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2dle

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==Solution structure of the fourth fn3 domain of human receptor-type tyrosine-protein phosphatase eta==
==Solution structure of the fourth fn3 domain of human receptor-type tyrosine-protein phosphatase eta==
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<StructureSection load='2dle' size='340' side='right' caption='[[2dle]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2dle' size='340' side='right'caption='[[2dle]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2dle]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DLE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DLE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2dle]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DLE FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRJ, DEP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dle OCA], [https://pdbe.org/2dle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dle RCSB], [https://www.ebi.ac.uk/pdbsum/2dle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dle ProSAT], [https://www.topsan.org/Proteins/RSGI/2dle TOPSAN]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dle OCA], [http://pdbe.org/2dle PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dle RCSB], [http://www.ebi.ac.uk/pdbsum/2dle PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dle ProSAT], [http://www.topsan.org/Proteins/RSGI/2dle TOPSAN]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PTPRJ_HUMAN PTPRJ_HUMAN]] Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET (variant MEN2A), KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling.<ref>PMID:9531590</ref> <ref>PMID:9780142</ref> <ref>PMID:10821867</ref> <ref>PMID:11259588</ref> <ref>PMID:12062403</ref> <ref>PMID:12370829</ref> <ref>PMID:12475979</ref> <ref>PMID:12913111</ref> <ref>PMID:14709717</ref> <ref>PMID:16778204</ref> <ref>PMID:16682945</ref> <ref>PMID:18348712</ref> <ref>PMID:19836242</ref> <ref>PMID:19332538</ref> <ref>PMID:19494114</ref> <ref>PMID:18936167</ref> <ref>PMID:21091576</ref> <ref>PMID:19922411</ref> <ref>PMID:21262971</ref>
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[https://www.uniprot.org/uniprot/PTPRJ_HUMAN PTPRJ_HUMAN] Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET (variant MEN2A), KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling.<ref>PMID:9531590</ref> <ref>PMID:9780142</ref> <ref>PMID:10821867</ref> <ref>PMID:11259588</ref> <ref>PMID:12062403</ref> <ref>PMID:12370829</ref> <ref>PMID:12475979</ref> <ref>PMID:12913111</ref> <ref>PMID:14709717</ref> <ref>PMID:16778204</ref> <ref>PMID:16682945</ref> <ref>PMID:18348712</ref> <ref>PMID:19836242</ref> <ref>PMID:19332538</ref> <ref>PMID:19494114</ref> <ref>PMID:18936167</ref> <ref>PMID:21091576</ref> <ref>PMID:19922411</ref> <ref>PMID:21262971</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
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*[[Tyrosine phosphatase|Tyrosine phosphatase]]
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*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Protein-tyrosine-phosphatase]]
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[[Category: Large Structures]]
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[[Category: Hayashi, F]]
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[[Category: Hayashi F]]
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[[Category: Izumi, K]]
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[[Category: Izumi K]]
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[[Category: Structural genomic]]
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[[Category: Yokoyama S]]
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[[Category: Yokoyama, S]]
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[[Category: Yoshida M]]
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[[Category: Yoshida, M]]
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[[Category: Cd148 antigen]]
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[[Category: Density-enhanced phosphatase 1]]
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[[Category: Hptp eta]]
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[[Category: Hydrolase]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Protein-tyrosine phosphatase eta]]
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[[Category: Protein-tyrosine phosphatase receptor type j]]
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[[Category: R-ptp-eta]]
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[[Category: Rsgi]]
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Current revision

Solution structure of the fourth fn3 domain of human receptor-type tyrosine-protein phosphatase eta

PDB ID 2dle

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