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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==
<StructureSection load='2dle' size='340' side='right'caption='[[2dle]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2dle' size='340' side='right'caption='[[2dle]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2dle]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2DLE FirstGlance]. <br>
<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>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PTPRJ, DEP1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>
<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>
<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>
</table>
</table>
== Function ==
== Function ==
[[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>
[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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Protein-tyrosine-phosphatase]]
[[Category: Hayashi F]]
[[Category: Hayashi, F]]
[[Category: Izumi K]]
[[Category: Izumi, K]]
[[Category: Yokoyama S]]
[[Category: Structural genomic]]
[[Category: Yoshida M]]
[[Category: Yokoyama, S]]
[[Category: Yoshida, M]]
[[Category: Cd148 antigen]]
[[Category: Density-enhanced phosphatase 1]]
[[Category: Hptp eta]]
[[Category: Hydrolase]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Protein-tyrosine phosphatase eta]]
[[Category: Protein-tyrosine phosphatase receptor type j]]
[[Category: R-ptp-eta]]
[[Category: Rsgi]]

Latest revision as of 21:43, 29 May 2024

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

Structural highlights

2dle is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

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.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ de la Fuente-Garcia MA, Nicolas JM, Freed JH, Palou E, Thomas AP, Vilella R, Vives J, Gaya A. CD148 is a membrane protein tyrosine phosphatase present in all hematopoietic lineages and is involved in signal transduction on lymphocytes. Blood. 1998 Apr 15;91(8):2800-9. PMID:9531590
  2. ↑ Tangye SG, Wu J, Aversa G, de Vries JE, Lanier LL, Phillips JH. Negative regulation of human T cell activation by the receptor-type protein tyrosine phosphatase CD148. J Immunol. 1998 Oct 15;161(8):3803-7. PMID:9780142
  3. ↑ Kovalenko M, Denner K, Sandstrom J, Persson C, Gross S, Jandt E, Vilella R, Bohmer F, Ostman A. Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1. J Biol Chem. 2000 May 26;275(21):16219-26. PMID:10821867
  4. ↑ Baker JE, Majeti R, Tangye SG, Weiss A. Protein tyrosine phosphatase CD148-mediated inhibition of T-cell receptor signal transduction is associated with reduced LAT and phospholipase Cgamma1 phosphorylation. Mol Cell Biol. 2001 Apr;21(7):2393-403. PMID:11259588 doi:http://dx.doi.org/10.1128/MCB.21.7.2393-2403.2001
  5. ↑ Persson C, Engstrom U, Mowbray SL, Ostman A. Primary sequence determinants responsible for site-selective dephosphorylation of the PDGF beta-receptor by the receptor-like protein tyrosine phosphatase DEP-1. FEBS Lett. 2002 Apr 24;517(1-3):27-31. PMID:12062403
  6. ↑ Holsinger LJ, Ward K, Duffield B, Zachwieja J, Jallal B. The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn). Oncogene. 2002 Oct 10;21(46):7067-76. PMID:12370829 doi:http://dx.doi.org/10.1038/sj.onc.1205858
  7. ↑ Palka HL, Park M, Tonks NK. Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1. J Biol Chem. 2003 Feb 21;278(8):5728-35. Epub 2002 Dec 9. PMID:12475979 doi:http://dx.doi.org/10.1074/jbc.M210656200
  8. ↑ Lin J, Weiss A. The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling. J Cell Biol. 2003 Aug 18;162(4):673-82. Epub 2003 Aug 11. PMID:12913111 doi:http://dx.doi.org/10.1083/jcb.200303040
  9. ↑ Kellie S, Craggs G, Bird IN, Jones GE. The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation. J Cell Sci. 2004 Feb 1;117(Pt 4):609-18. Epub 2004 Jan 6. PMID:14709717 doi:http://dx.doi.org/10.1242/jcs.00879
  10. ↑ Iervolino A, Iuliano R, Trapasso F, Viglietto G, Melillo RM, Carlomagno F, Santoro M, Fusco A. The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins. Cancer Res. 2006 Jun 15;66(12):6280-7. PMID:16778204 doi:http://dx.doi.org/10.1158/0008-5472.CAN-06-0228
  11. ↑ Balavenkatraman KK, Jandt E, Friedrich K, Kautenburger T, Pool-Zobel BL, Ostman A, Bohmer FD. DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients. Oncogene. 2006 Oct 12;25(47):6319-24. Epub 2006 May 8. PMID:16682945 doi:http://dx.doi.org/10.1038/sj.onc.1209647
  12. ↑ Tsuboi N, Utsunomiya T, Roberts RL, Ito H, Takahashi K, Noda M, Takahashi T. The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase. Biochem J. 2008 Jul 1;413(1):193-200. doi: 10.1042/BJ20071317. PMID:18348712 doi:http://dx.doi.org/10.1042/BJ20071317
  13. ↑ Tarcic G, Boguslavsky SK, Wakim J, Kiuchi T, Liu A, Reinitz F, Nathanson D, Takahashi T, Mischel PS, Ng T, Yarden Y. An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis. Curr Biol. 2009 Nov 17;19(21):1788-98. doi: 10.1016/j.cub.2009.09.048. PMID:19836242 doi:http://dx.doi.org/10.1016/j.cub.2009.09.048
  14. ↑ Sallee JL, Burridge K. Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells. J Biol Chem. 2009 May 29;284(22):14997-5006. doi: 10.1074/jbc.M901901200. Epub, 2009 Mar 30. PMID:19332538 doi:http://dx.doi.org/10.1074/jbc.M901901200
  15. ↑ Sacco F, Tinti M, Palma A, Ferrari E, Nardozza AP, Hooft van Huijsduijnen R, Takahashi T, Castagnoli L, Cesareni G. Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases. J Biol Chem. 2009 Aug 14;284(33):22048-58. doi: 10.1074/jbc.M109.002758. Epub, 2009 Jun 3. PMID:19494114 doi:http://dx.doi.org/10.1074/jbc.M109.002758
  16. ↑ Chabot C, Spring K, Gratton JP, Elchebly M, Royal I. New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival. Mol Cell Biol. 2009 Jan;29(1):241-53. doi: 10.1128/MCB.01374-08. Epub 2008 Oct, 20. PMID:18936167 doi:http://dx.doi.org/10.1128/MCB.01374-08
  17. ↑ Petermann A, Haase D, Wetzel A, Balavenkatraman KK, Tenev T, Guhrs KH, Friedrich S, Nakamura M, Mawrin C, Bohmer FD. Loss of the protein-tyrosine phosphatase DEP-1/PTPRJ drives meningioma cell motility. Brain Pathol. 2011 Jul;21(4):405-18. doi: 10.1111/j.1750-3639.2010.00464.x. Epub , 2010 Dec 27. PMID:21091576 doi:http://dx.doi.org/10.1111/j.1750-3639.2010.00464.x
  18. ↑ Omerovic J, Clague MJ, Prior IA. Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent negative regulators of PKB/Akt activation in Ras-mutated cancer cells. Biochem J. 2010 Jan 27;426(1):65-72. doi: 10.1042/BJ20091413. PMID:19922411 doi:http://dx.doi.org/10.1042/BJ20091413
  19. ↑ Arora D, Stopp S, Bohmer SA, Schons J, Godfrey R, Masson K, Razumovskaya E, Ronnstrand L, Tanzer S, Bauer R, Bohmer FD, Muller JP. Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling. J Biol Chem. 2011 Apr 1;286(13):10918-29. doi: 10.1074/jbc.M110.205021. Epub 2011, Jan 24. PMID:21262971 doi:10.1074/jbc.M110.205021
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