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Q9UQK1

- PPR3C_HUMAN

UniProt

Q9UQK1 - PPR3C_HUMAN

Protein

Protein phosphatase 1 regulatory subunit 3C

Gene

PPP1R3C

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    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.By similarity1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein serine/threonine phosphatase activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. dephosphorylation Source: GOC
    3. glucose metabolic process Source: Reactome
    4. glycogen biosynthetic process Source: Reactome
    5. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    Carbohydrate metabolism, Glycogen metabolism

    Enzyme and pathway databases

    ReactomeiREACT_169208. Glycogen synthesis.
    REACT_200783. 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:PPP1R5Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9293. PPP1R3C.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851V → A: No effect on interaction with EPM2A; when associated with A-87. 1 Publication
    Mutagenesisi87 – 871F → A: No effect on interaction with EPM2A; when associated with A-85. 1 Publication
    Mutagenesisi247 – 2471D → A: No interaction with EPM2A; when associated with A-250. 1 Publication
    Mutagenesisi250 – 2501D → A: No interaction with EPM2A; when associated with A-247. 1 Publication

    Organism-specific databases

    PharmGKBiPA33653.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 317317Protein phosphatase 1 regulatory subunit 3CPRO_0000285927Add
    BLAST

    Post-translational modificationi

    Ubiquitinated by NHLRC1/malin in a EPM2A/laforin-dependent manner.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiQ9UQK1.
    PRIDEiQ9UQK1.

    PTM databases

    PhosphoSiteiQ9UQK1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UQK1.
    BgeeiQ9UQK1.
    CleanExiHS_PPP1R3C.
    GenevestigatoriQ9UQK1.

    Organism-specific databases

    HPAiHPA027041.

    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 similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EPM2AO952785EBI-2506727,EBI-2506661

    Protein-protein interaction databases

    BioGridi111500. 8 interactions.
    IntActiQ9UQK1. 3 interactions.
    MINTiMINT-6783827.
    STRINGi9606.ENSP00000238994.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UQK1.
    SMRiQ9UQK1. 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 EPM2A1 PublicationAdd
    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.By similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG288354.
    HOGENOMiHOG000026799.
    HOVERGENiHBG052744.
    InParanoidiQ9UQK1.
    KOiK07189.
    OMAiIVHVQWK.
    OrthoDBiEOG7H4DTW.
    PhylomeDBiQ9UQK1.
    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.

    Q9UQK1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSCTRMIQVL DPRPLTSSVM PVDVAMRLCL AHSPPVKSFL GPYDEFQRRH    50
    FVNKLKPLKS CLNIKHKAKS QNDWKCSHNQ AKKRVVFADS KGLSLTAIHV 100
    FSDLPEEPAW DLQFDLLDLN DISSALKHHE EKNLILDFPQ PSTDYLSFRS 150
    HFQKNFVCLE NCSLQERTVT GTVKVKNVSF EKKVQIRITF DSWKNYTDVD 200
    CVYMKNVYGG TDSDTFSFAI DLPPVIPTEQ KIEFCISYHA NGQVFWDNND 250
    GQNYRIVHVQ WKPDGVQTQM APQDCAFHQT SPKTELESTI FGSPRLASGL 300
    FPEWQSWGRM ENLASYR 317
    Length:317
    Mass (Da):36,445
    Last modified:May 1, 2007 - v2
    Checksum:iFBFD6DE015F9AB2D
    GO

    Sequence cautioni

    The sequence AAD33215.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti109 – 1091A → S.
    Corresponds to variant rs7089948 [ dbSNP | Ensembl ].
    VAR_059775
    Natural varianti249 – 2491N → S Found in a patient with progressive myoclonic epilepsy type 2 also carrying two mutations in EPM2B. 1 Publication
    VAR_067339

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y18207 mRNA. Translation: CAA77082.1.
    AF110824 Genomic DNA. Translation: AAD33215.1. Sequence problems.
    AK313149 mRNA. Translation: BAG35967.1.
    BX537399 mRNA. Translation: CAD97641.1.
    AL359986 Genomic DNA. Translation: CAH69995.1.
    CH471066 Genomic DNA. Translation: EAW50107.1.
    BC012625 mRNA. Translation: AAH12625.1.
    CCDSiCCDS7416.1.
    RefSeqiNP_005389.1. NM_005398.5.
    UniGeneiHs.303090.
    Hs.744999.

    Genome annotation databases

    EnsembliENST00000238994; ENSP00000238994; ENSG00000119938.
    GeneIDi5507.
    KEGGihsa:5507.
    UCSCiuc001kho.3. human.

    Polymorphism databases

    DMDMi146325084.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y18207 mRNA. Translation: CAA77082.1 .
    AF110824 Genomic DNA. Translation: AAD33215.1 . Sequence problems.
    AK313149 mRNA. Translation: BAG35967.1 .
    BX537399 mRNA. Translation: CAD97641.1 .
    AL359986 Genomic DNA. Translation: CAH69995.1 .
    CH471066 Genomic DNA. Translation: EAW50107.1 .
    BC012625 mRNA. Translation: AAH12625.1 .
    CCDSi CCDS7416.1.
    RefSeqi NP_005389.1. NM_005398.5.
    UniGenei Hs.303090.
    Hs.744999.

    3D structure databases

    ProteinModelPortali Q9UQK1.
    SMRi Q9UQK1. Positions 134-262.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111500. 8 interactions.
    IntActi Q9UQK1. 3 interactions.
    MINTi MINT-6783827.
    STRINGi 9606.ENSP00000238994.

    Protein family/group databases

    CAZyi CBM21. Carbohydrate-Binding Module Family 21.

    PTM databases

    PhosphoSitei Q9UQK1.

    Polymorphism databases

    DMDMi 146325084.

    Proteomic databases

    PaxDbi Q9UQK1.
    PRIDEi Q9UQK1.

    Protocols and materials databases

    DNASUi 5507.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000238994 ; ENSP00000238994 ; ENSG00000119938 .
    GeneIDi 5507.
    KEGGi hsa:5507.
    UCSCi uc001kho.3. human.

    Organism-specific databases

    CTDi 5507.
    GeneCardsi GC10M093378.
    HGNCi HGNC:9293. PPP1R3C.
    HPAi HPA027041.
    MIMi 602999. gene.
    neXtProti NX_Q9UQK1.
    PharmGKBi PA33653.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG288354.
    HOGENOMi HOG000026799.
    HOVERGENi HBG052744.
    InParanoidi Q9UQK1.
    KOi K07189.
    OMAi IVHVQWK.
    OrthoDBi EOG7H4DTW.
    PhylomeDBi Q9UQK1.
    TreeFami TF105537.

    Enzyme and pathway databases

    Reactomei REACT_169208. Glycogen synthesis.
    REACT_200783. Myoclonic epilepsy of Lafora.

    Miscellaneous databases

    GeneWikii PPP1R3C.
    GenomeRNAii 5507.
    NextBioi 21304.
    PROi Q9UQK1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UQK1.
    Bgeei Q9UQK1.
    CleanExi HS_PPP1R3C.
    Genevestigatori Q9UQK1.

    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. "Amino acid sequence of a novel protein phosphatase 1 binding protein (R5) which is related to the liver- and muscle-specific glycogen binding subunits of protein phosphatase 1."
      Doherty M.J., Young P.R., Cohen P.T.W.
      FEBS Lett. 399:339-343(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PPP1CC.
      Tissue: Gall bladder1 Publication.
    2. "Protein targeting to glycogen/PPP1R5: screening of coding and flanking genomic regions for polymorphisms and association analysis with insulin action in Pima Indians."
      Permana P.A., Luczy-Bachman G., Bogardus C.
      Biochem. Biophys. Res. Commun. 258:184-186(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Retina.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Skeletal muscleImported.
    8. "Laforin, the dual-phosphatase responsible for Lafora disease, interacts with R5 (PTG), a regulatory subunit of protein phosphatase-1 that enhances glycogen accumulation."
      Fernandez-Sanchez M.E., Criado-Garcia O., Heath K.E., Garcia-Fojeda B., Medrano-Fernandez I., Gomez-Garre P., Sanz P., Serratosa J.M., Rodriguez de Cordoba S.
      Hum. Mol. Genet. 12:3161-3171(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPM2A, MUTAGENESIS OF VAL-85; PHE-87; ASP-247 AND ASP-250.
    9. "Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG)."
      Worby C.A., Gentry M.S., Dixon J.E.
      J. Biol. Chem. 283:4069-4076(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH EPM2A.
    10. Cited for: VARIANT SER-249.

    Entry informationi

    Entry nameiPPR3C_HUMAN
    AccessioniPrimary (citable) accession number: Q9UQK1
    Secondary accession number(s): B2R7X0, O95686
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3