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CIB1
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<h2 id="structure-and-function">Structure and function</h2> <p>CIB1 is a small protein with a molecular weight of approximately 22 kDa. It has a conserved calcium-binding <a href="/facts/EF_hand/UVAqabCP">EF hand</a> domain, which consists of two <a href="/facts/Alpha_helix/7CESPIYJ">alpha-helices</a> connected by a loop.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a><a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> CIB1 also has an integrin-binding domain, located near the N-terminus of the protein. In addition, CIB1 has a <a href="/facts/Coiled_coil/U0YEzcB4">coiled-coil</a> domain and a C-terminal domain.<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> CIB1 is involved in regulating <a href="/facts/Cell_adhesion/Vg4alzxb">cell adhesion</a>, <a href="/facts/Cell_migration/5ySAMquQ">migration</a>, and <a href="/facts/Cellular_differentiation/bCVqUG7w">differentiation</a>, as well as other cellular processes. It interacts with <a href="/facts/Integrin/DNYUGbBp">integrins</a>, which are transmembrane receptors that play a key role in cell signaling and adhesion to the extracellular matrix. CIB1 has also been shown to regulate other signaling pathways that are important for cell survival and proliferation.<a class="footnote-ref" id="fnref:10" href="#fn:10"><sup>10</sup></a> Upregulation of CIB1 expression has been observed in several types of <a href="/facts/Cancer/PVW6n1D0">cancer</a>, and it has been implicated in cancer development and progression.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> CIB1 is involved in several cellular processes that are important for cancer progression, including <a href="/facts/Cell_adhesion/Vg4alzxb">cell adhesion</a>, <a href="/facts/Cell_migration/5ySAMquQ">migration</a>, and invasion. It has been shown to interact with integrins, which are <a href="/facts/Cell_surface_receptor/0YGSjDdL">transmembrane receptors</a> that play a key role in these processes.<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> The structure and function of CIB1 make it an important protein in regulating various cellular processes, including those involved in cancer progression, and targeting it may offer potential therapeutic benefits. </p> <h2 id="cancer">Cancer</h2> <p>CIB1 expression has been observed in several types of cancer, including breast, lung, prostate, ovarian, and pancreatic cancer. In breast cancer, CIB1 expression has been shown to be higher in invasive ductal carcinoma compared to normal breast tissue.<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a> High levels of CIB1 expression have also been associated with poor <a href="/facts/Prognosis/3DEGwPag">prognosis</a> in breast cancer patients.<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a> CIB1 has been implicated in cancer development and progression. In breast cancer, CIB1 has been shown to promote <a href="/facts/Cell_proliferation/Jp3hWo2t">cell proliferation</a>, <a href="/facts/Cell_migration/5ySAMquQ">migration</a>, invasion, and <a href="/facts/Metastasis/4dadbm6z">metastasis</a>.<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a> CIB1 has also been shown to promote the growth of <a href="/facts/Prostate_cancer/Mx7XuDhm">prostate cancer</a> cells and the invasion of ovarian cancer cells.<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a> Targeting CIB1 has been explored as a potential therapeutic strategy for cancer. Small molecule inhibitors of CIB1 have shown promise in preclinical models of breast cancer. Silencing CIB1 expression has also been shown to sensitize cancer cells to <a href="/facts/Chemotherapy/fWTLbaUT">chemotherapy</a> and <a href="/facts/Radiation_therapy/j60q5EC6">radiation therapy</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> </p> <h2 id="male-infertility">Male infertility</h2> <p>CIB1 has been implicated in male fertility, specifically in sperm function and motility.<a class="footnote-ref" id="fnref:19" href="#fn:19"><sup>19</sup></a> CIB1 expression has been detected in human sperm, and its levels have been correlated with <a href="/facts/Sperm_motility/PKHcbdjk">sperm motility</a>. CIB1 has also been shown to be present in the acrosome region of the sperm, which plays a critical role in fertilization. Studies in mice have shown that CIB1 deficiency leads to impaired sperm motility and reduced fertility.<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> Male mice lacking CIB1 exhibited decreased sperm count and decreased sperm motility, resulting in reduced fertility. CIB1 was also found to be required for the proper formation of the sperm tail, which is critical for sperm motility.<a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a> In addition, CIB1 has been shown to regulate calcium signaling in sperm, which is important for sperm motility and fertilization. CIB1 interacts with the sperm-specific calcium channel <a href="/facts/CatSper/bsMhsoEd">CatSper</a>, which is important for regulating intracellular calcium levels in sperm.<a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a> </p> <h2 id="spermatogenesis">Spermatogenesis</h2> <p><a href="/facts/Spermatogenesis/8u8XNEV6">Spermatogenesis</a> is the process of producing mature spermatozoa from spermatogonia, the precursor cells in the testes. This process involves several stages, including <a href="/facts/Mitosis/ExxrSUs8">mitotic division</a>, <a href="/facts/Meiosis/Pj5Q6nGN">meiotic division</a>, and <a href="/facts/Differentiation_of_integrals/IWARdb9J">differentiation</a>, which results in the production of four haploid sperm cells from one diploid spermatogonium. CIB1 has been shown to play a critical role in spermatogenesis by regulating the differentiation of spermatogonia into spermatocytes. Studies have shown that CIB1 is expressed in spermatogonia, spermatocytes, and spermatids, indicating its role throughout the entire process of spermatogenesis.<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> In mice, CIB1 deficiency has been shown to lead to decreased spermatogonia proliferation and impaired differentiation into spermatocytes, resulting in reduced sperm production and male infertility.<a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a> In addition, CIB1 has been shown to regulate the expression of genes involved in spermatogenesis, including genes involved in <a href="/facts/Cell_proliferation/Jp3hWo2t">cell proliferation</a> and <a href="/facts/Cellular_differentiation/bCVqUG7w">differentiation</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> </p> <h2 id="interactions">Interactions</h2> <p>CIB1 has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with <a href="/facts/RAC3/bhvQyzN8">RAC3</a>,<a class="footnote-ref" id="fnref:29" href="#fn:29"><sup>29</sup></a> <a href="/facts/PSEN2/quI3TbR8">PSEN2</a>,<a class="footnote-ref" id="fnref:30" href="#fn:30"><sup>30</sup></a> <a href="/facts/DNA-PKcs/L7mc4Mg9">DNA-PKcs</a>,<a class="footnote-ref" id="fnref:31" href="#fn:31"><sup>31</sup></a> <a href="/facts/UBR5/7D16Q86u">UBR5</a><a class="footnote-ref" id="fnref:32" href="#fn:32"><sup>32</sup></a> and <a href="/facts/CD61/BH9jIKn6">CD61</a>.<a class="footnote-ref" id="fnref:33" href="#fn:33"><sup>33</sup></a> </p> <h2 id="further-reading">Further reading</h2> <ul><li>Wu X, Lieber MR (1997). "Interaction between DNA-dependent protein kinase and a novel protein, KIP". <i>Mutat. Res</i>. 385 (1): 13–20. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fs0921-8777%2897%2900035-9">10.1016/s0921-8777(97)00035-9</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9372844">9372844</a>.</li> <li>Seki N, Hayashi A, Abe M, et al. (1999). <a href="https://doi.org/10.1007%2Fs100380050089">"Chromosomal assignment of the gene for human DNA-PKcs interacting protein (KIP) on chromosome 15q25.3-q26.1 by somatic hybrid analysis and fluorescence in situ hybridization"</a>. <i>J. Hum. Genet</i>. 43 (4): 275–7. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1007%2Fs100380050089">10.1007/s100380050089</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9852683">9852683</a>.</li> <li>Stabler SM, Ostrowski LL, Janicki SM, Monteiro MJ (1999). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2133148">"A myristoylated calcium-binding protein that preferentially interacts with the Alzheimer's disease presenilin 2 protein"</a>. <i>J. Cell Biol</i>. 145 (6): 1277–92. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1083%2Fjcb.145.6.1277">10.1083/jcb.145.6.1277</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2133148">2133148</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10366599">10366599</a>.</li> <li>Kauselmann G, Weiler M, Wulff P, et al. (1999). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171621">"The polo-like protein kinases Fnk and Snk associate with a Ca(2+)- and integrin-binding protein and are regulated dynamically with synaptic plasticity"</a>. <i>EMBO J</i>. 18 (20): 5528–39. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1093%2Femboj%2F18.20.5528">10.1093/emboj/18.20.5528</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1171621">1171621</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10523297">10523297</a>.</li> <li>Hwang PM, Vogel HJ (2000). "Structures of the platelet calcium- and integrin-binding protein and the alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies". <i>J. Mol. Recognit</i>. 13 (2): 83–92. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2F%28SICI%291099-1352%28200003%2F04%2913%3A2%3C83%3A%3AAID-JMR491%3E3.0.CO%3B2-A">10.1002/(SICI)1099-1352(200003/04)13:2<83::AID-JMR491>3.0.CO;2-A</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10822252">10822252</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:42776144">42776144</a>.</li> <li>Holtrich U, Wolf G, Yuan J, et al. (2000). "Adhesion induced expression of the serine/threonine kinase Fnk in human macrophages". <i>Oncogene</i>. 19 (42): 4832–9. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2Fsj.onc.1203845">10.1038/sj.onc.1203845</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11039900">11039900</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:25807289">25807289</a>.</li> <li>Haataja L, Kaartinen V, Groffen J, Heisterkamp N (2002). <a href="https://doi.org/10.1074%2Fjbc.M105363200">"The small GTPase Rac3 interacts with the integrin-binding protein CIB and promotes integrin alpha(IIb)beta(3)-mediated adhesion and spreading"</a>. <i>J. Biol. Chem</i>. 277 (10): 8321–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M105363200">10.1074/jbc.M105363200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11756406">11756406</a>.</li> <li>Whitehouse C, Chambers J, Howe K, et al. (2002). <a href="https://doi.org/10.1046%2Fj.0014-2956.2001.02681.x">"NBR1 interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB) and shows developmentally restricted expression in the neural tube"</a>. <i>Eur. J. Biochem</i>. 269 (2): 538–45. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1046%2Fj.0014-2956.2001.02681.x">10.1046/j.0014-2956.2001.02681.x</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11856312">11856312</a>.</li> <li>Hollenbach AD, McPherson CJ, Lagutina I, Grosveld G (2002). "The EF-hand calcium-binding protein calmyrin inhibits the transcriptional and DNA-binding activity of Pax3". <i>Biochim. Biophys. Acta</i>. 1574 (3): 321–8. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fs0167-4781%2802%2900230-0">10.1016/s0167-4781(02)00230-0</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11997098">11997098</a>.</li> <li>Henderson MJ, Russell AJ, Hird S, et al. (2002). <a href="https://doi.org/10.1074%2Fjbc.M203527200">"EDD, the human hyperplastic discs protein, has a role in progesterone receptor coactivation and potential involvement in DNA damage response"</a>. <i>J. Biol. Chem</i>. 277 (29): 26468–78. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M203527200">10.1074/jbc.M203527200</a>. <a href="/facts/Hdl_(identifier)/rdebSxmC">hdl</a>:<a href="https://hdl.handle.net/1885%2F64590">1885/64590</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12011095">12011095</a>.</li> <li>Barry WT, Boudignon-Proudhon C, Shock DD, et al. (2002). <a href="https://doi.org/10.1074%2Fjbc.M202983200">"Molecular basis of CIB binding to the integrin alpha IIb cytoplasmic domain"</a>. <i>J. Biol. Chem</i>. 277 (32): 28877–83. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M202983200">10.1074/jbc.M202983200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12023286">12023286</a>.</li> <li>Strausberg RL, Feingold EA, Grouse LH, et al. (2003). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241">"Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences"</a>. <i>Proc. Natl. Acad. Sci. U.S.A</i>. 99 (26): 16899–903. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/2002PNAS...9916899M">2002PNAS...9916899M</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1073%2Fpnas.242603899">10.1073/pnas.242603899</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC139241">139241</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12477932">12477932</a>.</li> <li>Ma S, Liu MA, Yuan YL, Erikson RL (2003). "The serum-inducible protein kinase Snk is a G1 phase polo-like kinase that is inhibited by the calcium- and integrin-binding protein CIB". <i>Mol. Cancer Res</i>. 1 (5): 376–84. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12651910">12651910</a>.</li> <li>Naik UP, Naik MU (2003). <a href="https://doi.org/10.1182%2Fblood-2003-02-0591">"Association of CIB with GPIIb/IIIa during outside-in signaling is required for platelet spreading on fibrinogen"</a>. <i>Blood</i>. 102 (4): 1355–62. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1182%2Fblood-2003-02-0591">10.1182/blood-2003-02-0591</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12714504">12714504</a>.</li> <li>Naik MU, Naik UP (2004). <a href="https://doi.org/10.1182%2Fblood-2003-05-1703">"Calcium-and integrin-binding protein regulates focal adhesion kinase activity during platelet spreading on immobilized fibrinogen"</a>. <i>Blood</i>. 102 (10): 3629–36. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1182%2Fblood-2003-05-1703">10.1182/blood-2003-05-1703</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12881299">12881299</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:41760625">41760625</a>.</li> <li>Yamniuk AP, Nguyen LT, Hoang TT, Vogel HJ (2004). "Metal ion binding properties and conformational states of calcium- and integrin-binding protein". <i>Biochemistry</i>. 43 (9): 2558–68. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1021%2Fbi035432b">10.1021/bi035432b</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/14992593">14992593</a>.</li> <li>Lee GE, Yu EY, Cho CH, et al. (2004). <a href="https://doi.org/10.1074%2Fjbc.M401843200">"DNA-protein kinase catalytic subunit-interacting protein KIP binds telomerase by interacting with human telomerase reverse transcriptase"</a>. <i>J. Biol. Chem</i>. 279 (33): 34750–5. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M401843200">10.1074/jbc.M401843200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/15190070">15190070</a>.</li> <li>Lehner B, Sanderson CM (2004). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC442147">"A protein interaction framework for human mRNA degradation"</a>. <i>Genome Res</i>. 14 (7): 1315–23. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1101%2Fgr.2122004">10.1101/gr.2122004</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC442147">442147</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/15231747">15231747</a>.</li></ul> <h2 id="external-links">External links</h2> <ul><li>Human <a href="https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&singleSearch=knownCanonical&position=CIB1"><i>CIB1</i></a> genome location and <a href="https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_type=knownGene&hgg_gene=CIB1"><i>CIB1</i></a> gene details page in the <a href="/facts/UCSC_Genome_Browser/kwumPyLb">UCSC Genome Browser</a>.</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Naik UP, Patel PM, Parise LV (Apr 1997). "Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain". J Biol Chem. 272 (8): 4651–4. doi:10.1074/jbc.272.8.4651. PMID 9030514. <a href="https://doi.org/10.1074%2Fjbc.272.8.4651" target="_blank">https://doi.org/10.1074%2Fjbc.272.8.4651</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Hattori A, Seki N, Hayashi A, Kozuma S, Saito T (Aug 2000). "Genomic structure of mouse and human genes for DNA-PKcs interacting protein (KIP)". DNA Seq. 10 (6): 415–8. doi:10.3109/10425170009015612. PMID 10826701. S2CID 21570442. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>"Entrez Gene: CIB1 calcium and integrin binding 1 (calmyrin)". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10519" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10519</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>"Entrez Gene: CIB1 calcium and integrin binding 1 (calmyrin)". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10519" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10519</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>Leisner TM, Freeman TC, Black JL, Parise LV (August 2016). "CIB1: a small protein with big ambitions". The FASEB Journal. 30 (8): 2640–2650. doi:10.1096/fj.201500073R. ISSN 0892-6638. PMC 4970603. PMID 27118676. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4970603" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4970603</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Kretsinger RH, Nockolds CE (1973-05-10). "Carp muscle calcium-binding protein. II. Structure determination and general description". The Journal of Biological Chemistry. 248 (9): 3313–3326. doi:10.1016/S0021-9258(19)44043-X. ISSN 0021-9258. PMID 4700463. <a href="https://doi.org/10.1016%2FS0021-9258%2819%2944043-X" target="_blank">https://doi.org/10.1016%2FS0021-9258%2819%2944043-X</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>Leisner TM, Freeman TC, Black JL, Parise LV (August 2016). "CIB1: a small protein with big ambitions". The FASEB Journal. 30 (8): 2640–2650. doi:10.1096/fj.201500073R. ISSN 0892-6638. PMC 4970603. 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