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/ Regulation of the Pro-apoptotic scaffolding protein POSH by Akt. Regulation of the Pro-apoptotic scaffolding protein POSH by Akt. J. Biol. Chem. (0021-9258) 2007 imex curation Lyons TR., Thorburn J., Ryan PW., Thorburn A., Anderson SM., Kassenbrock CK. Apoptosis - Interactions involving proteins with a function related to apoptosis Detailed information on Akt1 and Akt2 taken from manufacturer's website. Ken.Kassenbrock@uchsc.edu davet Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Lyons TR., Thorburn J., Ryan PW., Thorburn A., Anderson SM., Kassenbrock CK. Apoptosis - Interactions involving proteins with a function related to apoptosis Detailed information on Akt1 and Akt2 taken from manufacturer's website. Ken.Kassenbrock@uchsc.edu Accepted 2007-SEP-28 by DAVET. J. Biol. Chem. (0021-9258) 2007 davet Only protein-protein interactions imex curation akt1_human RAC-alpha serine/threonine-protein kinase AKT1 PKB RAC RAC-PK-alpha Protein kinase B Proto-oncogene c-Akt Protein kinase B alpha protein protein human Homo sapiens Human MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA DIP protein P31749 original sequence version: 184 DIP protein P31749 original sequence version: 168 DIP protein P31749 original sequence version: 102 DIP protein P31749 original sequence version: 110 DIP protein P31749 original sequence version: 160 DIP protein P31749 original sequence version: 136 DIP protein P31749 original sequence version: 175 DIP protein P31749 original sequence version: 201 DIP protein P31749 original sequence version: 166 DIP protein P31749 original sequence version: 178 DIP protein P31749-1 original sequence version: 194 DIP protein P31749 original sequence version: 106 DIP protein P31749 original sequence version: 141 6EAFF4F8AD436714 akt2_human RAC-beta serine/threonine-protein kinase AKT2 RAC-PK-beta Protein kinase Akt-2 Protein kinase B beta protein protein human Homo sapiens Human MNEVSVIKEGWLHKRGEYIKTWRPRYFLLKSDGSFIGYKERPEAPDQTLPPLNNFSVAECQLMKTERPRPNTFVIRCLQWTTVIERTFHVDSPDEREEWMRAIQMVANSLKQRAPGEDPMDYKCGSPSDSSTTEEMEVAVSKARAKVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITPPDRYDSLGLLELDQRTHFPQFSYSASIRE DIP protein P31751 original sequence version: 137 DIP protein P31751 original sequence version: 155 B18C87A7246BFB24 sh3r1_human E3 ubiquitin-protein ligase SH3RF1 SH3RF1 POSH1 KIAA1494 POSH RNF142 SH3MD2 SH3 domain-containing RING finger protein 1 Plenty of SH3s SH3 multiple domains protein 2 RING finger protein 142 RING-type E3 ubiquitin transferase SH3RF1 protein protein human Homo sapiens Human MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVEELPSNILLVRLLDGIKQRPWKPGPGGGSGTNCTNALRSQSSTVANCSSKDLQSSQGGQQPRVQSWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIILRRQVDENWYHGEVNGIHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEGMLADKIGIFPISYVEFNSAAKQLIEWDKPPVPGVDAGECSSAAAQSSTAPKHSDTKKNTKKRHSFTSLTMANKSSQASQNRHSMEISPPVLISSSNPTAAARISELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPSDVPYQAALGTLNPPLPPPPLLAATVLASTPPGATAAAAAAGMGPRPMAGSTDQIAHLRPQTRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFPGNYVAPVTRAVTNASQAKVPMSTAGQTSRGVTMVSPSTAGGPAQKLQGNGVAGSPSVVPAAVVSAAHIQTSPQAKVLLHMTGQMTVNQARNAVRTVAAHNQERPTAAVTPIQVQNAAGLSPASVGLSHHSLASPQPAPLMPGSATHTAAISISRASAPLACAAAAPLTSPSITSASLEAEPSGRIVTVLPGLPTSPDSASSACGNSSATKPDKDSKKEKKGLLKLLSGASTKRKPRVSPPASPTLEVELGSAELPLQGAVGPELPPGGGHGRAGSCPVDGDGPVTTAVAGAALAQDAFHRKASSLDSAVPIAPPPRQACSSLGPVLNESRPVVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI DIP protein Q7Z6J0 original sequence version: 99 B3018000F03D0CF1 sh3rf1-akt1-1 1 4 enzyme target enzyme target substrate substrate unspecified role unspecified role n-terminal gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-1374207]The shifted ranges (53-720) couldn't be applied as the new full feature sequence is different from the previous one. [EBI-1374207]53-888 [EBI-1374207]Q7Z6J0,1 ecobb Escherichia coli (strain B / BL21) 2 enzyme enzyme unspecified role unspecified role n-terminal 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 spofr-sf_9 Spodoptera frugiperda insect cells Fall armyworm sf_9 insect cells Derived from pupal ovarian tissue of the fall armyworm Cloned from the parent cell line, IPLB-SF-21-AE (SF-21) derived from immature ovaries of fall armyworm Spodoptera frugiperda pupae cells are susceptible to Baculovirus infection phosphorylation phosphorylation reaction phosphorylation Phosphorylation of SH3RF1 on Ser-472, and to a lesser extent Ser-125, Ser-968 as confirmed by mass spectrometry analysis of tryptic peptides. It can be seen that full-length GST-POSH is indeed directly phosphorylated by both Akt1 and Akt2 in vitro, whereas GST alone is unmodified (Fig. 2B, compare lanes 5 and 6 with 2 and 3). Fig. 2B, 3 and 4 Mutation of Ser-472 of POSH (Q7Z6J0) reduced phosphorylation by Akt1 sh3rf1-akt2-1 1 4 enzyme target enzyme target substrate substrate unspecified role unspecified role n-terminal gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined [EBI-1374426]The shifted ranges (53-720) couldn't be applied as the new full feature sequence is different from the previous one. [EBI-1374426]53-888 [EBI-1374426]Q7Z6J0,1 ecobb Escherichia coli (strain B / BL21) 3 enzyme enzyme unspecified role unspecified role n-terminal 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 region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain spofr-sf_9 Spodoptera frugiperda insect cells Fall armyworm sf_9 insect cells Derived from pupal ovarian tissue of the fall armyworm Cloned from the parent cell line, IPLB-SF-21-AE (SF-21) derived from immature ovaries of fall armyworm Spodoptera frugiperda pupae cells are susceptible to Baculovirus infection phosphorylation phosphorylation reaction phosphorylation Phosphorylation of SH3RF1 on Ser-472, and to a lesser extent Ser-125, Ser-968 as confirmed by mass spectrometry analysis of tryptic peptides. It can be seen that full-length GST-POSH is indeed directly phosphorylated by both Akt1 and Akt2 in vitro, whereas GST alone is unmodified (Fig. 2B, compare lanes 5 and 6 with 2 and 3). Fig. 2B, 3 and 4 Mutation of Ser-472 of POSH (Q7Z6J0) reduced phosphorylation by Akt2