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C-terminal cytoplasmic fragment of PcdhgC5 (show PCDHGC5 Proteins) acts as a scaffold for CaMKP and CaMKI (show CAMK1 Proteins) to regulate CaMKP activity.
The POPX2 phosphatase regulates cancer cell motility and invasiveness.
The binding of POPX2 (PPM1F) to mDia1 or to an mDia-containing complex greatly decreases the ability of mDia1 to activate transcription from the serum response element (SRE).
PPM1F overexpression suppressed cell proliferation and invasion and counteracted the tumour-promoting role of miR (show MLXIP Proteins)-590, but PPM1F knockdown reversed these effects.
POPX2 is a negative regulator of TAK1 (show MAP3K7 Proteins) signaling pathway and modulates apoptosis through the regulation of TAK1 (show MAP3K7 Proteins) activity.
PPM1F could work downstream of alpha9-nAchR (show CHRNA4 Proteins) to promote nicotine-induced carcinogenic signals. Thus, PPM1F expression could be used for prognostic diagnosis, or inhibited as a potential strategy for cancer prevention and therapy.
This study, combined with our previous findings, suggests that a single ubiquitously expressed phosphatase POPX2 influences cancer metastasis via modulating multiple biological processes including MAPK (show MAPK1 Proteins) signaling and exosome cytokine secretion.
Overexpression of PPM1F is associated with metastasis of hepatocellular carcinoma.
POPX2 affects trafficking by determining the phosphorylation status of KIF3A (show KIF3A Proteins) at serine 690.
POPX2 might regulate cell motility through its regulation of the MAPK1 (show MAPK3 Proteins)/3, leading to changes in the cytoskeleton and cell motility.
hCaMKP activity is reversibly regulated by oxidation/reduction at Cys (show DNAJC5 Proteins)-359
FHOD1 (show FHOD1 Proteins) and PPM1F (direct regulators of the actin cytoskeleton) were identified as novel targets of miR (show MLXIP Proteins)-200c. Expression levels of FHOD1 (show FHOD1 Proteins) and PPM1F were inversely correlated with miR (show MLXIP Proteins)-200c level in breast cancer cell lines and breast cancer patient samples.
Data identify a biochemical pathway through which POPX2 exerts its apparent cellular function: the regulation of activity of glycogen synthase kinase-3, which in turn modulates extracellular signal-regulated kinase and cell motility.
The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase can interact with Rho guanine nucleotide exchange factors (PIX), and thus block the effects of p21-activated kinase 1 (PAK), a protein kinase mediating biological effects downstream of Rho GTPases. Calcium/calmodulin-dependent protein kinase II gamma (CAMK2G/CAMK-II) is found to be one of the substrates of this phosphatase. The overexpression of this phosphatase or CAMK2G has been shown to mediate caspase-dependent apoptosis. An alternatively spliced transcript variant has been identified, but its full-length nature has not been determined.
ca(2+)/calmodulin-dependent protein kinase phosphatase
, caM-kinase phosphatase
, calcium/calmodulin-dependent protein kinase phosphatase
, partner of PIX2
, protein phosphatase 1F
, Ca(2+)/calmodulin-dependent protein kinase phosphatase
, CaM-kinase phosphatase
, PP2C phosphatase
, partner of PIX 2
, protein fem-2 homolog
, protein phosphatase 1F (PP2C domain containing)