CSK21_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CSK21_MOUSE
• UniProt AC: Q60737
• Protein Name: Casein kinase II subunit alpha
• Gene Name: Csnk2a1
• Organism: Mus musculus (Mouse).
• Sequence Length: 391
• Subcellular Localization: Nucleus .
• 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. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry. Phosphorylates CCAR2 at 'Thr-454' (By similarity)..
• Protein Sequence: MSGPVPSRARVYTDVNTHRPREYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKDQARMSSTSMAGGSTPVSSANMMSGISSVPTPSPLGPLAGSPVIAAANSLGIPVPAAAGAQQ

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
2	Phosphorylation	------MSGPVPSRA ------CCCCCCCCC	52.37	22006019
12	Phosphorylation	VPSRARVYTDVNTHR CCCCCEEEEECCCCC	7.53	-
17	Phosphorylation	RVYTDVNTHRPREYW EEEEECCCCCCHHHC	21.07	-
102	Acetylation	ITLADIVKDPVSRTP EEHHHHHCCCCCCCC	57.56	22826441
102	Ubiquitination	ITLADIVKDPVSRTP EEHHHHHCCCCCCCC	57.56	22790023
122	Acetylation	HVNNTDFKQLYQTLT ECCCCCHHHHHHHHC	42.05	23954790
194	Phosphorylation	EYNVRVASRYFKGPE CEEEEEECHHCCCCE	25.34	23984901
247	Acetylation	DQLVRIAKVLGTEDL HHHHHHHHHHCCHHH	35.30	23236377
247	Ubiquitination	DQLVRIAKVLGTEDL HHHHHHHHHHCCHHH	35.30	22790023
255	Phosphorylation	VLGTEDLYDYIDKYN HHCCHHHHHHHHHCC	21.01	22817900
287	Phosphorylation	RWERFVHSENQHLVS HHHHHCCCCCCCCCC	32.70	29899451
294	Phosphorylation	SENQHLVSPEALDFL CCCCCCCCHHHHHHH	24.31	22817900
314	Phosphorylation	YDHQSRLTAREAMEH CCHHHCCCHHHHHHC	23.66	23140645
329	Ubiquitination	PYFYTVVKDQARMSS CCEEEEECCCHHCCC	39.52	22790023
335	Phosphorylation	VKDQARMSSTSMAGG ECCCHHCCCCCCCCC	25.55	-
344	Phosphorylation	TSMAGGSTPVSSANM CCCCCCCCCCCCCCC	30.86	-
357	Phosphorylation	NMMSGISSVPTPSPL CCCCCCCCCCCCCCC	30.14	22006019
360	Phosphorylation	SGISSVPTPSPLGPL CCCCCCCCCCCCCCC	33.95	-
362	Phosphorylation	ISSVPTPSPLGPLAG CCCCCCCCCCCCCCC	34.92	-
370	Phosphorylation	PLGPLAGSPVIAAAN CCCCCCCCCHHHHHH	15.47	-

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
344	T	Phosphorylation	Kinase	CDK1	P11440	Uniprot
360	T	Phosphorylation	Kinase	CDK1	P11440	Uniprot
362	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot
370	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
344	T	Phosphorylation	Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in prophase and metaphase and dephosphorylated during anaphase.	-
360	T	Phosphorylation	Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in prophase and metaphase and dephosphorylated during anaphase.	-
362	S	Phosphorylation	Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in prophase and metaphase and dephosphorylated during anaphase.	-
370	S	Phosphorylation	Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in prophase and metaphase and dephosphorylated during anaphase.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CSK21_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CSK21_MOUSE !!

Drug and Disease Associations

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