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P35814

- PPM1A_RABIT

UniProt

P35814 - PPM1A_RABIT

Protein

Protein phosphatase 1A

Gene

PPM1A

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    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 By similarity.By similarity

    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 1By similarity
    Metal bindingi60 – 601Manganese 2By similarity
    Metal bindingi61 – 611Manganese 1; via carbonyl oxygenBy similarity
    Metal bindingi239 – 2391Manganese 2By similarity
    Metal bindingi282 – 2821Manganese 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    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
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 382381Protein phosphatase 1APRO_0000057743Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Modified residuei375 – 3751PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein

    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.By similarity

    Protein-protein interaction databases

    STRINGi9986.ENSOCUP00000008575.

    Structurei

    3D structure databases

    ProteinModelPortaliP35814.
    SMRiP35814. Positions 2-368.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PP2C family.Curated

    Phylogenomic databases

    eggNOGiCOG0631.
    HOGENOMiHOG000233895.
    HOVERGENiHBG053647.

    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.

    P35814-1 [UniParc]FASTAAdd to Basket

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    MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPSGL    50
    ETWSFFAVYD GHAGSQVAKY CCEHLLDHIT NNQDFKGSAG APSVENVKNG 100
    IRTGFLEIDE HMRVMSEKKH GADRSGSTAV GVLISPQHTY FINCGDSRGL 150
    LCRNRKVHFF TQDHKPSNPL EKERIQNAGG SVMIQRVNGS LAVSRALGDF 200
    DYKCVHGKGP TEQLVSPEPE VHDIERSEED DQFIILACDG IWDVMGNEEL 250
    CDFVRSRLEV TDDLEKVCNE VVDTCLYKGS RDNMSVILIC FPNAPKVSPE 300
    AVKKEAELDK YLECRVEEIL KKQGEGVPDL VHVMRTLASE NIPSLPPGGE 350
    LASKRNVIEA VYNRLNPYKN DDTDSTSTDD MW 382
    Length:382
    Mass (Da):42,462
    Last modified:June 1, 1994 - v1
    Checksum:i46BCF1854FD1CA86
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S87757 mRNA. Translation: AAB21783.1.
    PIRiS22422.
    RefSeqiNP_001076167.1. NM_001082698.1.
    UniGeneiOcu.3308.

    Genome annotation databases

    GeneIDi100009431.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S87757 mRNA. Translation: AAB21783.1 .
    PIRi S22422.
    RefSeqi NP_001076167.1. NM_001082698.1.
    UniGenei Ocu.3308.

    3D structure databases

    ProteinModelPortali P35814.
    SMRi P35814. Positions 2-368.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9986.ENSOCUP00000008575.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100009431.

    Organism-specific databases

    CTDi 5494.

    Phylogenomic databases

    eggNOGi COG0631.
    HOGENOMi HOG000233895.
    HOVERGENi HBG053647.

    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

    1. "Mammalian protein serine/threonine phosphatase 2C: cDNA cloning and comparative analysis of amino acid sequences."
      Mann D.J., Campbell D.G., McGowan C.H., Cohen P.T.W.
      Biochim. Biophys. Acta 1130:100-104(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.

    Entry informationi

    Entry nameiPPM1A_RABIT
    AccessioniPrimary (citable) accession number: P35814
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 98 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3