| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Stimulated MBP kinases were identified as ERK 1 and ERK 2 . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| A 40 kDa myelin basic protein kinase , distinct from erk 1 and erk 2 , is activated in mitotic HeLa cells . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Accordingly , PK 41 effectively phosphorylated myelin basic protein , known to be a good substrate for Erk 1 . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| An in gel myelin basic protein kinase assay revealed that NGF activates predominantly Erk 1 . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| The concentrations of ERK 1 and ERK 2 were not altered by stimulating the cells for 16 h with immobilized anti CD 3 mAb or anti CD 3 mAb and phorbol myristate acetate . mAb to CD 3 and phorbol myristate acetate stimulated an increase in ERK 1 and ERK 2 MBP kinase activity . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| The activated MBP kinase was furthermore identified as an extracellular signal regulated kinase ( ERK 1 ) based on several criteria such as substrate specificity , molecular weight , activation dependent mobility shift , and recognition by anti ERK antibodies . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| In KB epidermoid cells , we previously showed that interleukin 1 alpha ( IL 1 ) and various mitogens activate the mitogen activated protein ( MAP ) kinases ERK 1 and ERK 2 , which phosphorylate both myelin basic protein ( MBP ) and a peptide containing Thr 669 of the epidermal growth factor receptor . ^^^ In cell free extracts made from gingival fibroblasts treated with platelet derived growth factor or HepG 2 hepatoma cells stimulated with phorbol myristate acetate , MBP and Thr 669 kinase were both elevated 4 fold , and ERK 1 and ERK 2 were tyrosine phosphorylated . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| The first MBP kinase activity was the only one stimulated by EGF and reacted with anti mitogen activated protein kinase ( MAPK ) antiserum recognising p42mapk and p44mapk isoforms . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Analysis of fractions from Mono Q anion exchange chromatography of lysates of cells exposed to 10 mM Ca2+ or 100 ng / ml EGF revealed a peak of MBP phosphorylation activity that was coeluted with p 42 and p 44 MAPK as shown by immunoblot analysis . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Release of fibroblast cells from early G 1 block was accompanied by a rapid rise in the myelin basic protein ( MBP ) kinase activity of p44mapk and p42mapk , which declined slowly over several hours to reach negligible values as cells enter S phase . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| In gel myelin basic protein ( MBP ) kinase assays revealed significant MBP kinase activity associated with ERK 1 and ERK 2 in total cell lysates and ERK 2 in PY 20 immunoprecipitates . ^^^ Furthermore , PY 20 immunoprecipitates demonstrated minimal MBP kinase associated with ERK 1 in response to EGF treatment . ^^^ EGF , in a concentration and time dependent manner , increases tyrosine phosphorylation and MBP kinase activity ( i . e . activation ) of ERK 2 , and to a lesser degree ERK 1 , suggesting that the activation of MAP kinase may mediate the mitogenic action of EGF in pGCs . . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Zymography of immunoprecipitated ERKs in myelin basic protein ( MBP ) containing polyacrylamide gels demonstrated dose dependent induction of ERK 1 and 2 activity by IGF 1 in GC cells with maximal activity occurring at 6 min . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| By using an ' ingel ' MBP kinase assay the activities of renaturable MBP kinases were detected , including several with molecular masses similar to those of ERK 1 and ERK 2 . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| In situ MBP kinase assays and immunoblotting established that peak 1 coincides with ERK 2 and peak 2 is not an activated form of ERK 1 or ERK 2 . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Several agents that act through G protein coupled receptors and also stimulate phosphoinositide specific phospholipase C ( PI PLC ) , including angiotensin 2 , vasopressin , norepinephrine , and prostaglandin ( PG ) F2alpha , activated the ERK 1 ( p44mapk ) and ERK 2 ( p42mapk ) members of the mitogen activated protein ( MAP ) kinase family in primary cultures of rat hepatocytes , measured as phosphorylation of myelin basic protein ( MBP ) by a partially purified enzyme , immunoblotting , and in gel assays . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Indeed , we show that ATP activates simultaneously MBP kinase activity and phosphotyrosine incorporation in p 42 Erk2 and p 44 Erk1 . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Importantly , the p 36 MBP kinase was immunologically different from MAPK superfamily molecules such as ERK 1 , JNK isoforms , and p 38 MAPK . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| MATERIALS AND METHODS : Using extracts from 23 human breast cancers and control tissue from the same resected specimens , the protein levels , phosphotransferase activities and subcellular locations of the mitogen activated protein ( MAP ) kinase isoforms p 42 Erk2 and p 44 Erk1 were examined , together with their phosphotransferase activities towards myelin basic protein ( MBP ) and a peptide substrate patterned after the Thr 669 site in the epidermal growth factor receptor ( EGFR T 669 ) that is phosphorylated by MAP kinase . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| We have now determined that stimulation of human primary and Jurkat T lymphocytes with ionomycin also results in the activation of ERK 1 and 2 as determined by ; shifts in the mobility of this enzyme on SDS PAGE gels , the binding of an antibody that recognizes only the activated form of this enzyme , and increased ability to phosphorylate myelin basic protein ( MBP ) . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| The major maturation activated MBP kinase ( p 45 Mapk ) was molecularly cloned based on tryptic sequence information obtained with the purified enzyme and shown to be highly related to human Erk 1 with 76 % amino acid identity . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Immunoprecipitation experiments with anti extracellular signal regulated kinase 1 ( ERK 1 ) or anti ERK 2 antibodies followed by MBP kinase assays , and direct in gel kinase assays for MBP , show that p44 / ERK1 but not p42 / ERK2 is stimulated in OA treated spermatocytes . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Both MAPKinase ( ERK 1 ) and phosphotyrosine antibodies immunoprecipitated MBP phosphorylating activity and detected a polypeptide band at M ( r ) approximately 47 kDa . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| The activation of insulin stimulated protein serine / threonine kinases has been investigated in CHO cell lines transfected with cDNAs encoding either wild type or mutant human insulin receptors . ( 1 ) Insulin treatment of CHO cells over expressing wild type insulin receptors resulted in the rapid and substantial ( 5 10 fold ) activation of cytosolic protein kinases which phosphorylated myelin basic protein , Kemptide and two peptide substrates based on sites phosphorylated on ribosomal protein S 6 in vivo . ( 2 ) Further fractionation of cytosolic extracts by MonoQ chromatography revealed two peaks of insulin stimulated myelin basic protein kinase activity which were highly related to the previously described mitogen activated protein ( MAP ) kinases ERK 1 and ERK 2 . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Here , we show that Ser 31 is phosphorylated by ERK 1 and ERK 2 , two myelin basic protein and microtubule associated protein kinases . ^^^ Protein kinase activity toward Ser 31 in TH was present in two peaks corresponding to myelin basic protein kinase activities previously identified as ERK 1 and ERK 2 . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| We extend our previous results and show that two forms of purified MEK activated the myelin basic protein kinase encoded by Erk 1 . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| In this communication we describe assays utilizing the Erk 1 protein fused to glutathione S transferase that permit the identification of protein kinase ( s ) that phosphorylate and activate the myelin basic protein kinase activity encoded by the Erk 1 gene . ^^^ The activation of the Erk 1 encoded myelin basic protein kinase required ATP and correlated directly with the degree of phosphorylation on the same amino acid residues previously shown to be phosphorylated in vivo . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Both ERK 1 and ERK 2 phosphorylated Raf 1 with reasonably high affinity ( Km for ERK 1 = 90 nM ; Km for ERK 2 = 120 nM ) , and produced similar , complex phosphopeptide maps ; both kinases also phosphorylated myelin basic protein . ^^^ The third kinase activity also phosphorylated Raf 1 and myelin basic protein but did not comigrate exactly with either immunoreactive ERK 1 or ERK 2 . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| In this paper , we study the precise timing of MAP kinase activation ( as measured by phosphorylation of exogenous myelin basic protein and shifts in mobility of ERK 1 and ERK 2 ) versus MPF activation ( as measured by phosphorylation of exogenous histone H 1 ) during mouse oocyte maturation and , in parallel , morphological events such as changes in microtubule organization and chromatin condensation . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Before and after cleavage of the GST Erk 1 protein with thrombin , it exhibited a relatively high level of myelin basic protein phosphotransferase activity , which could be reduced eightfold by treatment of the kinase with the protein tyrosine phosphatase CD 45 , but not by treatment with the protein serine / threonine phosphatase 2A . ^^^ A further fivefold stimulation of the myelin basic protein phosphotransferase activity of the GST Erk 1 was achieved in the presence of a partially purified MAP kinase kinase from sheep platelets . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Treatment of mesangial cells with PDGF and angiotensin 2 rapidly and dose dependently stimulated mitogen activated protein ( MAP ) kinase activity , as shown by an assay for activity in vitro using myelin basic protein as a substrate , and by immunoprecipitation of 32P labelled cells with specific antibodies against the 42 kDa and 44 kDa mitogen activated protein kinases p42mapk and p44mapk , respectively . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Using anti pTyr antibodies , we show that ERK 1 is phosphorylated on tyrosine in vivo and that it will phosphorylate myelin basic protein . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Insulin or EGF treatment for 5 min increased p42mapk and p44mapk activity to the same extent as determined by myelin basic protein kinase activity measurements and phosphotyrosine immunoblotting . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Raf 1 phosphorylation of MEK activated it , as judged by its ability to stimulate the phosphorylation of myelin basic protein by glutathione S transferase ERK 1 . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| By immunological criteria , these myelin basic protein kinases included the p42mapk and p44erk1 as well as other potentially novel 44 kDa MAP kinases . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Kinase assays on immunoprecipitates with myelin basic protein as substrate showed that ERK 1 and ERK 2 activation was detectable within 5 min after IL 1 stimulation and decreased to baseline within 60 min . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Myelin basic protein kinase activities corresponding to ERK 1 and ERK 2 immunoreactive proteins were activated twofold above the basal level within 5 min by 1 microM carbachol . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| The increase in tyrosine phosphorylation of these proteins during capacitation was accompanied by increased kinase activity , as determined by the ability of ERK 1 and ERK 2 to phosphorylate the substrate myelin basic protein . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| The ability of these fractions to activate MEK 1 was confirmed by examining the phosphorylation of myelin basic protein , a known substrate for ERKs , in the presence of functional MEK 1 and ERK 1 . ^^^ |
|
| Interacting proteins: P02686 and P27361 |
Pubmed |
SVM Score :0.0 |
| Analysis of the kinetic parameters of the recombinant proteins showed that ERK 2 is approximately 5 times more efficient than ERK 1 in phosphorylating myelin basic protein as a substrate , although the phosphorylating efficiency of the native ERK 1 and ERK 2 appeared to be the same . ^^^ |
|