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==Crystal Structure of Human Otubain2 and Ubiquitin Complex==
==Crystal Structure of Human Otubain2 and Ubiquitin Complex==
<StructureSection load='4fjv' size='340' side='right' caption='[[4fjv]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
<StructureSection load='4fjv' size='340' side='right'caption='[[4fjv]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4fjv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FJV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FJV FirstGlance]. <br>
<table><tr><td colspan='2'>[[4fjv]] is a 4 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=4FJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FJV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NEH:ETHANAMINE'>NEH</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NEH:ETHANAMINE'>NEH</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OTUB2, C14orf137, OTB2, OTU2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), UBC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4fjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fjv OCA], [https://pdbe.org/4fjv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fjv RCSB], [https://www.ebi.ac.uk/pdbsum/4fjv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fjv ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr>
<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=4fjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fjv OCA], [http://pdbe.org/4fjv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fjv RCSB], [http://www.ebi.ac.uk/pdbsum/4fjv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fjv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/OTUB2_HUMAN OTUB2_HUMAN]] Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains.<ref>PMID:12704427</ref> <ref>PMID:18954305</ref> [[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref> 
[https://www.uniprot.org/uniprot/OTUB2_HUMAN OTUB2_HUMAN] Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked polyubiquitin chains.<ref>PMID:12704427</ref> <ref>PMID:18954305</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Thioesterase|Thioesterase]]
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
*[[Ubiquitin|Ubiquitin]]
*[[3D structures of ubiquitin|3D structures of ubiquitin]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Ubiquitinyl hydrolase 1]]
[[Category: Large Structures]]
[[Category: Altun, M]]
[[Category: Altun M]]
[[Category: David, Y]]
[[Category: David Y]]
[[Category: Iphofer, A]]
[[Category: Iphofer A]]
[[Category: Kessler, B M]]
[[Category: Kessler BM]]
[[Category: Komsany, A]]
[[Category: Komsany A]]
[[Category: Kramer, H B]]
[[Category: Kramer HB]]
[[Category: Navon, A]]
[[Category: Navon A]]
[[Category: Nicholson, B]]
[[Category: Nicholson B]]
[[Category: Ren, J]]
[[Category: Ren J]]
[[Category: Stuart, D I]]
[[Category: Stuart DI]]
[[Category: Ternette, N]]
[[Category: Ternette N]]
[[Category: Walter, T S]]
[[Category: Walter TS]]
[[Category: Cleavage specificity]]
[[Category: Cysteine protease]]
[[Category: Deubiquitylation]]
[[Category: Hydrolase]]
[[Category: Nedd8]]
[[Category: Otubain]]
[[Category: Ubiquitin]]

Revision as of 19:53, 19 October 2022

Crystal Structure of Human Otubain2 and Ubiquitin Complex

4fjv, resolution 2.05Å

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