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P49443 (PPM1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein phosphatase 1A

EC=3.1.3.16
Alternative name(s):
Protein phosphatase 2C isoform alpha
Short name=PP2C-alpha
Protein phosphatase IA
Gene names
Name:Ppm1a
Synonyms:Pppm1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 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. Ref.5

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 magnesium or manganese ions per subunit.

Subunit structure

Monomer By similarity. Interacts with SMAD2; the interaction dephosphorylates SMAD2 in its C-terminal SXS motif resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the TGF-beta-mediated signaling. Interacts with SMAD2; the interaction dephosphorylates SMAD2 in its C-terminal SXS motif resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the TGF-beta-mediated signaling By similarity. Interacts with the phosphorylated form of IKBKB/IKKB By similarity.

Subcellular location

Nucleus By similarity. Cytoplasmcytosol. Membrane. Note: Weakly associates at the membrane and N-myristoylation mediates the membrane localization. Ref.4 Ref.5

Post-translational modification

N-myristoylation is essential for the recognition of its substrates for dephosphorylation.

Sequence similarities

Belongs to the PP2C family.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
Nucleus
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-terminal protein myristoylation

Inferred from direct assay Ref.5. Source: UniProtKB

Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of NF-kappaB import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of SMAD protein complex assembly

Inferred from electronic annotation. Source: Ensembl

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

peptidyl-threonine dephosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Inferred from mutant phenotype Ref.5. Source: UniProtKB

   Cellular_componentcytosol

Inferred from direct assay Ref.5. Source: UniProtKB

membrane

Inferred from direct assay Ref.5. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

voltage-gated calcium channel complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionR-SMAD binding

Inferred from sequence or structural similarity. Source: UniProtKB

calmodulin-dependent protein phosphatase activity

Inferred from electronic annotation. Source: Ensembl

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

manganese ion binding

Inferred from electronic annotation. Source: InterPro

phosphoprotein phosphatase activity

Inferred from direct assay PubMed 14654243Ref.5. Source: MGI

signal transducer activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 382381Protein phosphatase 1A
PRO_0000057742

Sites

Metal binding601Manganese 1 By similarity
Metal binding601Manganese 2 By similarity
Metal binding611Manganese 1; via carbonyl oxygen By similarity
Metal binding2391Manganese 2 By similarity
Metal binding2821Manganese 2 By similarity

Amino acid modifications

Modified residue3751Phosphoserine By similarity
Lipidation21N-myristoyl glycine Ref.5

Sequences

Sequence LengthMass (Da)Tools
P49443 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: DC206610E1583870

FASTA38242,433
        10         20         30         40         50         60 
MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPSGL ETWSFFAVYD 

        70         80         90        100        110        120 
GHAGSQVAKY CCEHLLDHIT NNQDFRGSAG APSVENVKNG IRTGFLEIDE HMRVMSEKKH 

       130        140        150        160        170        180 
GADRSGSTAV GVLISPQHTY FINCGDSRGL LCRNRKVHFF TQDHKPSNPL EKERIQNAGG 

       190        200        210        220        230        240 
SVMIQRVNGS LAVSRALGDF DYKCVHGKGP TEQLVSPEPE VHDIERSEED DQFIILACDG 

       250        260        270        280        290        300 
IWDVMGNEEL CDFVRSRLEV TDDLEKVCNE VVDTCLYKGS RDNMSVILIC FPSAPKVSAE 

       310        320        330        340        350        360 
AVKKEAELDK YLESRVEEII KKQVEGVPDL VHVMRTLASE NIPSLPPGGE LASKRNVIEA 

       370        380 
VYNRLNPYKN DDTDSASTDD MW 

« Hide

References

« Hide 'large scale' references
[1]"The cDNA sequence encoding mouse Mg2+ -dependent protein phosphatase alpha."
Kato S., Kobayashi T., Terasawa T., Ohnishi M., Sasahara Y., Kanamaru R., Tamura S.
Gene 145:311-312(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"Protein phosphatase 5 modulates SMAD3 function in the transforming growth factor-? pathway."
Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.
Cell. Signal. 24:1999-2006(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"N-Myristoylation is essential for protein phosphatases PPM1A and PPM1B to dephosphorylate their physiological substrates in cells."
Chida T., Ando M., Matsuki T., Masu Y., Nagaura Y., Takano-Yamamoto T., Tamura S., Kobayashi T.
Biochem. J. 449:741-749(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D28117 mRNA. Translation: BAA05662.1.
BC008595 mRNA. Translation: AAH08595.1.
CCDSCCDS25970.1.
PIRI53823.
RefSeqNP_032936.1. NM_008910.3.
XP_006515666.1. XM_006515603.1.
UniGeneMm.261045.

3D structure databases

ProteinModelPortalP49443.
SMRP49443. Positions 2-368.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202332. 3 interactions.
IntActP49443. 2 interactions.
MINTMINT-4108351.

PTM databases

PhosphoSiteP49443.

Proteomic databases

MaxQBP49443.
PaxDbP49443.
PRIDEP49443.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021514; ENSMUSP00000021514; ENSMUSG00000021096.
GeneID19042.
KEGGmmu:19042.
UCSCuc007nvu.2. mouse.

Organism-specific databases

CTD5494.
MGIMGI:99878. Ppm1a.

Phylogenomic databases

eggNOGCOG0631.
GeneTreeENSGT00740000115384.
HOGENOMHOG000233895.
HOVERGENHBG053647.
InParanoidP49443.
KOK04457.
OMAEVYAIER.
OrthoDBEOG7WMCJH.
PhylomeDBP49443.
TreeFamTF313590.

Gene expression databases

BgeeP49443.
GenevestigatorP49443.

Family and domain databases

Gene3D1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like_dom.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERPTHR13832. PTHR13832. 1 hit.
PfamPF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view]
SMARTSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMSSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPM1A. mouse.
NextBio295493.
PROP49443.
SOURCESearch...

Entry information

Entry namePPM1A_MOUSE
AccessionPrimary (citable) accession number: P49443
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot