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P49443 (PPM1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 107. 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.
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.

Catalytic activity

A phosphoprotein + H2O = a protein + 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.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the PP2C family.

Ontologies

Keywords
   Cellular componentNucleus
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMLipoprotein
Myristate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt receptor signaling pathway

Inferred from electronic annotation. Source: Compara

negative regulation of SMAD protein complex assembly

Inferred from electronic annotation. Source: Compara

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Compara

peptidyl-threonine dephosphorylation

Inferred from electronic annotation. Source: Compara

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

Inferred from electronic annotation. Source: Compara

positive regulation of Wnt receptor signaling pathway

Inferred from electronic annotation. Source: Compara

positive regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: Compara

protein dephosphorylation

Inferred from direct assay PubMed 14664809. Source: MGI

   Cellular_componentneuron projection

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

voltage-gated calcium channel complex

Inferred from electronic annotation. Source: Compara

   Molecular_functionR-SMAD binding

Inferred from sequence or structural similarity. Source: UniProtKB

calmodulin-dependent protein phosphatase activity

Inferred from electronic annotation. Source: Compara

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 14654243. Source: MGI

signal transducer activity

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Protein 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
Modified residue3771Phosphoserine Ref.3
Lipidation21N-myristoyl glycine By similarity

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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D28117 mRNA. Translation: BAA05662.1.
BC008595 mRNA. Translation: AAH08595.1.
IPIIPI00114802.
PIRI53823.
RefSeqNP_032936.1. NM_008910.3.
UniGeneMm.261045.

3D structure databases

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

PTM databases

PhosphoSiteP49443.

Proteomic databases

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.
GeneTreeENSGT00650000093052.
HOGENOMHOG000233895.
HOVERGENHBG053647.
InParanoidP49443.
KOK04457.
OMAEVYAIER.
OrthoDBEOG4GMTX1.

Gene expression databases

BgeeP49443.
GenevestigatorP49443.
GermOnlineENSMUSG00000021096. Mus musculus.

Family and domain databases

Gene3D1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProIPR001932. PP2C-like.
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]
SUPFAMSSF81606. PP2C-related. 1 hit.
SSF81601. PP2C_C. 1 hit.
PROSITEPS01032. PP2C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPM1A. mouse.
NextBio295493.
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: April 3, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families