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Protein

Casein kinase II subunit alpha

Gene

CSNK2A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation. Plays an important role in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-90' which is pivotal for its interaction with CLOCK and which controls CLOCK nuclear entry (PubMed:11239457, PubMed:11704824, PubMed:16193064, PubMed:19188443, PubMed:20625391, PubMed:22406621). Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma tissue (PubMed:24962073).7 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Enzyme regulationi

Constitutively active protein kinase whose activity is not directly affected by phosphorylation. Seems to be regulated by level of expression and localization.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei68ATPPROSITE-ProRule annotation1
Active sitei156Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi45 – 53ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • Hsp90 protein binding Source: UniProtKB
  • kinase activity Source: ParkinsonsUK-UCL
  • protein N-terminus binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • chaperone-mediated protein folding Source: UniProtKB
  • mitotic spindle checkpoint Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • positive regulation of cell growth Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of protein catabolic process Source: UniProtKB
  • positive regulation of Wnt signaling pathway Source: UniProtKB
  • protein folding Source: Reactome
  • protein phosphorylation Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • rhythmic process Source: UniProtKB-KW
  • signal transduction Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Biological rhythms, Cell cycle, Transcription, Transcription regulation, Wnt signaling pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS02228-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-1483191. Synthesis of PC.
R-HSA-201688. WNT mediated activation of DVL.
R-HSA-2514853. Condensation of Prometaphase Chromosomes.
R-HSA-445144. Signal transduction by L1.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
SignaLinkiP68400.
SIGNORiP68400.

Names & Taxonomyi

Protein namesi
Recommended name:
Casein kinase II subunit alpha (EC:2.7.11.1)
Short name:
CK II alpha
Gene namesi
Name:CSNK2A1
Synonyms:CK2A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:2457. CSNK2A1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • NuRD complex Source: BHF-UCL
  • plasma membrane Source: ProtInc
  • Sin3 complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi1457.
OpenTargetsiENSG00000101266.
PharmGKBiPA26957.

Chemistry databases

ChEMBLiCHEMBL3629.
GuidetoPHARMACOLOGYi1549.

Polymorphism and mutation databases

BioMutaiCSNK2A1.
DMDMi55977123.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000858831 – 391Casein kinase II subunit alphaAdd BLAST391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei344Phosphothreonine; by CDK11 Publication1
Modified residuei360Phosphothreonine; by CDK11 Publication1
Modified residuei362Phosphoserine; by CDK11 Publication1
Modified residuei370Phosphoserine; by CDK1Combined sources1 Publication1

Post-translational modificationi

Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in prophase and metaphase and dephosphorylated during anaphase. Phosphorylation does not directly affect casein kinase 2 activity, but may contribute to its regulation by forming binding sites for interacting proteins and/or targeting it to different compartments.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP68400.
MaxQBiP68400.
PaxDbiP68400.
PeptideAtlasiP68400.
PRIDEiP68400.

PTM databases

iPTMnetiP68400.
PhosphoSitePlusiP68400.
SwissPalmiP68400.

Miscellaneous databases

PMAP-CutDBB4DYS6.

Expressioni

Tissue specificityi

Expressed in gastric carcinoma tissue and the expression gradually increases with the progression of the carcinoma (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000101266.
CleanExiHS_CSNK2A1.
ExpressionAtlasiP68400. baseline and differential.
GenevisibleiP68400. HS.

Organism-specific databases

HPAiCAB020680.

Interactioni

Subunit structurei

Heterotetramer composed of two catalytic subunits (alpha chain and/or alpha' chain) and two regulatory subunits (beta chains). The tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation. Interacts with RNPS1. Interacts with SNAI1. Interacts with PML (isoform PML-12). Interacts with CCAR2.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBX4O00257-32EBI-347804,EBI-4392727
CSNK2A2P197846EBI-347804,EBI-347451
CSNK2BP6787017EBI-347804,EBI-348169
EIF3JO758222EBI-347804,EBI-366647
HDAC1Q135472EBI-347804,EBI-301834
KIF5CO602824EBI-347804,EBI-717170
MAGEA11P43364-23EBI-347804,EBI-10178634
NFYAP235113EBI-347804,EBI-389739
PMLP295902EBI-347804,EBI-295890
RNF111Q6ZNA44EBI-347804,EBI-2129175
RNF2Q994963EBI-347804,EBI-722416
SIRT1Q96EB64EBI-347804,EBI-1802965
SLC39A7Q925044EBI-347804,EBI-1051105
SSRP1Q089452EBI-347804,EBI-353771
STAC3Q96MF25EBI-347804,EBI-745680
SURF6O756832EBI-347804,EBI-2691252
THAP1Q9NVV93EBI-347804,EBI-741515
TP53P046372EBI-347804,EBI-366083

GO - Molecular functioni

  • Hsp90 protein binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107841. 434 interactors.
DIPiDIP-32682N.
IntActiP68400. 271 interactors.
MINTiMINT-142347.
STRINGi9606.ENSP00000217244.

Chemistry databases

BindingDBiP68400.

Structurei

Secondary structure

1391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 12Combined sources3
Turni13 – 18Combined sources6
Helixi21 – 24Combined sources4
Helixi26 – 28Combined sources3
Helixi36 – 38Combined sources3
Beta strandi39 – 47Combined sources9
Beta strandi49 – 58Combined sources10
Turni59 – 61Combined sources3
Beta strandi64 – 70Combined sources7
Turni72 – 74Combined sources3
Helixi75 – 88Combined sources14
Beta strandi97 – 102Combined sources6
Turni104 – 106Combined sources3
Beta strandi107 – 114Combined sources8
Turni118 – 120Combined sources3
Helixi121 – 124Combined sources4
Helixi125 – 127Combined sources3
Helixi130 – 149Combined sources20
Helixi159 – 161Combined sources3
Beta strandi162 – 165Combined sources4
Helixi166 – 168Combined sources3
Beta strandi170 – 173Combined sources4
Helixi176 – 178Combined sources3
Helixi195 – 197Combined sources3
Helixi200 – 203Combined sources4
Helixi212 – 227Combined sources16
Beta strandi230 – 233Combined sources4
Helixi238 – 249Combined sources12
Helixi251 – 261Combined sources11
Helixi267 – 269Combined sources3
Turni270 – 272Combined sources3
Helixi281 – 284Combined sources4
Turni287 – 289Combined sources3
Helixi290 – 292Combined sources3
Helixi295 – 304Combined sources10
Helixi309 – 311Combined sources3
Helixi315 – 318Combined sources4
Helixi322 – 324Combined sources3
Helixi325 – 331Combined sources7
Beta strandi333 – 335Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JWHX-ray3.10A/B1-337[»]
1NA7X-ray2.40A1-329[»]
1PJKX-ray2.50A2-335[»]
2PVRX-ray1.60A2-335[»]
2ZJWX-ray2.40A1-335[»]
3AMYX-ray2.30A1-335[»]
3AT2X-ray1.60A1-335[»]
3AT3X-ray2.60A1-335[»]
3AT4X-ray2.20A1-335[»]
3AXWX-ray2.50A1-335[»]
3BQCX-ray1.50A1-335[»]
3C13X-ray1.95A1-335[»]
3FWQX-ray2.30A/B1-335[»]
3H30X-ray1.56A/B1-334[»]
3JUHX-ray1.66A/B1-335[»]
3MB6X-ray1.75A1-331[»]
3MB7X-ray1.65A1-331[»]
3NGAX-ray2.71A/B1-333[»]
3NSZX-ray1.30A2-331[»]
3OWJX-ray1.85A1-331[»]
3OWKX-ray1.80A1-331[»]
3OWLX-ray2.10A1-331[»]
3PE1X-ray1.60A1-337[»]
3PE2X-ray1.90A1-337[»]
3PE4X-ray1.95B/D340-352[»]
3Q04X-ray1.80A3-330[»]
3Q9WX-ray1.70A1-336[»]
3Q9XX-ray2.20A/B1-336[»]
3Q9YX-ray1.80A1-336[»]
3Q9ZX-ray2.20A/B1-336[»]
3QA0X-ray2.50A/B1-336[»]
3R0TX-ray1.75A1-337[»]
3RPSX-ray2.30A/B1-335[»]
3TAXX-ray1.88B/D340-352[»]
3U4UX-ray2.20A1-333[»]
3U87X-ray2.90A/B1-325[»]
3U9CX-ray3.20A/B1-335[»]
3W8LX-ray2.40A/B1-335[»]
3WARX-ray1.04A1-335[»]
3WIKX-ray2.00A1-335[»]
3WILX-ray2.90A1-335[»]
3WOWX-ray2.50A1-335[»]
4DGLX-ray3.00C/D1-335[»]
4FBXX-ray2.33A1-335[»]
4GRBX-ray2.15A1-333[»]
4GUBX-ray2.20A1-333[»]
4GYWX-ray1.70B/D340-352[»]
4GYYX-ray1.85B/D340-352[»]
4GZ3X-ray1.90B/D340-352[»]
4IB5X-ray2.20A/B/C1-335[»]
4KWPX-ray1.25A1-336[»]
4MD7X-ray3.10E/F/G/H1-391[»]
4MD8X-ray3.30E/F/G/H1-391[»]
4MD9X-ray3.50E/F/G/H/K/L/M/P1-336[»]
4NH1X-ray3.30A/B1-335[»]
4RLLX-ray1.85A1-335[»]
4UB7X-ray2.10A1-335[»]
4UBAX-ray3.00A/B1-335[»]
5B0XX-ray2.30A1-335[»]
5CLPX-ray1.68A/B2-329[»]
5CQUX-ray2.35A1-335[»]
5CQWX-ray2.65A/B1-335[»]
5CS6X-ray1.88A/B2-329[»]
5CSHX-ray1.59A/B2-329[»]
5CSPX-ray1.50A2-329[»]
5CSVX-ray1.38A2-329[»]
5CU3X-ray1.79A/B2-329[»]
5CU4X-ray1.56A2-329[»]
5CU6X-ray1.36A2-329[»]
5CVFX-ray1.63A2-329[»]
5CVGX-ray1.25A2-329[»]
5CVHX-ray1.85A/B2-329[»]
5H8BX-ray2.55A/B1-333[»]
5H8EX-ray2.15A/B1-333[»]
5H8GX-ray2.00A1-333[»]
5HGVX-ray2.05B/D340-352[»]
ProteinModelPortaliP68400.
SMRiP68400.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68400.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 324Protein kinasePROSITE-ProRule annotationAdd BLAST286

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni36 – 41Interaction with beta subunitBy similarity6

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CK2 subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0668. Eukaryota.
ENOG410XNPP. LUCA.
GeneTreeiENSGT00390000004215.
HOGENOMiHOG000233021.
HOVERGENiHBG107282.
InParanoidiP68400.
KOiK03097.
PhylomeDBiP68400.
TreeFamiTF300483.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P68400-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY
60 70 80 90 100
SEVFEAINIT NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI
110 120 130 140 150
VKDPVSRTPA LVFEHVNNTD FKQLYQTLTD YDIRFYMYEI LKALDYCHSM
160 170 180 190 200
GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE FYHPGQEYNV RVASRYFKGP
210 220 230 240 250
ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD QLVRIAKVLG
260 270 280 290 300
TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF
310 320 330 340 350
LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN
360 370 380 390
MMSGISSVPT PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ Q
Length:391
Mass (Da):45,144
Last modified:November 23, 2004 - v1
Checksum:iD3B6F5D13FF7422D
GO
Isoform 2 (identifier: P68400-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-136: Missing.

Show »
Length:255
Mass (Da):29,181
Checksum:iABCEE52F34E7431B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti128L → F in CAA49758 (PubMed:8420794).Curated1
Sequence conflicti256D → G in CAA49758 (PubMed:8420794).Curated1
Sequence conflicti287S → R in CAA49758 (PubMed:8420794).Curated1
Sequence conflicti351M → V in CAA49758 (PubMed:8420794).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0419251 – 136Missing in isoform 2. 1 PublicationAdd BLAST136

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02853 mRNA. Translation: AAA56821.1.
M55265 mRNA. Translation: AAA35503.1.
S53149 mRNA. Translation: ABB72474.1.
X70251 Genomic DNA. Translation: CAA49758.1.
AK302583 mRNA. Translation: BAG63838.1.
BT019792 mRNA. Translation: AAV38595.1.
AB451279 mRNA. Translation: BAG70093.1.
AL049761 Genomic DNA. Translation: CAB65624.1.
CH471133 Genomic DNA. Translation: EAX10665.1.
CH471133 Genomic DNA. Translation: EAX10666.1.
CH471133 Genomic DNA. Translation: EAX10667.1.
CH471133 Genomic DNA. Translation: EAX10668.1.
CH471133 Genomic DNA. Translation: EAX10669.1.
BC011668 mRNA. Translation: AAH11668.1.
BC053532 mRNA. Translation: AAH53532.1.
BC071167 mRNA. Translation: AAH71167.1.
CCDSiCCDS13003.1. [P68400-1]
CCDS13004.1. [P68400-2]
PIRiA30319.
RefSeqiNP_001886.1. NM_001895.3. [P68400-1]
NP_808227.1. NM_177559.2. [P68400-1]
NP_808228.1. NM_177560.2. [P68400-2]
UniGeneiHs.644056.
Hs.654675.
Hs.741126.

Genome annotation databases

EnsembliENST00000217244; ENSP00000217244; ENSG00000101266. [P68400-1]
ENST00000349736; ENSP00000339247; ENSG00000101266. [P68400-1]
ENST00000400217; ENSP00000383076; ENSG00000101266. [P68400-2]
GeneIDi1457.
KEGGihsa:1457.
UCSCiuc002wdw.2. human. [P68400-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02853 mRNA. Translation: AAA56821.1.
M55265 mRNA. Translation: AAA35503.1.
S53149 mRNA. Translation: ABB72474.1.
X70251 Genomic DNA. Translation: CAA49758.1.
AK302583 mRNA. Translation: BAG63838.1.
BT019792 mRNA. Translation: AAV38595.1.
AB451279 mRNA. Translation: BAG70093.1.
AL049761 Genomic DNA. Translation: CAB65624.1.
CH471133 Genomic DNA. Translation: EAX10665.1.
CH471133 Genomic DNA. Translation: EAX10666.1.
CH471133 Genomic DNA. Translation: EAX10667.1.
CH471133 Genomic DNA. Translation: EAX10668.1.
CH471133 Genomic DNA. Translation: EAX10669.1.
BC011668 mRNA. Translation: AAH11668.1.
BC053532 mRNA. Translation: AAH53532.1.
BC071167 mRNA. Translation: AAH71167.1.
CCDSiCCDS13003.1. [P68400-1]
CCDS13004.1. [P68400-2]
PIRiA30319.
RefSeqiNP_001886.1. NM_001895.3. [P68400-1]
NP_808227.1. NM_177559.2. [P68400-1]
NP_808228.1. NM_177560.2. [P68400-2]
UniGeneiHs.644056.
Hs.654675.
Hs.741126.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JWHX-ray3.10A/B1-337[»]
1NA7X-ray2.40A1-329[»]
1PJKX-ray2.50A2-335[»]
2PVRX-ray1.60A2-335[»]
2ZJWX-ray2.40A1-335[»]
3AMYX-ray2.30A1-335[»]
3AT2X-ray1.60A1-335[»]
3AT3X-ray2.60A1-335[»]
3AT4X-ray2.20A1-335[»]
3AXWX-ray2.50A1-335[»]
3BQCX-ray1.50A1-335[»]
3C13X-ray1.95A1-335[»]
3FWQX-ray2.30A/B1-335[»]
3H30X-ray1.56A/B1-334[»]
3JUHX-ray1.66A/B1-335[»]
3MB6X-ray1.75A1-331[»]
3MB7X-ray1.65A1-331[»]
3NGAX-ray2.71A/B1-333[»]
3NSZX-ray1.30A2-331[»]
3OWJX-ray1.85A1-331[»]
3OWKX-ray1.80A1-331[»]
3OWLX-ray2.10A1-331[»]
3PE1X-ray1.60A1-337[»]
3PE2X-ray1.90A1-337[»]
3PE4X-ray1.95B/D340-352[»]
3Q04X-ray1.80A3-330[»]
3Q9WX-ray1.70A1-336[»]
3Q9XX-ray2.20A/B1-336[»]
3Q9YX-ray1.80A1-336[»]
3Q9ZX-ray2.20A/B1-336[»]
3QA0X-ray2.50A/B1-336[»]
3R0TX-ray1.75A1-337[»]
3RPSX-ray2.30A/B1-335[»]
3TAXX-ray1.88B/D340-352[»]
3U4UX-ray2.20A1-333[»]
3U87X-ray2.90A/B1-325[»]
3U9CX-ray3.20A/B1-335[»]
3W8LX-ray2.40A/B1-335[»]
3WARX-ray1.04A1-335[»]
3WIKX-ray2.00A1-335[»]
3WILX-ray2.90A1-335[»]
3WOWX-ray2.50A1-335[»]
4DGLX-ray3.00C/D1-335[»]
4FBXX-ray2.33A1-335[»]
4GRBX-ray2.15A1-333[»]
4GUBX-ray2.20A1-333[»]
4GYWX-ray1.70B/D340-352[»]
4GYYX-ray1.85B/D340-352[»]
4GZ3X-ray1.90B/D340-352[»]
4IB5X-ray2.20A/B/C1-335[»]
4KWPX-ray1.25A1-336[»]
4MD7X-ray3.10E/F/G/H1-391[»]
4MD8X-ray3.30E/F/G/H1-391[»]
4MD9X-ray3.50E/F/G/H/K/L/M/P1-336[»]
4NH1X-ray3.30A/B1-335[»]
4RLLX-ray1.85A1-335[»]
4UB7X-ray2.10A1-335[»]
4UBAX-ray3.00A/B1-335[»]
5B0XX-ray2.30A1-335[»]
5CLPX-ray1.68A/B2-329[»]
5CQUX-ray2.35A1-335[»]
5CQWX-ray2.65A/B1-335[»]
5CS6X-ray1.88A/B2-329[»]
5CSHX-ray1.59A/B2-329[»]
5CSPX-ray1.50A2-329[»]
5CSVX-ray1.38A2-329[»]
5CU3X-ray1.79A/B2-329[»]
5CU4X-ray1.56A2-329[»]
5CU6X-ray1.36A2-329[»]
5CVFX-ray1.63A2-329[»]
5CVGX-ray1.25A2-329[»]
5CVHX-ray1.85A/B2-329[»]
5H8BX-ray2.55A/B1-333[»]
5H8EX-ray2.15A/B1-333[»]
5H8GX-ray2.00A1-333[»]
5HGVX-ray2.05B/D340-352[»]
ProteinModelPortaliP68400.
SMRiP68400.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107841. 434 interactors.
DIPiDIP-32682N.
IntActiP68400. 271 interactors.
MINTiMINT-142347.
STRINGi9606.ENSP00000217244.

Chemistry databases

BindingDBiP68400.
ChEMBLiCHEMBL3629.
GuidetoPHARMACOLOGYi1549.

PTM databases

iPTMnetiP68400.
PhosphoSitePlusiP68400.
SwissPalmiP68400.

Polymorphism and mutation databases

BioMutaiCSNK2A1.
DMDMi55977123.

Proteomic databases

EPDiP68400.
MaxQBiP68400.
PaxDbiP68400.
PeptideAtlasiP68400.
PRIDEiP68400.

Protocols and materials databases

DNASUi1457.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217244; ENSP00000217244; ENSG00000101266. [P68400-1]
ENST00000349736; ENSP00000339247; ENSG00000101266. [P68400-1]
ENST00000400217; ENSP00000383076; ENSG00000101266. [P68400-2]
GeneIDi1457.
KEGGihsa:1457.
UCSCiuc002wdw.2. human. [P68400-1]

Organism-specific databases

CTDi1457.
DisGeNETi1457.
GeneCardsiCSNK2A1.
HGNCiHGNC:2457. CSNK2A1.
HPAiCAB020680.
MIMi115440. gene.
neXtProtiNX_P68400.
OpenTargetsiENSG00000101266.
PharmGKBiPA26957.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0668. Eukaryota.
ENOG410XNPP. LUCA.
GeneTreeiENSGT00390000004215.
HOGENOMiHOG000233021.
HOVERGENiHBG107282.
InParanoidiP68400.
KOiK03097.
PhylomeDBiP68400.
TreeFamiTF300483.

Enzyme and pathway databases

BioCyciZFISH:HS02228-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-1483191. Synthesis of PC.
R-HSA-201688. WNT mediated activation of DVL.
R-HSA-2514853. Condensation of Prometaphase Chromosomes.
R-HSA-445144. Signal transduction by L1.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
SignaLinkiP68400.
SIGNORiP68400.

Miscellaneous databases

ChiTaRSiCSNK2A1. human.
EvolutionaryTraceiP68400.
GeneWikiiCasein_kinase_2,_alpha_1.
GenomeRNAii1457.
PMAP-CutDBB4DYS6.
PROiP68400.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101266.
CleanExiHS_CSNK2A1.
ExpressionAtlasiP68400. baseline and differential.
GenevisibleiP68400. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCSK21_HUMAN
AccessioniPrimary (citable) accession number: P68400
Secondary accession number(s): B4DYS6
, D3DVV8, P19138, P20426, Q14013, Q5U065
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 23, 2004
Last modified: November 30, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Miscellaneous

Can use both ATP and GTP as phosphoryl donors. Phosphorylation by casein kinase 2 has been estimated to represent up to one quarter of the eukaryotic phosphoproteome. Casein kinase 2 has been found to be increased at protein level and up-regulated at the level of enzyme activity in the majority of cancers. However, elevated levels of casein kinase 2 are present in certain normal organs such as brain and testes.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.