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UniProtKB/Swiss-Prot entry P68400


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

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Entry information
Entry name CSK21_HUMAN
Primary accession number P68400
Secondary accession numbers P19138 P20426 Q14013
Integrated into Swiss-Prot on November 23, 2004
Sequence was last modified on November 23, 2004 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 55)
Name and origin of the protein
Protein name Casein kinase II subunit alpha
Synonyms CK II
EC 2.7.11.1
Gene name
Name: CSNK2A1
Synonyms: CK2A1
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].
DOI=10.1021/bi00435a066; PubMed=2752008 [NCBI, ExPASy, EBI, Israel, Japan]
Meisner H., Heller-Harrison R., Buxton J., Czech M.P.;
"Molecular cloning of the human casein kinase II alpha subunit.";
Biochemistry 28:4072-4076(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00488a034; PubMed=2174700 [NCBI, ExPASy, EBI, Israel, Japan]
Lozeman F.J., Litchfield D.W., Piening C., Takio K., Walsh K.A., Krebs E.G.;
"Isolation and characterization of human cDNA clones encoding the alpha and the alpha' subunits of casein kinase II.";
Biochemistry 29:8436-8447(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0014-5793(93)81197-8; PubMed=8420794 [NCBI, ExPASy, EBI, Israel, Japan]
Devilat I., Carvallo P.;
"Structure and sequence of an intronless gene for human casein kinase II-alpha subunit.";
FEBS Lett. 316:114-118(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, Muscle, and Uterus;
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).
[6]
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).
[7]
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).
[8]
INTERACTION WITH RNPS1.
DOI=10.1128/MCB.25.4.1446-1457.2005; PubMed=15684395 [NCBI, ExPASy, EBI, Israel, Japan]
Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A., Suzuki H., Endo H., Kidd V.J., Mayeda A.;
"Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 phosphorylation.";
Mol. Cell. Biol. 25:1446-1457(2005).
[9]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337, 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).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-329.
DOI=10.1107/S0907444903018900; PubMed=14646071 [NCBI, ExPASy, EBI, Israel, Japan]
Pechkova E., Zanotti G., Nicolini C.;
"Three-dimensional atomic structure of a catalytic subunit mutant of human protein kinase CK2.";
Acta Crystallogr. D 59:2133-2139(2003).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-335.
DOI=10.1016/S0022-2836(03)00638-7; PubMed=12860116 [NCBI, ExPASy, EBI, Israel, Japan]
Ermakova I., Boldyreff B., Issinger O.G., Niefind K.;
"Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit.";
J. Mol. Biol. 330:925-934(2003).
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
J02853; AAA56821.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M55265; AAA35503.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X70251; CAA49758.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL049761; CAB65624.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011668; AAH11668.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC053532; AAH53532.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC071167; AAH71167.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A30319; A30319.
RefSeq NP_001886.1; -.
NP_808227.1; -.
NP_808228.1; -.
UniGene Hs.654675
3D structure databases
PDB
1JWH; X-ray; 3.10 A; A/B=1-337.[ExPASy / RCSB / EBI]
1NA7; X-ray; 2.40 A; A=1-329.[ExPASy / RCSB / EBI]
1PJK; X-ray; 2.50 A; A=2-335.[ExPASy / RCSB / EBI]
1YMI; X-ray; 1.66 A; A=2-335.[ExPASy / RCSB / EBI]
2PVR; X-ray; 1.60 A; A=2-335.[ExPASy / RCSB / EBI]
2RKP; X-ray; 1.56 A; A=1-335.[ExPASy / RCSB / EBI]
3BQC; X-ray; 1.50 A; A=1-335.[ExPASy / RCSB / EBI]
3BW5; X-ray; 1.66 A; A=1-335.[ExPASy / RCSB / EBI]
3C13; X-ray; 1.95 A; A=1-335.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1JWH; -.
1NA7; -.
1PJK; -.
1YMI; -.
2PVR; -.
2RKP; -.
3BQC; -.
3BW5; -.
3C13; -.
ModBase P68400.
Protein-protein interaction databases
IntAct P68400; -.
PTM databases
PhosphoSite P68400; -.
Organism-specific databases
H-InvDB HIX0015555; -.
HGNC HGNC:2457; CSNK2A1.
GenAtlas CSNK2A1.
MIM 115440; gene. [NCBI / EBI]
PharmGKB PA26957; -.
GeneCards P68400.
Gene expression databases
ArrayExpress P68400; -.
CleanEx HS_CSNK2A1; -.
GermOnline ENSG00000101266; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (traceable author statement from ProtInc).
GO:0005886; Cellular component: plasma membrane (traceable author statement from ProtInc).
GO:0004682; Molecular function: protein kinase CK2 activity (traceable author statement from ProtInc).
GO:0047485; Molecular function: protein N-terminus binding (inferred from physical interaction from UniProtKB).
GO:0006468; Biological process: protein amino acid phosphorylation (traceable author statement from ProtInc).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P68400.
Genome annotation databases
Ensembl ENSG00000101266; Homo sapiens. [Contig view]
GeneID 1457; -.
KEGG hsa:1457; -.
Phylogenomic databases
HOVERGEN P68400; -.
Other
LinkHub P68400; -.
SOURCE CSNK2A1; Homo sapiens.
ProtoNet P68400.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; ATP-binding; Kinase; Nucleotide-binding; Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   391  391     Casein kinase II subunit alpha. PRO_0000085883
DOMAIN   39   324  286     Protein kinase. 
NP_BIND   45    53  9     ATP (By similarity). 
ACT_SITE   156   156        Proton acceptor. 
BINDING   68    68        ATP (By similarity). 
CONFLICT   128   128        L -> F (in Ref. 3; CAA49758). 
CONFLICT   256   256        D -> G (in Ref. 3; CAA49758). 
CONFLICT   287   287        S -> R (in Ref. 3; CAA49758). 
CONFLICT   351   351        M -> V (in Ref. 3; CAA49758). 
STRAND   10    12  3      
HELIX   15    18  4      
HELIX   21    24  4      
HELIX   26    28  3      
HELIX   36    38  3      
STRAND   39    47  9      
STRAND   49    58  10      
TURN   59    61  3      
STRAND   64    70  7      
HELIX   75    87  13      
STRAND   97   102  6      
TURN   104   106  3      
STRAND   108   113  6      
HELIX   121   124  4      
HELIX   130   149  20      
HELIX   159   161  3      
STRAND   162   165  4      
TURN   166   169  4      
STRAND   170   173  4      
HELIX   195   197  3      
HELIX   200   203  4      
HELIX   212   227  16      
STRAND   230   233  4      
HELIX   238   249  12      
HELIX   252   260  9      
HELIX   267   270  4      
TURN   281   284  4      
TURN   287   289  3      
HELIX   290   292  3      
HELIX   295   304  10      
HELIX   315   319  5      
HELIX   322   324  3      
Sequence information
Length: 391 AA [This is the length of the unprocessed precursor] Molecular weight: 45144 Da [This is the MW of the unprocessed precursor] CRC64: D3B6F5D13FF7422D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY SEVFEAINIT 

        70         80         90        100        110        120 
NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD 

       130        140        150        160        170        180 
FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE 

       190        200        210        220        230        240 
FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD 

       250        260        270        280        290        300 
QLVRIAKVLG TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF 

       310        320        330        340        350        360 
LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN MMSGISSVPT 

       370        380        390 
PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ Q 

P68400 in FASTA format

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