EC 2.3.2.27 - RING-type E3 ubiquitin transferase

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IntEnz Enzyme Nomenclature
EC 2.3.2.27

Names

Accepted name:
RING-type E3 ubiquitin transferase
Other names:
RING E3 ligase [misleading]
ubiquitin transferase RING E3
Systematic name:
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein]-L-lysine ubiquitin transferase (isopeptide bond-forming; RING-type)

Reaction

Comments:

RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the ε-amino group of an L-lysine residue of the acceptor protein. Unlike EC 2.3.2.26, HECT-type E3 ubiquitin transferase, the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32, cullin-RING-type E3 NEDD8 transferase). cf. EC 2.3.2.31, RBR-type E3 ubiquitin transferase. Formerly EC 6.3.2.19 and EC 6.3.2.21.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (1275) [show] [UniProt]

References

  1. Eisele, F., Wolf, D. H.
    Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1.
    FEBS Lett. 582: 4143-4146 (2008). [PMID: 19041308]
  2. Metzger, M. B., Hristova, V. A., Weissman, A. M.
    HECT and RING finger families of E3 ubiquitin ligases at a glance.
    J. Cell. Sci. 125: 531-537 (2012). [PMID: 22389392]
  3. Plechanovova, A., Jaffray, E. G., Tatham, M. H., Naismith, J. H., Hay, R. T.
    Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis.
    Nature 489: 115-120 (2012). [PMID: 22842904]
  4. Pruneda, J. N., Littlefield, P. J., Soss, S. E., Nordquist, K. A., Chazin, W. J., Brzovic, P. S., Klevit, R. E.
    Structure of an E3:E2~Ub complex reveals an allosteric mechanism shared among RING/U-box ligases.
    Mol. Cell 47: 933-942 (2012). [PMID: 22885007]
  5. Metzger, M. B., Pruneda, J. N., Klevit, R. E., Weissman, A. M.
    RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination.
    Biochim. Biophys. Acta 1843: 47-60 (2014). [PMID: 23747565]

[EC 2.3.2.27 created 2015, modified 2017]