mbinfo MBInfo http://www.mechanobio.info/ The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. Biochem. J. (0264-6021) 1996 imex curation Brindle N.P., Holt M.R., Davies J.E., Price C.J., Critchley D.R. Radiolabelled-Vasp bound to vinculin detected by fluorography. Source of Vasp and Vinculin provided by author. Author contact-emails not mentioned in the paper. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Brindle N.P., Holt M.R., Davies J.E., Price C.J., Critchley D.R. Radiolabelled-Vasp bound to vinculin detected by fluorography. Source of Vasp and Vinculin provided by author. Author contact-emails not mentioned in the paper. Accepted 2012-FEB-15 by ORCHARD Biochem. J. (0264-6021) 1996 Only protein-protein interactions imex curation The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. Biochem. J. (0264-6021) 1996 imex curation Brindle N.P., Holt M.R., Davies J.E., Price C.J., Critchley D.R. Radiolabelled-Vasp bound to vinculin detected by fluorography. Source of Vasp and Vinculin provided by author. Author contact-emails not mentioned in the paper. Only protein-protein interactions in vitro In vitro pull down pull down weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Brindle N.P., Holt M.R., Davies J.E., Price C.J., Critchley D.R. Radiolabelled-Vasp bound to vinculin detected by fluorography. Source of Vasp and Vinculin provided by author. Author contact-emails not mentioned in the paper. Accepted 2012-FEB-15 by ORCHARD Biochem. J. (0264-6021) 1996 Only protein-protein interactions imex curation The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. Biochem. J. (0264-6021) 1996 imex curation Brindle N.P., Holt M.R., Davies J.E., Price C.J., Critchley D.R. Radiolabelled-Vasp bound to vinculin detected by fluorography. Source of Vasp and Vinculin provided by author. Author contact-emails not mentioned in the paper. Only protein-protein interactions in vitro In vitro protein phosphatase assay protein phosphatase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Brindle N.P., Holt M.R., Davies J.E., Price C.J., Critchley D.R. Radiolabelled-Vasp bound to vinculin detected by fluorography. Source of Vasp and Vinculin provided by author. Author contact-emails not mentioned in the paper. Accepted 2012-FEB-15 by ORCHARD Biochem. J. (0264-6021) 1996 Only protein-protein interactions imex curation The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. The focal-adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. Biochem. J. (0264-6021) 1996 imex curation Brindle N.P., Holt M.R., Davies J.E., Price C.J., Critchley D.R. Radiolabelled-Vasp bound to vinculin detected by fluorography. Source of Vasp and Vinculin provided by author. Author contact-emails not mentioned in the paper. Only protein-protein interactions in vitro In vitro pull down pull down weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Brindle N.P., Holt M.R., Davies J.E., Price C.J., Critchley D.R. Radiolabelled-Vasp bound to vinculin detected by fluorography. Source of Vasp and Vinculin provided by author. Author contact-emails not mentioned in the paper. Accepted 2012-FEB-15 by ORCHARD Biochem. J. (0264-6021) 1996 Only protein-protein interactions imex curation kgp1_bovin cGMP-dependent protein kinase 1 PRKG1 PRKG1B PRKGR1A PRKGR1B cGMP-dependent protein kinase I protein protein bovin Bos taurus (Bovine) Bovine MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLHKCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFRKFTKSERSKDLIKEAILDNDFMKNLELSQIQEIVDCMYPVEYGKDSCIIKEGDVGSLVYVMEDGKVEVTKEGVKLCTMGPGKVFGELAILYNCTRTATVKTLVNVKLWAIDRQCFQTIMMRTGLIKHTEYMEFLKSVPTFQSLPEEILSKLADVLEETHYENGEYIIRQGARGDTFFIISKGKVNVTREDSPNEDPVFLRTLGKGDWFGEKALQGEDVRTANVIAAEAVTCLVIDRDSFKHLIGGLDDVSNKAYEDAEAKAKYEAEAAFFANLKLSDFNIIDTLGVGGFGRVELVQLKSEESKTFAMKILKKRHIVDTRQQEHIRSEKQIMQGAHSDFIVRLYRTFKDSKYLYMLMEACLGGELWTILRDRGSFEDSTTRFYTACVVEAFAYLHSKGIIYRDLKPENLILDHRGYAKLVDFGFAKKIGFGKKTWTFCGTPEYVAPEIILNKGHDISADYWSLGILMYELLTGSPPFSGPDPMKTYNIILRGIDMIEFPKKIAKNAANLIKKLCRDNPSERLGNLKNGVKDIQKHKWFEGFNWEGLRKGTLTPPIIPSVASPTDTSNFDSFPEDNDEPPPDDNSGWDIDF 9FE7A48422DA9CDF kapca_pig cAMP-dependent protein kinase catalytic subunit alpha PRKACA protein protein pig Sus scrofa (Pig) Pig MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVMLVKHKETGNHFAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEYSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF B65EC7C42DD56DE5 pp2aa_bovin Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform PPP2CA protein protein bovin Bos taurus (Bovine) Bovine MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL C602291F78F34555 vasp_human Vasodilator-stimulated phosphoprotein VASP protein protein human Homo sapiens Human MSETVICSSRATVMLYDDGNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQVVINCAIVRGVKYNQATPNFHQWRDARQVWGLNFGSKEDAAQFAAGMASALEALEGGGPPPPPALPTWSVPNGPSPEEVEQQKRQQPGPSEHIERRVSNAGGPPAPPAGGPPPPPGPPPPPGPPPPPGLPPSGVPAAAHGAGGGPPPAPPLPAAQGPGGGGAGAPGLAAAIAGAKLRKVSKQEEASGGPTAPKAESGRSGGGGLMEEMNAMLARRRKATQVGEKTPKDESANQEEPEARVPAQSESVRRPWEKNSTTLPRMKSSSSVTTSETQPCTPSSSDYSDLQRVKQELLEEVKKELQKVKEEIIEAFVQELRKRGSP DIP protein P50552 original sequence version: 88 17634B8134DEBF59 vinc_chick Vinculin VCL VINC1 Metavinculin protein protein chick Gallus gallus (Chicken) Chicken MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVSAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVRAAQMLQADPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNTKSQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALALIDSKMNQAKGWLRDPNAPPGDAGEQAIRQILDEAGKAGELCAGKERREILGTCKTLGQMTDQLADLRARGQGATPMAMQKAQQVSQGLDLLTAKVENAARKLEAMTNSKQAIAKKIDAAQNWLADPNGGSEGEEHIRGIMSEARKVAELCEEPKERDDILRSLGEISALTAKLSDLRRHGKGDSPEARALAKQIATSLQNLQSKTNRAVANTRPVKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGRRLANVMMGPYRQDLLAKCDRVDQLAAQLADLAARGEGESPQARAIAAQLQDSLKDLKARMQEAMTQEVSDVFSDTTTPIKLLAVAATAPSDTPNREEVFEERAANFENHAARLGATAEKAAAVGTANKTTVEGIQATVKSARELTPQVVSAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANMQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEHLHLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEAINQPMMMAARQLHDEARKWSSKPVTVINEAAEAGVDIDEEDDADVEFSLPSDIEDDYEPELLLMPTNQPVNQPILAAAQSLHREATKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGNKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ DIP protein P12003 original sequence version: 104 DIP protein P12003-2 original sequence version: 135 DIP protein P12003 original sequence version: 146 28CC2699C9511058 vasp-vcl-1 2 9 unspecified role unspecified role bait bait proline-rich motif sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain n-terminus gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role prey prey region 3h radiolabel 3h radiolabel 3H tritium H3 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined rabit-reticulocyte Oryctolagus cuniculus reticulocyte reticulocyte Reticulocytes physical association physical association Fig. 2. vcl-vasp-2 4 8 unspecified role unspecified role prey prey region 3h radiolabel 3h radiolabel 3H tritium H3 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Fig. 3, 4b and 5. c-terminal region required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain Fig. 5. rabit-reticulocyte Oryctolagus cuniculus reticulocyte reticulocyte Reticulocytes 9 unspecified role unspecified role bait bait proline-rich motif sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 19 21 physical association physical association Fig. 3, 4b and 5. prkg1-vasp-1 1 5 enzyme enzyme neutral component neutral component in vitro In vitro 8 enzyme target enzyme target substrate substrate neutral component neutral component region 3h radiolabel 3h radiolabel 3H tritium H3 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined rabit-reticulocyte Oryctolagus cuniculus reticulocyte reticulocyte Reticulocytes phosphorylation phosphorylation reaction phosphorylation Fig. 4A prkaca-vasp-2 1 6 enzyme enzyme neutral component neutral component in vitro In vitro 8 enzyme target enzyme target substrate substrate neutral component neutral component region 3h radiolabel 3h radiolabel 3H tritium H3 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined rabit-reticulocyte Oryctolagus cuniculus reticulocyte reticulocyte Reticulocytes phosphorylation phosphorylation reaction phosphorylation Porcine cAMP-dependent protein kinase has two catalytic subunits- alpha and beta. This entry involves catalytic subunit alpha. Fig. 4a ppp2ca-vasp-4 3 7 enzyme enzyme neutral component neutral component in vitro In vitro 8 enzyme target enzyme target substrate substrate neutral component neutral component region 3h radiolabel 3h radiolabel 3H tritium H3 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined rabit-reticulocyte Oryctolagus cuniculus reticulocyte reticulocyte Reticulocytes dephosphorylation dephosphorylation reaction dephosphorylation Fig. 4b. Bovine protein phosphatase 2A has two catalytic subunits-alpha and beta. The subunit included in this entry is catalytic subunit alpha.