{"context":{"query":">>uniprot>>ufeature","source_dataset":"uniprot","target_dataset":"ufeature"},"stats":{"queried":1,"total":100,"mapped":1},"pagination":{"has_next":true,"next_token":"-1[]P31749,1,P31749,84,5]["},"schema":"id|type|description|location_begin|location_end","mappings":[{"input":"P31749","source":"P31749|RAC-alpha serine/threonine-protein kinase","targets":["P31749_F0|chain|rac-alpha serine/threonine-protein kinase|1|480","P31749_F1|domain|ph|5|108","P31749_F10|binding site||86|86","P31749_F100|helix||354|363","P31749_F101|helix||374|383","P31749_F102|helix||388|390","P31749_F103|turn||396|398","P31749_F104|helix||399|403","P31749_F105|helix||406|408","P31749_F106|helix||413|417","P31749_F107|strand||430|433","P31749_F108|turn||436|438","P31749_F109|helix||440|443","P31749_F11|binding site||156|164","P31749_F110|strand||464|466","P31749_F111|strand||473|475","P31749_F12|binding site||179|179","P31749_F13|site|cleavage; by caspase-3|462|462","P31749_F14|modified residue|n6-acetyllysine|14|14","P31749_F15|modified residue|n6-acetyllysine|20|20","P31749_F16|modified residue|phosphoserine|124|124","P31749_F17|modified residue|phosphoserine; alternate|126|126","P31749_F18|modified residue|phosphoserine; alternate|129|129","P31749_F19|modified residue|phosphotyrosine; by tnk2|176|176","P31749_F2|domain|protein kinase|150|408","P31749_F20|modified residue|phosphothreonine; by ikke, pdpk1 and tbk1|308|308","P31749_F21|modified residue|phosphothreonine|448|448","P31749_F22|modified residue|phosphothreonine|450|450","P31749_F23|modified residue|phosphoserine; by ikke, mtor, prkdc and tbk1; alternate|473|473","P31749_F24|modified residue|phosphotyrosine|474|474","P31749_F25|modified residue|phosphoserine; by cdk2 and mtor|477|477","P31749_F26|modified residue|phosphothreonine; by cdk2 and mtor|479|479","P31749_F27|glycosylation site|o-linked (glcnac) serine; alternate|126|126","P31749_F28|glycosylation site|o-linked (glcnac) serine; alternate|129|129","P31749_F29|glycosylation site|o-linked (glcnac) threonine|305|305","P31749_F3|domain|agc-kinase c-terminal|409|480","P31749_F30|glycosylation site|o-linked (glcnac) threonine|312|312","P31749_F31|glycosylation site|o-linked (glcnac) serine; alternate|473|473","P31749_F32|disulfide bond||60|77","P31749_F33|disulfide bond||296|310","P31749_F34|cross-link|glycyl lysine isopeptide (lys-gly) (interchain with g-cter in ubiquitin)|284|284","P31749_F35|splice variant|in isoform 2.|1|62","P31749_F36|sequence variant|in proteuss and breast cancer; also detected in colorectal and ovarian cancer; somatic mutation; results in increased phosphorylation at t-308 and higher basal ubiquitination; the mutant protein is more efficiently recruited to the plasma membrane; alters phosphatidylinositiol phosphates lipid specificity of the akt1 ph domain; dbsnp:rs121434592.|17|17","P31749_F37|sequence variant|in cws6; impairs interaction with ptdins(3,4,5)p3 and ptdins(3,4)p2; dbsnp:rs397514644.|25|25","P31749_F38|sequence variant|in dbsnp:rs11555433.|167|167","P31749_F39|sequence variant|in cws6; dbsnp:rs397514645.|435|435","P31749_F4|region of interest|disordered|113|138","P31749_F40|mutagenesis site|substantial reduction of ubiquitination, phosphorylation at t-308 and s-473, akt activation as well as igf1-induced membrane recruitment. decrease in ubiquitination and phosphorylation at t-308 as well as impaired association with the membrane; when associated with k-17.|8|8","P31749_F41|mutagenesis site|impairs interaction with ptdins(3,4,5)p3 and ptdins(3,4)p2.|14|14","P31749_F42|mutagenesis site|substantial reduction of phosphorylation at t-308 and s-473, loss of akt activation, and loss of binding to pip3 as well as igf1-induced membrane recruitment.|14|14","P31749_F43|mutagenesis site|substantial reduction of ubiquitination, phosphorylation at t-308 and s-473, akt activation, loss of binding to pip3 as well as igf1-induced membrane recruitment.|14|14","P31749_F44|mutagenesis site|loss of membrane localization; when associated with q-20.|17|17","P31749_F45|mutagenesis site|substantial reduction of phosphorylation at t-308 and s-473, reduced akt activation, and reduced binding to pip3 as well as igf1-induced membrane recruitment. loss of membrane localization; when associated with k-17.|20|20","P31749_F46|mutagenesis site|slight increase of phosphorylation at t-308 and s-473.|20|20","P31749_F47|mutagenesis site|impairs interaction with ptdins(3,4,5)p3 and ptdins(3,4)p2.|25|25","P31749_F48|mutagenesis site|abolished binding to cyclin-a, preventing phosphorylation by cdk2.|76|78","P31749_F49|mutagenesis site|impairs interaction with ptdins(3,4,5)p3 and ptdins(3,4)p2.|86|86","P31749_F5|region of interest|disordered|450|480","P31749_F50|mutagenesis site|significant loss of interaction with tnk2. loss of membrane localization. significant reduction in phosphorylation on ser-473.|176|176","P31749_F51|mutagenesis site|abolished serine/threonine-protein kinase activity.|179|179","P31749_F52|mutagenesis site|abolished binding to cyclin-a, preventing phosphorylation by cdk2.|273|275","P31749_F53|mutagenesis site|reduces o-glcnac levels; reduces o-glcnac levels even more; when associated with a-312.|305|305","P31749_F54|mutagenesis site|abolishes phosphorylation at thr-308.|305|305","P31749_F55|mutagenesis site|5-fold activation and 18-fold activation; when associated with d-473.|308|308","P31749_F56|mutagenesis site|reduces o-glcnac levels; reduces o-glcnac levels even more; when associated with a-305.|312|312","P31749_F57|mutagenesis site|abolishes phosphorylation at thr-308.|312|312","P31749_F58|mutagenesis site|7-fold activation and 25-fold activation; when associated with d-308.|473|473","P31749_F59|mutagenesis site|55% inhibition of activation.|474|474","P31749_F6|active site|proton acceptor|274|274","P31749_F60|sequence conflict|in ref. 7; caa43372.|173|174","P31749_F61|sequence conflict|in ref. 7; caa43372.|202|202","P31749_F62|sequence conflict|in ref. 7; caa43372.|212|212","P31749_F63|sequence conflict|in ref. 7; caa43372.|246|246","P31749_F64|sequence conflict|in ref. 7; caa43372.|409|409","P31749_F65|sequence conflict|in ref. 7; caa43372.|476|476","P31749_F66|sequence conflict|in ref. 7; caa43372.|478|478","P31749_F67|sequence conflict|in ref. 1; aaa36539, 2; aal55732, 3; bag36922 and 4; bag70056/bag70181.|478|478","P31749_F68|helix||2|4","P31749_F69|strand||6|15","P31749_F7|binding site||14|19","P31749_F70|strand||17|19","P31749_F71|strand||22|30","P31749_F72|strand||33|40","P31749_F73|helix||42|44","P31749_F74|helix||45|48","P31749_F75|strand||52|56","P31749_F76|strand||61|65","P31749_F77|strand||67|69","P31749_F78|strand||72|79","P31749_F79|strand||82|89","P31749_F8|binding site||23|25","P31749_F80|helix||93|115","P31749_F81|helix||147|149","P31749_F82|strand||150|158","P31749_F83|strand||160|169","P31749_F84|turn||170|172","P31749_F85|strand||175|182","P31749_F86|helix||183|188","P31749_F87|helix||192|204","P31749_F88|strand||213|218"]}]}