InnateDB: Systems Biology of the Innate Immune Response

Mus musculus Protein: Ppp1cc

Summary

InnateDB Protein

IDBP-197972.6

Last Modified

2014-10-13 [Report errors or provide feedback]

Gene Symbol

Ppp1cc

Protein Name

protein phosphatase 1, catalytic subunit, gamma isoform

Synonyms

dis2m1; PP-1G; PP1;

Species

Mus musculus

Ensembl Protein

ENSMUSP00000083474

InnateDB Gene

IDBG-197968 (Ppp1cc)

Protein Structure

UniProt Annotation

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 Ca(2+)/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. {ECO:0000269PubMed:21712997, ECO:0000269PubMed:21930935}.

Subcellular Localization

Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cleavage furrow {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Nucleus speckle {ECO:0000250}. Midbody {ECO:0000250}. Mitochondrion {ECO:0000250}. 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). {ECO:0000250}.

Disease Associations

Tissue Specificity

Comments

Interactions

Number of Interactions

This gene and/or its encoded proteins are associated with 42 experimentally validated interaction(s) in this database.
They are also associated with 173 interaction(s) predicted by orthology.

Experimentally validated
Total	42 [view]
Protein-Protein	42 [view]
Protein-DNA	0
Protein-RNA	0
DNA-DNA	0
RNA-RNA	0
DNA-RNA	0

Predicted by orthology
Total	173 [view]

Gene Ontology

Molecular Function

Accession	GO Term
GO:0004722	protein serine/threonine phosphatase activity
GO:0005515	protein binding
GO:0016787	hydrolase activity
GO:0016791	phosphatase activity
GO:0019901	protein kinase binding
GO:0046872	metal ion binding

Biological Process

GO:0005977	glycogen metabolic process
GO:0006470	protein dephosphorylation
GO:0007049	cell cycle
GO:0032922	circadian regulation of gene expression
GO:0042752	regulation of circadian rhythm
GO:0043153	entrainment of circadian clock by photoperiod
GO:0051301	cell division

Cellular Component

GO:0000777	condensed chromosome kinetochore
GO:0005730	nucleolus
GO:0005739	mitochondrion
GO:0016607	nuclear speck
GO:0030496	midbody
GO:0032154	cleavage furrow
GO:0070688	MLL5-L complex
GO:0072357	PTW/PP1 phosphatase complex

Protein Structure and Domains

PDB ID

MGI:104872

InterPro

IPR004843 Calcineurin-like phosphoesterase domain, apaH type
IPR006186 Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase
IPR029052 Metallo-dependent phosphatase-like

PFAM

PF00149

PRINTS

PR00114

PIRSF

SMART

SM00156

TIGRFAMs

Post-translational Modifications

Modification

Cross-References

SwissProt