MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint gr_nwald-2013-3 Structural basis for the nuclear export activity of Importin13. in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Grünwald M., Lazzaretti D., Bono F. fulvia.bono@tuebingen.mpg.de EMBO J. (0261-4189) 2013 Only protein-protein interactions imex curation gr_nwald-2013-4 Structural basis for the nuclear export activity of Importin13. in vitro In vitro thermal shift thermal shift binding thermal shift predetermined predetermined participant predetermined Grünwald M., Lazzaretti D., Bono F. fulvia.bono@tuebingen.mpg.de EMBO J. (0261-4189) 2013 Only protein-protein interactions imex curation gr_nwald-2013-2 Structural basis for the nuclear export activity of Importin13. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column weight by comassie molecular weight estimation by coomasie staining weight by comassie Grünwald M., Lazzaretti D., Bono F. fulvia.bono@tuebingen.mpg.de EMBO J. (0261-4189) 2013 Only protein-protein interactions imex curation gr_nwald-2013-1 Structural basis for the nuclear export activity of Importin13. in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Grünwald M., Lazzaretti D., Bono F. fulvia.bono@tuebingen.mpg.de EMBO J. (0261-4189) 2013 Only protein-protein interactions imex curation ran_human GTP-binding nuclear protein Ran GTPase Ran Ras-related nuclear protein Ras-like protein TC4 Androgen receptor-associated protein 24 RAN ARA24 OK/SW-cl.81 protein protein human Homo sapiens Human MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL ipo13_human Importin-13 Ran-binding protein 13 Karyopherin-13 IPO13 KIAA0724 RANBP13 protein protein human Homo sapiens Human MERREEQPGAAGAGAAPALDFTVENVEKALHQLYYDPNIENKNLAQKWLMQAQVSPQAWHFSWQLLQPDKVPEIQYFGASALHIKISRYWSDIPTDQYESLKAQLFTQITRFASGSKIVLTRLCVALASLALSMMPDAWPCAVADMVRLFQAEDSPVDGQGRCLALLELLTVLPEEFQTSRLPQYRKGLVRTSLAVECGAVFPLLEQLLQQPSSPSCVRQKVLKCFSSWVQLEVPLQDCEALIQAAFAALQDSELFDSSVEAIVNAISQPDAQRYVNTLLKLIPLVLGLQEQLRQAVQNGDMETSHGICRIAVALGENHSRALLDQVEHWQSFLALVNMIMFCTGIPGHYPVNETTSSLTLTFWYTLQDDILSFEAEKQAVYQQVYRPVYFQLVDVLLHKAQFPSDEEYGFWSSDEKEQFRIYRVDISDTLMYVYEMLGAELLSNLYDKLGRLLTSSEEPYSWQHTEALLYGFQSIAETIDVNYSDVVPGLIGLIPRISISNVQLADTVMFTIGALSEWLADHPVMINSVLPLVLHALGNPELSVSSVSTLKKICRECKYDLPPYAANIVAVSQDVLMKQIHKTSQCMWLMQALGFLLSALQVEEILKNLHSLISPYIQQLEKLAEEIPNPSNKLAIVHILGLLSNLFTTLDISHHEDDHEGPELRKLPVPQGPNPVVVVLQQVFQLIQKVLSKWLNDAQVVEAVCAIFEKSVKTLLDDFAPMVPQLCEMLGRMYSTIPQASALDLTRQLVHIFAHEPAHFPPIEALFLLVTSVTLTLFQQGPRDHPDIVDSFMQLLAQALKRKPDLFLCERLDVKAVFQCAVLALKFPEAPTVKASCGFFTELLPRCGEVESVGKVVQEDGRMLLIAVLEAIGGQASRSLMDCFADILFALNKHCFSLLSMWIKEALQPPGFPSARLSPEQKDTFSQQILRERVNKRRVKEMVKEFTLLCRGLHGTDYTADY if1ax_human Eukaryotic translation initiation factor 1A, X-chromosomal Eukaryotic translation initiation factor 4C EIF1AX EIF1A EIF4C protein protein human Homo sapiens Human MPKNKGKGGKNRRRGKNENESEKRELVFKEDGQEYAQVIKMLGNGRLEAMCFDGVKRLCHIRGKLRKKVWINTSDIILVGLRDYQDNKADVILKYNADEARSLKAYGELPEHAKINETDTFGPGDDDEIQFDDIGDDDEDIDDI mgn_human Protein mago nashi homolog MAGOH MAGOHA protein protein human Homo sapiens Human MESDFYLRYYVGHKGKFGHEFLEFEFRPDGKLRYANNSNYKNDVMIRKEAYVHKSVMEELKRIIDDSEITKEDDALWPPPDRVGRQELEIVIGDEHISFTTSKIGSLIDVNQSKDPEGLRVFYYLVQDLKCLVFSLIGLHFKIKPI rbm8a_human RNA-binding protein 8A HSPC114 MDS014 RNA-binding motif protein 8A Ribonucleoprotein RBM8A RNA-binding protein Y14 Binder of OVCA1-1 RBM8A RBM8 protein protein human Homo sapiens Human MADVLDLHEAGGEDFAMDEDGDESIHKLKEKAKKRKGRGFGSEEGSRARMREDYDSVEQDGDEPGPQRSVEGWILFVTGVHEEATEEDIHDKFAEYGEIKNIHLNLDRRTGYLKGYTLVEYETYKEAQAAMEGLNGQDLMGQPISVDWCFVRGPPKGKRRGGRRRSRSPDRRRR ubc9_human SUMO-conjugating enzyme UBC9 UBE2I p18 SUMO-protein ligase UBC9 UBCE9 Ubiquitin carrier protein 9 Ubiquitin carrier protein I Ubiquitin-conjugating enzyme E2 I Ubiquitin-protein ligase I RING-type E3 SUMO transferase UBC9 protein protein human Homo sapiens Human MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS ipo13-eif1ax-1 1498803 n/a 1498807 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.Asp369Arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false tag 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 false n/a 1498809 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified physical association physical association false false false f2c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-eif1ax-2 1498803 n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.Asp369_Asp370delinsArgArg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false tag 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 false n/a 1498807 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a 1498809 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified physical association physical association false false false f2c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-eif1ax-3 1498803 n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.Glu436Arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false tag 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 false n/a 1498807 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a 1498809 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified physical association physical association false false false f2c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-eif1ax-4 1498803 n/a 1498809 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.[Glu436Arg;Asp481Arg] mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false tag 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 false n/a 1498807 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false f2c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-eif1ax-5 1498803 n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.Asp481Arg mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false tag 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 false n/a 1498809 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified n/a 1498807 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false f2c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-eif1ax-6 1498803 n/a 1498809 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.Arg938Glu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false tag 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 false n/a 1498807 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false f2c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-eif1ax-7 1498803 n/a 1498807 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified tag 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 false n/a 1498809 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified P47813:p.Glu30_Asp31delinsArgArg mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false f3c ipo13-eif1ax-8 1498803 n/a 1498807 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified P62826:p.[Arg95Glu;Lys130Glu] mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified tag 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 false n/a 1498809 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified physical association physical association false false false f3c Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). ipo13-magoh-3 1498803 n/a 1498810 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified tag 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 false n/a 1498811 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified physical association physical association false false false 1498803 f5a ipo13-magoh-4 1498803 n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified tag 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 false n/a 1498812 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified direct interaction direct interaction false false false 1498803 f5a ipo13-eif1ax-9 1498803 n/a 1498809 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified n/a 1498807 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role prey prey purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role bait bait purified purified O94829:p.Lys802_Arg803delinsGluGlu mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing certain certain sequence position certain certain certain sequence position certain false tag 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 false physical association physical association false false false f5a Consistent with the structural analysis, reverse charge mutations of Asp369I, Asp370I, Glu436I and Asp481I to arginine in BS1 or of Arg938I to glutamate in BS2 resulted in reduction or loss of binding to eIF1A in pull-down assays (Figure 2C; Supplementary Figure 1). Notably, an Imp13 mutant unable to bind to Mago-Y14 (Lys803Glu/Arg803GluI) is also less efficient in exporting eIF1A in vivo (Figure 4I and K), reflecting a reduction in binding to eIF1A in vitro (Figure 5A). eif1ax-ipo13-3 1498804 n/a 1498808 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified n/a 1498807 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a 1498809 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association false false false 1498804 f3d To better understand the mechanism of the Imp13 import/export cycle, we measured the KD values by differential scanning fluorimetry (DSF) (Niesen et al, 2007) (Figure 3D; Supplementary Figure 3). The estimated KD for the two import cargoes Mago-Y14 and Ubc9 is in a similar range with a value of 235±30nM and 370±20 nM, respectively. The KD value for RanGTP binding to Imp13, although not accurately calculated due to the upper detection limit of the method, falls in the low nanomolar or picomolar range (o100 nM) and is consistent with values measured for other karyopherins (Bischoff and Go¨rlich, 1997; Deane et al, 1997; Go¨ rlich et al, 1997; Lipowsky et al, 2000). The dissociation constant of the export cargo eIF1A to a preformed Imp13-RanGTP complex is 3±0.38 mM, 10-fold higher than the KD values of the import cargoes (Figure 3D). eif1ax-ipo13-4 1498804 n/a 1498807 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a 1498808 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association false false false f3d sf3 To better understand the mechanism of the Imp13 import/export cycle, we measured the KD values by differential scanning fluorimetry (DSF) (Niesen et al, 2007) (Figure 3D; Supplementary Figure 3). The estimated KD for the two import cargoes Mago-Y14 and Ubc9 is in a similar range with a value of 235±30nM and 370±20 nM, respectively. The KD value for RanGTP binding to Imp13, although not accurately calculated due to the upper detection limit of the method, falls in the low nanomolar or picomolar range (o100 nM) and is consistent with values measured for other karyopherins (Bischoff and Go¨rlich, 1997; Deane et al, 1997; Go¨ rlich et al, 1997; Lipowsky et al, 2000). The dissociation constant of the export cargo eIF1A to a preformed Imp13-RanGTP complex is 3±0.38 mM, 10-fold higher than the KD values of the import cargoes (Figure 3D). eif1ax-ipo13-5 1498804 n/a 1498812 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified n/a 1498808 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association false false false 1498804 f3d sf3 To better understand the mechanism of the Imp13 import/export cycle, we measured the KD values by differential scanning fluorimetry (DSF) (Niesen et al, 2007) (Figure 3D; Supplementary Figure 3). The estimated KD for the two import cargoes Mago-Y14 and Ubc9 is in a similar range with a value of 235±30nM and 370±20 nM, respectively. The KD value for RanGTP binding to Imp13, although not accurately calculated due to the upper detection limit of the method, falls in the low nanomolar or picomolar range (o100 nM) and is consistent with values measured for other karyopherins (Bischoff and Go¨rlich, 1997; Deane et al, 1997; Go¨ rlich et al, 1997; Lipowsky et al, 2000). The dissociation constant of the export cargo eIF1A to a preformed Imp13-RanGTP complex is 3±0.38 mM, 10-fold higher than the KD values of the import cargoes (Figure 3D). eif1ax-ipo13-6 1498804 n/a 1498811 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified n/a 1498810 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified n/a 1498808 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association false false false 1498804 f3d sf3 To better understand the mechanism of the Imp13 import/export cycle, we measured the KD values by differential scanning fluorimetry (DSF) (Niesen et al, 2007) (Figure 3D; Supplementary Figure 3). The estimated KD for the two import cargoes Mago-Y14 and Ubc9 is in a similar range with a value of 235±30nM and 370±20 nM, respectively. The KD value for RanGTP binding to Imp13, although not accurately calculated due to the upper detection limit of the method, falls in the low nanomolar or picomolar range (o100 nM) and is consistent with values measured for other karyopherins (Bischoff and Go¨rlich, 1997; Deane et al, 1997; Go¨ rlich et al, 1997; Lipowsky et al, 2000). The dissociation constant of the export cargo eIF1A to a preformed Imp13-RanGTP complex is 3±0.38 mM, 10-fold higher than the KD values of the import cargoes (Figure 3D). eif1ax-ipo13-1 1498805 n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified n/a 1498809 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a 1498807 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false physical association physical association false false false f2d f2e eif1ax-ipo13-2 1498805 n/a 1498809 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified n/a 1498808 weight by comassie molecular weight estimation by coomasie staining weight by comassie unspecified role unspecified role neutral component neutral component purified purified direct interaction direct interaction false false false f2d f2e eif1ax-ipo13 1498806 n/a 1498809 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a 1498807 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified range binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false n/a 1498808 predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified physical association physical association false false false f1 t1 f2a f2b sf2b