KAPCA_MOUSE - dbPTM
KAPCA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KAPCA_MOUSE
UniProt AC P05132
Protein Name cAMP-dependent protein kinase catalytic subunit alpha
Gene Name Prkaca
Organism Mus musculus (Mouse).
Sequence Length 351
Subcellular Localization Cytoplasm . Cell membrane. Nucleus. Mitochondrion . Membrane
Lipid-anchor . Translocates into the nucleus (monomeric catalytic subunit) (By similarity). The inactive holoenzyme is found in the cytoplasm. Distributed throughout the cytoplasm in meio
Protein Description Phosphorylates a large number of substrates in the cytoplasm and the nucleus. 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 CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock (By similarity). Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation (By similarity)..
Protein Sequence MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWETPSQNTAQLDQFDRIKTLGTGSFGRVMLVKHKESGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVAGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFTEF
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
2Myristoylation------MGNAAAAKK
------CCCHHHHHC		32.2711141074
2N-myristoyl glycine------MGNAAAAKK
------CCCHHHHHC		32.27-
3Deamidated asparagine-----MGNAAAAKKG
-----CCCHHHHHCC		25.71-
3Deamidation-----MGNAAAAKKG
-----CCCHHHHHCC		25.7111141074
11PhosphorylationAAAAKKGSEQESVKE
HHHHHCCCCHHHHHH		45.0111141074
14UbiquitinationAKKGSEQESVKEFLA
HHCCCCHHHHHHHHH		54.1427667366
15PhosphorylationKKGSEQESVKEFLAK
HCCCCHHHHHHHHHH		37.8827742792
22UbiquitinationSVKEFLAKAKEDFLK
HHHHHHHHHHHHHHH		63.2427667366
35PhosphorylationLKKWETPSQNTAQLD
HHHCCCCCCCCHHHH		43.4117203969
40UbiquitinationTPSQNTAQLDQFDRI
CCCCCCHHHHHHHHH		43.4627667366
48UbiquitinationLDQFDRIKTLGTGSF
HHHHHHHEECCCCCC		38.2927667366
49PhosphorylationDQFDRIKTLGTGSFG
HHHHHHEECCCCCCC		28.2224899341
52PhosphorylationDRIKTLGTGSFGRVM
HHHEECCCCCCCEEE		32.5326643407
54PhosphorylationIKTLGTGSFGRVMLV
HEECCCCCCCEEEEE		25.1024899341
85UbiquitinationQKVVKLKQIEHTLNE
HHCEEHHHEEHHCCH		57.6527667366
93UbiquitinationIEHTLNEKRILQAVN
EEHHCCHHHHHHHHC		43.6027667366
110PhosphorylationFLVKLEFSFKDNSNL
EEEEEEEEECCCCCE		23.2421659604
140PhosphorylationLRRIGRFSEPHARFY
HHHHCCCCCHHHHHH		49.1922323819
184PhosphorylationQQGYIQVTDFGFAKR
CCCEEEEECCCCEEE		14.8322817900
196PhosphorylationAKRVKGRTWTLCGTP
EEECCCCEEEECCCH		31.3222322096
198PhosphorylationRVKGRTWTLCGTPEY
ECCCCEEEECCCHHH		16.1422322096
200GlutathionylationKGRTWTLCGTPEYLA
CCCEEEECCCHHHHC		4.4522833525
202PhosphorylationRTWTLCGTPEYLAPE
CEEEECCCHHHHCCH		16.3822322096
205PhosphorylationTLCGTPEYLAPEIIL
EECCCHHHHCCHHHH		14.9025159016
213PhosphorylationLAPEIILSKGYNKAV
HCCHHHHCCCCHHHH		17.3925777480
214UbiquitinationAPEIILSKGYNKAVD
CCHHHHCCCCHHHHH		63.07-
263PhosphorylationVRFPSHFSSDLKDLL
CCCCCCCCHHHHHHH		19.9522210690
264PhosphorylationRFPSHFSSDLKDLLR
CCCCCCCHHHHHHHH		46.1222210690
267AcetylationSHFSSDLKDLLRNLL
CCCCHHHHHHHHHHH		51.8523236377
278UbiquitinationRNLLQVDLTKRFGNL
HHHHHHHHHHHHCCC		6.8127667366
280UbiquitinationLLQVDLTKRFGNLKN
HHHHHHHHHHCCCCC		53.69-
286UbiquitinationTKRFGNLKNGVNDIK
HHHHCCCCCCCCHHH		56.5122790023
310UbiquitinationWIAIYQRKVEAPFIP
EEEEEECCCCCCCCC		28.9727667366
318UbiquitinationVEAPFIPKFKGPGDT
CCCCCCCCCCCCCCC		55.6927667366
325PhosphorylationKFKGPGDTSNFDDYE
CCCCCCCCCCCCCCC		31.3325619855
326PhosphorylationFKGPGDTSNFDDYEE
CCCCCCCCCCCCCCH		39.9923375375
331PhosphorylationDTSNFDDYEEEEIRV
CCCCCCCCCHHHEEH		27.3825619855
339PhosphorylationEEEEIRVSINEKCGK
CHHHEEHCCCHHCCC		15.1725521595
344GlutathionylationRVSINEKCGKEFTEF
EHCCCHHCCCCCCCC		8.4222833525
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
11SPhosphorylationKinasePRKACAP05132
GPS
198TPhosphorylationKinasePRKACAP05132
GPS
198TPhosphorylationKinasePDK1O15530
PSP
198TPhosphorylationKinasePDK1Q9Z2A0
PSP
331YPhosphorylationKinaseEGFRQ01279
PSP
331YPhosphorylationKinaseSYKP43405
PSP
331YPhosphorylationKinasePDGFRAP26618
PSP
331YPhosphorylationKinasePDGFRBP05622
PSP
339SPhosphorylationKinasePKACAP17612
PSP
339SPhosphorylationKinasePRKACAP05132
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
3NAmidation

11141074
3NMyristoylation

11141074
3NPhosphorylation

11141074
11SAmidation

8395513
11SMyristoylation

8395513
11SPhosphorylation

8395513
198TPhosphorylation

8395513
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 KAPCA_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRZ1_SCHPOprz1physical
22496451
MBP_MOUSEMbpphysical
22496451
SRC_MOUSESrcphysical
11804588
SOX9_MOUSESox9physical
15889150
4EBP2_MOUSEEif4ebp2physical
8939971
LASP1_MOUSELasp1physical
15465019
LASP1_HUMANLASP1physical
15465019
PLPL2_MOUSEPnpla2physical
22733971
14332_ARATHGRF2physical
24211434
TAU_HUMANMAPTphysical
19138662
TAU_HUMANMAPTphysical
19647741
TFC5_YEASTBDP1physical
25970584
VATA_MOUSEAtp6v1aphysical
20525692
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KAPCA_MOUSE

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Related Literatures of Post-Translational Modification
Deamidation
ReferencePubMed
"Influence of myristoylation, phosphorylation, and deamidation on thestructural behavior of the N-terminus of the catalytic subunit ofcAMP-dependent protein kinase.";
Tholey A., Pipkorn R., Bossemeyer D., Kinzel V., Reed J.;
Biochemistry 40:225-231(2001).
Cited for: MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-11, AND DEAMIDATION ATASN-3.
Myristoylation
ReferencePubMed
"Influence of myristoylation, phosphorylation, and deamidation on thestructural behavior of the N-terminus of the catalytic subunit ofcAMP-dependent protein kinase.";
Tholey A., Pipkorn R., Bossemeyer D., Kinzel V., Reed J.;
Biochemistry 40:225-231(2001).
Cited for: MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-11, AND DEAMIDATION ATASN-3.
Phosphorylation
ReferencePubMed
"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-35, AND MASSSPECTROMETRY.
"Influence of myristoylation, phosphorylation, and deamidation on thestructural behavior of the N-terminus of the catalytic subunit ofcAMP-dependent protein kinase.";
Tholey A., Pipkorn R., Bossemeyer D., Kinzel V., Reed J.;
Biochemistry 40:225-231(2001).
Cited for: MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-11, AND DEAMIDATION ATASN-3.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-196, AND MASSSPECTROMETRY.
"Phosphorylation and activation of cAMP-dependent protein kinase byphosphoinositide-dependent protein kinase.";
Cheng X., Ma Y., Moore M., Hemmings B.A., Taylor S.S.;
Proc. Natl. Acad. Sci. U.S.A. 95:9849-9854(1998).
Cited for: PHOSPHORYLATION AT THR-198 BY PDPK1.

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