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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: P53042 (P53042)

Gene Name: Ppp5c

Organism: Rattus norvegicus (Rat)

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 (PubMed:11523989, PubMed:12176367, PubMed:15546861, PubMed:16549782, PubMed:16892053). 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 (By similarity). 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 (By similarity). Inhibits ASK1/MAP3K5-mediated apoptosis induced by oxidative stress (By similarity). 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 (By similarity). Regulates the circadian rhythms, through the dephosphorylation and activation of CSNK1E (By similarity). May modulate TGF-beta signaling pathway by the regulation of SMAD3 phosphorylation and protein expression levels (By similarity). 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 (PubMed:16549782). Dephosphorylate FNIP1, disrupting interaction with HSP90AA1/Hsp90 (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Cytoplasm. Cell membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR004843 Calcineurin-like_PHP_ApaH
IPR029052 Metallo-depent_PP-like
IPR041753 PP5_C
IPR013235 PPP_dom
IPR051134 PPP_phosphatase
IPR006186 Ser/Thr-sp_prot-phosphatase
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_rpt

The S-nitrosylation sites of P53042

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 77 NRSLAYLRTE C YGYALGDATR