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PTPRK plays dual roles in coordinating angiogenesis. It plays a positive role in cell proliferation, adhesion and tubule formation, but suppresses cell migration, in particular, the FGF-promoted migration.
PTPRK-RSPO3 (show RSPO3 Proteins) fusions and RNF43 (show RNF43 Proteins) mutations were found to be characteristic genetic features of traditional serrated adenomas (TSAs).
By regulating phosphorylation of SRC, RPTPkappa promotes the pathogenic action of rheumatoid arthritis fibroblast-like synoviocytes, mediating cross-activation of growth factor and inflammatory cytokine signalling by TGFbeta in RA FLS.
Notch (show NOTCH1 Proteins) and TGF-beta (show TGFB1 Proteins) act in concert to stimulate induction of PTPRK, which suppresses EGFR (show EGFR Proteins) activation in human keratinocytes.
Findings strongly indicate that the tyrosine phosphorylation of CD133, which is dephosphorylated by PTPRK, regulates AKT (show AKT1 Proteins) signaling and has a critical role in colon cancer progression.
PTPRK underexpression leads to STAT3 (show STAT3 Proteins) activation and contributes to nasal NK/T-cell lymphoma pathogenesis
PTPRK showed lower mRNA expression in duodenal mucose of celiac disease patients.
High expression of PTPRK is associated with prostate cancer.
Tumor derived mutations of protein tyrosine phosphatase receptor type k affect its function and alter sensitivity to chemotherapeutics in glioma.
PTPRK is a negative regulator of adhesion, invasion, migration, and proliferation of breast cancer cells.
RPTP-kappa is proteolytically processed to isoforms that have opposing effects on beta-catenin (show CTNNB1 Proteins) activity.
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP possesses an extracellular region, a single transmembrane region, and two tandem catalytic domains, and thus represents a receptor-type PTP. The extracellular region contains a meprin-A5 antigen-PTP mu (MAM) domain, an Ig-like domain and four fibronectin type III-like repeats. This PTP was shown to mediate homophilic intercellular interaction, possibly through the interaction with beta- and gamma-catenin at adherens junctions. Expression of this gene was found to be stimulated by TGF-beta 1, which may be important for the inhibition of keratinocyte proliferation.
dJ480J14.2.1 (protein tyrosine phosphatase, receptor type, K (R-PTP-KAPPA, protein tyrosine phosphatase kappa , protein tyrosine phosphatase kappa
, protein-tyrosine phosphatase kappa
, protein-tyrosine phosphatase, receptor type, kappa
, receptor-type tyrosine-protein phosphatase kappa
, protein tyrosine phosphatase, receptor type, K, extracellular region
, receptor-like protein tyrosine phosphatase kappa extracellular region (RPTPK)