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P19139

- CSK21_RAT

UniProt

P19139 - CSK21_RAT

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Protein
Casein kinase II subunit alpha
Gene
Csnk2a1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.2 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei68 – 681ATP By similarity
Active sitei156 – 1561Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi45 – 539ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein phosphatase regulator activity Source: Ensembl
  3. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. Wnt signaling pathway Source: UniProtKB-KW
  2. mitotic spindle checkpoint Source: UniProtKB
  3. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  4. positive regulation of Wnt signaling pathway Source: UniProtKB
  5. positive regulation of cell growth Source: UniProtKB
  6. positive regulation of cell proliferation Source: UniProtKB
  7. positive regulation of protein catabolic process Source: UniProtKB
  8. protein autophosphorylation Source: Ensembl
  9. protein phosphorylation Source: UniProtKB
  10. regulation of cell growth Source: RGD
  11. regulation of cell proliferation Source: RGD
  12. regulation of transcription, DNA-templated Source: UniProtKB-KW
  13. rhythmic process Source: UniProtKB-KW
  14. transcription, DNA-templated 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. 5301.
ReactomeiREACT_198291. Condensation of Prometaphase Chromosomes.
REACT_205007. WNT mediated activation of DVL.

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
ProteomesiUP000002494: Chromosome 3

Organism-specific databases

RGDi621663. Csnk2a1.

Subcellular locationi

GO - Cellular componenti

  1. protein kinase CK2 complex Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 391391Casein kinase II subunit alpha
PRO_0000085886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei344 – 3441Phosphothreonine; by CDK1 By similarity
Modified residuei360 – 3601Phosphothreonine; by CDK1 By similarity
Modified residuei362 – 3621Phosphoserine; by CDK1 By similarity
Modified residuei370 – 3701Phosphoserine; by CDK1 By similarity

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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP19139.
PRIDEiP19139.

PTM databases

PhosphoSiteiP19139.

Expressioni

Gene expression databases

GenevestigatoriP19139.

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 By similarity. Interacts with PML By similarity.

Protein-protein interaction databases

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

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123
Turni15 – 184
Helixi21 – 244
Helixi26 – 283
Helixi36 – 383
Beta strandi39 – 435
Beta strandi52 – 587
Turni59 – 613
Beta strandi64 – 696
Helixi75 – 8814
Beta strandi97 – 1026
Beta strandi109 – 1146
Helixi122 – 1254
Helixi130 – 14920
Helixi159 – 1613
Beta strandi162 – 1654
Turni166 – 1694
Beta strandi170 – 1734
Helixi195 – 1973
Helixi200 – 2034
Helixi212 – 22615
Beta strandi230 – 2334
Helixi240 – 24910
Helixi251 – 26010
Helixi267 – 2715
Helixi281 – 2844
Turni287 – 2926
Helixi295 – 30410
Helixi309 – 3113
Helixi315 – 3195
Helixi322 – 3243
Helixi325 – 3284

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R7IX-ray3.00A/B/C/D1-335[»]
ProteinModelPortaliP19139.
SMRiP19139. Positions 2-334.

Miscellaneous databases

EvolutionaryTraceiP19139.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 324286Protein kinase
Add
BLAST

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00390000004215.
HOGENOMiHOG000233021.
HOVERGENiHBG107282.
InParanoidiP19139.
KOiK03097.
OMAiNNTDFRS.
OrthoDBiEOG7QG446.
PhylomeDBiP19139.
TreeFamiTF300483.

Family and domain databases

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

MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY    50
SEVFEAINIT NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI 100
VKDPVSRTPA LVFEHVNNTD FKQLYQTLTD YDIRFYMYEI LKALDYCHSM 150
GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE FYHPGQEYNV RVASRYFKGP 200
ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD QLVRIAKVLG 250
TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF 300
LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMSSAGMA GGSTPVSSAN 350
MMSGISSVPT PSPLGPLAGS PVIAAANSLG IPVPAAAGAQ Q 391
Length:391
Mass (Da):45,073
Last modified:February 1, 1995 - v2
Checksum:i83A4E2CC80824F66
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006235220.1.
XP_006235283.1. XM_006235221.1.
XP_006235284.1. XM_006235222.1.
UniGeneiRn.203090.
Rn.4231.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L15618 mRNA. Translation: AAA74462.1 .
BC091130 mRNA. Translation: AAH91130.1 .
J02853 mRNA. No translation available.
PIRi B30319.
RefSeqi NP_446276.1. NM_053824.2.
XP_006235282.1. XM_006235220.1.
XP_006235283.1. XM_006235221.1.
XP_006235284.1. XM_006235222.1.
UniGenei Rn.203090.
Rn.4231.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2R7I X-ray 3.00 A/B/C/D 1-335 [» ]
ProteinModelPortali P19139.
SMRi P19139. Positions 2-334.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 250484. 4 interactions.
IntActi P19139. 4 interactions.
MINTi MINT-3372564.
STRINGi 10116.ENSRNOP00000007558.

Chemistry

BindingDBi P19139.

PTM databases

PhosphoSitei P19139.

Proteomic databases

PaxDbi P19139.
PRIDEi P19139.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000007558 ; ENSRNOP00000007558 ; ENSRNOG00000005276 .
GeneIDi 116549.
KEGGi rno:116549.
UCSCi RGD:621663. rat.

Organism-specific databases

CTDi 1457.
RGDi 621663. Csnk2a1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00390000004215.
HOGENOMi HOG000233021.
HOVERGENi HBG107282.
InParanoidi P19139.
KOi K03097.
OMAi NNTDFRS.
OrthoDBi EOG7QG446.
PhylomeDBi P19139.
TreeFami TF300483.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 5301.
Reactomei REACT_198291. Condensation of Prometaphase Chromosomes.
REACT_205007. WNT mediated activation of DVL.

Miscellaneous databases

EvolutionaryTracei P19139.
NextBioi 619175.
PROi P19139.

Gene expression databases

Genevestigatori P19139.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of cDNAs encoding the alpha and beta subunits of rat casein kinase 2 (CK-2): investigation of molecular regulation of CK-2 by androgens in rat ventral prostate."
    Ahmed K., Davis A., Hanten J., Lambert D., McIvor R.S., Goueli S.A.
    Cell. Mol. Biol. Res. 39:451-462(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "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].
    Tissue: Spleen.
  3. "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] OF 8-391.
  4. Cited for: PROTEIN SEQUENCE OF 22-68; 90-107; 173-191; 229-244; 248-268 AND 284-306, FUNCTION.
  5. "Phosphorylation by protein kinase CK2: a signaling switch for the caspase-inhibiting protein ARC."
    Li P.F., Li J., Mueller E.C., Otto A., Dietz R., von Harsdorf R.
    Mol. Cell 10:247-258(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS.
  6. "Crystal structures of catalytic and regulatory subunits of rat protein kinase CK2."
    Zhou W., Qin X., Yan X., Xie X., Li L., Fang S., Long J., Adelman J., Tang W.-J., Shen Y.
    Chin. Sci. Bull. 54:220-226(2009)
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-335.

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: September 3, 2014
This is version 129 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

External Data

Dasty 3

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