DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 2013 imex curation Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. DIP original experiment: DIP-252832X Nature 2013 IMEx Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 2013 imex curation Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. DIP original experiment: DIP-252828X Nature 2013 IMEx Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 2013 imex curation Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. DIP original experiment: DIP-252833X Nature 2013 IMEx Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 2013 imex curation Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. DIP original experiment: DIP-252834X Nature 2013 IMEx Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 2013 imex curation Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. Only protein-protein interactions in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. DIP original experiment: DIP-252829X Nature 2013 IMEx Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 2013 imex curation Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. Only protein-protein interactions in vitro In vitro fluorescence spectr classical fluorescence spectroscopy fluorescence spectr predetermined predetermined participant predetermined Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. DIP original experiment: DIP-252830X Nature 2013 IMEx Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 2013 imex curation Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. Only protein-protein interactions in vitro In vitro cosedimentation cosedimentation predetermined predetermined participant predetermined Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. DIP original experiment: DIP-252827X Nature 2013 IMEx Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 2013 imex curation Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. Only protein-protein interactions in vitro In vitro cosedimentation cosedimentation predetermined predetermined participant predetermined Kim HJ., Kim NC., Wang YD., Scarborough EA., Moore J., Diaz Z., MacLea KS., Freibaum B., Li S., Molliex A., Kanagaraj AP., Carter R., Boylan KB., Wojtas AM., Rademakers R., Pinkus JL., Greenberg SA., Trojanowski JQ., Traynor BJ., Smith BN., Topp S., Gkazi AS., Miller J., Shaw CE., Kottlors M., Kirschner J., Pestronk A., Li YR., Ford AF., Gitler AD., Benatar M., King OD., Kimonis VE., Ross ED., Weihl CC., Shorter J., Taylor JP. DIP original experiment: DIP-252831X Nature 2013 IMEx Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. p22626-2 Heterogeneous nuclear ribonucleoproteins A2/B1 hnRNP A2 HNRNPA2B1 HNRPA2B1 protein protein human Homo sapiens Human MEREKEQFRKLFIGGLSFETTEESLRNYYEQWGKLTDCVVMRDPASKRSRGFGFVTFSSMAEVDAAMAARPHSIDGRVVEPKRAVAREESGKPGAHVTVKKLFVGGIKEDTEEHHLRDYFEEYGKIDTIEIITDRQSGKKRGFGFVTFDDHDPVDKIVLQKYHTINGHNAEVRKALSRQEMQEVQSSRSGRGGNFGFGDSRGGGGNFGPGPGSNFRGGSDGYGSGRGFGDGYNGYGGGPGGGNFGGSPGYGGGRGGYGGGGPGYGNQGGGYGGGYDNYGGGNYGSGNYNDFGNYNQQPSNYGPMKSGNFGGSRNMGGPYGGGNYGPGGSGGSGGYGGRSRY DIP protein P22626-2 original sequence version: 157 DIP protein P22626-2 original sequence version: 149 Contains a glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) at position 5. 39E8AB6ED874FA7C p09651-2 Heterogeneous nuclear ribonucleoprotein A1 HNRNPA1 HNRPA1 Helix-destabilizing protein Single-strand RNA-binding protein hnRNP core protein A1 protein protein human Homo sapiens Human MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF DIP protein P09651-2 original sequence version: 107 DIP protein P09651-2 original sequence version: 179 Is twenty times more abundant than isoform A1-B. 59485C9FA1FF8AE1 hnrnpa1-1 3 10 unspecified role unspecified role unspecified role unspecified role Region 259-264 Region 259-264 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P09651-2:p.Asp262Val D262V mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D V This feature has been corrected as a result of our quality control procedures. The original label was 'D262V'. Wed May 02 17:11:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp262val' Tue Jun 30 20:04:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp262Val' in vitro In vitro direct interaction direct interaction hnrnpa2b1-1 7 9 unspecified role unspecified role unspecified role unspecified role Region 287-292 Region 287-292 required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P22626-2:p.Asp290Val D290V mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D V This feature has been corrected as a result of our quality control procedures. The original label was 'D290V'. Wed May 02 15:35:47 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp290val' Tue Jun 30 20:03:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp290Val' ecolx Escherichia coli direct interaction direct interaction hnrnpa2b1-2 6 9 unspecified role unspecified role unspecified role unspecified role P22626-2:p.Asp290Val D290V mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D V This feature has been corrected as a result of our quality control procedures. The original label was 'D290V'. Wed May 02 15:46:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp290val' Tue Jun 30 18:04:30 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp290Val' Region 287-292 Region 287-292 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction hnrnpa2b1-3 2 9 unspecified role unspecified role unspecified role unspecified role P22626-2:p.Asp290Val D290V mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D V This feature has been corrected as a result of our quality control procedures. The original label was 'D290V'. Wed May 02 16:00:59 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp290val' Tue Jun 30 20:13:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp290Val' ecolx Escherichia coli direct interaction direct interaction hnrnpa1-3 8 10 unspecified role unspecified role unspecified role unspecified role Region 259-264 Region 259-264 required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P09651-2:p.Asp262Val D262V/N mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D V Wed May 02 19:03:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp262val' Tue Jun 30 16:51:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp262Val' P09651-2:p.Asp262Asn mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain D N Wed May 02 14:39:35 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp262asn' Tue Jun 30 16:54:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp262Asn' ecolx Escherichia coli direct interaction direct interaction hnrnpa1-4 4 10 unspecified role unspecified role unspecified role unspecified role Region 259-264 Region 259-264 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P09651-2:p.Asp262Val D262V mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D V This feature has been corrected as a result of our quality control procedures. The original label was 'D262V'. Wed May 02 18:57:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp262val' Tue Jun 30 20:12:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp262Val' in vitro In vitro direct interaction direct interaction hnrnpa2b1-4 5 9 unspecified role unspecified role unspecified role unspecified role P22626-2:p.Asp290Val D290V mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D V This feature has been corrected as a result of our quality control procedures. The original label was 'D290V'. Wed May 02 17:33:42 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp290val' Tue Jun 30 19:54:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp290Val' Region 287-292 Region 287-292 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction hnrnpa1-5 1 10 unspecified role unspecified role unspecified role unspecified role P09651-2:p.Asp262Val D262V/N mutation increasing strength mutation increasing interaction strength mutation increasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain D V Wed May 02 19:50:00 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp262val' Tue Jun 30 18:09:15 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp262Val' P09651-2:p.Asp262Asn mutation increasing strength mutation increasing interaction strength mutation increasing strength certain certain sequence position certain certain certain sequence position certain D N Wed May 02 17:44:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp262asn' Tue Jun 30 17:51:52 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp262Asn' ecolx Escherichia coli direct interaction direct interaction