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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Serine/threonine-protein phosphatase 5

UniprotKB/SwissProt ID: PPP5_MOUSE (Q60676)

Gene Name: Ppp5c

Organism: Mus musculus (Mouse).

Function: 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. 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. 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. Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress. Plays a positive role in adipogenesis, mainly through the dephosphorylation and activation of PPARG transactivation function. Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1. Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E. May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels. Dephosphorylates and may play a role in the regulation of TAU/MAPT. Through their dephosphorylation, may play a role in the regulation of ions channels such as KCNH2.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Cytoplasm. Membrane (By similarity). Note=Predominantly nuclear. But also present in the cytoplasm.

Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR001440
IPR004843
IPR006186
IPR011236
IPR011990
IPR013026
IPR013235

The S-nitrosylation sites of PPP5_MOUSE

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
177NRSLAYLRTE C YGYALGDATR HHHHHHHHCC C HHHHHHHHHH 2.93%MC0822178444-
277NRSLAYLRTE C YGYALGDATR HHHHHHHHCC C HHHHHHHHHH 2.93%MC0819101475-
377NRSLAYLRTE C YGYALGDATR HHHHHHHHCC C HHHHHHHHHH 2.93%MC0821278135in vitro
477NRSLAYLRTE C YGYALGDATR HHHHHHHHCC C HHHHHHHHHH 2.93%MC0822865876in vivo
5404GRSVSKRGVS C QFGPDVTKAF CCCCCCCCEE E ECCHHHHHHH 3.45%MC0821278135in vitro