E3 ubiquitin ligases ubiquitinate target proteins

Dove KK, Stieglitz B, Duncan ED, Rittinger K, Klevit RE. Molecular insights into RBR E3 ligase ubiquitin transfer mechanisms. EMBO Reports. 2016 Jun 16;17(8):1221–35. doi: 10.15252/embr.201642641.; Nakagawa T, Nakayama K. Protein monoubiquitylation: targets and diverse functions. Genes Cells. 2015 Jul;20(7):543–62. PMID: 26085183; PMCID: PMC4744734.; Berndsen CE, Wolberger C. New insights into ubiquitin E3 ligase mechanism. Nature Structural & Molecular Biology. 2014 Apr 04;21(4):301–7. doi: 10.1038/nsmb.2780.; Metzger MB, Pruneda JN, Klevit RE, Weissman AM. RING-type E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 2014 Jan;1843(1):47–60. doi: 10.1016/j.bbamcr.2013.05.026.; Genschik P, Sumara I, Lechner E. The emerging family of CULLIN3-RING ubiquitin ligases (CRL3s): cellular functions and disease implications. EMBO J. 2013 Aug 28;32(17):2307–20. PMID: 23912815; PMCID: PMC3770339.; McDowell GS, Philpott A. Non-canonical ubiquitylation: Mechanisms and consequences. The International Journal of Biochemistry & Cell Biology. 2013 Aug;45(8):1833–42. doi: 10.1016/j.biocel.2013.05.026.; Skaar JR, Pagan JK, Pagano M. Mechanisms and function of substrate recruitment by F-box proteins. Nature Reviews Molecular Cell Biology. 2013 May 09;14(6):369–81. doi: 10.1038/nrm3582.; Lee EK, Diehl JA. SCFs in the new millennium. Oncogene. 2014 Apr 17;33(16):2011–8. doi: 10.1038/onc.2013.144. PMID: 23624913.; Metzger MB, Hristova VA, Weissman AM. HECT and RING finger families of E3 ubiquitin ligases at a glance. J Cell Sci. 2012 Feb 01;125(Pt 3):531–7. PMID: 22389392; PMCID: PMC3381717.; Komander D. The emerging complexity of protein ubiquitination. Biochem Soc Trans. 2009 Oct;37(Pt 5):937–53. doi: 10.1042/bst0370937. PMID: 19754430.; Deshaies RJ, Joazeiro CA. RING domain E3 ubiquitin ligases. Annu Rev Biochem. 2009;78():399–434. doi: 10.1146/annurev.biochem.78.101807.093809. PMID: 19489725.; Rotin D, Kumar S. Physiological functions of the HECT family of ubiquitin ligases. Nature Reviews Molecular Cell Biology. 2009 May 13;10(6):398–409. doi: 10.1038/nrm2690.; Lee J, Zhou P. DCAFs, the missing link of the CUL4-DDB1 ubiquitin ligase. Mol Cell. 2007 Jun 22;26(6):775–80. doi: 10.1016/j.molcel.2007.06.001. PMID: 17588513.

Metabolites



Enzyme

EC Number name full name note
3.6.4.-
2.3.2.23 E2 ubiquitin-conjugating enzyme S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine:[E2 ubiquitin-conjugating enzyme] ubiquitinyl transferase
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)
2.3.2.31 RBR-type E3 ubiquitin transferase [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:acceptor protein ubiquitin transferase (isopeptide bond-forming; RBR-type)
2.3.2.36 RING-type E3 ubiquitin transferase (cysteine targeting) [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (thioester bond-froming; RING-type)
2.7.11.1 non-specific serine/threonine protein kinase ATP:protein phosphotransferase (non-specific)


Proteins

Protein ID name full name