IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ http://www.ebi.ac.uk/ jaggi-2005-2 E-cadherin phosphorylation by protein kinase D1/protein kinase C{mu} is associated with altered cellular aggregation and motility in prostate cancer. human-lncap Human caucasian prostate carcinoma lncap Human caucasian prostate adenocarcinoma anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Jaggi M., Rao PS., Smith DJ., Wheelock MJ., Johnson KR., Hemstreet GP., Balaji KC. Cancer - Interactions investigated in the context of cancer PKD1 and E-cadherin were isolated from cell extracts. Phosphorylation was carried out in the presence of [32P]ATP. [32P]-labeled proteins were identified by autoradiography. A search on the internet revealed the details regarding the synthetic peptide Syntide-2. kcbalaji@unmc.edu Cancer Res. (0008-5472) 2005 Only protein-protein interactions imex curation jaggi-2005-4 E-cadherin phosphorylation by protein kinase D1/protein kinase C{mu} is associated with altered cellular aggregation and motility in prostate cancer. in vitro In vitro protein kinase assay protein kinase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Jaggi M., Rao PS., Smith DJ., Wheelock MJ., Johnson KR., Hemstreet GP., Balaji KC. Cancer - Interactions investigated in the context of cancer PKD1 and E-cadherin were isolated from cell extracts. Phosphorylation was carried out in the presence of [32P]ATP. [32P]-labeled proteins were identified by autoradiography. A search on the internet revealed the details regarding the synthetic peptide Syntide-2. kcbalaji@unmc.edu Cancer Res. (0008-5472) 2005 Only protein-protein interactions imex curation jaggi-2005-1 E-cadherin phosphorylation by protein kinase D1/protein kinase C{mu} is associated with altered cellular aggregation and motility in prostate cancer. human-lncap Human caucasian prostate carcinoma lncap Human caucasian prostate adenocarcinoma confocal microscopy confocal microscopy immunostaining immunostaining Jaggi M., Rao PS., Smith DJ., Wheelock MJ., Johnson KR., Hemstreet GP., Balaji KC. Cancer - Interactions investigated in the context of cancer PKD1 and E-cadherin were isolated from cell extracts. Phosphorylation was carried out in the presence of [32P]ATP. [32P]-labeled proteins were identified by autoradiography. A search on the internet revealed the details regarding the synthetic peptide Syntide-2. kcbalaji@unmc.edu Cancer Res. (0008-5472) 2005 Only protein-protein interactions imex curation jaggi-2005-3 E-cadherin phosphorylation by protein kinase D1/protein kinase C{mu} is associated with altered cellular aggregation and motility in prostate cancer. human-lncap Human caucasian prostate carcinoma lncap Human caucasian prostate adenocarcinoma anti bait coip anti bait coimmunoprecipitation anti bait coip weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Jaggi M., Rao PS., Smith DJ., Wheelock MJ., Johnson KR., Hemstreet GP., Balaji KC. Cancer - Interactions investigated in the context of cancer PKD1 and E-cadherin were isolated from cell extracts. Phosphorylation was carried out in the presence of [32P]ATP. [32P]-labeled proteins were identified by autoradiography. A search on the internet revealed the details regarding the synthetic peptide Syntide-2. kcbalaji@unmc.edu Cancer Res. (0008-5472) 2005 Only protein-protein interactions imex curation jaggi-2005-5 E-cadherin phosphorylation by protein kinase D1/protein kinase C{mu} is associated with altered cellular aggregation and motility in prostate cancer. human-c4_2 Homo sapiens c4-2 androgen-independent prostate cancer cells c4_2 Human androgen-independent prostate cancer cells C4-2 This cell line is also known as C4-2B. confocal microscopy confocal microscopy immunostaining immunostaining Jaggi M., Rao PS., Smith DJ., Wheelock MJ., Johnson KR., Hemstreet GP., Balaji KC. Cancer - Interactions investigated in the context of cancer PKD1 and E-cadherin were isolated from cell extracts. Phosphorylation was carried out in the presence of [32P]ATP. [32P]-labeled proteins were identified by autoradiography. A search on the internet revealed the details regarding the synthetic peptide Syntide-2. kcbalaji@unmc.edu Cancer Res. (0008-5472) 2005 Only protein-protein interactions imex curation jaggi-2005-6 E-cadherin phosphorylation by protein kinase D1/protein kinase C{mu} is associated with altered cellular aggregation and motility in prostate cancer. human-prostate_carcinoma Homo sapiens prostate carcinoma prostate_carcinoma Prostate carcinoma (cancer) confocal microscopy confocal microscopy immunostaining immunostaining Jaggi M., Rao PS., Smith DJ., Wheelock MJ., Johnson KR., Hemstreet GP., Balaji KC. Cancer - Interactions investigated in the context of cancer PKD1 and E-cadherin were isolated from cell extracts. Phosphorylation was carried out in the presence of [32P]ATP. [32P]-labeled proteins were identified by autoradiography. A search on the internet revealed the details regarding the synthetic peptide Syntide-2. kcbalaji@unmc.edu Cancer Res. (0008-5472) 2005 Only protein-protein interactions imex curation cadh1_human Cadherin-1 Epithelial cadherin Uvomorulin CAM 120/80 CDH1 CDHE UVO protein protein human Homo sapiens Human MGPWSRSLSALLLLLQVSSWLCQEPEPCHPGFDAESYTFTVPRRHLERGRVLGRVNFEDCTGRQRTAYFSLDTRFKVGTDGVITVKRPLRFHNPQIHFLVYAWDSTYRKFSTKVTLNTVGHHHRPPPHQASVSGIQAELLTFPNSSPGLRRQKRDWVIPPISCPENEKGPFPKNLVQIKSNKDKEGKVFYSITGQGADTPPVGVFIIERETGWLKVTEPLDRERIATYTLFSHAVSSNGNAVEDPMEILITVTDQNDNKPEFTQEVFKGSVMEGALPGTSVMEVTATDADDDVNTYNAAIAYTILSQDPELPDKNMFTINRNTGVISVVTTGLDRESFPTYTLVVQAADLQGEGLSTTATAVITVTDTNDNPPIFNPTTYKGQVPENEANVVITTLKVTDADAPNTPAWEAVYTILNDDGGQFVVTTNPVNNDGILKTAKGLDFEAKQQYILHVAVTNVVPFEVSLTTSTATVTVDVLDVNEAPIFVPPEKRVEVSEDFGVGQEITSYTAQEPDTFMEQKITYRIWRDTANWLEINPDTGAISTRAELDREDFEHVKNSTYTALIIATDNGSPVATGTGTLLLILSDVNDNAPIPEPRTIFFCERNPKPQVINIIDADLPPNTSPFTAELTHGASANWTIQYNDPTQESIILKPKMALEVGDYKINLKLMDNQNKDQVTTLEVSVCDCEGAAGVCRKAQPVEAGLQIPAILGILGGILALLILILLLLLFLRRRAVVKEPLLPPEDDTRDNVYYYDEEGGGEEDQDFDLSQLHRGLDARPEVTRNDVAPTLMSVPRYLPRPANPDEIGNFIDENLKAADTDPTAPPYDSLLVFDYEGSGSEAASLSSLNSSESDKDQDYDYLNEWGNRFKKLADMYGGGEDD kpcd1_human Serine/threonine-protein kinase D1 nPKC-D1 Protein kinase D Protein kinase C mu type nPKC-mu PRKD1 PKD PKD1 PRKCM protein protein human Homo sapiens Human MSAPPVLRPPSPLLPVAAAAAAAAAALVPGSGPGPAPFLAPVAAPVGGISFHLQIGLSREPVLLLQDSSGDYSLAHVREMACSIVDQKFPECGFYGMYDKILLFRHDPTSENILQLVKAASDIQEGDLIEVVLSASATFEDFQIRPHALFVHSYRAPAFCDHCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRRRRLSNVSLTGVSTIRTSSAELSTSAPDEPLLQKSPSESFIGREKRSNSQSYIGRPIHLDKILMSKVKVPHTFVIHSYTRPTVCQYCKKLLKGLFRQGLQCKDCRFNCHKRCAPKVPNNCLGEVTINGDLLSPGAESDVVMEEGSDDNDSERNSGLMDDMEEAMVQDAEMAMAECQNDSGEMQDPDPDHEDANRTISPSTSNNIPLMRVVQSVKHTKRKSSTVMKEGWMVHYTSKDTLRKRHYWRLDSKCITLFQNDTGSRYYKEIPLSEILSLEPVKTSALIPNGANPHCFEITTANVVYYVGENVVNPSSPSPNNSVLTSGVGADVARMWEIAIQHALMPVIPKGSSVGTGTNLHRDISVSISVSNCQIQENVDISTVYQIFPDEVLGSGQFGIVYGGKHRKTGRDVAIKIIDKLRFPTKQESQLRNEVAILQNLHHPGVVNLECMFETPERVFVVMEKLHGDMLEMILSSEKGRLPEHITKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDIHDQIQNAAFMYPPNPWKEISHEAIDLINNLLQVKMRKRYSVDKTLSHPWLQDYQTWLDLRELECKIGERYITHESDDLRWEKYAGEQGLQYPTHLINPSASHSDTPETEETEMKALGERVSIL syntide_2_peptide Syntide-2 synthetic peptide peptide peptide polypeptide oligopeptide oligopeptide polypeptide chemical synthesis Chemical synthesis (Chemical synthesis) PLARTLSVAGLPGKK An amino acid sequence which is not represented in UniProt The native peptide PLARTLSVAGLPGKK is a selective Substrate for CaM kinase II and PKC. it is also a poor substrate for phosphorylase kinase and is not phosphorylated by myosin light chain kinase. The sequence of PLARTLSVAGLPGKK is homologous to phosphorylation site 2 in glycogen synthase. prkd1-cdh1 PKD1 coimmunoprecipitates E-Cadherin in LNCaP lysates 668931 N/A 668937 unspecified role unspecified role prey prey N/A 668938 unspecified role unspecified role bait bait physical association physical association false false false 2 A cdh1-prkd1-1 PKD1 coimmunoprecipitates with E-Cadherin in LNCaP lysates 668931 N/A 668938 unspecified role unspecified role prey prey N/A 668937 unspecified role unspecified role bait bait physical association physical association false false false 2 A prkd1-cdh1-2 PKD1 phosphorylates E-Cadherin in an in vitro kinase assay 668932 N/A 668938 enzyme enzyme unspecified role unspecified role human-lncap Human caucasian prostate carcinoma lncap Human caucasian prostate adenocarcinoma N/A 668937 enzyme target enzyme target substrate substrate unspecified role unspecified role human-lncap Human caucasian prostate carcinoma lncap Human caucasian prostate adenocarcinoma phosphorylation phosphorylation reaction phosphorylation false false false 2 B, 3 B Go6976 - Phosphorylation of E-Cadherin by PKD1 is inhibited by Go6976. E-cadherin was phosphorylated. prkd1-syntide_2_pept PKD1 phosphorylates Syntide-2 in an in vitro kinase assay 668932 N/A 668938 enzyme enzyme unspecified role unspecified role human-lncap Human caucasian prostate carcinoma lncap Human caucasian prostate adenocarcinoma N/A 668939 enzyme target enzyme target substrate substrate unspecified role unspecified role chemical synthesis Chemical synthesis (Chemical synthesis) phosphorylation phosphorylation reaction phosphorylation false false false 2 B cdh1-prkd1 PKD1 colocalizes with E-Cadherin in LNCaP cells 668933 N/A 668937 unspecified role unspecified role neutral component neutral component N/A 668938 unspecified role unspecified role neutral component neutral component colocalization colocalization false false false 1 This colocalization was seen at cell borders. prkd1-cdh1-1 PKD1 coimmunoprecipitates E-Cadherin in LNCaP lysates 668934 N/A 668937 unspecified role unspecified role prey prey region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false N/A 668938 unspecified role unspecified role bait bait region 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false physical association physical association false false false 2 A cdh1-prkd1-2 PKD1 and E-Cadherin colocalize in C4-2 cells at cell junctions 668935 N/A 668937 unspecified role unspecified role neutral component neutral component N/A 668938 unspecified role unspecified role neutral component neutral component region gfp tag green fluorescent protein tag GFP green fluorescent protein GFP green fluorescent protein gfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false colocalization colocalization false false false 5 A Colocalization takes place at cell junctions. cdh1-prkd1-3 PKD1 and E-Cadherin colocalize in prostate cancer tissue samples at cell junctions 668936 N/A 668938 unspecified role unspecified role neutral component neutral component N/A 668937 unspecified role unspecified role neutral component neutral component colocalization colocalization false false false 5 B Colocalization takes place at cell junctions.