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Q3T0E7

- PP1A_BOVIN

UniProt

Q3T0E7 - PP1A_BOVIN

Protein

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Gene

PPP1CA

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
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    Functioni

    Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. May dephosphorylate CSNK1D and CSNK1E By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi64 – 641Manganese 1By similarity
    Metal bindingi66 – 661Manganese 1By similarity
    Metal bindingi92 – 921Manganese 1By similarity
    Metal bindingi92 – 921Manganese 2By similarity
    Metal bindingi124 – 1241Manganese 2By similarity
    Active sitei125 – 1251Proton donorBy similarity
    Metal bindingi173 – 1731Manganese 2By similarity
    Metal bindingi248 – 2481Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphatase activity Source: UniProtKB
    3. phosphoprotein phosphatase activity Source: UniProtKB-KW

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. circadian regulation of gene expression Source: UniProtKB
    4. entrainment of circadian clock by photoperiod Source: UniProtKB
    5. glycogen metabolic process Source: UniProtKB-KW
    6. protein dephosphorylation Source: UniProtKB
    7. regulation of circadian rhythm Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Biological rhythms, Carbohydrate metabolism, Cell cycle, Cell division, Glycogen metabolism

    Keywords - Ligandi

    Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (EC:3.1.3.16)
    Short name:
    PP-1A
    Gene namesi
    Name:PPP1CA
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Nucleusnucleoplasm By similarity. Nucleusnucleolus By similarity
    Note: Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting this protein to the nucleolus. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleolus Source: UniProtKB-SubCell
    3. nucleoplasm Source: UniProtKB-SubCell
    4. PTW/PP1 phosphatase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 330329Serine/threonine-protein phosphatase PP1-alpha catalytic subunitPRO_0000240131Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei305 – 3051N6-acetyllysineBy similarity
    Modified residuei306 – 3061PhosphotyrosineBy similarity
    Modified residuei320 – 3201PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylated. Dephosphorylated at Thr-320 in the presence of ionizing radiation By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ3T0E7.
    PRIDEiQ3T0E7.

    Interactioni

    Subunit structurei

    PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or PPP1CC, which is folded into its native form by inhibitor 2 and glycogen synthetase kinase 3, and then complexed to one or several targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen. Interacts with PPP1R15A and PPP1R15B; the interactions mediate binding to EIF2S1. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R9A, PPP1R9B and PPP1R7. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. Interacts with NOM1 and PPP1R8. Interacts with PPP1R16B. Interacts with RPSA only in the presence of PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the presence of PPP1R10/PNUTS. Interacts with PPP1R39. transition from mitosis into interphase. Interacts with TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site. Interacts with NEK2. Interacts with PHACTR4; which acts as an activator of PP1 activity. Interacts with FER; this promotes phosphorylation at Thr-320 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi172796. 3 interactions.
    IntActiQ3T0E7. 3 interactions.
    STRINGi9913.ENSBTAP00000016111.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3T0E7.
    SMRiQ3T0E7. Positions 7-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172697.
    HOVERGENiHBG000216.
    InParanoidiQ3T0E7.
    KOiK06269.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q3T0E7-1 [UniParc]FASTAAdd to Basket

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    MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP    50
    ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS 100
    LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK 150
    TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL 200
    LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV 250
    VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD 300
    KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK 330
    Length:330
    Mass (Da):37,512
    Last modified:October 11, 2005 - v1
    Checksum:i60C37E1AD9831DAC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC102424 mRNA. Translation: AAI02425.1.
    RefSeqiNP_001030393.1. NM_001035316.2.
    UniGeneiBt.48845.

    Genome annotation databases

    GeneIDi516175.
    KEGGibta:516175.

    Cross-referencesi

    Web resourcesi

    Protein Spotlight

    The things we forget - Issue 32 of March 2003

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC102424 mRNA. Translation: AAI02425.1 .
    RefSeqi NP_001030393.1. NM_001035316.2.
    UniGenei Bt.48845.

    3D structure databases

    ProteinModelPortali Q3T0E7.
    SMRi Q3T0E7. Positions 7-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 172796. 3 interactions.
    IntActi Q3T0E7. 3 interactions.
    STRINGi 9913.ENSBTAP00000016111.

    Chemistry

    BindingDBi Q3T0E7.

    Proteomic databases

    PaxDbi Q3T0E7.
    PRIDEi Q3T0E7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 516175.
    KEGGi bta:516175.

    Organism-specific databases

    CTDi 5499.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172697.
    HOVERGENi HBG000216.
    InParanoidi Q3T0E7.
    KOi K06269.

    Miscellaneous databases

    NextBioi 20872154.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Ileum.

    Entry informationi

    Entry nameiPP1A_BOVIN
    AccessioniPrimary (citable) accession number: Q3T0E7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 77 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. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3