2dkq: Difference between revisions

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[[Image:2dkq.png|left|200px]]


{{STRUCTURE_2dkq|  PDB=2dkq  |  SCENE=  }}
==Solution structure of the PTB domain of KIAA1075 protein from human==
 
<StructureSection load='2dkq' size='340' side='right'caption='[[2dkq]]' scene=''>
===Solution structure of the PTB domain of KIAA1075 protein from human===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2dkq]] 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=2DKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DKQ FirstGlance]. <br>
 
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2dkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dkq OCA], [https://pdbe.org/2dkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dkq RCSB], [https://www.ebi.ac.uk/pdbsum/2dkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dkq ProSAT], [https://www.topsan.org/Proteins/RSGI/2dkq TOPSAN]</span></td></tr>
[[2dkq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DKQ OCA].  
</table>
== Function ==
[https://www.uniprot.org/uniprot/TENS2_HUMAN TENS2_HUMAN] Tyrosine-protein phosphatase which regulates cell motility, proliferation and muscle-response to insulin (PubMed:15817639, PubMed:23401856). Phosphatase activity is mediated by binding to phosphatidylinositol-3,4,5-triphosphate (PtdIns(3,4,5)P3) via the SH2 domain (PubMed:30092354). In muscles and under catabolic conditions, dephosphorylates IRS1 leading to its degradation and muscle atrophy (PubMed:23401856, PubMed:30092354). Negatively regulates PI3K-AKT pathway activation (PubMed:15817639, PubMed:23401856, PubMed:30092354). Dephosphorylates nephrin NPHS1 in podocytes which regulates activity of the mTORC1 complex (PubMed:28955049). Under normal glucose conditions, NPHS1 outcompetes IRS1 for binding to phosphatidylinositol 3-kinase (PI3K) which balances mTORC1 activity but high glucose conditions lead to up-regulation of TNS2, increased NPHS1 dephosphorylation and activation of mTORC1, contributing to podocyte hypertrophy and proteinuria (PubMed:28955049). Required for correct podocyte morphology, podocyte-glomerular basement membrane interaction and integrity of the glomerular filtration barrier (By similarity). Enhances RHOA activation in the presence of DLC1 (PubMed:26427649). Plays a role in promoting DLC1-dependent remodeling of the extracellular matrix (PubMed:20069572).[UniProtKB:Q8CGB6]<ref>PMID:15817639</ref> <ref>PMID:20069572</ref> <ref>PMID:23401856</ref> <ref>PMID:26427649</ref> <ref>PMID:28955049</ref> <ref>PMID:30092354</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dk/2dkq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2dkq ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Inoue, M.]]
[[Category: Large Structures]]
[[Category: Kigawa, T.]]
[[Category: Inoue M]]
[[Category: Koshiba, S.]]
[[Category: Kigawa T]]
[[Category: Li, H.]]
[[Category: Koshiba S]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Li H]]
[[Category: Tochio, N.]]
[[Category: Tochio N]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama S]]
[[Category: Kiaa1075 protein]]
[[Category: National project on protein structural and functional analyse]]
[[Category: Nppsfa]]
[[Category: Ptb domain]]
[[Category: Riken structural genomics/proteomics initiative]]
[[Category: Rsgi]]
[[Category: Signaling protein]]
[[Category: Structural genomic]]

Latest revision as of 21:42, 29 May 2024

Solution structure of the PTB domain of KIAA1075 protein from humanSolution structure of the PTB domain of KIAA1075 protein from human

Structural highlights

2dkq 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

TENS2_HUMAN Tyrosine-protein phosphatase which regulates cell motility, proliferation and muscle-response to insulin (PubMed:15817639, PubMed:23401856). Phosphatase activity is mediated by binding to phosphatidylinositol-3,4,5-triphosphate (PtdIns(3,4,5)P3) via the SH2 domain (PubMed:30092354). In muscles and under catabolic conditions, dephosphorylates IRS1 leading to its degradation and muscle atrophy (PubMed:23401856, PubMed:30092354). Negatively regulates PI3K-AKT pathway activation (PubMed:15817639, PubMed:23401856, PubMed:30092354). Dephosphorylates nephrin NPHS1 in podocytes which regulates activity of the mTORC1 complex (PubMed:28955049). Under normal glucose conditions, NPHS1 outcompetes IRS1 for binding to phosphatidylinositol 3-kinase (PI3K) which balances mTORC1 activity but high glucose conditions lead to up-regulation of TNS2, increased NPHS1 dephosphorylation and activation of mTORC1, contributing to podocyte hypertrophy and proteinuria (PubMed:28955049). Required for correct podocyte morphology, podocyte-glomerular basement membrane interaction and integrity of the glomerular filtration barrier (By similarity). Enhances RHOA activation in the presence of DLC1 (PubMed:26427649). Plays a role in promoting DLC1-dependent remodeling of the extracellular matrix (PubMed:20069572).[UniProtKB:Q8CGB6][1] [2] [3] [4] [5] [6]

Evolutionary Conservation

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

References

  1. ↑ Hafizi S, Ibraimi F, Dahlback B. C1-TEN is a negative regulator of the Akt/PKB signal transduction pathway and inhibits cell survival, proliferation, and migration. FASEB J. 2005 Jun;19(8):971-3. Epub 2005 Apr 7. PMID:15817639 doi:http://dx.doi.org/10.1096/fj.04-2532fje
  2. ↑ Clark K, Howe JD, Pullar CE, Green JA, Artym VV, Yamada KM, Critchley DR. Tensin 2 modulates cell contractility in 3D collagen gels through the RhoGAP DLC1. J Cell Biochem. 2010 Mar 1;109(4):808-17. PMID:20069572 doi:10.1002/jcb.22460
  3. ↑ Koh A, Lee MN, Yang YR, Jeong H, Ghim J, Noh J, Kim J, Ryu D, Park S, Song P, Koo SH, Leslie NR, Berggren PO, Choi JH, Suh PG, Ryu SH. C1-Ten is a protein tyrosine phosphatase of insulin receptor substrate 1 (IRS-1), regulating IRS-1 stability and muscle atrophy. Mol Cell Biol. 2013 Apr;33(8):1608-20. PMID:23401856 doi:10.1128/MCB.01447-12
  4. ↑ Shih YP, Sun P, Wang A, Lo SH. Tensin1 positively regulates RhoA activity through its interaction with DLC1. Biochim Biophys Acta. 2015 Dec;1853(12):3258-65. PMID:26427649 doi:10.1016/j.bbamcr.2015.09.028
  5. ↑ Lee J, Koh A, Jeong H, Kim E, Ha TS, Saleem MA, Ryu SH. C1-Ten is a PTPase of nephrin, regulating podocyte hypertrophy through mTORC1 activation. Sci Rep. 2017 Sep 27;7(1):12346. PMID:28955049 doi:10.1038/s41598-017-12382-8
  6. ↑ Kim E, Kim DH, Singaram I, Jeong H, Koh A, Lee J, Cho W, Ryu SH. Cellular phosphatase activity of C1-Ten/Tensin2 is controlled by Phosphatidylinositol-3,4,5-triphosphate binding through the C1-Ten/Tensin2 SH2 domain. Cell Signal. 2018 Nov;51:130-138. PMID:30092354 doi:10.1016/j.cellsig.2018.07.009
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