dbPTM

KAP0_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KAP0_MOUSE
UniProt AC	Q9DBC7
Protein Name	cAMP-dependent protein kinase type I-alpha regulatory subunit
Gene Name	Prkar1a
Organism	Mus musculus (Mouse).
Sequence Length	381
Subcellular Localization	Cell membrane.
Protein Description	Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells..
Protein Sequence	MASGSMATSEEERSLRECELYVQKHNIQALLKDSIVQLCTTRPERPMAFLREYFERLEKEEARQIQCLQKTGIRTDSREDEISPPPPNPVVKGRRRRGAISAEVYTEEDAASYVRKVIPKDYKTMAALAKAIEKNVLFSHLDDNERSDIFDAMFPVSFIAGETVIQQGDEGDNFYVIDQGEMDVYVNNEWATSVGEGGSFGELALIYGTPRAATVKAKTNVKLWGIDRDSYRRILMGSTLRKRKMYEEFLSKVSILESLDKWERLTVADALEPVQFEDGQKIVVQGEPGDEFFIILEGTAAVLQRRSENEEFVEVGRLGPSDYFGEIALLMNRPRAATVVARGPLKCVKLDRPRFERVLGPCSDILKRNIQQYNSFVSLSV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MASGSMAT -------CCCCCCCC	6.38	-
2	Acetylation	------MASGSMATS ------CCCCCCCCC	23.69	-
3	Phosphorylation	-----MASGSMATSE -----CCCCCCCCCH	30.06	28066266
5	Phosphorylation	---MASGSMATSEEE ---CCCCCCCCCHHH	11.62	28066266
9	Phosphorylation	ASGSMATSEEERSLR CCCCCCCCHHHHHHH	33.21	28066266
14	Phosphorylation	ATSEEERSLRECELY CCCHHHHHHHHHHHH	34.75	28066266
18	S-nitrosylation	EERSLRECELYVQKH HHHHHHHHHHHHHHH	3.36	21278135
18	S-nitrosocysteine	EERSLRECELYVQKH HHHHHHHHHHHHHHH	3.36	-
67	Glutathionylation	EEARQIQCLQKTGIR HHHHHHHHHHHHCCC	4.67	24333276
70	Ubiquitination	RQIQCLQKTGIRTDS HHHHHHHHHCCCCCC	35.45	-
71	Phosphorylation	QIQCLQKTGIRTDSR HHHHHHHHCCCCCCC	25.53	27087446
75	Phosphorylation	LQKTGIRTDSREDEI HHHHCCCCCCCCCCC	36.08	25521595
77	Phosphorylation	KTGIRTDSREDEISP HHCCCCCCCCCCCCC	36.64	24925903
83	Phosphorylation	DSREDEISPPPPNPV CCCCCCCCCCCCCCC	29.34	24925903
92	Ubiquitination	PPPNPVVKGRRRRGA CCCCCCCCCCCCCCC	47.11	-
101	Phosphorylation	RRRRGAISAEVYTEE CCCCCCCEEEEECHH	20.17	15345747
105	Phosphorylation	GAISAEVYTEEDAAS CCCEEEEECHHHHHH	10.43	24511133
147	Phosphorylation	HLDDNERSDIFDAMF CCCCCCCCCHHHHHC	28.95	25367039
157	Phosphorylation	FDAMFPVSFIAGETV HHHHCCHHEECCCEE	15.92	25367039
163	Phosphorylation	VSFIAGETVIQQGDE HHEECCCEEEEECCC	23.22	25367039
175	Phosphorylation	GDEGDNFYVIDQGEM CCCCCCEEEEECCEE	11.62	25367039
185	Phosphorylation	DQGEMDVYVNNEWAT ECCEEEEEECCEEEC	8.00	25367039
192	Phosphorylation	YVNNEWATSVGEGGS EECCEEECCCCCCCC	25.64	25367039
193	Phosphorylation	VNNEWATSVGEGGSF ECCEEECCCCCCCCH	22.00	25367039
199	Phosphorylation	TSVGEGGSFGELALI CCCCCCCCHHHEEEE	40.72	25367039
207	Phosphorylation	FGELALIYGTPRAAT HHHEEEEECCCCCEE	18.79	25367039
209	Phosphorylation	ELALIYGTPRAATVK HEEEEECCCCCEEEE	7.82	25367039
214	Phosphorylation	YGTPRAATVKAKTNV ECCCCCEEEEECCCC	22.89	25367039
222	Ubiquitination	VKAKTNVKLWGIDRD EEECCCCEEEECCHH	40.36	-
244	Ubiquitination	GSTLRKRKMYEEFLS CCHHHHHHHHHHHHH	49.20	-
251	Phosphorylation	KMYEEFLSKVSILES HHHHHHHHHHHHHHC	36.01	18779572
252	Ubiquitination	MYEEFLSKVSILESL HHHHHHHHHHHHHCC	41.99	-
258	Phosphorylation	SKVSILESLDKWERL HHHHHHHCCCHHCCC	38.12	25293948
261	Ubiquitination	SILESLDKWERLTVA HHHHCCCHHCCCCHH	57.14	-
338	Phosphorylation	MNRPRAATVVARGPL HCCCCCEEEEECCCE	17.96	-
346	Ubiquitination	VVARGPLKCVKLDRP EEECCCEEEEECCCH	39.86	-
349	Ubiquitination	RGPLKCVKLDRPRFE CCCEEEEECCCHHHH	54.89	-
362	Glutathionylation	FERVLGPCSDILKRN HHHHHCHHHHHHHHH	5.61	24333276
362	S-palmitoylation	FERVLGPCSDILKRN HHHHHCHHHHHHHHH	5.61	26165157
367	Acetylation	GPCSDILKRNIQQYN CHHHHHHHHHHHHHH	43.67	22826441
375	Phosphorylation	RNIQQYNSFVSLSV- HHHHHHHCCEEECC-	23.30	29514104
380	Phosphorylation	YNSFVSLSV------ HHCCEEECC------	20.48	26643407

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 KAP0_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KAP0_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 KAP0_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of KAP0_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KAP0_MOUSE

Related Literatures of Post-Translational Modification

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-83, AND MASSSPECTROMETRY.	19131326 [Abstract]
"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-83, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.	18630941 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-83, AND MASSSPECTROMETRY.	17242355 [Abstract]
"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-83, AND MASSSPECTROMETRY.	17203969 [Abstract]
"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-77 AND SER-83, AND MASSSPECTROMETRY.	16452087 [Abstract]
"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 SER-101, AND MASSSPECTROMETRY.	15345747 [Abstract]