EPM2A_HUMAN - dbPTM
EPM2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPM2A_HUMAN
UniProt AC O95278
Protein Name Laforin {ECO:0000303|PubMed:11001928}
Gene Name EPM2A
Organism Homo sapiens (Human).
Sequence Length 331
Subcellular Localization Cytoplasm . Under glycogenolytic conditions localizes to the nucleus.
Isoform 1: Cytoplasm . Endoplasmic reticulum membrane
Peripheral membrane protein
Cytoplasmic side . Cell membrane . Colocalizes with glycogen synthase in punctate struct
Protein Description 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]
Protein Sequence MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALQEPGLWLGEVELAAEEAAQDGAEPGRVDTFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHVTIKLKHELGITAVMNFQTEWDIVQNSSGCNRYPEPMTPDTMIKLYREEGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDEEALARAQEDFFQKFGKVRSSVCSL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
25PhosphorylationPELLVVGSRPELGRW
CEEEEEECCCCCCCC		32.8111001928
25 (in isoform 2)Phosphorylation-32.8111001928
25 (in isoform 4)Phosphorylation-32.8111001928
25 (in isoform 5)Phosphorylation-32.8111001928
59 (in isoform 7)Phosphorylation-5.0924043423
61 (in isoform 6)Phosphorylation-5.15-
62 (in isoform 7)Phosphorylation-25.8924043423
67 (in isoform 7)Phosphorylation-10.1824043423
74 (in isoform 7)Phosphorylation-54.2524043423
75 (in isoform 8)Phosphorylation-21.5424043423
78 (in isoform 8)Phosphorylation-35.0424043423
79 (in isoform 7)Phosphorylation-33.4824043423
83 (in isoform 7)Phosphorylation-17.1424043423
83 (in isoform 8)Phosphorylation-17.1424043423
84 (in isoform 7)Phosphorylation-6.0924043423
86 (in isoform 5)Phosphorylation-6.4122817900
86 (in isoform 4)Phosphorylation-6.4122817900
86 (in isoform 2)Phosphorylation-6.4122817900
86PhosphorylationGRVDTFWYKFLKREP
CCCCCHHHHHHCCCC		6.4122817900
90 (in isoform 8)Phosphorylation-58.8224043423
95 (in isoform 8)Phosphorylation-43.3024043423
99 (in isoform 8)Phosphorylation-30.0924043423
100 (in isoform 8)Phosphorylation-39.1324043423
147 (in isoform 4)Phosphorylation-5.57-
150 (in isoform 7)Phosphorylation-15.54-
166 (in isoform 8)Phosphorylation-2.99-
213 (in isoform 2)Phosphorylation-28.8224043423
213PhosphorylationNRYPEPMTPDTMIKL
CCCCCCCCHHHHHHH		28.8224043423
216 (in isoform 2)Phosphorylation-23.2324043423
216PhosphorylationPEPMTPDTMIKLYRE
CCCCCHHHHHHHHHH		23.2324043423
221 (in isoform 2)Phosphorylation-15.8124043423
221PhosphorylationPDTMIKLYREEGLAY
HHHHHHHHHHCCCEE		15.8124043423
228 (in isoform 2)Phosphorylation-10.5224043423
228PhosphorylationYREEGLAYIWMPTPD
HHHCCCEEEEECCCC		10.5224043423
233 (in isoform 2)Phosphorylation-18.8024043423
233PhosphorylationLAYIWMPTPDMSTEG
CEEEEECCCCCCCCC		18.8024043423
237 (in isoform 2)Phosphorylation-30.5924043423
237PhosphorylationWMPTPDMSTEGRVQM
EECCCCCCCCCHHCH		30.5924043423
238PhosphorylationMPTPDMSTEGRVQML
ECCCCCCCCCHHCHH		35.5024043423
238 (in isoform 2)Phosphorylation-35.5024043423
304PhosphorylationMAKRPAVYIDEEALA
HCCCCEEEECHHHHH		12.54-
320UbiquitinationAQEDFFQKFGKVRSS
HHHHHHHHHCCHHHH		51.43-
325DimethylationFQKFGKVRSSVCSL-
HHHHCCHHHHHCCC-		27.05-
325MethylationFQKFGKVRSSVCSL-
HHHHCCHHHHHCCC-		27.0524380735
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
25SPhosphorylationKinaseAMPKQ9Y478
Uniprot
25SPhosphorylationKinasePRKAA1Q13131
GPS
-KUbiquitinationE3 ubiquitin ligaseNHLRC1Q6VVB1
PMID:15930137
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
25SPhosphorylation

21728993
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of EPM2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NFU1_HUMANNFU1physical
12915448
NHLC1_HUMANNHLRC1physical
16115820
GSK3B_HUMANGSK3Bphysical
16115820
NHLC1_HUMANNHLRC1physical
15930137
NHLC1_HUMANNHLRC1physical
18029386
AAPK2_HUMANPRKAA2physical
18029386
AAKB2_HUMANPRKAB2physical
18029386
EPM2A_HUMANEPM2Aphysical
18617530
NHLC1_HUMANNHLRC1physical
18617530
NHLC1_HUMANNHLRC1physical
21505799
PPR3D_HUMANPPP1R3Dphysical
23624058
EPM2A_HUMANEPM2Aphysical
23922729
NHLC1_HUMANNHLRC1physical
23922729
KPYM_HUMANPKMphysical
26493215
TOPRS_HUMANTOPORSphysical
26493215
COX5A_HUMANCOX5Aphysical
26493215
EPM2A_HUMANEPM2Aphysical
26493215
PPR3C_HUMANPPP1R3Cphysical
26493215
TDG_HUMANTDGphysical
26493215
PRS6A_HUMANPSMC3physical
26493215
HMGX4_HUMANHMGXB4physical
26493215
EI2BA_HUMANEIF2B1physical
26493215
NHLC1_HUMANNHLRC1physical
26648032
UBE2N_HUMANUBE2Nphysical
26546463
NHLC1_HUMANNHLRC1physical
26546463
SQSTM_HUMANSQSTM1physical
26546463
Drug and Disease Associations
Kegg Disease
H00810 Progressive myoclonic epilepsy (PME), including: Lafora disease (LBD); Unverricht-Lundborg disease (
OMIM Disease
254780Epilepsy, progressive myoclonic 2 (EPM2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPM2A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Laforin, a dual-specificity phosphatase involved in Lafora disease,is phosphorylated at Ser25 by AMP-activated protein kinase.";
Roma-Mateo C., Solaz-Fuster Mdel C., Gimeno-Alcaniz J.V.,Dukhande V.V., Donderis J., Worby C.A., Marina A., Criado O.,Koller A., Rodriguez De Cordoba S., Gentry M.S., Sanz P.;
Biochem. J. 439:265-275(2011).
Cited for: PHOSPHORYLATION AT SER-25 (ISOFORM 1), AND MUTAGENESIS OF SER-25;SER-168; THR-187 AND THR-194.

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