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PSMC5
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<h2 id="gene">Gene</h2> <p>The gene <i>PSMC5</i> encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. In addition to participation in proteasome functions, this subunit may participate in transcriptional regulation since it has been shown to interact with the thyroid hormone receptor and retinoid X receptor-alpha.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> The human <i>PSMC5</i> gene has 13 exons and locates at chromosome band 17q23.3. </p> <h2 id="protein">Protein</h2> <p>The human protein 26S protease regulatory subunit 8 is 45.6kDa in size and composed of 406 amino acids. The calculated theoretical pI of this protein is 8.23.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> </p> <h2 id="complex-assembly">Complex assembly</h2> <p>26S <a href="/facts/Proteasome/8vTtg2MI">proteasome</a> complex is usually consisted of a 20S core particle (CP, or 20S proteasome) and one or two 19S regulatory particles (RP, or 19S proteasome) on either one side or both side of the barrel-shaped 20S. The CP and RPs pertain distinct structural characteristics and biological functions. In brief, 20S sub complex presents three types proteolytic activities, including caspase-like, trypsin-like, and chymotrypsin-like activities. These proteolytic active sites located in the inner side of a chamber formed by 4 stacked rings of 20S subunits, preventing random protein-enzyme encounter and uncontrolled protein degradation. The 19S regulatory particles can recognize <a href="/facts/Ubiquitin/hpulmU3m">ubiquitin</a>-labeled protein as degradation substrate, unfold the protein to linear, open the gate of 20S core particle, and guide the substrate into the proteolytic chamber. To meet such functional complexity, 19S regulatory particle contains at least 18 constitutive subunits. These subunits can be categorized into two classes based on the ATP dependence of subunits, ATP-dependent subunits and ATP-independent subunits. According to the protein interaction and topological characteristics of this multisubunit complex, the 19S regulatory particle is composed of a base and a lid subcomplex. The base consists of a ring of six AAA ATPases (Subunit Rpt1-6, systematic nomenclature) and four non-ATPase subunits (<a href="/facts/PSMD2/fqt7H0yA">Rpn1</a>, <a href="/facts/PSMD1/0WTnUCq0">Rpn2</a>, <a href="/facts/PSMD4/SuDo5LGH">Rpn10</a>, and Rpn13). Thus, 26S protease regulatory subunit 4 (Rpt2) is an essential component of forming the base subcomplex of 19S regulatory particle. For the assembly of 19S base sub complex, four sets of pivotal assembly chaperons (Hsm3/S5b, Nas2/P27, Nas6/P28, and Rpn14/PAAF1, nomenclature in yeast/mammals) were identified by four groups independently.<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> These 19S regulatory particle base-dedicated chaperons all binds to individual ATPase subunits through the C-terminal regions. For example, Hsm3/S5b binds to the subunit <a href="/facts/PSMC2/RG40mLFe">Rpt1</a> and Rpt2 (this protein), Nas2/p27 to <a href="/facts/PSMC3/8RuCT3wb">Rpt5</a>, Nas6/p28 to <a href="/facts/PSMC4/aJWY1rKq">Rpt3</a>, and Rpn14/PAAAF1 to Rpt6 (this protein), respectively. Subsequently, three intermediate assembly modules are formed as following, the Nas6/p28-Rpt3-Rpt6-Rpn14/PAAF1 module, the Nas2/p27-Rpt4-Rpt5 module, and the Hsm3/S5b-Rpt1-Rpt2-Rpn2 module. Eventually, these three modules assemble together to form the heterohexameric ring of 6 Atlases with Rpn1. The final addition of <a href="/facts/ADRM1/s53qLepV">Rpn13</a> indicates the completion of 19S base sub complex assembly.<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a> </p> <h2 id="function">Function</h2> <p>As the degradation machinery that is responsible for ~70% of intracellular proteolysis,<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> proteasome complex (26S proteasome) plays a critical roles in maintaining the homeostasis of cellular proteome. Accordingly, misfolded proteins and damaged protein need to be continuously removed to recycle amino acids for new synthesis; in parallel, some key regulatory proteins fulfill their biological functions via selective degradation; furthermore, proteins are digested into peptides for MHC class I antigen presentation. To meet such complicated demands in biological process via spatial and temporal proteolysis, protein substrates have to be recognized, recruited, and eventually hydrolyzed in a well controlled fashion. Thus, 19S regulatory particle pertains a series of important capabilities to address these functional challenges. To recognize protein as designated substrate, 19S complex has subunits that are capable to recognize proteins with a special degradative tag, the ubiquitinylation. It also have subunits that can bind with nucleotides (e.g., ATPs) in order to facilitate the association between 19S and 20S particles, as well as to cause confirmation changes of alpha subunit C-terminals that form the substrate entrance of 20S complex. </p><p>The ATPases subunits assemble into a six-membered ring with a sequence of Rpt1–Rpt5–Rpt4–Rpt3–Rpt6–Rpt2, which interacts with the seven-membered alpha ring of 20S core particle and establishes an asymmetric interface between the 19S RP and the 20S CP.<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> Three C-terminal tails with HbYX motifs of distinct Rpt ATPases insert into pockets between two defined alpha subunits of the CP and regulate the gate opening of the central channels in the CP alpha ring.<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> Evidence showed that ATPase subunit Rpt5, along with other ubuiqintinated 19S proteasome subunits (<a href="/facts/ADRM1/s53qLepV">Rpn13</a>, <a href="/facts/PSMD4/SuDo5LGH">Rpn10</a>) and the deubiquitinating enzyme Uch37, can be ubiquitinated in situ by proteasome-associating ubiquitination enzymes. Ubiquitination of proteasome subunits can regulates proteasomal activity in response to the alteration of cellular ubiquitination levels.<a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a> </p> <h2 id="interactions">Interactions</h2> <p>PSMC5 has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with: </p> <ul><li><a href="/facts/PSMC3/8RuCT3wb">PSMC3</a>,<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a></li> <li><a href="/facts/PSMC4/aJWY1rKq">PSMC4</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></li> <li><a href="/facts/Sp1_transcription_factor/Tz4tCgbE">Sp1 transcription factor</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> and</li> <li><a href="/facts/XPB/1FaD6HIh">XPB</a>.<a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a></li></ul> <h2 id="children-with-psmc5-mutations">Children with PSMC5 Mutations</h2> <p>As of 2021, only 18 reports of children with PSMC5 mutations have been discovered. <GeneMatcher> There is one foundation that is performing research with children who has PSMC5 mutations called PSMC5 Foundation, <a href="http://www.psmc5.org">www.psmc5.org</a>. The aim is to find therapies and learn more about how to resolve issues with mutations. The common effects have been developmental delays, ranging from motor delays to minimal expressive language. </p> <h2 id="further-reading">Further reading</h2> <ul><li>Coux O, Tanaka K, Goldberg AL (1996). "Structure and functions of the 20S and 26S proteasomes". <i>Annu. Rev. Biochem</i>. 65 (1): 801–47. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1146%2Fannurev.bi.65.070196.004101">10.1146/annurev.bi.65.070196.004101</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8811196">8811196</a>.</li> <li>Goff SP (2003). <a href="https://doi.org/10.1016%2FS0092-8674%2803%2900602-0">"Death by deamination: a novel host restriction system for HIV-1"</a>. <i>Cell</i>. 114 (3): 281–3. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0092-8674%2803%2900602-0">10.1016/S0092-8674(03)00602-0</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12914693">12914693</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:16340355">16340355</a>.</li> <li>Nelbock P, Dillon PJ, Perkins A, Rosen CA (1990). "A cDNA for a protein that interacts with the human immunodeficiency virus Tat transactivator". <i>Science</i>. 248 (4963): 1650–3. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1990Sci...248.1650N">1990Sci...248.1650N</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1126%2Fscience.2194290">10.1126/science.2194290</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/2194290">2194290</a>.</li> <li>Akiyama K, Yokota K, Kagawa S, Shimbara N, DeMartino GN, Slaughter CA, Noda C, Tanaka K (1995). <a href="https://doi.org/10.1016%2F0014-5793%2895%2900304-R">"cDNA cloning of a new putative ATPase subunit p45 of the human 26S proteasome, a homolog of yeast transcriptional factor Sug1p"</a>. <i>FEBS Lett</i>. 363 (1–2): 151–6. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1995FEBSL.363..151A">1995FEBSL.363..151A</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0014-5793%2895%2900304-R">10.1016/0014-5793(95)00304-R</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7729537">7729537</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:638369">638369</a>.</li> <li>Lee JW, Choi HS, Gyuris J, Brent R, Moore DD (1995). <a href="https://doi.org/10.1210%2Fmend.9.2.7776974">"Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor"</a>. <i>Mol. Endocrinol</i>. 9 (2): 243–54. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1210%2Fmend.9.2.7776974">10.1210/mend.9.2.7776974</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7776974">7776974</a>.</li> <li>Lee JW, Ryan F, Swaffield JC, Johnston SA, Moore DD (1995). "Interaction of thyroid-hormone receptor with a conserved transcriptional mediator". <i>Nature</i>. 374 (6517): 91–4. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1995Natur.374...91L">1995Natur.374...91L</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F374091a0">10.1038/374091a0</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/7870181">7870181</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:4324595">4324595</a>.</li> <li>Shaw DR, Ennis HL (1993). "Molecular cloning and developmental regulation of Dictyostelium discoideum homologues of the human and yeast HIV1 Tat-binding protein". <i>Biochem. Biophys. Res. Commun</i>. 193 (3): 1291–6. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1006%2Fbbrc.1993.1765">10.1006/bbrc.1993.1765</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8323548">8323548</a>.</li> <li>Ohana B, Moore PA, Ruben SM, Southgate CD, Green MR, Rosen CA (1993). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC45615">"The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes"</a>. <i>Proc. Natl. Acad. Sci. U.S.A</i>. 90 (1): 138–42. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1993PNAS...90..138O">1993PNAS...90..138O</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.90.1.138">10.1073/pnas.90.1.138</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC45615">45615</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8419915">8419915</a>.</li> <li>Dubiel W, Ferrell K, Rechsteiner M (1993). "Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26 S protease". <i>FEBS Lett</i>. 323 (3): 276–8. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1993FEBSL.323..276D">1993FEBSL.323..276D</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2F0014-5793%2893%2981356-5">10.1016/0014-5793(93)81356-5</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8500623">8500623</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:26726988">26726988</a>.</li> <li>vom Baur E, Zechel C, Heery D, Heine MJ, Garnier JM, Vivat V, Le Douarin B, Gronemeyer H, Chambon P, Losson R (1996). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC449923">"Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1"</a>. <i>EMBO J</i>. 15 (1): 110–24. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fj.1460-2075.1996.tb00339.x">10.1002/j.1460-2075.1996.tb00339.x</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC449923">449923</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8598193">8598193</a>.</li> <li>Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". <i>Anal. Biochem</i>. 236 (1): 107–13. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1006%2Fabio.1996.0138">10.1006/abio.1996.0138</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8619474">8619474</a>.</li> <li>Wang W, Chevray PM, Nathans D (1996). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC38653">"Mammalian Sug1 and c-Fos in the nuclear 26S proteasome"</a>. <i>Proc. Natl. Acad. Sci. U.S.A</i>. 93 (16): 8236–40. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1996PNAS...93.8236W">1996PNAS...93.8236W</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.93.16.8236">10.1073/pnas.93.16.8236</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC38653">38653</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/8710853">8710853</a>.</li> <li>Seeger M, Ferrell K, Frank R, Dubiel W (1997). <a href="https://doi.org/10.1074%2Fjbc.272.13.8145">"HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation"</a>. <i>J. Biol. Chem</i>. 272 (13): 8145–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.272.13.8145">10.1074/jbc.272.13.8145</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9079628">9079628</a>.</li> <li>Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (1997). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139146">"Large-scale concatenation cDNA sequencing"</a>. <i>Genome Res</i>. 7 (4): 353–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1101%2Fgr.7.4.353">10.1101/gr.7.4.353</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139146">139146</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9110174">9110174</a>.</li> <li>Weeda G, Rossignol M, Fraser RA, Winkler GS, Vermeulen W, van 't Veer LJ, Ma L, Hoeijmakers JH, Egly JM (1997). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC146752">"The XPB subunit of repair/transcription factor TFIIH directly interacts with SUG1, a subunit of the 26S proteasome and putative transcription factor"</a>. <i>Nucleic Acids Res</i>. 25 (12): 2274–83. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Fnar%2F25.12.2274">10.1093/nar/25.12.2274</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC146752">146752</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9173976">9173976</a>.</li> <li>Chen Y, Sharp ZD, Lee WH (1997). <a href="https://doi.org/10.1074%2Fjbc.272.38.24081">"HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins"</a>. <i>J. Biol. Chem</i>. 272 (38): 24081–7. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.272.38.24081">10.1074/jbc.272.38.24081</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9295362">9295362</a>.</li> <li>Tipler CP, Hutchon SP, Hendil K, Tanaka K, Fishel S, Mayer RJ (1998). "Purification and characterization of 26S proteasomes from human and mouse spermatozoa". <i>Mol. Hum. Reprod</i>. 3 (12): 1053–60. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Fmolehr%2F3.12.1053">10.1093/molehr/3.12.1053</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9464850">9464850</a>.</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Tanahashi N, Suzuki M, Fujiwara T, Takahashi E, Shimbara N, Chung CH, Tanaka K (March 1998). "Chromosomal localization and immunological analysis of a family of human 26S proteasomal ATPases". Biochem Biophys Res Commun. 243 (1): 229–32. doi:10.1006/bbrc.1997.7892. PMID 9473509. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Hoyle J, Tan KH, Fisher EM (March 1997). "Localization of genes encoding two human one-domain members of the AAA family: PSMC5 (the thyroid hormone receptor-interacting protein, TRIP1) and PSMC3 (the Tat-binding protein, TBP1)". Hum Genet. 99 (2): 285–8. doi:10.1007/s004390050356. PMID 9048938. 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