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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.
31-JUL-2019, entry version 167.
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:
Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein]
+ phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136,
Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:11220751};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999,
ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;
Evidence={ECO:0000305|PubMed:11001928};
-!- CATALYTIC ACTIVITY:
Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
EC=3.1.3.16; Evidence={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/";
-----------------------------------------------------------------------
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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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL365193; -; NOT_ANNOTATED_CDS; 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]
CCDS; CCDS87452.1; -. [O95278-8]
CCDS; CCDS87453.1; -. [O95278-5]
CCDS; CCDS87454.1; -. [O95278-2]
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.
RefSeq; XP_011534418.1; XM_011536116.1. [O95278-8]
RefSeq; XP_016866789.1; XM_017011300.1.
RefSeq; XP_016866790.1; XM_017011301.1. [O95278-7]
RefSeq; XP_016866791.1; XM_017011302.1. [O95278-7]
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; -.
SMR; O95278; -.
BioGrid; 113679; 24.
IntAct; O95278; 4.
STRING; 9606.ENSP00000356489; -.
BindingDB; O95278; -.
ChEMBL; CHEMBL2311242; -.
CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DEPOD; O95278; -.
iPTMnet; O95278; -.
PhosphoSitePlus; O95278; -.
BioMuta; EPM2A; -.
EPD; O95278; -.
jPOST; O95278; -.
PaxDb; O95278; -.
PeptideAtlas; O95278; -.
PRIDE; O95278; -.
ProteomicsDB; 50779; -. [O95278-1]
ProteomicsDB; 50780; -. [O95278-2]
ProteomicsDB; 50782; -. [O95278-4]
ProteomicsDB; 50783; -. [O95278-5]
ProteomicsDB; 50784; -. [O95278-6]
ProteomicsDB; 50785; -. [O95278-7]
ProteomicsDB; 50786; -. [O95278-8]
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]
Ensembl; ENST00000650914; ENSP00000498790; ENSG00000112425. [O95278-8]
GeneID; 7957; -.
KEGG; hsa:7957; -.
UCSC; uc003qkw.4; human. [O95278-1]
CTD; 7957; -.
DisGeNET; 7957; -.
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; -.
KO; K14165; -.
OMA; VDGVYCH; -.
OrthoDB; 692580at2759; -.
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; Expressed in 222 organ(s), highest expression level in skeletal muscle tissue of rectus abdominis.
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:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:Ensembl.
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:Ensembl.
GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
GO; GO:0014009; P:glial cell proliferation; IEA:Ensembl.
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:0015813; P:L-glutamate transmembrane transport; IEA:Ensembl.
GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl.
GO; GO:0035305; P:negative regulation of dephosphorylation; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
GO; GO:2000465; P:regulation of glycogen (starch) synthase activity; IEA:Ensembl.
GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEA:Ensembl.
GO; GO:0042306; P:regulation of protein import into nucleus; IEA:Ensembl.
GO; GO:0045859; P:regulation of protein kinase activity; IEA:Ensembl.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
GO; GO:1904666; P:regulation of ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
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; 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.
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;
dbSNP:rs1362231306).
{ECO:0000269|PubMed:11175283,
ECO:0000269|PubMed:14532330}.
/FTId=VAR_019469.
VARIANT 88 88 F -> L (in EPM2; does not affect glycogen
binding; dbSNP:rs1034706422 and
dbSNP:rs1463000703).
{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


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WP1388: Glycogen Metabolism
WP2042: PKA-HCG-Glycogen Syntase
WP436: Glycogen Metabolism
WP576: Glycogen Metabolism
WP1189: Glycogen Metabolism
WP955: Glycogen Metabolism
WP317: Glycogen Metabolism
WP1073: Glycogen Metabolism
WP500: Glycogen Metabolism
WP835: Glycogen Metabolism
WP160: Glycogen Metabolism

Related Genes :
[EPM2A] Laforin (EC 3.1.3.-) (EC 3.1.3.16) (EC 3.1.3.48) (Glucan phosphatase) (Glycogen phosphatase) (Lafora PTPase) (LAFPTPase)
[Epm2a] Laforin (EC 3.1.3.-) (EC 3.1.3.16) (EC 3.1.3.48) (Glucan phosphatase) (Lafora PTPase) (LAFPTPase)
[Epm2a] Laforin (EC 3.1.3.-) (EC 3.1.3.16) (EC 3.1.3.48) (Glucan phosphatase) (Lafora PTPase) (LAFPTPase)
[EPM2A] Laforin (EC 3.1.3.-) (EC 3.1.3.16) (EC 3.1.3.48) (Glucan phosphatase) (Lafora PTPase) (LAFPTPase)
[hchA A8C65_13880 A9R57_25255 AKG99_20940 AMK83_16550 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BMT53_00170 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP008_02510 BvCmsKSP015_01352 BvCmsKSP036_04668 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsKSP083_03900 BvCmsNSNP027_04914 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP039_03266 BvCmsNSP047_03567 BvCmsNSP078_03451 BvCmsSINP011_04162 BvCmsSIP006_05510 BvCmsSIP082_02402 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 CDL37_00765 CIJ94_05515 COD46_23180 CQP61_17160 CRD98_26150 CY655_12940 D5618_21870 D9D20_21030 D9D43_06110 D9H68_20750 D9H70_25730 D9I87_15275 DL800_09215 DNQ41_14245 DQE83_22775 DTL43_21780 DTM25_06080 DU321_04440 E2855_02503 E2863_02392 EC95NR1_00961 ED648_25045 EFB45_10990 EPS97_16570 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 EVY21_22520 ExPECSC038_01920 EXX32_14605 EXX71_02385 EXX78_21815 EYD11_09165 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13462_05714 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMT91_24760 BvCmsC61A_00149 BvCmsH15A_00510 BvCmsKSNP120_04693 BvCmsKSP026_03873 BvCmsKSP076_04891 C4J69_22715 C7B08_25495 CR538_10415 D2F89_25795 D3Y67_22910 D9G42_11130 D9I97_22010 D9J11_25195 DP258_02540 E5M00_18610 EC3234A_36c00010 EC382_21100 ECTO6_01955 EFV06_13085 EPS71_23885 FORC82_1921 NCTC8500_02249 NCTC9037_02122 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[AHK4 CRE1 RAW1 WOL At2g01830 T23K3.2] Histidine kinase 4 (EC 2.7.13.3) (Arabidopsis histidine kinase 4) (AtHK4) (Cytokinin receptor CYTOKININ RESPONSE 1) (AtCRE1) (Cytokinin receptor CRE1) (Phosphoprotein phosphatase AHK4) (EC 3.1.3.16) (Protein AUTHENTIC HIS-KINASE 4) (Protein ROOT AS IN WOL 1) (Protein WOODEN LEG)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[pteN ptenA DDB_G0286557] Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (EC 3.1.3.16) (EC 3.1.3.48) (EC 3.1.3.67) (Pten 3-phosphoinositide phosphatase alpha)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[hchA A8M42_01610 AM465_15370 AWF59_019055 AZZ83_004235 B9N33_26475 BFD68_20845 C1I57_21890 C7B02_06890 CCZ14_26645 CCZ17_22700 CRT43_11430 CT143_08220 D3C88_02905 D9D33_15385 D9E49_19020 D9I20_10460 D9J46_03345 DNR41_00375 DS966_16070 DU333_03260 DW236_02290 ECTO124_02024 EGT48_04930 EPS76_06485 EPS91_17475 EPS94_00505 ERS085406_02591 EWK56_00075 ExPECSC007_02422 ExPECSC065_02714 HmCmsJML122_02218 NCTC10766_03778 NCTC7928_05955 NCTC8450_02317 NCTC9007_02951 NCTC9075_02834 NCTC9775_01269 SY51_11150 U12A_02105 U14A_02105] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.-) (EC 3.5.1.124) (Maillard deglycase)
[Ptpn6 Hcp Hcph Ptp1C] Tyrosine-protein phosphatase non-receptor type 6 (EC 3.1.3.48) (70Z-SHP) (Hematopoietic cell protein-tyrosine phosphatase) (PTPTY-42) (Protein-tyrosine phosphatase 1C) (PTP-1C) (SH-PTP1) (SHP-1)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Impad1 Impa3] Inositol monophosphatase 3 (IMP 3) (IMPase 3) (EC 3.1.3.25) (EC 3.1.3.7) (Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase) (Golgi-resident PAP phosphatase) (gPAPP) (Inositol monophosphatase domain-containing protein 1) (Inositol-1(or 4)-monophosphatase 3) (Myo-inositol monophosphatase A3)
[pyrG A6592_02570 A8M42_16405 A9R57_06965 AC067_22330 AC789_1c31020 ACN002_2797 ACN77_07080 ACN81_20385 ACU57_24415 ACU90_23015 AJ318_22735 AKG99_03555 AM270_00945 AM446_06950 AM464_05605 AM465_10605 AML07_12460 AML35_05300 APT94_17890 APU18_18535 APZ14_09290 ARC77_10140 AU473_08010 AUQ13_17535 AUS26_15660 AW059_10675 AW106_00665 AWE53_025360 AWF59_014510 AWG78_018325 AWP75_20610 AZZ83_003241 B1K96_20050 B7C53_10055 B9M99_21725 B9N33_09475 B9T59_19685 BANRA_01301 BANRA_01853 BANRA_03509 BANRA_03630 BANRA_04184 BANRA_04324 BB545_13920 BE963_03670 BEN53_16995 BET08_07180 BFD68_17190 BHF46_05050 BHS81_16640 BHS87_15735 BIQ87_15835 BIU72_09520 BIZ41_16885 BJJ90_05265 BK248_12970 BK292_23205 BK334_11935 BK373_15870 BK375_10085 BK383_11680 BK400_05820 BMT49_17330 BMT53_21250 BMT91_11105 BN17_26661 BTQ04_11510 BTQ06_23845 BUE81_06975 BvCms12BK_05148 BvCms2454_02052 BvCms35BK_01272 BvCmsA75A_01806 BvCmsC61A_01055 BvCmsF63A_03709 BvCmsH15A_01164 BvCmsHHP001_01156 BvCmsHHP019_01127 BvCmsHHP056_01979 BvCmsJ76A_03658 BvCmsKKNP011_03618 BvCmsKKP021_00792 BvCmsKKP036_03980 BvCmsKKP061_04391 BvCmsKSNP019_00375 BvCmsKSNP073_04203 BvCmsKSNP081_03790 BvCmsKSNP120_03969 BvCmsKSP011_02434 BvCmsKSP015_01987 BvCmsKSP018_02104 BvCmsKSP024_03358 BvCmsKSP026_00102 BvCmsKSP036_04364 BvCmsKSP039_02057 BvCmsKSP040_03316 BvCmsKSP045_02208 BvCmsKSP054_03892 BvCmsKSP058_00862 BvCmsKSP061_02833 BvCmsKSP067_03640 BvCmsKSP076_05173 BvCmsKSP081_02474 BvCmsKSP083_02177 BvCmsNSNP006_02217 BvCmsNSNP023_04008 BvCmsNSNP027_02902 BvCmsNSNP036_03047 BvCmsNSP007_01096 BvCmsNSP039_01404 BvCmsNSP045_00318 BvCmsNSP047_01557 BvCmsNSP052_01369 BvCmsNSP072_00181 BvCmsOUP014_01917 BvCmsSINP011_00512 BvCmsSINP012_00021 BvCmsSINP022_00781 BvCmsSINP036_01056 BvCmsSIP010_03098 BvCmsSIP019_01766 BvCmsSIP044_01614 BvCmsSIP082_01367 BVL39_12970 BW690_04975 BWP17_05185 BXT93_24405 BZL31_00820 BZL69_02125 C1I57_04860 C2M16_17770 C2U48_20025 C3449_06035 C4J69_11655 C4K41_05275 C4M78_00835 C5715_23540 C5N07_06155 C5P01_05005 C5P43_15935 C5P44_09340 C6669_14670 C6986_17750 C6B13_03370 C7235_05745 C7B02_19400 C7B06_11630 C7B07_14530 C7B08_01430 C9E25_03325 C9E67_05815 CA593_12975 CCZ14_04445 CCZ17_10850 CDL37_13440 CG692_07005 CIJ94_12220 COD30_01795 COD46_07095 CPA47_05400 CQP61_06810 CR538_05495 CR539_18815 CRE06_03485 CRM83_26360 CRT43_16405 CRT46_16440 CSB64_15850 CT143_09630 CT146_00680 CV83915_03339 CVH05_06295 CWM24_00790 CWS33_03125 CY655_17835 D0X26_06660 D1900_12730 D2183_19100 D2184_01135 D2185_02785 D2F89_14380 D3821_11140 D3O91_13425 D3Y67_06430 D4M06_10805 D7K63_03745 D7K66_09735 D7Y10_03025 D9D20_04450 D9D33_19300 D9D43_17525 D9E35_20180 D9F17_11720 D9G11_10545 D9G42_05640 D9G48_11875 D9H53_12755 D9H68_17340 D9H70_12195 D9H94_16855 D9I11_16725 D9I18_10690 D9I20_00375 D9I87_07250 D9I88_14405 D9I97_09750 D9J03_22055 D9J11_17735 D9J44_16360 D9J46_14445 D9J60_10045 D9K48_23835 D9K54_13555 D9L89_10810 D9L99_02095 D9N32_10755 D9X97_06540 DB357_11665 DB359_08835 DC440_05995 DD762_13665 DIV22_29760 DL455_11645 DL545_05995 DL800_20505 DM102_10625 DM129_10705 DMI04_14240 DNB37_12630 DNQ41_18960 DNR41_08670 DNX30_08935 DOY56_02000 DP258_16075 DP277_11440 DQE83_04685 DQO13_13250 DS732_20695 DS966_06010 DTL43_09355 DTL90_02675 DTM10_03745 DTM25_22630 DTM45_13530 DU321_06150 DU333_12515 DW236_13020 DWB25_05920 E0E06_12020 E2855_03617 E2863_03463 E4Z89_05020 E5M00_06220 EAI42_07155 EAI44_18400 EAI46_14335 EAI52_12500 EB509_19080 EB510_16355 EB515_03490 EC1094V2_904 EC3234A_48c00890 EC3426_03921 EC382_15705 EC95NR1_02021 Eco118UI_16400 ECONIH1_15890 ECs3640 ECTO124_01152 ECTO6_01068 ED225_00710 ED600_14885 ED607_09825 ED611_00710 ED648_01520 ED903_09700 ED944_03505 EEA45_12675 EEP23_14050 EF173_03685 EFB45_09310 EFV06_07140 EFV07_19330 EFV08_05820 EGT48_09620 EGY17_03100 EIA08_07275 EIA21_04795 EJC48_07220 EJC75_12775 EJH97_05405 EKI52_20580 EL75_0914 EL79_0915 EL80_0918 EO240_11330 EO241_20205 EPS71_16810 EPS86_06805 EPS91_16285 EPS94_11415 EPS97_09215 EPT01_17055 EQ820_17285 EQ823_14605 EQ825_07980 EQ830_01100 ERL57_14345 ERS085365_02427 ERS085366_03042 ERS085374_03279 ERS085386_03410 ERS085416_02898 ERS139211_02072 ERS150873_02003 ERS150876_01467 EVY14_17325 EVY21_09330 EWK56_05345 EWK57_07880 ExPECSC007_02175 ExPECSC022_03623 ExPECSC036_01290 ExPECSC038_01963 ExPECSC065_01289 EXX06_06960 EXX09_09010 EXX13_05855 EXX23_03700 EXX24_19085 EXX29_07810 EXX30_11455 EXX32_11595 EXX39_16105 EXX40_00470 EXX53_03685 EXX55_06445 EXX69_04660 EXX71_16235 EXX73_09105 EXX77_13495 EXX78_11575 EXX87_15385 EYD11_05205 EYY78_11015 FORC28_1110 FORC82_1067 GJ11_18025 HmCms184_04776 HmCmsJML072_03065 HmCmsJML074_04422 HmCmsJML079_03779 HmCmsJML122_00699 HmCmsJML146_01816 HmCmsJML204_00525 HMPREF3040_01161 HW43_18180 JD73_16335 MJ49_17095 MS6198_30910 MS8345_02965 NCTC10082_03473 NCTC10090_04050 NCTC10418_01701 NCTC10764_00296 NCTC10766_00690 NCTC10767_02309 NCTC11022_02860 NCTC11112_00121 NCTC11181_03277 NCTC12950_01251 NCTC13127_01436 NCTC13462_04807 NCTC13846_01212 NCTC7927_01209 NCTC8500_01090 NCTC8960_03783 NCTC9007_03892 NCTC9036_01135 NCTC9037_01243 NCTC9044_00576 NCTC9045_01221 NCTC9050_04166 NCTC9058_00847 NCTC9062_02131 NCTC9075_01630 NCTC9077_01409 NCTC9081_05851 NCTC9117_01609 NCTC9119_01271 NCTC9434_01004 NCTC9702_01298 NCTC9706_03296 NCTC9775_04845 NCTC9777_02704 NCTC9969_01292 PU06_02080 RG28_07675 RK56_023165 SAMEA3472033_01264 SAMEA3472043_01265 SAMEA3472044_02272 SAMEA3472047_00339 SAMEA3472056_05455 SAMEA3472070_01673 SAMEA3472080_03155 SAMEA3472090_00131 SAMEA3472108_00527 SAMEA3472110_03462 SAMEA3472112_03722 SAMEA3472114_02432 SAMEA3472147_03296 SAMEA3484427_03298 SAMEA3484429_03415 SAMEA3484434_01581 SAMEA3485101_02257 SAMEA3485113_02257 SAMEA3752372_03639 SAMEA3752553_01510 SAMEA3752557_03040 SAMEA3752559_02995 SAMEA3752620_01282 SAMEA3753064_02287 SAMEA3753097_02219 SAMEA3753164_01192 SAMEA3753290_02847 SAMEA3753300_01107 SK85_03024 SY51_15605 U12A_02895 U14A_02898 UC41_20365 UN91_03645 WQ89_10170 WR15_06090 YDC107_1339] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[] Genome polyprotein [Cleaved into: Capsid protein C (Core protein); Protein prM; Peptide pr; Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Non-structural protein 2A-alpha (NS2A-alpha); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[] Genome polyprotein [Cleaved into: Capsid protein C (Capsid protein) (Core protein); Protein prM (Precursor membrane protein); Peptide pr (Peptide precursor); Small envelope protein M (Matrix protein); Envelope protein E; Non-structural protein 1 (NS1); Non-structural protein 2A (NS2A); Serine protease subunit NS2B (Flavivirin protease NS2B regulatory subunit) (Non-structural protein 2B); Serine protease NS3 (EC 3.4.21.91) (EC 3.6.1.15) (EC 3.6.4.13) (Flavivirin protease NS3 catalytic subunit) (Non-structural protein 3); Non-structural protein 4A (NS4A); Peptide 2k; Non-structural protein 4B (NS4B); RNA-directed RNA polymerase NS5 (EC 2.1.1.56) (EC 2.1.1.57) (EC 2.7.7.48) (Non-structural protein 5)]
[ACP1] Low molecular weight phosphotyrosine protein phosphatase (LMW-PTP) (LMW-PTPase) (EC 3.1.3.48) (Adipocyte acid phosphatase) (Low molecular weight cytosolic acid phosphatase) (EC 3.1.3.2) (Red cell acid phosphatase 1)
[PTPN4] Tyrosine-protein phosphatase non-receptor type 4 (EC 3.1.3.48) (Protein-tyrosine phosphatase MEG1) (MEG) (PTPase-MEG1)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[PTPN9] Tyrosine-protein phosphatase non-receptor type 9 (EC 3.1.3.48) (Protein-tyrosine phosphatase MEG2) (PTPase MEG2)

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