DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu The first armadillo repeat is involved in the recognition and regulation of beta-catenin phosphorylation by protein kinase CK1. The first armadillo repeat is involved in the recognition and regulation of beta-catenin phosphorylation by protein kinase CK1. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Bustos VH., Ferrarese A., Venerando A., Marin O., Allende JE., Pinna LA. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Bustos VH., Ferrarese A., Venerando A., Marin O., Allende JE., Pinna LA. DIP original experiment: DIP-264288X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx The first armadillo repeat is involved in the recognition and regulation of beta-catenin phosphorylation by protein kinase CK1. The first armadillo repeat is involved in the recognition and regulation of beta-catenin phosphorylation by protein kinase CK1. The first armadillo repeat is involved in the recognition and regulation of beta-catenin phosphorylation by protein kinase CK1. Proceedings of the National Academy of Sciences of the United States of America 2006 imex curation Bustos VH., Ferrarese A., Venerando A., Marin O., Allende JE., Pinna LA. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Bustos VH., Ferrarese A., Venerando A., Marin O., Allende JE., Pinna LA. DIP original experiment: DIP-264287X Proceedings of the National Academy of Sciences of the United States of America 2006 IMEx The first armadillo repeat is involved in the recognition and regulation of beta-catenin phosphorylation by protein kinase CK1. ctnb1_rat Catenin beta-1 Ctnnb1 Catnb Beta-catenin protein protein rat Rattus norvegicus (Rat) Rat MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEEEDVDTSQVLYEWEQGFSQSFTQEQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDAAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYTYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGPHLTDPSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSMGGTQQQFVEGVRMEEIVEGCTGALHILARDVHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCELAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMAWNETADLGLDIGAQGEALGYRQDDPSYRSFHSGGYGQDALGMDPMMEHEMGGHHPGADYPVDGLPDLGHAQDLMDGLPPGDSNQLAWFDTDL DIP protein Q9WU82 original sequence version: 140 DIP protein Q9WU82 original sequence version: 93 DIP protein Q9WU82 original sequence version: 115 9C29186B6DD54B87 ctnb1_xenla Catenin beta-1 ctnnb1 Beta-catenin protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MATQADLMELDMAMEPDRKAAVSHWQQQSYLDSGIHSGATTTAPSLSGKGNPEDEDVDTNQVLYEWEQGFSQSFTQDQVADIDGQYAMTRAQRVRAAMFPETLDEGMQIPSTQFDSAHPTNVQRLAEPSQMLKHAVVNLINYQDDAELATRAIPELTKLLNDEDQVVVNKAAVMVHQLSKKEASRHAIMRSPQMVSAIVRTMQNTNDVETARCTAGTLHNLSHHREGLLAIFKSGGIPALVKMLGSPVDSVLFYAITTLHNLLLHQEGAKMAVRLAGGLQKMVALLNKTNVKFLAITTDCLQILAYGNQESKLIILASGGPQALVNIMRTYSYEKLLWTTSRVLKVLSVCSSNKPAIVEAGGMQALGLHLTDSSQRLVQNCLWTLRNLSDAATKQEGMEGLLGTLVQLLGSDDINVVTCAAGILSNLTCNNYKNKMMVCQVGGIEALVRTVLRAGDREDITEPAICALRHLTSRHQEAEMAQNAVRLHYGLPVVVKLLHPPSHWPLIKATVGLIRNLALCPANHAPLREQGAIPRLVQLLVRAHQDTQRRTSIGGTQQQFVEGVRMEEIVEGCTGALHILARDIHNRIVIRGLNTIPLFVQLLYSPIENIQRVAAGVLCDVAQDKEAAEAIEAEGATAPLTELLHSRNEGVATYAAAVLFRMSEDKPQDYKKRLSVELTSSLFRTEPMPWNEAADLGLDIGAQGEPLGYRQDDSSYRSFHAAGYGQDAMGMDSMMDHDMGGHHPGADYPVDGLPDLSHAQDLMDGLPPGDSNQLAWFDTDL DIP protein P26233 original sequence version: 86 DIP protein P26233 original sequence version: 53 DIP protein P26233 original sequence version: 70 mint Binds to the cytoplasmic domain of the cell-cell adhesion molecule E-cadherin, and perhaps to other (membrane) proteins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Essential component of the vertebrate Wnt-signaling pathway and is required for formation of the embryonic axis 3ECD27232239F799 q8jgt0_danre csnk1a1 protein protein danre Danio rerio (Zebrafish) Brachydanio rerio Zebrafish MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSGGQGQQAQTPTGF DIP protein Q8JGT0 original sequence version: 107 csnk1a1-ctnnb1-1 2 4 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 36-64 Region 36-64 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain in vitro In vitro 5 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation csnk1a1-ctnnb1-2 1 5 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli 3 enzyme target enzyme target substrate substrate unspecified role unspecified role pS45 pS45 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 western blot western blot Immuno blot Immuno blot certain certain sequence position certain certain certain sequence position certain Region 1-131 Region 1-131 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation