| UniProt ID | 2A5G_MOUSE | |
|---|---|---|
| UniProt AC | Q60996 | |
| Protein Name | Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform | |
| Gene Name | Ppp2r5c | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 524 | |
| Subcellular Localization | Nucleus. Chromosome, centromere. | |
| Protein Description | The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation (By similarity).. | |
| Protein Sequence | MLTCNKAGSGMVVDAASSNGPFQPVALLHIRDVPPADQEKLFIQKLRQCCVLFDFVSDPLSDLKWKEVKRAALSEMVEYITHNRNVITEPIYPEAVHMFAVNMFRTLPPSSNPTGAEFDPEEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFVLQLLELFDSEDPRERDFLKTTLHRIYGKFLGLRAYIRKQINNIFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKIFLLKVLLPLHKVKSLSVYHPQLAYCVVQFLEKDSTLTEPVVMALLKYWPKTHSPKEVMFLNELEEILDVIEPSEFVKIMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMSLISDNAAKILPIMFPSLYRNSKTHWNKTIHGLIYNALKLFMEMNQKLFDDCTQQFKAEKLKEKLKMKEREEAWVKIENLAKANPQYAVYSQASAVSIPVAMETDGPQFEDVQMLKKTVSDEARQAQKELKKDRPLVRRKSELPQDPHTEKALEAHCRASELLSQDGR | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MLTCNKAG -------CCCCCCCC | 6.71 | - | |
| 64 | Ubiquitination | SDPLSDLKWKEVKRA CCCHHHCCHHHHHHH | 62.30 | - | |
| 192 | Acetylation | TLHRIYGKFLGLRAY HHHHHHHHHHCHHHH | 22.05 | 22826441 | |
| 279 | Phosphorylation | VQFLEKDSTLTEPVV HHHHHCCCCCCHHHH | 36.06 | - | |
| 333 | Ubiquitination | PLFRQLAKCVSSPHF HHHHHHHHHHCCCCH | 43.70 | - | |
| 354 | Phosphorylation | LYYWNNEYIMSLISD HHHCCCHHHHHHHCC | 12.21 | - | |
| 357 | Phosphorylation | WNNEYIMSLISDNAA CCCHHHHHHHCCCHH | 17.00 | - | |
| 360 | Phosphorylation | EYIMSLISDNAAKIL HHHHHHHCCCHHHHH | 30.06 | - | |
| 373 | Phosphorylation | ILPIMFPSLYRNSKT HHHHCCHHHHHCCCC | 27.11 | 28285833 | |
| 375 | Phosphorylation | PIMFPSLYRNSKTHW HHCCHHHHHCCCCHH | 16.46 | 28285833 | |
| 385 | Phosphorylation | SKTHWNKTIHGLIYN CCCHHHHHHHHHHHH | 18.26 | 25521595 | |
| 497 | Phosphorylation | RPLVRRKSELPQDPH CCCCCCHHCCCCCCH | 42.42 | 26824392 | |
| 520 | Phosphorylation | CRASELLSQDGR--- HHHHHHHCCCCC--- | 38.56 | 30635358 |
| 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 2A5G_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of 2A5G_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 2A5G_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| 2AAA_HUMAN | PPP2R1A | physical | 26496610 | |
| 2AAB_HUMAN | PPP2R1B | physical | 26496610 | |
| U2AF2_HUMAN | U2AF2 | physical | 26496610 | |
| ADNP2_HUMAN | ADNP2 | physical | 26496610 | |
| ELL2_HUMAN | ELL2 | physical | 26496610 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND MASSSPECTROMETRY. | |