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 Phosphorylation of hormone-sensitive lipase by protein kinase A in vitro promotes an increase in its hydrophobic surface area. Phosphorylation of hormone-sensitive lipase by protein kinase A in vitro promotes an increase in its hydrophobic surface area. FEBS J. (1742-464X) 2009 Krintel C., Mörgelin M., Logan DT., Holm C. suggested by aryamontri in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Krintel C., Mörgelin M., Logan DT., Holm C. suggested by aryamontri FEBS J. (1742-464X) 2009 lips_rat Hormone-sensitive lipase Lipe Monoacylglycerol lipase LIPE Retinyl ester hydrolase protein protein rat Rattus norvegicus (Rat) Rat MKPRRPISFTREITAMEPSSTSVSRPEWRPEAQQTLTDYPGSRELQEFGIPQKQSLPNEATAQQGAEFQQEQGVQQSTLLQKLLTPLAFPVPQQSFPSHKVHSDQQEATSQNGPGAGKVHTTQKELEHRDEHVGTAESGPAEPPPATEVEATSIAQAVSGPDKKLPTQTDLVSQERAEQSDPTAQQTPLVQGVKSDQGSLIESGILARLQKLAIQQPSQEWKTFLDCVTESDMEKYLNSSSKSNPPEPSGGTVIPGTLPSKQKPDCGKMSGYGGKLPHGKKGILQKHKHYWDTASAFSHSMDLRTMTQSLVALAEDNMAFFSSQGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRASHNLAELEAYLAALTQLRALAYYAQRLLTINRPGVLFFEGDEGLSADFLQDYVTLHKGCFYGRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNITEIEVLSSLANMASTTVRVSRLLSLPPEAFEMPLTSDPKLTVTISPPLAHTGPGPVLARLISYDLREGQDSKMLNSLAKSEGPRLELRPRPQQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIISIDYSLAPEAPFPRALEECFFAYCWAVKHCELLGSTGERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLQSSASPSRLLSLMDPLLPLSVLSKCVSAYSGTETEDHFDSDQKALGVMGLVQRDTSLFLRDLRLGASSWLNSFLELSGRKPHKTPLPATETLRPTDSGRLTESMRRSVSEAALAQPEGLLGTDSLKKLTIKDLSFKGNSEPSDSPEMSQSMETLGPSTPSDVNFFLRSGNSQEEAETRDDISPMDGIPRVRAAFPDGFHPRRSSQGVLHMPLYSSPIVKNPFMSPLLAPDVMLKTLPPVHLVACALDPMLDDSVMFARRLKDLGQPVTLKVVEDLPHGFLSLAALCRETRQAAELCVQRIRLILTPPAAPLT mint In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production 13B10C9315AC87F1 kapca_mouse cAMP-dependent protein kinase catalytic subunit alpha Prkaca Pkaca protein protein mouse Mus musculus Mouse MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLVKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF DIP protein P05132 original sequence version: 185 DIP protein P05132 original sequence version: 186 DIP protein P05132-1 original sequence version: 145 DIP protein P05132-1 original sequence version: 193 DIP protein P05132-1 original sequence version: 199 DIP protein P05132 original sequence version: 163 DIP protein P05132 original sequence version: 192 DIP protein P05132-1 original sequence version: 197 DIP protein P05132-1 original sequence version: 149 02F85D66EB21A1FA lipe-prkaca 1 HSL 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme target enzyme target substrate substrate neutral component neutral component over-expressed over expressed level over-expressed purified purified his tagged 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 PKA 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined enzyme enzyme neutral component neutral component purified purified phosphorylation phosphorylation reaction phosphorylation F4A homomint mint