IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. 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. (0964-6906) 2003 imex curation Fernandez-Sanchez ME., Criado-Garcia O., Heath KE., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa JM., Rodriguez de Cordoba S. srdecordoba@cib.csic.es 23-Feb-2010: Contacted by JYOTI. human skeletal muscle and brain cDNA libraries orchard Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid nucleotide sequence nucleotide sequence identification sequence cloning sequence cloning nucleotide sequence Fernandez-Sanchez ME., Criado-Garcia O., Heath KE., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa JM., Rodriguez de Cordoba S. srdecordoba@cib.csic.es Accepted 2009-Not a month!-11 by ORCHARD. 23-Feb-2010: Contacted by JYOTI. human skeletal muscle and brain cDNA libraries Hum. Mol. Genet. (0964-6906) 2003 orchard Only protein-protein interactions imex curation Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. 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. (0964-6906) 2003 imex curation Fernandez-Sanchez ME., Criado-Garcia O., Heath KE., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa JM., Rodriguez de Cordoba S. srdecordoba@cib.csic.es 23-Feb-2010: Contacted by JYOTI. human skeletal muscle and brain cDNA libraries orchard Only protein-protein interactions mouse-c2c12 Mouse C3H muscle myoblast c2c12 Mouse C3H muscle myoblast fluorescence fluorescence technology fluorescence tag fluorescence tag visualisation by fluorescence tag fluorescence Fernandez-Sanchez ME., Criado-Garcia O., Heath KE., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa JM., Rodriguez de Cordoba S. Untagged molecules identified by immunostaining srdecordoba@cib.csic.es Accepted 2009-Not a month!-11 by ORCHARD. 23-Feb-2010: Contacted by JYOTI. human skeletal muscle and brain cDNA libraries Hum. Mol. Genet. (0964-6906) 2003 orchard Only protein-protein interactions imex curation Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. 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. (0964-6906) 2003 imex curation Fernandez-Sanchez ME., Criado-Garcia O., Heath KE., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa JM., Rodriguez de Cordoba S. srdecordoba@cib.csic.es 23-Feb-2010: Contacted by JYOTI. human skeletal muscle and brain cDNA libraries orchard Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Fernandez-Sanchez ME., Criado-Garcia O., Heath KE., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa JM., Rodriguez de Cordoba S. srdecordoba@cib.csic.es Accepted 2009-Not a month!-11 by ORCHARD. 23-Feb-2010: Contacted by JYOTI. human skeletal muscle and brain cDNA libraries Hum. Mol. Genet. (0964-6906) 2003 orchard Only protein-protein interactions imex curation Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. 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. (0964-6906) 2003 imex curation Fernandez-Sanchez ME., Criado-Garcia O., Heath KE., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa JM., Rodriguez de Cordoba S. srdecordoba@cib.csic.es 23-Feb-2010: Contacted by JYOTI. human skeletal muscle and brain cDNA libraries orchard Only protein-protein interactions in vitro In vitro pull down pull down western blot western blot Immuno blot Immuno blot Fernandez-Sanchez ME., Criado-Garcia O., Heath KE., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa JM., Rodriguez de Cordoba S. srdecordoba@cib.csic.es Accepted 2009-Not a month!-11 by ORCHARD. 23-Feb-2010: Contacted by JYOTI. human skeletal muscle and brain cDNA libraries Hum. Mol. Genet. (0964-6906) 2003 orchard Only protein-protein interactions imex curation Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation. 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. (0964-6906) 2003 imex curation Fernandez-Sanchez ME., Criado-Garcia O., Heath KE., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa JM., Rodriguez de Cordoba S. srdecordoba@cib.csic.es 23-Feb-2010: Contacted by JYOTI. human skeletal muscle and brain cDNA libraries orchard Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column western blot western blot Immuno blot Immuno blot Fernandez-Sanchez ME., Criado-Garcia O., Heath KE., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa JM., Rodriguez de Cordoba S. srdecordoba@cib.csic.es Accepted 2009-Not a month!-11 by ORCHARD. 23-Feb-2010: Contacted by JYOTI. human skeletal muscle and brain cDNA libraries Hum. Mol. Genet. (0964-6906) 2003 orchard Only protein-protein interactions imex curation epm2a_human Laforin EPM2A Lafora PTPase Glycogen phosphatase Glucan phosphatase protein protein human Homo sapiens Human MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALQEPGLWLGEVELAAEEAAQDGAEPGRVDTFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHVTIKLKHELGITAVMNFQTEWDIVQNSSGCNRYPEPMTPDTMIKLYREEGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDEEALARAQEDFFQKFGKVRSSVCSL DD79F917262AB458 gys1_human Glycogen [starch] synthase, muscle GYS1 GYS protein protein human Homo sapiens Human MPLNRTLSMSSLPGLEDWEDEFDLENAVLFEVAWEVANKVGGIYTVLQTKAKVTGDEWGDNYFLVGPYTEQGVRTQVELLEAPTPALKRTLDSMNSKGCKVYFGRWLIEGGPLVVLLDVGASAWALERWKGELWDTCNIGVPWYDREANDAVLFGFLTTWFLGEFLAQSEEKPHVVAHFHEWLAGVGLCLCRARRLPVATIFTTHATLLGRYLCAGAVDFYNNLENFNVDKEAGERQIYHRYCMERAAAHCAHVFTTVSQITAIEAQHLLKRKPDIVTPNGLNVKKFSAMHEFQNLHAQSKARIQEFVRGHFYGHLDFNLDKTLYFFIAGRYEFSNKGADVFLEALARLNYLLRVNGSEQTVVAFFIMPARTNNFNVETLKGQAVRKQLWDTANTVKEKFGRKLYESLLVGSLPDMNKMLDKEDFTMMKRAIFATQRQSFPPVCTHNMLDDSSDPILTTIRRIGLFNSSADRVKVIFHPEFLSSTSPLLPVDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSISTNLSGFGCFMEEHIADPSAYGIYILDRRFRSLDDSCSQLTSFLYSFCQQSRRQRIIQRNRTERLSDLLDWKYLGRYYMSARHMALSKAFPEHFTYEPNEADAAQGYRYPRPASVPPSPSLSRHSSPHQSEDEEDPRNGPLEEDGERYDEDEEAAKDRRNIRAPEWPRRASCTSSTSGSKRNSVDTATSSSLSTPSEPLSPTSSLGEERN 0E321BBFDEB0BD7F ppr3c_human Protein phosphatase 1 regulatory subunit 3C PPP1R3C PPP1R5 Protein phosphatase 1 regulatory subunit 5 Protein targeting to glycogen protein protein human Homo sapiens Human MSCTRMIQVLDPRPLTSSVMPVDVAMRLCLAHSPPVKSFLGPYDEFQRRHFVNKLKPLKSCLNIKHKAKSQNDWKCSHNQAKKRVVFADSKGLSLTAIHVFSDLPEEPAWDLQFDLLDLNDISSALKHHEEKNLILDFPQPSTDYLSFRSHFQKNFVCLENCSLQERTVTGTVKVKNVSFEKKVQIRITFDSWKNYTDVDCVYMKNVYGGTDSDTFSFAIDLPPVIPTEQKIEFCISYHANGQVFWDNNDGQNYRIVHVQWKPDGVQTQMAPQDCAFHQTSPKTELESTIFGSPRLASGLFPEWQSWGRMENLASYR FBFD6DE015F9AB2D glycogen small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) epm2a-epm2a-1 1 6 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind range range certain certain sequence position certain 6 unspecified role unspecified role bait bait physical association physical association epm2a-r5-1 1 8 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 6 unspecified role unspecified role bait bait physical association physical association epm2a-r5-3 4 8 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminal gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role prey prey chlae-cos_7 Cercopithecus aethiops simian cells transformed with SV40 Grivet cos_7 cercopithecus aethiops, by transformation with SV40 physical association physical association Fig. 3B Recombinant human laforin expressed in COS7 cells were mixed with the GST-R5 fragments, the complexes precipitated with glutathione-agarose beads and the proteins in the precipitate analyzed by western blot with a rabbit anti-human laforin antibody. epm2a-r5-4 3 8 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Q9UQK1:p.[Asp247Ala;Asp250Ala] asp247ala, asp250ala mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D A certain certain sequence position certain certain certain sequence position certain D A Wed May 02 19:40:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp247ala,asp250ala' Tue Jun 30 19:34:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Asp247Ala;Asp250Ala]' Q9UQK1:p.[Val85Ala;Phe87Ala] val85ala, phe87ala non-disruptive mutation mutation mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain V A certain certain sequence position certain certain certain sequence position certain F A Wed May 02 17:58:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val85ala,phe87ala' Tue Jun 30 17:15:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Val85Ala;Phe87Ala]' 6 unspecified role unspecified role bait bait physical association physical association Fig. 3A, 3C Q9UQK1 - sequence refered to in the paper appears to have been subsequently withdrawn, so coordinates have been remapped to current UniProtKB sequence. Using yeast two-hybrid assays we report here that laforin interacts with itself and with R5, one of the glycogen targeting regulatory subunits of protein phosphatase 1 (PP1) epm2a-r5-5 2 6 unspecified role unspecified role neutral component neutral component mouse-c2c12 Mouse C3H muscle myoblast c2c12 Mouse C3H muscle myoblast 8 unspecified role unspecified role neutral component neutral component region egfp tag enhanced green fluorescent protein tag enhanced green fluorescent protein EGFP enhanced green fluorescent protein EGFP egfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined mouse-c2c12 Mouse C3H muscle myoblast c2c12 Mouse C3H muscle myoblast colocalization colocalization Fig. 4A Co-transfection experiments in C2C12 murine myoblasts with R5 and laforin demonstrate co-localization of both proteins (Fig. 4A). lafptpase-gys1 2 7 unspecified role unspecified role neutral component neutral component region egfp tag enhanced green fluorescent protein tag enhanced green fluorescent protein EGFP enhanced green fluorescent protein EGFP egfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 6 unspecified role unspecified role neutral component neutral component mouse-c2c12 Mouse C3H muscle myoblast c2c12 Mouse C3H muscle myoblast colocalization colocalization Fig. 4C, D epm2a-r5-6 3 6 unspecified role unspecified role bait bait O95278:p.Trp32Gly mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain W G Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019467 Wed May 02 16:26:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp32gly' Tue Jun 30 16:14:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp32Gly' O95278:p.Phe84Leu mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain F L Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019469 Wed May 02 18:07:46 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe84leu' Tue Jun 30 17:12:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe84Leu' O95278:p.Arg108Cys mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R C Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019472 Wed May 02 14:57:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg108cys' Tue Jun 30 19:54:11 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg108Cys' O95278:p.Thr194Ile mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain T I Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019476 Wed May 02 20:17:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr194ile' Tue Jun 30 20:01:53 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr194Ile' O95278:p.Gly240Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain G S Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019477 Wed May 02 15:41:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly240ser' Tue Jun 30 18:45:54 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly240Ser' O95278:p.Gly279Ser mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain G S Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019478 Wed May 02 20:20:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly279ser' Tue Jun 30 19:50:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly279Ser' O95278:p.Gln293Leu mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Q L Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019479 Wed May 02 16:49:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln293leu' Tue Jun 30 15:41:16 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln293Leu' O95278:p.Tyr294Asn mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y N Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019480 Wed May 02 15:55:21 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr294asn' Tue Jun 30 17:14:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr294Asn' O95278:p.Pro301Leu mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain P L Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019481 Wed May 02 17:00:13 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro301leu' Tue Jun 30 17:38:19 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro301Leu' O95278:p.Cys266Ser mutation increasing mutation increasing interaction mutation increasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain C S Wed May 02 19:25:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'cys266ser' Tue Jun 30 16:22:40 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Cys266Ser' 8 unspecified role unspecified role prey prey physical association physical association Fig. 5B Using yeast two-hybrid assays we report here that laforin interacts with itself and with R5, one of the glycogen targeting regulatory subunits of protein phosphatase 1 (PP1) epm2a-epm2a-2 3 6 unspecified role unspecified role bait bait O95278:p.Gln293Leu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Q L Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019479 Wed May 02 18:31:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln293leu' Tue Jun 30 16:41:32 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln293Leu' O95278:p.Pro301Leu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain P L Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019481 Wed May 02 15:08:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro301leu' Tue Jun 30 17:57:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro301Leu' O95278:p.Arg108Cys mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R C Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019472 Wed May 02 14:32:01 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg108cys' Tue Jun 30 19:21:03 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg108Cys' O95278:p.Thr194Ile mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain T I Variant in EPM2 (Epilepsy, progressive myoclonic 2; MIM:254780 ); UniProt FTId: VAR_019476 Wed May 02 15:11:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr194ile' Tue Jun 30 17:38:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr194Ile' 6 unspecified role unspecified role prey prey physical association physical association Fig. 5A. epm2a-glyc 5 9 unspecified role unspecified role neutral component neutral component 6 unspecified role unspecified role neutral component neutral component O95278:p.Trp32Gly mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain W G Wed May 02 16:17:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'trp32gly' Tue Jun 30 17:47:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Trp32Gly' O95278:p.Arg108Cys mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R C Wed May 02 17:39:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg108cys' Tue Jun 30 20:10:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg108Cys' O95278:p.Gly279Ser mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain G S Wed May 02 18:02:39 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly279ser' Tue Jun 30 19:42:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly279Ser' O95278:p.Gln293Leu mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Q L Wed May 02 20:00:36 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gln293leu' Tue Jun 30 19:33:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gln293Leu' O95278:p.Tyr294Asn mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y N Wed May 02 15:23:41 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr294asn' Tue Jun 30 16:11:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr294Asn' O95278:p.Pro301Leu mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain P L Wed May 02 20:15:04 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'pro301leu' Tue Jun 30 16:17:05 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Pro301Leu' in vitro In vitro direct interaction direct interaction Fig. 1D Glycogen binding studies of recombinant WT and mutant laforin.