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P62142

- PP1B_RAT

UniProt

P62142 - PP1B_RAT

Protein

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Gene

Ppp1cb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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 (PP1) is essential for cell division, it participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. 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. 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.
    [Myosin light-chain] phosphate + H2O = [myosin light-chain] + phosphate.

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    Inhibited by the toxins okadaic acid, tautomycin and microcystin Leu-Arg. The phosphatase activity of the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited by Salubrinal, a drug that protects cells from endoplasmic reticulum stress By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi63 – 631Manganese 1By similarity
    Metal bindingi65 – 651Manganese 1By similarity
    Metal bindingi91 – 911Manganese 1By similarity
    Metal bindingi91 – 911Manganese 2By similarity
    Metal bindingi123 – 1231Manganese 2By similarity
    Active sitei124 – 1241Proton donorBy similarity
    Metal bindingi172 – 1721Manganese 2By similarity
    Metal bindingi247 – 2471Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. myosin-light-chain-phosphatase activity Source: UniProtKB
    3. myosin phosphatase activity Source: UniProtKB
    4. phosphatase activity Source: UniProtKB
    5. phosphoprotein phosphatase activity Source: RGD
    6. protein binding Source: IntAct

    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: RGD
    7. regulation of cell adhesion Source: UniProtKB
    8. regulation of circadian rhythm Source: UniProtKB
    9. regulation of glycogen biosynthetic process Source: RGD
    10. regulation of glycogen catabolic process Source: RGD

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

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

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_194641. Downregulation of TGF-beta receptor signaling.
    REACT_198294. Regulation of PLK1 Activity at G2/M Transition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP1-beta catalytic subunit (EC:3.1.3.16, EC:3.1.3.53)
    Short name:
    PP-1B
    Gene namesi
    Name:Ppp1cb
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 6

    Organism-specific databases

    RGDi3376. Ppp1cb.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Nucleusnucleoplasm By similarity. Nucleusnucleolus By similarity
    Note: Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleus to nuclear speckles By similarity.By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. glycogen granule Source: RGD
    3. nucleolus Source: UniProtKB-SubCell
    4. nucleoplasm Source: UniProtKB-SubCell
    5. protein phosphatase type 1 complex Source: RGD
    6. 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 – 327326Serine/threonine-protein phosphatase PP1-beta catalytic subunitPRO_0000058783Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei316 – 3161PhosphothreonineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP62142.
    PRIDEiP62142.

    PTM databases

    PhosphoSiteiP62142.

    Expressioni

    Gene expression databases

    GenevestigatoriP62142.

    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. The targeting or regulatory subunits determine the substrate specificity of PP1. 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. PPP1R15A and PPP1R15B 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 PPP1R7 and PPP1R12C. Interacts with PPP1R16B. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8. Interacts with PPP1R12A and NUAK1; the interaction is direct. Interacts with TRIM28; the interaction is weak By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ppp1r9aO358672EBI-352326,EBI-7092421
    Rpl5P098952EBI-352326,EBI-916235

    Protein-protein interaction databases

    IntActiP62142. 7 interactions.
    MINTiMINT-4568111.
    STRINGi10116.ENSRNOP00000006190.

    Structurei

    3D structure databases

    ProteinModelPortaliP62142.
    SMRiP62142. Positions 1-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000062911.
    HOGENOMiHOG000172697.
    HOVERGENiHBG000216.
    InParanoidiP62142.
    KOiK06269.
    OMAiPDLQGME.
    OrthoDBiEOG7TJ3K3.
    PhylomeDBiP62142.
    TreeFamiTF354243.

    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.

    P62142-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI    50
    LLELEAPLKI CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL 100
    ETICLLLAYK IKYPENFFLL RGNHECASIN RIYGFYDECK RRFNIKLWKT 150
    FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ SMEQIRRIMR PTDVPDTGLL 200
    CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL DLICRAHQVV 250
    EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK 300
    KAKYQYGGLN SGRPVTPPRT ANPPKKR 327
    Length:327
    Mass (Da):37,187
    Last modified:January 23, 2007 - v3
    Checksum:iE8356022E9B94ECD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D90164 mRNA. Translation: BAA14195.1.
    BC062033 mRNA. Translation: AAH62033.1.
    PIRiI76571.
    RefSeqiNP_037197.1. NM_013065.2.
    UniGeneiRn.128769.
    Rn.39034.

    Genome annotation databases

    EnsembliENSRNOT00000006190; ENSRNOP00000006190; ENSRNOG00000004612.
    GeneIDi25594.
    KEGGirno:25594.
    UCSCiRGD:3376. rat.

    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
    D90164 mRNA. Translation: BAA14195.1 .
    BC062033 mRNA. Translation: AAH62033.1 .
    PIRi I76571.
    RefSeqi NP_037197.1. NM_013065.2.
    UniGenei Rn.128769.
    Rn.39034.

    3D structure databases

    ProteinModelPortali P62142.
    SMRi P62142. Positions 1-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P62142. 7 interactions.
    MINTi MINT-4568111.
    STRINGi 10116.ENSRNOP00000006190.

    Chemistry

    BindingDBi P62142.

    PTM databases

    PhosphoSitei P62142.

    Proteomic databases

    PaxDbi P62142.
    PRIDEi P62142.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000006190 ; ENSRNOP00000006190 ; ENSRNOG00000004612 .
    GeneIDi 25594.
    KEGGi rno:25594.
    UCSCi RGD:3376. rat.

    Organism-specific databases

    CTDi 5500.
    RGDi 3376. Ppp1cb.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00530000062911.
    HOGENOMi HOG000172697.
    HOVERGENi HBG000216.
    InParanoidi P62142.
    KOi K06269.
    OMAi PDLQGME.
    OrthoDBi EOG7TJ3K3.
    PhylomeDBi P62142.
    TreeFami TF354243.

    Enzyme and pathway databases

    Reactomei REACT_194641. Downregulation of TGF-beta receptor signaling.
    REACT_198294. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    NextBioi 607279.
    PROi P62142.

    Gene expression databases

    Genevestigatori P62142.

    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. "Identification of members of the protein phosphatase 1 gene family in the rat and enhanced expression of protein phosphatase 1 alpha gene in rat hepatocellular carcinomas."
      Sasaki K., Shima H., Kitagawa Y., Irino S., Sugimura T., Nagao M.
      Jpn. J. Cancer Res. 81:1272-1280(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Erratum
      Sasaki K., Shima H., Kitagawa Y., Irino S., Sugimura T., Nagao M.
      Jpn. J. Cancer Res. 82:873-873(1991) [PubMed] [Europe PMC] [Abstract]
    3. "Differential expression of protein phosphatase 1 isoforms in mammalian brain."
      da Cruz e Silva E.F., Fox C.A., Ouimet C.C., Gustafson E., Watson S.J., Greengard P.
      J. Neurosci. 15:3375-3389(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    4. "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].
      Tissue: Prostate.
    5. "Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography."
      Moorhead G., MacKintosh C., Morrice N., Cohen P.
      FEBS Lett. 362:101-105(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 26-35.

    Entry informationi

    Entry nameiPP1B_RAT
    AccessioniPrimary (citable) accession number: P62142
    Secondary accession number(s): P37140
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 104 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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