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P62141

- PP1B_MOUSE

UniProt

P62141 - PP1B_MOUSE

Protein

Serine/threonine-protein phosphatase PP1-beta catalytic subunit

Gene

Ppp1cb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (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.2 Publications

    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. protein binding Source: MGI
    6. protein serine/threonine phosphatase activity Source: MGI

    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 cell adhesion Source: UniProtKB
    8. 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

    Enzyme and pathway databases

    ReactomeiREACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    REACT_215733. Downregulation of TGF-beta receptor signaling.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:104871. 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. cytoplasm Source: MGI
    2. MLL5-L complex Source: Ensembl
    3. nucleolus 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 – 327326Serine/threonine-protein phosphatase PP1-beta catalytic subunitPRO_0000058780Add
    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

    MaxQBiP62141.
    PaxDbiP62141.
    PRIDEiP62141.

    PTM databases

    PhosphoSiteiP62141.

    Expressioni

    Gene expression databases

    BgeeiP62141.
    GenevestigatoriP62141.

    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. 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 PPP1R12A and NUAK1; the interaction is direct. Interacts with TRIM28; the interaction is weak By similarity. Interacts with PPP1R15A; the interaction mediates binding to EIF2S1. 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 TRIM28; the interaction is weak By similarity. Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with PPP1R15B; the interaction mediates binding to EIF2S1.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi202336. 8 interactions.
    IntActiP62141. 9 interactions.
    MINTiMINT-4428444.
    STRINGi10090.ENSMUSP00000015100.

    Structurei

    3D structure databases

    ProteinModelPortaliP62141.
    SMRiP62141. Positions 1-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    GeneTreeiENSGT00530000062911.
    HOVERGENiHBG000216.
    InParanoidiQ542E7.
    KOiK06269.
    OMAiPDLQGME.
    OrthoDBiEOG7TJ3K3.
    PhylomeDBiP62141.
    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.

    P62141-1 [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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641I → N in BAC40733. (PubMed:16141072)Curated
    Sequence conflicti148 – 1481W → R in BAE42366. (PubMed:16141072)Curated
    Sequence conflicti223 – 2231S → F in BAE38902. (PubMed:16141072)Curated
    Sequence conflicti250 – 2501V → E in BAB23473. (PubMed:16141072)Curated
    Sequence conflicti269 – 2691P → S in BAE42366. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27073 mRNA. Translation: AAA37527.1.
    AK004686 mRNA. Translation: BAB23473.1.
    AK088893 mRNA. Translation: BAC40636.1.
    AK089067 mRNA. Translation: BAC40733.1.
    AK147112 mRNA. Translation: BAE27684.1.
    AK160743 mRNA. Translation: BAE35984.1.
    AK166168 mRNA. Translation: BAE38608.1.
    AK166623 mRNA. Translation: BAE38902.1.
    AK168141 mRNA. Translation: BAE40108.1.
    AK169379 mRNA. Translation: BAE41126.1.
    AK171283 mRNA. Translation: BAE42366.1.
    BC046832 mRNA. Translation: AAH46832.1.
    CCDSiCCDS19193.1.
    PIRiD32550.
    RefSeqiNP_766295.2. NM_172707.3.
    UniGeneiMm.241931.
    Mm.456635.

    Genome annotation databases

    EnsembliENSMUST00000015100; ENSMUSP00000015100; ENSMUSG00000014956.
    ENSMUST00000131300; ENSMUSP00000121550; ENSMUSG00000014956.
    GeneIDi19046.
    KEGGimmu:19046.
    UCSCiuc008wzq.2. mouse.

    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
    M27073 mRNA. Translation: AAA37527.1 .
    AK004686 mRNA. Translation: BAB23473.1 .
    AK088893 mRNA. Translation: BAC40636.1 .
    AK089067 mRNA. Translation: BAC40733.1 .
    AK147112 mRNA. Translation: BAE27684.1 .
    AK160743 mRNA. Translation: BAE35984.1 .
    AK166168 mRNA. Translation: BAE38608.1 .
    AK166623 mRNA. Translation: BAE38902.1 .
    AK168141 mRNA. Translation: BAE40108.1 .
    AK169379 mRNA. Translation: BAE41126.1 .
    AK171283 mRNA. Translation: BAE42366.1 .
    BC046832 mRNA. Translation: AAH46832.1 .
    CCDSi CCDS19193.1.
    PIRi D32550.
    RefSeqi NP_766295.2. NM_172707.3.
    UniGenei Mm.241931.
    Mm.456635.

    3D structure databases

    ProteinModelPortali P62141.
    SMRi P62141. Positions 1-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202336. 8 interactions.
    IntActi P62141. 9 interactions.
    MINTi MINT-4428444.
    STRINGi 10090.ENSMUSP00000015100.

    Chemistry

    BindingDBi P62141.

    PTM databases

    PhosphoSitei P62141.

    Proteomic databases

    MaxQBi P62141.
    PaxDbi P62141.
    PRIDEi P62141.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000015100 ; ENSMUSP00000015100 ; ENSMUSG00000014956 .
    ENSMUST00000131300 ; ENSMUSP00000121550 ; ENSMUSG00000014956 .
    GeneIDi 19046.
    KEGGi mmu:19046.
    UCSCi uc008wzq.2. mouse.

    Organism-specific databases

    CTDi 5500.
    MGIi MGI:104871. Ppp1cb.

    Phylogenomic databases

    eggNOGi COG0639.
    GeneTreei ENSGT00530000062911.
    HOVERGENi HBG000216.
    InParanoidi Q542E7.
    KOi K06269.
    OMAi PDLQGME.
    OrthoDBi EOG7TJ3K3.
    PhylomeDBi P62141.
    TreeFami TF354243.

    Enzyme and pathway databases

    Reactomei REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
    REACT_215733. Downregulation of TGF-beta receptor signaling.

    Miscellaneous databases

    ChiTaRSi PPP1CB. mouse.
    NextBioi 295509.
    PROi P62141.
    SOURCEi Search...

    Gene expression databases

    Bgeei P62141.
    Genevestigatori P62141.

    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. "The fission yeast dis2+ gene required for chromosome disjoining encodes one of two putative type 1 protein phosphatases."
      Ohkura H., Kinoshita N., Miyatani S., Toda T., Yanagida M.
      Cell 57:997-1007(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Dendritic cell, Embryonic head, Embryonic heart, Embryonic kidney, Lung, Mammary gland, Morula and Thymus.
    3. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    4. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 26-35; 60-73 AND 150-167, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    5. "Inhibition of a constitutive translation initiation factor 2alpha phosphatase, CReP, promotes survival of stressed cells."
      Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H.P., Ron D.
      J. Cell Biol. 163:767-775(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R15B.
    6. "Nck in a complex containing the catalytic subunit of protein phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling and cell survival to endoplasmic reticulum stress."
      Latreille M., Larose L.
      J. Biol. Chem. 281:26633-26644(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
    7. "Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock."
      Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.
      PLoS ONE 6:E21325-E21325(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN CLOCK.
    8. "The period of the circadian oscillator is primarily determined by the balance between casein kinase 1 and protein phosphatase 1."
      Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.
      Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CIRCADIAN CLOCK.

    Entry informationi

    Entry nameiPP1B_MOUSE
    AccessioniPrimary (citable) accession number: P62141
    Secondary accession number(s): P37140
    , Q3TBE5, Q3TL90, Q542E7, Q8C285, Q9DBY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 117 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    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