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PTK2B
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<h2 id="function">Function</h2> <p>This gene encodes a cytoplasmic protein tyrosine kinase that is involved in calcium-induced regulation of ion channels and activation of the <a href="/facts/MAPK_signaling_pathway/jfpd0YvE">MAP kinase signaling pathway</a>. The encoded protein may represent an important signaling intermediate between neuropeptide-activated receptors or neurotransmitters that increase calcium flux and the downstream signals that regulate neuronal activity.<a class="footnote-ref" id="fnref:3" href="#fn:3"><sup>3</sup></a> </p><p>The encoded protein undergoes rapid tyrosine phosphorylation and activation in response to increases in the intracellular calcium concentration <a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> , <a href="/facts/Nicotinic_acetylcholine_receptor/k2s2pPHr">nicotinic acetylcholine receptor</a> activation, membrane depolarization, or <a href="/facts/Protein_kinase_C/6WSQgAWv">protein kinase C</a> activation.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> In addition, SOCE-induced Pyk2 activation mediates disassembly of <a href="/facts/Endothelial/L4ENFVnw">endothelial</a> <a href="/facts/Adherens_junctions/CNFe2Qaj">adherens junctions</a>, via tyrosine (Y1981-residue) phosphorylation of VE-PTP.<a class="footnote-ref" id="fnref:6" href="#fn:6"><sup>6</sup></a> </p><p>This protein has been shown to bind a CRK-associated substrate, a nephrocystin, a GTPase regulator associated with <a href="/facts/Focal_Adhesion_Kinase/lx4qXfst">FAK</a>, and the SH2 domain of <a href="/facts/GRB2/uaFzqAbM">GRB2</a>.<a class="footnote-ref" id="fnref:7" href="#fn:7"><sup>7</sup></a> </p><p>The encoded protein is a member of the FAK subfamily of protein tyrosine kinases but lacks significant sequence similarity to kinases from other subfamilies. Four transcript variants encoding two different isoforms have been found for this gene.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> </p> <h2 id="interactions">Interactions</h2> <p>PTK2B has been shown to <a href="/facts/Protein-protein_interaction/etvm9Wmg">interact</a> with: </p> <ul><li><a href="/facts/BCAR1/b0nN7UAL">BCAR1</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></li> <li><a href="/facts/Cbl_gene/YND39pME">Cbl gene</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></li> <li><a href="/facts/DDEF2/JLK8zT4K">DDEF2</a>,<a class="footnote-ref" id="fnref:14" href="#fn:14"><sup>14</sup></a></li> <li><a href="/facts/DLG3/Iz8MeFY6">DLG3</a>,<a class="footnote-ref" id="fnref:15" href="#fn:15"><sup>15</sup></a></li> <li><a href="/facts/DLG4/d23IStkv">DLG4</a>,<a class="footnote-ref" id="fnref:16" href="#fn:16"><sup>16</sup></a></li> <li><a href="/facts/Ewing_sarcoma_breakpoint_region_1/YEMEaKFx">Ewing sarcoma breakpoint region 1</a>,<a class="footnote-ref" id="fnref:17" href="#fn:17"><sup>17</sup></a></li> <li><a href="/facts/FYN/Vap0K3Vn">FYN</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><a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a></li> <li><a href="/facts/GRIN2A/KE9KrAEj">GRIN2A</a>,<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a><a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a></li> <li><a href="/facts/Gelsolin/FxNYGoz0">Gelsolin</a>,<a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a></li> <li><a href="/facts/NPHP1/elkQXcHb">NPHP1</a>,<a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a></li> <li><a href="/facts/PITPNM1/xnd43tll">PITPNM1</a>,<a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a></li> <li><a href="/facts/PTPN11/JswVqKP3">PTPN11</a>,<a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a></li> <li><a href="/facts/PTPN6/gCEKFay6">PTPN6</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/Paxillin/f8bBseWR">Paxillin</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><a class="footnote-ref" id="fnref:31" href="#fn:31"><sup>31</sup></a></li> <li><a href="/facts/RAS_p21_protein_activator_1/K0u6eU1P">RAS p21 protein activator 1</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/RB1CC1/q4GtVBMU">RB1CC1</a>,<a class="footnote-ref" id="fnref:34" href="#fn:34"><sup>34</sup></a></li> <li><a href="/facts/SORBS2/j27svCGX">SORBS2</a>,<a class="footnote-ref" id="fnref:35" href="#fn:35"><sup>35</sup></a></li> <li><a href="/facts/Src_(gene)/5SCJqCU4">Src</a>,<a class="footnote-ref" id="fnref:36" href="#fn:36"><sup>36</sup></a><a class="footnote-ref" id="fnref:37" href="#fn:37"><sup>37</sup></a><a class="footnote-ref" id="fnref:38" href="#fn:38"><sup>38</sup></a> and</li> <li><a href="/facts/TGFB1I1/7glThcHB">TGFB1I1</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><a class="footnote-ref" id="fnref:41" href="#fn:41"><sup>41</sup></a></li></ul> <ul><li>VE-PTP<a class="footnote-ref" id="fnref:42" href="#fn:42"><sup>42</sup></a></li></ul> <h2 id="see-also">See also</h2> <ul><li><a href="/facts/Tyrosine_kinase/26Ln0qJ4">Tyrosine kinase</a></li></ul> <h2 id="further-reading">Further reading</h2> <ul><li>Avraham S, Avraham H (1997). "Characterization of the novel focal adhesion kinase RAFTK in hematopoietic cells". <i>Leuk. Lymphoma</i>. 27 (3–4): 247–56. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.3109%2F10428199709059681">10.3109/10428199709059681</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9402324">9402324</a>.</li> <li>Schlaepfer DD, Hauck CR, Sieg DJ (1999). <a href="http://nbn-resolving.de/urn:nbn:de:bsz:352-opus-37555">"Signaling through focal adhesion kinase"</a>. <i>Prog. Biophys. Mol. Biol</i>. 71 (3–4): 435–78. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0079-6107%2898%2900052-2">10.1016/S0079-6107(98)00052-2</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10354709">10354709</a>.</li> <li>Loeser RF (2002). "Integrins and cell signaling in chondrocytes". <i>Biorheology</i>. 39 (1–2): 119–24. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12082274">12082274</a>.</li></ul> <h2 id="external-links">External links</h2> <ul><li>Overview of all the structural information available in the <a href="/facts/Protein_Data_Bank/oUhq4ABD">PDB</a> for <a href="/facts/UniProt/lfDDHjAl">UniProt</a>: <i><a href="https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/Q14289">Q14289</a></i> (Protein-tyrosine kinase 2-beta) at the <a href="/facts/PDBe-KB/p1WX7lPH">PDBe-KB</a>.</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Lev S, Moreno H, Martinez R, Canoll P, Peles E, Musacchio JM, Plowman GD, Rudy B, Schlessinger J (September 1995). "Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions". Nature. 376 (6543): 737–45. Bibcode:1995Natur.376..737L. doi:10.1038/376737a0. PMID 7544443. S2CID 4320927. <a href="https://doi.org/10.1038%2F376737a0" target="_blank">https://doi.org/10.1038%2F376737a0</a> <a href="#fnref:1" class="footnote-back-ref">↩</a></p></li> <li id="fn:2"><p>Avraham S, London R, Fu Y, Ota S, Hiregowdara D, Li J, Jiang S, Pasztor LM, White RA, Groopman JE (1995). "Identification and characterization of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain". J. Biol. Chem. 270 (46): 27742–51. doi:10.1074/jbc.270.46.27742. PMID 7499242. <a href="https://doi.org/10.1074%2Fjbc.270.46.27742" target="_blank">https://doi.org/10.1074%2Fjbc.270.46.27742</a> <a href="#fnref:2" class="footnote-back-ref">↩</a></p></li> <li id="fn:3"><p>"Entrez Gene: PTK2B PTK2B protein tyrosine kinase 2 beta". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2185" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2185</a> <a href="#fnref:3" class="footnote-back-ref">↩</a></p></li> <li id="fn:4"><p>Soni D, Regmi SC, Wang DM, DebRoy A, Zhao YY, Vogel SM, Malik AB, Tiruppathi C (Apr 2017). "Pyk2 Phosphorylation of VE-PTP Downstream of STIM1 induced Ca2+ entry Regulates Disassembly of Adherens Junctions". American Journal of Physiology. Lung Cellular and Molecular Physiology. 312 (6): L1003 – L1017. doi:10.1152/ajplung.00008.2017. PMC 5495943. PMID 28385807. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5495943" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5495943</a> <a href="#fnref:4" class="footnote-back-ref">↩</a></p></li> <li id="fn:5"><p>"Entrez Gene: PTK2B PTK2B protein tyrosine kinase 2 beta". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2185" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2185</a> <a href="#fnref:5" class="footnote-back-ref">↩</a></p></li> <li id="fn:6"><p>Soni D, Regmi SC, Wang DM, DebRoy A, Zhao YY, Vogel SM, Malik AB, Tiruppathi C (Apr 2017). "Pyk2 Phosphorylation of VE-PTP Downstream of STIM1 induced Ca2+ entry Regulates Disassembly of Adherens Junctions". American Journal of Physiology. Lung Cellular and Molecular Physiology. 312 (6): L1003 – L1017. doi:10.1152/ajplung.00008.2017. PMC 5495943. PMID 28385807. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5495943" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5495943</a> <a href="#fnref:6" class="footnote-back-ref">↩</a></p></li> <li id="fn:7"><p>"Entrez Gene: PTK2B PTK2B protein tyrosine kinase 2 beta". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2185" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2185</a> <a href="#fnref:7" class="footnote-back-ref">↩</a></p></li> <li id="fn:8"><p>"Entrez Gene: PTK2B PTK2B protein tyrosine kinase 2 beta". <a href="https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2185" target="_blank">https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2185</a> <a href="#fnref:8" class="footnote-back-ref">↩</a></p></li> <li id="fn:9"><p>Manié SN, Beck AR, Astier A, Law SF, Canty T, Hirai H, Druker BJ, Avraham H, Haghayeghi N, Sattler M, Salgia R, Griffin JD, Golemis EA, Freedman AS (February 1997). "Involvement of p130(Cas) and p105(HEF1), a novel Cas-like docking protein, in a cytoskeleton-dependent signaling pathway initiated by ligation of integrin or antigen receptor on human B cells". J. Biol. Chem. 272 (7): 4230–6. doi:10.1074/jbc.272.7.4230. hdl:20.500.12613/9177. PMID 9020138. <a href="https://doi.org/10.1074%2Fjbc.272.7.4230" target="_blank">https://doi.org/10.1074%2Fjbc.272.7.4230</a> <a href="#fnref:9" class="footnote-back-ref">↩</a></p></li> <li id="fn:10"><p>Anfosso F, Bardin N, Vivier E, Sabatier F, Sampol J, Dignat-George F (January 2001). "Outside-in signaling pathway linked to CD146 engagement in human endothelial cells". J. Biol. Chem. 276 (2): 1564–9. doi:10.1074/jbc.M007065200. PMID 11036077. <a href="https://doi.org/10.1074%2Fjbc.M007065200" target="_blank">https://doi.org/10.1074%2Fjbc.M007065200</a> <a href="#fnref:10" class="footnote-back-ref">↩</a></p></li> <li id="fn:11"><p>Astier A, Avraham H, Manie SN, Groopman J, Canty T, Avraham S, Freedman AS (January 1997). "The related adhesion focal tyrosine kinase is tyrosine-phosphorylated after beta1-integrin stimulation in B cells and binds to p130cas". J. Biol. Chem. 272 (1): 228–32. doi:10.1074/jbc.272.1.228. PMID 8995252. <a href="https://doi.org/10.1074%2Fjbc.272.1.228" target="_blank">https://doi.org/10.1074%2Fjbc.272.1.228</a> <a href="#fnref:11" class="footnote-back-ref">↩</a></p></li> <li id="fn:12"><p>Haglund K, Ivankovic-Dikic I, Shimokawa N, Kruh GD, Dikic I (May 2004). "Recruitment of Pyk2 and Cbl to lipid rafts mediates signals important for actin reorganization in growing neurites". J. Cell Sci. 117 (Pt 12): 2557–68. doi:10.1242/jcs.01148. PMID 15128873. S2CID 14083271. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:12" class="footnote-back-ref">↩</a></p></li> <li id="fn:13"><p>Sanjay A, Houghton A, Neff L, DiDomenico E, Bardelay C, Antoine E, Levy J, Gailit J, Bowtell D, Horne WC, Baron R (January 2001). "Cbl associates with Pyk2 and Src to regulate Src kinase activity, alpha(v)beta(3) integrin-mediated signaling, cell adhesion, and osteoclast motility". J. Cell Biol. 152 (1): 181–95. doi:10.1083/jcb.152.1.181. PMC 2193648. PMID 11149930. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2193648" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2193648</a> <a href="#fnref:13" class="footnote-back-ref">↩</a></p></li> <li id="fn:14"><p>Andreev J, Simon JP, Sabatini DD, Kam J, Plowman G, Randazzo PA, Schlessinger J (March 1999). "Identification of a new Pyk2 target protein with Arf-GAP activity". Mol. Cell. Biol. 19 (3): 2338–50. doi:10.1128/MCB.19.3.2338. PMC 84026. PMID 10022920. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84026" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84026</a> <a href="#fnref:14" class="footnote-back-ref">↩</a></p></li> <li id="fn:15"><p>Seabold GK, Burette A, Lim IA, Weinberg RJ, Hell JW (April 2003). "Interaction of the tyrosine kinase Pyk2 with the N-methyl-D-aspartate receptor complex via the Src homology 3 domains of PSD-95 and SAP102". J. Biol. Chem. 278 (17): 15040–8. doi:10.1074/jbc.M212825200. PMID 12576483. <a href="https://doi.org/10.1074%2Fjbc.M212825200" target="_blank">https://doi.org/10.1074%2Fjbc.M212825200</a> <a href="#fnref:15" class="footnote-back-ref">↩</a></p></li> <li id="fn:16"><p>Seabold GK, Burette A, Lim IA, Weinberg RJ, Hell JW (April 2003). "Interaction of the tyrosine kinase Pyk2 with the N-methyl-D-aspartate receptor complex via the Src homology 3 domains of PSD-95 and SAP102". J. Biol. Chem. 278 (17): 15040–8. doi:10.1074/jbc.M212825200. PMID 12576483. <a href="https://doi.org/10.1074%2Fjbc.M212825200" target="_blank">https://doi.org/10.1074%2Fjbc.M212825200</a> <a href="#fnref:16" class="footnote-back-ref">↩</a></p></li> <li id="fn:17"><p>Felsch JS, Lane WS, Peralta EG (May 1999). "Tyrosine kinase Pyk2 mediates G-protein-coupled receptor regulation of the Ewing sarcoma RNA-binding protein EWS". Curr. Biol. 9 (9): 485–8. Bibcode:1999CBio....9..485F. doi:10.1016/s0960-9822(99)80214-0. PMID 10322114. S2CID 15389306. <a href="https://doi.org/10.1016%2Fs0960-9822%2899%2980214-0" target="_blank">https://doi.org/10.1016%2Fs0960-9822%2899%2980214-0</a> <a href="#fnref:17" class="footnote-back-ref">↩</a></p></li> <li id="fn:18"><p>Ganju RK, Hatch WC, Avraham H, Ona MA, Druker B, Avraham S, Groopman JE (March 1997). "RAFTK, a novel member of the focal adhesion kinase family, is phosphorylated and associates with signaling molecules upon activation of mature T lymphocytes". J. Exp. Med. 185 (6): 1055–63. doi:10.1084/jem.185.6.1055. PMC 2196239. PMID 9091579. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196239" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196239</a> <a href="#fnref:18" class="footnote-back-ref">↩</a></p></li> <li id="fn:19"><p>Katagiri T, Takahashi T, Sasaki T, Nakamura S, Hattori S (June 2000). "Protein-tyrosine kinase Pyk2 is involved in interleukin-2 production by Jurkat T cells via its tyrosine 402". J. Biol. Chem. 275 (26): 19645–52. doi:10.1074/jbc.M909828199. PMID 10867021. <a href="https://doi.org/10.1074%2Fjbc.M909828199" target="_blank">https://doi.org/10.1074%2Fjbc.M909828199</a> <a href="#fnref:19" class="footnote-back-ref">↩</a></p></li> <li id="fn:20"><p>Qian D, Lev S, van Oers NS, Dikic I, Schlessinger J, Weiss A (April 1997). "Tyrosine phosphorylation of Pyk2 is selectively regulated by Fyn during TCR signaling". J. Exp. Med. 185 (7): 1253–9. doi:10.1084/jem.185.7.1253. PMC 2196260. PMID 9104812. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196260" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196260</a> <a href="#fnref:20" class="footnote-back-ref">↩</a></p></li> <li id="fn:21"><p>Seabold GK, Burette A, Lim IA, Weinberg RJ, Hell JW (April 2003). "Interaction of the tyrosine kinase Pyk2 with the N-methyl-D-aspartate receptor complex via the Src homology 3 domains of PSD-95 and SAP102". J. Biol. Chem. 278 (17): 15040–8. doi:10.1074/jbc.M212825200. PMID 12576483. <a href="https://doi.org/10.1074%2Fjbc.M212825200" target="_blank">https://doi.org/10.1074%2Fjbc.M212825200</a> <a href="#fnref:21" class="footnote-back-ref">↩</a></p></li> <li id="fn:22"><p>Liu Y, Zhang G, Gao C, Hou X (August 2001). "NMDA receptor activation results in tyrosine phosphorylation of NMDA receptor subunit 2A(NR2A) and interaction of Pyk2 and Src with NR2A after transient cerebral ischemia and reperfusion". Brain Res. 909 (1–2): 51–8. doi:10.1016/s0006-8993(01)02619-1. PMID 11478920. S2CID 21062909. <a href="/wiki/Doi_(identifier)" target="_blank">/wiki/Doi_(identifier)</a> <a href="#fnref:22" class="footnote-back-ref">↩</a></p></li> <li id="fn:23"><p>Wang Q, Xie Y, Du QS, Wu XJ, Feng X, Mei L, McDonald JM, Xiong WC (February 2003). "Regulation of the formation of osteoclastic actin rings by proline-rich tyrosine kinase 2 interacting with gelsolin". J. Cell Biol. 160 (4): 565–75. doi:10.1083/jcb.200207036. PMC 2173747. PMID 12578912. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173747" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173747</a> <a href="#fnref:23" class="footnote-back-ref">↩</a></p></li> <li id="fn:24"><p>Benzing T, Gerke P, Höpker K, Hildebrandt F, Kim E, Walz G (August 2001). "Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggers phosphorylation of Pyk2". Proc. Natl. Acad. Sci. U.S.A. 98 (17): 9784–9. Bibcode:2001PNAS...98.9784B. doi:10.1073/pnas.171269898. PMC 55530. PMID 11493697. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC55530" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC55530</a> <a href="#fnref:24" class="footnote-back-ref">↩</a></p></li> <li id="fn:25"><p>Lev S, Hernandez J, Martinez R, Chen A, Plowman G, Schlessinger J (March 1999). "Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein". Mol. Cell. Biol. 19 (3): 2278–88. doi:10.1128/mcb.19.3.2278. PMC 84020. PMID 10022914. <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84020" target="_blank">https://www.ncbi.nlm.nih.gov/pmc/articles/PMC84020</a> <a href="#fnref:25" class="footnote-back-ref">↩</a></p></li> <li id="fn:26"><p>Chauhan D, Pandey P, Hideshima T, Treon S, Raje N, Davies FE, Shima Y, Tai YT, Rosen S, Avraham S, Kharbanda S, Anderson KC (September 2000). "SHP2 mediates the protective effect of interleukin-6 against dexamethasone-induced apoptosis in multiple myeloma cells". J. Biol. Chem. 275 (36): 27845–50. doi:10.1074/jbc.M003428200. PMID 10880513. <a href="https://doi.org/10.1074%2Fjbc.M003428200" target="_blank">https://doi.org/10.1074%2Fjbc.M003428200</a> <a href="#fnref:26" class="footnote-back-ref">↩</a></p></li> <li id="fn:27"><p>Ganju RK, Brubaker SA, Chernock RD, Avraham S, Groopman JE (June 2000). "Beta-chemokine receptor CCR5 signals through SHP1, SHP2, and Syk". J. Biol. Chem. 275 (23): 17263–8. doi:10.1074/jbc.M000689200. PMID 10747947. <a href="https://doi.org/10.1074%2Fjbc.M000689200" target="_blank">https://doi.org/10.1074%2Fjbc.M000689200</a> <a href="#fnref:27" class="footnote-back-ref">↩</a></p></li> <li id="fn:28"><p>Kumar S, Avraham S, Bharti A, Goyal J, Pandey P, Kharbanda S (October 1999). 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