| UniProt ID | PP1A_RABIT | |
|---|---|---|
| UniProt AC | P62139 | |
| Protein Name | Serine/threonine-protein phosphatase PP1-alpha catalytic subunit | |
| Gene Name | PPP1CA | |
| Organism | Oryctolagus cuniculus (Rabbit). | |
| Sequence Length | 330 | |
| Subcellular Localization | Cytoplasm. Nucleus. Nucleus, nucleoplasm. Nucleus, nucleolus. Primarily nuclear and largely excluded from the nucleolus. Highly mobile in cells and can be relocalized through interaction with targeting subunits. NOM1 plays a role in targeting this pr | |
| Protein Description | 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. 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. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development. 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). Dephosphorylates CENPA (By similarity). Dephosphorylates the 'Ser-139' residue of ATG16L1 causing dissociation of ATG12-ATG5-ATG16L1 complex, thereby inhibiting autophagy (By similarity).. | |
| Protein Sequence | MSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKNKGKYGQFSGLNPGGRPITPPRNSAKAKK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSDSEKLNL ------CCHHHHCCH | 50.25 | - | |
| 2 | Phosphorylation | ------MSDSEKLNL ------CCHHHHCCH | 50.25 | - | |
| 22 | Phosphorylation | RLLEVQGSRPGKNVQ HHHHHCCCCCCCCEE | 20.43 | - | |
| 305 | Acetylation | PADKNKGKYGQFSGL CCCCCCCCCCCCCCC | 48.06 | - | |
| 306 | Phosphorylation | ADKNKGKYGQFSGLN CCCCCCCCCCCCCCC | 25.48 | - | |
| 320 | Phosphorylation | NPGGRPITPPRNSAK CCCCCCCCCCCCCCC | 29.89 | - | |
| 325 | Phosphorylation | PITPPRNSAKAKK-- CCCCCCCCCCCCC-- | 32.21 | - |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PP1A_RABIT !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of PP1A_RABIT !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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