8f15

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:50, 9 October 2024) (edit) (undo)
 
Line 8: Line 8:
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8f15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f15 OCA], [https://pdbe.org/8f15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f15 RCSB], [https://www.ebi.ac.uk/pdbsum/8f15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f15 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=8f15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8f15 OCA], [https://pdbe.org/8f15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8f15 RCSB], [https://www.ebi.ac.uk/pdbsum/8f15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8f15 ProSAT]</span></td></tr>
</table>
</table>
-
== Disease ==
+
 
-
[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.
+
==See Also==
-
== Function ==
+
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
-
[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>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Structure of the STUB1 TPR domain in complex with H202, an all-D Helicon Polypeptide

PDB ID 8f15

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8f15"
Personal tools