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Protein

Protein phosphatase 1 regulatory subunit 3C

Gene

PPP1R3C

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 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. pathogenesis Source: Reactome
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9UQK1.
CleanExiHS_PPP1R3C.
ExpressionAtlasiQ9UQK1. baseline and differential.
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. 18 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.
GeneTreeiENSGT00530000062978.
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

        10         20         30         40         50
MSCTRMIQVL DPRPLTSSVM PVDVAMRLCL AHSPPVKSFL GPYDEFQRRH
60 70 80 90 100
FVNKLKPLKS CLNIKHKAKS QNDWKCSHNQ AKKRVVFADS KGLSLTAIHV
110 120 130 140 150
FSDLPEEPAW DLQFDLLDLN DISSALKHHE EKNLILDFPQ PSTDYLSFRS
160 170 180 190 200
HFQKNFVCLE NCSLQERTVT GTVKVKNVSF EKKVQIRITF DSWKNYTDVD
210 220 230 240 250
CVYMKNVYGG TDSDTFSFAI DLPPVIPTEQ KIEFCISYHA NGQVFWDNND
260 270 280 290 300
GQNYRIVHVQ WKPDGVQTQM APQDCAFHQT SPKTELESTI FGSPRLASGL
310
FPEWQSWGRM ENLASYR
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9UQK1.
SMRiQ9UQK1. Positions 134-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111500. 18 interactions.
IntActiQ9UQK1. 3 interactions.
MINTiMINT-6783827.
STRINGi9606.ENSP00000238994.

Protein family/group databases

CAZyiCBM21. Carbohydrate-Binding Module Family 21.

PTM databases

PhosphoSiteiQ9UQK1.

Polymorphism databases

DMDMi146325084.

Proteomic databases

PaxDbiQ9UQK1.
PRIDEiQ9UQK1.

Protocols and materials databases

DNASUi5507.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5507.
GeneCardsiGC10M093378.
HGNCiHGNC:9293. PPP1R3C.
HPAiHPA027041.
MIMi602999. gene.
neXtProtiNX_Q9UQK1.
PharmGKBiPA33653.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG288354.
GeneTreeiENSGT00530000062978.
HOGENOMiHOG000026799.
HOVERGENiHBG052744.
InParanoidiQ9UQK1.
KOiK07189.
OMAiIVHVQWK.
OrthoDBiEOG7H4DTW.
PhylomeDBiQ9UQK1.
TreeFamiTF105537.

Enzyme and pathway databases

ReactomeiREACT_169208. Glycogen synthesis.
REACT_200783. Myoclonic epilepsy of Lafora.

Miscellaneous databases

ChiTaRSiPPP1R3C. human.
GeneWikiiPPP1R3C.
GenomeRNAii5507.
NextBioi21304.
PROiQ9UQK1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UQK1.
CleanExiHS_PPP1R3C.
ExpressionAtlasiQ9UQK1. baseline and differential.
GenevestigatoriQ9UQK1.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 92 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.