Tissue Specificity | Expressed in brain, cerebellum, spinal cord, medulla, heart, liver, skeletal muscle and pancreas. |
Function | E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin-dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen accumulation. Polyubiquitinates EPM2A/laforin and ubiquitinates AGL and targets them for proteasome-dependent degradation. Also promotes proteasome-independent protein degradation through the macroautophagy pathway. |
Protein Name | E3 Ubiquitin-Protein Ligase Nhlrc1MalinNhl Repeat-Containing Protein 1Ring-Type E3 Ubiquitin Transferase Nhlrc1 |
Database Links | Reactome: R-HSA-3322077Reactome: R-HSA-3785653 |
Cellular Localisation | Endoplasmic ReticulumNucleusLocalizes At The Endoplasmic Reticulum AndTo A Lesser ExtentIn The Nucleus |
Alternative Antibody Names | Anti-E3 Ubiquitin-Protein Ligase Nhlrc1 antibodyAnti-Malin antibodyAnti-Nhl Repeat-Containing Protein 1 antibodyAnti-Ring-Type E3 Ubiquitin Transferase Nhlrc1 antibodyAnti-NHLRC1 antibodyAnti-EPM2B antibody |
Information sourced from Uniprot.org