Primary Information |
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| BoMiProt ID | Bomi4496 |
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| Protein Name | Casein kinase II subunit beta/Phosvitin/CK2N |
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| Organism | Bos taurus |
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| Uniprot ID | P67868 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001039919.1 |
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| Aminoacid Length | 215 |
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| Molecular Weight | 24942 |
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| FASTA Sequence |
Download |
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| Gene Name | CSNK2B |
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| Gene ID | 539235 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | Role in ribosomal L5 phosphorylation, in ribosomal assembly, or ribosomal transport in the intact cells. |
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| 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. |
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| Significance in milk | phosphorylation of milk proteins |
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| PTMs | Acetylation, Isopeptide bond formation, Phosphorylation, Ubl conjugation,SUMOylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|P67868|CSK2B_BOVIN Casein kinase II subunit beta OS=Bos taurus OX=9913 GN=CSNK2B PE=1 SV=1
MS*2S*3SEEVS*8WISWFCGLRGNEFFCEVDEDYIQDKFNLT*37GLNEQVPHYRQALDMILDLEPDE
ELEDNPNQS*69DLIEQAAEMLYGLIHARYILTNRGIAQMLEKYQQGDFGYCPRVYCENQPML
PIGLSDIPGEAMVKLYCPKCMDVYTPKSSRHHHTDGAYFGTGFPHMLFMVHPEYRPKRPA
NQFVPRLYGFKIHPMAYQLQLQAASNFKS*209PVKTIR
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| Predicted Disorder Regions | 1-5, 58-71, 211-215 |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| 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 |
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| 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. |
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