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Protein

Casein kinase II subunit alpha

Gene

Csnk2a1

Organism
Rattus norvegicus (Rat)
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. Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated degradation (By similarity). 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. Phosphorylates CCAR2 at 'Thr-454' (By similarity).By similarity2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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

Sites

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

Regions

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

GO - Molecular functioni

GO - Biological processi

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. 5301.
ReactomeiR-RNO-1483191. Synthesis of PC.
R-RNO-201688. WNT mediated activation of DVL.
R-RNO-2514853. Condensation of Prometaphase Chromosomes.
R-RNO-445144. Signal transduction by L1.
R-RNO-6804756. Regulation of TP53 Activity through Phosphorylation.
R-RNO-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi621663. Csnk2a1.

Subcellular locationi

  • Nucleus By similarity

GO - Cellular componenti

  • nucleus Source: UniProtKB-SubCell
  • protein kinase CK2 complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000858861 – 391Casein kinase II subunit alphaAdd BLAST391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei344Phosphothreonine; by CDK1By similarity1
Modified residuei360Phosphothreonine; by CDK1By similarity1
Modified residuei362Phosphoserine; by CDK1By similarity1
Modified residuei370Phosphoserine; by CDK1By similarity1

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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP19139.
PRIDEiP19139.

PTM databases

iPTMnetiP19139.
PhosphoSitePlusiP19139.

Expressioni

Gene expression databases

BgeeiENSRNOG00000005276.
GenevisibleiP19139. RN.

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, SNAI1, PML and CCAR2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi250484. 4 interactors.
IntActiP19139. 4 interactors.
MINTiMINT-3372564.
STRINGi10116.ENSRNOP00000007558.

Chemistry databases

BindingDBiP19139.

Structurei

Secondary structure

1391
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 12Combined sources3
Turni15 – 18Combined sources4
Helixi21 – 24Combined sources4
Helixi26 – 28Combined sources3
Helixi36 – 38Combined sources3
Beta strandi39 – 43Combined sources5
Beta strandi52 – 58Combined sources7
Turni59 – 61Combined sources3
Beta strandi64 – 69Combined sources6
Helixi75 – 88Combined sources14
Beta strandi97 – 102Combined sources6
Beta strandi109 – 114Combined sources6
Helixi122 – 125Combined sources4
Helixi130 – 149Combined sources20
Helixi159 – 161Combined sources3
Beta strandi162 – 165Combined sources4
Turni166 – 169Combined sources4
Beta strandi170 – 173Combined sources4
Helixi195 – 197Combined sources3
Helixi200 – 203Combined sources4
Helixi212 – 226Combined sources15
Beta strandi230 – 233Combined sources4
Helixi240 – 249Combined sources10
Helixi251 – 260Combined sources10
Helixi267 – 271Combined sources5
Helixi281 – 284Combined sources4
Turni287 – 292Combined sources6
Helixi295 – 304Combined sources10
Helixi309 – 311Combined sources3
Helixi315 – 319Combined sources5
Helixi322 – 324Combined sources3
Helixi325 – 328Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R7IX-ray3.00A/B/C/D1-335[»]
ProteinModelPortaliP19139.
SMRiP19139.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19139.

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 subunit6

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.
InParanoidiP19139.
KOiK03097.
OMAiWHSFVTS.
OrthoDBiEOG091G0AZY.
PhylomeDBiP19139.
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]

Sequencei

Sequence statusi: Complete.

P19139-1 [UniParc]FASTAAdd to basket

« 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 QARMSSAGMA GGSTPVSSAN
360 370 380 390
MMSGISSVPT PSPLGPLAGS PVIAAANSLG IPVPAAAGAQ Q
Length:391
Mass (Da):45,073
Last modified:February 1, 1995 - v2
Checksum:i83A4E2CC80824F66
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L15618 mRNA. Translation: AAA74462.1.
BC091130 mRNA. Translation: AAH91130.1.
J02853 mRNA. No translation available.
PIRiB30319.
RefSeqiNP_446276.1. NM_053824.2.
XP_006235282.1. XM_006235220.3.
XP_006235283.1. XM_006235221.3.
UniGeneiRn.203090.
Rn.4231.

Genome annotation databases

EnsembliENSRNOT00000007558; ENSRNOP00000007558; ENSRNOG00000005276.
GeneIDi116549.
KEGGirno:116549.
UCSCiRGD:621663. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L15618 mRNA. Translation: AAA74462.1.
BC091130 mRNA. Translation: AAH91130.1.
J02853 mRNA. No translation available.
PIRiB30319.
RefSeqiNP_446276.1. NM_053824.2.
XP_006235282.1. XM_006235220.3.
XP_006235283.1. XM_006235221.3.
UniGeneiRn.203090.
Rn.4231.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R7IX-ray3.00A/B/C/D1-335[»]
ProteinModelPortaliP19139.
SMRiP19139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250484. 4 interactors.
IntActiP19139. 4 interactors.
MINTiMINT-3372564.
STRINGi10116.ENSRNOP00000007558.

Chemistry databases

BindingDBiP19139.

PTM databases

iPTMnetiP19139.
PhosphoSitePlusiP19139.

Proteomic databases

PaxDbiP19139.
PRIDEiP19139.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000007558; ENSRNOP00000007558; ENSRNOG00000005276.
GeneIDi116549.
KEGGirno:116549.
UCSCiRGD:621663. rat.

Organism-specific databases

CTDi1457.
RGDi621663. Csnk2a1.

Phylogenomic databases

eggNOGiKOG0668. Eukaryota.
ENOG410XNPP. LUCA.
GeneTreeiENSGT00390000004215.
HOGENOMiHOG000233021.
HOVERGENiHBG107282.
InParanoidiP19139.
KOiK03097.
OMAiWHSFVTS.
OrthoDBiEOG091G0AZY.
PhylomeDBiP19139.
TreeFamiTF300483.

Enzyme and pathway databases

BRENDAi2.7.11.1. 5301.
ReactomeiR-RNO-1483191. Synthesis of PC.
R-RNO-201688. WNT mediated activation of DVL.
R-RNO-2514853. Condensation of Prometaphase Chromosomes.
R-RNO-445144. Signal transduction by L1.
R-RNO-6804756. Regulation of TP53 Activity through Phosphorylation.
R-RNO-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

EvolutionaryTraceiP19139.
PROiP19139.

Gene expression databases

BgeeiENSRNOG00000005276.
GenevisibleiP19139. RN.

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_RAT
AccessioniPrimary (citable) accession number: P19139
Secondary accession number(s): Q5BKC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.