6efk: Difference between revisions

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<StructureSection load='6efk' size='340' side='right'caption='[[6efk]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='6efk' size='340' side='right'caption='[[6efk]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6efk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EFK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EFK FirstGlance]. <br>
<table><tr><td colspan='2'>[[6efk]] is a 4 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=6EFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EFK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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]] 1.5&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </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=6efk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6efk OCA], [https://pdbe.org/6efk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6efk RCSB], [https://www.ebi.ac.uk/pdbsum/6efk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6efk ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6efk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6efk OCA], [http://pdbe.org/6efk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6efk RCSB], [http://www.ebi.ac.uk/pdbsum/6efk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6efk ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
[[http://www.uniprot.org/uniprot/CHIP_HUMAN CHIP_HUMAN]] Cerebellar ataxia - hypogonadism. The disease is caused by mutations affecting the gene represented in this entry.  
[https://www.uniprot.org/uniprot/CHIP_HUMAN CHIP_HUMAN] Cerebellar ataxia - hypogonadism. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CHIP_HUMAN CHIP_HUMAN]] E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation.<ref>PMID:10330192</ref> <ref>PMID:11146632</ref> <ref>PMID:11557750</ref> <ref>PMID:15466472</ref> <ref>PMID:19103148</ref> <ref>PMID:19567782</ref> <ref>PMID:19713937</ref> <ref>PMID:23990462</ref>
[https://www.uniprot.org/uniprot/CHIP_HUMAN CHIP_HUMAN] E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation.<ref>PMID:10330192</ref> <ref>PMID:11146632</ref> <ref>PMID:11557750</ref> <ref>PMID:15466472</ref> <ref>PMID:19103148</ref> <ref>PMID:19567782</ref> <ref>PMID:19713937</ref> <ref>PMID:23990462</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 6efk" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6efk" style="background-color:#fffaf0;"></div>
==See Also==
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: RING-type E3 ubiquitin transferase]]
[[Category: Basu K]]
[[Category: Basu, K]]
[[Category: Bohn M-F]]
[[Category: Bohn, M F]]
[[Category: Craik CS]]
[[Category: Craik, C S]]
[[Category: Gestwicki JE]]
[[Category: Gestwicki, J E]]
[[Category: Ravalin M]]
[[Category: Ravalin, M]]
[[Category: C-terminus of hsc70-interacting protein]]
[[Category: Chip]]
[[Category: Heat shock protein 70]]
[[Category: Hsp70]]
[[Category: Ligase]]

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