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SLAMF1
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<h2 id="gene">Gene</h2> <p>The <a href="/facts/Gene/e1swwPY6">gene</a> encoding SLAMF1 <a href="/facts/Receptor_(biochemistry)/tjTAC76a">receptor</a> is located on the human <a href="/facts/Chromosome_1/2ujmYz2w">chromosome 1</a>. It consists of eight <a href="/facts/Exon/8KWJtLuN">exons</a> and seven <a href="/facts/Intron/LS6YdBEK">introns</a>. <a href="/facts/Alternative_splicing/nNRwPVNK">Alternative splicing</a> of SLAMF1 transcripts results in several <a href="/facts/Protein_isoform/oWmzfg4l">isoforms</a> of the <a href="/facts/Protein/Jxmagu3E">protein</a>, including the conventional transmembrane isoform (mCD150), secreted isoform (sCD150) cytoplasmic isoform (cCD150), and the novel transmembrane isoform (nCD150).<a class="footnote-ref" id="fnref:4" href="#fn:4"><sup>4</sup></a> </p><p>SLAMF1 is expressed in <a href="/facts/Hematopoietic_stem_cell/RQNE9IRu">hematopoietic stem cells</a>. It is also used as one of the markers for their identification.<a class="footnote-ref" id="fnref:5" href="#fn:5"><sup>5</sup></a> Furthermore, its expression was detected in <a href="/facts/Thymocyte/zBuBsKJJ">thymocytes</a>, <a href="/facts/Natural_killer_T_cell/fokQzmL3">NKT cells</a>, <a href="/facts/T_cell/5z6PQ9UN">T cells</a>, <a href="/facts/B_cell/6Y1tgwwp">B cells</a>, <a href="/facts/Monocyte/FW4NNMKM">monocytes</a>, <a href="/facts/Macrophage/z7hkQu3o">macrophages</a> and <a href="/facts/Dendritic_cell/19KBuKFK">dendritic cells</a>. <a href="/facts/Monocyte/FW4NNMKM">Monocytes</a>, <a href="/facts/Macrophage/z7hkQu3o">macrophages</a> and <a href="/facts/Dendritic_cell/19KBuKFK">dendritic cells</a> express SLAMF1 after their activation. The activation of <a href="/facts/T_cell/5z6PQ9UN">T cells</a> and <a href="/facts/Plasma_cell/1fY4bFHR">plasma cell</a> differentiation leads to the increased expression of this <a href="/facts/Receptor_(biochemistry)/tjTAC76a">receptor</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> The interaction of SLAMF1 <a href="/facts/Promoter_(genetics)/YDYBzLfg">promoter</a> and <a href="/facts/Enhancer_(genetics)/E5NU74sw">enhancers</a> with the <a href="/facts/EBF1/9UWnUlxK">Early B-cell factor 1 (EBF1)</a> is required for the expression of SLAMF1 gene in <a href="/facts/B_cell/6Y1tgwwp">B cells</a>. <a href="/facts/STAT6/lfhIB0LS">STAT6</a>, <a href="/facts/IRF4/0ljxfbqc">IRF4</a>, and <a href="/facts/NF-%CE%BAB/qcpt5vuQ">NF-kB</a> factors involved in the transfer of the signals from the <a href="/facts/B-cell_receptor/J6qRYYkN">B-cell receptor</a>, its co-receptors and <a href="/facts/Interleukin-4_receptor/1Xh5aYyA">IL-4R</a>, also play important role in the regulation of SLAMF1 expression.<a class="footnote-ref" id="fnref:8" href="#fn:8"><sup>8</sup></a> The expression of SLAMF1 is not restricted to <a href="/facts/White_blood_cell/vsDunUK0">immune cells</a> and their progenitors. From non-immune cells, <a href="/facts/Platelet/I0xrDVGa">platelets</a> express SLAMF1.<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> </p> <h2 id="structure">Structure</h2> <p>SLAMF1 is a type I <a href="/facts/Transmembrane_protein/0vQH5HrM">transmembrane protein</a> belonging to the <a href="/facts/Immunoglobulin_superfamily/Wveu4BIL">immunoglobulin superfamily</a>.<a class="footnote-ref" id="fnref:11" href="#fn:11"><sup>11</sup></a> Its molecular weight is between 70 kDa and 95 kDa. The extracellular region of the <a href="/facts/Receptor_(biochemistry)/tjTAC76a">receptor</a> is composed of one Ig variable-like <a href="/facts/Protein_domain/oUpFcSsl">domain</a> and one Ig constant 2-like <a href="/facts/Protein_domain/oUpFcSsl">domain</a>. The intracellular region of the <a href="/facts/Receptor_(biochemistry)/tjTAC76a">receptor</a> contains two intracellular tyrosine-based switch motives (ITSMs) that interact with <a href="/facts/SH2_domain/1kEmHvzY">SH2 domain</a>-containing <a href="/facts/Protein/Jxmagu3E">proteins</a>. However, nCD150 intracellular region differs from other <a href="/facts/Protein_isoform/oWmzfg4l">isoforms</a> of this <a href="/facts/Protein/Jxmagu3E">protein</a>, it lacks ITSMs. sCD150 isoform lacks the <a href="/facts/Transmembrane_domain/D1j0PwSR">transmembrane domain</a> and therefore, it can not be anchored to the <a href="/facts/Cell_membrane/vAXSD0DT">cell membrane</a>.<a class="footnote-ref" id="fnref:12" href="#fn:12"><sup>12</sup></a> </p> <h2 id="signaling">Signaling</h2> <p>The <a href="/facts/Receptor_(biochemistry)/tjTAC76a">receptor</a> SLAMF1 mediates homophilic interactions as most of the <a href="/facts/Receptor_(biochemistry)/tjTAC76a">receptors</a> from the <a href="/facts/Signalling_lymphocyte_activation_molecule_family/IWqQUrXC">SLAMF</a>. <a href="/facts/Cell_signaling/6oYAVP9I">Signaling</a> from SLAMF1 <a href="/facts/Receptor_(biochemistry)/tjTAC76a">receptor</a> can be activating or inhibitory. The type of the signal depends on the <a href="/facts/Cell_type/1boyDWXb">cell type</a>, <a href="/facts/Cellular_differentiation/bCVqUG7w">differentiation</a> stage, and the combination of signals from other <a href="/facts/Receptor_(biochemistry)/tjTAC76a">receptors</a>.<a class="footnote-ref" id="fnref:13" href="#fn:13"><sup>13</sup></a> </p><p><a href="/facts/SH2_domain/1kEmHvzY">SH2 domain</a>-containing <a href="/facts/Protein/Jxmagu3E">proteins</a>, specifically <a href="/facts/Signal_transducing_adaptor_protein/flz9ya87">adaptor proteins</a> <a href="/facts/SH2D1A/LcaX6RRS">SAP</a> and <a href="/facts/SH2D1B/HRTDGtoK">EAT-2</a>, and <a href="/facts/Phosphatase/LBJs1fXx">phosphatases</a> <a href="/facts/PTPN6/gCEKFay6">SHP-1</a>, <a href="/facts/PTPN11/JswVqKP3">SHP-2</a> and <a href="/facts/INPP5D/8gnQQNMq">SHIP</a>, interact with ITSMs in the intracellular region of SLAMF1.<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> Binding of <a href="/facts/SH2D1A/LcaX6RRS">SAP</a> to ITSMs leads to the activation of the <a href="/facts/Kinase/dhlHpjnD">kinase</a> <a href="/facts/FYN/qCAEbIAb">Fyn</a> that phosphorylates <a href="/facts/Tyrosine/RJhEgE4C">tyrosines</a> of SLAMF1 and recruits downstream <a href="/facts/Cell_signaling/6oYAVP9I">signaling</a> <a href="/facts/Protein/Jxmagu3E">proteins</a>. Because of the high affinity of <a href="/facts/SH2D1A/LcaX6RRS">SAP</a> to <a href="/facts/Tyrosine/RJhEgE4C">tyrosine</a> phosphorylated ITSMs, it outcompetes the <a href="/facts/Phosphatase/LBJs1fXx">phosphatases</a> which are the mediators of the inhibitory signal. Therefore, the expression and availability of <a href="/facts/SH2D1A/LcaX6RRS">SAP</a> play a crucial role in the determination of the type of the signal.<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> </p> <h2 id="function">Function</h2> <p>SLAMF1 is involved in the regulation of <a href="/facts/Thymocyte/zBuBsKJJ">thymocyte</a> development, <a href="/facts/T_cell/5z6PQ9UN">T cell</a> <a href="/facts/Cell_proliferation/Jp3hWo2t">proliferation</a>, <a href="/facts/Cellular_differentiation/bCVqUG7w">differentiation</a> and <a href="/facts/T_cell/5z6PQ9UN">T cell</a> function, such as the cytotoxic activity of <a href="/facts/Cytotoxic_T_cell/e5eRg3XJ">CD8+ T cells</a> and the production of <a href="/facts/Interleukin_4/FacDJ3TY">IL-4</a>, <a href="/facts/Interleukin_13/zEaRbEqc">IL-13</a> and <a href="/facts/Interferon_gamma/r51CXVph">IFNγ</a>. In <a href="/facts/B_cell/6Y1tgwwp">B cells</a>, it regulates the <a href="/facts/Cell_proliferation/Jp3hWo2t">proliferation</a> and the <a href="/facts/Antibody/MX8pdTdP">antibody</a> production.<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> SLAMF1 acts as a self-ligand during the interaction between <a href="/facts/B_cell/6Y1tgwwp">B cells</a> and <a href="/facts/T_cell/5z6PQ9UN">T cells</a> and promotes <a href="/facts/Lymphocyte/pS2pv2Ma">lymphocyte</a> activation.<a class="footnote-ref" id="fnref:20" href="#fn:20"><sup>20</sup></a> </p><p>The development of <a href="/facts/Natural_killer_T_cell/fokQzmL3">NKT cells</a> is dependent on a signal mediated by <a href="/facts/SH2D1A/LcaX6RRS">SAP</a>. It was found out that the homophilic interaction of SLAMF1 or SLAMF6 is required for <a href="/facts/SH2D1A/LcaX6RRS">SAP</a> recruitment in <a href="/facts/Natural_killer_T_cell/fokQzmL3">NKT cells</a>. This interaction mediates a secondary signal crucial for <a href="/facts/Natural_killer_T_cell/fokQzmL3">NKT cell</a> <a href="/facts/Cellular_differentiation/bCVqUG7w">differentiation</a> and expansion in the <a href="/facts/Thymus/YYEJu7KA">thymus</a>.<a class="footnote-ref" id="fnref:21" href="#fn:21"><sup>21</sup></a> </p><p>SLAMF1 expression in <a href="/facts/Macrophage/z7hkQu3o">macrophages</a> is associated with killing of <a href="/facts/Gram-negative_bacteria/S1PbVtp4">Gram-negative bacteria</a>. SLAMF1 acts as a bacterial sensor. It is internalized after the recognition of <a href="/facts/Gram-negative_bacteria/S1PbVtp4">Gram-negative bacteria</a>, and it plays a role in the regulation of <a href="/facts/Phagosome/tEHvpGy9">phagosome</a> maturation, <a href="/facts/Reactive_oxygen_species/GpwSRugH">ROS</a> and <a href="/facts/Nitric_oxide/UvhdvDzp">NO</a> production. The absence of SLAMF1 in <a href="/facts/Phagocyte/1vbsR9er">phagocytes</a> leads, among other things, to the disruption of <a href="/facts/Cytokine/SdWpWABH">cytokine</a> production.<a class="footnote-ref" id="fnref:22" href="#fn:22"><sup>22</sup></a> </p> <h2 id="role-of-slamf1-in-diseases">Role of SLAMF1 in diseases</h2> <h3>Viral infections</h3> <p>SLAMF1 is a <a href="/facts/Receptor_(biochemistry)/tjTAC76a">receptor</a> for <i>Morbilliviruses.</i><a class="footnote-ref" id="fnref:23" href="#fn:23"><sup>23</sup></a> This <a href="/facts/Genus/m8EFjSms">genus</a> of <a href="/facts/Virus/mf88Bcbl">viruses</a> includes agents causing <a href="/facts/Measles/tepQCUIG">measles</a> in humans, <a href="/facts/Rinderpest/LFwtm3KT">rinderpest</a> in cattle and <a href="/facts/Canine_distemper/Il7tF7rX">distemper</a> in dogs and cats.<a class="footnote-ref" id="fnref:24" href="#fn:24"><sup>24</sup></a> Ig variable-like <a href="/facts/Protein_domain/oUpFcSsl">domain</a> of SLAMF1 binds to <a href="/facts/Hemagglutinin/1PphF1Ut">hemagglutinin</a> on the surface of the <a href="/facts/Virus/mf88Bcbl">virus</a> and this interaction mediates the <a href="/facts/Virus/mf88Bcbl">virus</a> entry into the host <a href="/facts/Cell_(biology)/bLM9UQvy">cell</a>.<a class="footnote-ref" id="fnref:25" href="#fn:25"><sup>25</sup></a> </p> <h3>Cancer</h3> <p>SLAMF1 is expressed in <a href="/facts/Cancer_cell/HXSQQjhw">cancer cells</a> in some types of <a href="/facts/Tumors_of_the_hematopoietic_and_lymphoid_tissues/tzyyShka">hematologic malignancies</a> (<a href="/facts/Cutaneous_T-cell_lymphoma/gVeNtJ9N">cutaneous T-cell lymphoma</a>, few types of <a href="/facts/Non-Hodgkin_lymphoma/KIFxt74F">B-cell non-Hodgkin´s lymphoma</a>, <a href="/facts/Hodgkin_lymphoma/mCeqnGty">Hodgkin´s lymphoma</a> and about 50 % of <a href="/facts/Chronic_lymphocytic_leukemia/jbaDruD9">chronic lymphocytic leukemia</a> cases).<a class="footnote-ref" id="fnref:26" href="#fn:26"><sup>26</sup></a> It regulates <a href="/facts/Cancer_cell/HXSQQjhw">cancer cell</a> growth and survival by activating <a href="/facts/PI3K/AKT/mTOR_pathway/bgWlgxQJ">PI3K/Akt/mTOR signaling pathway</a>. Therefore, SLAMF1 could be used as a diagnostical and prognostic marker in these cancer types.<a class="footnote-ref" id="fnref:27" href="#fn:27"><sup>27</sup></a> Several cases of <a href="/facts/Leukemia/WpEfW0Qh">leukemia</a> or <a href="/facts/Hodgkin_lymphoma/mCeqnGty">Hodgkin´s lymphoma</a> remission after <a href="/facts/Measles_morbillivirus/96sVRzuL">measles virus</a> infection or <a href="/facts/Vaccination/3SfpzPsd">vaccination</a> have been described. Therefore, SLAMF1 could be used as a target for cancer therapy which is based on the <a href="/facts/Measles_morbillivirus/96sVRzuL">measles virus</a>-mediated <a href="/facts/Lysis/th8pXeEn">lysis</a> of the <a href="/facts/Cancer_cell/HXSQQjhw">cancer cells</a>.<a class="footnote-ref" id="fnref:28" href="#fn:28"><sup>28</sup></a> </p><p>nCD150 isoform was found in <a href="/facts/Central_nervous_system_tumor/BkaCy7kU">tumors of the central nervous system</a>, such as <a href="/facts/Glioblastoma/hJojdA5x">glioblastoma</a>, anaplastic and diffuse <a href="/facts/Astrocytoma/AhLdpaep">astrocytoma</a> and <a href="/facts/Ependymoma/6GF8lmD9">ependymoma</a>.<a class="footnote-ref" id="fnref:29" href="#fn:29"><sup>29</sup></a> </p> <h2 id="further-reading">Further reading</h2> <ul><li>Punnonen J, Cocks BG, Carballido JM, Bennett B, Peterson D, Aversa G, de Vries JE (March 1997). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196230">"Soluble and membrane-bound forms of signaling lymphocytic activation molecule (SLAM) induce proliferation and Ig synthesis by activated human B lymphocytes"</a>. <i>The Journal of Experimental Medicine</i>. 185 (6): 993–1004. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1084%2Fjem.185.6.993">10.1084/jem.185.6.993</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196230">2196230</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9091591">9091591</a>.</li> <li>Sayos J, Wu C, Morra M, Wang N, Zhang X, Allen D, et al. (October 1998). "The X-linked lymphoproliferative-disease gene product SAP regulates signals induced through the co-receptor SLAM". <i>Nature</i>. 395 (6701): 462–469. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/1998Natur.395..462S">1998Natur.395..462S</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F26683">10.1038/26683</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/9774102">9774102</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:4324402">4324402</a>.</li> <li>Mikhalap SV, Shlapatska LM, Berdova AG, Law CL, Clark EA, Sidorenko SP (May 1999). <a href="https://doi.org/10.4049%2Fjimmunol.162.10.5719">"CDw150 associates with src-homology 2-containing inositol phosphatase and modulates CD95-mediated apoptosis"</a>. <i>Journal of Immunology</i>. 162 (10): 5719–5727. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.4049%2Fjimmunol.162.10.5719">10.4049/jimmunol.162.10.5719</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10229804">10229804</a>.</li> <li>Li SC, Gish G, Yang D, Coffey AJ, Forman-Kay JD, Ernberg I, et al. (December 1999). <a href="https://doi.org/10.1016%2FS0960-9822%2800%2980080-9">"Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A"</a>. <i>Current Biology</i>. 9 (23): 1355–1362. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS0960-9822%2800%2980080-9">10.1016/S0960-9822(00)80080-9</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10607564">10607564</a>.</li> <li>Rogge L, Bianchi E, Biffi M, Bono E, Chang SY, Alexander H, et al. (May 2000). "Transcript imaging of the development of human T helper cells using oligonucleotide arrays". <i>Nature Genetics</i>. 25 (1): 96–101. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F75671">10.1038/75671</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10802665">10802665</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:5449948">5449948</a>.</li> <li>Tatsuo H, Ono N, Tanaka K, Yanagi Y (August 2000). "SLAM (CDw150) is a cellular receptor for measles virus". <i>Nature</i>. 406 (6798): 893–897. <a href="/facts/Bibcode_(identifier)/9HtdQSGB">Bibcode</a>:<a href="https://ui.adsabs.harvard.edu/abs/2000Natur.406..893T">2000Natur.406..893T</a>. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1038%2F35022579">10.1038/35022579</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/10972291">10972291</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:4409405">4409405</a>.</li> <li>Lewis J, Eiben LJ, Nelson DL, Cohen JI, Nichols KE, Ochs HD, et al. (July 2001). <a href="https://zenodo.org/record/1229600">"Distinct interactions of the X-linked lymphoproliferative syndrome gene product SAP with cytoplasmic domains of members of the CD2 receptor family"</a>. <i>Clinical Immunology</i>. 100 (1): 15–23. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1006%2Fclim.2001.5035">10.1006/clim.2001.5035</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11414741">11414741</a>.</li> <li>Kruse M, Meinl E, Henning G, Kuhnt C, Berchtold S, Berger T, et al. (August 2001). <a href="https://doi.org/10.4049%2Fjimmunol.167.4.1989">"Signaling lymphocytic activation molecule is expressed on mature CD83+ dendritic cells and is up-regulated by IL-1 beta"</a>. <i>Journal of Immunology</i>. 167 (4): 1989–1995. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.4049%2Fjimmunol.167.4.1989">10.4049/jimmunol.167.4.1989</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11489980">11489980</a>.</li> <li>Bleharski JR, Niazi KR, Sieling PA, Cheng G, Modlin RL (September 2001). <a href="https://doi.org/10.4049%2Fjimmunol.167.6.3174">"Signaling lymphocytic activation molecule is expressed on CD40 ligand-activated dendritic cells and directly augments production of inflammatory cytokines"</a>. <i>Journal of Immunology</i>. 167 (6): 3174–3181. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.4049%2Fjimmunol.167.6.3174">10.4049/jimmunol.167.6.3174</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/11544303">11544303</a>.</li> <li>Murabayashi N, Kurita-Taniguchi M, Ayata M, Matsumoto M, Ogura H, Seya T (July 2002). "Susceptibility of human dendritic cells (DCs) to measles virus (MV) depends on their activation stages in conjunction with the level of CDw150: role of Toll stimulators in DC maturation and MV amplification". <i>Microbes and Infection</i>. 4 (8): 785–794. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2FS1286-4579%2802%2901598-8">10.1016/S1286-4579(02)01598-8</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12270725">12270725</a>.</li> <li>Li C, Iosef C, Jia CY, Han VK, Li SS (February 2003). <a href="https://doi.org/10.1074%2Fjbc.M206649200">"Dual functional roles for the X-linked lymphoproliferative syndrome gene product SAP/SH2D1A in signaling through the signaling lymphocyte activation molecule (SLAM) family of immune receptors"</a>. <i>The Journal of Biological Chemistry</i>. 278 (6): 3852–3859. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M206649200">10.1074/jbc.M206649200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12458214">12458214</a>.</li> <li>Hahm B, Arbour N, Naniche D, Homann D, Manchester M, Oldstone MB (March 2003). <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC149525">"Measles virus infects and suppresses proliferation of T lymphocytes from transgenic mice bearing human signaling lymphocytic activation molecule"</a>. <i>Journal of Virology</i>. 77 (6): 3505–3515. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1128%2FJVI.77.6.3505-3515.2003">10.1128/JVI.77.6.3505-3515.2003</a>. <a href="/facts/PMC_(identifier)/dX1zMt71">PMC</a> <a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC149525">149525</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12610126">12610126</a>.</li> <li>Del Valle JM, Engel P, Martín M (May 2003). <a href="https://doi.org/10.1074%2Fjbc.M301569200">"The cell surface expression of SAP-binding receptor CD229 is regulated via its interaction with clathrin-associated adaptor complex 2 (AP-2)"</a>. <i>The Journal of Biological Chemistry</i>. 278 (19): 17430–17437. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1074%2Fjbc.M301569200">10.1074/jbc.M301569200</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12621057">12621057</a>.</li> <li>Ferrand V, Li C, Romeo G, Yin L (May 2003). "Absence of SLAM mutations in EBV-associated lymphoproliferative disease patients". <i>Journal of Medical Virology</i>. 70 (1): 131–136. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1002%2Fjmv.10373">10.1002/jmv.10373</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/12629654">12629654</a>. <a href="/facts/S2CID_(identifier)/ldJsHa2Y">S2CID</a> <a href="https://api.semanticscholar.org/CorpusID:44309832">44309832</a>.</li> <li>Laaksonen K, Junikka M, Lahesmaa R, Terho EO, Savolainen J (December 2003). <a href="https://doi.org/10.1016%2Fj.jaci.2003.08.043">"In vitro allergen-induced mRNA expression of signaling lymphocytic activation molecule by PBMC of patients with allergic rhinitis is increased during specific pollen immunotherapy"</a>. <i>The Journal of Allergy and Clinical Immunology</i>. 112 (6): 1171–1177. <a href="/facts/Doi_(identifier)/muM9Etpq">doi</a>:<a href="https://doi.org/10.1016%2Fj.jaci.2003.08.043">10.1016/j.jaci.2003.08.043</a>. <a href="/facts/PMID_(identifier)/JlHAvMHt">PMID</a> <a href="https://pubmed.ncbi.nlm.nih.gov/14657878">14657878</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/Q13291">Q13291</a></i> (Signaling lymphocytic activation molecule) at the <a href="/facts/PDBe-KB/p1WX7lPH">PDBe-KB</a>.</li></ul> <h2 id="references">References</h2> <ol> <li id="fn:1"><p>Cocks BG, Chang CC, Carballido JM, Yssel H, de Vries JE, Aversa G (July 1995). 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