2dkq

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Current revision (18:42, 29 May 2024) (edit) (undo)
 
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==Solution structure of the PTB domain of KIAA1075 protein from human==
==Solution structure of the PTB domain of KIAA1075 protein from human==
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<StructureSection load='2dkq' size='340' side='right'caption='[[2dkq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2dkq' size='340' side='right'caption='[[2dkq]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2dkq]] 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=2DKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DKQ FirstGlance]. <br>
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<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>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TENC1 ([https://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>
<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>
<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>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/TNS2_HUMAN TNS2_HUMAN]] Regulates cell motility and proliferation. May have phosphatase activity. Reduces AKT1 phosphorylation. Lowers AKT1 kinase activity and interferes with AKT1 signaling.<ref>PMID:15817639</ref>
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Inoue, M]]
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[[Category: Inoue M]]
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[[Category: Kigawa, T]]
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[[Category: Kigawa T]]
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[[Category: Koshiba, S]]
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[[Category: Koshiba S]]
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[[Category: Li, H]]
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[[Category: Li H]]
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[[Category: Structural genomic]]
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[[Category: Tochio N]]
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[[Category: Tochio, N]]
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[[Category: Yokoyama S]]
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[[Category: Yokoyama, S]]
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[[Category: Kiaa1075 protein]]
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[[Category: National project on protein structural and functional analyse]]
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[[Category: Nppsfa]]
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[[Category: Ptb domain]]
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[[Category: Rsgi]]
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[[Category: Signaling protein]]
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Current revision

Solution structure of the PTB domain of KIAA1075 protein from human

PDB ID 2dkq

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OCA

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