KAP3_MOUSE - dbPTM
KAP3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSIEIPAGL
------CCCCCCCCH
29.0020415495
71PhosphorylationAAGGGIPSKGVNFAE
HCCCCCCCCCCCCCC
39.8725338131
83PhosphorylationFAEEPMRSDSENGEE
CCCCCCCCCCCCCCH
38.9625521595
85PhosphorylationEEPMRSDSENGEEEE
CCCCCCCCCCCCHHH
33.9225521595
112PhosphorylationNRFTRRASVCAEAYN
HHHHHHHHCHHHHHC
18.8724925903
118PhosphorylationASVCAEAYNPDEEED
HHCHHHHHCCCCCCC
20.8025521595
129PhosphorylationEEEDDAESRIIHPKT
CCCCCHHHCCCCCCC
30.4225619855
174UbiquitinationAMFEKLVKEGEHVID
HHHHHHHHCCCCEEC
71.1322790023
200PhosphorylationDRGTFDIYVKCDGVG
ECCEEEEEEEECCCC
8.83-
256AcetylationTFRRIIVKNNAKKRK
EEEEEHHCCCHHHHH
33.79-
256UbiquitinationTFRRIIVKNNAKKRK
EEEEEHHCCCHHHHH
33.7927667366
265PhosphorylationNAKKRKMYESFIESL
CHHHHHHHHHHHHHC
16.0829899451
267PhosphorylationKKRKMYESFIESLPF
HHHHHHHHHHHHCHH
17.6527180971
281PhosphorylationFLKSLEVSERLKVVD
HHHHCCHHHCCEEEE
13.9728059163
357UbiquitinationELALVTNKPRAASAH
EEEEEECCCCCCHHH
26.8927667366
362PhosphorylationTNKPRAASAHAIGTV
ECCCCCCHHHHHHHH
21.4323684622
368PhosphorylationASAHAIGTVKCLAMD
CHHHHHHHHHHHHCC
15.6425338131
396PhosphorylationIMKRNIATYEEQLVA
HHHHHHCCHHHHHHH
27.8929895711
397PhosphorylationMKRNIATYEEQLVAL
HHHHHCCHHHHHHHH
14.4029895711

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KAP3_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAPCA_HUMANPRKACAphysical
26496610
KAPCB_HUMANPRKACBphysical
26496610
KAP2_HUMANPRKAR2Aphysical
26496610
MYOME_HUMANPDE4DIPphysical
26496610
AKAP9_HUMANAKAP9physical
26496610
CK5P2_HUMANCDK5RAP2physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KAP3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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