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E3 ubiquitin-protein ligase KCMF1

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme and then transfers it to targeted substrates, promoting their degradation by the proteasome^1,2,3,4,5. Together with UBR4, component of the N-end rule pathway: ubiquitinates proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their degradation^6,7. Does not ubiquitinate proteins that are acetylated at the N-terminus⁸. Together with UBR4, part of a protein quality control pathway that catalyzes ubiquitination and degradation of proteins that have been oxidized in response to reactive oxygen species (ROS): recognizes proteins with an Arg-CysO3(H) degron at the N-terminus, and mediates assembly of heterotypic 'Lys-63'-/'Lys-27'-linked branched ubiquitin chains on oxidized proteins, leading to their degradation by autophagy⁹. Catalytic component of the SIFI complex, a multiprotein complex required to inhibit the mitochondrial stress response after a specific stress event has been resolved: ubiquitinates and degrades (1) components of the HRI-mediated signaling of the integrated stress response, such as DELE1 and EIF2AK1/HRI, as well as (2) unimported mitochondrial precursors¹⁰. Within the SIFI complex, UBR4 initiates ubiquitin chain that are further elongated or branched by KCMF1¹¹.

AlphaFold DB , UniProt , Accession Q9P0J7, Species HUMAN (Homo sapiens, Human), Gene KCMF1, Length 381 aa.