Ovarian tumor domain proteases

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 03;154(1):169–84. PMID: 23827681; PMCID: PMC3705208.; Licchesi JDF, Mieszczanek J, Mevissen TET, Rutherford TJ, Akutsu M, Virdee S, Oualid FE, Chin JW, Ovaa H, Bienz M, Komander D. An ankyrin-repeat ubiquitin-binding domain determines TRABID's specificity for atypical ubiquitin chains. Nature Structural & Molecular Biology. 2011 Dec 11;19(1):62–71. doi: 10.1038/nsmb.2169.; Nakada S, Tai I, Panier S, Al-Hakim A, Iemura S, Juang YC, O'Donnell L, Kumakubo A, Munro M, Sicheri F, Gingras AC, Natsume T, Suda T, Durocher D. Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1. Nature. 2010 Aug 19;466(7309):941–6. doi: 10.1038/nature09297. PMID: 20725033.; Bremm A, Freund SMV, Komander D. Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne. Nature Structural & Molecular Biology. 2010 Jul 11;17(8):939–47. doi: 10.1038/nsmb.1873.; Komander D, Clague MJ, Urbé S. Breaking the chains: structure and function of the deubiquitinases. Nature Reviews Molecular Cell Biology. 2009 Aug;10(8):550–63. doi: 10.1038/nrm2731.; Wang T, Yin L, Cooper EM, Lai M, Dickey S, Pickart CM, Fushman D, Wilkinson KD, Cohen RE, Wolberger C. Evidence for Bidentate Substrate Binding as the Basis for the K48 Linkage Specificity of Otubain 1. Journal of Molecular Biology. 2009 Mar;386(4):1011–23. doi: 10.1016/j.jmb.2008.12.085.; Edelmann MJ, Iphöfer A, Akutsu M, Altun M, di Gleria K, Kramer HB, Fiebiger E, Dhe-Paganon S, Kessler BM. Structural basis and specificity of human otubain 1-mediated deubiquitination. Biochem J. 2009 Mar 01;418(2):379–90. doi: 10.1042/bj20081318. PMID: 18954305.; Messick TE, Russell NS, Iwata AJ, Sarachan KL, Shiekhattar R, Shanks JR, Reyes-Turcu FE, Wilkinson KD, Marmorstein R. Structural Basis for Ubiquitin Recognition by the Otu1 Ovarian Tumor Domain Protein. Journal of Biological Chemistry. 2008 Apr;283(16):11038–49. doi: 10.1074/jbc.m704398200.; Lin S, Chung JY, Lamothe B, Rajashankar K, Lu M, Lo Y, Lam AY, Darnay BG, Wu H. Molecular Basis for the Unique Deubiquitinating Activity of the NF-?B Inhibitor A20. Journal of Molecular Biology. 2008 Feb;376(2):526–40. doi: 10.1016/j.jmb.2007.11.092.; Komander D, Barford D. Structure of the A20 OTU domain and mechanistic insights into deubiquitination. Biochem J. 2008 Jan 01;409(1):77–85. doi: 10.1042/bj20071399. PMID: 17961127.; Wertz IE, O'Rourke KM, Zhou H, Eby M, Aravind L, Seshagiri S, Wu P, Wiesmann C, Baker R, Boone DL, Ma A, Koonin EV, Dixit VM. De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling. Nature. 2004 Aug 05;430(7000):694–9. doi: 10.1038/nature02794. PMID: 15258597.

Metabolites

H2O

Formula: H2O (18.0105642)

CAS ID: 7732-18-5

ATP(4-)

Formula: C10H12N5O13P3 (502.9644492)

CAS ID:

ADP(3-)

Formula: C10H12N5O10P2 (424.0059412)

CAS ID:



Enzyme

EC Number name full name note
2.3.2.-
2.7.10.2 non-specific protein-tyrosine kinase ATP:[protein]-L-tyrosine O-phosphotransferase (non-specific)
2.7.11.1 non-specific serine/threonine protein kinase ATP:protein phosphotransferase (non-specific)
2.7.11.22 cyclin-dependent kinase ATP:cyclin phosphotransferase
2.7.11.23 [RNA-polymerase]-subunit kinase ATP:[DNA-directed RNA polymerase] phosphotransferase
3.1.3.16 protein-serine/threonine phosphatase protein-serine/threonine-phosphate phosphohydrolase
3.1.3.48 protein-tyrosine-phosphatase protein-tyrosine-phosphate phosphohydrolase
3.1.3.67 phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase 1-phosphatidyl-1D-myo-inositol-3,4,5-trisphosphate 3-phosphohydrolase
3.4.19.12 ubiquitinyl hydrolase 1
3.6.4.6 vesicle-fusing ATPase ATP phosphohydrolase (vesicle-fusing)


Proteins

Protein ID name full name