Summary: Casein kinase II regulatory subunit

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Wikipedia: CSNK2B
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CSNK2B Edit Wikipedia article

Casein kinase 2, beta polypeptide

PDB rendering based on 1jwh.

Available structures

PDB

Ortholog search: PDBe, RCSB

List of PDB id codes
1DS5, 1JWH, 1QF8, 3EED, 4DGL, 4MD7, 4MD8, 4MD9, 4NH1

Identifiers

Symbols

CSNK2B ; CK2B; CK2N; CSK2B; G5A

External IDs

OMIM: 115441 MGI: 88548 HomoloGene: 55572 ChEMBL: 2358 GeneCards: CSNK2B Gene

EC number

2.7.11.1

Gene ontology
Molecular function	• protein serine/threonine kinase activity • receptor binding • protein binding • transcription factor binding • protein kinase regulator activity • protein domain specific binding • identical protein binding • metal ion binding
Cellular component	• nucleus • cytoplasm • cytosol • plasma membrane • protein kinase CK2 complex • PcG protein complex • extracellular vesicular exosome
Biological process	• mitotic cell cycle • protein phosphorylation • signal transduction • axon guidance • negative regulation of cell proliferation • positive regulation of pathway-restricted SMAD protein phosphorylation • Wnt signaling pathway • positive regulation of activin receptor signaling pathway • adiponectin-activated signaling pathway • negative regulation of blood vessel endothelial cell migration • cellular protein complex assembly • regulation of protein kinase activity • regulation of DNA binding • endothelial tube morphogenesis
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 6:
31.63 – 31.64 Mb

Chr 17:
35.12 – 35.12 Mb

PubMed search

[1]

[2]

Casein kinase II regulatory subunit

structure of ck2 beta subunit crystallized in the presence of a p21waf1 peptide

Identifiers

Symbol

CK_II_beta

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Casein kinase II subunit beta is an protein that in humans is encoded by the CSNK2B gene.^[1]^[2]

This gene encodes the beta subunit of casein kinase II, a ubiquitous protein kinase which regulates metabolic pathways, signal transduction, transcription, translation, and replication. The enzyme localizes to the endoplasmic reticulum and the Golgi apparatus.^[3]

Casein kinase, a ubiquitous, well-conserved protein kinase involved in cell metabolism and differentiation, is characterised by its preference for Serine or Threonine in acidic stretches of amino acids. The enzyme is a tetramer of 2 alpha- and 2 beta-subunits.^[4]^[5] However, some species (e.g., mammals) possess 2 related forms of the alpha-subunit (alpha and alpha'), while others (e.g., fungi) possess 2 related beta-subunits (beta and beta').^[6] The alpha-subunit is the catalytic unit and contains regions characteristic of serine/threonine protein kinases. The beta-subunit is believed to be regulatory, possessing an N-terminal auto-phosphorylation site, an internal acidic domain, and a potential metal-binding motif.^[6] 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 binding a metal such as zinc.^[7] The mammalian beta-subunit gene promoter shares common features with those of other mammalian protein kinases and is closely related to the promoter of the regulatory subunit of cAMP-dependent protein kinase.^[6]

Interactions

CSNK2B has been shown to interact with CD163,^[8] CSNK2A2,^[9]^[10]^[11]^[12] Casein kinase 2, alpha 1,^[10]^[11]^[12]^[13]^[14] FGF1,^[15] TRIB3,^[16] CDC34,^[17] Ribosomal protein L5,^[9]^[13]^[18]^[19] BTF3,^[20] BRCA1,^[21] RNF7,^[13] P70-S6 Kinase 1^[22] and APC.^[23]

References

^ Yang-Feng TL, Teitz T, Cheung MC, Kan YW, Canaani D (March 1991). "Assignment of the human casein kinase II beta-subunit gene to 6p12----p21". Genomics 8 (4): 741–2. doi:10.1016/0888-7543(90)90266-W. PMID 2276748.
^ Mucher G, Becker J, Knapp M, Buttner R, Moser M, Rudnik-Schoneborn S, Somlo S, Germino G, Onuchic L, Avner E, Guay-Woodford L, Zerres K (April 1998). "Fine mapping of the autosomal recessive polycystic kidney disease locus (PKHD1) and the genes MUT, RDS, CSNK2 beta, and GSTA1 at 6p21.1-p12". Genomics 48 (1): 40–5. doi:10.1006/geno.1997.5145. PMID 9503014.
^ "Entrez Gene: CSNK2B casein kinase 2, beta polypeptide".
^ Jakobi R, Voss H, Pyerin W (July 1989). "Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta". Eur. J. Biochem. 183 (1): 227–33. doi:10.1111/j.1432-1033.1989.tb14917.x. PMID 2666134.
^ Voss H, Wirkner U, Jakobi R, Hewitt NA, Schwager C, Zimmermann J, Ansorge W, Pyerin W (July 1991). "Structure of the gene encoding human casein kinase II subunit beta". J. Biol. Chem. 266 (21): 13706–11. PMID 1856204.
^ ^a ^b ^c Bidwai AP, Reed JC, Glover CV (May 1995). "Cloning and disruption of CKB1, the gene encoding the 38-kDa beta subunit of Saccharomyces cerevisiae casein kinase II (CKII). Deletion of CKII regulatory subunits elicits a salt-sensitive phenotype". J. Biol. Chem. 270 (18): 10395–404. doi:10.1074/jbc.270.18.10395. PMID 7737972.
^ Reed JC, Bidwai AP, Glover CV (July 1994). "Cloning and disruption of CKB2, the gene encoding the 32-kDa regulatory beta'-subunit of Saccharomyces cerevisiae casein kinase II". J. Biol. Chem. 269 (27): 18192–200. PMID 8027080.
^ Ritter, M; Buechler C; Kapinsky M; Schmitz G (April 2001). "Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C". Eur. J. Immunol. (Germany) 31 (4): 999–1009. doi:10.1002/1521-4141(200104)31:4<999::AID-IMMU999>3.0.CO;2-R. ISSN 0014-2980. PMID 11298324.
^ ^a ^b Lehner, Ben; Semple Jennifer I; Brown Stephanie E; Counsell Damian; Campbell R Duncan; Sanderson Christopher M (January 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics (United States) 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. ISSN 0888-7543. PMID 14667819.
^ ^a ^b Kim, M S; Lee Y T; Kim J M; Cha J Y; Bae Y S (February 1998). "Characterization of protein interaction among subunits of protein kinase CKII in vivo and in vitro". Mol. Cells (KOREA) 8 (1): 43–8. ISSN 1016-8478. PMID 9571630.
^ ^a ^b Marin, O; Meggio F; Sarno S; Pinna L A (June 1997). "Physical dissection of the structural elements responsible for regulatory properties and intersubunit interactions of protein kinase CK2 beta-subunit". Biochemistry (UNITED STATES) 36 (23): 7192–8. doi:10.1021/bi962885q. ISSN 0006-2960. PMID 9188720.
^ ^a ^b Bosc, D G; Graham K C; Saulnier R B; Zhang C; Prober D; Gietz R D; Litchfield D W (May 2000). "Identification and characterization of CKIP-1, a novel pleckstrin homology domain-containing protein that interacts with protein kinase CK2". J. Biol. Chem. (UNITED STATES) 275 (19): 14295–306. doi:10.1074/jbc.275.19.14295. ISSN 0021-9258. PMID 10799509.
^ ^a ^b ^c Ahn, B H; Kim T H; Bae Y S (October 2001). "Mapping of the interaction domain of the protein kinase CKII beta subunit with target proteins". Mol. Cells (Korea (South)) 12 (2): 158–63. ISSN 1016-8478. PMID 11710515.
^ Kusk, M; Ahmed R; Thomsen B; Bendixen C; Issinger O G; Boldyreff B (January 1999). "Interactions of protein kinase CK2beta subunit within the holoenzyme and with other proteins". Mol. Cell. Biochem. (NETHERLANDS) 191 (1–2): 51–8. doi:10.1023/A:1006840613986. ISSN 0300-8177. PMID 10094392.
^ Skjerpen, Camilla Skiple; Nilsen Trine; Wesche Jørgen; Olsnes Sjur (August 2002). "Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity". EMBO J. (England) 21 (15): 4058–69. doi:10.1093/emboj/cdf402. ISSN 0261-4189. PMC 126148. PMID 12145206.
^ Zhou, Ying; Li Lu; Liu Qiongming; Xing Guichun; Kuai Xuezhang; Sun Jing; Yin Xiushan; Wang Jian; Zhang Lingqiang; He Fuchu (May 2008). "E3 ubiquitin ligase SIAH1 mediates ubiquitination and degradation of TRB3". Cell. Signal. (England) 20 (5): 942–8. doi:10.1016/j.cellsig.2008.01.010. ISSN 0898-6568. PMID 18276110.
^ Block, K; Boyer T G; Yew P R (November 2001). "Phosphorylation of the human ubiquitin-conjugating enzyme, CDC34, by casein kinase 2". J. Biol. Chem. (United States) 276 (44): 41049–58. doi:10.1074/jbc.M106453200. ISSN 0021-9258. PMID 11546811.
^ Boldyreff, B; Issinger O G (February 1997). "A-Raf kinase is a new interacting partner of protein kinase CK2 beta subunit". FEBS Lett. (NETHERLANDS) 403 (2): 197–9. doi:10.1016/S0014-5793(97)00010-0. ISSN 0014-5793. PMID 9042965.
^ Kim, J M; Cha J Y; Marshak D R; Bae Y S (September 1996). "Interaction of the beta subunit of casein kinase II with the ribosomal protein L5". Biochem. Biophys. Res. Commun. (UNITED STATES) 226 (1): 180–6. doi:10.1006/bbrc.1996.1330. ISSN 0006-291X. PMID 8806611.
^ Grein, S; Pyerin W (January 1999). "BTF3 is a potential new substrate of protein kinase CK2". Mol. Cell. Biochem. (NETHERLANDS) 191 (1–2): 121–8. doi:10.1023/A:1006806226764. ISSN 0300-8177. PMID 10094400.
^ O'Brien, K A; Lemke S J; Cocke K S; Rao R N; Beckmann R P (July 1999). "Casein kinase 2 binds to and phosphorylates BRCA1". Biochem. Biophys. Res. Commun. (UNITED STATES) 260 (3): 658–64. doi:10.1006/bbrc.1999.0892. ISSN 0006-291X. PMID 10403822.
^ Panasyuk, Ganna; Nemazanyy Ivan; Zhyvoloup Alexander; Bretner Maria; Litchfield David W; Filonenko Valeriy; Gout Ivan T (October 2006). "Nuclear export of S6K1 II is regulated by protein kinase CK2 phosphorylation at Ser-17". J. Biol. Chem. (United States) 281 (42): 31188–201. doi:10.1074/jbc.M602618200. ISSN 0021-9258. PMID 16895915.
^ Homma, Miwako Kato; Li Dongxia; Krebs Edwin G; Yuasa Yasuhito; Homma Yoshimi (April 2002). "Association and regulation of casein kinase 2 activity by adenomatous polyposis coli protein". Proc. Natl. Acad. Sci. U.S.A. (United States) 99 (9): 5959–64. doi:10.1073/pnas.092143199. ISSN 0027-8424. PMC 122884. PMID 11972058.

Casein kinase II regulatory subunit Provide feedback

No Pfam abstract.

External database links

PANDIT:	PF01214
PROSITE:	PDOC00845
Pseudofam:	PF01214
SCOP:	1qf8
SYSTERS:	CK_II_beta

This tab holds annotation information from the InterPro database.

InterPro entry IPR000704

Casein kinase, a ubiquitous well-conserved protein kinase involved in cell metabolism and differentiation, is characterised by its preference for Ser or Thr in acidic stretches of amino acids. The enzyme is a tetramer of 2 alpha- and 2 beta-subunits [PUBMED:2666134, PUBMED:1856204]. However, some species (e.g., mammals) possess 2 related forms of the alpha-subunit (alpha and alpha'), while others (e.g., fungi) possess 2 related beta-subunits (beta and beta') [PUBMED:7737972].

The alpha-subunit is the catalytic unit and contains regions characteristic of serine/threonine protein kinases. The beta-subunit is believed to be regulatory, possessing an N-terminal auto-phosphorylation site, an internal acidic domain, and a potential metal-binding motif [PUBMED:7737972]. The beta subunit contains, in its central section, a cysteine-rich motif, CX(n)C, that could be involved in binding a metal such as zinc [PUBMED:8027080]. The mammalian beta-subunit gene promoter shares common features with those of other mammalian protein kinases and is closely related to the promoter of the regulatory subunit of cAMP-dependent protein kinase [PUBMED:7737972].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Cellular component	protein kinase CK2 complex (GO:0005956)
Molecular function	protein kinase regulator activity (GO:0019887)

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

There are various ways to view or download the sequence alignments that we store. We provide several sequence viewers and a plain-text Stockholm-format file for download.

Alignment types

We make a range of alignments for each Pfam-A family:

seed: the curated alignment from which the HMM for the family is built
full: the alignment generated by searching the sequence database using the HMM
RP15/RP35/RP55/RP75: Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
NCBI: alignment generated by searching the NCBI sequence database using the family HMM
meta: alignment generated by searching the metagenomics sequence database using the family HMM

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

	Seed (66)	Full (783)	Representative proteomes				NCBI (729)	Meta (15)
	Seed (66)	Full (783)	RP15 (212)	RP35 (307)	RP55 (426)	RP75 (504)	NCBI (729)	Meta (15)
Jalview	View	View	View	View	View	View	View	View
HTML	View	View	View	View	View	View
PP/heatmap	₁	View	View	View	View	View
Pfam viewer	View	View

¹Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: available, not generated, — not available.

Format an alignment

	Seed (66)	Full (783)	Representative proteomes				NCBI (729)	Meta (15)
	Seed (66)	Full (783)	RP15 (212)	RP35 (307)	RP55 (426)	RP75 (504)	NCBI (729)	Meta (15)
Alignment:
Format:
Order:	Tree Alphabetical
Sequence:	Inserts lower case All upper case
Gaps:
Download/view:	Download View

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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

	Seed (66)	Full (783)	Representative proteomes				NCBI (729)	Meta (15)
	Seed (66)	Full (783)	RP15 (212)	RP35 (307)	RP55 (426)	RP75 (504)	NCBI (729)	Meta (15)
Raw Stockholm	Download	Download	Download	Download	Download	Download	Download	Download
Gzipped	Download	Download	Download	Download	Download	Download	Download	Download

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation

Seed source:

Prosite

Previous IDs:

none

Type:

Domain

Author:

Finn RD, Bateman A

Number in seed:

66

Number in full:

783

Average length of the domain:

179.10 aa

Average identity of full alignment:

47 %

Average coverage of the sequence by the domain:

69.13 %

HMM information

HMM build commands:

build method: hmmbuild -o /dev/null HMM SEED

search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq

Model details:

Parameter	Sequence	Domain
Gathering cut-off	20.1	20.1
Trusted cut-off	22.2	21.1
Noise cut-off	20.0	17.3

Model length:

184

Family (HMM) version:

13

Download:

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Species distribution

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family
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Unmapped species names

The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.

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Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.

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Interactive tree

For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.

We also count the number of unique sequences on which each domain is found, which is shown in green. Note that a domain may appear multiple times on the same sequence, leading to the difference between these two numbers.

Finally, we group sequences from the same organism according to the NCBI code that is assigned by UniProt, allowing us to count the number of distinct sequences on which the domain is found. This value is shown in the pink boxes.

We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.

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Interactions

There are 2 interactions for this family. More...

Pkinase CK_II_beta

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CK_II_beta domain has been found. There are 22 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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Archea	Eukaryota
Bacteria	Other sequences
Viruses	Unclassified
Viroids	Unclassified sequence

Family: CK_II_beta (PF01214)

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Summary: Casein kinase II regulatory subunit

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CSNK2B Edit Wikipedia article

Interactions

References

Further reading

Casein kinase II regulatory subunit Provide feedback

External database links

InterPro entry IPR000704

Gene Ontology

Domain organisation

Alignments

Alignment types

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Format an alignment

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External links

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Trees

Curation and family details

Curation

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Species distribution

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How the sunburst is generated

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Interactions

Structures