Entity Details

Primary name EPM2A_HUMAN
Entity type UniProt
Source Source Link

Details

AccessionO95278
EntryNameEPM2A_HUMAN
FullNameLaforin
TaxID9606
Evidenceevidence at protein level
Length331
SequenceStatuscomplete
DateCreated2004-07-19
DateModified2021-06-02

Ontological Relatives

GenesEPM2A

GO terms

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GOName
GO:0000045 autophagosome assembly
GO:0001558 regulation of cell growth
GO:0004373 glycogen (starch) synthase activity
GO:0004722 protein serine/threonine phosphatase activity
GO:0004725 protein tyrosine phosphatase activity
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0005977 glycogen metabolic process
GO:0005978 glycogen biosynthetic process
GO:0006470 protein dephosphorylation
GO:0006816 calcium ion transport
GO:0007005 mitochondrion organization
GO:0008138 protein tyrosine/serine/threonine phosphatase activity
GO:0010629 negative regulation of gene expression
GO:0010923 negative regulation of phosphatase activity
GO:0014009 glial cell proliferation
GO:0015813 L-glutamate transmembrane transport
GO:0016055 Wnt signaling pathway
GO:0016239 positive regulation of macroautophagy
GO:0016311 dephosphorylation
GO:0016791 phosphatase activity
GO:0019203 carbohydrate phosphatase activity
GO:0030246 carbohydrate binding
GO:0030425 dendrite
GO:0031396 regulation of protein ubiquitination
GO:0033137 negative regulation of peptidyl-serine phosphorylation
GO:0035305 negative regulation of dephosphorylation
GO:0035335 peptidyl-tyrosine dephosphorylation
GO:0042306 regulation of protein import into nucleus
GO:0042803 protein homodimerization activity
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0043204 perikaryon
GO:0045786 negative regulation of cell cycle
GO:0045859 regulation of protein kinase activity
GO:0046835 carbohydrate phosphorylation
GO:0046838 phosphorylated carbohydrate dephosphorylation
GO:0046959 habituation
GO:0046983 protein dimerization activity
GO:0061136 regulation of proteasomal protein catabolic process
GO:0098556 cytoplasmic side of rough endoplasmic reticulum membrane
GO:0106306 protein serine phosphatase activity
GO:0106307 protein threonine phosphatase activity
GO:1903076 regulation of protein localization to plasma membrane
GO:1904666 regulation of ubiquitin protein ligase activity
GO:2000465 regulation of glycogen (starch) synthase activity
GO:2001069 glycogen binding
GO:2001070 starch binding

Subcellular Location

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Subcellular Location
Cell membrane
Cytoplasm
Endoplasmic reticulum membrane
Nucleus

Domains

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DomainNameCategoryType
IPR000387 Tyrosine specific protein phosphatases domainDomainDomain
IPR002044 Carbohydrate binding module family 20DomainDomain
IPR013783 Immunoglobulin-like foldFamilyHomologous superfamily
IPR013784 Carbohydrate-binding-like foldFamilyHomologous superfamily
IPR016130 Protein-tyrosine phosphatase, active siteSiteActive site
IPR020422 Dual specificity protein phosphatase domainDomainDomain
IPR029021 Protein-tyrosine phosphatase-likeFamilyHomologous superfamily
IPR034831 Laforin, CBM20 domainDomainDomain
IPR042942 LaforinFamilyFamily

Diseases

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Disease IDSourceNameDescription
254780 OMIMEpilepsy, progressive myoclonic 2 (EPM2)A form of progressive myoclonic epilepsy, a clinically and genetically heterogeneous group of disorders defined by the combination of action and reflex myoclonus, other types of epileptic seizures, and progressive neurodegeneration and neurocognitive impairment. EPM2 is an autosomal recessive and severe form of adolescent-onset progressive epilepsy. Typically, as seizures increase in frequency, cognitive function declines towards dementia, and affected individuals die usually within 10 years after onset. EPM2 occurs worldwide, but it is particularly common in the mediterranean countries of southern Europe and northern Africa, in southern India and in the Middle East. At the cellular level, it is characterized by accumulation of starch-like polyglucosans called Lafora bodies (LBs) that are most abundant in organs with the highest glucose metabolism: brain, heart, liver and skeletal muscle. Among other conditions involving polyglucosans, EPM2 is unique in that the inclusions are in neuronal dendrites but not axons and the forming polyglucosan fibrils are associated with the endoplasmic reticulum. The disease is caused by variants affecting the gene represented in this entry.

Interactions

29 interactions

InteractorPartnerSourcesPublicationsLink
EPM2A_HUMANEPM2A_HUMANBioGRID, IntAct14532330 18617530 23922729 26493215 30041081 details
EPM2A_HUMANPPR3C_HUMANBioGRID, IntAct14532330 18070875 26493215 30041081 details
EPM2A_HUMANNHLC1_HUMANBioGRID, UniProt15930137 16115820 18029386 18617530 21505799 22578008 23922729 26546463 26648032 30041081 31758957 details
EPM2A_HUMANAAKB2_HUMANBioGRID, IntAct18029386 28514442 details
EPM2A_HUMANCCKN_HUMANIntAct32814053 details
EPM2A_HUMANLAMP2_HUMANIntAct32814053 details
EPM2A_HUMANSHLB1_HUMANIntAct32814053 details
EPM2A_HUMANNFU1_HUMANBioGRID, HPRD12915448 details
EPM2A_HUMANGSK3B_HUMANBioGRID16115820 details
EPM2A_HUMANAAPK2_HUMANBioGRID18029386 details
EPM2A_HUMANAAPK1_HUMANBioGRID21728993 details
EPM2A_HUMANPPR3D_HUMANBioGRID23624058 30041081 details
EPM2A_HUMANSRPK2_HUMANBioGRID26167880 details
EPM2A_HUMANKPYM_HUMANBioGRID26493215 details
EPM2A_HUMANTOPRS_HUMANBioGRID26493215 details
EPM2A_HUMANCOX5A_HUMANBioGRID26493215 details
EPM2A_HUMANTDG_HUMANBioGRID26493215 details
EPM2A_HUMANPRS6A_HUMANBioGRID26493215 details
EPM2A_HUMANHMGX4_HUMANBioGRID26493215 details
EPM2A_HUMANEI2BA_HUMANBioGRID26493215 details
EPM2A_HUMANGYS1_HUMANIntAct14532330 details
EPM2A_HUMANCHIP_HUMANBioGRID21652633 details
EPM2A_HUMANUBE2N_HUMANBioGRID26546463 details
EPM2A_HUMANSQSTM_HUMANBioGRID26546463 details
EPM2A_HUMANATX1_HUMANBioGRID29852174 details
EPM2A_HUMANBECN1_HUMANBioGRID31758957 details
EPM2A_HUMANPI3R4_HUMANBioGRID31758957 details
EPM2A_HUMANPK3C3_HUMANBioGRID31758957 details
EPM2A_HUMANEPMIP_HUMANHPRD12782127 details