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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.6 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei68 – 681ATPPROSITE-ProRule annotation
Active sitei156 – 1561Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi45 – 539ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  • axon guidance Source: Reactome
  • chaperone-mediated protein folding Source: UniProtKB
  • mitotic cell cycle Source: Reactome
  • 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 phosphorylation Source: UniProtKB
  • 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

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_150260. Condensation of Prometaphase Chromosomes.
REACT_22272. Signal transduction by L1.
REACT_264384. WNT mediated activation of DVL.
SignaLinkiP68400.

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
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:2457. CSNK2A1.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26957.

Polymorphism and mutation databases

BioMutaiCSNK2A1.
DMDMi55977123.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Casein kinase II subunit alphaPRO_0000085883Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei344 – 3441Phosphothreonine; by CDK11 Publication
Modified residuei360 – 3601Phosphothreonine; by CDK11 Publication
Modified residuei362 – 3621Phosphoserine; by CDK11 Publication
Modified residuei370 – 3701Phosphoserine; by CDK12 Publications

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

MaxQBiP68400.
PaxDbiP68400.
PRIDEiP68400.

PTM databases

PhosphoSiteiP68400.

Miscellaneous databases

PMAP-CutDBB4DYS6.

Expressioni

Gene expression databases

BgeeiP68400.
CleanExiHS_CSNK2A1.
ExpressionAtlasiP68400. baseline and differential.
GenevestigatoriP68400.

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).8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBX4O00257-32EBI-347804,EBI-4392727
CSNK2A2P197844EBI-347804,EBI-347451
CSNK2BP6787015EBI-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
SIRT1Q96EB64EBI-347804,EBI-1802965
SLC39A7Q925044EBI-347804,EBI-1051105
SSRP1Q089452EBI-347804,EBI-353771
STAC3Q96MF23EBI-347804,EBI-745680
THAP1Q9NVV93EBI-347804,EBI-741515
TP53P046372EBI-347804,EBI-366083

Protein-protein interaction databases

BioGridi107841. 370 interactions.
DIPiDIP-32682N.
IntActiP68400. 232 interactions.
MINTiMINT-142347.
STRINGi9606.ENSP00000217244.

Structurei

Secondary structure

1
391
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123Combined sources
Turni13 – 186Combined sources
Helixi21 – 244Combined sources
Helixi26 – 283Combined sources
Helixi36 – 383Combined sources
Beta strandi39 – 479Combined sources
Beta strandi49 – 5810Combined sources
Turni59 – 613Combined sources
Beta strandi64 – 707Combined sources
Helixi75 – 8814Combined sources
Beta strandi97 – 1026Combined sources
Turni104 – 1063Combined sources
Beta strandi107 – 1148Combined sources
Helixi121 – 1244Combined sources
Helixi125 – 1273Combined sources
Helixi130 – 14920Combined sources
Helixi159 – 1613Combined sources
Beta strandi162 – 1654Combined sources
Helixi166 – 1683Combined sources
Beta strandi170 – 1734Combined sources
Helixi176 – 1783Combined sources
Helixi195 – 1973Combined sources
Helixi200 – 2034Combined sources
Helixi212 – 22716Combined sources
Beta strandi230 – 2334Combined sources
Helixi238 – 24912Combined sources
Helixi251 – 26111Combined sources
Helixi267 – 2693Combined sources
Turni270 – 2723Combined sources
Helixi281 – 2844Combined sources
Turni287 – 2893Combined sources
Helixi290 – 2923Combined sources
Helixi295 – 30410Combined sources
Helixi309 – 3113Combined sources
Helixi315 – 3184Combined sources
Helixi322 – 3243Combined sources
Helixi325 – 3317Combined sources
Beta strandi333 – 3353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4BXAX-ray2.65A/B1-335[»]
4BXBX-ray2.35A1-335[»]
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[»]
ProteinModelPortaliP68400.
SMRiP68400. Positions 2-359.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68400.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 324286Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni36 – 416Interaction with beta subunitBy similarity

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

eggNOGiCOG0515.
GeneTreeiENSGT00390000004215.
HOGENOMiHOG000233021.
HOVERGENiHBG107282.
InParanoidiP68400.
KOiK03097.
OMAiLYQYIDK.
OrthoDBiEOG7QG446.
PhylomeDBiP68400.
TreeFamiTF300483.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti128 – 1281L → F in CAA49758 (PubMed:8420794).Curated
Sequence conflicti256 – 2561D → G in CAA49758 (PubMed:8420794).Curated
Sequence conflicti287 – 2871S → R in CAA49758 (PubMed:8420794).Curated
Sequence conflicti351 – 3511M → V in CAA49758 (PubMed:8420794).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 136136Missing in isoform 2. 1 PublicationVSP_041925Add
BLAST

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.1. 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
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[»]
4BXAX-ray2.65A/B1-335[»]
4BXBX-ray2.35A1-335[»]
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[»]
ProteinModelPortaliP68400.
SMRiP68400. Positions 2-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107841. 370 interactions.
DIPiDIP-32682N.
IntActiP68400. 232 interactions.
MINTiMINT-142347.
STRINGi9606.ENSP00000217244.

Chemistry

BindingDBiP68400.
ChEMBLiCHEMBL3629.
GuidetoPHARMACOLOGYi1549.

PTM databases

PhosphoSiteiP68400.

Polymorphism and mutation databases

BioMutaiCSNK2A1.
DMDMi55977123.

Proteomic databases

MaxQBiP68400.
PaxDbiP68400.
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.1. human. [P68400-1]

Organism-specific databases

CTDi1457.
GeneCardsiGC20M000459.
HGNCiHGNC:2457. CSNK2A1.
HPAiCAB020680.
MIMi115440. gene.
neXtProtiNX_P68400.
PharmGKBiPA26957.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00390000004215.
HOGENOMiHOG000233021.
HOVERGENiHBG107282.
InParanoidiP68400.
KOiK03097.
OMAiLYQYIDK.
OrthoDBiEOG7QG446.
PhylomeDBiP68400.
TreeFamiTF300483.

Enzyme and pathway databases

BRENDAi2.7.11.1. 2681.
ReactomeiREACT_150260. Condensation of Prometaphase Chromosomes.
REACT_22272. Signal transduction by L1.
REACT_264384. WNT mediated activation of DVL.
SignaLinkiP68400.

Miscellaneous databases

ChiTaRSiCSNK2A1. human.
EvolutionaryTraceiP68400.
GeneWikiiCasein_kinase_2,_alpha_1.
GenomeRNAii1457.
NextBioi5989.
PMAP-CutDBB4DYS6.
PROiP68400.
SOURCEiSearch...

Gene expression databases

BgeeiP68400.
CleanExiHS_CSNK2A1.
ExpressionAtlasiP68400. baseline and differential.
GenevestigatoriP68400.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the human casein kinase II alpha subunit."
    Meisner H., Heller-Harrison R., Buxton J., Czech M.P.
    Biochemistry 28:4072-4076(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Structure and sequence of an intronless gene for human casein kinase II-alpha subunit."
    Devilat I., Carvallo P.
    FEBS Lett. 316:114-118(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "The DNA sequence and comparative analysis of human chromosome 20."
    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.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung, Muscle and Uterus.
  10. "Phosphorylation of casein kinase II by p34cdc2. Identification of phosphorylation sites using phosphorylation site mutants in vitro."
    Bosc D.G., Slominski E., Sichler C., Litchfield D.W.
    J. Biol. Chem. 270:25872-25878(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-344; THR-360; SER-362 AND SER-370.
  11. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H.
  12. "Protein kinase CK2 is involved in G2 arrest and apoptosis following spindle damage in epithelial cells."
    Sayed M., Pelech S., Wong C., Marotta A., Salh B.
    Oncogene 20:6994-7005(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL CYCLE.
  13. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SSRP1 AND SUPT16H.
  14. "Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing procaspase-8."
    Shin S., Lee Y., Kim W., Ko H., Choi H., Kim K.
    EMBO J. 24:3532-3542(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS.
  15. "Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 phosphorylation."
    Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A., Suzuki H., Endo H., Kidd V.J., Mayeda A.
    Mol. Cell. Biol. 25:1446-1457(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNPS1.
  16. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Evidence for regulation of mitotic progression through temporal phosphorylation and dephosphorylation of CK2alpha."
    St-Denis N.A., Derksen D.R., Litchfield D.W.
    Mol. Cell. Biol. 29:2068-2081(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL CYCLE.
  18. "One-thousand-and-one substrates of protein kinase CK2?"
    Meggio F., Pinna L.A.
    FASEB J. 17:349-368(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  19. "Protein kinase CK2 in health and disease: Protein kinase CK2: from structures to insights."
    Niefind K., Raaf J., Issinger O.G.
    Cell. Mol. Life Sci. 66:1800-1816(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON STRUCTURE.
  20. "Protein kinase CK2 in health and disease: From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival."
    St-Denis N.A., Litchfield D.W.
    Cell. Mol. Life Sci. 66:1817-1829(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  21. "Protein kinase CK2 in health and disease: Cellular functions of protein kinase CK2: a dynamic affair."
    Filhol O., Cochet C.
    Cell. Mol. Life Sci. 66:1830-1839(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  22. "Protein kinase CK2 in health and disease: CK2: the kinase controlling the Hsp90 chaperone machinery."
    Miyata Y.
    Cell. Mol. Life Sci. 66:1840-1849(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN REGULATION OF HSP90.
  23. "Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-kappaB signaling: linking development and cancer."
    Dominguez I., Sonenshein G.E., Seldin D.C.
    Cell. Mol. Life Sci. 66:1850-1857(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION IN WNT SIGNALING.
  24. "Phosphorylation of serine 11 and serine 92 as new positive regulators of human Snail1 function: potential involvement of casein kinase-2 and the cAMP-activated kinase protein kinase A."
    MacPherson M.R., Molina P., Souchelnytskyi S., Wernstedt C., Martin-Perez J., Portillo F., Cano A.
    Mol. Biol. Cell 21:244-253(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNAI1.
  25. "Functional polymorphism of the CK2alpha intronless gene plays oncogenic roles in lung cancer."
    Hung M.S., Lin Y.C., Mao J.H., Kim I.J., Xu Z., Yang C.T., Jablons D.M., You L.
    PLoS ONE 5:E11418-E11418(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PML.
  26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA."
    Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A., Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J., Scaglioni P.P.
    Cancer Res. 72:2275-2284(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PML.
  29. "Crystallization and preliminary characterization of crystals of human protein kinase CK2."
    Niefind K., Guerra B., Ermakowa I., Issinger O.G.
    Acta Crystallogr. D 56:1680-1684(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337, SUBUNIT.
  30. "Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme."
    Niefind K., Guerra B., Ermakowa I., Issinger O.G.
    EMBO J. 20:5320-5331(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337 IN COMPLEX WITH CSNK2B, SUBUNIT.
  31. "Three-dimensional atomic structure of a catalytic subunit mutant of human protein kinase CK2."
    Pechkova E., Zanotti G., Nicolini C.
    Acta Crystallogr. D 59:2133-2139(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-329.
  32. "Crystal structure of a C-terminal deletion mutant of human protein kinase CK2 catalytic subunit."
    Ermakova I., Boldyreff B., Issinger O.G., Niefind K.
    J. Mol. Biol. 330:925-934(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-335.

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: May 27, 2015
This is version 131 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

External Data

Dasty 3

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 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.