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P63088 (PP1G_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit

Short name=PP-1G
EC=3.1.3.16
Alternative name(s):
Protein phosphatase 1C catalytic subunit
Gene names
Name:Ppp1cc
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 2 manganese ions per subunit.

Enzyme regulation

Inactivated by binding to URI1 By similarity.

Subunit structure

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-2interacts 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. Ref.3 Ref.4 Ref.5 Ref.6

Subcellular location

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.

Post-translational modification

Phosphorylated by NEK2 By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processBiological rhythms
Carbohydrate metabolism
Cell cycle
Cell division
Glycogen metabolism
   Cellular componentCentromere
Chromosome
Cytoplasm
Kinetochore
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
   LigandManganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

circadian regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

entrainment of circadian clock by photoperiod

Inferred from sequence or structural similarity. Source: UniProtKB

glycogen metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

neuron differentiation

Inferred from direct assay PubMed 17202132. Source: MGI

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentPTW/PP1 phosphatase complex

Inferred from sequence or structural similarity. Source: UniProtKB

cleavage furrow

Inferred from electronic annotation. Source: UniProtKB-SubCell

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

dendritic spine

Inferred from direct assay PubMed 7724573. Source: RGD

midbody

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 11588169. Source: UniProtKB

protein serine/threonine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Gamma-1 (identifier: P63088-1)

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.
Isoform Gamma-2 (identifier: P63088-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 323322Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
PRO_0000058789

Sites

Active site1251Proton donor By similarity
Metal binding641Manganese 1 By similarity
Metal binding661Manganese 1 By similarity
Metal binding921Manganese 1 By similarity
Metal binding921Manganese 2
Metal binding1241Manganese 2
Metal binding1731Manganese 2
Metal binding2481Manganese 2

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3071Phosphothreonine By similarity

Natural variations

Alternative sequence315 – 3239GMITKQAKK → VGSGLNPSIQKASNYRNNTV LYE in isoform Gamma-2.
VSP_011566

Experimental info

Isoform Gamma-2:
Sequence conflict2141L → F in BAA14197. Ref.1

Secondary structure

...................................................... 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Gamma-1 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 4E28412C16898615

FASTA32336,984
        10         20         30         40         50         60 
MADIDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK 

        70         80         90        100        110        120 
ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL 

       130        140        150        160        170        180 
LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL 

       190        200        210        220        230        240 
QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD 

       250        260        270        280        290        300 
LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE 

       310        320 
KKKPNATRPV TPPRGMITKQ AKK 

« Hide

Isoform Gamma-2 [UniParc].

Checksum: E6F271155E0E67D7
Show »

FASTA33738,504

References

[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.
+Additional computationally mapped references.

Web resources

Protein Spotlight

The things we forget - Issue 32 of March 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90165 mRNA. Translation: BAA14196.1.
D90166 mRNA. Translation: BAA14197.1.
PIRI76572.
I76573.
RefSeqNP_071943.1. NM_022498.2. [P63088-1]
UniGeneRn.1495.
Rn.234216.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2O8AX-ray2.61A/B2-323[»]
2O8GX-ray2.50A/B2-323[»]
ProteinModelPortalP63088.
SMRP63088. Positions 6-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP63088. 7 interactions.
MINTMINT-4591365.

PTM databases

PhosphoSiteP63088.

Proteomic databases

PaxDbP63088.
PRIDEP63088.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000048851; ENSRNOP00000047912; ENSRNOG00000001269. [P63088-2]
GeneID24669.
KEGGrno:24669.
UCSCRGD:3377. rat. [P63088-1]

Organism-specific databases

CTD5501.
RGD3377. Ppp1cc.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172697.
HOVERGENHBG000216.
KOK06269.
OMAPRSMITK.
OrthoDBEOG7TJ3K3.
TreeFamTF354243.

Enzyme and pathway databases

ReactomeREACT_205051. Metabolism.

Gene expression databases

GenevestigatorP63088.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP63088.
NextBio295513.
PROP63088.

Entry information

Entry namePP1G_RAT
AccessionPrimary (citable) accession number: P63088
Secondary accession number(s): O09186 expand/collapse secondary AC list , O09189, P37139, Q64679
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: July 9, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references