PPP5C
entrez
5536
canonical
uniprot
P53041
canonical
ensembl
ENSG00000011485
resolver
ensp
ENSP00000012443
resolver
ensp
ENSP00000556915
resolver
enst
ENST00000012443
resolver
genesymbol
PPP5C
resolver
genesymbol_syn
PPP5
resolver
hgnc
HGNC:9322
resolver
uniprot
Q16722
resolver
uniprot
Q53XV2
resolver
uniprot_entry
PPP5_HUMAN
resolver
uniprot_sec
Q16722
resolver
uniprot_sec
Q53XV2
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. {ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:19601647, ECO:0000269|PubMed:19948726, ECO:0000269|PubMed:22399290, ECO:0000269|PubMed:9000529}.
uniprot
proteins
amino_acid_sequence
MAMAEGERTECAEPPRDEPPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECYGYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQECNKIVKQKAFERAIAGDEHKRSVVDSLDIESMTIEDEYSGPKLEDGKVTISFMKELMQWYKDQKKLHRKCAYQILVQVKEVLSKLSTLVETTLKETEKITVCGDTHGQFYDLLNIFELNGLPSETNPYIFNGDFVDRGSFSVEVILTLFGFKLLYPDHFHLLRGNHETDNMNQIYGFEGEVKAKYTAQMYELFSEVFEWLPLAQCINGKVLIMHGGLFSEDGVTLDDIRKIERNRQPPDSGPMCDLLWSDPQPQNGRSISKRGVSCQFGPDVTKAFLEENNLDYIIRSHEVKAEGYEVAHGGRCVTVFSAPNYCDQMGNKASYIHLQGSDLRPQFHQFTAVPHPNVKPMAYANTLLQLGMM
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: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:30699359, PubMed:9000529). 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:30699359, PubMed:9000529). 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). {ECO:0000250|UniProtKB:P53042, ECO:0000250|UniProtKB:Q60676, ECO:0000269|PubMed:14734805, ECO:0000269|PubMed:14764652, ECO:0000269|PubMed:14871926, ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:15546861, ECO:0000269|PubMed:16260606, ECO:0000269|PubMed:16790549, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:19948726, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:22399290, ECO:0000269|PubMed:22781750, ECO:0000269|PubMed:23102700, ECO:0000269|PubMed:30699359, ECO:0000269|PubMed:9000529}.
uniprot
proteins
mass_dalton
56879
uniprot
proteins
mutagenesis
MUTAGEN 32; /note="K->A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6."; /evidence="ECO:0000269|PubMed:22399290"; MUTAGEN 74; /note="R->A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6."; /evidence="ECO:0000269|PubMed:22399290"; MUTAGEN 83; /note="G->N: No effect on interaction with HSP90AA1."; /evidence="ECO:0000269|PubMed:16531226"; MUTAGEN 93; /note="K->E: Decreases interaction with RAC1 and translocation to the membrane in presence of active RAC1."; /evidence="ECO:0000269|PubMed:19948726"; MUTAGEN 97; /note="K->A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6. Loss of interaction with RAF1."; /evidence="ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:22399290"; MUTAGEN 101; /note="R->A: Loss of interaction with HSP90AA1. No effect on interaction with S100A1, S100A2 and S100A6."; /evidence="ECO:0000269|PubMed:22399290"; MUTAGEN 304; /note="H->Q: Catalytically inactive; no effect on interaction with CRY2 but increases the stability of the interaction with CSNK1E. No effect on RAF1 phosphorylation."; /evidence="ECO:0000269|PubMed:16790549, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:19948726
uniprot
proteins
post_translational_modification
PTM: Activated by at least two different proteolytic cleavages producing a 56 kDa and a 50 kDa form. {ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:23102700}.
uniprot
proteins
protein_family
PP-5 (PP-T) subfamily
uniprot
proteins
protein_family
PPP phosphatase family
uniprot
proteins
pubmed
14734805
uniprot
proteins
pubmed
14764652
uniprot
proteins
pubmed
14871926
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15155720
uniprot
proteins
pubmed
15383005
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15546861
uniprot
proteins
pubmed
15577939
uniprot
proteins
pubmed
16260606
uniprot
proteins
pubmed
16531226
uniprot
proteins
pubmed
16790549
uniprot
proteins
pubmed
16892053
uniprot
proteins
pubmed
19176521
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19601647
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19948726
uniprot
proteins
pubmed
21144835
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22399290
uniprot
proteins
pubmed
22781750
uniprot
proteins
pubmed
23102700
uniprot
proteins
pubmed
27353360
uniprot
proteins
pubmed
29127155
uniprot
proteins
pubmed
30699359
uniprot
proteins
pubmed
7925273
uniprot
proteins
pubmed
8561788
uniprot
proteins
pubmed
8666404
uniprot
proteins
pubmed
9000529
uniprot
proteins
pubmed
9405394
uniprot
proteins
pubmed
9482716
uniprot
proteins
sequence_length
499
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15383005}. Cytoplasm {ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:19948726}. Cell membrane {ECO:0000269|PubMed:19948726}. Note=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). {ECO:0000269|PubMed:15383005, ECO:0000269|PubMed:19948726}.
uniprot
proteins