EC 2.3.2.26 - HECT-type E3 ubiquitin transferase

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IntEnz Enzyme Nomenclature
EC 2.3.2.26

Names

Accepted name:
HECT-type E3 ubiquitin transferase
Other names:
HECT E3 ligase [misleading]
ubiquitin transferase HECT-E3
Systematic name:
S-ubiquitinyl-[HECT-type E3-ubiquitin transferase]-L-cysteine:acceptor protein ubiquitin transferase (isopeptide bond-forming)

Reactions

Comments:

In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond. In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in 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. cf. EC 2.3.2.27, RING-type E3 ubiquitin transferase and EC 2.3.2.31, RBR-type E3 ubiquitin transferase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (131) [show] [UniProt]

References

  1. Maspero, E., Mari, S., Valentini, E., Musacchio, A., Fish, A., Pasqualato, S., Polo, S.
    Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation.
    EMBO Rep. 12: 342-349 (2011). [PMID: 21399620]
  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]

[EC 2.3.2.26 created 2015, modified 2017]