1qym: Difference between revisions

No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='1qym' size='340' side='right'caption='[[1qym]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1qym' size='340' side='right'caption='[[1qym]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qym]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1QYM FirstGlance]. <br>
<table><tr><td colspan='2'>[[1qym]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QYM FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PSMD10 ([http://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">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1qym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qym OCA], [http://pdbe.org/1qym PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qym RCSB], [http://www.ebi.ac.uk/pdbsum/1qym PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qym ProSAT]</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=1qym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qym OCA], [https://pdbe.org/1qym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qym RCSB], [https://www.ebi.ac.uk/pdbsum/1qym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qym ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PSD10_HUMAN PSD10_HUMAN]] Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pahway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.<ref>PMID:10613832</ref> <ref>PMID:11900540</ref> <ref>PMID:11779854</ref> <ref>PMID:16023600</ref> <ref>PMID:18040287</ref> <ref>PMID:19490896</ref> <ref>PMID:19729910</ref> <ref>PMID:20628200</ref>  Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export.<ref>PMID:10613832</ref> <ref>PMID:11900540</ref> <ref>PMID:11779854</ref> <ref>PMID:16023600</ref> <ref>PMID:18040287</ref> <ref>PMID:19490896</ref> <ref>PMID:19729910</ref> <ref>PMID:20628200</ref>
[https://www.uniprot.org/uniprot/PSD10_HUMAN PSD10_HUMAN] Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pahway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.<ref>PMID:10613832</ref> <ref>PMID:11900540</ref> <ref>PMID:11779854</ref> <ref>PMID:16023600</ref> <ref>PMID:18040287</ref> <ref>PMID:19490896</ref> <ref>PMID:19729910</ref> <ref>PMID:20628200</ref>  Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export.<ref>PMID:10613832</ref> <ref>PMID:11900540</ref> <ref>PMID:11779854</ref> <ref>PMID:16023600</ref> <ref>PMID:18040287</ref> <ref>PMID:19490896</ref> <ref>PMID:19729910</ref> <ref>PMID:20628200</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 27: Line 27:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Buessow, K]]
[[Category: Buessow K]]
[[Category: Delbrueck, H]]
[[Category: Delbrueck H]]
[[Category: Heinemann, U]]
[[Category: Heinemann U]]
[[Category: Manjasetty, B A]]
[[Category: Manjasetty BA]]
[[Category: Niesen, F]]
[[Category: Niesen F]]
[[Category: Quedenau, C]]
[[Category: Quedenau C]]
[[Category: Sievert, V]]
[[Category: Sievert V]]
[[Category: Ankyrin repeat]]
[[Category: Oncoprotein]]
[[Category: Structural genomic]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA