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Sequence of EPM2A_MOUSE

EC Number:3.1.3.16

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
protein-serine/threonine phosphatase
Q9WUA5
Mus musculus
330
36958
Reaction
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate
Other sequences found for EC No. 3.1.3.16

General information:

Sequence
show sequence in fasta format
  0 MLFRFGVVVP PAVAGARQEL LLAGSRPELG RWEPHGAVRL RPAGTAAGAA ALALQEPGLW
 60 LAEVELEAYE EAGGAEPGRV DTFWYKFLQR EPGGELHWEG NGPHHDRCCT YNEDNLVDGV
120 YCLPVGHWIE ATGHTNEMKH TTDFYFNIAG HQAMHYSRIL PNIWLGSCPR QLEHVTIKLK
180 HELGVTAVMN FQTEWDIIQN SSGCNRYPEP MTPDTMMKLY KEEGLSYIWM PTPDMSTEGR
240 VQMLPQAVCL LHALLENGHT VYVHCNAGVG RSTAAVCGWL HYVIGWNLRK VQYFIMAKRP
300 AVYIDEDALA QAQQDFSQKF GKVHSSICAL
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
30739
Ganesh S.,Amano K.,Delgado-Escueta A.V.,Yamakawa K.
Isolation and characterization of mouse homologue for the human epilepsy gene, EPM2A.
Biochem. Biophys. Res. Commun.
257
24-28
1999
30740
Church D.M.,Goodstadt L.,Hillier L.W.,Zody M.C.,Goldstein S.,She X.,Bult C.J.,Agarwala R.,Cherry J.L.,DiCuccio M.,Hlavina W.,Kapustin Y.,Meric P.,Maglott D.,Birtle Z.,Marques A.C.,Graves T.,Zhou S.,Teague B.,Potamousis K.,Churas C.,Place M.,Herschleb J.,Runnheim R.,Forrest D.,Amos-Landgraf J.,Schwartz D.C.,Cheng Z.,Lindblad-Toh K.,Eichler E.E.,Ponting C.P.
Lineage-specific biology revealed by a finished genome assembly of the mouse.
PLoS Biol.
7
0-0
2009
30742
Carninci P.,Kasukawa T.,Katayama S.,Gough J.,Frith M.C.,Maeda N.,Oyama R.,Ravasi T.,Lenhard B.,Wells C.,Kodzius R.,Shimokawa K.,Bajic V.B.,Brenner S.E.,Batalov S.,Forrest A.R.,Zavolan M.,Davis M.J.,Wilming L.G.,Aidinis V.,Allen J.E.,Ambesi-Impiombato A.,Apweiler R.,Aturaliya R.N.,Bailey T.L.,Bansal M.,Baxter L.,Beisel K.W.,Bersano T.,Bono H.,Chalk A.M.,Chiu K.P.,Choudhary V.,Christoffels A.,Clutterbuck D.R.,Crowe M.L.,Dalla E.,Dalrymple B.P.,de Bono B.,Della Gatta G.,di Bernardo D.,Down T.,Engstrom P.,Fagiolini M.,Faulkner G.,Fletcher C.F.,Fukushima T.,Furuno M.,Futaki S.,Gariboldi M.,Georgii-Hemming P.,Gingeras T.R.,Gojobori T.,Green R.E.,Gustincich S.,Harbers M.,Hayashi Y.,Hensch T.K.,Hirokawa N.,Hill D.,Huminiecki L.,Iacono M.,Ikeo K.,Iwama A.,Ishikawa T.,Jakt M.,Kanapin A.,Katoh M.,Kawasawa Y.,Kelso J.,Kitamura H.,Kitano H.,Kollias G.,Krishnan S.P.,Kruger A.,Kummerfeld S.K.,Kurochkin I.V.,Lareau L.F.,Lazarevic D.,Lipovich L.,Liu J.,Liuni S.,McWilliam S.,Madan Babu M.,Madera M.,Marchionni L.,Matsuda H.,Matsuzawa S.,Miki H.,Mignone F.,Miyake S.,Morris K.,Mottagui-Tabar S.,Mulder N.,Nakano N.,Nakauchi H.,Ng P.,Nilsson R.,Nishiguchi S.,Nishikawa S.,Nori F.,Ohara O.,Okazaki Y.,Orlando V.,Pang K.C.,Pavan W.J.,Pavesi G.,Pesole G.,Petrovsky N.,Piazza S.,Reed J.,Reid J.F.,Ring B.Z.,Ringwald M.,Rost B.,Ruan Y.,Salzberg S.L.,Sandelin A.,Schneider C.,Schoenbach C.,Sekiguchi K.,Semple C.A.,Seno S.,Sessa L.,Sheng Y.,Shibata Y.,Shimada H.,Shimada K.,Silva D.,Sinclair B.,Sperling S.,Stupka E.,Sugiura K.,Sultana R.,Takenaka Y.,Taki K.,Tammoja K.,Tan S.L.,Tang S.,Taylor M.S.,Tegner J.,Teichmann S.A.,Ueda H.R.,van Nimwegen E.,Verardo R.,Wei C.L.,Yagi K.,Yamanishi H.,Zabarovsky E.,Zhu S.,Zimmer A.,Hide W.,Bult C.,Grimmond S.M.,Teasdale R.D.,Liu E.T.,Brusic V.,Quackenbush J.,Wahlestedt C.,Mattick J.S.,Hume D.A.,Kai C.,Sasaki D.,Tomaru Y.,Fukuda S.,Kanamori-Katayama M.,Suzuki M.,Aoki J.,Arakawa T.,Iida J.,Imamura K.,Itoh M.,Kato T.,Kawaji H.,Kawagashira N.,Kawashima T.,Kojima M.,Kondo S.,Konno H.,Nakano K.,Ninomiya N.,Nishio T.,Okada M.,Plessy C.,Shibata K.,Shiraki T.,Suzuki S.,Tagami M.,Waki K.,Watahiki A.,Okamura-Oho Y.,Suzuki H.,Kawai J.,Hayashizaki Y.
The transcriptional landscape of the mammalian genome.
Science
309
1559-1563
2005
30743
Ganesh S.,Agarwala K.L.,Amano K.,Suzuki T.,Delgado-Escueta A.V.,Yamakawa K.
Regional and developmental expression of Epm2a gene and its evolutionary conservation.
Biochem. Biophys. Res. Commun.
283
1046-1053
2001
30744
Ganesh S.,Delgado-Escueta A.V.,Sakamoto T.,Avila M.R.,Machado-Salas J.,Hoshii Y.,Akagi T.,Gomi H.,Suzuki T.,Amano K.,Agarwala K.L.,Hasegawa Y.,Bai D.S.,Ishihara T.,Hashikawa T.,Itohara S.,Cornford E.M.,Niki H.,Yamakawa K.
Targeted disruption of the Epm2a gene causes formation of Lafora inclusion bodies, neurodegeneration, ataxia, myoclonus epilepsy and impaired behavioral response in mice.
Hum. Mol. Genet.
11
1251-1262
2002
30745
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
30746
Tagliabracci V.S.,Turnbull J.,Wang W.,Girard J.M.,Zhao X.,Skurat A.V.,Delgado-Escueta A.V.,Minassian B.A.,Depaoli-Roach A.A.,Roach P.J.
Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo.
Proc. Natl. Acad. Sci. U.S.A.
104
19262-19266
2007
30747
Tagliabracci V.S.,Girard J.M.,Segvich D.,Meyer C.,Turnbull J.,Zhao X.,Minassian B.A.,Depaoli-Roach A.A.,Roach P.J.
Abnormal metabolism of glycogen phosphate as a cause for Lafora disease.
J. Biol. Chem.
283
33816-33825
2008
30748
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
30749
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
30750
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
30751
Tiberia E.,Turnbull J.,Wang T.,Ruggieri A.,Zhao X.C.,Pencea N.,Israelian J.,Wang Y.,Ackerley C.A.,Wang P.,Liu Y.,Minassian B.A.
Increased laforin and laforin binding to glycogen underlie Lafora body formation in malin-deficient Lafora disease.
J. Biol. Chem.
287
25650-25659
2012
30752
Nitschke F.,Wang P.,Schmieder P.,Girard J.M.,Awrey D.E.,Wang T.,Israelian J.,Zhao X.,Turnbull J.,Heydenreich M.,Kleinpeter E.,Steup M.,Minassian B.A.
Hyperphosphorylation of glucosyl C6 carbons and altered structure of glycogen in the neurodegenerative epilepsy Lafora disease.
Cell Metab.
17
756-767
2013
30753
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
30754
Gayarre J.,Duran-Trio L.,Criado Garcia O.,Aguado C.,Juana-Lopez L.,Crespo I.,Knecht E.,Bovolenta P.,Rodriguez de Cordoba S.
The phosphatase activity of laforin is dispensable to rescue Epm2a-/-mice from Lafora disease.
Brain
137
806-818
2014
30755
Liu Y.,Zeng L.,Ma K.,Baba O.,Zheng P.,Liu Y.,Wang Y.
Laforin-malin complex degrades polyglucosan bodies in concert with glycogen debranching enzyme and brain isoform glycogen phosphorylase.
Mol. Neurobiol.
49
645-657
2014