DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes. Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Ertürk-Hasdemir D., Broemer M., Leulier F., Lane WS., Paquette N., Hwang D., Kim CH., Stöven S., Meier P., Silverman N. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Ertürk-Hasdemir D., Broemer M., Leulier F., Lane WS., Paquette N., Hwang D., Kim CH., Stöven S., Meier P., Silverman N. DIP original experiment: DIP-260326X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes. Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes. Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Ertürk-Hasdemir D., Broemer M., Leulier F., Lane WS., Paquette N., Hwang D., Kim CH., Stöven S., Meier P., Silverman N. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Ertürk-Hasdemir D., Broemer M., Leulier F., Lane WS., Paquette N., Hwang D., Kim CH., Stöven S., Meier P., Silverman N. DIP original experiment: DIP-260328X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes. Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes. Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Ertürk-Hasdemir D., Broemer M., Leulier F., Lane WS., Paquette N., Hwang D., Kim CH., Stöven S., Meier P., Silverman N. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Ertürk-Hasdemir D., Broemer M., Leulier F., Lane WS., Paquette N., Hwang D., Kim CH., Stöven S., Meier P., Silverman N. DIP original experiment: DIP-260327X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Two roles for the Drosophila IKK complex in the activation of Relish and the induction of antimicrobial peptide genes. q94527-1 Nuclear factor NF-kappa-B p110 subunit C p110 Rel-p110 Relish protein CG11992 A B Rel protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MNMNQYYDLDNGKNVMFMNDASSTSGYSSSTSPNSTNRSFSPAHSPKTMELQTDFANLNLPGGNSPHQPPMANSPYQNQLLNNGGICQLGATNLINSTGVSFGVANVTSFGNMYMDHQYFVPAPATVPPSQNFGYHQNGLASDGDIKHVPQLRIVEQPVEKFRFRYKSEMHGTHGSLNGANSKRTPKTFPEVTLCNYDGPAVIRCSLFQTNLDSPHSHQLVVRKDDRDVCDPHDLHVSKERGYVAQFINMGIIHTAKKYIFEELCKKKQDRLVFQMNRRELSHKQLQELHQETEREAKDMNLNQVRLCFEAFKIEDNGAWVPLAPPVYSNAINNRKSAQTGELRIVRLSKPTGGVMGNDELILLVEKVSKKNIKVRFFEEDEDGETVWEAYAKFRESDVHHQYAIVCQTPPYKDKDVDREVNVYIELIRPSDDERSFPALPFRYKPRSVIVSRKRRRTGSSANSSSSGTESSNNSLDLPKTLGLAQPPNGLPNLSQHDQTISEEFGREKHLNEFIASEDFRKLIEHNSSDLEKICQLDMGELQHDGHNRAEVPSHRNRTIKCLDDLFEIYKQDRISPIKISHHKVEKWFIEHALNNYNRDTLLHEVISHKKDKLKLAIQTIQVMNYFNLKDVVNSTLNADGDSALHVACQQDRAHYIRPLLGMGCNPNLKNNAGNTPLHVAVKEEHLSCVESFLNGVPTVQLDLSLTNDDGLTPLHMAIRQNKYDVAKKLISYDRTSISVANTMDGNNALHMAVLEQSVELLVLILDAQNENLTDILQAQNAAGHTPLELAERKANDRVVQLLKNVYPEKGELAMTWIPCKVKEEIDSSSDESSDAGQLEIKSEEMDIETKDEDSVELDLSSGPRRQKDESSRDTEMDNNKLQLLLKNKFIYDRLCSLLNQPLGHGSDPQDRKWMQLARQTHLKQFAFIWLGAEDLLDHVKRKGASVEFSTFARALQAVDPQAYALLVNPT DIP protein Q94527-1 original sequence version: 94 DIP protein Q94527-1 original sequence version: 118 ikkb_drome Inhibitor of nuclear factor kappa-B kinase subunit beta IKKbeta Cactus kinase IKK DIK IKK-like protein Immune response deficient protein 5 Lipopolysaccharide-activated kinase ird5 CG4201 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MITVVFCFSDCHGGIQILGRMSSVNKIKLNENNKMHSFGNWERCRNLGEGGFGLVIHWRNRTTGREIATKHIKEMGALSADQQVKLSERWNKELNWSRQFKNFPHIVAGVDIEDPDFLEYLNGMFSAKLPVIVLEYCNGGDVRKRLQSPENANGLTEFEVRQILGALRKALHFLHSQCGICHRDLKPDNIVIQRGVDGKKIYKLTDFGLARGTPDQTMVQSVVGTRHYYAPEVVENGFYNSTVDLWSFGVIAYELVTGELPFIPHQTLKNIILNLIKKPAKCIAITEDPEDNTRFVNQFELPQTHHLSRPWAAQFTKWLASPLNSNYKERGQLAANNVPVVFADLDKILNMNVLTIFAVNNCERLEYAVSAEMTMKDLIALIVLDTGMDEKELYFVLPTSHPHKTITPKSTPLQLYVEEWSDTSKDSRKWTKRSNPPVMLYIFQVKKECDYKIPEPILSILSRKFIANKFKTKERWLQKRVVLDMLYVLTKEQARYEMLVSGINERALSLEDEMMENSFIDSIDKQRIIISFAYDQLTSLLKEAQAKIPSRQLISSAQWEKLNRNYNFIIQSAKSIRSFLEACLREAKDMVKTTNQLRKEVCEKDLFDCARFYKKYLCNGAIISPSELNNDAEEFAKSRFKLYNEGEARHLPKSIDHMHYLYFKTKESIPVLLQQFCDIKKEIFQINLQMLMSASSTPPPKLELSAAMDRLAISSGSPSSDPFDSLRTINAIEEAERINNILVNEMKIDHY DIP protein Q9VEZ5 original sequence version: 117 0BD2452BED2F8E78 ird5-1 2 5 putative self putative self unspecified role unspecified role Q9VEZ5:p.Lys70Ala K50A mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain K A Wed May 02 16:51:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys70ala' Tue Jun 30 16:29:06 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys70Ala' spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm phosphorylation phosphorylation reaction phosphorylation true ird5-rel-1 1 5 enzyme enzyme unspecified role unspecified role Q9VEZ5:p.Lys70Ala K50A mutation disrupting rate mutation disrupting interaction rate mutation disrupting rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain K A Wed May 02 17:47:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys70ala' Tue Jun 30 18:50:55 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys70Ala' spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 4 enzyme target enzyme target substrate substrate unspecified role unspecified role pS528/529 pS528/529 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations western blot western blot Immuno blot Immuno blot certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm phosphorylation phosphorylation reaction phosphorylation ird5-rel-2 3 5 enzyme enzyme unspecified role unspecified role spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 4 enzyme target enzyme target substrate substrate unspecified role unspecified role pS528/529 pS528/529 opser O-phospho-L-serine (2S)-2-amino-3-(phosphonooxy)propanoic acid 2-amino-3-hydroxypropanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)propanoic acid ACT_SITE Phosphoserine intermediate MOD_RES Phosphoserine O-phospho-L-serine O-phosphonoserine O-phosphorylated L-serine O3-phosphoserine serine phosphate ester OPSer Phospho Phospho Seryl Phosphorylation phosphorylations western blot western blot Immuno blot Immuno blot certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain certain certain sequence position certain Q94527-1:p.[Ser528Ala;Ser529Ala] S528A/S529A mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain S A certain certain sequence position certain certain certain sequence position certain S A This feature has been corrected as a result of our quality control procedures. The original label was 'S528A/S529A'. Wed May 02 16:39:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser528ala,ser529ala' Tue Jun 30 17:05:14 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Ser528Ala;Ser529Ala]' in vitro In vitro phosphorylation phosphorylation reaction phosphorylation