3rzu: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry~~ 3rzu is ~~ON HOLD~~

==The Crystal Structure of the Catalytic Domain of AMSH==

~~Authors~~: ~~Davies~~, C.W., ~~Das~~, C.

== 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 guided tour on the structure components use [https://proteopedia.org/fgij/fg.htm?mol=3RZU FirstGlance].

~~Description~~: The ~~Crystal Structure~~ of the ~~Catalytic Domain~~ of ~~AMSH~~

</td></tr><tr id='method'><td class="sblockLbl">[[Empirical_models|Method:]]</td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr>

<tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[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]</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 ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Das C]]

[[Category: Davies CW]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 3rzu is ON HOLD
+==The Crystal Structure of the Catalytic Domain of AMSH==
+<StructureSection load='3rzu' size='340' side='right'caption='[[3rzu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-Authors: Davies, C.W., Das, C.
+== 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>
-Description: The Crystal Structure of the Catalytic Domain of AMSH
+</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]]