PPP5C

This gene encodes a serine/threonine phosphatase which is a member of the protein phosphatase catalytic subunit family. Proteins in this family participate in pathways regulated by reversible phosphorylation at serine and threonine residues; many of these pathways are involved in the regulation of cell growth and differentiation. The product of this gene has been shown to participate in signaling pathways in response to hormones or cellular stress, and elevated levels of this protein may be associated with breast cancer development. Alternative splicing results in multiple transcript variants.

PPP5C

Serine/threonine-protein phosphatase that dephosphorylates a myriad of proteins involved in different signaling pathways including the kinases CSNK1E, ASK1/MAP3K5, PRKDC and RAF1, the nuclear receptors NR3C1, PPARG, ESR1 and ESR2, SMAD proteins and TAU/MAPT (PubMed:14734805, PubMed:14764652, PubMed:14871926, PubMed:15383005, PubMed:15546861, PubMed:16260606, PubMed:16790549, PubMed:16892053, PubMed:19176521, PubMed:19948726, PubMed:21144835, PubMed:22399290, PubMed:22781750, PubMed:23102700, PubMed:9000529, PubMed:30699359).
Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses (PubMed:14734805, PubMed:14764652, PubMed:14871926, PubMed:15383005, PubMed:15546861, PubMed:16260606, PubMed:16790549, PubMed:16892053, PubMed:19176521, PubMed:19948726, PubMed:21144835, PubMed:22399290, PubMed:22781750, PubMed:23102700, PubMed:9000529, PubMed:30699359).
Participates in the control of DNA damage response mechanisms such as checkpoint activation and DNA damage repair through, for instance, the regulation ATM/ATR-signaling and dephosphorylation of PRKDC and TP53BP1 (PubMed:14871926, PubMed:16260606, PubMed:21144835).
Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress (PubMed:23102700).
Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function (By similarity).
Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1 (By similarity).
Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E (PubMed:16790549).
May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels (PubMed:22781750).
Dephosphorylates and may play a role in the regulation of TAU/MAPT (PubMed:15546861).
Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2 (By similarity).
Dephosphorylate FNIP1, disrupting interaction with HSP90AA1/Hsp90 (PubMed:30699359).

Double-strand break repairTAS:Reactome
MAPK cascadeTAS:Reactome
Mitotic cell cycleManual Assertion Based On ExperimentTAS:ProtInc
Peptidyl-serine dephosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Peptidyl-threonine dephosphorylationManual Assertion Based On ExperimentTAS:ARUK-UCL
Positive regulation of I-kappaB kinase/NF-kappaB signalingManual Assertion Based On ExperimentHMP:UniProtKB
Protein dephosphorylationManual Assertion Based On ExperimentTAS:ProtInc
Response to arachidonic acidBy SimilarityISS:ARUK-UCL
Response to lead ionISS:ARUK-UCL
Response to morphineIEA:Ensembl
Transcription, DNA-templatedManual Assertion Based On ExperimentTAS:ProtInc

Nucleus
Cytoplasm
Cell membrane
Predominantly nuclear (PubMed:15383005).
But also present in the cytoplasm (PubMed:15383005).
Translocates from the cytoplasm to the plasma membrane in a RAC1-dependent manner (PubMed:19948726).

Activated by at least two different proteolytic cleavages producing a 56 kDa and a 50 kDa form.