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<body class="skin--responsive skin-vector skin-vector-search-vue mediawiki ltr sitedir-ltr mw-hide-empty-elt ns-0 ns-subject page-Histon_H3 rootpage-Histon_H3 skin-vector-2022 action-view">
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<h1 id="firstHeading" class="firstHeading mw-first-heading"><span class="mw-page-title-main">Histon H3</span></h1>
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<div id="mw-content-text" class="mw-body-content mw-content-ltr" lang="de" dir="ltr"><div class="mw-content-ltr mw-parser-output" lang="de" dir="ltr"><table class="wikitable hintergrundfarbe-basis infobox float-right" id="Vorlage_Infobox_Protein_H3_histone,_family_3A" style="font-size:90%; margin-top:0; width:350px;" summary="Infobox Protein">
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<th colspan="3" style="background:#90EE90; color:#202122;">H3 histone, family 3A
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<th colspan="3" style="background:#90EE90; color:#202122;;">Eigenschaften des menschlichen Proteins
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<th colspan="3" style="background:#90EE90; color:#202122;">Bezeichner
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<td><a href="Human_Genome_Organisation" title="Human Genome Organisation">Gen-Namen</a>
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<td colspan="2" class="" style="text-align:center;"><i><a rel="nofollow" class="external text" href="https://www.genenames.org/tools/search/#!/all?query=4764">H3F3A</a></i>, H3F3
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<td>Externe IDs
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<ul><li><a href="Online_Mendelian_Inheritance_in_Man" title="Online Mendelian Inheritance in Man">OMIM</a>: <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/omim/601128">601128</a></li>
<li><a href="UniProt" title="UniProt">UniProt</a> <a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprotkb/Q66I33">Q66I33</a></li></ul>
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</p><table class="wikitable hintergrundfarbe-basis infobox float-right" id="Vorlage_Infobox_Protein_H3_histone,_family_3B_(H3.3B)" style="font-size:90%; margin-top:0; width:350px;" summary="Infobox Protein">
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<th colspan="3" style="background:#90EE90; color:#202122;">H3 histone, family 3B (H3.3B)
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<th colspan="3" style="background:#90EE90; color:#202122;;">Eigenschaften des menschlichen Proteins
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<th colspan="3" style="background:#90EE90; color:#202122;">Bezeichner
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<td><a href="Human_Genome_Organisation" title="Human Genome Organisation">Gen-Name</a>
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<td colspan="2" class="" style="text-align:center;"><i><a rel="nofollow" class="external text" href="https://www.genenames.org/tools/search/#!/all?query=4765">H3F3B</a></i>
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<td>Externe IDs
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<td colspan="2" class="">
<ul><li><a href="Online_Mendelian_Inheritance_in_Man" title="Online Mendelian Inheritance in Man">OMIM</a>: <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/omim/601058">601058</a></li>
<li><a href="UniProt" title="UniProt">UniProt</a> <a rel="nofollow" class="external text" href="https://www.uniprot.org/uniprotkb/P84243">P84243</a></li></ul>
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<th colspan="3" style="background:#90EE90; color:#202122;">Vorkommen
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<td style="background:#C3FDB8; color:#202122;">Homologie-Familie
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<td colspan="2" style="text-align:center;"><a rel="nofollow" class="external text" href="http://hogenom.univ-lyon1.fr/query_sequence?seq=P84243">Hovergen</a>
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</p><p><b>Histon H3</b> ist eines der fünf Haupt-<a href="Histon" title="Histon">Histon</a>-<a href="Protein" title="Protein">Proteine</a> des <a href="Chromatin" title="Chromatin">Chromatins</a> in <a href="Eukaryoten" title="Eukaryoten">eukaryotischen Zellen</a>. Bestehend aus einer globulären Hauptdomäne und einem langen N-terminalen Ende, spielt es eine Rolle in der Struktur der <a href="Nukleosom" title="Nukleosom">Nukleosomen</a> und somit der „Perlenschnur“-Struktur der Chromatinfäden.
</p><p>Das <a href="N-terminal" class="mw-redirect" title="N-terminal">N-terminale</a> Ende des Histons H3 ragt aus dem kugeligen Kern des Nukleosomes heraus und kann durch verschiedene <a href="Epigenetik" title="Epigenetik">epigenetische</a> Modifikationen verändert werden. Diese <a href="Histonmodifikation" title="Histonmodifikation">Histonmodifikationen</a> sind kovalente Anhänge von Methyl- oder Acetylgruppen an die Aminosäuren <a href="Lysin" title="Lysin">Lysin</a> und <a href="Arginin" title="Arginin">Arginin</a> und die Phosphorylierung von <a href="Serin" title="Serin">Serin</a> oder <a href="Threonin" title="Threonin">Threonin</a>. Die Methylierung von Lysin 9 wird mit der Stilllegung von Genen assoziiert (siehe <a href="Heterochromatin_Protein_1" class="mw-redirect" title="Heterochromatin Protein 1">HP1</a>), dem sog. „<a href="Gen-Silencing" title="Gen-Silencing">Gen-Silencing</a>“ und der Bildung von relativ inaktiven DNA-Regionen, dem sogenannten <a href="Heterochromatin" title="Heterochromatin">Heterochromatin</a>. Die Acetylierung von Histon H3 findet unter dem Einfluss der <a href="Enzym" title="Enzym">Enzymfamilie</a> der Histon-Acetyltransferasen (HAT) an verschiedenen Lysin-Positionen am Histonende statt. Die Acetylierung von Lysin 14 findet häufig in aktiv <a href="Transkription_(Biologie)" title="Transkription (Biologie)">transkribierten</a> Genregionen statt.
</p><p>Mutationen in der Histon H3-Proteinfamilie finden sich typischerweise in den seltenen <a href="Riesenzelltumor" title="Riesenzelltumor">Riesenzelltumoren</a> des Bindegewebes und des Knochens.<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>
</p>
<div class="mw-heading mw-heading2"><h2 id="Andere_Histon-Proteine">Andere Histon-Proteine</h2></div>
<ul><li><a href="Histon_H1" title="Histon H1">H1</a></li>
<li><a href="Histon_H2A" title="Histon H2A">H2A</a></li>
<li><a href="Histon_H2B" class="mw-redirect" title="Histon H2B">H2B</a></li>
<li><a href="Histon_H4" title="Histon H4">H4</a></li></ul>
<div class="mw-heading mw-heading2"><h2 id="Literatur">Literatur</h2></div>
<ul><li>Wells D, Brown D: <cite style="font-style:italic">Histone and histone gene compilation and alignment update</cite>. In: <cite style="font-style:italic"><a href="Nucleic_Acids_Research" title="Nucleic Acids Research">Nucleic Acids Research</a>.</cite> 19 Suppl. Jahrgang, April 1991, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>2173–88</span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/2041803?dopt=Abstract">PMID 2041803</a>, <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC331351/">PMC 331351</a> (freier Volltext).<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Abook&rfr_id=info:sid/de.wikipedia.org:Histon+H3&rft.atitle=Histone+and+histone+gene+compilation+and+alignment+update&rft.au=Wells+D%2C+Brown+D&rft.btitle=Nucleic+Acids+Research.&rft.date=1991-04&rft.genre=book&rft.pages=2173-88&rft.pmc=331351&rft.pmid=2041803&rft.volume=19+Suppl.+Jahrgang" style="display:none"> </span></li>
<li>Thatcher TH, Gorovsky MA: <cite style="font-style:italic">Phylogenetic analysis of the core histones H2A, H2B, H3, and H4</cite>. In: <cite style="font-style:italic">Nucleic Acids Res.</cite> 22. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>2</span>, Januar 1994, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>174–9</span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/8121801?dopt=Abstract">PMID 8121801</a>, <a rel="nofollow" class="external text" href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC307768/">PMC 307768</a> (freier Volltext).<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Histon+H3&rft.atitle=Phylogenetic+analysis+of+the+core+histones+H2A%2C+H2B%2C+H3%2C+and+H4&rft.au=Thatcher+TH%2C+Gorovsky+MA&rft.date=1994-01&rft.genre=journal&rft.issue=2&rft.jtitle=Nucleic+Acids+Res.&rft.pages=174-9&rft.pmc=307768&rft.pmid=8121801&rft.volume=22.+Jahrgang" style="display:none"> </span></li>
<li>Lachner M, O’Carroll D, Rea S, Mechtler K, Jenuwein T: <cite style="font-style:italic">Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins</cite>. In: <cite style="font-style:italic"><a href="Nature" title="Nature">Nature</a></cite>. 410. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>6824</span>, März 2001, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>116–20</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1038/35065132">10.1038/35065132</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/11242053?dopt=Abstract">PMID 11242053</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Histon+H3&rft.atitle=Methylation+of+histone+H3+lysine+9+creates+a+binding+site+for+HP1+proteins&rft.au=Lachner+M%2C+O%E2%80%99Carroll+D%2C+Rea+S%2C+...&rft.date=2001-03&rft.doi=10.1038%2F35065132&rft.genre=journal&rft.issue=6824&rft.jtitle=Nature&rft.pages=116-20&rft.pmid=11242053&rft.volume=410.+Jahrgang" style="display:none"> </span></li>
<li>Hake SB, Garcia BA, Duncan EM, <i>et al.</i>: <cite style="font-style:italic">Expression patterns and post-translational modifications associated with mammalian histone H3 variants</cite>. In: <cite style="font-style:italic"><a href="J._Biol._Chem." class="mw-redirect" title="J. Biol. Chem.">J. Biol. Chem.</a></cite> 281. Jahrgang, <span style="white-space:nowrap">Nr.<span style="display:inline-block;width:.2em"> </span>1</span>, Januar 2006, <span style="white-space:nowrap">S.<span style="display:inline-block;width:.2em"> </span>559–68</span>, <a href="Digital_Object_Identifier" title="Digital Object Identifier">doi</a>:<span class="uri-handle" style="white-space:nowrap"><a rel="nofollow" class="external text" href="https://doi.org/10.1074/jbc.M509266200">10.1074/jbc.M509266200</a></span>, <a class="external mw-magiclink-pmid" rel="nofollow" href="https://www.ncbi.nlm.nih.gov/pubmed/16267050?dopt=Abstract">PMID 16267050</a>.<span class="Z3988" title="ctx_ver=Z39.88-2004&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rfr_id=info:sid/de.wikipedia.org:Histon+H3&rft.atitle=Expression+patterns+and+post-translational+modifications+associated+with+mammalian+histone+H3+variants&rft.au=Hake+SB%2C+Garcia+BA%2C+Duncan+EM%2C+...&rft.date=2006-01&rft.doi=10.1074%2Fjbc.M509266200&rft.genre=journal&rft.issue=1&rft.jtitle=J.+Biol.+Chem.&rft.pages=559-68&rft.pmid=16267050&rft.volume=281.+Jahrgang" style="display:none"> </span></li></ul>
<div class="mw-heading mw-heading2"><h2 id="Einzelnachweise">Einzelnachweise</h2></div>
<ol class="references">
<li id="cite_note-1"><span class="mw-cite-backlink"><a href="#cite_ref-1">↑</a></span> <span class="reference-text">Edwin Choy, Francis J. Hornicek, Yen-Lin Chen, Daniel I. Rosenthal, Darcy A. Kerr: <i>Case 26-2016: A 28-year-old woman with back pain and a lesion in the lumbar spine</i> <a href="New_England_Journal_of_Medicine" class="mw-redirect" title="New England Journal of Medicine">New England Journal of Medicine</a> 2016, Band 375, Ausgabe 8 vom 25. August 2016, Seiten 779–788, <a href="https://doi.org/10.1056/NEJMcpc1505482" class="extiw external" title="doi:10.1056/NEJMcpc1505482">DOI:10.1056/NEJMcpc1505482</a></span>
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