Casein kinase II subunit alpha' - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P19784 (CSK22_HUMAN)

Last modified February 9, 2010. Version 108. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Casein kinase II subunit alpha'
      Short name=CK II alpha'
    EC=2.7.11.1

Gene names

Name:	CSNK2A2
Synonyms:	CK2A2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha and alpha' chains contain the catalytic site. Participates in Wnt signaling. CK2 phosphorylates 'Ser-392' of p53/TP53 following UV irradiation. Ref.3
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Tetramer composed of an alpha chain, an alpha' and two beta chains. Also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation.
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily. Contains 1 protein kinase domain.

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Ontologies

Keywords
Biological process	Wnt signaling pathway
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	Wnt receptor signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein N-terminus binding Inferred from physical interaction. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
CSNK2B	P67870	2	EBI-347451,EBI-348169
RNPS1	Q15287	1	EBI-347451,EBI-395959

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 350

350

Casein kinase II subunit alpha'

PRO_0000085891

Regions

Domain

40 – 325

286

Protein kinase

Nucleotide binding

46 – 54

ATP By similarity

Sites

Active site

157

Proton acceptor By similarity

Binding site

ATP By similarity

Amino acid modifications

Modified residue

Phosphotyrosine

Modified residue

Phosphoserine Ref.5

Modified residue

Phosphoserine Ref.5

Modified residue

N6-acetyllysine Ref.8

Modified residue

240

Phosphotyrosine

Modified residue

288

Phosphoserine Ref.5

Modified residue

343

Phosphoserine

Natural variations

Natural variant

188

E → A: dbSNP rs55911801. Ref.9

VAR_040416

Secondary structure

350

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P19784-1 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 3ECB92F6BD3DD7F1
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FASTA

350

41,213

        10         20         30         40         50         60 
MPGPAAGSRA RVYAEVNSLR SREYWDYEAH VPSWGNQDDY QLVRKLGRGK YSEVFEAINI 

        70         80         90        100        110        120 
TNNERVVVKI LKPVKKKKIK REVKILENLR GGTNIIKLID TVKDPVSKTP ALVFEYINNT 

       130        140        150        160        170        180 
DFKQLYQILT DFDIRFYMYE LLKALDYCHS KGIMHRDVKP HNVMIDHQQK KLRLIDWGLA 

       190        200        210        220        230        240 
EFYHPAQEYN VRVASRYFKG PELLVDYQMY DYSLDMWSLG CMLASMIFRR EPFFHGQDNY 

       250        260        270        280        290        300 
DQLVRIAKVL GTEELYGYLK KYHIDLDPHF NDILGQHSRK RWENFIHSEN RHLVSPEALD 

       310        320        330        340        350 
LLDKLLRYDH QQRLTAKEAM EHPYFYPVVK EQSQPCADNA VLSSGLTAAR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of human cDNA clones encoding the alpha and the alpha' subunits of casein kinase II." Lozeman F.J., Litchfield D.W., Piening C., Takio K., Walsh K.A., Krebs E.G. Biochemistry 29:8436-8447(1990) [PubMed: 2174700] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
[3]	"A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1." Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H. Mol. Cell 7:283-292(2001) [PubMed: 11239457] [Abstract] Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H.
[4]	"p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex." Keller D.M., Lu H. J. Biol. Chem. 277:50206-50213(2002) [PubMed: 12393879] [Abstract] Cited for: INTERACTION WITH SSRP1 AND SUPT16H.
[5]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-21 AND SER-288, MASS SPECTROMETRY.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13; SER-18; SER-21; TYR-240; SER-288 AND SER-343, MASS SPECTROMETRY.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-97, MASS SPECTROMETRY.
[9]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-188.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M55268 mRNA. Translation: AAA51548.1.
BC008812 mRNA. Translation: AAH08812.1.

IPI

IPI00020602.

PIR

B35838.

RefSeq

NP_001887.1.

UniGene

Hs.82201

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3E3B	X-ray	3.20	X	1-334	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-318N.

IntAct

P19784. 7 interactions.

STRING

P19784.

PTM databases

PhosphoSite

P19784.

2-D gel databases

SWISS-2DPAGE

P19784.

Proteomic databases

PeptideAtlas

P19784.

PRIDE

P19784.

Genome annotation databases

Ensembl

ENST00000262506; ENSP00000262506; ENSG00000070770; Homo sapiens. [Genome view]

GeneID

1459.

KEGG

hsa:1459.

UCSC

uc002enc.1. human.

Organism-specific databases

CTD

1459.

GeneCards

GC16M056749.

H-InvDB

HIX0013086.

HGNC

HGNC:2459. CSNK2A2.

MIM

115442. gene.

PharmGKB

PA26959.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16169.

HOGENOM

HBG755340.

HOVERGEN

P19784.

InParanoid

P19784.

OMA

PSWGNQD.

OrthoDB

EOG9GF60S.

PhylomeDB

P19784.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

Pathway_Interaction_DB

nfkappabatypicalpathway. Atypical NF-kappaB pathway.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Gene expression databases

ArrayExpress

P19784.

Bgee

P19784.

CleanEx

HS_CSNK2A2.

Genevestigator

P19784.

GermOnline

ENSG00000070770. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

5997.

SOURCE

Search...

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Entry information

Entry name

CSK22_HUMAN

Accession

Primary (citable) accession number: P19784

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	February 9, 2010
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents