Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q7TMB3

- PPR3C_MOUSE

UniProt

Q7TMB3 - PPR3C_MOUSE

Protein

Protein phosphatase 1 regulatory subunit 3C

Gene

Ppp1r3c

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types.10 Publications

    GO - Molecular functioni

    1. protein phosphatase binding Source: MGI

    GO - Biological processi

    1. glycogen biosynthetic process Source: MGI
    2. glycogen metabolic process Source: MGI
    3. protein targeting Source: MGI

    Keywords - Biological processi

    Carbohydrate metabolism, Glycogen metabolism

    Enzyme and pathway databases

    ReactomeiREACT_188939. Glycogen synthesis.
    REACT_203841. Myoclonic epilepsy of Lafora.

    Protein family/group databases

    CAZyiCBM21. Carbohydrate-Binding Module Family 21.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase 1 regulatory subunit 3C
    Alternative name(s):
    Protein phosphatase 1 regulatory subunit 5
    Short name:
    PP1 subunit R5
    Protein targeting to glycogen
    Short name:
    PTG
    Gene namesi
    Name:Ppp1r3cImported
    Synonyms:Ppp1r5By similarity
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1858229. Ppp1r3c.

    Pathology & Biotechi

    Disruption phenotypei

    Mice display embryonic lethality when homozygous. Heterozygotes display decreased protein levels, decreased glycogen accumulation and glycogen synthase activity, reduced insulin-stimulated glycogen synthesis and progressive age-dependent glucose intolerance. When Ppp1r3c is silenced in adults, they display decreased PP1 activity and glycogen accumulation, increased phosphorylation of glycogen phosphorylase, increased GLUT1 levels, increased glucose uptake and increased glycogen degradation.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851V → A: Abolishes binding to PP1 but has no effect on binding to glycogen synthase, glycogen phosphorylase or glycogen; when associated with A-87. 1 Publication
    Mutagenesisi87 – 871F → A: Abolishes binding to PP1 but has no effect on binding to glycogen synthase, glycogen phosphorylase or glycogen; when associated with A-85. 1 Publication
    Mutagenesisi247 – 2471D → A: Abolishes binding to glycogen synthase and glycogen phosphorylase but has no effect on binding to PP1 or glycogen; when associated with A-250. 1 Publication
    Mutagenesisi250 – 2501E → A: Abolishes binding to glycogen synthase and glycogen phosphorylase but has no effect on binding to PP1 or glycogen; when associated with A-247. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 317317Protein phosphatase 1 regulatory subunit 3CPRO_0000285928Add
    BLAST

    Post-translational modificationi

    Ubiquitinated by NHLRC1/malin in a EPM2A/laforin-dependent manner.By similarity

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiQ7TMB3.
    PRIDEiQ7TMB3.

    Expressioni

    Gene expression databases

    BgeeiQ7TMB3.
    GenevestigatoriQ7TMB3.

    Interactioni

    Subunit structurei

    Interacts with PPP1CC catalytic subunit of PP1 and associates with glycogen. Forms complexes with glycogen phosphorylase, glycogen synthase and phosphorylase kinase which is necessary for its regulation of PP1 activity. Also interacts with EPM2A/laforin.By similarity1 Publication

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000084578.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7TMB3.
    SMRiQ7TMB3. Positions 134-262.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini149 – 257109CBM21PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni141 – 263123Interaction with EPM2ABy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi84 – 874PP1-binding motif

    Domaini

    The N-terminal region is required for binding to PP1, the central region is required for binding to glycogen and the C-terminal region is required for binding to glycogen phosphorylase, glycogen synthase and phosphorylase kinase.1 Publication

    Sequence similaritiesi

    Contains 1 CBM21 (carbohydrate binding type-21) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG288354.
    GeneTreeiENSGT00530000062978.
    HOGENOMiHOG000026799.
    HOVERGENiHBG052744.
    InParanoidiQ7TMB3.
    KOiK07189.
    OMAiIVHVQWK.
    OrthoDBiEOG7H4DTW.
    PhylomeDBiQ7TMB3.
    TreeFamiTF105537.

    Family and domain databases

    InterProiIPR005036. CBM_21.
    IPR017434. Pase-1_Glycogen_target-su_met.
    [Graphical view]
    PfamiPF03370. CBM_21. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038207. PP1_GT_animal. 1 hit.
    PROSITEiPS51159. CBM21. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q7TMB3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSCTRMIHVL DPRPLTSSVM PVDMAMRICL AHSPPLKSFL GPYNGFQRRN    50
    FVNKLKPLKP CLSVKQEAKS QSEWKSPHNQ AKKRVVFADS KGLSLTAIHV 100
    FSDLPEEPAW DLQFDLLDLN DISSSLKLHE EKNLVFDFPQ PSTDYLSFRD 150
    RFQKNFVCLE NCSLQDRTVT GTVKVKNVSF EKKVQVRITF DTWKTYTDVD 200
    CVYMKNVYSS SDSDTFSFAI DLPRVIPTEE KIEFCISYHA NGRIFWDNNE 250
    GQNYRIVHVQ WKPDGVQTQV APKDCAFQQG PPKTEIEPTV FGSPRLASGL 300
    FPEWQSWGRV ENLTSYR 317
    Length:317
    Mass (Da):36,460
    Last modified:October 1, 2003 - v1
    Checksum:i8DC8941B733649D6
    GO

    Sequence cautioni

    The sequence AAB49689.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti165 – 1651Q → E in AAB49689. (PubMed:9045612)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC052769 mRNA. Translation: AAH52769.1.
    BC054739 mRNA. Translation: AAH54739.1.
    U89924 mRNA. Translation: AAB49689.1. Different initiation.
    AK078506 mRNA. Translation: BAC37313.1.
    CCDSiCCDS37968.1.
    RefSeqiNP_058550.1. NM_016854.2.
    UniGeneiMm.24724.

    Genome annotation databases

    EnsembliENSMUST00000087321; ENSMUSP00000084578; ENSMUSG00000067279.
    GeneIDi53412.
    KEGGimmu:53412.
    UCSCiuc008hhs.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC052769 mRNA. Translation: AAH52769.1 .
    BC054739 mRNA. Translation: AAH54739.1 .
    U89924 mRNA. Translation: AAB49689.1 . Different initiation.
    AK078506 mRNA. Translation: BAC37313.1 .
    CCDSi CCDS37968.1.
    RefSeqi NP_058550.1. NM_016854.2.
    UniGenei Mm.24724.

    3D structure databases

    ProteinModelPortali Q7TMB3.
    SMRi Q7TMB3. Positions 134-262.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000084578.

    Protein family/group databases

    CAZyi CBM21. Carbohydrate-Binding Module Family 21.

    Proteomic databases

    PaxDbi Q7TMB3.
    PRIDEi Q7TMB3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000087321 ; ENSMUSP00000084578 ; ENSMUSG00000067279 .
    GeneIDi 53412.
    KEGGi mmu:53412.
    UCSCi uc008hhs.1. mouse.

    Organism-specific databases

    CTDi 5507.
    MGIi MGI:1858229. Ppp1r3c.

    Phylogenomic databases

    eggNOGi NOG288354.
    GeneTreei ENSGT00530000062978.
    HOGENOMi HOG000026799.
    HOVERGENi HBG052744.
    InParanoidi Q7TMB3.
    KOi K07189.
    OMAi IVHVQWK.
    OrthoDBi EOG7H4DTW.
    PhylomeDBi Q7TMB3.
    TreeFami TF105537.

    Enzyme and pathway databases

    Reactomei REACT_188939. Glycogen synthesis.
    REACT_203841. Myoclonic epilepsy of Lafora.

    Miscellaneous databases

    NextBioi 310221.
    PROi Q7TMB3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q7TMB3.
    Genevestigatori Q7TMB3.

    Family and domain databases

    InterProi IPR005036. CBM_21.
    IPR017434. Pase-1_Glycogen_target-su_met.
    [Graphical view ]
    Pfami PF03370. CBM_21. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038207. PP1_GT_animal. 1 hit.
    PROSITEi PS51159. CBM21. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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/6Imported.
      Tissue: BrainImported and Olfactory epitheliumImported.
    2. "PTG, a protein phosphatase 1-binding protein with a role in glycogen metabolism."
      Printen J.A., Brady M.J., Saltiel A.R.
      Science 275:1475-1478(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-317, FUNCTION, ASSOCIATION WITH GLYCOGEN, INTERACTION WITH PPP1CC.
    3. "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] OF 126-317.
      Strain: C57BL/6JImported.
      Tissue: Muellerian ductImported.
    4. "Role of protein targeting to glycogen (PTG) in the regulation of protein phosphatase-1 activity."
      Brady M.J., Printen J.A., Mastick C.C., Saltiel A.R.
      J. Biol. Chem. 272:20198-20204(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "Overexpression of protein targeting to glycogen (PTG) in rat hepatocytes causes profound activation of glycogen synthesis independent of normal hormone- and substrate-mediated regulatory mechanisms."
      Berman H.K., O'Doherty R.M., Anderson P., Newgard C.B.
      J. Biol. Chem. 273:26421-26425(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Distinctive regulatory and metabolic properties of glycogen-targeting subunits of protein phosphatase-1 (PTG, GL, GM/RGl) expressed in hepatocytes."
      Gasa R., Jensen P.B., Berman H.K., Brady M.J., DePaoli-Roach A.A., Newgard C.B.
      J. Biol. Chem. 275:26396-26403(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Identification of binding sites on protein targeting to glycogen for enzymes of glycogen metabolism."
      Fong N.M., Jensen T.C., Shah A.S., Parekh N.N., Saltiel A.R., Brady M.J.
      J. Biol. Chem. 275:35034-35039(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF VAL-85; PHE-87; ASP-247 AND GLU-250.
    8. "Overexpression of protein targeting to glycogen in cultured human muscle cells stimulates glycogen synthesis independent of glycogen and glucose 6-phosphate levels."
      Lerin C., Montell E., Berman H.K., Newgard C.B., Gomez-Foix A.M.
      J. Biol. Chem. 275:39991-39995(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Activation of direct and indirect pathways of glycogen synthesis by hepatic overexpression of protein targeting to glycogen."
      O'Doherty R.M., Jensen P.B., Anderson P., Jones J.G., Berman H.K., Kearney D., Newgard C.B.
      J. Clin. Invest. 105:479-488(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Protein targeting to glycogen overexpression results in the specific enhancement of glycogen storage in 3T3-L1 adipocytes."
      Greenberg C.C., Meredith K.N., Yan L., Brady M.J.
      J. Biol. Chem. 278:30835-30842(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "PTG gene deletion causes impaired glycogen synthesis and developmental insulin resistance."
      Crosson S.M., Khan A., Printen J., Pessin J.E., Saltiel A.R.
      J. Clin. Invest. 111:1423-1432(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    12. "The glycogenic action of protein targeting to glycogen in hepatocytes involves multiple mechanisms including phosphorylase inactivation and glycogen synthase translocation."
      Green A.R., Aiston S., Greenberg C.C., Freeman S., Poucher S.M., Brady M.J., Agius L.
      J. Biol. Chem. 279:46474-46482(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Central role for protein targeting to glycogen in the maintenance of cellular glycogen stores in 3T3-L1 adipocytes."
      Greenberg C.C., Danos A.M., Brady M.J.
      Mol. Cell. Biol. 26:334-342(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiPPR3C_MOUSE
    AccessioniPrimary (citable) accession number: Q7TMB3
    Secondary accession number(s): O08541, Q8BJW8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 69 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3