CPLM-000825

Genbank Nucleotide ID

Casein kinase II subunit alpha'

Protein Synonyms/Alias

Mus musculus (Mouse)

Position	Peptide	Type	References
103	IKLIDTVKDPVSKTP	acetylation	[1]
248	DQLVRIAKVLGTDEL	acetylation	[1]
260	DELYGYLKKYHIDLD	ubiquitination	[2]

[1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]

Functional 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).

DOMAIN 40 325 Protein kinase.
NP_BIND 46 54 ATP (By similarity).
ACT_SITE 157 157 Proton acceptor (By similarity).
BINDING 69 69 ATP (By similarity).
MOD_RES 13 13 Phosphotyrosine (By similarity).
MOD_RES 18 18 Phosphoserine (By similarity).
MOD_RES 21 21 Phosphoserine (By similarity).
MOD_RES 97 97 N6-acetyllysine (By similarity).
MOD_RES 288 288 Phosphoserine (By similarity).

Acetylation; Apoptosis; ATP-binding; Cell cycle; Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transcription; Transcription regulation; Transferase; Wnt signaling pathway.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0031519; C:PcG protein complex; IEA:Compara.
GO:0005956; C:protein kinase CK2 complex; TAS:MGI.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO:0071174; P:mitotic spindle checkpoint; ISS:UniProtKB.
GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.

IPR011009; Kinase-like_dom.
IPR000719; Prot_kinase_cat_dom.
IPR017441; Protein_kinase_ATP_BS.
IPR002290; Ser/Thr_dual-sp_kinase_dom.
IPR008271; Ser/Thr_kinase_AS.

PS00107; PROTEIN_KINASE_ATP
PS50011; PROTEIN_KINASE_DOM
PS00108; PROTEIN_KINASE_ST