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O62829

- PPM1A_BOVIN

UniProt

O62829 - PPM1A_BOVIN

Protein

Protein phosphatase 1A

Gene

PPM1A

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      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. magnesium ion binding Source: InterPro
    2. manganese ion binding Source: InterPro
    3. phosphoprotein phosphatase activity Source: AgBase
    4. protein serine/threonine phosphatase activity Source: InterPro
    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. N-terminal protein myristoylation Source: UniProtKB
    4. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: AgBase
    5. protein dephosphorylation Source: UniProtKB
    6. signal transduction Source: GOC

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_203853. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_209268. 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
    Gene namesi
    Name:PPM1A
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 10

    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_0000057740Add
    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

    Proteomic databases

    PRIDEiO62829.

    Interactioni

    Subunit structurei

    Monomer. 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

    STRINGi9913.ENSBTAP00000024128.

    Structurei

    3D structure databases

    ProteinModelPortaliO62829.
    SMRiO62829. Positions 2-368.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PP2C family.Curated

    Phylogenomic databases

    eggNOGiCOG0631.
    GeneTreeiENSGT00740000115384.
    HOGENOMiHOG000233895.
    HOVERGENiHBG053647.
    InParanoidiO62829.
    KOiK04457.
    OMAiEVYAIER.
    OrthoDBiEOG7WMCJH.
    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.

    O62829-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPSGL    50
    ETWSFFAVYD GHAGSQVAKY CCEHLLDHIT NNQDFKGSAG APSVENVKNG 100
    IRTGFLEIDE HMRVMSEKKH GADRSGSTAV GVLISPQHTY FINCGDSRGL 150
    LCRNRKVYFF TQDHKPSNPL EKERIQNAGG SVMIQRVNGS LAVSRALGDF 200
    DYKCVHGKGP TEQLVSPEPE VHDIERSEED DQFIILACDG IWDVMGNEEL 250
    CDFVRSRLEV TDDLEKVCNE VVDTCLYKGS RDNMSVILIC FPNAPKVSPE 300
    AVKKEEELDK YLESRVEEII KKQGEGVPDL VHVMRTLASE NIPSLPPGGE 350
    LASKRNVIEA VYNRLNPYKN DDTDSTSTDD MW 382
    Length:382
    Mass (Da):42,530
    Last modified:August 1, 1998 - v1
    Checksum:iA716B3FA0E7E21C2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005457 mRNA. Translation: CAA06554.1.
    RefSeqiNP_776854.1. NM_174429.2.
    UniGeneiBt.4671.

    Genome annotation databases

    EnsembliENSBTAT00000024128; ENSBTAP00000024128; ENSBTAG00000018127.
    GeneIDi281994.
    KEGGibta:281994.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ005457 mRNA. Translation: CAA06554.1 .
    RefSeqi NP_776854.1. NM_174429.2.
    UniGenei Bt.4671.

    3D structure databases

    ProteinModelPortali O62829.
    SMRi O62829. Positions 2-368.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000024128.

    Proteomic databases

    PRIDEi O62829.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000024128 ; ENSBTAP00000024128 ; ENSBTAG00000018127 .
    GeneIDi 281994.
    KEGGi bta:281994.

    Organism-specific databases

    CTDi 5494.

    Phylogenomic databases

    eggNOGi COG0631.
    GeneTreei ENSGT00740000115384.
    HOGENOMi HOG000233895.
    HOVERGENi HBG053647.
    InParanoidi O62829.
    KOi K04457.
    OMAi EVYAIER.
    OrthoDBi EOG7WMCJH.
    TreeFami TF313590.

    Enzyme and pathway databases

    Reactomei REACT_203853. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_209268. Regulation of AMPK activity via LKB1.

    Miscellaneous databases

    NextBioi 20805862.

    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. "Protein phosphatase type-2C isozymes present in vertebrate retinae: purification, characterization, and localization in photoreceptors."
      Klumpp S., Selke D., Fischer D., Baumann A., Mueller F., Thanos S.
      J. Neurosci. Res. 51:328-338(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Retina.

    Entry informationi

    Entry nameiPPM1A_BOVIN
    AccessioniPrimary (citable) accession number: O62829
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 108 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