LipidDB ID

LipidDB-10090-00318

Entry Name

UniProt Accession

P49443;

Theoretical PI

5.19

Molecular Weight

42432.71

Genbank Protein ID

BAA05662.1; AAH08595.1;

Genbank Nucleotide ID

D28117; BC008595;

Protein Name

Protein phosphatase 1A

Protein Synonyms/Alias

3.1.3.16; Protein phosphatase 2C isoform alpha; PP2C-alpha; Protein phosphatase IA;

Gene Name

Ppm1a

Gene Synonyms/Alias

Pppm1a;

Created Date

01-FEB-1996

Organism

Mus musculus (Mouse)

NCBI Taxa ID

10090

Reference

[1] Chida T, Ando M, Matsuki T, Masu Y, Nagaura Y, Takano-Yamamoto T, Tamura S,Kobayashi T. N-Myristoylation is essential for protein phosphatases PPM1A andPPM1B to dephosphorylate their physiological substrates in cells. Biochem J. 2013Feb 1;449(3):741-9. doi: 10.1042/BJ20121201.[PMID:23088624]

Functional Description

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 (By similarity). Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB.

Sequence Annotation

Metal binding site: 60 60 Manganese 1.
Metal binding site: 60 60 Manganese 2.
Metal binding site: 61 61 Manganese 1; via carbonyl oxygen.
Metal binding site: 239 239 Manganese 2.
Metal binding site: 282 282 Manganese 2.
Modified residue: 375 375 Phosphoserine.

Protein Length

382 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005829; C:cytosol; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProtKB
GO:0043005; C:neuron projection; IEA:Ensembl
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005891; C:voltage-gated calcium channel complex; IEA:Ensembl
GO:0033192; F:calmodulin-dependent protein phosphatase activity; IEA:Ensembl
GO:0000287; F:magnesium ion binding; IEA:InterPro
GO:0030145; F:manganese ion binding; IEA:InterPro
GO:0004721; F:phosphoprotein phosphatase activity; IDA:MGI
GO:0070412; F:R-SMAD binding; ISS:UniProtKB
GO:0004871; F:signal transducer activity; IEA:Ensembl
GO:0006499; P:N-terminal protein myristoylation; IDA:UniProtKB
GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB
GO:0042347; P:negative regulation of NF-kappaB import into nucleus; ISS:UniProtKB
GO:0010991; P:negative regulation of SMAD protein complex assembly; IEA:Ensembl
GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl
GO:0035970; P:peptidyl-threonine dephosphorylation; IEA:Ensembl
GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl
GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl
GO:0030177; P:positive regulation of Wnt signaling pathway; IEA:Ensembl
GO:0006470; P:protein dephosphorylation; IMP:UniProtKB
GO:0016055; P:Wnt signaling pathway; IEA:Ensembl

Interpro

InterPro; IPR001932; PP2C-like_dom
InterPro; IPR012911; PP2C_C
InterPro; IPR000222; PP2C_Mn2_Asp60_BS
InterPro; IPR015655; Protein_Pase_2C

Pfam

Pfam; PF00481; PP2C;
Pfam; PF07830; PP2C_C;

SMART

SMART; SM00331; PP2C_SIG;
SMART; SM00332; PP2Cc;

PROSITE

PROSITE; PS01032; PP2C;

PRINTS