| UniProt ID | PDE4A_RAT | |
|---|---|---|
| UniProt AC | P54748 | |
| Protein Name | cAMP-specific 3',5'-cyclic phosphodiesterase 4A | |
| Gene Name | Pde4a | |
| Organism | Rattus norvegicus (Rat). | |
| Sequence Length | 844 | |
| Subcellular Localization | Cytoplasm, perinuclear region. | |
| Protein Description | Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes.. | |
| Protein Sequence | MEPPAAPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPIRIQQRGYPDSAERSETERSPHRPIERADAVDTGDRPGLRTTRMSWPSSFHGTGTGGGSSRRLEAENGPTPSPGRSPLDSQASPGLVLHAGATTSQRRESFLYRSDSDYDMSPKAVSRSSSVASEAHAEDLIVTPFAQVLASLRSVRSNFSLLTNVPIPSNKRSPLGGPPSVCKATLSEETCQQLARETLEELDWCLEQLETMQTYRSVSEMASHKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNEVEIPSPTPRQRAFQQPPPSVLRQSQPMSQITGLKKLVHTGSLNTNVPRFGVKTDQEDLLAQELENLSKWGLNIFCVSEYAGGRSLSCIMYTIFQERDLLKKFHIPVDTMMMYMLTLEDHYHADVAYHNSLHAADVLQSTHVLLATPALDAVFTDLEILAALFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEENCDIFQNLSKRQRQSLRKMVIDMVLATDMSKHMTLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLRNMVHCADLSNPTKPLELYRQWTDRIMAEFFQQGDRERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNRDWYHSAIRQSPSPPLEEEPGGLGHPSLPDKFQFELTLEEEEEEDSLEVPGLPTTEETFLAAEDARAQAVDWSKVKGPSTTVVEVAERLKQETASAYGAPQESMEAVGCSFSPGTPILPDVRTLSSSEEAPGLLGLPSTAAEVEAPRDHLAATRACSACSGTSGDNSAIISAPGRWGSGGDPA | |
| 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 |
|---|---|---|---|---|---|
| 11 | Phosphorylation | PAAPSERSLSLSLPG CCCCCCCCCCCCCCC | 20.47 | 27097102 | |
| 13 | Phosphorylation | APSERSLSLSLPGPR CCCCCCCCCCCCCCC | 19.70 | 23984901 | |
| 15 | Phosphorylation | SERSLSLSLPGPREG CCCCCCCCCCCCCCC | 29.19 | 23984901 | |
| 140 | Phosphorylation | TTSQRRESFLYRSDS CCHHHHHHHHCCCCC | 20.81 | 27097102 | |
| 145 | Phosphorylation | RESFLYRSDSDYDMS HHHHHCCCCCCCCCC | 28.10 | 22673903 | |
| 147 | Phosphorylation | SFLYRSDSDYDMSPK HHHCCCCCCCCCCHH | 39.04 | 25403869 | |
| 149 | Phosphorylation | LYRSDSDYDMSPKAV HCCCCCCCCCCHHHC | 19.93 | 22673903 | |
| 152 | Phosphorylation | SDSDYDMSPKAVSRS CCCCCCCCHHHCCCC | 21.98 | 25403869 | |
| 160 | Phosphorylation | PKAVSRSSSVASEAH HHHCCCCHHHHCHHH | 27.93 | - | |
| 204 | Phosphorylation | PIPSNKRSPLGGPPS CCCCCCCCCCCCCCC | 26.53 | - | |
| 274 | Phosphorylation | HLSEMSRSGNQVSEY HHHHHHCCCCHHHHH | 34.49 | 25575281 | |
| 279 | Phosphorylation | SRSGNQVSEYISNTF HCCCCHHHHHHHHHH | 18.21 | 16641100 | |
| 281 | Phosphorylation | SGNQVSEYISNTFLD CCCHHHHHHHHHHHC | 11.35 | 16641100 | |
| 297 | Phosphorylation | QNEVEIPSPTPRQRA CCCCCCCCCCHHHHH | 47.25 | 23800682 | |
| 333 | Phosphorylation | KKLVHTGSLNTNVPR HHHHHCCCCCCCCCC | 21.43 | 25403869 | |
| 530 | Phosphorylation | VIDMVLATDMSKHMT HHHHHHHCCHHHHHH | 28.24 | 22673903 | |
| 533 | Phosphorylation | MVLATDMSKHMTLLA HHHHCCHHHHHHHHH | 23.40 | 22673903 | |
| 672 | Phosphorylation | YHSAIRQSPSPPLEE HHHHHHCCCCCCCCC | 19.93 | 27097102 | |
| 674 | Phosphorylation | SAIRQSPSPPLEEEP HHHHCCCCCCCCCCC | 44.38 | 27097102 | |
| 688 | Phosphorylation | PGGLGHPSLPDKFQF CCCCCCCCCCCCEEE | 47.03 | 27097102 | |
| 788 | Phosphorylation | DVRTLSSSEEAPGLL CCCCCCCCCCCCCCC | 35.76 | 22108457 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PDE4A_RAT !! | ||||||
* 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 PDE4A_RAT !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Phosphorylation of cAMP-specific PDE4A5 (phosphodiesterase-4A5) byMK2 (MAPKAPK2) attenuates its activation through protein kinase Aphosphorylation."; MacKenzie K.F., Wallace D.A., Hill E.V., Anthony D.F., Henderson D.J.,Houslay D.M., Arthur J.S., Baillie G.S., Houslay M.D.; Biochem. J. 435:755-769(2011). Cited for: PHOSPHORYLATION AT SER-147, AND MUTAGENESIS OF SER-147 AND SER-161. | |