ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P67870


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CSK2B_HUMAN
Primary accession number P67870
Secondary accession numbers P07312 P13862 Q4VX47
Integrated into Swiss-Prot on October 11, 2004
Sequence was last modified on October 11, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 57)
Name and origin of the protein
Protein name Casein kinase II subunit beta
Synonyms CK II beta
Phosvitin
G5a
Gene name
Name: CSNK2B
Synonyms: CK2N, G5A
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2666134 [NCBI, ExPASy, EBI, Israel, Japan]
Jakobi R., Voss H., Pyerin W.;
"Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta.";
Eur. J. Biochem. 183:227-233(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0921-8777(90)90036-5; PubMed=1694965 [NCBI, ExPASy, EBI, Israel, Japan]
Teitz T., Eli D., Penner M., Bakhanashvili M., Naiman T., Timme T.L., Wood C.M., Moses R.E., Canaani D.;
"Expression of the cDNA for the beta subunit of human casein kinase II confers partial UV resistance on xeroderma pigmentosum cells.";
Mutat. Res. 236:85-97(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00449a014; PubMed=2513884 [NCBI, ExPASy, EBI, Israel, Japan]
Heller-Harrison R.A., Meisner H., Czech M.P.;
"Cloning and characterization of a cDNA encoding the beta subunit of human casein kinase II.";
Biochemistry 28:9053-9058(1989).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1856204 [NCBI, ExPASy, EBI, Israel, Japan]
Voss A., Wirkner U., Jacobi R., Hewitt N., Schwager C., Zimmermann J., Ansorge W., Pyerin W.;
"Structure of the gene encoding human casein kinase II subunit beta.";
J. Biol. Chem. 266:13706-13711(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi025791r; PubMed=12102635 [NCBI, ExPASy, EBI, Israel, Japan]
Singh L.S., Kalafatis M.;
"Sequencing of full-length cDNA encoding the alpha and beta subunits of human casein kinase II from human platelets and megakaryocytic cells. Expression of the casein kinase IIalpha intronless gene in a megakaryocytic cell line.";
Biochemistry 41:8935-8940(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1101/gr.1736803; PubMed=14656967 [NCBI, ExPASy, EBI, Israel, Japan]
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Shiina S., Tamiya G., Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PHOSPHORYLATION.
PubMed=2300566 [NCBI, ExPASy, EBI, Israel, Japan]
Ackerman P., Glover C.V., Osheroff N.;
"Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its beta subunit.";
Proc. Natl. Acad. Sci. U.S.A. 87:821-825(1990).
[13]
INTERACTION WITH CD163.
DOI=10.1002/1521-4141(200104)31:4<999::AID-IMMU999>3.0.CO;2-R; PubMed=11298324 [NCBI, ExPASy, EBI, Israel, Japan]
Ritter M., Buechler C., Kapinsky M., Schmitz G.;
"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. 31:999-1009(2001).
[14]
FUNCTION, AND INTERACTION WITH SSRP1 AND SUPT16H.
DOI=10.1016/S1097-2765(01)00176-9; PubMed=11239457 [NCBI, ExPASy, EBI, Israel, Japan]
Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H.;
"A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1.";
Mol. Cell 7:283-292(2001).
[15]
INTERACTION WITH SSRP1 AND SUPT16H.
DOI=10.1074/jbc.M209820200; PubMed=12393879 [NCBI, ExPASy, EBI, Israel, Japan]
Keller D.M., Lu H.;
"p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex.";
J. Biol. Chem. 277:50206-50213(2002).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-3; SER-4 AND SER-209, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[17]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), AND SUBUNIT.
DOI=10.1107/S0907444900013627; PubMed=11092945 [NCBI, ExPASy, EBI, Israel, Japan]
Niefind K., Guerra B., Ermakowa I., Issinger O.G.;
"Crystallization and preliminary characterization of crystals of human protein kinase CK2.";
Acta Crystallogr. D 56:1680-1684(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X16937; CAA34811.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X16312; CAA34379.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M30448; AAA52123.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X57152; CAA40442.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY113186; AAM50092.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541699; CAG46500.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF129756; AAD18081.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000025; BAB63386.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ314868; ABC40727.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662899; CAI96141.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL662899; CAI18393.2; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL670886; CAI17800.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL805934; CAI18523.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC112017; AAI12018.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC112019; AAI12020.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39459; A39459.
RefSeq NP_001311.3; -.
UniGene Hs.73527
3D structure databases
PDB
1DS5; X-ray; 3.16 A; E/F/G/H=181-203.[ExPASy / RCSB / EBI]
1JWH; X-ray; 3.10 A; C/D=1-215.[ExPASy / RCSB / EBI]
1QF8; X-ray; 1.74 A; A/B=1-182.[ExPASy / RCSB / EBI]
3EED; X-ray; 2.80 A; A/B=1-193.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DS5; -.
1JWH; -.
1QF8; -.
3EED; -.
ModBase P67870.
Protein-protein interaction databases
IntAct P67870; -.
PTM databases
PhosphoSite P67870; -.
Organism-specific databases
H-InvDB HIX0032813; -.
HIX0057736; -.
HIX0057989; -.
HGNC HGNC:2460; CSNK2B.
GenAtlas CSNK2B.
HPA CAB013087; -.
CAB016059; -.
HPA005944; -.
MIM 115441; gene. [NCBI / EBI]
PharmGKB PA26960; -.
GeneCards P67870.
Gene expression databases
ArrayExpress P67870; -.
CleanEx HS_CSNK2B; -.
GermOnline ENSG00000204435; Homo sapiens.
Ontologies
GO
GO:0005956; Cellular component: protein kinase CK2 complex (non-traceable author statement from UniProtKB).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0019904; Molecular function: protein domain specific binding (inferred from physical interaction from UniProtKB).
GO:0008605; Molecular function: protein kinase CK2 regulator activity (non-traceable author statement from UniProtKB).
GO:0004674; Molecular function: protein serine/threonine kinase activity (traceable author statement from UniProtKB).
GO:0016055; Biological process: Wnt receptor signaling pathway (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016149; Casein_kin_II_reg-sub_a-hlx.
IPR016150; Casein_kin_II_reg-sub_b-sht.
IPR000704; Casein_kinase_II_reg-sub.
Graphical view of domain structure.
Gene3D G3DSA:1.10.1820.10; Casein_kin_II_reg-sub_a-hlx; 1.
G3DSA:2.20.25.20; Casein_kin_II_reg-sub_b-sht; 1.
PANTHER PTHR11740; CAS_kinase_II; 1.
Pfam PF01214; CK_II_beta; 1.
Pfam graphical view of domain structure.
PRINTS PR00472; CASNKINASEII.
ProDom PD003829; CAS_kinase_II; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS01101; CK2_BETA; 1.
ProtoNet P67870.
Genome annotation databases
Ensembl ENSG00000204435; Homo sapiens. [Contig view]
ENSG00000206300; Homo sapiens. [Contig view]
ENSG00000206406; Homo sapiens. [Contig view]
GeneID 1460; -.
KEGG hsa:1460; -.
Phylogenomic databases
HOGENOM P67870; -.
HOVERGEN P67870; -.
Other
LinkHub P67870; -.
NextBio 6001; -.
SOURCE CSNK2B; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Phosphoprotein; Wnt signaling pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   215  215     Casein kinase II subunit beta. PRO_0000068236
COMPBIAS   55    64  10     Asp/Glu-rich (acidic). 
MOD_RES   2     2        Phosphoserine; by autocatalysis. 
MOD_RES   3     3        Phosphoserine. 
MOD_RES   4     4        Phosphoserine. 
MOD_RES   209   209        Phosphoserine. 
CONFLICT   194   194        P -> A (in Ref. 3; AAA52123). 
HELIX   9    15  7      
HELIX   27    31  5      
HELIX   33    36  4      
HELIX   39    41  3      
HELIX   46    53  8      
HELIX   67    87  21      
HELIX   91   102  12      
TURN   103   106  4      
HELIX   112   114  3      
STRAND   120   122  3      
STRAND   134   136  3      
TURN   138   140  3      
HELIX   149   151  3      
HELIX   156   158  3      
HELIX   163   170  8      
HELIX   172   174  3      
STRAND   195   197  3      
Sequence information
Length: 215 AA [This is the length of the unprocessed precursor] Molecular weight: 24942 Da [This is the MW of the unprocessed precursor] CRC64: E465B1E699B0E0EC [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE 

        70         80         90        100        110        120 
ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML 

       130        140        150        160        170        180 
PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA 

       190        200        210 
NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTIR 

P67870 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!