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/ http://www.ebi.ac.uk/ mortier-2006-1 Soluble interleukin-15 receptor alpha (IL-15R alpha)-sushi as a selective and potent agonist of IL-15 action through IL-15R beta/gamma. Hyperagonist IL-15 x IL-15R alpha fusion proteins. in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Mortier E., Quemener A., Vusio P., Lorenzen I., Boublik Y., Grotzinger J., Plet A., Jacques Y. BioCreative - Critical Assessment of Information Extraction systems in Biology yjacques@nantes.inserm.fr J. Biol. Chem. (0021-9258) 2006 Only protein-protein interactions imex curation i15ra_human Interleukin-15 receptor subunit alpha IL15RA protein protein human Homo sapiens Human MAPRRARGCRTLGLPALLLLLLLRPPATRGITCPPPMSVEHADIWVKSYSLYSRERYICNSGFKRKAGTSSLTECVLNKATNVAHWTTPSLKCIRDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKEPAASSPSSNNTAATTAAIVPGSQLMPSKSPSTGTTEISSHESSHGTPSQTTAKNWELTASASHQPPGVYPQGHSDTTVAISTSTVLLCGLSAVSLLACYLKSRQTPPLASVEMEAMEALPVTWGTSSRDEDLENCSHHL il15_human Interleukin-15 IL15 protein protein human Homo sapiens Human MRISKPHLRSISIQCYLCLLLNSHFLTEAGIHVFILGCFSAGLPKTEANWVNVISDLKKIEDLIQSMHIDATLYTESDVHPSCKVTAMKCFLLELQVISLESGDASIHDTVENLIILANNSLSSNGNVTESGCKECEELEEKNIKEFLQSFVHIVQMFINTS il15-il15ra sIL-15Ralpha-IL-2 502688 N/A 502689 unspecified role unspecified role bait bait n-terminal sIL-15Ralpha-IL-2 binding region binding-associated region binding region range range certain certain sequence position certain false c-terminal human IL-2 - used as a tag for purification fusion protein fusion protein c-term range C-terminal range c-term range c-term range C-terminal range c-term range false crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. N/A 502690 unspecified role unspecified role prey prey c-terminal recombinant humanIL-15 from Peprotech Inc. sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) physical association physical association false false false The recombinant IL-15 from Peprotech Inc. corresponds to residues 48-162 of the Uniprot entry except at position 48 there is met substituted for ala. 1 A kon =3.7 E5 per M per S; koff =1.4 E-5 per s; Kd=3.8 E-11 M These results indicate that the sushi domain is responsible for most of the binding affinity of IL-15 but that it does not fully reconstitute the high affinity binding displayed by the full-length extracellular domain. The IL-15Ralpha proteins are annotated to begin at residue 31 as the Uniprot annotation indicates residues 1-30 constitute a signal peptide, which should be removed when expressed in CHO cells. il15-il15ra-1 sIL-15Ralpha-sushi-IL-2 CHO 502688 N/A 502690 unspecified role unspecified role prey prey c-terminal recombinant humanIL-15 from Peprotech Inc. sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) N/A 502689 unspecified role unspecified role bait bait c-terminal human IL-2 - used as a tag for purification fusion protein fusion protein c-term range C-terminal range c-term range c-term range C-terminal range c-term range false n-terminal sIL-15Ralpha-sushi-IL-2 binding region binding-associated region binding region range range range range false crigr-cho chinese hamster ovary cell line cho chinese hamster ovary cell line Also called LR73 cells. physical association physical association false false false The recombinant IL-15 from Peprotech Inc. corresponds to residues 48-162 of the Uniprot entry except at position 48 there is met substituted for ala. 1 B kon=3.1 E5 per M per s; koff =1.3 E-4 per s; Kd =4.2 E-10 M These results indicate that the sushi domain is responsible for most of the binding affinity of IL-15 but that it does not fully reconstitute the high affinity binding displayed by the full-length extracellular domain. The IL-15Ralpha proteins are annotated to begin at residue 31 as the Uniprot annotation indicates residues 1-30 constitute a signal peptide, which should be removed when expressed in CHO cells. il15-il15ra-2 sIL-15Ralpha-sushi E. coli 502688 N/A 502690 unspecified role unspecified role prey prey c-terminal recombinant humanIL-15 from Peprotech Inc. sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false ecoli Escherichia coli (strain K12) N/A 502689 unspecified role unspecified role bait bait n-terminal sIL-15Ralpha-sushi binding region binding-associated region binding region range range range range false ecoli Escherichia coli (strain K12) physical association physical association false false false The recombinant IL-15 from Peprotech Inc. corresponds to residues 48-162 of the Uniprot entry except at position 48 there is met substituted for ala. 1 C kon =2.5 E5 per M per s ; koff=3.8 E-4 per s; Kd= 1.5 E-9 M It is not clear if the signal peptide (Uniprot annotation indicates it is residues 1-30 of the sequence) is removed from the sIL-15Ralpha-sushi expressed in E. coli (referred to in the annotation topic kinetics). Nor is it clear if this protein is fused to human Il-2, but it seems not as IL-2 is not included in the name of the construct. These results indicate that the sushi domain is responsible for most of the binding affinity of IL-15 but that it does not fully reconstitute the high affinity binding displayed by the full-length extracellular domain. The IL-15Ralpha proteins are annotated to begin at residue 31 as the Uniprot annotation indicates residues 1-30 constitute a signal peptide, which should be removed when expressed in CHO cells.