Gene Ontology annotation through association of InterPro records with GO terms

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Gene Ontology annotation based on curation of immunofluorescence data

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes.

Laforin is a cell membrane and endoplasmic reticulum-associated protein tyrosine phosphatase.

A unique carbohydrate binding domain targets the lafora disease phosphatase to glycogen.

Alternative splicing modulates subcellular localization of laforin.

The Lafora disease gene product laforin interacts with HIRIP5, a phylogenetically conserved protein containing a NifU-like domain.

Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation.

Loss of function of the cytoplasmic isoform of the protein laforin (EPM2A) causes Lafora progressive myoclonus epilepsy.

Laforin preferentially binds the neurotoxic starch-like polyglucosans, which form in its absence in progressive myoclonus epilepsy.

Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin.

Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates.

A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease.

Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG).

Lafora disease in the Indian population: EPM2A and NHLRC1 gene mutations and their impact on subcellular localization of laforin and malin.

Modulation of functional properties of laforin phosphatase by alternative splicing reveals a novel mechanism for the EPM2A gene in Lafora progressive myoclonus epilepsy.

Lafora progressive myoclonus epilepsy: NHLRC1 mutations affect glycogen metabolism.

Identification and characterization of novel splice variants of the human EPM2A gene mutated in Lafora progressive myoclonus epilepsy.

Early-onset Lafora body disease.

Dimeric quaternary structure of human laforin.

Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease.

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2).

Glycogen synthesis

NHLRC1 mediated ubiquitination of EPM2A (laforin) and PPP1RC3 (PTG) associated with glycogen-GYG2

EPM2A dimer binds PPP1R3C:phosphoglycogen-GYG1 complex

NHLRC1 mediated ubiquitination of EPM2A and PPP1RC3 associated with glycogen-GYG1

EPM2A dimer dephosphorylates phosphoglycogen-GYG2

EPM2A dimer dephosphorylates phosphoglycogen-GYG1

EPM2A dimer binds PPP1R3C:phosphoglycogen-GYG2 complex

Defective EPM2A does not dephosphorylate phosphoglycogen (type 2A disease)

Defective NHLRC1 does not ubiquitinate EPM2A (laforin) and PPP1R3C (PTG) (type 2B disease)

Abnormal metabolism of glycogen phosphate as a cause for Lafora disease.

Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo.

Increased laforin and laforin binding to glycogen underlie Lafora body formation in malin-deficient Lafora disease.

Glycogen metabolism in tissues from a mouse model of Lafora disease.

Abnormal glycogen chain length pattern, not hyperphosphorylation, is critical in Lafora disease.

Skeletal Muscle Glycogen Chain Length Correlates with Insolubility in Mouse Models of Polyglucosan-Associated Neurodegenerative Diseases.

Mechanistic Insights into Glucan Phosphatase Activity against Polyglucan Substrates.

Laforin, the most common protein mutated in Lafora disease, regulates autophagy.

The carbohydrate-binding domain of overexpressed STBD1 is important for its stability and protein-protein interactions.

Dimerization of Laforin is required for its optimal phosphatase activity, regulation of GSK3beta phosphorylation, and Wnt signaling.

Glycogen and related polysaccharides inhibit the laforin dual-specificity protein phosphatase.

The phosphatase activity of laforin is dispensable to rescue Epm2a-/- mice from Lafora disease.