CSK22_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CSK22_MOUSE
• UniProt AC: O54833
• Protein Name: Casein kinase II subunit alpha'
• Gene Name: Csnk2a2
• Organism: Mus musculus (Mouse).
• Sequence Length: 350
• Protein Description: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins (By similarity)..
• Protein Sequence: MPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGQDNYDQLVRIAKVLGTDELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCAENTVLSSGLTAAR

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
13	Phosphorylation	AGSRARVYAEVNSLR CCCHHEEEEEHHHHH	7.47	29514104
18	Phosphorylation	RVYAEVNSLRSREYW EEEEEHHHHHCCCCC	30.27	26824392
21	Phosphorylation	AEVNSLRSREYWDYE EEHHHHHCCCCCCEE	34.45	25293948
24	Phosphorylation	NSLRSREYWDYEAHV HHHHCCCCCCEEECC	11.50	25293948
27	Phosphorylation	RSREYWDYEAHVPSW HCCCCCCEEECCCCC	10.81	25293948
33	Phosphorylation	DYEAHVPSWGNQDDY CEEECCCCCCCHHHH	46.67	25293948
97	Acetylation	RGGTNIIKLIDTVKD CCCCEEHHHHHHCCC	35.28	-
103	Acetylation	IKLIDTVKDPVSKTP HHHHHHCCCCCCCCC	59.41	23236377
103	Malonylation	IKLIDTVKDPVSKTP HHHHHHCCCCCCCCC	59.41	26320211
195	Phosphorylation	EYNVRVASRYFKGPE HCCCEEEHHHCCCCE	25.34	23684622
230	Malonylation	LASMIFRKEPFFHGQ HHHHHHHCCCCCCCC	60.02	26320211
248	Acetylation	DQLVRIAKVLGTDEL HHHHHHHHHHCCHHH	35.30	23236377
260	Ubiquitination	DELYGYLKKYHIDLD HHHHHHHHHHCCCCC	42.68	22790023
288	Phosphorylation	RWENFIHSENRHLVS HHHHHCCCCCCCCCC	31.58	22817900
330	Ubiquitination	PYFYPVVKEQSQPCA CCCHHHHCCCCCCCC	50.71	-
333	Phosphorylation	YPVVKEQSQPCAENT HHHHCCCCCCCCCCC	36.86	-
347	O-linked_Glycosylation	TVLSSGLTAAR---- CEECCCCCCCC----	23.07	55411583

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

Oops, there are no upstream regulatory protein records of CSK22_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CSK22_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CSK22_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CSK22_MOUSE !!

Drug and Disease Associations

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