UniProt ID | PTPA_MOUSE | |
---|---|---|
UniProt AC | P58389 | |
Protein Name | Serine/threonine-protein phosphatase 2A activator | |
Gene Name | Ptpa | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 323 | |
Subcellular Localization | Cytoplasm. Nucleus. | |
Protein Description | PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A (By similarity).. | |
Protein Sequence | MAEGERQPPPDSSEETPPTTQNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFDYKVSEAIEKLVALLDTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDQEAENLVATVVPTHLAAAVPEVAVYLKEAVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQVAIVFKVFDRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPHLEPRHFVDEKAVSENHKDYMFLQCILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIHPVTSG | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAEGERQPP ------CCCCCCCCC | 33.24 | - | |
12 | Phosphorylation | ERQPPPDSSEETPPT CCCCCCCCCCCCCCC | 45.48 | 25293948 | |
13 | Phosphorylation | RQPPPDSSEETPPTT CCCCCCCCCCCCCCC | 47.00 | 25293948 | |
16 | Phosphorylation | PPDSSEETPPTTQNF CCCCCCCCCCCCCCC | 30.43 | 25293948 | |
19 | Phosphorylation | SSEETPPTTQNFIIP CCCCCCCCCCCCEEE | 42.07 | 25293948 | |
20 | Phosphorylation | SEETPPTTQNFIIPK CCCCCCCCCCCEEEC | 27.56 | 25293948 | |
103 | Malonylation | QPSRFGNKAYRTWYA CCCCCCCHHHHHHHH | 47.37 | 26320211 | |
286 | Acetylation | SAVPSWSKVNQGLIR ECCCCHHHHCHHHHH | 38.66 | 23236377 | |
296 | Malonylation | QGLIRMYKAECLEKF HHHHHHHHHHHHHHC | 28.50 | 26320211 | |
296 | Acetylation | QGLIRMYKAECLEKF HHHHHHHHHHHHHHC | 28.50 | 22826441 | |
302 | Acetylation | YKAECLEKFPVIQHF HHHHHHHHCCEEEEE | 41.86 | 22826441 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of PTPA_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PTPA_MOUSE !! |
* 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 PTPA_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of PTPA_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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