MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Protein kinase C alpha-mediated phosphorylation of PIM-1L promotes the survival and proliferation of acute myeloid leukemia cells. Protein kinase C alpha-mediated phosphorylation of PIM-1L promotes the survival and proliferation of acute myeloid leukemia cells. Biochemical and biophysical research communications 2018 imex curation Takami M., Katayama K., Noguchi K., Sugimoto Y. katayama-kz@pha.keio.ac.jp 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro protein kinase assay protein kinase assay autoradiography autoradiography Takami M., Katayama K., Noguchi K., Sugimoto Y. katayama-kz@pha.keio.ac.jp Accepted 2018-OCT-10 AT 15:54 BST AT 15:54 BST by LUANA Biochemical and biophysical research communications 2018 Only protein-protein interactions imex curation imex curation Protein kinase C alpha-mediated phosphorylation of PIM-1L promotes the survival and proliferation of acute myeloid leukemia cells. Protein kinase C alpha-mediated phosphorylation of PIM-1L promotes the survival and proliferation of acute myeloid leukemia cells. Biochemical and biophysical research communications 2018 imex curation Takami M., Katayama K., Noguchi K., Sugimoto Y. katayama-kz@pha.keio.ac.jp 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-293 Homo sapiens transformed primary embryonal kidney cells Human 293 Transformed human primary embryonal kidney cells. The Cell type named 293 is synonymous with HEK-293. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Takami M., Katayama K., Noguchi K., Sugimoto Y. katayama-kz@pha.keio.ac.jp Accepted 2018-OCT-10 AT 15:54 BST AT 15:54 BST by LUANA Biochemical and biophysical research communications 2018 Only protein-protein interactions imex curation imex curation p11309-2 Serine/threonine-protein kinase pim-1 Pim-1L PIM1 protein protein human Homo sapiens Human MPHEPHEPLTPPFSALPDPAGAPSRRQSRQRPQLSSDSPSAFRASRSHSRNATRSHSHSHSPRHSLRHSPGSGSCGSSSGHRPCADILEVGMLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSK Initiates from CTG codon. 18C421B7CFF87818 kpca_human Protein kinase C alpha type PRKCA PKCA PRKACA protein protein human Homo sapiens Human MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV 9EB157789A062349 kapca_human cAMP-dependent protein kinase catalytic subunit alpha PRKACA PKACA protein protein human Homo sapiens Human MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVMLVKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF DIP protein P17612 original sequence version: 171 DIP protein P17612 original sequence version: 175 DIP protein P17612 original sequence version: 178 DIP protein P17612-1 original sequence version: 177 DIP protein P17612 original sequence version: 186 DIP protein P17612 original sequence version: 102 DIP protein P17612-1 original sequence version: 102 BF6D3ECD2614E5AB pim1-prkca-1 1 4 enzyme enzyme neutral component neutral component purified purified ecoli Escherichia coli (strain K12) 3 enzyme target enzyme target substrate substrate neutral component neutral component purified purified flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P11309-2:p.Lys158Arg mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain K R Tue Jun 30 19:44:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys158Arg' P11309-2:p.Ser65Ala mutation decreasing rate mutation decreasing interaction rate mutation decreasing rate certain certain sequence position certain certain certain sequence position certain S A Wed Sep 26 12:02:46 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ser65ala' Tue Jun 30 19:10:08 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ser65Ala' phosser65 phosres phosphorylated residue PhosRes Phospho Phosphorylation Phosphorylation (O of Serine, Threonine, Tyrosine and Aspartate, N epsilon of Lysine) certain certain sequence position certain certain certain sequence position certain resulting-ptm resulting-ptm resulting ptm resulting-ptm ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation f1c f1e The kinase-dead PIM-1L-K158R [29] was used to avoid PIM-1L autophosphorylation. No phosphorylation bands were observed when PIM-1L-K158R alone was incubated (Fig. 1C). PIM-1L-K158R phosphorylation bands (44 kDa) were detected when incubated with PKA and PKCα (Fig. 1C). PKCα phosphorylated all of the PIM-1L mutants, but the phosphorylation levels of PIM-1L-K158R•S65A and -K158R•S65A•367A were lower than those of PIM-1L-K158R and -K158R•S367A (Fig. 1E). pim1-prkca-2 1 5 enzyme enzyme neutral component neutral component purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecoli Escherichia coli (strain K12) 3 enzyme target enzyme target substrate substrate neutral component neutral component purified purified flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P11309-2:p.Lys158Arg mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain K R Tue Jun 30 17:46:04 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys158Arg' ecoli Escherichia coli (strain K12) phosphorylation phosphorylation reaction phosphorylation f1c The kinase-dead PIM-1L-K158R [29] was used to avoid PIM-1L autophosphorylation. No phosphorylation bands were observed when PIM-1L-K158R alone was incubated (Fig. 1C). PIM-1L-K158R phosphorylation bands (44 kDa) were detected when incubated with PKA and PKCα (Fig. 1C). pim1-prkca-3 2 4 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed P17252:p.Ala25Glu mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain A E Tue Jun 30 17:03:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ala25Glu' 3 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined P11309-2:p.Lys158Arg mutation with no effect mutation with no effect mutation with no effect mutation not affecting interaction certain certain sequence position certain certain certain sequence position certain K R Wed Sep 26 12:08:05 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys158arg' Tue Jun 30 16:42:17 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys158Arg' physical association physical association f1d Immunoprecipitation–western blotting revealed that transfection of pcDNA3.1-HA-PKCα-WT did not increase the phosphorylated PIM-1L-K158R. In contrast, transfection of pcDNA3.1-HA-PKCα-A25E increased the phosphorylated band of PIM-1L-K158R (Fig. 1D). PKCα phosphorylated all of the PIM-1L mutants, but the phosphorylation levels of PIM-1L-K158R•S65A and -K158R•S65A•367A were lower than those of PIM-1L-K158R and -K158R•S367A (Fig. 1E).