DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ nesi-2010-1 ecolx Escherichia coli pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Nesić D., Miller MC., Quinkert ZT., Stein M., Chait BT., Stebbins CE. DIP original experiment: DIP-133953X Nature structural & molecular biology 2010 IMEx Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates. Nesić D., Miller MC., Quinkert ZT., Stein M., Chait BT., Stebbins CE. Only protein-protein interactions imex curation nesi-2010-2 in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Nesić D., Miller MC., Quinkert ZT., Stein M., Chait BT., Stebbins CE. DIP original experiment: DIP-133957X Nature structural & molecular biology 2010 IMEx Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates. Nesić D., Miller MC., Quinkert ZT., Stein M., Chait BT., Stebbins CE. Only protein-protein interactions imex curation nesi-2010-3 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Nesić D., Miller MC., Quinkert ZT., Stein M., Chait BT., Stebbins CE. DIP original experiment: DIP-133955X Nature structural & molecular biology 2010 IMEx Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates. Nesić D., Miller MC., Quinkert ZT., Stein M., Chait BT., Stebbins CE. Only protein-protein interactions imex curation nesi-2010-4 ecolx Escherichia coli ms of complexes mass spectrometry studies of complexes ms of complexes predetermined predetermined participant predetermined Nesić D., Miller MC., Quinkert ZT., Stein M., Chait BT., Stebbins CE. DIP original experiment: DIP-133958X Nature structural & molecular biology 2010 IMEx Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates. Nesić D., Miller MC., Quinkert ZT., Stein M., Chait BT., Stebbins CE. Only protein-protein interactions imex curation nesi-2010-5 in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Nesić D., Miller MC., Quinkert ZT., Stein M., Chait BT., Stebbins CE. DIP original experiment: DIP-133956X Nature structural & molecular biology 2010 IMEx Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates. Nesić D., Miller MC., Quinkert ZT., Stein M., Chait BT., Stebbins CE. Only protein-protein interactions imex curation nesi-2010-6 ecolx Escherichia coli 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 Nesić D., Miller MC., Quinkert ZT., Stein M., Chait BT., Stebbins CE. DIP original experiment: DIP-133954X Nature structural & molecular biology 2010 IMEx Helicobacter pylori CagA inhibits PAR1-MARK family kinases by mimicking host substrates. Nesić D., Miller MC., Quinkert ZT., Stein M., Chait BT., Stebbins CE. Only protein-protein interactions imex curation caga_helpy Cytotoxicity-associated immunodominant antigen 120 kDa protein CAG pathogenicity island protein 26 cai HP_0547 cagA cag26 protein protein helpy Helicobacter pylori Campylobacter pylori MTNETIDQTRTPDQTQSQTAFDPQQFINNLQVAFIKVDNVVASFDPDQKPIVDKNDRDNRQAFDGISQLREEYSNKAIKNPTKKNQYFSDFIDKSNDLINKDNLIDVESSTKSFQKFGDQRYQIFTSWVSHQKDPSKINTRSIRNFMENIIQPPIPDDKEKAEFLKSAKQSFAGIIIGNQIRTDQKFMGVFDESLKERQEAEKNGGPTGGDWLDIFLSFIFNKKQSSDVKEAINQEPVPHVQPDIATTTTDIQGLPPEARDLLDERGNFSKFTLGDMEMLDVEGVADIDPNYKFNQLLIHNNALSSVLMGSHNGIEPEKVSLLYAGNGGFGDKHDWNATVGYKDQQGNNVATLINVHMKNGSGLVIAGGEKGINNPSFYLYKEDQLTGSQRALSQEEIRNKVDFMEFLAQNNTKLDNLSEKEKEKFQNEIEDFQKDSKAYLDALGNDRIAFVSKKDTKHSALITEFNNGDLSYTLKDYGKKADKALDREKNVTLQGSLKHDGVMFVDYSNFKYTNASKNPNKGVGATNGVSHLEAGFNKVAVFNLPDLNNLAITSFVRRNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFNKAVAEAKSTGNYDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARAIAYTQNLKGIKRELSDKLEKISKDLKDFSKSFDEFKNGKNKDFSKAEETLKALKGSVKDLGINPEWISKVENLNAALNEFKNGKNKDFSKVTQAKSDLENSVKDVIINQKVTDKVDNLNQAVSVAKAMGDFSRVEQVLADLKNFSKEQLAQQAQKNEDFNTGKNSELYQSVKNSVNKTLVGNGLSGIEATALAKNFSDIKKELNEKFKNFNNNNNGLKNSTEPIYAKVNKKKTGQVASPEEPIYTQVAKKVNAKIDRLNQIASGLGGVGQAAGFPLKRHDKVDDLSKVGLSASPEPIYATIDDLGGPFPLKRHDKVDDLSKVGRSRNQELAQKIDNLNQAVSEAKAGFFGNLEQTIDKLKDSTKKNVMNLYVESAKKVPASLSAKLDNYAINSHTRINSNIQNGAINEKATGMLTQKNPEWLKLVNDKIVAHNVGSVSLSEYDKIGFNQKNMKDYSDSFKFSTKLNNAVKDIKSGFTHFLANAFSTGYYCLARENAEHGIKNVNTKGGFQKS mark2_human Serine/threonine-protein kinase MARK2 MAP/microtubule affinity-regulating kinase 2 ELKL motif kinase 1 PAR1 homolog MARK2 EMK1 PAR1 homolog b protein protein human Homo sapiens Human MSSARTPLPTLNERDTEQPTLGHLDSKPSSKSNMIRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYKSSELEGDTITLKPRPSADLTNSSAPSPSHKVQRSVSANPKQRRFSDQAAGPAIPTSNSYSKKTQSNNAENKRPEEDRESGRKASSTAKVPASPLPGLERKKTTPTPSTNSVLSTSTNRSRNSPLLERASLGQASIQNGKDSLTMPGSRASTASASAAVSAARPRQHQKSMSASVHPNKASGLPPTESNCEVPRPSTAPQRVPVASPSAHNISSSGGAPDRTNFPRGVSSRSTFHAGQLRQVRDQQNLPYGVTPASPSGHSQGRRGASGSIFSKFTSKFVRRNLSFRFARRNLNEPESKDRVETLRPHVVGSGGNDKEKEEFREAKPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHEKYMLLCMHGTPGHEDFVQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL taok1_human Serine/threonine-protein kinase TAO1 Prostate-derived sterile 20-like kinase 2 Thousand and one amino acid protein kinase 1 TAOK1 KIAA1361 MAP3K16 MARKK MARK Kinase Kinase from chicken homolog B protein protein human Homo sapiens Human MPSTNRAGSLKDPEIAELFFKEDPEKLFTDLREIGHGSFGAVYFARDVRTNEVVAIKKMSYSGKQSTEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHTMIHRDIKAGNILLTEPGQVKLADFGSASMASPANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESPTLQSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKHIFVLRERPETVLIDLIQRTKDAVRELDNLQYRKMKKLLFQEAHNGPAVEAQEEEEEQDHGVGRTGTVNSVGSNQSIPSMSISASSQSSSVNSLPDVSDDKSELDMMEGDHTVMSNSSVIHLKPEEENYREEGDPRTRASDPQSPPQVSRHKSHYRNREHFATIRTASLVTRQMQEHEQDSELREQMSGYKRMRRQHQKQLMTLENKLKAEMDEHRLRLDKDLETQRNNFAAEMEKLIKKHQAAMEKEAKVMSNEEKKFQQHIQAQQKKELNSFLESQKREYKLRKEQLKEELNENQSTPKKEKQEWLSKQKENIQHFQAEEEANLLRRQRQYLELECRRFKRRMLLGRHNLEQDLVREELNKRQTQKDLEHAMLLRQHESMQELEFRHLNTIQKMRCELIRLQHQTELTNQLEYNKRRERELRRKHVMEVRQQPKSLKSKELQIKKQFQDTCKIQTRQYKALRNHLLETTPKSEHKAVLKRLKEEQTRKLAILAEQYDHSINEMLSTQALRLDEAQEAECQVLKMQLQQELELLNAYQSKIKMQAEAQHDRELRELEQRVSLRRALLEQKIEEEMLALQNERTERIRSLLERQAREIEAFDSESMRLGFSNMVLSNLSPEAFSHSYPGASGWSHNPTGGPGPHWGHPMGGPPQAWGHPMQGGPQPWGHPSGPMQGVPRGSSMGVRNSPQALRRTASGGRTEQGMSRSTSVTSQISNGSHMSYT tr1tau TR1 peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) KNVKSKIGSTENLK caga-mark2-1 3200645 N/A 3200651 unspecified role unspecified role bait bait EPIYA repeat domain Region 885-981 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range false P55980:p.Leu950Gly L950G mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P55980:p.Arg952Gly R952G mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P55980:p.Val956Gly V956G mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false P55980:p.Leu959Gly L959G mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3200652 unspecified role unspecified role prey prey Kinase domain Region 39-364 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false Q7KZI7:p.[Glu136Gly;Phe138Gly;Asp139Gly] E136G/F138G/D139G mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli physical association physical association false false false mark2-taok1-1 3200646 N/A 3200653 enzyme enzyme unspecified role unspecified role Region 1-314 Region 1-314 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm N/A 3200652 enzyme target enzyme target substrate substrate unspecified role unspecified role Kinase domain Region 39-364 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation false false false caga-mark2-2 3200647 N/A 3200651 unspecified role unspecified role unspecified role unspecified role EPIYA repeat domain Region 885-1006 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3200652 unspecified role unspecified role unspecified role unspecified role Kinase domain Region 39-364 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false caga-mark2-3 3200648 N/A 3200651 unspecified role unspecified role unspecified role unspecified role EPIYA repeat domain Region 885-1006 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3200652 unspecified role unspecified role unspecified role unspecified role Kinase domain Region 39-364 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false mark2-tr1tau-1 3200649 N/A 3200654 enzyme target enzyme target substrate substrate unspecified role unspecified role in vitro In vitro N/A 3200652 enzyme enzyme unspecified role unspecified role Kinase domain Region 39-364 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation false false false caga-mark2-4 3200650 N/A 3200651 unspecified role unspecified role unspecified role unspecified role EPIYA repeat domain Region 885-981 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli N/A 3200652 unspecified role unspecified role unspecified role unspecified role Kinase domain Region 39-364 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain false ecolx Escherichia coli direct interaction direct interaction false false false