Ppm1k
entrez
243382
canonical
uniprot
Q8BXN7
canonical
ensembl
ENSMUSG00000037826
resolver
ensp
ENSMUSP00000041395
resolver
enst
ENSMUST00000042766
resolver
genesymbol
Ppm1k
resolver
genesymbol_syn
Pp2cm
resolver
uniprot
B9EHW0
resolver
uniprot_entry
B9EHW0_MOUSE
resolver
uniprot_entry
PPM1K_MOUSE
resolver
amino_acid_sequence
MLSAAFITLLRSGGNQVKKRVLLSSILLQDHRQATPACYFSTSEARCSRFDPDGSGQPATWDNFGIWDNRIDEPILLPPSIKYGKPIPKISLENVGCASLIGKRKENEDRFGFAQLTEEVLYFAVYDGHGGPAAADFCHTHMEKCVMDLLPREKDLETVLTLAFLEIDKAFASYAHLSADASLLTSGTTATVALLRDGVELVVASVGDSRALLCRKGKPMKLTTDHTPERKDEKERIKKFGGFVAWNSLGQPHVNGRLAMTRSIGDLDLKASGVIAEPETTRIKLYHADDSFLVLTTDGINFMVNSQEICDFVNQCHDPKEAAHSVTEQAIQYGTEDNSTAVVVPFGAWGKYKNSEITFSFSRSFASSGRWA
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. Forms a functional kinase and phosphatase pair with BCKDK, serving as a metabolic regulatory node that coordinates branched-chain amino acids (BCAAs) with glucose and lipid metabolism via two distinct phosphoprotein targets: mitochondrial BCKDHA subunit of the branched-chain alpha-ketoacid dehydrogenase (BCKDH) complex and cytosolic ACLY, a lipogenic enzyme of Krebs cycle (By similarity). At high levels of branched-chain ketoacids, dephosphorylates and activates mitochondrial BCKDH complex, a multisubunit complex consisting of three multimeric components each involved in different steps of BCAA catabolism: E1 composed of BCKDHA and BCKDHB, E2 core composed of DBT monomers, and E3 composed of DLD monomers. Tightly associates with the E2 component of BCKDH complex and dephosphorylates BCKDHA on Ser-334 (By similarity). Regulates the reversible phosphorylation of ACLY in response to changes in cellular carbohydrate abundance such as occurs during fasting to feeding metabolic transition. At fasting state, appears to dephosphorylate ACLY on Ser-455 and inactivate it. Refeeding stimulates MLXIPL/ChREBP transcription factor, leading to increased BCKDK to PPM1K expression ratio, phosphorylation and activation of ACLY that ultimately results in the generation of malonyl-CoA and oxaloacetate immediate substrates of de novo lipogenesis and gluconeogenesis, respectively (By similarity). 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) (PubMed:17374715, PubMed:19411760). {ECO:0000250|UniProtKB:Q8N3J5, ECO:0000269|PubMed:17374715, ECO:0000269|PubMed:19411760}.
uniprot
proteins
mass_dalton
40918
uniprot
proteins
pathway_participation
PATHWAY: Protein modification. {ECO:0000250|UniProtKB:Q8N3J5}.
uniprot
proteins
protein_family
PP2C family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17336929
uniprot
proteins
pubmed
17374715
uniprot
proteins
pubmed
19411760
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22589535
uniprot
proteins
sequence_length
372
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8N3J5}. Note=Detected in the cytosolic compartment of liver cells. {ECO:0000250|UniProtKB:A6K136}.
uniprot
proteins