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P63088

- PP1G_RAT

UniProt

P63088 - PP1G_RAT

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Protein

Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Gene

Ppp1cc

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II. 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.

Cofactori

Binds 2 manganese ions per subunit.

Enzyme regulationi

Inactivated by binding to URI1.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Manganese 1By similarity
Metal bindingi66 – 661Manganese 1By similarity
Metal bindingi92 – 921Manganese 1By similarity
Metal bindingi92 – 921Manganese 21 Publication
Metal bindingi124 – 1241Manganese 21 Publication
Active sitei125 – 1251Proton donorBy similarity
Metal bindingi173 – 1731Manganese 21 Publication
Metal bindingi248 – 2481Manganese 21 Publication

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphatase activity Source: UniProtKB
  3. poly(A) RNA binding Source: Ensembl
  4. protein serine/threonine phosphatase activity Source: UniProtKB

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. neuron differentiation Source: MGI
  7. protein dephosphorylation Source: UniProtKB
  8. regulation of circadian rhythm Source: UniProtKB
Complete GO annotation...

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_194781. Separation of Sister Chromatids.
REACT_198611. Resolution of Sister Chromatid Cohesion.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (EC:3.1.3.16)
Short name:
PP-1G
Alternative name(s):
Protein phosphatase 1C catalytic subunit
Gene namesi
Name:Ppp1cc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 12

Organism-specific databases

RGDi3377. Ppp1cc.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. Cleavage furrow By similarity. Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity. Chromosomecentromerekinetochore By similarity. Nucleus speckle By similarity. Midbody By similarity. Mitochondrion By similarity
Note: Rapidly exchanges between the nucleolar, nucleoplasmic and cytoplasmic compartments. Highly mobile in cells and can be relocalized through interaction with targeting subunits. In the presence of PPP1R8 relocalizes from the nucleolus to nuclear speckles. Shows a dynamic targeting to specific sites throughout the cell cycle. Highly concentrated in nucleoli of interphase cells and localizes at kinetochores early in mitosis. Relocalization to chromosome-containing regions occurs at the transition from early to late anaphase. Also accumulates at the cleavage furrow and midbody by telophase. Colocalizes with SPZ1 in the nucleus. Colocalizes with URI1 at mitochondrion (By similarity).By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. dendritic spine Source: RGD
  3. kinetochore Source: UniProtKB-KW
  4. mitochondrion Source: UniProtKB
  5. MLL5-L complex Source: Ensembl
  6. nucleolus Source: Ensembl
  7. PTW/PP1 phosphatase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Kinetochore, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 323322Serine/threonine-protein phosphatase PP1-gamma catalytic subunitPRO_0000058789Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei307 – 3071PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylated by NEK2.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP63088.
PRIDEiP63088.

PTM databases

PhosphoSiteiP63088.

Expressioni

Gene expression databases

ExpressionAtlasiP63088. baseline.
GenevestigatoriP63088.

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. PPP1R12A, PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A (in skeletal muscle), PPP1R3B (in sliver), 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 PPP1R3B, PPP1R7 and CDCA2. Isoform gamma-2 interacts with SPZ1. Interacts with IKFZ1; the interaction targets PPP1CC to pericentromeric heterochromatin, dephosphorylates IKAROS, stabilizes it and prevents it from degradation. Interacts with NOM1 and PPP1R8. Component of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with PPP1R8 (By similarity). Interacts with NEK2. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Grm1P2338515EBI-80049,EBI-4410410
Grm5P3142419EBI-80049,EBI-2902734
Grm7P354004EBI-80049,EBI-6936416
Grm7Q6333711EBI-80049,EBI-6935714
Ppp1r9aO358672EBI-80049,EBI-7092421
Ppp1r9bO352743EBI-80049,EBI-80022

Protein-protein interaction databases

IntActiP63088. 7 interactions.
MINTiMINT-4591365.

Structurei

Secondary structure

1
323
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 179Combined sources
Turni18 – 214Combined sources
Helixi32 – 4817Combined sources
Beta strandi51 – 555Combined sources
Beta strandi57 – 626Combined sources
Helixi69 – 7911Combined sources
Beta strandi87 – 893Combined sources
Beta strandi94 – 985Combined sources
Helixi100 – 11314Combined sources
Turni115 – 1173Combined sources
Beta strandi118 – 1203Combined sources
Helixi128 – 1314Combined sources
Helixi136 – 1438Combined sources
Helixi146 – 15611Combined sources
Beta strandi162 – 1654Combined sources
Turni166 – 1683Combined sources
Beta strandi169 – 1746Combined sources
Helixi183 – 1875Combined sources
Beta strandi197 – 1993Combined sources
Helixi200 – 2067Combined sources
Beta strandi214 – 2185Combined sources
Beta strandi222 – 2276Combined sources
Helixi229 – 23911Combined sources
Beta strandi242 – 2465Combined sources
Beta strandi253 – 2586Combined sources
Turni259 – 2624Combined sources
Beta strandi263 – 2675Combined sources
Helixi272 – 2743Combined sources
Beta strandi279 – 2857Combined sources
Beta strandi290 – 2967Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2O8AX-ray2.61A/B2-323[»]
2O8GX-ray2.50A/B2-323[»]
ProteinModelPortaliP63088.
SMRiP63088. Positions 6-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63088.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0639.
HOGENOMiHOG000172697.
HOVERGENiHBG000216.
InParanoidiP63088.
KOiK06269.
OMAiPRSMITK.
OrthoDBiEOG7TJ3K3.
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Gamma-1 (identifier: P63088-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADIDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP
60 70 80 90 100
ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS
110 120 130 140 150
LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK
160 170 180 190 200
TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL
210 220 230 240 250
LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV
260 270 280 290 300
VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE
310 320
KKKPNATRPV TPPRGMITKQ AKK
Length:323
Mass (Da):36,984
Last modified:September 13, 2004 - v1
Checksum:i4E28412C16898615
GO
Isoform Gamma-2 (identifier: P63088-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     315-323: GMITKQAKK → VGSGLNPSIQKASNYRNNTVLYE

Show »
Length:337
Mass (Da):38,504
Checksum:iE6F271155E0E67D7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform Gamma-2 (identifier: P63088-2)
Sequence conflicti214 – 2141L → F in BAA14197. (PubMed:2177460)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei315 – 3239GMITKQAKK → VGSGLNPSIQKASNYRNNTV LYE in isoform Gamma-2. 1 PublicationVSP_011566

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90165 mRNA. Translation: BAA14196.1.
D90166 mRNA. Translation: BAA14197.1.
PIRiI76572.
I76573.
RefSeqiNP_071943.1. NM_022498.2. [P63088-1]
UniGeneiRn.1495.
Rn.234216.

Genome annotation databases

EnsembliENSRNOT00000048851; ENSRNOP00000047912; ENSRNOG00000001269. [P63088-2]
GeneIDi24669.
KEGGirno:24669.
UCSCiRGD:3377. rat. [P63088-1]

Keywords - Coding sequence diversityi

Alternative splicing

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
D90165 mRNA. Translation: BAA14196.1 .
D90166 mRNA. Translation: BAA14197.1 .
PIRi I76572.
I76573.
RefSeqi NP_071943.1. NM_022498.2. [P63088-1 ]
UniGenei Rn.1495.
Rn.234216.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2O8A X-ray 2.61 A/B 2-323 [» ]
2O8G X-ray 2.50 A/B 2-323 [» ]
ProteinModelPortali P63088.
SMRi P63088. Positions 6-299.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P63088. 7 interactions.
MINTi MINT-4591365.

PTM databases

PhosphoSitei P63088.

Proteomic databases

PaxDbi P63088.
PRIDEi P63088.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000048851 ; ENSRNOP00000047912 ; ENSRNOG00000001269 . [P63088-2 ]
GeneIDi 24669.
KEGGi rno:24669.
UCSCi RGD:3377. rat. [P63088-1 ]

Organism-specific databases

CTDi 5501.
RGDi 3377. Ppp1cc.

Phylogenomic databases

eggNOGi COG0639.
HOGENOMi HOG000172697.
HOVERGENi HBG000216.
InParanoidi P63088.
KOi K06269.
OMAi PRSMITK.
OrthoDBi EOG7TJ3K3.
TreeFami TF354243.

Enzyme and pathway databases

Reactomei REACT_194641. Downregulation of TGF-beta receptor signaling.
REACT_194781. Separation of Sister Chromatids.
REACT_198611. Resolution of Sister Chromatid Cohesion.

Miscellaneous databases

EvolutionaryTracei P63088.
NextBioi 295513.
PROi P63088.

Gene expression databases

ExpressionAtlasi P63088. baseline.
Genevestigatori P63088.

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] (ISOFORMS GAMMA-1 AND GAMMA-2), ALTERNATIVE SPLICING.
  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. "Regulation of neurabin I interaction with protein phosphatase 1 by phosphorylation."
    McAvoy T., Allen P.B., Obaishi H., Nakanishi H., Takai Y., Greengard P., Nairn A.C., Hemmings H.C. Jr.
    Biochemistry 38:12943-12949(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 42-58 AND 212-234, INTERACTION WITH PPP1R9A.
    Strain: Sprague-Dawley.
  4. "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: INTERACTION WITH PPP1R3B.
  5. "Identification of the separate domains in the hepatic glycogen-targeting subunit of protein phosphatase 1 that interact with phosphorylase a, glycogen and protein phosphatase 1."
    Armstrong C.G., Doherty M.J., Cohen P.T.W.
    Biochem. J. 336:699-704(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R3B.
  6. "Brain actin-associated protein phosphatase 1 holoenzymes containing spinophilin, neurabin, and selected catalytic subunit isoforms."
    MacMillan L.B., Bass M.A., Cheng N., Howard E.F., Tamura M., Strack S., Wadzinski B.E., Colbran R.J.
    J. Biol. Chem. 274:35845-35854(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  7. "Structural basis for regulation of protein phosphatase 1 by inhibitor-2."
    Hurley T.D., Yang J., Zhang L., Goodwin K.D., Zou Q., Cortese M., Dunker A.K., DePaoli-Roach A.A.
    J. Biol. Chem. 282:28874-28883(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-323 IN COMPLEX WITH MANGANESE AND M.MUSCULUS INHIBITOR PPP1R2.

Entry informationi

Entry nameiPP1G_RAT
AccessioniPrimary (citable) accession number: P63088
Secondary accession number(s): O09186
, O09189, P37139, Q64679
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: October 29, 2014
This is version 109 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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