KAPCB_MOUSE - dbPTM
KAPCB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAPCB_MOUSE
UniProt AC P68181
Protein Name cAMP-dependent protein kinase catalytic subunit beta
Gene Name Prkacb
Organism Mus musculus (Mouse).
Sequence Length 351
Subcellular Localization Cytoplasm. Cell membrane. Membrane
Lipid-anchor . Nucleus. Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm..
Protein Description Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassembly, as well as regulation of intracellular transport mechanisms and ion flux. [PubMed: 9368018 Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates GPKOW which regulates its ability to bind RNA (By similarity]
Protein Sequence MGNTAIAKKGSEVESVKEFLAKAKEDFLRKWENPPPSNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVEFPFLVRLEYSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFRGSGDTSNFDDYEEEEIRVSITEKCGKEFCEF
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
2N-myristoyl glycine------MGNTAIAKK
------CCCCCCCCC		39.95-
2Myristoylation------MGNTAIAKK
------CCCCCCCCC		39.959368018
3Deamidated asparagine-----MGNTAIAKKG
-----CCCCCCCCCC		25.66-
3Deamidation-----MGNTAIAKKG
-----CCCCCCCCCC		25.66-
8PhosphorylationMGNTAIAKKGSEVES
CCCCCCCCCCCCCHH		52.10-
8 (in isoform 4)Phosphorylation-52.1021454597
9PhosphorylationGNTAIAKKGSEVESV
CCCCCCCCCCCCHHH		59.66-
9UbiquitinationGNTAIAKKGSEVESV
CCCCCCCCCCCCHHH		59.6627667366
9 (in isoform 4)Phosphorylation-59.6621454597
11PhosphorylationTAIAKKGSEVESVKE
CCCCCCCCCCHHHHH		47.55-
11UbiquitinationTAIAKKGSEVESVKE
CCCCCCCCCCHHHHH		47.5527667366
12UbiquitinationAIAKKGSEVESVKEF
CCCCCCCCCHHHHHH		60.0027667366
13 (in isoform 4)Phosphorylation-7.7125266776
15 (in isoform 4)Phosphorylation-43.6025266776
22UbiquitinationSVKEFLAKAKEDFLR
HHHHHHHHHHHHHHH		63.2427667366
24UbiquitinationKEFLAKAKEDFLRKW
HHHHHHHHHHHHHHC		58.0527667366
27 (in isoform 4)Phosphorylation-8.1421454597
27PhosphorylationLAKAKEDFLRKWENP
HHHHHHHHHHHCCCC		8.14-
34 (in isoform 4)Phosphorylation-30.5727600695
34PhosphorylationFLRKWENPPPSNAGL
HHHHCCCCCCCCCCH		30.5724719451
35UbiquitinationLRKWENPPPSNAGLE
HHHCCCCCCCCCCHH		57.4427667366
35 (in isoform 2)Ubiquitination-57.44-
36UbiquitinationRKWENPPPSNAGLED
HHCCCCCCCCCCHHH		41.2827667366
37 (in isoform 4)Phosphorylation-45.1225266776
48UbiquitinationLEDFERKKTLGTGSF
HHHHHHHHCCCCCCC		56.0222790023
48 (in isoform 2)Ubiquitination-56.0222790023
49PhosphorylationEDFERKKTLGTGSFG
HHHHHHHCCCCCCCC		33.1924899341
52PhosphorylationERKKTLGTGSFGRVM
HHHHCCCCCCCCEEE		32.5326643407
54PhosphorylationKKTLGTGSFGRVMLV
HHCCCCCCCCEEEEE		25.1024899341
69PhosphorylationKHKATEQYYAMKILD
ECCCCCHHHHHHHHC		6.2226032504
70PhosphorylationHKATEQYYAMKILDK
CCCCCHHHHHHHHCH		10.42-
71UbiquitinationKATEQYYAMKILDKQ
CCCCHHHHHHHHCHH		6.4527667366
80UbiquitinationKILDKQKVVKLKQIE
HHHCHHHCEEHHHHE		4.2027667366
81UbiquitinationILDKQKVVKLKQIEH
HHCHHHCEEHHHHEH		8.5027667366
93UbiquitinationIEHTLNEKRILQAVE
HEHHCCHHHHHHHCC		43.6027667366
95UbiquitinationHTLNEKRILQAVEFP
HHCCHHHHHHHCCCC		5.0427667366
140PhosphorylationLRRIGRFSEPHARFY
HHHHCCCCCHHHHHH		49.1922323819
140UbiquitinationLRRIGRFSEPHARFY
HHHHCCCCCHHHHHH		49.1927667366
196PhosphorylationAKRVKGRTWTLCGTP
EEECCCCEEEECCCH		31.3222322096
198PhosphorylationRVKGRTWTLCGTPEY
ECCCCEEEECCCHHH		16.1422322096
202PhosphorylationRTWTLCGTPEYLAPE
CEEEECCCHHHHCCH		16.3822322096
205PhosphorylationTLCGTPEYLAPEIIL
EECCCHHHHCCHHHH		14.9025159016
213PhosphorylationLAPEIILSKGYNKAV
HCCHHHHCCCCHHHH		17.3925777480
214UbiquitinationAPEIILSKGYNKAVD
CCHHHHCCCCHHHHH		63.07-
263PhosphorylationVRFPSHFSSDLKDLL
CCCCCCCCHHHHHHH		19.9522210690
264PhosphorylationRFPSHFSSDLKDLLR
CCCCCCCHHHHHHHH		46.1222210690
267 (in isoform 2)Ubiquitination-51.85-
273 (in isoform 2)Ubiquitination-2.60-
273UbiquitinationLKDLLRNLLQVDLTK
HHHHHHHHHHHHHHH		2.6027667366
274UbiquitinationKDLLRNLLQVDLTKR
HHHHHHHHHHHHHHH		5.5027667366
280UbiquitinationLLQVDLTKRFGNLKN
HHHHHHHHHHCCCCC		53.6922790023
280 (in isoform 2)Ubiquitination-53.6922790023
286 (in isoform 2)Ubiquitination-56.5122790023
286UbiquitinationTKRFGNLKNGVSDIK
HHHHCCCCCCCCCCC		56.5122790023
305UbiquitinationFATTDWIAIYQRKVE
EEECCEEEEEECCCC		7.0927667366
305 (in isoform 2)Ubiquitination-7.09-
306UbiquitinationATTDWIAIYQRKVEA
EECCEEEEEECCCCC		1.9027667366
318UbiquitinationVEAPFIPKFRGSGDT
CCCCCCCCCCCCCCC		42.7622790023
318 (in isoform 2)Ubiquitination-42.7622790023
322PhosphorylationFIPKFRGSGDTSNFD
CCCCCCCCCCCCCCC		29.2825619855
325PhosphorylationKFRGSGDTSNFDDYE
CCCCCCCCCCCCCCC		29.1525619855
326PhosphorylationFRGSGDTSNFDDYEE
CCCCCCCCCCCCCCH		39.9925619855
331PhosphorylationDTSNFDDYEEEEIRV
CCCCCCCCCHHEEEE		27.3825619855
333UbiquitinationSNFDDYEEEEIRVSI
CCCCCCCHHEEEEEE		55.4927667366
339PhosphorylationEEEEIRVSITEKCGK
CHHEEEEEEEHHHCH		17.5925521595
341PhosphorylationEEIRVSITEKCGKEF
HEEEEEEEHHHCHHH		23.1425619855
365Ubiquitination---------------------
---------------------		27667366
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 KAPCB_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KAPCB_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 KAPCB_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CALX_HUMANCANXphysical
26496610
GOGA3_HUMANGOLGA3physical
26496610
PCM1_HUMANPCM1physical
26496610
PCNT_HUMANPCNTphysical
26496610
KAPCA_HUMANPRKACAphysical
26496610
KAP0_HUMANPRKAR1Aphysical
26496610
KAP1_HUMANPRKAR1Bphysical
26496610
KAP2_HUMANPRKAR2Aphysical
26496610
PRKX_HUMANPRKXphysical
26496610
AKAP1_HUMANAKAP1physical
26496610
OFD1_HUMANOFD1physical
26496610
PKP4_HUMANPKP4physical
26496610
VAPB_HUMANVAPBphysical
26496610
MYOME_HUMANPDE4DIPphysical
26496610
MOONR_HUMANKIAA0753physical
26496610
CE170_HUMANCEP170physical
26496610
SCO2_HUMANSCO2physical
26496610
AKAP9_HUMANAKAP9physical
26496610
FR1OP_HUMANFGFR1OPphysical
26496610
AKP13_HUMANAKAP13physical
26496610
AKA11_HUMANAKAP11physical
26496610
MARE1_HUMANMAPRE1physical
26496610
CP131_HUMANCEP131physical
26496610
CEP68_HUMANCEP68physical
26496610
FGOP2_HUMANFGFR1OP2physical
26496610
CEP72_HUMANCEP72physical
26496610
CK5P2_HUMANCDK5RAP2physical
26496610
CSPP1_HUMANCSPP1physical
26496610
CCD77_HUMANCCDC77physical
26496610
TBC31_HUMANTBC1D31physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KAPCB_MOUSE

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Two novel brain-specific splice variants of the murine Cbeta gene ofcAMP-dependent protein kinase.";
Guthrie C.R., Skalhegg B.S., McKnight G.S.;
J. Biol. Chem. 272:29560-29565(1997).
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7 (ISOFORM 2), NUCLEOTIDESEQUENCE [GENOMIC DNA] OF 1-8 (ISOFORM 3), FUNCTION, MYRISTOYLATION ATGLY-2, AND TISSUE SPECIFICITY.
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 THR-198, 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 THR-198, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-69, AND MASSSPECTROMETRY.

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