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 | ||
* 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 | ||||||
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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. |