2xa6
From Proteopedia
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| - | == | + | |
| - | <StructureSection load='2xa6' size='340' side='right' caption='[[2xa6 | + | ==Structural basis for homodimerization of the Src-associated during mitosis, 68 kD protein (Sam68) Qua1 domain== |
| + | <StructureSection load='2xa6' size='340' side='right'caption='[[2xa6]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2xa6]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2xa6]] is a 2 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=2XA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XA6 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </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=2xa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xa6 OCA], [https://pdbe.org/2xa6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xa6 RCSB], [https://www.ebi.ac.uk/pdbsum/2xa6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xa6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KHDR1_HUMAN KHDR1_HUMAN] Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export.<ref>PMID:9013542</ref> <ref>PMID:9045636</ref> <ref>PMID:11585385</ref> <ref>PMID:1374686</ref> [UniProtKB:Q60749][UniProtKB:Q8UUW7] Isoform 3, which is expressed in growth-arrested cells only, inhibits S phase.<ref>PMID:9013542</ref> <ref>PMID:9045636</ref> <ref>PMID:11585385</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xa/2xa6_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xa/2xa6_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | + | </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=2xa6 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 2xa6" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Brack-Werner | + | [[Category: Large Structures]] |
| - | [[Category: Kateb | + | [[Category: Brack-Werner R]] |
| - | [[Category: Madl | + | [[Category: Kateb F]] |
| - | [[Category: Meyer | + | [[Category: Madl T]] |
| - | [[Category: Sattler | + | [[Category: Meyer NH]] |
| - | [[Category: Tripsianes | + | [[Category: Sattler M]] |
| - | [[Category: Vincendeaux | + | [[Category: Tripsianes K]] |
| - | + | [[Category: Vincendeaux M]] | |
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Current revision
Structural basis for homodimerization of the Src-associated during mitosis, 68 kD protein (Sam68) Qua1 domain
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