Deubiquitination

Eletr ZM, Wilkinson KD. Regulation of proteolysis by human deubiquitinating enzymes. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 2014 Jan;1843(1):114–28. doi: 10.1016/j.bbamcr.2013.06.027.; Lee J, Baek K, Soetandyo N, Ye Y. Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells. Nature Communications. 2013 Mar 05;4(1):1568. doi: 10.1038/ncomms2532.; Cotto-Rios XM, Békés M, Chapman J, Ueberheide B, Huang TT. Deubiquitinases as a signaling target of oxidative stress. Cell Rep. 2012 Dec 27;2(6):1475–84. PMID: 23219552; PMCID: PMC3534866.; Burrows JF, Johnston JA. Regulation of cellular responses by deubiquitinating enzymes: an update. Front Biosci (Landmark Ed). 2012 Jan 01;17(3):1184–200. doi: 10.2741/3980. PMID: 22201797.; Kimura Y, Tanaka K. Regulatory mechanisms involved in the control of ubiquitin homeostasis. Journal of Biochemistry. 2010 Apr 23;147(6):793–8. doi: 10.1093/jb/mvq044.; Katz EJ, Isasa M, Crosas B. A new map to understand deubiquitination. Biochem Soc Trans. 2010 Feb;38(Pt 1):21–8. doi: 10.1042/bst0380021. PMID: 20074029.; Reyes-Turcu FE, Wilkinson KD. Polyubiquitin binding and disassembly by deubiquitinating enzymes. Chem Rev. 2009 Apr;109(4):1495–508. PMID: 19243136; PMCID: PMC2734106.; Nijman SM, Luna-Vargas MP, Velds A, Brummelkamp TR, Dirac AM, Sixma TK, Bernards R. A genomic and functional inventory of deubiquitinating enzymes. Cell. 2005 Dec 02;123(5):773–86. doi: 10.1016/j.cell.2005.11.007. PMID: 16325574.; Amerik AY, Hochstrasser M. Mechanism and function of deubiquitinating enzymes. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 2004 Nov;1695(1-3):189–207. doi: 10.1016/j.bbamcr.2004.10.003.; Kim JH, Park KC, Chung SS, Bang O, Chung CH. Deubiquitinating enzymes as cellular regulators. J Biochem. 2003 Jul;134(1):9–18. doi: 10.1093/jb/mvg107. PMID: 12944365.; Lam YA, Xu W, DeMartino GN, Cohen RE. Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature. 1997 Feb 20;385(6618):737–40. doi: 10.1038/385737a0. PMID: 9034192.; Haas AL, Bright PM. The dynamics of ubiquitin pools within cultured human lung fibroblasts. Journal of Biological Chemistry. 1987 Jan;262(1):345–51. doi: 10.1016/s0021-9258(19)75933-x.

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:

L-lysinium(1+)

Formula: C6H15N2O2 (147.113347)

CAS ID: 56-87-1



Enzyme

EC Number name full name note
3.4.19.-
2.3.2.27 RING-type E3 ubiquitin transferase [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming; RING-type)
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
2.7.11.25 mitogen-activated protein kinase kinase kinase ATP:protein phosphotransferase (MAPKKKK-activated)
2.7.7.7 DNA-directed DNA polymerase deoxynucleoside-triphosphate:DNA deoxynucleotidyltransferase (DNA-directed)
3.4.19.12 ubiquitinyl hydrolase 1
4.2.99.18 DNA-(apurinic or apyrimidinic site) lyase DNA-(apurinic or apyrimidinic site) 5'-phosphomonoester-lyase


Proteins

Protein ID name full name