Gene interactions and pathways from curated databases and text-mining

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PTPRA — SRC

Pathways - manually collected, often from reviews:

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

Text-mined interactions from Literome

Mustelin et al., Science's STKE : signal transduction knowledge environment 2002 : Meeting at mitosis : cell cycle-specific regulation of c-Src by RPTPalpha
Vulin et al., Endocrinology 2005 : We present evidence that inhibition of insulin increased prolactin gene transcription was secondary to RPTPalpha activation of Src , reflecting its role as mediator of integrin responses
Chen et al., J Biol Chem 2006 : Protein-tyrosine phosphatase-alpha ( PTPalpha ) activates Src family kinases (SFKs) to promote the integrin stimulated early autophosphorylation of focal adhesion kinase ( FAK )
Wu et al., Oncogene 2008 (Neuroblastoma) : Catalytically inactive receptor protein-tyrosine phosphatase-alpha overexpression inhibited alpha4beta1 stimulated NB motility and Src activation consistent with alpha4 regulated Src activity occurring through Src Tyr-529 dephosphorylation
Zheng et al., Int J Cancer 2008 (Breast Neoplasms...) : We show that siRNA mediated suppression of protein tyrosine phosphatase alpha ( PTP alpha ) reduces Src activity 2 to 4-fold in breast, colon and other human cancer cell lines
Vacaresse et al., J Biol Chem 2008 : We studied how RPTPalpha affects substrate specificity and regulation of c-Src and Fyn in response to epidermal growth factor and platelet derived growth factor
Vacaru et al., Mol Cell Biol 2010 : Receptor protein tyrosine phosphatase alpha ( RPTPalpha ) is the mitotic activator of the protein tyrosine kinase Src ... Based on our results, we propose a new model for mitotic activation of Src in which PP2A mediated dephosphorylation of RPTPalpha pSer204 facilitates Src binding, leading to RPTPalpha mediated dephosphorylation of Src pTyr527 and pTyr416 and hence modest activation of Src
Wang et al., Acta Biochim Biophys Sin (Shanghai) 2013 (Breast Neoplasms) : Protein tyrosine phosphatase alpha ( PTPa ) functions as an activator of Src by dephosphorylating Tyr527/530, a critical negative regulatory site
den Hertog et al., EMBO J 1993 (Neuroblastoma) : Receptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation ... Endogenous pp60c-src kinase activity is enhanced in the RPTP alpha transfected cells, which may be due to direct dephosphorylation of the regulatory Tyr residue at position 527 in pp60c-src by RPTP alpha