4lad: Difference between revisions

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<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=4lad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lad OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lad RCSB], [http://www.ebi.ac.uk/pdbsum/4lad PDBsum]</span></td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/UB2G2_HUMAN UB2G2_HUMAN]] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Involved in endoplasmic reticulum-associated degradation (ERAD).<ref>PMID:20061386</ref> <ref>PMID:22607976</ref> [[http://www.uniprot.org/uniprot/AMFR_HUMAN AMFR_HUMAN]] E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis as a receptor for the GPI/autocrine motility factor.<ref>PMID:10456327</ref> <ref>PMID:11724934</ref> <ref>PMID:16168377</ref> <ref>PMID:19103148</ref>

== Publication Abstract from PubMed ==

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@@ Line 9: / Line 9: @@
 <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=4lad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lad OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lad RCSB], [http://www.ebi.ac.uk/pdbsum/4lad PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/UB2G2_HUMAN UB2G2_HUMAN]] Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Involved in endoplasmic reticulum-associated degradation (ERAD).<ref>PMID:20061386</ref> <ref>PMID:22607976</ref>  [[http://www.uniprot.org/uniprot/AMFR_HUMAN AMFR_HUMAN]] E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis as a receptor for the GPI/autocrine motility factor.<ref>PMID:10456327</ref> <ref>PMID:11724934</ref> <ref>PMID:16168377</ref> <ref>PMID:19103148</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==