PPM1A
entrez
5494
canonical
uniprot
P35813
canonical
ensembl
ENSG00000100614
resolver
ensp
ENSP00000314850
resolver
ensp
ENSP00000327255
resolver
ensp
ENSP00000378514
resolver
ensp
ENSP00000563107
resolver
ensp
ENSP00000563111
resolver
ensp
ENSP00000563119
resolver
ensp
ENSP00000563121
resolver
ensp
ENSP00000563126
resolver
ensp
ENSP00000563129
resolver
ensp
ENSP00000563136
resolver
ensp
ENSP00000563137
resolver
ensp
ENSP00000563147
resolver
ensp
ENSP00000563150
resolver
ensp
ENSP00000623973
resolver
ensp
ENSP00000623990
resolver
ensp
ENSP00000624000
resolver
genesymbol
PPM1A
resolver
genesymbol_syn
PPPM1A
resolver
hgnc
HGNC:9275
resolver
uniprot
B2R8E4
resolver
uniprot
B5BU11
resolver
uniprot
J3KNM0
resolver
uniprot
O75551
resolver
uniprot_entry
B2R8E4_HUMAN
resolver
uniprot_entry
PPM1A_HUMAN
resolver
uniprot_sec
B5BU11
resolver
uniprot_sec
J3KNM0
resolver
uniprot_sec
O75551
resolver
amino_acid_sequence
MGAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLESWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVHFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFDYKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELCDFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPNAPKVSPEAVKKEAELDKYLECRVEEIIKKQGEGVPDLVHVMRTLASENIPSLPPGGELASKRNVIEAVYNRLNPYKNDDTDSTSTDDMW
uniprot
proteins
ec_number
3.1.3.16
uniprot
proteins
function
FUNCTION: Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling. Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB. {ECO:0000269|PubMed:16751101, ECO:0000269|PubMed:18930133}.
uniprot
proteins
mass_dalton
42448
uniprot
proteins
mutagenesis
MUTAGEN 239; /note="D->N: No effect on binding SMAD2."; /evidence="ECO:0000269|PubMed:16751101
uniprot
proteins
post_translational_modification
PTM: N-myristoylation is essential for the recognition of its substrates for dephosphorylation. {ECO:0000250}.
uniprot
proteins
protein_family
PP2C family
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
1311954
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16751101
uniprot
proteins
pubmed
18930133
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20213681
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22781750
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25255805
uniprot
proteins
pubmed
30267671
uniprot
proteins
pubmed
9003755
uniprot
proteins
pubmed
9707433
uniprot
proteins
sequence_length
382
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16751101}. Cytoplasm, cytosol {ECO:0000269|PubMed:22781750}. Membrane {ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:25255805}; Lipid-anchor {ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:25255805}. Note=Weakly associates at the membrane and N-myristoylation mediates the membrane localization. {ECO:0000250|UniProtKB:P49443}.
uniprot
proteins