View source for 5vbd


==Crystal structure of a putative UBL domain of USP9X==
<StructureSection load='5vbd' size='340' side='right'caption='[[5vbd]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vbd]] is a 1 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=5VBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VBD 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=5vbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vbd OCA], [https://pdbe.org/5vbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vbd RCSB], [https://www.ebi.ac.uk/pdbsum/5vbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vbd ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/USP9X_HUMAN USP9X_HUMAN] X-linked non-syndromic intellectual disability. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/USP9X_HUMAN USP9X_HUMAN] Deubiquitinase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. May therefore play an important regulatory role at the level of protein turnover by preventing degradation of proteins through the removal of conjugated ubiquitin. Specifically hydrolyzes 'Lys-48'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitins chains. Essential component of TGF-beta/BMP signaling cascade. Specifically deubiquitinates monoubiquitinated SMAD4, opposing the activity of E3 ubiquitin-protein ligase TRIM33. Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions (PubMed:25944111). Regulates chromosome alignment and segregation in mitosis by regulating the localization of BIRC5/survivin to mitotic centromeres. Involved in axonal growth and neuronal cell migration (PubMed:16322459, PubMed:18254724, PubMed:19135894, PubMed:24607389).<ref>PMID:16322459</ref> <ref>PMID:18254724</ref> <ref>PMID:19135894</ref> <ref>PMID:24607389</ref> <ref>PMID:25944111</ref> 

==See Also==
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arrowsmith CH]]
[[Category: Bountra C]]
[[Category: Chern Y]]
[[Category: Dong A]]
[[Category: Edwards AM]]
[[Category: Hou F]]
[[Category: Li Y]]
[[Category: Tempel W]]
[[Category: Tong Y]]