-output .hlist ol>li{counter-increment:listitem}.mw-parser-output .hlist ol>li::before{content:" "counter(listitem)"\a0 "}.mw-parser-output .hlist dd ol>li:first-child::before,.mw-parser-output .hlist dt ol>li:first-child::before,.mw-parser-output .hlist li ol>li:first-child::before{content:" ("counter(listitem)"\a0 "}</style><style data-mw-deduplicate="TemplateStyles:r1236075235">.mw-parser-output .navbox{box-sizing:border-box;border:1px solid #a2a9b1;width:100%;clear:both;font-size:88%;text-align:center;padding:1px;margin:1em auto 0}.mw-parser-output .navbox .navbox{margin-top:0}.mw-parser-output .navbox+.navbox,.mw-parser-output .navbox+.navbox-styles+.navbox{margin-top:-1px}.mw-parser-output .navbox-inner,.mw-parser-output .navbox-subgroup{width:100%}.mw-parser-output .navbox-group,.mw-parser-output .navbox-title,.mw-parser-output .navbox-abovebelow{padding:0.25em 1em;line-height:1.5em;text-align:center}.mw-parser-output .navbox-group{white-space:nowrap;text-align:right}.mw-parser-output .navbox,.mw-parser-output .navbox-subgroup{background-color:#fdfdfd}.mw-parser-output .navbox-list{line-height:1.5em;border-color:#fdfdfd}.mw-parser-output .navbox-list-with-group{text-align:left;border-left-width:2px;border-left-style:solid}.mw-parser-output tr+tr>.navbox-abovebelow,.mw-parser-output tr+tr>.navbox-group,.mw-parser-output tr+tr>.navbox-image,.mw-parser-output tr+tr>.navbox-list{border-top:2px solid #fdfdfd}.mw-parser-output .navbox-title{background-color:#ccf}.mw-parser-output .navbox-abovebelow,.mw-parser-output .navbox-group,.mw-parser-output .navbox-subgroup .navbox-title{background-color:#ddf}.mw-parser-output .navbox-subgroup .navbox-group,.mw-parser-output .navbox-subgroup .navbox-abovebelow{background-color:#e6e6ff}.mw-parser-output .navbox-even{background-color:#f7f7f7}.mw-parser-output .navbox-odd{background-color:transparent}.mw-parser-output .navbox .hlist td dl,.mw-parser-output .navbox .hlist td ol,.mw-parser-output .navbox .hlist td ul,.mw-parser-output .navbox td.hlist dl,.mw-parser-output .navbox td.hlist ol,.mw-parser-output .navbox td.hlist ul{padding:0.125em 0}.mw-parser-output .navbox .navbar{display:block;font-size:100%}.mw-parser-output .navbox-title .navbar{float:left;text-align:left;margin-right:0.5em}body.skin--responsive .mw-parser-output .navbox-image img{max-width:none!important}@media print{body.ns-0 .mw-parser-output .navbox{display:none!important}}</style></div><div role="navigation" class="navbox" aria-labelledby="Transcription_(Bacterial,_Eukaryotic)" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><style data-mw-deduplicate="TemplateStyles:r1239400231">.mw-parser-output .navbar{display:inline;font-size:88%;font-weight:normal}.mw-parser-output .navbar-collapse{float:left;text-align:left}.mw-parser-output .navbar-boxtext{word-spacing:0}.mw-parser-output .navbar ul{display:inline-block;white-space:nowrap;line-height:inherit}.mw-parser-output .navbar-brackets::before{margin-right:-0.125em;content:"[ "}.mw-parser-output .navbar-brackets::after{margin-left:-0.125em;content:" ]"}.mw-parser-output .navbar li{word-spacing:-0.125em}.mw-parser-output .navbar a>span,.mw-parser-output .navbar a>abbr{text-decoration:inherit}.mw-parser-output .navbar-mini abbr{font-variant:small-caps;border-bottom:none;text-decoration:none;cursor:inherit}.mw-parser-output .navbar-ct-full{font-size:114%;margin:0 7em}.mw-parser-output .navbar-ct-mini{font-size:114%;margin:0 4em}html.skin-theme-clientpref-night .mw-parser-output .navbar li a abbr{color:var(--color-base)!important}@media(prefers-color-scheme:dark){html.skin-theme-clientpref-os .mw-parser-output .navbar li a abbr{color:var(--color-base)!important}}@media print{.mw-parser-output .navbar{display:none!important}}</style><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Transcription" title="Template:Transcription"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Transcription" title="Template talk:Transcription"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Transcription" title="Special:EditPage/Template:Transcription"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Transcription_(Bacterial,_Eukaryotic)" style="font-size:114%;margin:0 4em"><a href="/wiki/Transcription_(genetics)" class="mw-redirect" title="Transcription (genetics)">Transcription</a> (<a href="/wiki/Bacterial_transcription" title="Bacterial transcription">Bacterial</a>, <a href="/wiki/Eukaryotic_transcription" title="Eukaryotic transcription">Eukaryotic</a>)</div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Transcriptional_regulation" title="Transcriptional regulation">Transcriptional regulation</a></th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%">prokaryotic</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Operon" title="Operon">Operon</a> <ul><li><a href="/wiki/Lac_operon" title="Lac operon">lac operon</a></li> <li><a href="/wiki/Trp_operon" title="Trp operon">trp operon</a></li> <li><a href="/wiki/Gab_operon" title="Gab operon">gab operon</a></li> <li><a href="/wiki/Gua_Operon" title="Gua Operon">Gua Operon</a></li> <li><a href="/wiki/L-arabinose_operon" title="L-arabinose operon">ara operon</a></li> <li><a href="/wiki/Gal_operon" title="Gal operon">gal operon</a></li></ul></li> <li><a href="/wiki/Repressor" title="Repressor">Repressor</a> <ul><li><a href="/wiki/Lac_repressor" title="Lac repressor">lac repressor</a></li> <li><a href="/wiki/Tryptophan_repressor" title="Tryptophan repressor">trp repressor</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">eukaryotic</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"></div><table class="nowraplinks navbox-subgroup" style="border-spacing:0"><tbody><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Histone-modifying_enzymes" title="Histone-modifying enzymes">Histone-modifying enzymes</a><br />(<a href="/wiki/Histone" title="Histone">histone</a>/<a href="/wiki/Nucleosome" title="Nucleosome">nucleosome</a>):</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Histone_methylation" title="Histone methylation">Histone methylation</a>/<a href="/wiki/Histone_methyltransferase" title="Histone methyltransferase">Histone methyltransferase</a> <ul><li><a href="/wiki/EZH2" title="EZH2">EZH2</a></li></ul></li> <li><a href="/wiki/Demethylase" title="Demethylase">Histone demethylase</a></li> <li><a href="/wiki/Histone_acetylation_and_deacetylation" title="Histone acetylation and deacetylation">Histone acetylation and deacetylation</a> <ul><li><a href="/wiki/Histone_deacetylase" title="Histone deacetylase">Histone deacetylase</a> <a href="/wiki/HDAC1" title="HDAC1">HDAC1</a></li> <li><a class="mw-selflink selflink">Histone acetyltransferase</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/DNA_methylation" title="DNA methylation">DNA methylation</a>:</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><ul><li><a href="/wiki/DNA_methyltransferase" title="DNA methyltransferase">DNA methyltransferase</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/Chromatin_remodeling" title="Chromatin remodeling">Chromatin remodeling</a>:</th><td class="navbox-list-with-group navbox-list navbox-even" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/CHD7" title="CHD7">CHD7</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">both</th><td class="navbox-list-with-group navbox-list navbox-odd" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Transcription_coregulator" title="Transcription coregulator">Transcription coregulator</a> <ul><li><a href="/wiki/Activator_(genetics)" title="Activator (genetics)">Activator</a></li> <li><a href="/wiki/Coactivator_(genetics)" title="Coactivator (genetics)">Coactivator</a></li> <li><a href="/wiki/Corepressor" title="Corepressor">Corepressor</a></li></ul></li> <li><a href="/wiki/Inducer" title="Inducer">Inducer</a></li></ul> </div></td></tr></tbody></table><div></div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Promotion</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Promoter_(genetics)" title="Promoter (genetics)">Promoter</a> <ul><li><a href="/wiki/Pribnow_box" title="Pribnow box">Pribnow box</a></li> <li><a href="/wiki/TATA_box" title="TATA box">TATA box</a></li> <li><a href="/wiki/B_recognition_element" title="B recognition element">BRE</a></li> <li><a href="/wiki/CAAT_box" title="CAAT box">CAAT box</a></li> <li><a href="/wiki/Response_element" title="Response element">Response element</a></li></ul></li> <li><a href="/wiki/Enhancer_(genetics)" title="Enhancer (genetics)">Enhancer</a> <ul><li><a href="/wiki/E-box" title="E-box">E-box</a></li> <li><a href="/wiki/Response_element" title="Response element">Response element</a></li></ul></li> <li><a href="/wiki/Insulator_(genetics)" title="Insulator (genetics)">Insulator</a></li> <li><a href="/wiki/Silencer_(DNA)" class="mw-redirect" title="Silencer (DNA)">Silencer</a></li> <li><a href="/wiki/Internal_control_region" title="Internal control region">Internal control region</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Initiation</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Bacterial_transcription#Initiation" title="Bacterial transcription">Bacterial</a></li> <li><a href="/wiki/Eukaryotic_transcription#Initiation" title="Eukaryotic transcription">Eukaryotic</a></li> <li><a href="/wiki/Archaeal_transcription_factor_B" title="Archaeal transcription factor B">Archaeal transcription factor B</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Elongation</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Bacterial_transcription#Elongation" title="Bacterial transcription">bacterial</a> <a href="/wiki/RNA_polymerase" title="RNA polymerase">RNA polymerase</a>: <a href="/wiki/RpoB" title="RpoB">rpoB</a></li> <li><a href="/wiki/Eukaryotic_transcription#Transcription_process" title="Eukaryotic transcription">eukaryotic</a> <a href="/wiki/RNA_polymerase" title="RNA polymerase">RNA polymerase</a>: <a href="/wiki/RNA_polymerase_II" title="RNA polymerase II">RNA polymerase II</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Termination<br />(<a href="/wiki/Bacterial_transcription#Termination" title="Bacterial transcription">bacterial</a>,<br /> <a href="/wiki/Eukaryotic_transcription#Termination" title="Eukaryotic transcription">eukaryotic</a>)</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Terminator_(genetics)" title="Terminator (genetics)">Terminator</a></li> <li><a href="/wiki/Intrinsic_termination" title="Intrinsic termination">Intrinsic termination</a></li> <li><a href="/wiki/Rho_factor" title="Rho factor">Rho factor</a></li></ul> </div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235"></div><div role="navigation" class="navbox" aria-labelledby="Transferases:_acyltransferases_(EC_2.3)" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231"><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Acyltransferases" title="Template:Acyltransferases"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Acyltransferases" title="Template talk:Acyltransferases"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Acyltransferases" title="Special:EditPage/Template:Acyltransferases"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Transferases:_acyltransferases_(EC_2.3)" style="font-size:114%;margin:0 4em"><a href="/wiki/Transferase" title="Transferase">Transferases</a>: <a href="/wiki/Acyltransferase" title="Acyltransferase">acyltransferases</a> (<a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC</a> 2.3)</div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_2)#EC_2.3.1:_Transferring_groups_other_than_amino-acyl_groups" title="List of EC numbers (EC 2)">2.3.1</a>: other than amino-acyl groups</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><i><a href="/wiki/Acetyltransferase" title="Acetyltransferase">acetyltransferases</a>:</i> <a href="/wiki/Thiolase" title="Thiolase">Acetyl-Coenzyme A acetyltransferase</a></li> <li><a href="/wiki/N-Acetylglutamate_synthase" title="N-Acetylglutamate synthase">N-Acetylglutamate synthase</a></li> <li><a href="/wiki/Choline_acetyltransferase" title="Choline acetyltransferase">Choline acetyltransferase</a></li> <li><a href="/wiki/Dihydrolipoyl_transacetylase" title="Dihydrolipoyl transacetylase">Dihydrolipoyl transacetylase</a></li> <li><a href="/wiki/Acetyl-CoA_C-acyltransferase" class="mw-redirect" title="Acetyl-CoA C-acyltransferase">Acetyl-CoA C-acyltransferase</a></li> <li><a href="/wiki/Beta-galactoside_transacetylase" class="mw-redirect" title="Beta-galactoside transacetylase">Beta-galactoside transacetylase</a></li> <li><a href="/wiki/Chloramphenicol_acetyltransferase" title="Chloramphenicol acetyltransferase">Chloramphenicol acetyltransferase</a></li> <li><a href="/wiki/N-acetyltransferase" title="N-acetyltransferase">N-acetyltransferase</a> <ul><li><a href="/wiki/Serotonin_N-acetyl_transferase" class="mw-redirect" title="Serotonin N-acetyl transferase">Serotonin N-acetyl transferase</a></li> <li><a href="/wiki/HGSNAT" title="HGSNAT">HGSNAT</a></li> <li><a href="/wiki/ARD1A" class="mw-redirect" title="ARD1A">ARD1A</a></li></ul></li> <li><a class="mw-selflink selflink">Histone acetyltransferase</a> <ul><li><a href="/wiki/P300-CBP_coactivator_family" title="P300-CBP coactivator family">P300/CBP</a></li> <li><a href="/wiki/NAT2" class="mw-redirect" title="NAT2">NAT2</a></li></ul></li></ul> <ul><li><i><a href="/wiki/Palmitoyltransferase" class="mw-redirect" title="Palmitoyltransferase">palmitoyltransferases</a>:</i> <a href="/wiki/Carnitine_O-palmitoyltransferase" title="Carnitine O-palmitoyltransferase">Carnitine O-palmitoyltransferase</a> <ul><li><a href="/wiki/Carnitine_palmitoyltransferase_I" title="Carnitine palmitoyltransferase I">CPT1</a></li> <li><a href="/wiki/Carnitine_palmitoyltransferase_II" title="Carnitine palmitoyltransferase II">CPT2</a></li></ul></li> <li><a href="/wiki/Serine_C-palmitoyltransferase" title="Serine C-palmitoyltransferase">Serine C-palmitoyltransferase</a> <ul><li><a href="/wiki/SPTLC1" title="SPTLC1">SPTLC1</a></li> <li><a href="/wiki/SPTLC2" title="SPTLC2">SPTLC2</a></li></ul></li></ul> <ul><li><i>other:</i> <a href="/wiki/Acyltransferase_like_2" title="Acyltransferase like 2">Acyltransferase like 2</a></li> <li><a href="/wiki/Aminolevulinic_acid_synthase" title="Aminolevulinic acid synthase">Aminolevulinic acid synthase</a></li> <li><a href="/wiki/Beta-ketoacyl-ACP_synthase" title="Beta-ketoacyl-ACP synthase">Beta-ketoacyl-ACP synthase</a></li> <li><a href="/wiki/Glyceronephosphate_O-acyltransferase" title="Glyceronephosphate O-acyltransferase">Glyceronephosphate O-acyltransferase</a></li> <li><a href="/wiki/Lecithin%E2%80%94cholesterol_acyltransferase" class="mw-redirect" title="Lecithin—cholesterol acyltransferase">Lecithin—cholesterol acyltransferase </a></li></ul> <ul><li><a href="/wiki/Glycerol-3-phosphate_O-acyltransferase" title="Glycerol-3-phosphate O-acyltransferase">Glycerol-3-phosphate O-acyltransferase</a></li> <li><a href="/wiki/1-acylglycerol-3-phosphate_O-acyltransferase" title="1-acylglycerol-3-phosphate O-acyltransferase">1-acylglycerol-3-phosphate O-acyltransferase</a></li> <li><a href="/wiki/2-acylglycerol-3-phosphate_O-acyltransferase" title="2-acylglycerol-3-phosphate O-acyltransferase">2-acylglycerol-3-phosphate O-acyltransferase</a></li> <li><a href="/wiki/ABHD5" title="ABHD5">ABHD5</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_2)#EC_2.3.2:_Aminoacyltransferases" title="List of EC numbers (EC 2)">2.3.2</a>: <a href="/wiki/Aminoacyltransferase" title="Aminoacyltransferase">Aminoacyltransferases</a></th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Gamma-glutamyl_transpeptidase" class="mw-redirect" title="Gamma-glutamyl transpeptidase">Gamma-glutamyl transpeptidase</a></li> <li><a href="/wiki/Peptidyl_transferase" class="mw-redirect" title="Peptidyl transferase">Peptidyl transferase</a></li> <li><a href="/wiki/Transglutaminase" title="Transglutaminase">Transglutaminase</a> <ul><li><a href="/wiki/Tissue_transglutaminase" title="Tissue transglutaminase">Tissue transglutaminase</a></li> <li><a href="/wiki/Keratinocyte_transglutaminase" title="Keratinocyte transglutaminase">Keratinocyte transglutaminase</a></li> <li><a href="/wiki/Factor_XIII" title="Factor XIII">Factor XIII</a></li></ul></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%"><a href="/wiki/List_of_EC_numbers_(EC_2)#EC_2.3.3:_Acyl_groups_converted_into_alkyl_on_transfer" title="List of EC numbers (EC 2)">2.3.3</a>: converted into alkyl on transfer</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Citrate_synthase" title="Citrate synthase">Citrate synthase</a></li> <li><a href="/wiki/Decylcitrate_synthase" title="Decylcitrate synthase">Decylcitrate synthase</a></li> <li><a href="/wiki/Citrate_(Re)-synthase" title="Citrate (Re)-synthase">Citrate (Re)-synthase</a></li> <li><a href="/wiki/Decylhomocitrate_synthase" title="Decylhomocitrate synthase">Decylhomocitrate synthase</a></li> <li><a href="/wiki/2-methylcitrate_synthase" title="2-methylcitrate synthase">2-methylcitrate synthase</a></li> <li><a href="/wiki/2-ethylmalate_synthase" title="2-ethylmalate synthase">2-ethylmalate synthase</a></li> <li><a href="/wiki/3-ethylmalate_synthase" title="3-ethylmalate synthase">3-ethylmalate synthase</a></li> <li><a href="/wiki/ATP_citrate_lyase" class="mw-redirect" title="ATP citrate lyase">ATP citrate lyase</a></li> <li><a href="/wiki/Malate_synthase" title="Malate synthase">Malate synthase</a></li> <li><a href="/wiki/Hydroxymethylglutaryl-CoA_synthase" title="Hydroxymethylglutaryl-CoA synthase">HMG-CoA synthase</a> <ul><li><a href="/wiki/HMGCS2" title="HMGCS2">HMGCS2</a></li></ul></li> <li><a href="/wiki/2-hydroxyglutarate_synthase" title="2-hydroxyglutarate synthase">2-hydroxyglutarate synthase</a></li> <li><a href="/wiki/3-propylmalate_synthase" title="3-propylmalate synthase">3-propylmalate synthase</a></li> <li><a href="/wiki/2-isopropylmalate_synthase" title="2-isopropylmalate synthase">2-isopropylmalate synthase</a></li> <li><a href="/wiki/Homocitrate_synthase" title="Homocitrate synthase">Homocitrate synthase</a></li> <li><a href="/wiki/Sulfoacetaldehyde_acetyltransferase" title="Sulfoacetaldehyde acetyltransferase">Sulfoacetaldehyde acetyltransferase</a></li></ul> </div></td></tr></tbody></table></div> <div class="navbox-styles"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1236075235"></div><div role="navigation" class="navbox" aria-labelledby="Enzymes" style="padding:3px"><table class="nowraplinks mw-collapsible autocollapse navbox-inner" style="border-spacing:0;background:transparent;color:inherit"><tbody><tr><th scope="col" class="navbox-title" colspan="2"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1129693374"><link rel="mw-deduplicated-inline-style" href="mw-data:TemplateStyles:r1239400231"><div class="navbar plainlinks hlist navbar-mini"><ul><li class="nv-view"><a href="/wiki/Template:Enzymes" title="Template:Enzymes"><abbr title="View this template">v</abbr></a></li><li class="nv-talk"><a href="/wiki/Template_talk:Enzymes" title="Template talk:Enzymes"><abbr title="Discuss this template">t</abbr></a></li><li class="nv-edit"><a href="/wiki/Special:EditPage/Template:Enzymes" title="Special:EditPage/Template:Enzymes"><abbr title="Edit this template">e</abbr></a></li></ul></div><div id="Enzymes" style="font-size:114%;margin:0 4em"><a href="/wiki/Enzyme" title="Enzyme">Enzymes</a></div></th></tr><tr><th scope="row" class="navbox-group" style="width:1%">Activity</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Active_site" title="Active site">Active site</a></li> <li><a href="/wiki/Binding_site" title="Binding site">Binding site</a></li> <li><a href="/wiki/Catalytic_triad" title="Catalytic triad">Catalytic triad</a></li> <li><a href="/wiki/Oxyanion_hole" title="Oxyanion hole">Oxyanion hole</a></li> <li><a href="/wiki/Enzyme_promiscuity" title="Enzyme promiscuity">Enzyme promiscuity</a></li> <li><a href="/wiki/Diffusion-limited_enzyme" title="Diffusion-limited enzyme">Diffusion-limited enzyme</a></li> <li><a href="/wiki/Cofactor_(biochemistry)" title="Cofactor (biochemistry)">Cofactor</a></li> <li><a href="/wiki/Enzyme_catalysis" title="Enzyme catalysis">Enzyme catalysis</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Regulation</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Allosteric_regulation" title="Allosteric regulation">Allosteric regulation</a></li> <li><a href="/wiki/Cooperativity" title="Cooperativity">Cooperativity</a></li> <li><a href="/wiki/Enzyme_inhibitor" title="Enzyme inhibitor">Enzyme inhibitor</a></li> <li><a href="/wiki/Enzyme_activator" title="Enzyme activator">Enzyme activator</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Classification</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Enzyme_Commission_number" title="Enzyme Commission number">EC number</a></li> <li><a href="/wiki/Protein_superfamily" title="Protein superfamily">Enzyme superfamily</a></li> <li><a href="/wiki/Protein_family" title="Protein family">Enzyme family</a></li> <li><a href="/wiki/List_of_enzymes" title="List of enzymes">List of enzymes</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Kinetics</th><td class="navbox-list-with-group navbox-list navbox-even hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><a href="/wiki/Enzyme_kinetics" title="Enzyme kinetics">Enzyme kinetics</a></li> <li><a href="/wiki/Eadie%E2%80%93Hofstee_diagram" title="Eadie–Hofstee diagram">Eadie–Hofstee diagram</a></li> <li><a href="/wiki/Hanes%E2%80%93Woolf_plot" title="Hanes–Woolf plot">Hanes–Woolf plot</a></li> <li><a href="/wiki/Lineweaver%E2%80%93Burk_plot" title="Lineweaver–Burk plot">Lineweaver–Burk plot</a></li> <li><a href="/wiki/Michaelis%E2%80%93Menten_kinetics" title="Michaelis–Menten kinetics">Michaelis–Menten kinetics</a></li></ul> </div></td></tr><tr><th scope="row" class="navbox-group" style="width:1%">Types</th><td class="navbox-list-with-group navbox-list navbox-odd hlist" style="width:100%;padding:0"><div style="padding:0 0.25em"> <ul><li><b>EC1 <a href="/wiki/Oxidoreductase" title="Oxidoreductase">Oxidoreductases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_1)" title="List of EC numbers (EC 1)">list</a>)</li> <li><b>EC2 <a href="/wiki/Transferase" title="Transferase">Transferases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_2)" title="List of EC numbers (EC 2)">list</a>)</li> <li><b>EC3 <a href="/wiki/Hydrolase" title="Hydrolase">Hydrolases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_3)" title="List of EC numbers (EC 3)">list</a>)</li> <li><b>EC4 <a href="/wiki/Lyase" title="Lyase">Lyases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_4)" title="List of EC numbers (EC 4)">list</a>)</li> <li><b>EC5 <a href="/wiki/Isomerase" title="Isomerase">Isomerases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_5)" title="List of EC numbers (EC 5)">list</a>)</li> <li><b>EC6 <a href="/wiki/Ligase" title="Ligase">Ligases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_6)" title="List of EC numbers (EC 6)">list</a>)</li> <li><b>EC7 <a href="/wiki/Translocase" title="Translocase">Translocases</a></b> (<a href="/wiki/List_of_EC_numbers_(EC_7)" title="List of EC numbers (EC 7)">list</a>)</li></ul> </div></td></tr></tbody></table></div> <style data-mw-deduplicate="TemplateStyles:r1130092004">.mw-parser-output .portal-bar{font-size:88%;font-weight:bold;display:flex;justify-content:center;align-items:baseline}.mw-parser-output .portal-bar-bordered{padding:0 2em;background-color:#fdfdfd;border:1px solid #a2a9b1;clear:both;margin:1em auto 0}.mw-parser-output .portal-bar-related{font-size:100%;justify-content:flex-start}.mw-parser-output .portal-bar-unbordered{padding:0 1.7em;margin-left:0}.mw-parser-output .portal-bar-header{margin:0 1em 0 0.5em;flex:0 0 auto;min-height:24px}.mw-parser-output .portal-bar-content{display:flex;flex-flow:row wrap;flex:0 1 auto;padding:0.15em 0;column-gap:1em;align-items:baseline;margin:0;list-style:none}.mw-parser-output .portal-bar-content-related{margin:0;list-style:none}.mw-parser-output .portal-bar-item{display:inline-block;margin:0.15em 0.2em;min-height:24px;line-height:24px}@media screen and (max-width:768px){.mw-parser-output .portal-bar{font-size:88%;font-weight:bold;display:flex;flex-flow:column wrap;align-items:baseline}.mw-parser-output .portal-bar-header{text-align:center;flex:0;padding-left:0.5em;margin:0 auto}.mw-parser-output .portal-bar-related{font-size:100%;align-items:flex-start}.mw-parser-output .portal-bar-content{display:flex;flex-flow:row wrap;align-items:center;flex:0;column-gap:1em;border-top:1px solid #a2a9b1;margin:0 auto;list-style:none}.mw-parser-output .portal-bar-content-related{border-top:none;margin:0;list-style:none}}.mw-parser-output .navbox+link+.portal-bar,.mw-parser-output .navbox+style+.portal-bar,.mw-parser-output .navbox+link+.portal-bar-bordered,.mw-parser-output .navbox+style+.portal-bar-bordered,.mw-parser-output .sister-bar+link+.portal-bar,.mw-parser-output .sister-bar+style+.portal-bar,.mw-parser-output .portal-bar+.navbox-styles+.navbox,.mw-parser-output .portal-bar+.navbox-styles+.sister-bar{margin-top:-1px}</style><div class="portal-bar noprint metadata noviewer portal-bar-unbordered" role="navigation" aria-label="Portals"><span class="portal-bar-header"><a href="/wiki/Wikipedia:Contents/Portals" title="Wikipedia:Contents/Portals">Portal</a>:</span><ul class="portal-bar-content"><li class="portal-bar-item"><span class="nowrap"><span typeof="mw:File"><a href="/wiki/File:Issoria_lathonia.jpg" class="mw-file-description"><img alt="icon" src="//upload.wikimedia.org/wikipedia/commons/thumb/2/2d/Issoria_lathonia.jpg/21px-Issoria_lathonia.jpg" decoding="async" width="21" height="15" class="mw-file-element" srcset="//upload.wikimedia.org/wikipedia/commons/thumb/2/2d/Issoria_lathonia.jpg/32px-Issoria_lathonia.jpg 1.5x, //upload.wikimedia.org/wikipedia/commons/thumb/2/2d/Issoria_lathonia.jpg/42px-Issoria_lathonia.jpg 2x" data-file-width="629" data-file-height="445" /></a></span> </span><a href="/wiki/Portal:Biology" title="Portal:Biology">Biology</a></li></ul></div>    </div><noscript><img src="https://login.wikimedia.org/wiki/Special:CentralAutoLogin/start?type=1x1" alt="" width="1" height="1" style="border: none; position: absolute;"></noscript> <div class="printfooter" data-nosnippet="">Retrieved from "<a dir="ltr" href="https://en.wikipedia.org/w/index.php?title=Histone_acetyltransferase&oldid=1242313011">https://en.wikipedia.org/w/index.php?title=Histone_acetyltransferase&oldid=1242313011</a>"</div></div> <div id="catlinks" class="catlinks" data-mw="interface"><div id="mw-normal-catlinks" class="mw-normal-catlinks"><a href="/wiki/Help:Category" title="Help:Category">Categories</a>: <ul><li><a href="/wiki/Category:Transferases" title="Category:Transferases">Transferases</a></li><li><a href="/wiki/Category:EC_2.3.1" title="Category:EC 2.3.1">EC 2.3.1</a></li><li><a href="/wiki/Category:Epigenetics" title="Category:Epigenetics">Epigenetics</a></li></ul></div><div id="mw-hidden-catlinks" class="mw-hidden-catlinks mw-hidden-cats-hidden">Hidden categories: <ul><li><a href="/wiki/Category:Articles_with_short_description" title="Category:Articles with short description">Articles with short description</a></li><li><a href="/wiki/Category:Short_description_matches_Wikidata" title="Category:Short description matches Wikidata">Short description matches Wikidata</a></li><li><a href="/wiki/Category:All_articles_with_unsourced_statements" title="Category:All articles with unsourced statements">All articles with unsourced statements</a></li><li><a href="/wiki/Category:Articles_with_unsourced_statements_from_April_2021" title="Category:Articles with unsourced statements from April 2021">Articles with unsourced statements from April 2021</a></li></ul></div></div> </div> </main> </div> <div class="mw-footer-container"> <footer id="footer" class="mw-footer" > <ul id="footer-info"> <li id="footer-info-lastmod"> This page was last edited on 26 August 2024, at 04:41<span class="anonymous-show"> (UTC)</span>.</li> <li id="footer-info-copyright">Text is available under the <a href="/wiki/Wikipedia:Text_of_the_Creative_Commons_Attribution-ShareAlike_4.0_International_License" title="Wikipedia:Text of the Creative Commons Attribution-ShareAlike 4.0 International License">Creative Commons Attribution-ShareAlike 4.0 License</a>; additional terms may apply. By using this site, you agree to the <a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Terms_of_Use" class="extiw" title="foundation:Special:MyLanguage/Policy:Terms of Use">Terms of Use</a> and <a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Privacy_policy" class="extiw" title="foundation:Special:MyLanguage/Policy:Privacy policy">Privacy Policy</a>. Wikipedia® is a registered trademark of the <a rel="nofollow" class="external text" href="https://wikimediafoundation.org/">Wikimedia Foundation, Inc.</a>, a non-profit organization.</li> </ul> <ul id="footer-places"> <li id="footer-places-privacy"><a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Privacy_policy">Privacy policy</a></li> <li id="footer-places-about"><a href="/wiki/Wikipedia:About">About Wikipedia</a></li> <li id="footer-places-disclaimers"><a href="/wiki/Wikipedia:General_disclaimer">Disclaimers</a></li> <li id="footer-places-contact"><a href="//en.wikipedia.org/wiki/Wikipedia:Contact_us">Contact Wikipedia</a></li> <li id="footer-places-wm-codeofconduct"><a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Universal_Code_of_Conduct">Code of Conduct</a></li> <li id="footer-places-developers"><a href="https://developer.wikimedia.org">Developers</a></li> <li id="footer-places-statslink"><a href="https://stats.wikimedia.org/#/en.wikipedia.org">Statistics</a></li> <li id="footer-places-cookiestatement"><a href="https://foundation.wikimedia.org/wiki/Special:MyLanguage/Policy:Cookie_statement">Cookie statement</a></li> <li id="footer-places-mobileview"><a href="//en.m.wikipedia.org/w/index.php?title=Histone_acetyltransferase&mobileaction=toggle_view_mobile" class="noprint stopMobileRedirectToggle">Mobile view</a></li> </ul> <ul id="footer-icons" class="noprint"> <li id="footer-copyrightico"><a href="https://wikimediafoundation.org/" class="cdx-button cdx-button--fake-button cdx-button--size-large cdx-button--fake-button--enabled"><img src="/static/images/footer/wikimedia-button.svg" width="84" height="29" alt="Wikimedia Foundation" loading="lazy"></a></li> <li id="footer-poweredbyico"><a href="https://www.mediawiki.org/" class="cdx-button cdx-button--fake-button cdx-button--size-large cdx-button--fake-button--enabled"><img src="/w/resources/assets/poweredby_mediawiki.svg" alt="Powered by MediaWiki" width="88" height="31" loading="lazy"></a></li> </ul> </footer> </div> </div> </div> <div class="vector-settings" id="p-dock-bottom"> <ul></ul> </div><script>(RLQ=window.RLQ||[]).push(function(){mw.config.set({"wgHostname":"mw-web.codfw.main-f69cdc8f6-49vgg","wgBackendResponseTime":198,"wgPageParseReport":{"limitreport":{"cputime":"0.743","walltime":"0.899","ppvisitednodes":{"value":3825,"limit":1000000},"postexpandincludesize":{"value":164404,"limit":2097152},"templateargumentsize":{"value":2486,"limit":2097152},"expansiondepth":{"value":12,"limit":100},"expensivefunctioncount":{"value":4,"limit":500},"unstrip-depth":{"value":1,"limit":20},"unstrip-size":{"value":203936,"limit":5000000},"entityaccesscount":{"value":0,"limit":400},"timingprofile":["100.00% 730.927 1 -total"," 43.52% 318.119 1 Template:Reflist"," 32.99% 241.144 32 Template:Cite_journal"," 12.30% 89.931 1 Template:Short_description"," 11.95% 87.350 5 Template:Navbox"," 10.79% 78.857 1 Template:Transcription"," 8.52% 62.289 2 Template:Infobox"," 6.28% 45.934 1 Template:Citation_needed"," 6.28% 45.869 1 Template:Infobox_enzyme"," 6.05% 44.239 5 Template:Main_other"]},"scribunto":{"limitreport-timeusage":{"value":"0.422","limit":"10.000"},"limitreport-memusage":{"value":6189170,"limit":52428800}},"cachereport":{"origin":"mw-web.codfw.main-f69cdc8f6-lwkv4","timestamp":"20241122142623","ttl":2592000,"transientcontent":false}}});});</script> <script type="application/ld+json">{"@context":"https:\/\/schema.org","@type":"Article","name":"Histone acetyltransferase","url":"https:\/\/en.wikipedia.org\/wiki\/Histone_acetyltransferase","sameAs":"http:\/\/www.wikidata.org\/entity\/Q1036906","mainEntity":"http:\/\/www.wikidata.org\/entity\/Q1036906","author":{"@type":"Organization","name":"Contributors to Wikimedia projects"},"publisher":{"@type":"Organization","name":"Wikimedia Foundation, Inc.","logo":{"@type":"ImageObject","url":"https:\/\/www.wikimedia.org\/static\/images\/wmf-hor-googpub.png"}},"datePublished":"2004-03-26T03:24:21Z","dateModified":"2024-08-26T04:41:33Z","image":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/f\/fb\/5trm.jpg","headline":"enzymes that catalyze acyl group transfer from acetyl-CoA to histones"}</script> </body> </html>