Q8MJ46 (PP1G_CANFA) Reviewed, UniProtKB/Swiss-Prot
Last modified June 11, 2014. Version 77. History...
Names and origin
|Protein names||Recommended name:|
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
Protein phosphatase 1C catalytic subunit
|Organism||Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]|
|Taxonomic identifier||9615 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›|
|Sequence length||323 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at transcript level|
General annotation (Comments)
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 By similarity.
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.
Binds 2 manganese ions per subunit By similarity.
Inactivated by binding to URI1 By similarity.
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 liver), 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. 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. Interacts with NEK2. Interacts with PPP1R42; the interaction is direct. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner By similarity.
Cytoplasm By similarity. Nucleus By similarity. Cleavage furrow By similarity. Nucleus › nucleolus By similarity. Nucleus › nucleoplasm By similarity. Chromosome › centromere › kinetochore 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.
Phosphorylated by NEK2 By similarity.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Initiator methionine||1||1||Removed By similarity|
|Chain||2 – 323||322||Serine/threonine-protein phosphatase PP1-gamma catalytic subunit||PRO_0000058786|
|Active site||125||1||Proton donor By similarity|
|Metal binding||64||1||Manganese 1 By similarity|
|Metal binding||66||1||Manganese 1 By similarity|
|Metal binding||92||1||Manganese 1 By similarity|
|Metal binding||92||1||Manganese 2 By similarity|
|Metal binding||124||1||Manganese 2 By similarity|
|Metal binding||173||1||Manganese 2 By similarity|
|Metal binding||248||1||Manganese 2 By similarity|
Amino acid modifications
|Modified residue||2||1||N-acetylalanine By similarity|
|Modified residue||307||1||Phosphothreonine By similarity|
|Protein Spotlight |
The things we forget - Issue 32 of March 2003
|AF525130 mRNA. Translation: AAM88379.1.|
|RefSeq||NP_001003033.1. NM_001003033.1. |
3D structure databases
|SMR||Q8MJ46. Positions 6-300. |
Protein-protein interaction databases
Protocols and materials databases
Genome annotation databases
Family and domain databases
|Gene3D||22.214.171.124. 1 hit. |
|InterPro||IPR004843. Calcineurin-like_PHP_apaH. |
|Pfam||PF00149. Metallophos. 1 hit. |
|PRINTS||PR00114. STPHPHTASE. |
|SMART||SM00156. PP2Ac. 1 hit. |
|SUPFAM||SSF56300. SSF56300. 1 hit. |
|PROSITE||PS00125. SER_THR_PHOSPHATASE. 1 hit. |
|Accession||Primary (citable) accession number: Q8MJ46|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|