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P62139

- PP1A_RABIT

UniProt

P62139 - PP1A_RABIT

Protein

Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

Gene

PPP1CA

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (21 Jun 2004)
      Previous versions | rss
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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.1 Publication

    Sites

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

    GO - Molecular functioni

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

    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
    Synonyms:PPP1A
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

    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_0000058776Add
    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

    PRIDEiP62139.

    Expressioni

    Tissue specificityi

    Detected in skeletal muscle (at protein level). Detected in skeletal muscle.1 Publication

    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 TRIM28; the interaction dephosphorylates TRIM28 on 'Ser-824' and forms a complex at the p21 promoter site By similarity. Interacts with PPP1R39. 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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GRIN2BQ132242EBI-2008988,EBI-2256942From a different organism.
    PPP1R11O609272EBI-2008988,EBI-1048104From a different organism.

    Protein-protein interaction databases

    BioGridi1172319. 78 interactions.
    IntActiP62139. 3 interactions.
    MINTiMINT-106725.

    Structurei

    Secondary structure

    1
    330
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 1810
    Turni19 – 224
    Helixi32 – 4817
    Beta strandi51 – 555
    Beta strandi57 – 626
    Helixi69 – 7911
    Beta strandi87 – 893
    Beta strandi94 – 985
    Helixi100 – 11314
    Turni115 – 1173
    Beta strandi118 – 1203
    Helixi128 – 1347
    Helixi136 – 1438
    Helixi146 – 15611
    Beta strandi162 – 1654
    Turni166 – 1683
    Beta strandi169 – 1746
    Helixi183 – 1886
    Beta strandi197 – 1993
    Helixi200 – 2067
    Beta strandi214 – 2185
    Beta strandi222 – 2276
    Helixi229 – 23911
    Beta strandi242 – 2465
    Beta strandi254 – 2585
    Turni259 – 2624
    Beta strandi263 – 2675
    Beta strandi274 – 2763
    Beta strandi280 – 2856
    Beta strandi291 – 2966

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FJMX-ray2.10A/B1-330[»]
    ProteinModelPortaliP62139.
    SMRiP62139. Positions 7-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62139.

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    HOVERGENiHBG000216.

    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]
    ProtoNetiSearch...

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: P62139-1) [UniParc]FASTAAdd to Basket

    Also known as: 1-alpha-2

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    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:June 21, 2004 - v1
    Checksum:i60C37E1AD9831DAC
    GO
    Isoform 1 (identifier: P62139-2) [UniParc] [UniParc]FASTAAdd to Basket

    Also known as: 1-alpha-1

    The sequence of this isoform differs from the canonical sequence as follows:
         2-33: SDSEKLNLDSIIGRLLEVQGSRPGKNVQLTEN → MVTIMTTSEYLSGY

    Note: No experimental confirmation available.

    Show »
    Length:312
    Mass (Da):35,597
    Checksum:iF8F24487D1110507
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 3332SDSEK…QLTEN → MVTIMTTSEYLSGY in isoform 1. 1 PublicationVSP_010642Add
    BLAST

    Sequence conflict

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti309 – 3091F → L in CAA68693. (PubMed:2822491)Curated
    Sequence conflicti309 – 3091F → L in CAA30645. (PubMed:2835264)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00701 mRNA. Translation: CAA68693.1.
    X07798 mRNA. Translation: CAA30645.1.
    X14832 mRNA. Translation: CAA32941.1.
    PIRiS04335. PARB11.
    RefSeqiNP_001095176.1. NM_001101706.1.
    UniGeneiOcu.2075.

    Genome annotation databases

    GeneIDi100009298.

    Keywords - Coding sequence diversityi

    Alternative splicing

    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
    Y00701 mRNA. Translation: CAA68693.1 .
    X07798 mRNA. Translation: CAA30645.1 .
    X14832 mRNA. Translation: CAA32941.1 .
    PIRi S04335. PARB11.
    RefSeqi NP_001095176.1. NM_001101706.1.
    UniGenei Ocu.2075.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FJM X-ray 2.10 A/B 1-330 [» ]
    ProteinModelPortali P62139.
    SMRi P62139. Positions 7-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 1172319. 78 interactions.
    IntActi P62139. 3 interactions.
    MINTi MINT-106725.

    Chemistry

    BindingDBi P62139.

    Proteomic databases

    PRIDEi P62139.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100009298.

    Organism-specific databases

    CTDi 5499.

    Phylogenomic databases

    eggNOGi COG0639.
    HOVERGENi HBG000216.

    Miscellaneous databases

    EvolutionaryTracei P62139.

    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. "Isolation and sequence analysis of a cDNA clone encoding a type-1 protein phosphatase catalytic subunit: homology with protein phosphatase 2A."
      Berndt N., Campbell D.G., Caudwell F.B., Cohen P., da Cruz e Silva E.F., da Cruz e Silva O.B., Cohen P.T.W.
      FEBS Lett. 223:340-346(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
      Strain: New Zealand white.
      Tissue: Skeletal muscle.
    2. "Molecular cloning of a cDNA for the catalytic subunit of rabbit muscle phosphorylase phosphatase."
      Bai G., Zhang Z., Amin J., Deans-Zirattu S.A., Lee E.Y.C.
      FASEB J. 2:3010-3016(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Muscle.
    3. "Two isoforms of protein phosphatase 1 may be produced from the same gene."
      Cohen P.T.W.
      FEBS Lett. 232:17-23(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: New Zealand white.
      Tissue: Skeletal muscle.
    4. "The major type-1 protein phosphatase catalytic subunits are the same gene products in rabbit skeletal muscle and rabbit liver."
      Cohen P.T.W., Schelling D.L., da Cruz e Silva O.B., Barker H.M., Cohen P.
      Biochim. Biophys. Acta 1008:125-128(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: New Zealand white.
      Tissue: Liver.
    5. "FLJ23654 encodes a heart protein phosphatase 1-binding protein (Hepp1)."
      Chen C.Y., Lai N.S., Yang J.J., Huang H.L., Hung W.C., Li C., Lin T.H., Huang H.B.
      Biochem. Biophys. Res. Commun. 391:698-702(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R39.
    6. "Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1."
      Goldberg J., Huang H.B., Kwon Y.G., Greengard P., Nairn A.C., Kuriyan J.
      Nature 376:745-753(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, COFACTOR.

    Entry informationi

    Entry nameiPP1A_RABIT
    AccessioniPrimary (citable) accession number: P62139
    Secondary accession number(s): P08128
    , P08129, P20653, P22802
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: June 21, 2004
    Last modified: October 1, 2014
    This is version 95 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi