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 Mechanism for activation of the growth factor-activated AGC kinases by turn motif phosphorylation. Mechanism for activation of the growth factor-activated AGC kinases by turn motif phosphorylation. EMBO J. (0261-4189) 2007 imex curation Hauge C., Antal TL., Hirschberg D., Doehn U., Thorup K., Idrissova L., Hansen K., Jensen ON., Jørgensen TJ., Biondi RM., Frödin M. 2009-01-08 Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Hauge C., Antal TL., Hirschberg D., Doehn U., Thorup K., Idrissova L., Hansen K., Jensen ON., Jørgensen TJ., Biondi RM., Frödin M. EMBO J. (0261-4189) 2007 2009-01-08 Only protein-protein interactions imex curation ks6b1_rat Ribosomal protein S6 kinase beta-1 Rps6kb1 Ribosomal protein S6 kinase I 70 kDa ribosomal protein S6 kinase 1 p70 ribosomal S6 kinase alpha protein protein rat Rattus norvegicus (Rat) Rat MRRRRRRDGFYPAPDFRHREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDSTLSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSPVKFSPGDFWGRGASASTANPQTPVEYPMETSGIEQMDVTTSGEASAPLPIRQPNSGPYKKQAFPMISKRPEHLRMNL 013BA13EFB3508D7 pdk1_rat [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial Pdk1 Pdh Pyruvate dehydrogenase kinase isoform 1 PDK p48 protein protein rat Rattus norvegicus (Rat) Rat MRLARLLRGGTSVRPLCAVPCASRSLASDSASGSGPASESGVPGQVDFYARFSPSPLSMKQFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAKTIYEFTDTVIRIRNRHNDVIPTMAQGVTEYKESFGVDPVTSQNVQYFLDRFYMSRISIRMLLNQHSLLFGGKGSPSHRKHIGSINPNCDVVEVIKDGYENARRLCDLYYVNSPELELEELNAKSPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHADKGVYPPIQVHVTLGEEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVETSRAVPLAGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIKALSTESIERLPVYNKAAWKHYRTNHEADDWCVPSREPKDMTTFRSS mint Inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism A8C304507D64ED61 pkn2_rat Serine/threonine-protein kinase N2 Pkn2 Prk2 Prkcl2 Cardiolipin-activated protein kinase Pak2 PKN gamma Pak2 p140 kinase Protein kinase C-like 2 Protein-kinase C-related kinase 2 Protease-activated kinase 2 protein protein rat Rattus norvegicus (Rat) Rat MASNPDRGEILLTELQVDSRPLPFSENVSAVQKLDFSDTIVQQKLDDVKDRIKREIRKELKIKEGAENLRKVTTDKKNLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDYTDCPRTPDTPNSDSRSSTSNNRRLMALQKQLDIELKVKQGAENMIQMYSNGPSKDRKLHGTAQQLLQDNKTKIEVIRMHILQAVLTNELAFDNAKPVISPLELRNGRIIEHHFRIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNELPKNHPKSSVVIEELSLVASPTLSPRQSMLSTQNQYSTLSKPAALTGTLEVRLWGAKISWENVPGRSKATSVALPGWSPSENRSSFMSRTSKSKSGSSRNLLKTDDLSNDVCAVLKLDNTVVGQTIWKPISNQSWDQKFTLELDRSRELEISVYWRDWRSLCAVKFLRLEDFLDNQRHGMALYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPTVNHSGTFSPQTPVPATVPVVDARTPELAPPASDSTVTKLDFDLEPEAPPAPPRASSLGEIDDSSELRVLDIPGQGSETVFDIENDRNNMRPKSKSEYELNIPDSSRSCWSVGELEDKRSQQRFQFNLQDFRCCAVLGRGHFGKVLLAEYKHTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHTDVFSEPRAVFYAACVVLGLQYLHEHKIVYRDLKLDNLLLDTEASVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNPERRLGAGEKDAEDVKKHPFFRLTDWSALLDKKVKPPFVPTIRGREDVSNFDDEFTSEAPILTPPREPRILLEEEQEMFRDFDYVADWC mint Exhibits a preference for highly basic protein substrates AE71D30379715C3D akt1_rat RAC-alpha serine/threonine-protein kinase Akt1 RAC-PK-alpha Protein kinase B Protein kinase B alpha protein protein rat Rattus norvegicus (Rat) Rat MNDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVEQRESPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKRQEEETMDFRSGSPSDNSGAEEMEVALAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA DIP protein P47196 original sequence version: 132 mint homomint General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I (By similarity). Mediates insulin-stimulated protein synthesis, partly by playing a role in both insulin-induced phosphorylation of 4E-BP1 and in insulin-induced activation of p70 S6 kinase. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase 5DCAAE7134366D04 rps6kb1-rps6kb1 1 s6k1 2 peptide synthesis peptide synthesis predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-4790643: original sequence: 366-395 : EPPFKPLLQSEEDVSQFDSKFTRQTPVDS s6k1 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified undefined mutation mutation decreasing interaction mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Wed Jul 06 16:38:51 BST 2016 Sequence change details about this feature cannot be ascertained or do not fit with the current version of the referenced protein, so they have been deleted as a result of our quality control procedures. The original label was 'mutation decreasing' Lys144Asn range MINT-4790638: original sequence: 144-144 : AKDTAHTKAERNILEEVKHP binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-4790635: original sequence: 1-364 : MRRRRRRDGFYPAPDFRHREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLAR phosphorylation phosphorylation reaction phosphorylation F5B F5C F5A EMBO-Journal The kinase activity increases when S371 and T389 amino acids are phosphorylated. homomint mint pdk1-rps6kb1-1 1 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified s6k1 2 peptide synthesis peptide synthesis predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-4790655: original sequence: 366-395 : EPPFKPLLQSEEDVSQFDSKFTRQTPVDS phosphorylation phosphorylation reaction phosphorylation EMBO-Journal SF6C homomint mint akt1-pkn2 1 PKBalpha 5 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-4790686: original sequence: 143-479 : HRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLGPEAKSLLSGLLKKDPTQRLGGGSEDAKEIMQHRFFANIVWQDVYEKKLSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASG Prk2 4 peptide synthesis peptide synthesis predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component purified purified binding site binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain range MINT-4790678: original sequence: 955-982 : APILTPPREPRILLEEEQEMFRDFDYV phosphorylation phosphorylation reaction phosphorylation EMBO-Journal SF6B The kinase activity increases when T958 amino acid is phosphorylated. homomint mint