Casein kinase II subunit beta (CSNK2B)

The protein contains 215 amino acids for an estimated molecular weight of 24942 Da.

 

Regulatory subunit of casein kinase II/CK2. As part of the kinase complex regulates the basal catalytic activity of the alpha subunit a constitutively active serine/threonine-protein kinase that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (PubMed:11239457, PubMed:16818610). Participates in Wnt signaling (By similarity). (updated: Oct. 7, 2020)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

This protein is annotated as membranous in Gene Ontology.


Interpro domains
Total structural coverage: 100%
Model score: 100
No model available.

(right-click above to access to more options from the contextual menu)

VariantDescription
POBINDS; unknown pathological significance; associated in cis with 5-E--R-215 del
POBINDS
POBINDS
POBINDS
POBINDS

The reference OMIM entry for this protein is 115441

Casein kinase ii, beta; csnk2b
Casein kinase ii, beta subunit; ck2b
Phosvitin

CLONING

Phosvitin/casein kinase type II (CK2) is a ubiquitous, highly conserved enzyme consisting of subunits alpha (115440), alpha-prime (115442), and beta. It is a ubiquitous messenger-independent serine/threonine kinase, localized in both the cytoplasm and the nucleus. Jakobi et al. (1989) prepared subunit beta from human placenta and determined the amino acid sequence of a protease digestion peptide. The deduced nucleotide sequence was used for the synthesis of a mixture of 20-mers as a hybridization probe to screen a lambda-gt10 HeLa cell cDNA library for clones encoding the beta subunit. The beta subunit presumably serves regulatory functions. Heller-Harrison et al. (1989) found evidence of a single gene. They described a cDNA of 2.57 kb containing 96 bp of 5-prime untranslated sequence, 645 bp of open reading frame, and 1,832 bp of 3-prime untranslated sequence.

GENE STRUCTURE

Voss et al. (1991) analyzed the structure of the gene encoding human casein kinase II subunit beta and Boldyreff and Issinger (1995) determined the structure of the mouse counterpart. The latter is composed of 7 exons contained within 7,874 bp. The lengths of the mouse coding exons correspond exactly to the lengths of the exons in the human CK2B gene. Both genes contain a first untranslated exon. Despite common features, a striking difference concerned the human CK2A subunit binding domain at position -170 to -239 of the human gene. This domain has no counterpart in the mouse gene.

MAPPING

By hybridization to spot-blotting filters of flow-sorted human chromosomes followed by in situ hybridization, Yang-Feng et al. (1990) mapped the CSNK2B gene to 6p21.1. Albertella et al. (1996) characterized the genes in the central 1,100-kb class III region of the major histocompatibility complex. One of the genes found in this region was identified as CSNK2B. This would suggest that CSNK2B is located in the 6p21.3 region rather than the 6p21.1 region.

GENE FUNCTION

Sarno et al. (2000) reported that a C-terminally truncated form of CK2-beta lacking residues 170 to 215 could not stably associate with the catalytic CK2 subunits. This CK2-beta mutant retained its central homodimerization domain and still existed as a dimer. However, the mutant was defective in a number of other properties mediated by elements still present in its N-terminal half, notably downregulation of catalytic activity, autophosphorylation, and responsiveness to polycationic effectors. All these functions were restored by simultaneous addition of a synthetic peptide reproducing the CK2-beta deleted region, which was able to associate with the catalytic subunits and to stimulate catalytic activity. This peptide includes a segment that shares similarity with a region of cyclin A (see 604036) involved in activation of CDK2 (116953), and Sarno et al. (2000) found that a peptide reproducing this sequence (residues 181 to 203) interacted with the CK2-alpha subunit and stimulated its catalytic activity. This smaller peptide also partially restored the ability of truncated CK2-beta to autophosphorylate. Sarno et al. (2000) concluded that residues 181 to 203 are essential for the regulatory properties of CK2-beta. Phosphorylation of the human p53 protein (191170) at ser392 is responsive to ultraviolet (UV) but not gamma irradiation. Keller et al. (2001) identified and purified a mammalian UV-activated protein kinase complex that phosphorylates ser392 in vitro. This kin ... More on the omim web site

Subscribe to this protein entry history

Oct. 20, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 25, 2017: Additional information
No protein expression data in P. Mayeux work for CSNK2B

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 115441 was added.

Jan. 27, 2016: Protein entry updated
Automatic update: model status changed

Jan. 24, 2016: Protein entry updated
Automatic update: model status changed