| UniProt ID | PDE8A_MOUSE | |
|---|---|---|
| UniProt AC | O88502 | |
| Protein Name | High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A | |
| Gene Name | Pde8a | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 823 | |
| Subcellular Localization | ||
| Protein Description | Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in maintaining basal levels of the cyclic nucleotide and/or in the cAMP regulation of germ cell development. Binding to RAF1 reduces RAF1 'Ser-259' inhibitory-phosphorylation and stimulates RAF1-dependent EGF-activated ERK-signaling. Protects against cell death induced by hydrogen peroxide and staurosporine.. | |
| Protein Sequence | MGCAPSIHTSENRTFSHSDGEDEDVDVDVPGPAPRSIQRWSTAPGLVEPQPRDNGASKVSVADVQFGPMRFHQDQLQVLLVFTKEDSQCNGFHRACEKAGFKCTVTKEVQTVLTCFQDKLHDIIIIDHRYPRQMDAETLCRSIRSSKFSENTVIVGVVRRVDKEESSLMPFLAAGFTRRFIENPNVMACYNELLQLACGEVRSQLKLRACNSVFTALEKSQEAIEITSEDHIIQYANPAFESTMGYQSGELIGKELAQVPINEKKGDLLDAINSCVTVDKEWQGVYHTQKKNGDNIQQNVKIIPVIGQGGKIRHYVSIIRVCNGNNKVETTTECVQTDSQTDNQAGKHKDRRKHSMDAKAVSSRTSDVSSQRRHSSLARIHSMMIEAPITKVINIINAAQENSPVPVTEALNRVLDILRTTELYSPQFNAQDDPHATDLVGGLMSDGLRRFSGNEYILATKNLPPLSNNLATPVSLHDVPPRIALAIENEEQWDFDIFELEVATQNRPLIYLGLKTFARFGMCEFLQCSETTLRSWFQMIESNYHSSNPYHNSTHAADVLHATAYFLSRDKIKETLDRIDEVAALIAATVHDVDHPGRTNSFLCNAGNQLAVLYNDTAVLESHHVALAFQLTLENDQCNIFKQMERNDYRTLRQSIIDMVLATEMTKHFEHVNKFINSINKPLTAQESEEPDRSLEDIKAMLKTPESRALIKRMMIKCADVSNPCRPLEHCIEWAARISEEYFSQTDEEKQLDLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFVDLPNLMQHLDDNFRYWKGLDEKKLRSLRPPPE | |
| 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 |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MGCAPSIHTSENR --CCCCCCCCCCCCC | 14.42 | 25338131 | |
| 14 | Phosphorylation | IHTSENRTFSHSDGE CCCCCCCEECCCCCC | 40.86 | 28833060 | |
| 16 | Phosphorylation | TSENRTFSHSDGEDE CCCCCEECCCCCCCC | 22.82 | 25521595 | |
| 18 | Phosphorylation | ENRTFSHSDGEDEDV CCCEECCCCCCCCCC | 46.22 | 25521595 | |
| 36 | Phosphorylation | VPGPAPRSIQRWSTA CCCCCCCCCCCCCCC | 23.24 | 24719451 | |
| 41 | Phosphorylation | PRSIQRWSTAPGLVE CCCCCCCCCCCCCCC | 19.51 | 27180971 | |
| 42 | Phosphorylation | RSIQRWSTAPGLVEP CCCCCCCCCCCCCCC | 29.88 | 26160508 | |
| 215 | Phosphorylation | RACNSVFTALEKSQE HHHHHHHHHHHHCHH | 28.33 | 22807455 | |
| 264 | Ubiquitination | AQVPINEKKGDLLDA HCCCCCCCCCCHHHH | 58.53 | 27667366 | |
| 311 | Ubiquitination | PVIGQGGKIRHYVSI EEECCCCCEEEEEEE | 43.31 | - | |
| 355 | Phosphorylation | HKDRRKHSMDAKAVS CCHHHHHHHCHHHHH | 22.76 | 19367708 | |
| 369 | Phosphorylation | SSRTSDVSSQRRHSS HHCCCCHHHHHHHHH | 26.24 | 27841257 | |
| 375 | Phosphorylation | VSSQRRHSSLARIHS HHHHHHHHHHHHHHH | 25.82 | 22324799 | |
| 376 | Phosphorylation | SSQRRHSSLARIHSM HHHHHHHHHHHHHHH | 21.66 | 22324799 | |
| 382 | Phosphorylation | SSLARIHSMMIEAPI HHHHHHHHHHCCCCH | 14.00 | 27180971 | |
| 403 | Phosphorylation | INAAQENSPVPVTEA HHHHHHCCCCCHHHH | 26.90 | 25293948 | |
| 420 | Phosphorylation | RVLDILRTTELYSPQ HHHHHHHHCCCCCCC | 22.60 | 25293948 | |
| 421 | Phosphorylation | VLDILRTTELYSPQF HHHHHHHCCCCCCCC | 19.98 | 25293948 | |
| 424 | Phosphorylation | ILRTTELYSPQFNAQ HHHHCCCCCCCCCCC | 16.45 | 25293948 | |
| 425 | Phosphorylation | LRTTELYSPQFNAQD HHHCCCCCCCCCCCC | 25.50 | 25293948 | |
| 452 | Phosphorylation | SDGLRRFSGNEYILA CCCCHHCCCCCEEEE | 38.61 | 25521595 | |
| 456 | Phosphorylation | RRFSGNEYILATKNL HHCCCCCEEEEECCC | 12.77 | 25159016 | |
| 460 | Phosphorylation | GNEYILATKNLPPLS CCCEEEEECCCCCCC | 19.61 | 25159016 | |
| 694 | Phosphorylation | ESEEPDRSLEDIKAM CCCCCCCCHHHHHHH | 43.41 | 19060867 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 355 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 355 | S | Phosphorylation |
| - |
* 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 PDE8A_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of PDE8A_MOUSE !! | ||||
| 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-452, AND MASSSPECTROMETRY. | |