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SIN3A
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<h2 id="function">Function</h2> <p>The <a href="/facts/Protein/Jxmagu3E">protein</a> encoded by this gene is a <a href="/facts/Transcription_(genetics)/bDgp9HDN">transcriptional</a> regulatory protein. It contains paired <a href="/facts/Amphipathic/FkmYh9JI">amphipathic</a> helix (PAH) domains, which are important for protein-protein interactions and may mediate repression by the Mad-Max complex.<a class="footnote-ref" id="fnref:3" href="#fn:3"><sup>3</sup></a> </p> <h2 id="interactions">Interactions</h2> <p>SIN3A has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with: </p> <ul><li><a href="/facts/CABIN1/pFtk1c5l">CABIN1</a><a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a></li> <li><a href="/facts/HBP1/KVd6vjj0">HBP1</a>,<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a></li> <li><a href="/facts/HDAC1/6Ah3cBy1">HDAC1</a>,<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a><a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a><a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a><a class="footnote-ref" id="fnref:9" href="#fn:9"><sup>9</sup></a><a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a><a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a><a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a><a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a><a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a><a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a><a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a><a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a><a class="footnote-ref" id="fnref:18" href="#fn:18"><sup>18</sup></a><a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a></li> <li><a href="/facts/HDAC9/2TECeSsP">HDAC9</a>,<a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a><a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a></li> <li><a href="/facts/Histone_deacetylase_2/FRWRaCRL">Histone deacetylase 2</a>,<a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a><a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a><a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a><a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a><a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a><a class="footnote-ref" id="fnref:27" href="#fn:27"><sup>27</sup></a><a class="footnote-ref" id="fnref:28" href="#fn:28"><sup>28</sup></a></li> <li><a href="/facts/Host_cell_factor_C1/0zXTA8FB">Host cell factor C1</a>,<a class="footnote-ref" id="fnref:29" href="#fn:29"><sup>29</sup></a><a class="footnote-ref" id="fnref:30" href="#fn:30"><sup>30</sup></a></li> <li><a href="/facts/IKZF1/23yhRe9M">IKZF1</a>,<a class="footnote-ref" id="fnref:31" href="#fn:31"><sup>31</sup></a><a class="footnote-ref" id="fnref:32" href="#fn:32"><sup>32</sup></a><a class="footnote-ref" id="fnref:33" href="#fn:33"><sup>33</sup></a></li> <li><a href="/facts/ING1/DJ9fFRXd">ING1</a>,<a class="footnote-ref" id="fnref:34" href="#fn:34"><sup>34</sup></a></li> <li><a href="/facts/KLF11/HBGvSARR">KLF11</a>,<a class="footnote-ref" id="fnref:35" href="#fn:35"><sup>35</sup></a><a class="footnote-ref" id="fnref:36" href="#fn:36"><sup>36</sup></a></li> <li><a href="/facts/MNT_(gene)/qAGGYEoY">MNT</a>,<a class="footnote-ref" id="fnref:37" href="#fn:37"><sup>37</sup></a></li> <li><a href="/facts/MXD1/lL9udPCF">MXD1</a>,<a class="footnote-ref" id="fnref:38" href="#fn:38"><sup>38</sup></a><a class="footnote-ref" id="fnref:39" href="#fn:39"><sup>39</sup></a><a class="footnote-ref" id="fnref:40" href="#fn:40"><sup>40</sup></a></li> <li><a href="/facts/Methyl-CpG-binding_domain_protein_2/aqRrV8IQ">Methyl-CpG-binding domain protein 2</a>,<a class="footnote-ref" id="fnref:41" href="#fn:41"><sup>41</sup></a></li> <li><a href="/facts/Nuclear_receptor_co-repressor_2/hyspxexv">Nuclear receptor co-repressor 2</a>,<a class="footnote-ref" id="fnref:42" href="#fn:42"><sup>42</sup></a><a class="footnote-ref" id="fnref:43" href="#fn:43"><sup>43</sup></a></li> <li><a href="/facts/OGT_(gene)/tgNe1KLR">OGT</a>,<a class="footnote-ref" id="fnref:44" href="#fn:44"><sup>44</sup></a></li> <li><a href="/facts/PHF12/gkNmy9pT">PHF12</a>,<a class="footnote-ref" id="fnref:45" href="#fn:45"><sup>45</sup></a></li> <li><a href="/facts/Promyelocytic_leukemia_protein/QdCl05AJ">Promyelocytic leukemia protein</a>,<a class="footnote-ref" id="fnref:46" href="#fn:46"><sup>46</sup></a></li> <li><a href="/facts/RBBP4/FVBhhPGM">RBBP4</a>,<a class="footnote-ref" id="fnref:47" href="#fn:47"><sup>47</sup></a><a class="footnote-ref" id="fnref:48" href="#fn:48"><sup>48</sup></a></li> <li><a href="/facts/RBBP7/Vn7ubLJo">RBBP7</a>,<a class="footnote-ref" id="fnref:49" href="#fn:49"><sup>49</sup></a><a class="footnote-ref" id="fnref:50" href="#fn:50"><sup>50</sup></a></li> <li><a href="/facts/SAP130/0G3RC29j">SAP130</a>,<a class="footnote-ref" id="fnref:51" href="#fn:51"><sup>51</sup></a></li> <li><a href="/facts/SAP30/9Y758sYv">SAP30</a>,<a class="footnote-ref" id="fnref:52" href="#fn:52"><sup>52</sup></a><a class="footnote-ref" id="fnref:53" href="#fn:53"><sup>53</sup></a><a class="footnote-ref" id="fnref:54" href="#fn:54"><sup>54</sup></a><a class="footnote-ref" id="fnref:55" href="#fn:55"><sup>55</sup></a><a class="footnote-ref" id="fnref:56" href="#fn:56"><sup>56</sup></a><a class="footnote-ref" id="fnref:57" href="#fn:57"><sup>57</sup></a></li> <li><a href="/facts/SMARCA2/zS0H4fJs">SMARCA2</a>,<a class="footnote-ref" id="fnref:58" href="#fn:58"><sup>58</sup></a></li> <li><a href="/facts/SMARCA4/tTMYE8oQ">SMARCA4</a>,<a class="footnote-ref" id="fnref:59" href="#fn:59"><sup>59</sup></a><a class="footnote-ref" id="fnref:60" href="#fn:60"><sup>60</sup></a></li> <li><a href="/facts/SMARCC1/wdr1Bcy8">SMARCC1</a>,<a class="footnote-ref" id="fnref:61" href="#fn:61"><sup>61</sup></a><a class="footnote-ref" id="fnref:62" href="#fn:62"><sup>62</sup></a></li> <li><a href="/facts/SUDS3/pusLGA5w">SUDS3</a>,<a class="footnote-ref" id="fnref:63" href="#fn:63"><sup>63</sup></a><a class="footnote-ref" id="fnref:64" href="#fn:64"><sup>64</sup></a></li> <li><a href="/facts/TAL1/jmvG7Enh">TAL1</a>,<a class="footnote-ref" id="fnref:65" href="#fn:65"><sup>65</sup></a> and</li> <li><a href="/facts/Zinc_finger_and_BTB_domain-containing_protein_16/8ScfHtFk">Zinc finger and BTB domain-containing protein 16</a>.<a class="footnote-ref" id="fnref:66" href="#fn:66"><sup>66</sup></a><a class="footnote-ref" id="fnref:67" href="#fn:67"><sup>67</sup></a><a class="footnote-ref" id="fnref:68" href="#fn:68"><sup>68</sup></a></li></ul> <h2 id="see-also">See also</h2> <ul><li><a href="/facts/Transcription_coregulator/Fo5fXd6e">Transcription coregulator</a></li></ul> <h2 id="further-reading">Further reading</h2> <ul><li>Zhang Y, Dufau ML (June 2003). <a href="https://zenodo.org/record/1260176">"Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes"</a>. <i>The Journal of Steroid Biochemistry and Molecular Biology</i>. 85 (2–5): 401–14. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0960-0760%2803%2900230-9">10.1016/S0960-0760(03)00230-9</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12943729">12943729</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:28512341">28512341</a>.</li> <li>Ayer DE, Lawrence QA, Eisenman RN (March 1995). <a href="https://doi.org/10.1016%2F0092-8674%2895%2990355-0">"Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3"</a>. <i>Cell</i>. 80 (5): 767–76. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0092-8674%2895%2990355-0">10.1016/0092-8674(95)90355-0</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7889570">7889570</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:8749951">8749951</a>.</li> <li>Hurlin PJ, Quéva C, Koskinen PJ, Steingrímsson E, Ayer DE, Copeland NG, Jenkins NA, Eisenman RN (November 1995). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC394680">"Mad3 and Mad4: novel Max-interacting transcriptional repressors that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation"</a>. <i>The EMBO Journal</i>. 14 (22): 5646–59. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fj.1460-2075.1995.tb00252.x">10.1002/j.1460-2075.1995.tb00252.x</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC394680">394680</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8521822">8521822</a>.</li> <li>Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE (May 1997). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2980214-7">"Histone deacetylase activity is required for full transcriptional repression by mSin3A"</a>. <i>Cell</i>. 89 (3): 341–7. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2980214-7">10.1016/S0092-8674(00)80214-7</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9150133">9150133</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:14233219">14233219</a>.</li> <li>Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN (May 1997). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2980215-9">"Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression"</a>. <i>Cell</i>. 89 (3): 349–56. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2980215-9">10.1016/S0092-8674(00)80215-9</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9150134">9150134</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:13490886">13490886</a>.</li> <li>Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D (May 1997). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2980216-0">"Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex"</a>. <i>Cell</i>. 89 (3): 357–64. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2980216-0">10.1016/S0092-8674(00)80216-0</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9150135">9150135</a>.</li> <li>Meroni G, Reymond A, Alcalay M, Borsani G, Tanigami A, Tonlorenzi R, Lo Nigro C, Messali S, Zollo M, Ledbetter DH, Brent R, Ballabio A, Carrozzo R (May 1997). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1169897">"Rox, a novel bHLHZip protein expressed in quiescent cells that heterodimerizes with Max, binds a non-canonical E box and acts as a transcriptional repressor"</a>. <i>The EMBO Journal</i>. 16 (10): 2892–906. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Femboj%2F16.10.2892">10.1093/emboj/16.10.2892</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1169897">1169897</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9184233">9184233</a>.</li> <li>Lin RJ, Nagy L, Inoue S, Shao W, Miller WH, Evans RM (February 1998). <a href="https://doi.org/10.1038%2F35895">"Role of the histone deacetylase complex in acute promyelocytic leukaemia"</a>. <i>Nature</i>. 391 (6669): 811–4. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1998Natur.391..811L">1998Natur.391..811L</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F35895">10.1038/35895</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9486654">9486654</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:4383951">4383951</a>.</li> <li>David G, Alland L, Hong SH, Wong CW, DePinho RA, Dejean A (May 1998). "Histone deacetylase associated with mSin3A mediates repression by the acute promyelocytic leukemia-associated PLZF protein". <i>Oncogene</i>. 16 (19): 2549–56. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2Fsj.onc.1202043">10.1038/sj.onc.1202043</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9627120">9627120</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:655636">655636</a>.</li> <li>Wong CW, Privalsky ML (October 1998). <a href="https://doi.org/10.1074%2Fjbc.273.42.27695">"Components of the SMRT corepressor complex exhibit distinctive interactions with the POZ domain oncoproteins PLZF, PLZF-RARalpha, and BCL-6"</a>. <i>The Journal of Biological Chemistry</i>. 273 (42): 27695–702. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.273.42.27695">10.1074/jbc.273.42.27695</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9765306">9765306</a>.</li> <li>Zhang Y, LeRoy G, Seelig HP, Lane WS, Reinberg D (October 1998). <a href="https://doi.org/10.1016%2FS0092-8674%2800%2981758-4">"The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities"</a>. <i>Cell</i>. 95 (2): 279–89. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2800%2981758-4">10.1016/S0092-8674(00)81758-4</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9790534">9790534</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:18786866">18786866</a>.</li> <li>Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL (October 1998). "Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex". <i>Nature</i>. 395 (6705): 917–21. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1998Natur.395..917T">1998Natur.395..917T</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F27699">10.1038/27699</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9804427">9804427</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:4355885">4355885</a>.</li> <li>Koipally J, Renold A, Kim J, Georgopoulos K (June 1999). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171390">"Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes"</a>. <i>The EMBO Journal</i>. 18 (11): 3090–100. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Femboj%2F18.11.3090">10.1093/emboj/18.11.3090</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171390">1171390</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10357820">10357820</a>.</li> <li>Boutell JM, Thomas P, Neal JW, Weston VJ, Duce J, Harper PS, Jones AL (September 1999). <a href="https://doi.org/10.1093%2Fhmg%2F8.9.1647">"Aberrant interactions of transcriptional repressor proteins with the Huntington's disease gene product, huntingtin"</a>. <i>Human Molecular Genetics</i>. 8 (9): 1647–55. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Fhmg%2F8.9.1647">10.1093/hmg/8.9.1647</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10441327">10441327</a>.</li> <li>Zhang Y, Ng HH, Erdjument-Bromage H, Tempst P, Bird A, Reinberg D (August 1999). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC316920">"Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation"</a>. <i>Genes & Development</i>. 13 (15): 1924–35. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1101%2Fgad.13.15.1924">10.1101/gad.13.15.1924</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC316920">316920</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10444591">10444591</a>.</li> <li>Kao HY, Downes M, Ordentlich P, Evans RM (January 2000). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC316336">"Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression"</a>. <i>Genes & Development</i>. 14 (1): 55–66. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1101%2Fgad.14.1.55">10.1101/gad.14.1.55</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC316336">316336</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10640276">10640276</a>.</li> <li>Huang S, Brandt SJ (March 2000). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110841">"mSin3A regulates murine erythroleukemia cell differentiation through association with the TAL1 (or SCL) transcription factor"</a>. <i>Molecular and Cellular Biology</i>. 20 (6): 2248–59. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1128%2FMCB.20.6.2248-2259.2000">10.1128/MCB.20.6.2248-2259.2000</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC110841">110841</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10688671">10688671</a>.</li> <li>Koipally J, Georgopoulos K (June 2000). <a href="https://doi.org/10.1074%2Fjbc.M000254200">"Ikaros interactions with CtBP reveal a repression mechanism that is independent of histone deacetylase activity"</a>. <i>The Journal of Biological Chemistry</i>. 275 (26): 19594–602. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M000254200">10.1074/jbc.M000254200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10766745">10766745</a>.</li></ul> <h2 id="external-links">External links</h2> <ul><li><a href="https://meshb.nlm.nih.gov/record/ui?name=SIN3A+protein%2C+human">SIN3A+protein,+human</a> at the U.S. National Library of Medicine <a href="/facts/Medical_Subject_Headings/C57g2JuF">Medical Subject Headings</a> (MeSH)</li> <li><a href="/facts/ENCODE/X7hhKpsg">FactorBook</a> <a href="http://www.factorbook.org/mediawiki/index.php/Sin3Ak-20">Sin3Ak-20</a></li></ul> <p> <i>This article incorporates text from the <a href="/facts/United_States_National_Library_of_Medicine/Hzty0MCX">United States National Library of Medicine</a>, which is in the <a href="/facts/Public_domain/YWKMDKw4">public domain</a>.</i> </p> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Yu F, Thiesen J, Strätling WH (May 2000). 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