6pgv

Structural highlights

Function

JOS2_HUMAN Cleaves 'Lys-63'-linked poly-ubiquitin chains, and with lesser efficiency 'Lys-48'-linked poly-ubiquitin chains (in vitro). May act as a deubiquitinating enzyme.^{[1] [2] [3]}

See Also

• 3D structures of ubiquitin

References

1. ↑ Tzvetkov N, Breuer P. Josephin domain-containing proteins from a variety of species are active de-ubiquitination enzymes. Biol Chem. 2007 Sep;388(9):973-8. PMID:17696782 doi:10.1515/BC.2007.107
2. ↑ Weeks SD, Grasty KC, Hernandez-Cuebas L, Loll PJ. Crystal Structure of a Josephin-Ubiquitin Complex: EVOLUTIONARY RESTRAINTS ON ATAXIN-3 DEUBIQUITINATING ACTIVITY. J Biol Chem. 2011 Feb 11;286(6):4555-65. Epub 2010 Nov 30. PMID:21118805 doi:10.1074/jbc.M110.177360
3. ↑ Seki T, Gong L, Williams AJ, Sakai N, Todi SV, Paulson HL. JosD1, a membrane-targeted deubiquitinating enzyme, is activated by ubiquitination and regulates membrane dynamics, cell motility, and endocytosis. J Biol Chem. 2013 Jun 14;288(24):17145-55. doi: 10.1074/jbc.M113.463406. Epub, 2013 Apr 26. PMID:23625928 doi:http://dx.doi.org/10.1074/jbc.M113.463406