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==Structure of the PUB domain from Ubiquitin Regulatory X domain protein 1 (UBXD1)==
<StructureSection load='6sap' size='340' side='right'caption='[[6sap]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6sap]] 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=6SAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SAP FirstGlance]. <br>
</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=6sap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sap OCA], [https://pdbe.org/6sap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sap RCSB], [https://www.ebi.ac.uk/pdbsum/6sap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sap ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UBXN6_HUMAN UBXN6_HUMAN] May negatively regulate the ATPase activity of VCP, an ATP-driven segregase that associates with different cofactors to control a wide variety of cellular processes (PubMed:26475856). As a cofactor of VCP, it may play a role in the transport of CAV1 to lysosomes for degradation (PubMed:21822278, PubMed:23335559). It may also play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins (PubMed:19275885). Together with VCP and other cofactors, it may play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes (PubMed:27753622).<ref>PMID:19275885</ref> <ref>PMID:21822278</ref> <ref>PMID:23335559</ref> <ref>PMID:26475856</ref> <ref>PMID:27753622</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
AAA+ ATPase p97/valosin-containing protein (VCP)/Cdc48 is a key player in various cellular stress responses in which it unfolds ubiquitinated proteins to facilitate their degradation by the proteasome. P97 works in different cellular processes using alternative sets of cofactors and is implicated in multiple degenerative diseases. Ubiquitin regulatory X domain protein 1 (UBXD1) has been linked to pathogenesis and is unique amongst p97 cofactors because it interacts with both termini of p97. Its N-domain binds to the N-domain and N/D1 interface of p97 and regulates its ATPase activity. The PUB (peptide:N-glycanase and UBA or UBX-containing proteins) domain binds the p97 C-terminus, but how it controls p97 function is still unknown. Here we present the NMR structure of UBXD1-PUB together with binding studies, mutational analysis, and a model of UBXD1-PUB in complex with the p97 C-terminus. While the binding pocket is conserved among PUB domains, UBXD1-PUB features a unique loop and turn regions suggesting a role in coordinating interaction with downstream regulators and substrate processing.

Structure of the PUB Domain from Ubiquitin Regulatory X Domain Protein 1 (UBXD1) and Its Interaction with the p97 AAA+ ATPase.,Blueggel M, van den Boom J, Meyer H, Bayer P, Beuck C Biomolecules. 2019 Dec 14;9(12). pii: biom9120876. doi: 10.3390/biom9120876. PMID:31847414<ref>PMID:31847414</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6sap" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bayer P]]
[[Category: Beuck C]]
[[Category: Blueggel M]]