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XB-ART-5699
FEBS Lett 2003 Feb 27;5371-3:203-9. doi: 10.1016/s0014-5793(03)00127-3.
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Molecular cloning and characterization of TPP36 and its isoform TPP32, novel substrates of Abl tyrosine kinase.

Tsuchiya K , Kawano Y , Kojima T , Nagata K , Takao T , Okada M , Shinohara H , Maki K , Toyama-Sorimachi N , Miyasaka N , Watanabe M , Karasuyama H .


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We have molecularly cloned TPP36, a novel 36 kDa protein with 281 amino acids that was identified as a protein phosphorylated in B progenitor cells following stimulation with pervanadate/H(2)O(2). Analysis with anti-TPP36 antiserum revealed that TPP36 was expressed ubiquitously and had an isoform with 236 amino acids, designated TPP32. TPP36/32 were localized mainly in cytoplasm despite the presence of a typical nuclear localization signal sequence. These proteins were phosphorylated preferentially by Abl among a panel of tyrosine kinases examined. Phosphorylation of tyrosine 120 in TPP36/32 led to an apparent mobility shift in sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting conformational change in the phosphorylated protein. Thus, TPP36/32 appear to be novel substrates of Abl tyrosine kinase.

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Species referenced: Xenopus
Genes referenced: abl1