| First Author | Tsuchiya K | Year | 2003 |
| Journal | FEBS Lett | Volume | 537 |
| Issue | 1-3 | Pages | 203-9 |
| PubMed ID | 12606058 | Mgi Jnum | J:82341 |
| Mgi Id | MGI:2652310 | Doi | 10.1016/s0014-5793(03)00127-3 |
| Citation | Tsuchiya K, et al. (2003) Molecular cloning and characterization of TPP36 and its isoform TPP32, novel substrates of Abl tyrosine kinase. FEBS Lett 537(1-3):203-9 |
| abstractText | 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. |
