Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Laforin (EC 3.1.3.-) (EC 3.1.3.16) (EC 3.1.3.48) (Glucan phosphatase) (Glycogen phosphatase) (Lafora PTPase) (LAFPTPase)

 EPM2A_HUMAN             Reviewed;         331 AA.
O95278; B3KMU5; B4DRZ2; O95483; Q5T3F5; Q6IS15; Q8IU96; Q8IX24;
Q8IX25; Q9BS66; Q9UEN2;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 2.
27-SEP-2017, entry version 154.
RecName: Full=Laforin {ECO:0000303|PubMed:11001928};
EC=3.1.3.- {ECO:0000269|PubMed:16901901, ECO:0000269|PubMed:23922729, ECO:0000269|PubMed:25538239, ECO:0000269|PubMed:25544560, ECO:0000269|PubMed:26231210};
EC=3.1.3.16 {ECO:0000305|PubMed:11001928};
EC=3.1.3.48 {ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:11220751};
AltName: Full=Glucan phosphatase {ECO:0000303|PubMed:16901901, ECO:0000303|PubMed:25538239};
AltName: Full=Glycogen phosphatase {ECO:0000303|PubMed:25538239, ECO:0000303|PubMed:25544560};
AltName: Full=Lafora PTPase;
Short=LAFPTPase {ECO:0000303|PubMed:11175283};
Name=EPM2A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
TISSUE SPECIFICITY, VARIANTS EPM2 CYS-108; SER-279 AND LEU-293, AND
VARIANT ASP-114.
PubMed=9771710; DOI=10.1038/2470;
Minassian B.A., Lee J.R., Herbrick J.-A., Huizenga J., Soder S.,
Mungall A.J., Dunham I., Gardner R., Fong C.G., Carpenter S.,
Jardim L., Satishchandra P., Andermann E., Snead O.C. III,
Lopes-Cendes I., Tsui L.-C., Delgado-Escueta A.V., Rouleau G.A.,
Scherer S.W.;
"Mutations in a gene encoding a novel protein tyrosine phosphatase
cause progressive myoclonus epilepsy.";
Nat. Genet. 20:171-174(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTIONAL CHARACTERIZATION,
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF
VARIANTS EPM2 HIS-171 AND LEU-293.
TISSUE=Fetal brain;
PubMed=11001928; DOI=10.1093/oxfordjournals.hmg.a018916;
Ganesh S., Agarwala K.L., Ueda K., Akagi T., Shoda K., Usui T.,
Hashikawa T., Osada H., Delgado-Escueta A.V., Yamakawa K.;
"Laforin, defective in the progressive myoclonus epilepsy of Lafora
type, is a dual-specificity phosphatase associated with
polyribosomes.";
Hum. Mol. Genet. 9:2251-2261(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Lee J.R., Scherer S.W.;
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), AND NUCLEOTIDE SEQUENCE [MRNA]
OF 25-331 (ISOFORM 4).
TISSUE=Cerebellum, and Fetal brain;
Ganesh S., Yamakawa K.;
"Cloning of differentially spliced transcripts of the EPM2A gene.";
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 8).
TISSUE=Fetal brain, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
TISSUE=Hypothalamus, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 82-331 (ISOFORMS 1 AND 2), AND VARIANTS
EPM2 HIS-171; ILE-194; SER-279 AND ASN-294.
PubMed=9931343; DOI=10.1093/hmg/8.2.345;
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.;
"A novel protein tyrosine phosphatase gene is mutated in progressive
myoclonus epilepsy of the Lafora type (EPM2).";
Hum. Mol. Genet. 8:345-352(1999).
[10]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF
CYS-266, AND ACTIVE SITE.
PubMed=11220751;
DOI=10.1002/1531-8249(20010201)49:2<271::AID-ANA52>3.3.CO;2-4;
Minassian B.A., Andrade D.M., Ianzano L., Young E.J., Chan E.,
Ackerley C.A., Scherer S.W.;
"Laforin is a cell membrane and endoplasmic reticulum-associated
protein tyrosine phosphatase.";
Ann. Neurol. 49:271-275(2001).
[11]
ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION (ISOFORM 2).
PubMed=11883934; DOI=10.1006/bbrc.2002.6590;
Ganesh S., Suzuki T., Yamakawa K.;
"Alternative splicing modulates subcellular localization of laforin.";
Biochem. Biophys. Res. Commun. 291:1134-1137(2002).
[12]
GLYCOGEN-BINDING, DOMAIN, SUBCELLULAR LOCATION, CHARACTERIZATION OF
VARIANT EPM2 GLY-32, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS
OF LYS-87 AND CYS-266.
PubMed=11739371; DOI=10.1074/jbc.C100686200;
Wang J., Stuckey J.A., Wishart M.J., Dixon J.E.;
"A unique carbohydrate binding domain targets the Lafora disease
phosphatase to glycogen.";
J. Biol. Chem. 277:2377-2380(2002).
[13]
INTERACTION WITH EPM2AIP1.
PubMed=12782127; DOI=10.1016/S0888-7543(03)00094-6;
Ianzano L., Zhao X.C., Minassian B.A., Scherer S.W.;
"Identification of a novel protein interacting with laforin, the EPM2A
progressive myoclonus epilepsy gene product.";
Genomics 81:579-587(2003).
[14]
INTERACTION WITH HIRIP5.
PubMed=12915448; DOI=10.1093/hmg/ddg253;
Ganesh S., Tsurutani N., Suzuki T., Ueda K., Agarwala K.L., Osada H.,
Delgado-Escueta A.V., Yamakawa K.;
"The Lafora disease gene product laforin interacts with HIRIP5, a
phylogenetically conserved protein containing a NifU-like domain.";
Hum. Mol. Genet. 12:2359-2368(2003).
[15]
FUNCTION, CATALYTIC ACTIVITY, SELF-INTERACTION, SUBCELLULAR LOCATION,
GLYCOGEN-BINDING, INTERACTION WITH PPP1R3C, TISSUE SPECIFICITY,
MUTAGENESIS OF ASP-235 AND CYS-266, ACTIVE SITE, AND CHARACTERIZATION
OF VARIANTS EPM2 GLY-32; LEU-84; CYS-108; ILE-194; SER-240; SER-279;
LEU-293; ASN-294 AND LEU-301.
PubMed=14532330; DOI=10.1093/hmg/ddg340;
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.;
"Laforin, the dual-phosphatase responsible for Lafora disease,
interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1
that enhances glycogen accumulation.";
Hum. Mol. Genet. 12:3161-3171(2003).
[16]
BINDING TO GLYCOGEN AND LAFORA BODIES, DOMAIN, CHARACTERIZATION OF
VARIANTS EPM2 PRO-25; LYS-28; GLY-32 AND LEU-88, AND CHARACTERIZATION
OF VARIANT PRO-46.
PubMed=14706656; DOI=10.1016/j.bbrc.2003.12.043;
Ganesh S., Tsurutani N., Suzuki T., Hoshii Y., Ishihara T.,
Delgado-Escueta A.V., Yamakawa K.;
"The carbohydrate-binding domain of Lafora disease protein targets
Lafora polyglucosan bodies.";
Biochem. Biophys. Res. Commun. 313:1101-1109(2004).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND BINDING TO LAFORA GLUCAN BODIES.
PubMed=15102711; DOI=10.1093/hmg/ddh130;
Chan E.M., Ackerley C.A., Lohi H., Ianzano L., Cortez M.A.,
Shannon P., Scherer S.W., Minassian B.A.;
"Laforin preferentially binds the neurotoxic starch-like
polyglucosans, which form in its absence in progressive myoclonus
epilepsy.";
Hum. Mol. Genet. 13:1117-1129(2004).
[18]
INTERACTION WITH NHLRC1, AND POLYUBIQUITINATION.
PubMed=15930137; DOI=10.1073/pnas.0503285102;
Gentry M.S., Worby C.A., Dixon J.E.;
"Insights into Lafora disease: malin is an E3 ubiquitin ligase that
ubiquitinates and promotes the degradation of laforin.";
Proc. Natl. Acad. Sci. U.S.A. 102:8501-8506(2005).
[19]
FUNCTION AS A GLUCAN PHOSPHATASE, CATALYTIC ACTIVITY, AND INTERACTION
WITH PPP1R3B; PPP1R3C AND PPP1R3D.
PubMed=16901901; DOI=10.1074/jbc.M606117200;
Worby C.A., Gentry M.S., Dixon J.E.;
"Laforin, a dual specificity phosphatase that dephosphorylates complex
carbohydrates.";
J. Biol. Chem. 281:30412-30418(2006).
[20]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=16971387; DOI=10.1074/jbc.M607778200;
Liu Y., Wang Y., Wu C., Liu Y., Zheng P.;
"Dimerization of Laforin is required for its optimal phosphatase
activity, regulation of GSK3beta phosphorylation, and Wnt signaling.";
J. Biol. Chem. 281:34768-34774(2006).
[21]
SUBCELLULAR LOCATION.
PubMed=17908927; DOI=10.1101/gad.1553207;
Cheng A., Zhang M., Gentry M.S., Worby C.A., Dixon J.E., Saltiel A.R.;
"A role for AGL ubiquitination in the glycogen storage disorders of
Lafora and Cori's disease.";
Genes Dev. 21:2399-2409(2007).
[22]
FUNCTION (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY, HOMODIMERIZATION,
SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH NHLRC1 AND
GLYCOGEN.
PubMed=18617530; DOI=10.1093/hmg/ddn199;
Dubey D., Ganesh S.;
"Modulation of functional properties of laforin phosphatase by
alternative splicing reveals a novel mechanism for the EPM2A gene in
Lafora progressive myoclonus epilepsy.";
Hum. Mol. Genet. 17:3010-3020(2008).
[23]
FUNCTION, AND INTERACTION WITH PPP1R3C.
PubMed=18070875; DOI=10.1074/jbc.M708712200;
Worby C.A., Gentry M.S., Dixon J.E.;
"Malin decreases glycogen accumulation by promoting the degradation of
protein targeting to glycogen (PTG).";
J. Biol. Chem. 283:4069-4076(2008).
[24]
FUNCTION, AND COMPLEX FORMATION WITH NHLRC1 AND HSP70.
PubMed=19036738; DOI=10.1093/hmg/ddn398;
Garyali P., Siwach P., Singh P.K., Puri R., Mittal S., Sengupta S.,
Parihar R., Ganesh S.;
"The malin-laforin complex suppresses the cellular toxicity of
misfolded proteins by promoting their degradation through the
ubiquitin-proteasome system.";
Hum. Mol. Genet. 18:688-700(2009).
[25]
INTERACTION WITH MAPT.
PubMed=19542233; DOI=10.1074/jbc.M109.009688;
Puri R., Suzuki T., Yamakawa K., Ganesh S.;
"Hyperphosphorylation and aggregation of Tau in laforin-deficient
mice, an animal model for Lafora disease.";
J. Biol. Chem. 284:22657-22663(2009).
[26]
FUNCTION.
PubMed=20453062; DOI=10.1093/hmg/ddq190;
Aguado C., Sarkar S., Korolchuk V.I., Criado O., Vernia S., Boya P.,
Sanz P., de Cordoba S.R., Knecht E., Rubinsztein D.C.;
"Laforin, the most common protein mutated in Lafora disease, regulates
autophagy.";
Hum. Mol. Genet. 19:2867-2876(2010).
[27]
PHOSPHORYLATION AT SER-25, MUTAGENESIS OF SER-25; SER-168; THR-187 AND
THR-194, AND INTERACTION WITH NHLRC1; PPP1R3C AND PRKAA2.
PubMed=21728993; DOI=10.1042/BJ20110150;
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.;
"Laforin, a dual-specificity phosphatase involved in Lafora disease,
is phosphorylated at Ser25 by AMP-activated protein kinase.";
Biochem. J. 439:265-275(2011).
[28]
INTERACTION WITH PRDM8.
PubMed=22961547; DOI=10.1093/brain/aws205;
Turnbull J., Girard J.M., Lohi H., Chan E.M., Wang P., Tiberia E.,
Omer S., Ahmed M., Bennett C., Chakrabarty A., Tyagi A., Liu Y.,
Pencea N., Zhao X., Scherer S.W., Ackerley C.A., Minassian B.A.;
"Early-onset Lafora body disease.";
Brain 135:2684-2698(2012).
[29]
ALTERNATIVE SPLICING (ISOFORMS 4; 5; 6; 7 AND 9), FUNCTION (ISOFORMS 2
AND 7), INTERACTION WITH NHLRC1 AND GLYCOGEN, SUBCELLULAR LOCATION,
SUBUNIT, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-266, AND ACTIVE SITE.
PubMed=22036712; DOI=10.1016/j.ygeno.2011.10.001;
Dubey D., Parihar R., Ganesh S.;
"Identification and characterization of novel splice variants of the
human EPM2A gene mutated in Lafora progressive myoclonus epilepsy.";
Genomics 99:36-43(2012).
[30]
FUNCTION, AND INTERACTION WITH PPP1R3D.
PubMed=23624058; DOI=10.1016/j.biocel.2013.04.019;
Rubio-Villena C., Garcia-Gimeno M.A., Sanz P.;
"Glycogenic activity of R6, a protein phosphatase 1 regulatory
subunit, is modulated by the laforin-malin complex.";
Int. J. Biochem. Cell Biol. 45:1479-1488(2013).
[31]
CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH NHLRC1, SUBUNIT, AND
MUTAGENESIS OF 109-CYS-CYS-110; CYS-123; CYS-169; CYS-205; CYS-250;
CYS-266; CYS-329 AND 329-CYS--CYS-331.
PubMed=23922729; DOI=10.1371/journal.pone.0069523;
Sanchez-Martin P., Raththagala M., Bridges T.M., Husodo S.,
Gentry M.S., Sanz P., Roma-Mateo C.;
"Dimerization of the glucan phosphatase laforin requires the
participation of cysteine 329.";
PLoS ONE 8:E69523-E69523(2013).
[32]
CATALYTIC ACTIVITY, FUNCTION, MOTIF, AND CHARACTERIZATION OF VARIANT
EPM2 GLY-32.
PubMed=26231210; DOI=10.1074/jbc.M115.658203;
Meekins D.A., Raththagala M., Auger K.D., Turner B.D., Santelia D.,
Koetting O., Gentry M.S., Vander Kooi C.W.;
"Mechanistic insights into glucan phosphatase activity against
polyglucan substrates.";
J. Biol. Chem. 290:23361-23370(2015).
[33] {ECO:0000244|PDB:4R30}
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 148-331, FUNCTION AS GLUCAN
PHOSPHATASE, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF CYS-169;
ARG-171; ASP-197; ASP-235; CYS-266; ARG-272 AND CYS-329.
PubMed=25538239; DOI=10.1074/jbc.M114.627406;
Sankhala R.S., Koksal A.C., Ho L., Nitschke F., Minassian B.A.,
Cingolani G.;
"Dimeric quaternary structure of human laforin.";
J. Biol. Chem. 290:4552-4559(2015).
[34] {ECO:0000244|PDB:4RKK}
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-329 IN COMPLEX WITH
MALTOHEXAOSE AND PHOSPHATE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT,
MUTAGENESIS OF VAL-8; LYS-87; TRP-99; ILE-126; THR-142; ASP-197;
MET-236 AND CYS-266, AND CHARACTERIZATION OF VARIANTS EPM2 GLY-32;
HIS-171; SER-240; ASN-294 AND LEU-301.
PubMed=25544560; DOI=10.1016/j.molcel.2014.11.020;
Raththagala M., Brewer M.K., Parker M.W., Sherwood A.R., Wong B.K.,
Hsu S., Bridges T.M., Paasch B.C., Hellman L.M., Husodo S.,
Meekins D.A., Taylor A.O., Turner B.D., Auger K.D., Dukhande V.V.,
Chakravarthy S., Sanz P., Woods V.L. Jr., Li S., Vander Kooi C.W.,
Gentry M.S.;
"Structural mechanism of laforin function in glycogen
dephosphorylation and lafora disease.";
Mol. Cell 57:261-272(2015).
[35]
VARIANTS EPM2 LEU-84; SER-240 AND LEU-301.
PubMed=11175283; DOI=10.1038/sj.ejhg.5200571;
Gomez-Garre P., Sanz Y., Rodriguez de Cordoba S.R., Serratosa J.M.;
"Mutational spectrum of the EPM2A gene in progressive myoclonus
epilepsy of Lafora: high degree of allelic heterogeneity and
prevalence of deletions.";
Eur. J. Hum. Genet. 8:946-954(2000).
[36]
VARIANT PRO-46.
PubMed=11735300; DOI=10.1006/mcpr.2001.0371;
Ganesh S., Shoda K., Amano K., Uchiyama A., Kumada S., Moriyama N.,
Hirose S., Yamakawa K.;
"Mutation screening for Japanese Lafora's disease patients:
identification of novel sequence variants in the coding and upstream
regulatory regions of EPM2A gene.";
Mol. Cell. Probes 15:281-289(2001).
[37]
VARIANTS EPM2 PRO-25; CYS-108; HIS-171 AND LEU-293, AND
CHARACTERIZATION OF VARIANTS EPM2 GLY-32; CYS-108; ILE-194; SER-279
AND ASN-294.
PubMed=12019207; DOI=10.1093/hmg/11.11.1263;
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.;
"Genotype-phenotype correlations for EPM2A mutations in Lafora's
progressive myoclonus epilepsy: exon 1 mutations associate with an
early-onset cognitive deficit subphenotype.";
Hum. Mol. Genet. 11:1263-1271(2002).
[38]
VARIANT EPM2 ALA-187.
PubMed=12560877; DOI=10.1007/s100380300006;
Ki C.S., Kong S.Y., Seo D.W., Hong S.B., Kim H.J., Kim J.W.;
"Two novel mutations in the EPM2A gene in a Korean patient with
Lafora's progressive myoclonus epilepsy.";
J. Hum. Genet. 48:51-54(2003).
[39]
VARIANT EPM2 PRO-91.
PubMed=15009235; DOI=10.1111/j.0013-9580.2004.33203.x;
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.;
"A novel exon 1 mutation in a patient with atypical Lafora progressive
myoclonus epilepsy seen as childhood-onset cognitive deficit.";
Epilepsia 45:294-295(2004).
[40]
VARIANTS EPM2 PRO-91; HIS-171 AND SER-279, CATALYTIC ACTIVITY, AND
SUBCELLULAR LOCATION.
PubMed=14722920; DOI=10.1002/humu.10306;
Ianzano L., Young E.J., Zhao X.C., Chan E.M., Rodriguez M.T.,
Torrado M.V., Scherer S.W., Minassian B.A.;
"Loss of function of the cytoplasmic isoform of the protein laforin
(EPM2A) causes Lafora progressive myoclonus epilepsy.";
Hum. Mutat. 23:170-176(2004).
[41]
VARIANT PRO-46.
PubMed=16021330; DOI=10.1007/s10038-005-0263-7;
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.;
"Mutations in the NHLRC1 gene are the common cause for Lafora disease
in the Japanese population.";
J. Hum. Genet. 50:347-352(2005).
[42]
VARIANTS EPM2 ASN-140; TYR-148; LYS-210 AND TRP-310, CHARACTERIZATION
OF VARIANT EPM2 TRP-310, AND SUBCELLULAR LOCATION.
PubMed=18311786; DOI=10.1002/humu.20737;
Singh S., Satishchandra P., Shankar S.K., Ganesh S.;
"Lafora disease in the Indian population: EPM2A and NHLRC1 gene
mutations and their impact on subcellular localization of laforin and
malin.";
Hum. Mutat. 29:E1-12(2008).
-!- FUNCTION: Plays an important role in preventing glycogen
hyperphosphorylation and the formation of insoluble aggregates,
via its activity as glycogen phosphatase, and by promoting the
ubiquitination of proteins involved in glycogen metabolism via its
interaction with the E3 ubiquitin ligase NHLRC1/malin. Shows
strong phosphatase activity towards complex carbohydrates in
vitro, avoiding glycogen hyperphosphorylation which is associated
with reduced branching and formation of insoluble aggregates
(PubMed:16901901, PubMed:23922729, PubMed:26231210,
PubMed:25538239, PubMed:25544560). Dephosphorylates
phosphotyrosine and synthetic substrates, such as para-
nitrophenylphosphate (pNPP), and has low activity with
phosphoserine and phosphothreonine substrates (in vitro)
(PubMed:11001928, PubMed:11220751, PubMed:11739371,
PubMed:14532330, PubMed:16971387, PubMed:18617530,
PubMed:22036712, PubMed:23922729, PubMed:14722920). Has been shown
to dephosphorylate MAPT (By similarity). 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
(PubMed:23922729). Also promotes proteasome-independent protein
degradation through the macroautophagy pathway (PubMed:20453062).
{ECO:0000250|UniProtKB:Q9WUA5, ECO:0000269|PubMed:11001928,
ECO:0000269|PubMed:11220751, ECO:0000269|PubMed:11739371,
ECO:0000269|PubMed:14532330, ECO:0000269|PubMed:14722920,
ECO:0000269|PubMed:16901901, ECO:0000269|PubMed:16971387,
ECO:0000269|PubMed:18070875, ECO:0000269|PubMed:18617530,
ECO:0000269|PubMed:19036738, ECO:0000269|PubMed:20453062,
ECO:0000269|PubMed:22036712, ECO:0000269|PubMed:23624058,
ECO:0000269|PubMed:23922729, ECO:0000269|PubMed:25538239,
ECO:0000269|PubMed:25544560, ECO:0000269|PubMed:26231210}.
-!- FUNCTION: Isoform 2: does not bind to glycogen (PubMed:18617530).
Lacks phosphatase activity and might function as a dominant-
negative regulator for the phosphatase activity of isoform 1 and
isoform 7 (PubMed:18617530, PubMed:22036712).
{ECO:0000269|PubMed:18617530, ECO:0000269|PubMed:22036712}.
-!- FUNCTION: Isoform 7: has phosphatase activity (in vitro).
{ECO:0000269|PubMed:22036712}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:11220751}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
{ECO:0000305|PubMed:11001928}.
-!- SUBUNIT: Homodimer (PubMed:16971387, PubMed:18617530,
PubMed:23922729, PubMed:25538239, PubMed:25544560). Interacts with
itself (PubMed:14532330). Interacts with PPP1R3B, PPP1R3C,
PPP1R3D, HIRIP5, and EPM2AIP1 (PubMed:12782127, PubMed:12915448,
PubMed:14532330, PubMed:16901901, PubMed:18070875). Binds glycogen
and Lafora bodies (PubMed:11739371, PubMed:14532330,
PubMed:14706656, PubMed:15102711, PubMed:18617530,
PubMed:22036712). Interacts with NHLRC1/malin (via the NHL
repeats) (PubMed:15930137, PubMed:22036712, PubMed:23922729).
Forms a complex with NHLRC1/malin and HSP70 (PubMed:19036738).
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 (PubMed:19542233). Isoform 1 and
isoform 2 interact to form a heterodimeric complex that lacks
phosphatase activity (in vitro) (PubMed:18617530). Active
phosphatase isoform 7 and isoform 1 interact with each other, but
give rise to lower phosphatase activity than isoform 1 or isoform
7 by themselves (in vitro) (PubMed:22036712). Active phosphatase
isoform 7 and inactive isoform 2 interact with each other, but
give rise to lower phosphatase activity than isoform 7 by itself
(in vitro) (PubMed:22036712). Interacts with PRDM8
(PubMed:22961547). {ECO:0000269|PubMed:11739371,
ECO:0000269|PubMed:12782127, ECO:0000269|PubMed:12915448,
ECO:0000269|PubMed:14532330, ECO:0000269|PubMed:14706656,
ECO:0000269|PubMed:15102711, ECO:0000269|PubMed:15930137,
ECO:0000269|PubMed:16901901, ECO:0000269|PubMed:16971387,
ECO:0000269|PubMed:18070875, ECO:0000269|PubMed:18617530,
ECO:0000269|PubMed:19542233, ECO:0000269|PubMed:22036712,
ECO:0000269|PubMed:22961547, ECO:0000269|PubMed:23624058,
ECO:0000269|PubMed:23922729, ECO:0000269|PubMed:25538239,
ECO:0000269|PubMed:25544560}.
-!- INTERACTION:
Q6VVB1:NHLRC1; NbExp=7; IntAct=EBI-2506661, EBI-6426628;
Q9UQK1:PPP1R3C; NbExp=5; IntAct=EBI-2506661, EBI-2506727;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11001928,
ECO:0000269|PubMed:11220751, ECO:0000269|PubMed:11739371,
ECO:0000269|PubMed:15102711, ECO:0000269|PubMed:17908927}.
Note=Under glycogenolytic conditions localizes to the nucleus.
{ECO:0000269|PubMed:17908927}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm
{ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:11739371,
ECO:0000269|PubMed:11883934, ECO:0000269|PubMed:14532330,
ECO:0000269|PubMed:18311786, ECO:0000269|PubMed:18617530,
ECO:0000269|PubMed:22036712}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:14722920,
ECO:0000269|PubMed:18311786}; Peripheral membrane protein
{ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:18311786};
Cytoplasmic side {ECO:0000269|PubMed:11001928,
ECO:0000269|PubMed:18311786}. Cell membrane
{ECO:0000269|PubMed:11220751}. Note=Colocalizes with glycogen
synthase in punctate structures in the cytoplasm (PubMed:11739371,
PubMed:14532330). Primarily associated with polyribosomes at the
rough endoplasmic reticulum, and also detected at the plasma
membrane (PubMed:11001928, PubMed:11220751, PubMed:11883934,
PubMed:18311786). {ECO:0000269|PubMed:11001928,
ECO:0000269|PubMed:11220751, ECO:0000269|PubMed:11739371,
ECO:0000269|PubMed:11883934, ECO:0000269|PubMed:14532330,
ECO:0000269|PubMed:18311786}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:18617530}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:11883934}; Peripheral membrane protein
{ECO:0000269|PubMed:11883934}; Cytoplasmic side
{ECO:0000269|PubMed:11883934}. Cell membrane
{ECO:0000269|PubMed:11883934}. Nucleus
{ECO:0000269|PubMed:11883934, ECO:0000269|PubMed:14722920,
ECO:0000269|PubMed:18617530}. Note=Also found in the nucleus.
{ECO:0000269|PubMed:11883934, ECO:0000269|PubMed:18617530}.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm
{ECO:0000269|PubMed:22036712}. Nucleus
{ECO:0000269|PubMed:22036712}.
-!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm
{ECO:0000269|PubMed:22036712}. Nucleus
{ECO:0000269|PubMed:22036712}.
-!- SUBCELLULAR LOCATION: Isoform 7: Cytoplasm
{ECO:0000269|PubMed:22036712}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=8;
Name=1; Synonyms=A, LDH1 {ECO:0000303|PubMed:11883934}, Laf331
{ECO:0000303|PubMed:22036712};
IsoId=O95278-1; Sequence=Displayed;
Name=2; Synonyms=B, C-terISO, Laf317
{ECO:0000303|PubMed:22036712};
IsoId=O95278-2; Sequence=VSP_011017, VSP_011018;
Note=Produced by alternative splicing.;
Name=4; Synonyms=Laf152 {ECO:0000303|PubMed:22036712};
IsoId=O95278-4; Sequence=VSP_011015, VSP_011016;
Note=Produced by alternative splicing. May be due to an intron
retention.;
Name=5; Synonyms=Laf224 {ECO:0000303|PubMed:22036712};
IsoId=O95278-5; Sequence=VSP_042496, VSP_042497;
Note=Produced by alternative splicing.;
Name=6; Synonyms=Laf88 {ECO:0000303|PubMed:22036712};
IsoId=O95278-6; Sequence=VSP_042494;
Note=Produced by alternative initiation at Met-244 of isoform 1.
Transcript amplified but protein not detected.
{ECO:0000269|PubMed:22036712};
Name=7; Synonyms=Laf177 {ECO:0000303|PubMed:22036712};
IsoId=O95278-7; Sequence=VSP_042495;
Note=Produced by alternative splicing. Active phosphatase.
{ECO:0000269|PubMed:22036712};
Name=8;
IsoId=O95278-8; Sequence=VSP_042493;
Note=Produced by alternative splicing. No experimental
confirmation available.;
Name=9; Synonyms=POCR {ECO:0000303|PubMed:22036712};
IsoId=B3EWF7-1; Sequence=External;
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.;
-!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, kidney,
pancreas and brain. Isoform 4 is also expressed in the placenta.
{ECO:0000269|PubMed:14532330, ECO:0000269|PubMed:9771710}.
-!- DOMAIN: The CBM20 domain mediates binding to cytoplasmic glycogen
and to Lafora polyglucosan bodies. {ECO:0000269|PubMed:11739371,
ECO:0000269|PubMed:14706656}.
-!- PTM: Polyubiquitinated by NHLRC1/malin.
{ECO:0000269|PubMed:15930137}.
-!- PTM: 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.
{ECO:0000269|PubMed:21728993}.
-!- DISEASE: 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. {ECO:0000269|PubMed:11001928,
ECO:0000269|PubMed:11175283, ECO:0000269|PubMed:11739371,
ECO:0000269|PubMed:12019207, ECO:0000269|PubMed:12560877,
ECO:0000269|PubMed:14532330, ECO:0000269|PubMed:14706656,
ECO:0000269|PubMed:14722920, ECO:0000269|PubMed:15009235,
ECO:0000269|PubMed:18311786, ECO:0000269|PubMed:25544560,
ECO:0000269|PubMed:26231210, ECO:0000269|PubMed:9771710,
ECO:0000269|PubMed:9931343}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAO15523.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=BAG51107.1; Type=Frameshift; Positions=223; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=The Lafora progressive myoclonus epilepsy
mutation and polymorphism database;
URL="http://projects.tcag.ca/lafora/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF084535; AAC83347.2; -; mRNA.
EMBL; AF284580; AAG18377.1; -; mRNA.
EMBL; AF454491; AAO15523.1; ALT_SEQ; mRNA.
EMBL; AF454492; AAO15524.1; -; mRNA.
EMBL; AF454493; AAO15525.1; -; mRNA.
EMBL; AF454494; AAO15526.1; -; mRNA.
EMBL; AK022721; BAG51107.1; ALT_FRAME; mRNA.
EMBL; AK299497; BAG61454.1; -; mRNA.
EMBL; AL023806; CAI21419.1; -; Genomic_DNA.
EMBL; AL365193; CAI21419.1; JOINED; Genomic_DNA.
EMBL; AL365193; CAI21675.1; -; Genomic_DNA.
EMBL; AL023806; CAI21675.1; JOINED; Genomic_DNA.
EMBL; CH471051; EAW47844.1; -; Genomic_DNA.
EMBL; BC005286; AAH05286.1; -; mRNA.
EMBL; BC070047; AAH70047.1; -; mRNA.
EMBL; AJ130763; CAA10199.1; -; mRNA.
EMBL; AJ130764; CAA10200.1; -; mRNA.
CCDS; CCDS5206.1; -. [O95278-1]
RefSeq; NP_001018051.1; NM_001018041.1. [O95278-2]
RefSeq; NP_005661.1; NM_005670.3. [O95278-1]
RefSeq; XP_006715627.1; XM_006715564.3. [O95278-5]
RefSeq; XP_011534418.1; XM_011536116.1. [O95278-8]
RefSeq; XP_016866789.1; XM_017011300.1. [O95278-7]
RefSeq; XP_016866790.1; XM_017011301.1. [O95278-7]
RefSeq; XP_016866791.1; XM_017011302.1. [O95278-7]
UniGene; Hs.486696; -.
PDB; 4R30; X-ray; 2.30 A; A/B/C/D=148-331.
PDB; 4RKK; X-ray; 2.40 A; A/C=1-329.
PDBsum; 4R30; -.
PDBsum; 4RKK; -.
ProteinModelPortal; O95278; -.
SMR; O95278; -.
BioGrid; 113679; 23.
IntAct; O95278; 5.
STRING; 9606.ENSP00000356489; -.
BindingDB; O95278; -.
ChEMBL; CHEMBL2311242; -.
CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DEPOD; O95278; -.
iPTMnet; O95278; -.
PhosphoSitePlus; O95278; -.
BioMuta; RNF213; -.
PaxDb; O95278; -.
PeptideAtlas; O95278; -.
PRIDE; O95278; -.
DNASU; 7957; -.
Ensembl; ENST00000367519; ENSP00000356489; ENSG00000112425. [O95278-1]
Ensembl; ENST00000435470; ENSP00000405913; ENSG00000112425. [O95278-2]
Ensembl; ENST00000611340; ENSP00000480268; ENSG00000112425. [O95278-8]
Ensembl; ENST00000618445; ENSP00000480339; ENSG00000112425. [O95278-2]
Ensembl; ENST00000638262; ENSP00000492876; ENSG00000112425. [O95278-5]
Ensembl; ENST00000638778; ENSP00000491353; ENSG00000112425. [O95278-8]
Ensembl; ENST00000638783; ENSP00000491338; ENSG00000112425. [O95278-8]
Ensembl; ENST00000639423; ENSP00000492701; ENSG00000112425. [O95278-8]
Ensembl; ENST00000639465; ENSP00000491180; ENSG00000112425. [O95278-8]
GeneID; 7957; -.
KEGG; hsa:7957; -.
UCSC; uc003qkw.4; human. [O95278-1]
CTD; 7957; -.
DisGeNET; 7957; -.
EuPathDB; HostDB:ENSG00000112425.13; -.
GeneCards; EPM2A; -.
GeneReviews; EPM2A; -.
HGNC; HGNC:3413; EPM2A.
HPA; HPA053643; -.
HPA; HPA055468; -.
MalaCards; EPM2A; -.
MIM; 254780; phenotype.
MIM; 607566; gene.
neXtProt; NX_O95278; -.
OpenTargets; ENSG00000112425; -.
Orphanet; 501; Lafora disease.
PharmGKB; PA27832; -.
eggNOG; KOG1716; Eukaryota.
eggNOG; COG2453; LUCA.
GeneTree; ENSGT00390000010101; -.
HOGENOM; HOG000285975; -.
HOVERGEN; HBG051493; -.
KO; K14165; -.
OMA; GHTDEMK; -.
OrthoDB; EOG091G0GBM; -.
PhylomeDB; O95278; -.
TreeFam; TF332841; -.
BRENDA; 3.1.3.16; 2681.
Reactome; R-HSA-3322077; Glycogen synthesis.
Reactome; R-HSA-3785653; Myoclonic epilepsy of Lafora.
SIGNOR; O95278; -.
ChiTaRS; EPM2A; human.
GenomeRNAi; 7957; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112425; -.
CleanEx; HS_EPM2A; -.
ExpressionAtlas; O95278; baseline and differential.
Genevisible; O95278; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0098556; C:cytoplasmic side of rough endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
GO; GO:0019203; F:carbohydrate phosphatase activity; IDA:UniProtKB.
GO; GO:2001069; F:glycogen binding; IDA:UniProtKB.
GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:2001070; F:starch binding; IEA:InterPro.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
GO; GO:0005978; P:glycogen biosynthetic process; TAS:Reactome.
GO; GO:0005977; P:glycogen metabolic process; IMP:UniProtKB.
GO; GO:0046959; P:habituation; IEA:Ensembl.
GO; GO:0035305; P:negative regulation of dephosphorylation; IDA:UniProtKB.
GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
GO; GO:0007399; P:nervous system development; IEA:Ensembl.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:UniProtKB.
GO; GO:0046838; P:phosphorylated carbohydrate dephosphorylation; IDA:UniProtKB.
GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
CDD; cd05806; CBM20_laforin; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR013784; Carb-bd-like_fold.
InterPro; IPR034831; CBM20_laforin.
InterPro; IPR002044; CBM_fam20.
InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
InterPro; IPR024950; DUSP.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
PANTHER; PTHR10159; PTHR10159; 1.
Pfam; PF00686; CBM_20; 1.
Pfam; PF00782; DSPc; 1.
SMART; SM01065; CBM_2; 1.
SMART; SM00195; DSPc; 1.
SUPFAM; SSF49452; SSF49452; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS51166; CBM20; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Alternative splicing; Autophagy;
Carbohydrate metabolism; Cell membrane; Complete proteome; Cytoplasm;
Disease mutation; Endoplasmic reticulum; Epilepsy;
Glycogen metabolism; Glycogen storage disease; Hydrolase; Membrane;
Nucleus; Phosphoprotein; Polymorphism; Protein phosphatase;
Reference proteome; Ubl conjugation.
CHAIN 1 331 Laforin.
/FTId=PRO_0000094838.
DOMAIN 1 124 CBM20. {ECO:0000255|PROSITE-
ProRule:PRU00594}.
DOMAIN 243 311 Tyrosine-protein phosphatase.
REGION 103 107 Substrate binding. {ECO:0000244|PDB:4RKK,
ECO:0000269|PubMed:25544560}.
REGION 267 272 Substrate binding. {ECO:0000244|PDB:4RKK,
ECO:0000269|PubMed:25544560}.
MOTIF 266 272 Glucan phosphatase signature motif
CXAGXGR. {ECO:0000305|PubMed:25544560,
ECO:0000305|PubMed:26231210}.
ACT_SITE 266 266 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000305|PubMed:11220751,
ECO:0000305|PubMed:11739371,
ECO:0000305|PubMed:14532330,
ECO:0000305|PubMed:22036712,
ECO:0000305|PubMed:25538239,
ECO:0000305|PubMed:25544560}.
BINDING 32 32 Substrate. {ECO:0000244|PDB:4RKK,
ECO:0000269|PubMed:25544560}.
BINDING 87 87 Substrate. {ECO:0000244|PDB:4RKK,
ECO:0000269|PubMed:25544560}.
BINDING 197 197 Substrate. {ECO:0000244|PDB:4RKK,
ECO:0000269|PubMed:25544560}.
BINDING 235 235 Substrate. {ECO:0000244|PDB:4RKK,
ECO:0000269|PubMed:25544560}.
BINDING 241 241 Substrate. {ECO:0000244|PDB:4RKK,
ECO:0000269|PubMed:25544560}.
BINDING 304 304 Substrate. {ECO:0000244|PDB:4RKK,
ECO:0000269|PubMed:25544560}.
SITE 329 329 Required for homodimerization.
{ECO:0000269|PubMed:23922729}.
MOD_RES 25 25 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:21728993}.
VAR_SEQ 1 243 Missing (in isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042494.
VAR_SEQ 1 159 MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLR
PAGTAAGDGALALQEPGLWLGEVELAAEEAAQDGAEPGRVD
TFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDGVYC
LPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSR -> M
IFNK (in isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042495.
VAR_SEQ 1 138 Missing (in isoform 8).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.4}.
/FTId=VSP_042493.
VAR_SEQ 102 199 NGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHT
TDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHVTIKLKHE
LGITAVMNFQTEWDIV -> IASRRLPPAQSGSSGPHPQPG
PRPRAGPAGPGGARPGLFARVPAHSPGDLG (in
isoform 4). {ECO:0000303|Ref.4}.
/FTId=VSP_011015.
VAR_SEQ 160 293 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_042496.
VAR_SEQ 200 331 Missing (in isoform 4).
{ECO:0000303|Ref.4}.
/FTId=VSP_011016.
VAR_SEQ 294 331 YFLMAKRPAVYIDEEALARAQEDFFQKFGKVRSSVCSL ->
PSTDAAPGGVPAACAAGEGTHRVRALQRWGGPLHRGCLRLA
PVCDGLESEEGAVFPHGQEAGCLH (in isoform 5).
{ECO:0000305}.
/FTId=VSP_042497.
VAR_SEQ 310 320 LARAQEDFFQK -> ASQDTFPL (in isoform 2).
{ECO:0000303|PubMed:9771710,
ECO:0000303|PubMed:9931343}.
/FTId=VSP_011017.
VAR_SEQ 321 331 Missing (in isoform 2).
{ECO:0000303|PubMed:9771710,
ECO:0000303|PubMed:9931343}.
/FTId=VSP_011018.
VARIANT 25 25 S -> P (in EPM2; atypical form; does not
affect glycogen binding).
{ECO:0000269|PubMed:12019207,
ECO:0000269|PubMed:14706656}.
/FTId=VAR_019465.
VARIANT 28 28 E -> K (in EPM2; does not affect glycogen
binding). {ECO:0000269|PubMed:14706656}.
/FTId=VAR_019466.
VARIANT 32 32 W -> G (in EPM2; impairs protein
stability; affects phosphatase activity;
abolishes glycogen binding; abolishes
phosphatase activity with insoluble
glucan; disrupts the interaction with
PPP1R3C; dbSNP:rs104893955).
{ECO:0000269|PubMed:11739371,
ECO:0000269|PubMed:12019207,
ECO:0000269|PubMed:14532330,
ECO:0000269|PubMed:14706656,
ECO:0000269|PubMed:25544560,
ECO:0000269|PubMed:26231210}.
/FTId=VAR_019467.
VARIANT 46 46 A -> P (does not affect glycogen binding;
dbSNP:rs374338349).
{ECO:0000269|PubMed:11735300,
ECO:0000269|PubMed:14706656,
ECO:0000269|PubMed:16021330}.
/FTId=VAR_019468.
VARIANT 84 84 F -> L (in EPM2; affects phosphatase
activity and glycogen binding; disrupts
the interaction with PPP1R3C).
{ECO:0000269|PubMed:11175283,
ECO:0000269|PubMed:14532330}.
/FTId=VAR_019469.
VARIANT 88 88 F -> L (in EPM2; does not affect glycogen
binding). {ECO:0000269|PubMed:14706656}.
/FTId=VAR_019470.
VARIANT 91 91 R -> P (in EPM2; atypical form; learning
difficuties with childhood-onset).
{ECO:0000269|PubMed:14722920,
ECO:0000269|PubMed:15009235}.
/FTId=VAR_019471.
VARIANT 108 108 R -> C (in EPM2; loss of phosphatase
activity; reduced self-interaction
capacity; disrupts the interaction with
PPP1R3C; dbSNP:rs137852915).
{ECO:0000269|PubMed:12019207,
ECO:0000269|PubMed:14532330,
ECO:0000269|PubMed:9771710}.
/FTId=VAR_019472.
VARIANT 114 114 E -> D. {ECO:0000269|PubMed:9771710}.
/FTId=VAR_019473.
VARIANT 140 140 K -> N (in EPM2).
{ECO:0000269|PubMed:18311786}.
/FTId=VAR_046383.
VARIANT 148 148 N -> Y (in EPM2).
{ECO:0000269|PubMed:18311786}.
/FTId=VAR_046384.
VARIANT 171 171 R -> H (in EPM2; results in ubiquitin-
positive perinuclear aggregates; no
effect on glycogen binding; abolishes
phosphatase activity; may affect proper
folding; dbSNP:rs137852916).
{ECO:0000269|PubMed:11001928,
ECO:0000269|PubMed:12019207,
ECO:0000269|PubMed:14722920,
ECO:0000269|PubMed:25544560,
ECO:0000269|PubMed:9931343}.
/FTId=VAR_019474.
VARIANT 187 187 T -> A (in EPM2; abolishes interaction
with NHLRC1).
{ECO:0000269|PubMed:12560877}.
/FTId=VAR_019475.
VARIANT 194 194 T -> 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;
dbSNP:rs375544596).
{ECO:0000269|PubMed:12019207,
ECO:0000269|PubMed:14532330,
ECO:0000269|PubMed:9931343}.
/FTId=VAR_019476.
VARIANT 210 210 E -> K (in EPM2).
{ECO:0000269|PubMed:18311786}.
/FTId=VAR_046385.
VARIANT 240 240 G -> S (in EPM2; impaired phosphatase
activity; does not affect glycogen
binding; disrupts the interaction with
PPP1R3C). {ECO:0000269|PubMed:11175283,
ECO:0000269|PubMed:14532330,
ECO:0000269|PubMed:25544560}.
/FTId=VAR_019477.
VARIANT 279 279 G -> S (in EPM2; results in ubiquitin-
positive perinuclear aggregates; loss of
phosphatase activity; affects glycogen
binding; disrupts the interaction with
PPP1R3C; dbSNP:rs137852917).
{ECO:0000269|PubMed:12019207,
ECO:0000269|PubMed:14532330,
ECO:0000269|PubMed:14722920,
ECO:0000269|PubMed:9771710,
ECO:0000269|PubMed:9931343}.
/FTId=VAR_019478.
VARIANT 293 293 Q -> 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; dbSNP:rs796052427).
{ECO:0000269|PubMed:11001928,
ECO:0000269|PubMed:12019207,
ECO:0000269|PubMed:14532330,
ECO:0000269|PubMed:9771710}.
/FTId=VAR_019479.
VARIANT 294 294 Y -> N (in EPM2; results in ubiquitin-
positive perinuclear aggregates; impairs
phosphatase activity; affects glycogen
binding; disrupts the interaction with
PPP1R3C). {ECO:0000269|PubMed:12019207,
ECO:0000269|PubMed:14532330,
ECO:0000269|PubMed:25544560,
ECO:0000269|PubMed:9931343}.
/FTId=VAR_019480.
VARIANT 301 301 P -> L (in EPM2; impairs protein
stability; impairs phosphatase activity;
affects glycogen binding; disrupts the
interaction with PPP1R3C;
dbSNP:rs796052428).
{ECO:0000269|PubMed:11175283,
ECO:0000269|PubMed:14532330,
ECO:0000269|PubMed:25544560}.
/FTId=VAR_019481.
VARIANT 310 310 L -> W (in EPM2; causes location of
isoform 1 at cytoplasmic punctae; does
not affect homodimerization of isoform 1
but prevents heterodimerization of
isoform 1 and isoform 2).
{ECO:0000269|PubMed:18311786}.
/FTId=VAR_046386.
MUTAGEN 8 8 V->A: Loss of phosphatase activity. No
effect on glycogen binding.
{ECO:0000269|PubMed:25544560}.
MUTAGEN 25 25 S->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.
{ECO:0000269|PubMed:21728993}.
MUTAGEN 25 25 S->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.
{ECO:0000269|PubMed:21728993}.
MUTAGEN 87 87 K->A: Loss of phosphatase activity.
Abolishes glycogen binding.
{ECO:0000269|PubMed:11739371,
ECO:0000269|PubMed:25544560}.
MUTAGEN 99 99 W->A: Strongly reduces phosphatase
activity. Strongly reduces glycogen
binding. {ECO:0000269|PubMed:25544560}.
MUTAGEN 109 110 CC->SS: No effect on homodimerization or
carbohydrate binding. Decreased
phosphatase activity.
{ECO:0000269|PubMed:23922729}.
MUTAGEN 123 123 C->S: No effect on homodimerization or
carbohydrate binding. Decreased
phosphatase activity.
{ECO:0000269|PubMed:23922729}.
MUTAGEN 126 126 I->T: Strongly decreased phosphatase
activity. No effect on glycogen binding.
{ECO:0000269|PubMed:25544560}.
MUTAGEN 142 142 T->A: Strongly decreased phosphatase
activity. No effect on glycogen binding.
{ECO:0000269|PubMed:25544560}.
MUTAGEN 168 168 S->A,D: Abolishes interaction with
NHLRC1. {ECO:0000269|PubMed:21728993}.
MUTAGEN 169 169 C->S: No effect on homodimerization or
carbohydrate binding. Decreased
phosphatase activity.
{ECO:0000269|PubMed:23922729}.
MUTAGEN 169 169 C->S: No effect on phosphatase activity.
{ECO:0000269|PubMed:25538239}.
MUTAGEN 171 171 R->A: No effect on phosphatase activity.
{ECO:0000269|PubMed:25538239}.
MUTAGEN 187 187 T->D: Abolishes interaction with NHLRC1.
{ECO:0000269|PubMed:21728993}.
MUTAGEN 194 194 T->D: Does not affect interaction with
NHLRC1, PPP1R3C or PRKAA2.
{ECO:0000269|PubMed:21728993}.
MUTAGEN 197 197 D->A: Strongly decreased phosphatase
activity. No effect on glycogen binding.
{ECO:0000269|PubMed:25538239,
ECO:0000269|PubMed:25544560}.
MUTAGEN 205 205 C->S: No effect on homodimerization or
carbohydrate binding. Decreased
phosphatase activity.
{ECO:0000269|PubMed:23922729}.
MUTAGEN 235 235 D->A: Complete loss of phosphatase
activity. Does not affect glycogen
binding. {ECO:0000269|PubMed:14532330,
ECO:0000269|PubMed:25538239}.
MUTAGEN 236 236 M->A: Complete loss of phosphatase
activity. No effect on glycogen binding.
{ECO:0000269|PubMed:25544560}.
MUTAGEN 250 250 C->S: No effect on homodimerization or
carbohydrate binding. Decreased
phosphatase activity.
{ECO:0000269|PubMed:23922729}.
MUTAGEN 251 251 L->A: Impairs protein stability. Strongly
reduces phosphatase activity. No effect
on glycogen binding.
{ECO:0000269|PubMed:25544560}.
MUTAGEN 266 266 C->S: Complete loss of phosphatase
activity. Does not affect glycogen
binding. Does not affect self-
interaction. Increases the interaction
with PPP1R3C.
{ECO:0000269|PubMed:11220751,
ECO:0000269|PubMed:11739371,
ECO:0000269|PubMed:14532330,
ECO:0000269|PubMed:22036712,
ECO:0000269|PubMed:23922729,
ECO:0000269|PubMed:25538239,
ECO:0000269|PubMed:25544560}.
MUTAGEN 272 272 R->A: Complete loss of phosphatase
activity. {ECO:0000269|PubMed:25538239}.
MUTAGEN 321 321 F->S: Impairs protein stability. Strongly
reduces phosphatase activity. No effect
on glycogen binding.
{ECO:0000269|PubMed:25544560}.
MUTAGEN 329 331 Missing: Fails to homodimerize. Does not
affect carbohydrate binding or
phosphatase activity.
{ECO:0000269|PubMed:23922729}.
MUTAGEN 329 329 C->S: Fails to homodimerize. Does not
affect carbohydrate binding, interaction
with NHLRC1, phosphatase activity, or
ubiquitination by NHLRC1.
{ECO:0000269|PubMed:23922729}.
MUTAGEN 329 329 C->S: No effect on homodimerization.
{ECO:0000269|PubMed:25538239}.
CONFLICT 193 193 Q -> K (in Ref. 8; AAH70047).
{ECO:0000305}.
CONFLICT 248 248 A -> P (in Ref. 4; AAO15523).
{ECO:0000305}.
CONFLICT 258 258 K -> E (in Ref. 5; BAG61454).
{ECO:0000305}.
CONFLICT 294 294 Y -> H (in Ref. 5; BAG61454).
{ECO:0000305}.
STRAND 1 9 {ECO:0000244|PDB:4RKK}.
HELIX 11 14 {ECO:0000244|PDB:4RKK}.
STRAND 19 26 {ECO:0000244|PDB:4RKK}.
HELIX 27 29 {ECO:0000244|PDB:4RKK}.
TURN 30 32 {ECO:0000244|PDB:4RKK}.
HELIX 34 36 {ECO:0000244|PDB:4RKK}.
STRAND 58 67 {ECO:0000244|PDB:4RKK}.
STRAND 84 91 {ECO:0000244|PDB:4RKK}.
STRAND 97 103 {ECO:0000244|PDB:4RKK}.
HELIX 104 106 {ECO:0000244|PDB:4RKK}.
STRAND 108 110 {ECO:0000244|PDB:4RKK}.
HELIX 114 116 {ECO:0000244|PDB:4RKK}.
STRAND 121 123 {ECO:0000244|PDB:4RKK}.
HELIX 138 151 {ECO:0000244|PDB:4RKK}.
STRAND 157 161 {ECO:0000244|PDB:4R30}.
STRAND 164 167 {ECO:0000244|PDB:4R30}.
HELIX 173 177 {ECO:0000244|PDB:4R30}.
HELIX 178 183 {ECO:0000244|PDB:4R30}.
STRAND 188 191 {ECO:0000244|PDB:4R30}.
HELIX 195 201 {ECO:0000244|PDB:4R30}.
HELIX 203 205 {ECO:0000244|PDB:4R30}.
STRAND 208 210 {ECO:0000244|PDB:4R30}.
HELIX 214 223 {ECO:0000244|PDB:4R30}.
STRAND 227 230 {ECO:0000244|PDB:4R30}.
HELIX 238 258 {ECO:0000244|PDB:4R30}.
STRAND 262 265 {ECO:0000244|PDB:4R30}.
HELIX 271 283 {ECO:0000244|PDB:4R30}.
HELIX 289 296 {ECO:0000244|PDB:4R30}.
STRAND 303 305 {ECO:0000244|PDB:4R30}.
HELIX 307 321 {ECO:0000244|PDB:4R30}.
SEQUENCE 331 AA; 37158 MW; DD79F917262AB458 CRC64;
MRFRFGVVVP PAVAGARPEL LVVGSRPELG RWEPRGAVRL RPAGTAAGDG ALALQEPGLW
LGEVELAAEE AAQDGAEPGR VDTFWYKFLK REPGGELSWE GNGPHHDRCC TYNENNLVDG
VYCLPIGHWI EATGHTNEMK HTTDFYFNIA GHQAMHYSRI LPNIWLGSCP RQVEHVTIKL
KHELGITAVM NFQTEWDIVQ NSSGCNRYPE PMTPDTMIKL YREEGLAYIW MPTPDMSTEG
RVQMLPQAVC LLHALLEKGH IVYVHCNAGV GRSTAAVCGW LQYVMGWNLR KVQYFLMAKR
PAVYIDEEAL ARAQEDFFQK FGKVRSSVCS L


Related products :

Catalog number Product name Quantity
EIAAB13124 Epm2a,Lafora PTPase,Laforin,LAFPTPase,Mouse,Mus musculus
EIAAB13122 Epm2a,Lafora PTPase,Laforin,LAFPTPase,Rat,Rattus norvegicus
20-372-60229 epilepsy. progressive myoclonus type 2A. Lafora disease (laforin) (EPM2A). transcript variant 1 - Mouse monoclonal anti-human EPM2A antibody; EC 3.1.3.48; EC 3.1.3.16; Lafora PTPase; LAFPTPase Monoclo 0.1 mg
EIAAB13123 EPM2A,Homo sapiens,Human,Lafora PTPase,Laforin,LAFPTPase
EIAAB13121 Canis familiaris,Canis lupus familiaris,Dog,EPM2A,Lafora PTPase,Laforin,LAFPTPase
EIAAB31954 ACP1,Adipocyte acid phosphatase,Homo sapiens,Human,LMW-PTP,LMW-PTPase,Low molecular weight cytosolic acid phosphatase,Low molecular weight phosphotyrosine protein phosphatase,Red cell acid phosphatase
EIAAB32113 Homo sapiens,Human,PP1G,PPP1R3A,Protein phosphatase 1 glycogen-associated regulatory subunit,Protein phosphatase 1 regulatory subunit 3A,Protein phosphatase type-1 glycogen targeting subunit,RG1
EIAAB32112 Oryctolagus cuniculus,PP1G,PPP1R3A,Protein phosphatase 1 glycogen-associated regulatory subunit,Protein phosphatase 1 regulatory subunit 3A,Protein phosphatase type-1 glycogen targeting subunit,Rabbit
EIAAB32111 Mouse,Mus musculus,Pp1g,Ppp1r3a,Protein phosphatase 1 glycogen-associated regulatory subunit,Protein phosphatase 1 regulatory subunit 3A,Protein phosphatase type-1 glycogen targeting subunit,RG1
EIAAB31957 Acp1,LMW-PTP,LMW-PTPase,Low molecular weight cytosolic acid phosphatase,Low molecular weight phosphotyrosine protein phosphatase,Mouse,Mus musculus
EIAAB31959 Acp1,LMW-PTP,LMW-PTPase,Low molecular weight cytosolic acid phosphatase,Low molecular weight phosphotyrosine protein phosphatase,Rat,Rattus norvegicus
EIAAB31958 ACP1,Bos taurus,Bovine,LMW-PTP,LMW-PTPase,Low molecular weight cytosolic acid phosphatase,Low molecular weight phosphotyrosine protein phosphatase
EIAAB31955 ACP1,LMW-PTP,LMW-PTPase,Low molecular weight cytosolic acid phosphatase,Low molecular weight phosphotyrosine protein phosphatase,Pig,Sus scrofa
EIAAB32114 33 kDa glycogen-binding protein,Hepatic glycogen-targeting protein phosphatase 1 regulatory subunit GL,PP1 subunit R4,Ppp1r3b,Ppp1r4,Protein phosphatase 1 regulatory subunit 3B,Protein phosphatase 1 r
EIAAB33103 GLEPP1,Glomerular epithelial protein 1,Homo sapiens,Human,Protein tyrosine phosphatase U2,PTPase U2,PTPRO,PTPU2,PTP-U2,Receptor-type tyrosine-protein phosphatase O,R-PTP-O
15-288-21480 Receptor-type tyrosine-protein phosphatase O - EC 3.1.3.48; Glomerular epithelial protein 1; Protein tyrosine phosphatase U2; PTPase U2; PTP-U2 Polyclonal 0.05 mg
15-288-21480 Receptor-type tyrosine-protein phosphatase O - EC 3.1.3.48; Glomerular epithelial protein 1; Protein tyrosine phosphatase U2; PTPase U2; PTP-U2 Polyclonal 0.1 mg
EIAAB31956 ACP1,Chicken,Gallus gallus,LMW-PTP,LMW-PTPase,Low molecular weight cytosolic acid phosphatase,Low molecular weight phosphotyrosine protein phosphatase,RCJMB04_11a4
EIAAB33058 Homo sapiens,Human,Protein-tyrosine phosphatase MEG2,PTPase MEG2,PTPN9,Tyrosine-protein phosphatase non-receptor type 9
EIAAB33047 Homo sapiens,Human,MEG,Protein-tyrosine phosphatase MEG1,PTPase-MEG1,PTPN4,Tyrosine-protein phosphatase non-receptor type 4
EIAAB33057 Mouse,Mus musculus,Protein-tyrosine phosphatase MEG2,PTPase MEG2,Ptpn9,Tyrosine-protein phosphatase non-receptor type 9
EPN1 EPM2A Gene epilepsy, progressive myoclonus type 2A, Lafora disease (laforin)
15-288-21491A Tyrosine-protein phosphatase non-receptor type 4 - EC 3.1.3.48; Protein-tyrosine phosphatase MEG1; PTPase-MEG1; MEG Polyclonal 0.1 mg
15-288-21491A Tyrosine-protein phosphatase non-receptor type 4 - EC 3.1.3.48; Protein-tyrosine phosphatase MEG1; PTPase-MEG1; MEG Polyclonal 0.05 mg
E12411663 Rat protein tyrosine phosphatase(PTP per PTPase) ELISA kit 1


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur