UniProt ID | KAP3_MOUSE | |
---|---|---|
UniProt AC | P31324 | |
Protein Name | cAMP-dependent protein kinase type II-beta regulatory subunit | |
Gene Name | Prkar2b | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 416 | |
Subcellular Localization | Cytoplasm. Cell membrane. Colocalizes with PJA2 in the cytoplasm and at the cell membrane.. | |
Protein Description | Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells. Type II regulatory chains mediate membrane association by binding to anchoring proteins, including the MAP2 kinase.. | |
Protein Sequence | MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGAARFGHEGRTWGDAGAAAGGGIPSKGVNFAEEPMRSDSENGEEEEAAEAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKEGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEVSERLKVVDVIGTKVYNDGEQIIAQGDLADSFFIVESGEVKITMKRKGKSEVEENGAVEIARCFRGQYFGELALVTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVALFGTNMDIVEPTA | |
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 | Phosphorylation | ------MSIEIPAGL ------CCCCCCCCH | 29.00 | 20415495 | |
71 | Phosphorylation | AAGGGIPSKGVNFAE HCCCCCCCCCCCCCC | 39.87 | 25338131 | |
83 | Phosphorylation | FAEEPMRSDSENGEE CCCCCCCCCCCCCCH | 38.96 | 25521595 | |
85 | Phosphorylation | EEPMRSDSENGEEEE CCCCCCCCCCCCHHH | 33.92 | 25521595 | |
112 | Phosphorylation | NRFTRRASVCAEAYN HHHHHHHHCHHHHHC | 18.87 | 24925903 | |
118 | Phosphorylation | ASVCAEAYNPDEEED HHCHHHHHCCCCCCC | 20.80 | 25521595 | |
129 | Phosphorylation | EEEDDAESRIIHPKT CCCCCHHHCCCCCCC | 30.42 | 25619855 | |
174 | Ubiquitination | AMFEKLVKEGEHVID HHHHHHHHCCCCEEC | 71.13 | 22790023 | |
200 | Phosphorylation | DRGTFDIYVKCDGVG ECCEEEEEEEECCCC | 8.83 | - | |
256 | Acetylation | TFRRIIVKNNAKKRK EEEEEHHCCCHHHHH | 33.79 | - | |
256 | Ubiquitination | TFRRIIVKNNAKKRK EEEEEHHCCCHHHHH | 33.79 | 27667366 | |
265 | Phosphorylation | NAKKRKMYESFIESL CHHHHHHHHHHHHHC | 16.08 | 29899451 | |
267 | Phosphorylation | KKRKMYESFIESLPF HHHHHHHHHHHHCHH | 17.65 | 27180971 | |
281 | Phosphorylation | FLKSLEVSERLKVVD HHHHCCHHHCCEEEE | 13.97 | 28059163 | |
357 | Ubiquitination | ELALVTNKPRAASAH EEEEEECCCCCCHHH | 26.89 | 27667366 | |
362 | Phosphorylation | TNKPRAASAHAIGTV ECCCCCCHHHHHHHH | 21.43 | 23684622 | |
368 | Phosphorylation | ASAHAIGTVKCLAMD CHHHHHHHHHHHHCC | 15.64 | 25338131 | |
396 | Phosphorylation | IMKRNIATYEEQLVA HHHHHHCCHHHHHHH | 27.89 | 29895711 | |
397 | Phosphorylation | MKRNIATYEEQLVAL HHHHHCCHHHHHHHH | 14.40 | 29895711 |
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 KAP3_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KAP3_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 KAP3_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
KAPCA_HUMAN | PRKACA | physical | 26496610 | |
KAPCB_HUMAN | PRKACB | physical | 26496610 | |
KAP2_HUMAN | PRKAR2A | physical | 26496610 | |
MYOME_HUMAN | PDE4DIP | physical | 26496610 | |
AKAP9_HUMAN | AKAP9 | physical | 26496610 | |
CK5P2_HUMAN | CDK5RAP2 | physical | 26496610 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY. | |
"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-112, AND MASSSPECTROMETRY. | |
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY. | |
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY. | |
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASSSPECTROMETRY. |