| Post Translational Modifications | Dephosphorylated by DUSP22 at Ser-1694 and Tyr-1697, leading to subsequent ubiquitination and proteasomal degradation. 'Lys-48'-linked ubiquitinated at Lys-94, Lys-779 and Lys-1599 following DUSP22-mediated dephosphorylation of Ser-1694 and Tyr-1697 which promotes UBR2 interaction with the SCF(FBW1A) E3 ubiquitin-protein ligase complex. |
| Function | E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues (N-degrons) that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Recognizes both type-1 and type-2 N-degrons, containing positively charged amino acids (Arg, Lys and His) and bulky and hydrophobic amino acids, respectively. Does not ubiquitinate proteins that are acetylated at the N-terminus. In contrast, it strongly binds methylated N-degrons. Plays a critical role in chromatin inactivation and chromosome-wide transcriptional silencing during meiosis via ubiquitination of histone H2A. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth. Required for spermatogenesis, promotes, with Tex19.1, SPO11-dependent recombination foci to accumulate and drive robust homologous chromosome synapsis. Polyubiquitinates LINE-1 retrotransposon encoded, LIRE1, which induces degradation, inhibiting LINE-1 retrotransposon mobilization. Catalyzes ubiquitination and degradation of the N-terminal part of NLRP1 following NLRP1 activation by pathogens and other damage-associated signals: ubiquitination promotes degradation of the N-terminal part and subsequent release of the cleaved C-terminal part of NLRP1, which polymerizes and forms the NLRP1 inflammasome followed by host cell pyroptosis. Plays a role in T-cell receptor signaling by inducing 'Lys-63'-linked ubiquitination of lymphocyte cell-specific kinase LCK. This activity is regulated by DUSP22, which induces 'Lys-48'-linked ubiquitination of UBR2, leading to its proteasomal degradation by SCF E3 ubiquitin-protein ligase complex. |
| Protein Name | E3 Ubiquitin-Protein Ligase Ubr2N-Recognin-2Ubiquitin-Protein Ligase E3-Alpha-2Ubiquitin-Protein Ligase E3-Alpha-Ii |
| Database Links | Reactome: R-HSA-983168 |
| Cellular Localisation | NucleusChromosomeAssociated With Chromatin During Meiosis |
| Alternative Antibody Names | Anti-E3 Ubiquitin-Protein Ligase Ubr2 antibodyAnti-N-Recognin-2 antibodyAnti-Ubiquitin-Protein Ligase E3-Alpha-2 antibodyAnti-Ubiquitin-Protein Ligase E3-Alpha-Ii antibodyAnti-UBR2 antibodyAnti-C6orf133 antibodyAnti-KIAA0349 antibody |
Information sourced from Uniprot.org
