Ppp5c
entrez
19060
canonical
uniprot
Q60676
canonical
ensembl
ENSMUSG00000003099
resolver
ensp
ENSMUSP00000003183
resolver
ensp
ENSMUSP00000122783
resolver
enst
ENSMUST00000003183
resolver
genesymbol
Ppp5c
resolver
uniprot
G5E819
resolver
uniprot
O35299
resolver
uniprot_entry
PPP5_MOUSE
resolver
uniprot_sec
G5E819
resolver
uniprot_sec
O35299
resolver
activity_regulation
ACTIVITY REGULATION: Autoinhibited. In the autoinhibited state, the TPR domain interacts with the catalytic region and prevents substrate access to the catalytic pocket. Allosterically activated by various polyunsaturated fatty acids, free long-chain fatty-acids and long-chain fatty acyl-CoA esters, arachidonic acid being the most effective activator. HSP90A and probably RAC1, GNA12 and GNA13 can also release the autoinhibition by the TPR repeat. Activation by RAC1, GNA12 and GNA13 is synergistic with the one produced by fatty acids binding. Inhibited by okadaic acid.
uniprot
proteins
amino_acid_sequence
MAMAEGERTECAETPRDEPPADGTLKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPGNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPNDKDAKMKYQECSKIVKQKAFERAIAGDEHRRSVVDSLDIESMTIEDEYSGPKLEDGKVTITFMKDLMQWYKDQKKLHRKCAYQILVQVKEVLCKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSVSKRGVSCQFGPDVTKAFLEENQLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLLQLGMM
uniprot
proteins
ec_number
3.1.3.16
uniprot
proteins
function
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:17376776, PubMed:21994940, PubMed:22526606). 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 (PubMed:17376776). 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 (PubMed:21994940). Also dephosphorylates and inhibits the anti-adipogenic effect of NR3C1 (PubMed:21994940). 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 (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:P53041, ECO:0000250|UniProtKB:P53042, ECO:0000269|PubMed:17376776, ECO:0000269|PubMed:21994940, ECO:0000269|PubMed:22526606}.
uniprot
proteins
mass_dalton
56877
uniprot
proteins
post_translational_modification
PTM: Activated by at least two different proteolytic cleavages producing a 56 kDa and a 50 kDa form. {ECO:0000250}.
uniprot
proteins
protein_family
PP-5 (PP-T) subfamily
uniprot
proteins
protein_family
PPP phosphatase family
uniprot
proteins
pubmed
12522145
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16790549
uniprot
proteins
pubmed
17376776
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21994940
uniprot
proteins
pubmed
22526606
uniprot
proteins
pubmed
7972012
uniprot
proteins
pubmed
9195923
uniprot
proteins
sequence_length
499
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21994940}. Cytoplasm {ECO:0000269|PubMed:21994940}. Cell membrane {ECO:0000250|UniProtKB:P53041}. Note=Predominantly nuclear. But also present in the cytoplasm. Translocates from the cytoplasm to the plasma membrane in a RAC1-dependent manner. {ECO:0000250|UniProtKB:P53041}.
uniprot
proteins