NHLRC1 report

I. Expression across cell types

Insufficient scRNA-seq data for expression of NHLRC1 at single-cell level.

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of NHLRC1 at tissue level.

III. Associated gene sets

GO_0000209Biological processprotein polyubiquitination
GO_0005978Biological processglycogen biosynthetic process
GO_0034976Biological processresponse to endoplasmic reticulum stress
GO_0001932Biological processregulation of protein phosphorylation
GO_0031398Biological processpositive regulation of protein ubiquitination
GO_0006914Biological processautophagy
GO_1903076Biological processregulation of protein localization to plasma membrane
GO_0043161Biological processproteasome-mediated ubiquitin-dependent protein catabolic process
GO_0017148Biological processnegative regulation of translation
GO_0048471Cellular componentperinuclear region of cytoplasm
GO_0005654Cellular componentnucleoplasm
GO_0005783Cellular componentendoplasmic reticulum
GO_0005829Cellular componentcytosol
GO_0005634Cellular componentnucleus
GO_0061630Molecular functionubiquitin protein ligase activity
GO_0030371Molecular functiontranslation repressor activity
GO_0046872Molecular functionmetal ion binding
GO_0004842Molecular functionubiquitin-protein transferase activity
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameNHLRC1
Protein nameE3 ubiquitin-protein ligase NHLRC1 (EC 2.3.2.27) (Malin) (NHL repeat-containing protein 1) (RING-type E3 ubiquitin transferase NHLRC1)
SynonymsEPM2B
DescriptionFUNCTION: 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. .

AccessionsQ6VVB1
ENST00000340650.6