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O95278

- EPM2A_HUMAN

UniProt

O95278 - EPM2A_HUMAN

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Protein
Laforin
Gene
EPM2A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Has both dual-specificity protein phosphatase and glucan phosphatase activities. Together with the E3 ubiquitin ligase NHLRC1/malin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. Dephosphorylates phosphotyrosine, phosphoserine and phosphothreonine substrates in vitro. Has also been shown to dephosphorylate MAPT. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates. Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin. Also promotes proteasome-independent protein degradation through the macroautophagy pathway. Isoform 2, an inactive phosphatase, could function as a dominant-negative regulator for the phosphatase activity of isoform 1.9 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei266 – 2661Phosphocysteine intermediate1 Publication
Sitei329 – 3291Required for homodimerization

GO - Molecular functioni

  1. carbohydrate phosphatase activity Source: Reactome
  2. phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Source: RefGenome
  3. protein binding Source: UniProtKB
  4. protein serine/threonine phosphatase activity Source: UniProtKB
  5. protein tyrosine phosphatase activity Source: UniProtKB
  6. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  7. starch binding Source: InterPro

GO - Biological processi

  1. autophagy Source: UniProtKB-KW
  2. carbohydrate metabolic process Source: Reactome
  3. glucose metabolic process Source: Reactome
  4. glycogen biosynthetic process Source: Reactome
  5. glycogen metabolic process Source: UniProtKB
  6. habituation Source: Ensembl
  7. inositol phosphate dephosphorylation Source: RefGenome
  8. nervous system development Source: Ensembl
  9. peptidyl-tyrosine dephosphorylation Source: GOC
  10. protein dephosphorylation Source: UniProtKB
  11. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Autophagy, Carbohydrate metabolism, Glycogen metabolism

Enzyme and pathway databases

ReactomeiREACT_169208. Glycogen synthesis.
REACT_200783. Myoclonic epilepsy of Lafora.

Protein family/group databases

CAZyiCBM20. Carbohydrate-Binding Module Family 20.

Names & Taxonomyi

Protein namesi
Recommended name:
Laforin (EC:3.1.3.-, EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Glucan phosphatase
Lafora PTPase
Short name:
LAFPTPase
Gene namesi
Name:EPM2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:3413. EPM2A.

Subcellular locationi

Cytoplasm
Note: Under glycogenolytic conditions localizes to the nucleus.6 Publications
Isoform 1 : Endoplasmic reticulum. Cell membrane
Note: Primarily associated with polyribosomes at the endoplasmic reticulum, also found at the plasma membrane.6 Publications
Isoform 2 : Endoplasmic reticulum. Cell membrane. Nucleus
Note: Also found in the nucleus.6 Publications
Isoform 4 : Cytoplasm. Nucleus 6 Publications
Isoform 5 : Cytoplasm. Nucleus 6 Publications
Isoform 7 : Cytoplasm 6 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. endoplasmic reticulum Source: UniProtKB-SubCell
  4. nucleus Source: RefGenome
  5. plasma membrane Source: UniProtKB-SubCell
  6. polysome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Epilepsy, progressive myoclonic 2 (EPM2) [MIM:254780]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.13 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251S → P in EPM2; atypical form; does not affect glycogen binding. 2 Publications
VAR_019465
Natural varianti28 – 281E → K in EPM2; does not affect glycogen binding. 1 Publication
VAR_019466
Natural varianti32 – 321W → G in EPM2; affects phosphatase activity; abolishes glycogen binding; reduced binding to Lafora bodies; disrupts the interaction with PPP1R3C; significant protein amount targeted to the nucleus. 4 Publications
VAR_019467
Natural varianti84 – 841F → L in EPM2; affects phosphatase activity and glycogen binding; disrupts the interaction with PPP1R3C. 2 Publications
VAR_019469
Natural varianti88 – 881F → L in EPM2; does not affect glycogen binding. 1 Publication
VAR_019470
Natural varianti91 – 911R → P in EPM2; atypical form; learning difficuties with childhood-onset. 2 Publications
VAR_019471
Natural varianti108 – 1081R → C in EPM2; loss of phosphatase activity; reduced self-interaction capacity; disrupts the interaction with PPP1R3C. 3 Publications
VAR_019472
Natural varianti140 – 1401K → N in EPM2. 1 Publication
VAR_046383
Natural varianti148 – 1481N → Y in EPM2. 1 Publication
VAR_046384
Natural varianti171 – 1711R → H in EPM2; results in ubiquitin-positive perinuclear aggregates; may affect proper folding. 4 Publications
VAR_019474
Natural varianti187 – 1871T → A in EPM2; abolishes interaction with NHLRC1. 1 Publication
VAR_019475
Natural varianti194 – 1941T → I in EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; reduced self-interaction capacity; abolishes interaction with NHLRC1, PPP1R3C and PRKAA2; no effect on phosphorylation of protein. 3 Publications
VAR_019476
Natural varianti210 – 2101E → K in EPM2. 1 Publication
VAR_046385
Natural varianti240 – 2401G → S in EPM2; very slight loss of phosphatase activity; does not affect glycogen binding; disrupts the interaction with PPP1R3C. 2 Publications
VAR_019477
Natural varianti279 – 2791G → S in EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C. 5 Publications
VAR_019478
Natural varianti293 – 2931Q → L in EPM2; results in ubiquitin-positive perinuclear aggregates; may affect proper folding; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C. 4 Publications
VAR_019479
Natural varianti294 – 2941Y → N in EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C. 3 Publications
VAR_019480
Natural varianti301 – 3011P → L in EPM2; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C. 2 Publications
VAR_019481
Natural varianti310 – 3101L → W in EPM2; alters the subcellular localization of isoform 1; does not affect homodimerization of isoform 1 but prevents heterodimerization of isoform 1 and isoform 2. 1 Publication
VAR_046386

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251S → A: Partial loss of phosphatase activity. Abolishes homodimerization. Abolishes interaction with NHLRC1, PPP1R3C and PRKAA2. Does not affect glycogen binding. Reduces stability of the protein. 1 Publication
Mutagenesisi25 – 251S → D: Partial loss of phosphatase activity. Increases interaction with NHLRC1. Does not affect interaction with NHLRC1, PPP1R3C or PRKAA2. Does not affect binding to carbohydrate. Does not affect homodimerization. 1 Publication
Mutagenesisi87 – 871K → A: Partial loss of phosphatase activity. Abolishes glycogen binding. 1 Publication
Mutagenesisi109 – 1102CC → SS: No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity.
Mutagenesisi123 – 1231C → S: No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity. 1 Publication
Mutagenesisi168 – 1681S → A or D: Abolishes interaction with NHLRC1. 1 Publication
Mutagenesisi169 – 1691C → S: No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity. 1 Publication
Mutagenesisi187 – 1871T → D: Abolishes interaction with NHLRC1. 1 Publication
Mutagenesisi194 – 1941T → D: Does not affect interaction with NHLRC1, PPP1R3C or PRKAA2. 1 Publication
Mutagenesisi205 – 2051C → S: No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity. 1 Publication
Mutagenesisi235 – 2351D → A: Loss of phosphatase activity. Does not affect glycogen binding. 1 Publication
Mutagenesisi250 – 2501C → S: No effect on homodimerization or carbohydrate binding. Decreased phosphatase activity. 1 Publication
Mutagenesisi266 – 2661C → S: Complete loss of phosphatase activity. Does not affect glycogen binding. Does not affect self-interaction. Increases the interaction with PPP1R3C. 3 Publications
Mutagenesisi329 – 3313Missing: Fails to homodimerize. Does not affect carbohydrate binding or phosphatase activity. 1 Publication
Mutagenesisi329 – 3291C → S: Fails to homodimerize. Does not affect carbohydrate binding, interaction with NHLRC1, phosphatase activity, or ubiquitination by NHLRC1. 1 Publication

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

MIMi254780. phenotype.
Orphaneti501. Lafora disease.
PharmGKBiPA27832.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Laforin
PRO_0000094838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Phosphoserine; by AMPK1 Publication

Post-translational modificationi

Polyubiquitinated by NHLRC1/malin.
Phosphorylation on Ser-25 by AMPK affects the phosphatase activity of the enzyme and its ability to homodimerize and interact with NHLRC1, PPP1R3C or PRKAA2.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO95278.
PRIDEiO95278.

PTM databases

PhosphoSiteiO95278.

Expressioni

Tissue specificityi

Expressed in heart, skeletal muscle, kidney, pancreas and brain. Isoform 4 is also expressed in the placenta.1 Publication

Gene expression databases

ArrayExpressiO95278.
BgeeiO95278.
CleanExiHS_EPM2A.
GenevestigatoriO95278.

Organism-specific databases

HPAiHPA053643.
HPA055468.

Interactioni

Subunit structurei

Interacts with itself; however no biological function has been identified for the dimer. Interacts with PPP1R3B, PPP1R3C, HIRIP5, and EPM2AIP1. Binds glycogen and Lafora bodies. Interacts with NHLRC1/malin (via the NHL repeats). Forms a complex with NHLRC1/malin and HSP70. Interacts with PPP1R3D; in the presence of NHLC1/malin the interaction leads to ubiquitination and autophagic degradation of PPP1R3D. Interacts (via the phosphatase domain) with MAPT/Tau; the interaction dephosphorylates MAPT. Isoform 2 does not bind glycogen. Isoform 1 and isoform 2 interact to form a heterodimeric complex inactive as phosphatase in vitro. Active phosphatase isoform 7 interacts with isoform 1 or isoform 2 to form a heterodimeric complex inactive as phosphatase in vitro.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP1R3CQ9UQK15EBI-2506661,EBI-2506727

Protein-protein interaction databases

BioGridi113679. 13 interactions.
IntActiO95278. 2 interactions.
STRINGi9606.ENSP00000356489.

Structurei

3D structure databases

ProteinModelPortaliO95278.
SMRiO95278. Positions 8-108, 154-301.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 124124CBM20
Add
BLAST
Domaini243 – 31169Tyrosine-protein phosphatase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG243912.
HOGENOMiHOG000285975.
HOVERGENiHBG051493.
InParanoidiO95278.
KOiK14165.
OMAiHWIEVSG.
PhylomeDBiO95278.
TreeFamiTF332841.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00686. CBM_20. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view]
SMARTiSM01065. CBM_2. 1 hit.
[Graphical view]
SUPFAMiSSF49452. SSF49452. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEiPS51166. CBM20. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing and alternative initiation. Align

Isoform 1 (identifier: O95278-1) [UniParc]FASTAAdd to Basket

Also known as: A, LDH1, Laf331

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MRFRFGVVVP PAVAGARPEL LVVGSRPELG RWEPRGAVRL RPAGTAAGDG    50
ALALQEPGLW LGEVELAAEE AAQDGAEPGR VDTFWYKFLK REPGGELSWE 100
GNGPHHDRCC TYNENNLVDG VYCLPIGHWI EATGHTNEMK HTTDFYFNIA 150
GHQAMHYSRI LPNIWLGSCP RQVEHVTIKL KHELGITAVM NFQTEWDIVQ 200
NSSGCNRYPE PMTPDTMIKL YREEGLAYIW MPTPDMSTEG RVQMLPQAVC 250
LLHALLEKGH IVYVHCNAGV GRSTAAVCGW LQYVMGWNLR KVQYFLMAKR 300
PAVYIDEEAL ARAQEDFFQK FGKVRSSVCS L 331
Length:331
Mass (Da):37,158
Last modified:May 1, 2000 - v2
Checksum:iDD79F917262AB458
GO
Isoform 2 (identifier: O95278-2) [UniParc]FASTAAdd to Basket

Also known as: B, C-terISO, Laf317

The sequence of this isoform differs from the canonical sequence as follows:
     310-320: LARAQEDFFQK → ASQDTFPL
     321-331: Missing.

Note: Produced by alternative splicing.

Show »
Length:317
Mass (Da):35,519
Checksum:i5646A039398AC24D
GO
Isoform 3 (identifier: O95278-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     75-100: GAEPGRVDTFWYKFLKREPGGELSWE → LVKIGSAPETRSKIFPRFTIRRRLSR

Note: Produced by alternative splicing. No experimental confirmation available.

Show »
Length:331
Mass (Da):37,188
Checksum:i65E7EC44AE20B083
GO
Isoform 4 (identifier: O95278-4) [UniParc]FASTAAdd to Basket

Also known as: Laf152

The sequence of this isoform differs from the canonical sequence as follows:
     102-199: NGPHHDRCCT...MNFQTEWDIV → IASRRLPPAQ...VPAHSPGDLG
     200-331: Missing.

Note: Produced by alternative splicing.

Show »
Length:152
Mass (Da):15,804
Checksum:i60CD9293F2267EC4
GO
Isoform 5 (identifier: O95278-5) [UniParc]FASTAAdd to Basket

Also known as: Laf224

The sequence of this isoform differs from the canonical sequence as follows:
     160-293: Missing.
     294-331: YFLMAKRPAV...GKVRSSVCSL → PSTDAAPGGV...PHGQEAGCLH

Note: Produced by alternative splicing.

Show »
Length:224
Mass (Da):24,134
Checksum:i66ECE43870086B2A
GO
Isoform 6 (identifier: O95278-6) [UniParc]FASTAAdd to Basket

Also known as: Laf88

The sequence of this isoform differs from the canonical sequence as follows:
     1-243: Missing.

Note: Produced by alternative initiation at Met-244 of isoform 1. Transcript amplified but protein not detected.

Show »
Length:88
Mass (Da):9,933
Checksum:iD28FAB18CC285D07
GO
Isoform 7 (identifier: O95278-7) [UniParc]FASTAAdd to Basket

Also known as: Laf177

The sequence of this isoform differs from the canonical sequence as follows:
     1-159: MRFRFGVVVP...AGHQAMHYSR → MIFNK

Note: Produced by alternative splicing. Active phosphatase.

Show »
Length:177
Mass (Da):20,256
Checksum:i5AE29B26B72E7BF7
GO
Isoform 8 (identifier: O95278-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-138: Missing.

Note: Produced by alternative splicing. No experimental confirmation available.

Show »
Length:193
Mass (Da):22,160
Checksum:i3DC9436A9885B915
GO
Isoform 9 (identifier: B3EWF7-1) [UniParc]FASTAAdd to Basket

Also known as: POCR

The sequence of this isoform can be found in the external entry B3EWF7.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by alternative initiation. Arises due to the use of an alternative initiation codon in exon 1 out of frame with isoform 1 and results in a completely different isoform.

Length:344
Mass (Da):35,169
GO

Sequence cautioni

The sequence BAG51107.1 differs from that shown. Reason: Frameshift at position 223.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251S → P in EPM2; atypical form; does not affect glycogen binding. 2 Publications
VAR_019465
Natural varianti28 – 281E → K in EPM2; does not affect glycogen binding. 1 Publication
VAR_019466
Natural varianti32 – 321W → G in EPM2; affects phosphatase activity; abolishes glycogen binding; reduced binding to Lafora bodies; disrupts the interaction with PPP1R3C; significant protein amount targeted to the nucleus. 4 Publications
VAR_019467
Natural varianti46 – 461A → P Does not affect glycogen binding. 3 Publications
VAR_019468
Natural varianti84 – 841F → L in EPM2; affects phosphatase activity and glycogen binding; disrupts the interaction with PPP1R3C. 2 Publications
VAR_019469
Natural varianti88 – 881F → L in EPM2; does not affect glycogen binding. 1 Publication
VAR_019470
Natural varianti91 – 911R → P in EPM2; atypical form; learning difficuties with childhood-onset. 2 Publications
VAR_019471
Natural varianti108 – 1081R → C in EPM2; loss of phosphatase activity; reduced self-interaction capacity; disrupts the interaction with PPP1R3C. 3 Publications
VAR_019472
Natural varianti114 – 1141E → D.1 Publication
VAR_019473
Natural varianti140 – 1401K → N in EPM2. 1 Publication
VAR_046383
Natural varianti148 – 1481N → Y in EPM2. 1 Publication
VAR_046384
Natural varianti171 – 1711R → H in EPM2; results in ubiquitin-positive perinuclear aggregates; may affect proper folding. 4 Publications
VAR_019474
Natural varianti187 – 1871T → A in EPM2; abolishes interaction with NHLRC1. 1 Publication
VAR_019475
Natural varianti194 – 1941T → I in EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; reduced self-interaction capacity; abolishes interaction with NHLRC1, PPP1R3C and PRKAA2; no effect on phosphorylation of protein. 3 Publications
VAR_019476
Natural varianti210 – 2101E → K in EPM2. 1 Publication
VAR_046385
Natural varianti240 – 2401G → S in EPM2; very slight loss of phosphatase activity; does not affect glycogen binding; disrupts the interaction with PPP1R3C. 2 Publications
VAR_019477
Natural varianti279 – 2791G → S in EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C. 5 Publications
VAR_019478
Natural varianti293 – 2931Q → L in EPM2; results in ubiquitin-positive perinuclear aggregates; may affect proper folding; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C. 4 Publications
VAR_019479
Natural varianti294 – 2941Y → N in EPM2; results in ubiquitin-positive perinuclear aggregates; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C. 3 Publications
VAR_019480
Natural varianti301 – 3011P → L in EPM2; loss of phosphatase activity; affects glycogen binding; disrupts the interaction with PPP1R3C. 2 Publications
VAR_019481
Natural varianti310 – 3101L → W in EPM2; alters the subcellular localization of isoform 1; does not affect homodimerization of isoform 1 but prevents heterodimerization of isoform 1 and isoform 2. 1 Publication
VAR_046386

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 243243Missing in isoform 6.
VSP_042494Add
BLAST
Alternative sequencei1 – 159159MRFRF…MHYSR → MIFNK in isoform 7.
VSP_042495Add
BLAST
Alternative sequencei1 – 138138Missing in isoform 8.
VSP_042493Add
BLAST
Alternative sequencei75 – 10026GAEPG…ELSWE → LVKIGSAPETRSKIFPRFTI RRRLSR in isoform 3.
VSP_011014Add
BLAST
Alternative sequencei102 – 19998NGPHH…EWDIV → IASRRLPPAQSGSSGPHPQP GPRPRAGPAGPGGARPGLFA RVPAHSPGDLG in isoform 4.
VSP_011015Add
BLAST
Alternative sequencei160 – 293134Missing in isoform 5.
VSP_042496Add
BLAST
Alternative sequencei200 – 331132Missing in isoform 4.
VSP_011016Add
BLAST
Alternative sequencei294 – 33138YFLMA…SVCSL → PSTDAAPGGVPAACAAGEGT HRVRALQRWGGPLHRGCLRL APVCDGLESEEGAVFPHGQE AGCLH in isoform 5.
VSP_042497Add
BLAST
Alternative sequencei310 – 32011LARAQEDFFQK → ASQDTFPL in isoform 2.
VSP_011017Add
BLAST
Alternative sequencei321 – 33111Missing in isoform 2.
VSP_011018Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti193 – 1931Q → K in AAH70047. 1 Publication
Sequence conflicti248 – 2481A → P in AAO15523. 1 Publication
Sequence conflicti258 – 2581K → E in BAG61454. 1 Publication
Sequence conflicti294 – 2941Y → H in BAG61454. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF084535 mRNA. Translation: AAC83347.2.
AF284580 mRNA. Translation: AAG18377.1.
AF454491 mRNA. Translation: AAO15523.1.
AF454492 mRNA. Translation: AAO15524.1.
AF454493 mRNA. Translation: AAO15525.1.
AF454494 mRNA. Translation: AAO15526.1.
AK022721 mRNA. Translation: BAG51107.1. Frameshift.
AK299497 mRNA. Translation: BAG61454.1.
AL023806, AL365193 Genomic DNA. Translation: CAI21419.1.
AL365193, AL023806 Genomic DNA. Translation: CAI21675.1.
CH471051 Genomic DNA. Translation: EAW47844.1.
BC005286 mRNA. Translation: AAH05286.1.
BC070047 mRNA. Translation: AAH70047.1.
AJ130763 mRNA. Translation: CAA10199.1.
AJ130764 mRNA. Translation: CAA10200.1.
CCDSiCCDS5206.1. [O95278-1]
RefSeqiNP_001018051.1. NM_001018041.1. [O95278-2]
NP_005661.1. NM_005670.3. [O95278-1]
XP_006715627.1. XM_006715564.1. [O95278-5]
XP_006715628.1. XM_006715565.1. [O95278-7]
UniGeneiHs.486696.

Genome annotation databases

EnsembliENST00000367519; ENSP00000356489; ENSG00000112425. [O95278-1]
GeneIDi7957.
KEGGihsa:7957.
UCSCiuc003qku.3. human. [O95278-7]
uc003qkv.3. human. [O95278-2]
uc003qkw.3. human. [O95278-1]
uc010khr.3. human. [O95278-5]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

The Lafora progressive myoclonus epilepsy mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF084535 mRNA. Translation: AAC83347.2 .
AF284580 mRNA. Translation: AAG18377.1 .
AF454491 mRNA. Translation: AAO15523.1 .
AF454492 mRNA. Translation: AAO15524.1 .
AF454493 mRNA. Translation: AAO15525.1 .
AF454494 mRNA. Translation: AAO15526.1 .
AK022721 mRNA. Translation: BAG51107.1 . Frameshift.
AK299497 mRNA. Translation: BAG61454.1 .
AL023806 , AL365193 Genomic DNA. Translation: CAI21419.1 .
AL365193 , AL023806 Genomic DNA. Translation: CAI21675.1 .
CH471051 Genomic DNA. Translation: EAW47844.1 .
BC005286 mRNA. Translation: AAH05286.1 .
BC070047 mRNA. Translation: AAH70047.1 .
AJ130763 mRNA. Translation: CAA10199.1 .
AJ130764 mRNA. Translation: CAA10200.1 .
CCDSi CCDS5206.1. [O95278-1 ]
RefSeqi NP_001018051.1. NM_001018041.1. [O95278-2 ]
NP_005661.1. NM_005670.3. [O95278-1 ]
XP_006715627.1. XM_006715564.1. [O95278-5 ]
XP_006715628.1. XM_006715565.1. [O95278-7 ]
UniGenei Hs.486696.

3D structure databases

ProteinModelPortali O95278.
SMRi O95278. Positions 8-108, 154-301.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113679. 13 interactions.
IntActi O95278. 2 interactions.
STRINGi 9606.ENSP00000356489.

Chemistry

ChEMBLi CHEMBL2311242.

Protein family/group databases

CAZyi CBM20. Carbohydrate-Binding Module Family 20.

PTM databases

PhosphoSitei O95278.

Proteomic databases

PaxDbi O95278.
PRIDEi O95278.

Protocols and materials databases

DNASUi 7957.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367519 ; ENSP00000356489 ; ENSG00000112425 . [O95278-1 ]
GeneIDi 7957.
KEGGi hsa:7957.
UCSCi uc003qku.3. human. [O95278-7 ]
uc003qkv.3. human. [O95278-2 ]
uc003qkw.3. human. [O95278-1 ]
uc010khr.3. human. [O95278-5 ]

Organism-specific databases

CTDi 7957.
GeneCardsi GC06M145822.
GeneReviewsi EPM2A.
HGNCi HGNC:3413. EPM2A.
HPAi HPA053643.
HPA055468.
MIMi 254780. phenotype.
607566. gene.
neXtProti NX_O95278.
Orphaneti 501. Lafora disease.
PharmGKBi PA27832.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG243912.
HOGENOMi HOG000285975.
HOVERGENi HBG051493.
InParanoidi O95278.
KOi K14165.
OMAi HWIEVSG.
PhylomeDBi O95278.
TreeFami TF332841.

Enzyme and pathway databases

Reactomei REACT_169208. Glycogen synthesis.
REACT_200783. Myoclonic epilepsy of Lafora.

Miscellaneous databases

GenomeRNAii 7957.
NextBioi 30475.
PROi O95278.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95278.
Bgeei O95278.
CleanExi HS_EPM2A.
Genevestigatori O95278.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR013784. Carb-bd-like_fold.
IPR002044. CBM_fam20.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00686. CBM_20. 1 hit.
PF00782. DSPc. 1 hit.
[Graphical view ]
SMARTi SM01065. CBM_2. 1 hit.
[Graphical view ]
SUPFAMi SSF49452. SSF49452. 1 hit.
SSF52799. SSF52799. 1 hit.
PROSITEi PS51166. CBM20. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, PROBABLE FUNCTION, TISSUE SPECIFICITY, VARIANTS EPM2 CYS-108; SER-279 AND LEU-293, VARIANT ASP-114.
  2. "Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes."
    Ganesh S., Agarwala K.L., Ueda K., Akagi T., Shoda K., Usui T., Hashikawa T., Osada H., Delgado-Escueta A.V., Yamakawa K.
    Hum. Mol. Genet. 9:2251-2261(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTIONAL CHARACTERIZATION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS EPM2 HIS-171 AND LEU-293.
    Tissue: Fetal brain.
  3. Lee J.R., Scherer S.W.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Cloning of differentially spliced transcripts of the EPM2A gene."
    Ganesh S., Yamakawa K.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), NUCLEOTIDE SEQUENCE [MRNA] OF 25-331 (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] OF 75-331 (ISOFORM 3).
    Tissue: Cerebellum and Fetal brain.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 8).
    Tissue: Fetal brain and Teratocarcinoma.
  6. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
    Tissue: Hypothalamus and Kidney.
  9. "A novel protein tyrosine phosphatase gene is mutated in progressive myoclonus epilepsy of the Lafora type (EPM2)."
    Serratosa J.M., Gomez-Garre P., Gallardo M.E., Anta B., de Bernabe D.B., Lindhout D., Augustijn P.B., Tassinari C.A., Malafosse R.M., Topcu M., Grid D., Dravet C., Berkovic S.F., de Cordoba S.R.
    Hum. Mol. Genet. 8:345-352(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 82-331 (ISOFORMS 1 AND 2), VARIANTS EPM2 HIS-171; ILE-194; SER-279 AND ASN-294.
  10. "Laforin is a cell membrane and endoplasmic reticulum-associated protein tyrosine phosphatase."
    Minassian B.A., Andrade D.M., Ianzano L., Young E.J., Chan E., Ackerley C.A., Scherer S.W.
    Ann. Neurol. 49:271-275(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "Alternative splicing modulates subcellular localization of laforin."
    Ganesh S., Suzuki T., Yamakawa K.
    Biochem. Biophys. Res. Commun. 291:1134-1137(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING, SUBCELLULAR LOCATION (ISOFORM 2).
  12. "A unique carbohydrate binding domain targets the Lafora disease phosphatase to glycogen."
    Wang J., Stuckey J.A., Wishart M.J., Dixon J.E.
    J. Biol. Chem. 277:2377-2380(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOGEN-BINDING, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT EPM2 GLY-32, ACTIVE SITE, MUTAGENESIS OF LYS-87 AND CYS-266.
  13. "Identification of a novel protein interacting with laforin, the EPM2A progressive myoclonus epilepsy gene product."
    Ianzano L., Zhao X.C., Minassian B.A., Scherer S.W.
    Genomics 81:579-587(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPM2AIP1.
  14. "The Lafora disease gene product laforin interacts with HIRIP5, a phylogenetically conserved protein containing a NifU-like domain."
    Ganesh S., Tsurutani N., Suzuki T., Ueda K., Agarwala K.L., Osada H., Delgado-Escueta A.V., Yamakawa K.
    Hum. Mol. Genet. 12:2359-2368(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIRIP5.
  15. "Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation."
    Fernandez-Sanchez M.E., Criado-Garcia O., Heath K.E., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa J.M., Rodriguez de Cordoba S.
    Hum. Mol. Genet. 12:3161-3171(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-INTERACTION, INTERACTION WITH PPP1R3C, MUTAGENESIS OF ASP-235 AND CYS-266, CHARACTERIZATION OF VARIANTS EPM2 GLY-32; LEU-84; CYS-108; ILE-194; SER-240; SER-279; LEU-293; ASN-294 AND LEU-301.
  16. "The carbohydrate-binding domain of Lafora disease protein targets Lafora polyglucosan bodies."
    Ganesh S., Tsurutani N., Suzuki T., Hoshii Y., Ishihara T., Delgado-Escueta A.V., Yamakawa K.
    Biochem. Biophys. Res. Commun. 313:1101-1109(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING TO LAFORA BODIES, CHARACTERIZATION OF VARIANTS EPM2 PRO-25; LYS-28; GLY-32 AND LEU-88, CHARACTERIZATION OF VARIANT PRO-46.
  17. "Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin."
    Gentry M.S., Worby C.A., Dixon J.E.
    Proc. Natl. Acad. Sci. U.S.A. 102:8501-8506(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NHLRC1, POLYUBIQUITINATION.
  18. "Laforin, a dual specificity phosphatase that dephosphorylates complex carbohydrates."
    Worby C.A., Gentry M.S., Dixon J.E.
    J. Biol. Chem. 281:30412-30418(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A GLUCAN PHOSPHATASE, INTERACTION WITH PPP1R3B; PPP1R3C AND PPP1R3D.
  19. "A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease."
    Cheng A., Zhang M., Gentry M.S., Worby C.A., Dixon J.E., Saltiel A.R.
    Genes Dev. 21:2399-2409(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  20. "Modulation of functional properties of laforin phosphatase by alternative splicing reveals a novel mechanism for the EPM2A gene in Lafora progressive myoclonus epilepsy."
    Dubey D., Ganesh S.
    Hum. Mol. Genet. 17:3010-3020(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMODIMERIZATION, HETERODIMERIZATION, SUBCELLULAR LOCATION.
  21. "Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)."
    Worby C.A., Gentry M.S., Dixon J.E.
    J. Biol. Chem. 283:4069-4076(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPP1R3C.
  22. "The malin-laforin complex suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system."
    Garyali P., Siwach P., Singh P.K., Puri R., Mittal S., Sengupta S., Parihar R., Ganesh S.
    Hum. Mol. Genet. 18:688-700(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COMPLEX FORMATION WITH NHLRC1 AND HSP70.
  23. "Hyperphosphorylation and aggregation of Tau in laforin-deficient mice, an animal model for Lafora disease."
    Puri R., Suzuki T., Yamakawa K., Ganesh S.
    J. Biol. Chem. 284:22657-22663(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAPT.
  24. "Laforin, the most common protein mutated in Lafora disease, regulates autophagy."
    Aguado C., Sarkar S., Korolchuk V.I., Criado O., Vernia S., Boya P., Sanz P., de Cordoba S.R., Knecht E., Rubinsztein D.C.
    Hum. Mol. Genet. 19:2867-2876(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "Laforin, a dual-specificity phosphatase involved in Lafora disease, is phosphorylated at Ser25 by AMP-activated protein kinase."
    Roma-Mateo C., Solaz-Fuster Mdel C., Gimeno-Alcaniz J.V., Dukhande V.V., Donderis J., Worby C.A., Marina A., Criado O., Koller A., Rodriguez De Cordoba S., Gentry M.S., Sanz P.
    Biochem. J. 439:265-275(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-25 (ISOFORM 1), MUTAGENESIS OF SER-25; SER-168; THR-187 AND THR-194.
  26. "Identification and characterization of novel splice variants of the human EPM2A gene mutated in Lafora progressive myoclonus epilepsy."
    Dubey D., Parihar R., Ganesh S.
    Genomics 99:36-43(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 4; 5; 6; 7 AND 9).
  27. "Glycogenic activity of R6, a protein phosphatase 1 regulatory subunit, is modulated by the laforin-malin complex."
    Rubio-Villena C., Garcia-Gimeno M.A., Sanz P.
    Int. J. Biochem. Cell Biol. 45:1479-1488(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPP1R3D.
  28. "Dimerization of the glucan phosphatase laforin requires the participation of cysteine 329."
    Sanchez-Martin P., Raththagala M., Bridges T.M., Husodo S., Gentry M.S., Sanz P., Roma-Mateo C.
    PLoS ONE 8:E69523-E69523(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 109-CYS-CYS-110; CYS-123; CYS-169; CYS-205; CYS-250; CYS-266; CYS-329 AND 329-CYS--CYS-331.
  29. "Mutational spectrum of the EPM2A gene in progressive myoclonus epilepsy of Lafora: high degree of allelic heterogeneity and prevalence of deletions."
    Gomez-Garre P., Sanz Y., Rodriguez de Cordoba S.R., Serratosa J.M.
    Eur. J. Hum. Genet. 8:946-954(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EPM2 LEU-84; SER-240 AND LEU-301.
  30. "Mutation screening for Japanese Lafora's disease patients: identification of novel sequence variants in the coding and upstream regulatory regions of EPM2A gene."
    Ganesh S., Shoda K., Amano K., Uchiyama A., Kumada S., Moriyama N., Hirose S., Yamakawa K.
    Mol. Cell. Probes 15:281-289(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRO-46.
  31. "Genotype-phenotype correlations for EPM2A mutations in Lafora's progressive myoclonus epilepsy: exon 1 mutations associate with an early-onset cognitive deficit subphenotype."
    Ganesh S., Delgado-Escueta A.V., Suzuki T., Francheschetti S., Riggio C., Avanzini G., Rabinowicz A., Bohlega S., Bailey J., Alonso M.E., Rasmussen A., Thomson A.E., Ochoa A., Prado A.J., Medina M.T., Yamakawa K.
    Hum. Mol. Genet. 11:1263-1271(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EPM2 PRO-25; CYS-108; HIS-171 AND LEU-293, CHARACTERIZATION OF VARIANTS EPM2 GLY-32; CYS-108; ILE-194; SER-279 AND ASN-294.
  32. "Two novel mutations in the EPM2A gene in a Korean patient with Lafora's progressive myoclonus epilepsy."
    Ki C.S., Kong S.Y., Seo D.W., Hong S.B., Kim H.J., Kim J.W.
    J. Hum. Genet. 48:51-54(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EPM2 ALA-187.
  33. "A novel exon 1 mutation in a patient with atypical Lafora progressive myoclonus epilepsy seen as childhood-onset cognitive deficit."
    Annesi G., Sofia V., Gambardella A., Ciro Candiano I.C., Spadafora P., Annesi F., Cutuli N., De Marco E.V., Civitelli D., Carrideo S., Tarantino P., Barone R., Zappia M., Quattrone A.
    Epilepsia 45:294-295(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EPM2 PRO-91.
  34. "Loss of function of the cytoplasmic isoform of the protein laforin (EPM2A) causes Lafora progressive myoclonus epilepsy."
    Ianzano L., Young E.J., Zhao X.C., Chan E.M., Rodriguez M.T., Torrado M.V., Scherer S.W., Minassian B.A.
    Hum. Mutat. 23:170-176(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EPM2 PRO-91; HIS-171 AND SER-279.
  35. "Mutations in the NHLRC1 gene are the common cause for Lafora disease in the Japanese population."
    Singh S., Suzuki T., Uchiyama A., Kumada S., Moriyama N., Hirose S., Takahashi Y., Sugie H., Mizoguchi K., Inoue Y., Kimura K., Sawaishi Y., Yamakawa K., Ganesh S.
    J. Hum. Genet. 50:347-352(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PRO-46.
  36. "Lafora disease in the Indian population: EPM2A and NHLRC1 gene mutations and their impact on subcellular localization of laforin and malin."
    Singh S., Satishchandra P., Shankar S.K., Ganesh S.
    Hum. Mutat. 29:E1-12(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EPM2 ASN-140; TYR-148; LYS-210 AND TRP-310, CHARACTERIZATION OF VARIANT EPM2 TRP-310.

Entry informationi

Entry nameiEPM2A_HUMAN
AccessioniPrimary (citable) accession number: O95278
Secondary accession number(s): B3KMU5
, B4DRZ2, O95483, Q5T3F5, Q6IS15, Q8IU96, Q8IX24, Q8IX25, Q9BS66, Q9UEN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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