Search by BoMiProt ID - Bomi4496

Primary Information

BoMiProt ID Bomi4496
Protein Name Casein kinase II subunit beta/Phosvitin/CK2N
Organism Bos taurus
Uniprot IDP67868
Milk FractionWhey
Ref Sequence ID NP_001039919.1
Aminoacid Length 215
Molecular Weight 24942
FASTA Sequence Download
Gene Name CSNK2B
Gene ID 539235
Protein Existence Status reviewed

Secondary Information

Protein Function Role in ribosomal L5 phosphorylation, in ribosomal assembly, or ribosomal transport in the intact cells.
Biochemical Properties exists as a heterotetramer with alpha 2 beta 2, alpha alpha'beta 2, or alpha'2 beta 2. The alpha or alpha' subunits catalyze protein phosphorylation.Beta subunit may be to mediate the interaction of the catalytic subunit with target proteins.Beta subunit is highly conserved The beta subunit is a highly conserved protein of about 25kDa that contains, in its central section, a cysteine-rich motif, CX(n)C, that could be involved in bindinfg to Zn.Possessing an N-terminal auto-phosphorylation site, an internal acidic domain, and a potential metal-binding motif.
Significance in milk phosphorylation of milk proteins
PTMs Acetylation, Isopeptide bond formation, Phosphorylation, Ubl conjugation,SUMOylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions 1-5, 58-71, 211-215
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Autophosphorylation on Ser2 and Ser3 and Ser 4 on beta subunit for its activity and holoenzyme conformation.Within the free catalytic subunits,this occurs intermolecularly at Y182 on CK2α and Y183 on CK2α,resulting in increased catalytic activity through modulating interactions between the residue and the N-terminal of the kinase.CK2α S347 (which is proximal to the CDK1-phosphorylation site T344) is O-GlcNAc glycosylated. This glycosylation antagonizes CDK1-mediated phosphorylation of CK2 and increases its susceptibility to proteasomal degradation.K79 and K102 are SUMOylated.Phosphorylation of the CK2 substrates AP1, calnexin, DNA ligase 1 (LIG1), and Jun-D increased after inhibiting SUMOylation, suggesting thatSUMOylation regulates CK2 activity
Bibliography 1.Roffey SE, Litchfield DW. CK2 Regulation: Perspectives in 2021. Biomedicines. 2021 Sep 30;9(10):1361. doi: 10.3390/biomedicines9101361. PMID: 34680478; PMCID: PMC8533506. 2.Reed JC, Bidwai AP, Glover CV. Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory beta'-subunit of Saccharomyces cerevisiae casein kinase II. J Biol Chem. 1994 Jul 8;269(27):18192-200. PMID: 8027080.