Ppm1k
entrez
312381
canonical
uniprot
A6K136
canonical
ensembl
ENSRNOG00000006893
resolver
ensembl
ENSRNOG00055011498
resolver
ensembl
ENSRNOG00060022630
resolver
ensembl
ENSRNOG00065011574
resolver
ensp
ENSRNOP00000009202
resolver
ensp
ENSRNOP00055015759
resolver
ensp
ENSRNOP00060032450
resolver
ensp
ENSRNOP00065014385
resolver
enst
ENSRNOT00000009202
resolver
enst
ENSRNOT00055019538
resolver
enst
ENSRNOT00060039241
resolver
enst
ENSRNOT00065018813
resolver
genesymbol
Ppm1k
resolver
uniprot
D4A7X5
resolver
uniprot_entry
PPM1K_RAT
resolver
uniprot_sec
D4A7X5
resolver
amino_acid_sequence
MLSTAFITLVRSGRNQVKKRVLLSSILLQDHRQMTPACYCSISEPRCSRFDPDGSGQPATWDNFGIWDNRIDEPILLPPSIKYGKPIPKISLENVGCASLIGKRKENEDRFGFAQLTEEVLYFAVYDGHGGPAAADFCHTHMEKCVTDLLPREKDLETVLTLAFLEIDKAFSSYAHLSADASLLTSGTTATVALLRDGVELVVASVGDSRALLCRKGKPMKLTTDHTPERKDEKERIKKCGGFVAWNSLGQPHVNGRLAMTRSIGDLDLKASGVIAEPETTRIKLYHADDSFLVLTTDGINFMVNSQEICDFVNQCHDPKEAAHAVTEQAIQYGTEDNSTAVVVPFGAWGKYKNSEITFSFSRSFASSGRWA
uniprot
proteins
ec_number
3.1.3.16
uniprot
proteins
ec_number
3.1.3.52
uniprot
proteins
function
FUNCTION: Serine/threonine-protein phosphatase component of macronutrients metabolism. Together with BCKDK serves as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) and protein synthesis with glucose and lipid metabolism via two distinct phosphoprotein targets: BCKDHA/E1a subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and ACLY, a lipogenic enzyme of Krebs cycle (By similarity) (PubMed:29779826). At high levels of branched-chain ketoacids (BCKAs), dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three components, heterotetrameric E1 composed of BCKDHA and BCKDHB chains, 24-meric E2 core composed of DBT and homodimeric E3 composed of DLD, each involved in different steps of BCAA catabolism. Tightly associates with the E2 subunit of BCKDH complex and dephosphorylates Ser-333 of BCKDHA chain of the E1 subunit likely through on-off binding to individual E2 subunits of the 24-meric E2 core to increase the efficiency of the dephosphorylation reaction (By similarity). Appears to dephosphorylate and inactivate cytosolic ACLY in response to changes of cellular carbohydrate abundance. Overnutrition and in particular high-fructose diet, activates MLXIPL/ChREBP leading to increased BCKDK to PPM1K ratio, phosphorylation of ACLY on Ser-454 and activation of its enzymatic activity that ultimately results in the generation of acetyl-CoA and malonyl-CoA immediate substrates of de novo lipogenesis (By similarity) (PubMed:29779826). Recognizes phosphosites having SxS or RxxS motifs and strictly depends on Mn(2+) ions for the phosphatase activity (By similarity). Regulates Ca(2+)-induced opening of mitochondrial transition pore and apoptotic cell death (By similarity). {ECO:0000250|UniProtKB:Q8N3J5, ECO:0000269|PubMed:29779826}.
uniprot
proteins
mass_dalton
41014
uniprot
proteins
pathway_participation
PATHWAY: Protein modification. {ECO:0000269|PubMed:29779826}.
uniprot
proteins
protein_family
PP2C family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
29779826
uniprot
proteins
sequence_length
372
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8N3J5, ECO:0000305|PubMed:29779826}. Note=Detected in the cytosolic compartment of liver cells. {ECO:0000269|PubMed:29779826}.
uniprot
proteins