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P49443

- PPM1A_MOUSE

UniProt

P49443 - PPM1A_MOUSE

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Protein
Protein phosphatase 1A
Gene
Ppm1a, Pppm1a
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Cofactori

Binds 2 magnesium or manganese ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601Manganese 1 By similarity
Metal bindingi60 – 601Manganese 2 By similarity
Metal bindingi61 – 611Manganese 1; via carbonyl oxygen By similarity
Metal bindingi239 – 2391Manganese 2 By similarity
Metal bindingi282 – 2821Manganese 2 By similarity

GO - Molecular functioni

  1. R-SMAD binding Source: UniProtKB
  2. calmodulin-dependent protein phosphatase activity Source: Ensembl
  3. magnesium ion binding Source: InterPro
  4. manganese ion binding Source: InterPro
  5. phosphoprotein phosphatase activity Source: MGI
  6. signal transducer activity Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. N-terminal protein myristoylation Source: UniProtKB
  2. Wnt signaling pathway Source: Ensembl
  3. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  4. negative regulation of NF-kappaB import into nucleus Source: UniProtKB
  5. negative regulation of SMAD protein complex assembly Source: Ensembl
  6. negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  7. peptidyl-threonine dephosphorylation Source: Ensembl
  8. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  9. positive regulation of Wnt signaling pathway Source: Ensembl
  10. positive regulation of transcription, DNA-templated Source: Ensembl
  11. protein dephosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_220701. Regulation of AMPK activity via LKB1.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ppm1a
Synonyms:Pppm1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:99878. Ppm1a.

Subcellular locationi

Nucleus By similarity. Cytoplasmcytosol. Membrane
Note: Weakly associates at the membrane and N-myristoylation mediates the membrane localization.2 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
  3. neuron projection Source: Ensembl
  4. nucleus Source: UniProtKB-SubCell
  5. voltage-gated calcium channel complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 382381Protein phosphatase 1A
PRO_0000057742Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei375 – 3751Phosphoserine By similarity

Post-translational modificationi

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

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiP49443.
PaxDbiP49443.
PRIDEiP49443.

PTM databases

PhosphoSiteiP49443.

Expressioni

Gene expression databases

BgeeiP49443.
GenevestigatoriP49443.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi202332. 3 interactions.
IntActiP49443. 2 interactions.
MINTiMINT-4108351.

Structurei

3D structure databases

ProteinModelPortaliP49443.
SMRiP49443. Positions 2-368.

Family & Domainsi

Sequence similaritiesi

Belongs to the PP2C family.

Phylogenomic databases

eggNOGiCOG0631.
GeneTreeiENSGT00740000115384.
HOGENOMiHOG000233895.
HOVERGENiHBG053647.
InParanoidiP49443.
KOiK04457.
OMAiEVYAIER.
OrthoDBiEOG7WMCJH.
PhylomeDBiP49443.
TreeFamiTF313590.

Family and domain databases

Gene3Di1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProiIPR001932. PP2C-like_dom.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view]
PANTHERiPTHR13832. PTHR13832. 1 hit.
PfamiPF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view]
SMARTiSM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEiPS01032. PP2C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49443-1 [UniParc]FASTAAdd to Basket

« Hide

MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPSGL    50
ETWSFFAVYD GHAGSQVAKY CCEHLLDHIT NNQDFRGSAG APSVENVKNG 100
IRTGFLEIDE HMRVMSEKKH GADRSGSTAV GVLISPQHTY FINCGDSRGL 150
LCRNRKVHFF TQDHKPSNPL EKERIQNAGG SVMIQRVNGS LAVSRALGDF 200
DYKCVHGKGP TEQLVSPEPE VHDIERSEED DQFIILACDG IWDVMGNEEL 250
CDFVRSRLEV TDDLEKVCNE VVDTCLYKGS RDNMSVILIC FPSAPKVSAE 300
AVKKEAELDK YLESRVEEII KKQVEGVPDL VHVMRTLASE NIPSLPPGGE 350
LASKRNVIEA VYNRLNPYKN DDTDSASTDD MW 382
Length:382
Mass (Da):42,433
Last modified:February 1, 1996 - v1
Checksum:iDC206610E1583870
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D28117 mRNA. Translation: BAA05662.1.
BC008595 mRNA. Translation: AAH08595.1.
CCDSiCCDS25970.1.
PIRiI53823.
RefSeqiNP_032936.1. NM_008910.3.
XP_006515666.1. XM_006515603.1.
UniGeneiMm.261045.

Genome annotation databases

EnsembliENSMUST00000021514; ENSMUSP00000021514; ENSMUSG00000021096.
GeneIDi19042.
KEGGimmu:19042.
UCSCiuc007nvu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D28117 mRNA. Translation: BAA05662.1 .
BC008595 mRNA. Translation: AAH08595.1 .
CCDSi CCDS25970.1.
PIRi I53823.
RefSeqi NP_032936.1. NM_008910.3.
XP_006515666.1. XM_006515603.1.
UniGenei Mm.261045.

3D structure databases

ProteinModelPortali P49443.
SMRi P49443. Positions 2-368.
ModBasei Search...

Protein-protein interaction databases

BioGridi 202332. 3 interactions.
IntActi P49443. 2 interactions.
MINTi MINT-4108351.

PTM databases

PhosphoSitei P49443.

Proteomic databases

MaxQBi P49443.
PaxDbi P49443.
PRIDEi P49443.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000021514 ; ENSMUSP00000021514 ; ENSMUSG00000021096 .
GeneIDi 19042.
KEGGi mmu:19042.
UCSCi uc007nvu.2. mouse.

Organism-specific databases

CTDi 5494.
MGIi MGI:99878. Ppm1a.

Phylogenomic databases

eggNOGi COG0631.
GeneTreei ENSGT00740000115384.
HOGENOMi HOG000233895.
HOVERGENi HBG053647.
InParanoidi P49443.
KOi K04457.
OMAi EVYAIER.
OrthoDBi EOG7WMCJH.
PhylomeDBi P49443.
TreeFami TF313590.

Enzyme and pathway databases

Reactomei REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_220701. Regulation of AMPK activity via LKB1.

Miscellaneous databases

ChiTaRSi PPM1A. mouse.
NextBioi 295493.
PROi P49443.
SOURCEi Search...

Gene expression databases

Bgeei P49443.
Genevestigatori P49443.

Family and domain databases

Gene3Di 1.10.10.430. 1 hit.
3.60.40.10. 1 hit.
InterProi IPR001932. PP2C-like_dom.
IPR012911. PP2C_C.
IPR000222. PP2C_Mn2_Asp60_BS.
IPR015655. Protein_Pase_2C.
[Graphical view ]
PANTHERi PTHR13832. PTHR13832. 1 hit.
Pfami PF00481. PP2C. 1 hit.
PF07830. PP2C_C. 1 hit.
[Graphical view ]
SMARTi SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view ]
SUPFAMi SSF81601. SSF81601. 1 hit.
SSF81606. SSF81606. 1 hit.
PROSITEi PS01032. PP2C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiPPM1A_MOUSE
AccessioniPrimary (citable) accession number: P49443
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi