DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. Nature structural & molecular biology 2009 imex curation Díaz-Moreno I., Hollingworth D., Frenkiel TA., Kelly G., Martin S., Howell S., García-Mayoral M., Gherzi R., Briata P., Ramos A. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Díaz-Moreno I., Hollingworth D., Frenkiel TA., Kelly G., Martin S., Howell S., García-Mayoral M., Gherzi R., Briata P., Ramos A. DIP original experiment: DIP-132962X Nature structural & molecular biology 2009 IMEx Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. Nature structural & molecular biology 2009 imex curation Díaz-Moreno I., Hollingworth D., Frenkiel TA., Kelly G., Martin S., Howell S., García-Mayoral M., Gherzi R., Briata P., Ramos A. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Díaz-Moreno I., Hollingworth D., Frenkiel TA., Kelly G., Martin S., Howell S., García-Mayoral M., Gherzi R., Briata P., Ramos A. DIP original experiment: DIP-132963X Nature structural & molecular biology 2009 IMEx Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. Nature structural & molecular biology 2009 imex curation Díaz-Moreno I., Hollingworth D., Frenkiel TA., Kelly G., Martin S., Howell S., García-Mayoral M., Gherzi R., Briata P., Ramos A. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Díaz-Moreno I., Hollingworth D., Frenkiel TA., Kelly G., Martin S., Howell S., García-Mayoral M., Gherzi R., Briata P., Ramos A. DIP original experiment: DIP-132961X Nature structural & molecular biology 2009 IMEx Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding. 1433z_mouse 14-3-3 protein zeta/delta Ywhaz Protein kinase C inhibitor protein 1 SEZ-2 protein protein mouse Mus musculus Mouse MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEERNLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREYREKIETELRDICNDVLSLLEKFLIPNASQPESKVFYLKMKGDYYRYLAEVAAGDDKKGIVDQSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDTQGDEAEAGEGGEN DIP protein P63101 original sequence version: 72 2164DF3793B45B7A fubp2_human Far upstream element-binding protein 2 KH type-splicing regulatory protein p75 KHSRP FUBP2 protein protein human Homo sapiens Human MSDYSTGGPPPGPPPPAGGGGGAGGAGGGPPPGPPGAGDRGGGGPGGGGPGGGSAGGPSQPPGGGGPGIRKDAFADAVQRARQIAAKIGGDAATTVNNSTPDFGFGGQKRQLEDGDQPESKKLASQGDSISSQLGPIHPPPRTSMTEEYRVPDGMVGLIIGRGGEQINKIQQDSGCKVQISPDSGGLPERSVSLTGAPESVQKAKMMLDDIVSRGRGGPPGQFHDNANGGQNGTVQEIMIPAGKAGLVIGKGGETIKQLQERAGVKMILIQDGSQNTNVDKPLRIIGDPYKVQQACEMVMDILRERDQGGFGDRNEYGSRIGGGIDVPVPRHSVGVVIGRSGEMIKKIQNDAGVRIQFKQDDGTGPEKIAHIMGPPDRCEHAARIINDLLQSLRSGPPGPPGGPGMPPGGRGRGRGQGNWGPPGGEMTFSIPTHKCGLVIGRGGENVKAINQQTGAFVEISRQLPPNGDPNFKLFIIRGSPQQIDHAKQLIEEKIEGPLCPVGPGPGGPGPAGPMGPFNPGPFNQGPPGAPPHAGGPPPHQYPPQGWGNTYPQWQPPAPHDPSKAAAAAADPNAAWAAYYSHYYQQPPGPVPGPAPAPAAPPAQGEPPQPPPTGQSDYTKAWEEYYKKIGQQPQQPGAPPQQDYTKAWEEYYKKQAQVATGGGPGAPPGSQPDYSAAWAEYYRQQAAYYGQTPGPGGPQPPPTQQGQQQAQ DIP protein Q92945 original sequence version: 95 DIP protein Q92945 original sequence version: 98 DIP protein Q92945 original sequence version: 128 AB0B7C0B5B938114 kh1peptide KH1-derived peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) YGLPERSVSLTGAPES 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 kh1peptide-ywhaz-1 3 4 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role pSer9 pSer9 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 certain certain sequence position certain certain certain sequence position certain in vitro In vitro direct interaction direct interaction khsrp-ywhaz-1 2 4 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role Region 130-218 Region 130-218 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli direct interaction direct interaction akt1-khsrp-1 1 7 enzyme enzyme unspecified role unspecified role spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 5 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 130-218 Region 130-218 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q92945:p.Ser193Ala S193A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis 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 'S193A'. Wed May 02 18:26:53 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser193ala' Tue Jun 30 19:34:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser193Ala' ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation