| Interacting proteins: P09429 and P17252 |
Pubmed |
SVM Score :0.0 |
| HMG 1 , extracted and purified from rat brain was phosphorylated in vitro equally well by PKC alpha , beta , gamma and delta . ^^^ |
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| Interacting proteins: P09429 and P17252 |
Pubmed |
SVM Score :0.0 |
| Here we report on the types of posttranslational modifications found in vivo on the HMG 1 and HMG Y proteins isolated from two human breast epithelial cell lines , MCF 7 and MCF 7 / PKC alpha , that represent different stages of neoplastic progression . ^^^ Using MALDI mass spectrometry , we show that the HMG Y protein is more highly modified than the HMG 1 protein in both the MCF 7 and the MCF 7 / PKC alpha cells . ^^^ Significantly , the HMG Y protein isolated from the highly metastatic MCF 7 / PKC alpha cells possesses a unique constellation of phosphorylations , methylations , and acetylations not found on the HMG 1 protein isolated from either the MCF 7 or MCF 7 / PKC alpha cells . ^^^ We further demonstrate that some of the same amino acid residues phosphorylated on recombinant HMGI ( Y ) proteins by purified PKC in vitro are also phosphorylated on the HMG 1 ( Y ) proteins isolated from MCF 7 / PKC alpha cells , suggesting that PKC phosphorylates these proteins in vivo . ^^^ |
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| Interacting proteins: P09429 and P17252 |
Pubmed |
SVM Score :0.0 |
| NA |
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