Nhlrc1

E3 ubiquitin-protein ligase NHLRC1

401 amino acids

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.

42.69 kDa

MGEEATAVAAAGVRPELVREAEVSLLECKVCFERFGHWQQRRPRNLPCGHVVCLACVAALAHPRTLGLECPFCRRACRACDTSDCLPVLHLLELLGSTLHASPAALSAAPFAPGTLTCYHAFGGWGTLVNPTGLALCPKTGRVVVVHDGKRRVKIFDSGGGGAHQFGEKGDAAHDVKYPLDVAVTNDCHVVVTDAGDCSLKVFDFFGQIKLVVGKQFSLPWGVEITPHNGVLVTDAEAGTLHLLEADFPEGVLRRIERLQAHLCSPRGLAVSWLTGAIAVLEHPCAFGRTGCNNTRVKVFNSTMQLIGQVDSFGLNLLFPSKVTASAVTFDHQGNVIVADTSGPAIVCLGKPEEFPALKPIITHGLSRPVALAFTKENSLLVLDTASHSIKVFKVMEGNGG

Nhlrc1

E3 ubiquitin-protein ligase NHLRC1

396 amino acids

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.

42.089 kDa

MGEEAAGVRPELVREAEVSLLECKVCFERFGHRQQRRPRNLPCGHVVCLACVAALAHPRTLALECPFCRRACRACDTSDCLPVLHLLELLGSTLHASPAALSAASCAPGALTCYHAFGGWGTLVNPTGLALCPKTGRVVVVHDGKRRVKIFDSGGGGAHQFGEKGDAAHDVKYPLDVAVTNDCHVVVTDAGDCSLKVFDFFGQIKLVVGKQFSLPWGVEITPHNGVLVTDAEAGTLHLLEADFPEGVLRRIERLQAHLCNPRGVAVSWLTGAIAVLEHPCALGTSSGNNTRVKVFNSSMQLIGQVDSFGLNLLFPSKITASAVTFDHQGNVIVADTSGPAIVCLGKPEEFPALKPMVTHGLSRPVALVFTKENSLLVLDSASHSIKVFKVMEGNGG

NHLRC1

E3 ubiquitin-protein ligase NHLRC1

395 amino acids

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.

42.293 kDa

MAAEASESGPALHELMREAEISLLECKVCFEKFGHRQQRRPRNLSCGHVVCLACVAALAHPRTLALECPFCRRACRGCDTSDCLPVLHLIELLGSALRQSPAAHRAAPSAPGALTCHHTFGGWGTLVNPTGLALCPKTGRVVVVHDGRRRVKIFDSGGGCAHQFGEKGDAAQDIRYPVDVTITNDCHVVVTDAGDRSIKVFDFFGQIKLVIGGQFSLPWGVETTPQNGIVVTDAEAGSLHLLDVDFAEGVLRRTERLQAHLCNPRGVAVSWLTGAIAVLEHPLALGTGVCSTRVKVFSSSMQLVGQVDTFGLSLYFPSKITASAVTFDHQGNVIVADTSGPAILCLGKPEEFPVPKPMVTHGLSHPVALTFTKENSLLVLDTASHSIKVYKVDWG