View source for 3rzu


==The Crystal Structure of the Catalytic Domain of AMSH==
<StructureSection load='3rzu' size='340' side='right'caption='[[3rzu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3rzu]] is a 7 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=3RZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RZU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=3rzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rzu OCA], [https://pdbe.org/3rzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rzu RCSB], [https://www.ebi.ac.uk/pdbsum/3rzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rzu ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/STABP_HUMAN STABP_HUMAN] Microcephaly-capillary malformation syndrome. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/STABP_HUMAN STABP_HUMAN] Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Plays a role in signal transduction for cell growth and MYC induction mediated by IL-2 and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling by antagonizing the inhibitory action of SMAD6 and SMAD7. Has a key role in regulation of cell surface receptor-mediated endocytosis and ubiquitin-dependent sorting of receptors to lysosomes. Endosomal localization of STAMBP is required for efficient EGFR degradation but not for its internalization (By similarity). Involved in the negative regulation of PI3K-AKT-mTOR and RAS-MAP signaling pathways.<ref>PMID:10383417</ref> <ref>PMID:11483516</ref> <ref>PMID:15314065</ref> <ref>PMID:17261583</ref> <ref>PMID:23542699</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Das C]]
[[Category: Davies CW]]