4boq

From Proteopedia

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m (Protected "4boq" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4boq| PDB=4boq | SCENE= }}
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===Structure of OTUD2 OTU domain===
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{{ABSTRACT_PUBMED_23827681}}
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The entry 4boq is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/OTU1_HUMAN OTU1_HUMAN]] Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Able to cleave both polyubiquitin and di-ubiquitin.
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Authors: Mevissen, T.E.T., Hospenthal, M.K., Geurink, P.P., Elliott, P.R., Akutsu, M., Arnaudo, N., Ekkebus, R., Kulathu, Y., Wauer, T., El Oualid, F., Freund, S.M.V., Ovaa, H., Komander, D.
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==About this Structure==
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[[4boq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BOQ OCA].
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Description: Structure of OTUD2 OTU domain
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==Reference==
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<ref group="xtra">PMID:023827681</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
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[[Category: Ubiquitinyl hydrolase 1]]
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[[Category: Akutsu, M.]]
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[[Category: Arnaudo, N.]]
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[[Category: Ekkebus, R.]]
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[[Category: Elliott, P R.]]
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[[Category: Freund, S M.V.]]
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[[Category: Geurink, P P.]]
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[[Category: Hospenthal, M K.]]
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[[Category: Komander, D.]]
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[[Category: Kulathu, Y.]]
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[[Category: Mevissen, T E.T.]]
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[[Category: Oualid, F El.]]
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[[Category: Ovaa, H.]]
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[[Category: Wauer, T.]]
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[[Category: Hydrolase]]

Revision as of 04:58, 18 July 2013

Template:STRUCTURE 4boq

Contents

Structure of OTUD2 OTU domain

Template:ABSTRACT PUBMED 23827681

Function

[OTU1_HUMAN] Hydrolase that can remove conjugated ubiquitin from proteins and participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. May act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Able to cleave both polyubiquitin and di-ubiquitin.

About this Structure

4boq is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Mevissen TE, Hospenthal MK, Geurink PP, Elliott PR, Akutsu M, Arnaudo N, Ekkebus R, Kulathu Y, Wauer T, El Oualid F, Freund SM, Ovaa H, Komander D. OTU Deubiquitinases Reveal Mechanisms of Linkage Specificity and Enable Ubiquitin Chain Restriction Analysis. Cell. 2013 Jul 3;154(1):169-84. doi: 10.1016/j.cell.2013.05.046. PMID:23827681 doi:10.1016/j.cell.2013.05.046

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