ZNRF2
Domain
The RING-type zinc finger domain is required for E3 ligase activity.
Function
E3 ubiquitin-protein ligase that plays a role in the establishment and maintenance of neuronal transmission and plasticity. Ubiquitinates the Na(+)/K(+) ATPase alpha-1 subunit/ATP1A1 and thereby influences its endocytosis and/or degradation (PubMed:22797923). Acts also as a positive regulator of mTORC1 activation by amino acids, which functions upstream of the V-ATPase and of Rag-GTPases (PubMed:27244671). In turn, phosphorylation by mTOR leads to its inhibition via targeting to the cytosol allowing a self-regulating feedback mechanism (PubMed:27244671).
Pathway
Protein modification; protein ubiquitination.
Post-translational modifications
Phosphorylated; leading to binding to YWHAE (PubMed:22797923). Phosphorylated by MTOR at Ser-145 and dephosphorylated by PP6C. Ser-145 phosphorylation stimulates vesicle-to-cytosol translocation (PubMed:27244671).
Tissue Specificity
Highly expressed in the brain, with higher expression during development than in adult. Expressed also in mammary glands, testis, colon and kidney.
Cellular localization
- Endosome membrane
- Peripheral membrane protein
- Lysosome membrane
- Peripheral membrane protein
- Presynaptic cell membrane
- Peripheral membrane protein
- Cytoplasm
Alternative names
RNF202, ZNRF2, E3 ubiquitin-protein ligase ZNRF2, Protein Ells2, RING finger protein 202, RING-type E3 ubiquitin transferase ZNRF2, Zinc/RING finger protein 2