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Casein kinase II subunit alpha' (CK II alpha') (EC 2 7 11 1)

 CSK22_MOUSE             Reviewed;         350 AA.
O54833;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
17-JUN-2020, entry version 185.
RecName: Full=Casein kinase II subunit alpha';
Short=CK II alpha';
EC=2.7.11.1;
Name=Csnk2a2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=9503019; DOI=10.1006/geno.1997.5154;
Xu X., Rich E.S. Jr., Seldin D.C.;
"Murine protein kinase CK2 alpha': cDNA and genomic cloning and chromosomal
mapping.";
Genomics 48:79-86(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=9694889; DOI=10.1074/jbc.273.33.21291;
Orlandini M., Semplici F., Ferruzzi R., Meggio F., Pinna L.A., Oliviero S.;
"Protein kinase CK2alpha' is induced by serum as a delayed early gene and
cooperates with Ha-ras in fibroblast transformation.";
J. Biol. Chem. 273:21291-21297(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=129; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[4]
DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=10471512; DOI=10.1038/12729;
Xu X., Toselli P.A., Russell L.D., Seldin D.C.;
"Globozoospermia in mice lacking the casein kinase II alpha' catalytic
subunit.";
Nat. Genet. 23:118-121(1999).
[5]
INTERACTION WITH CSNKA2IP.
PubMed=19273531; DOI=10.1093/nar/gkp094;
Bai X., Silvius D., Chan E.D., Escalier D., Xu S.X.;
"Identification and characterization of a novel testis-specific gene CKT2,
which encodes a substrate for protein kinase CK2.";
Nucleic Acids Res. 37:2699-2711(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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 (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- ACTIVITY REGULATION: Constitutively active protein kinase whose
activity is not directly affected by phosphorylation. Seems to be
regulated by level of expression and localization (By similarity).
{ECO:0000250}.
-!- SUBUNIT: 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 (By similarity).
Interacts with CSNKA2IP (via C-terminus) (PubMed:19273531).
{ECO:0000250|UniProtKB:P19784, ECO:0000269|PubMed:19273531}.
-!- TISSUE SPECIFICITY: Highly expressed in brain, testis and mature
epididymal spermatozoa. Weakly expressed in kidney, liver, lung, spleen
and thymus (at protein level). {ECO:0000269|PubMed:10471512}.
-!- DISRUPTION PHENOTYPE: Infertile male mice with oligospermia and
globozoospermia. {ECO:0000269|PubMed:10471512}.
-!- 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.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; AF012251; AAC53552.1; -; mRNA.
EMBL; AJ001420; CAA04753.1; -; mRNA.
EMBL; BC057862; AAH57862.1; -; mRNA.
CCDS; CCDS22562.1; -.
RefSeq; NP_034104.1; NM_009974.3.
SMR; O54833; -.
BioGRID; 198946; 10.
CORUM; O54833; -.
IntAct; O54833; 8.
MINT; O54833; -.
STRING; 10090.ENSMUSP00000055919; -.
ChEMBL; CHEMBL5326; -.
iPTMnet; O54833; -.
PhosphoSitePlus; O54833; -.
EPD; O54833; -.
PaxDb; O54833; -.
PeptideAtlas; O54833; -.
PRIDE; O54833; -.
Antibodypedia; 15225; 308 antibodies.
Ensembl; ENSMUST00000056919; ENSMUSP00000055919; ENSMUSG00000046707.
Ensembl; ENSMUST00000212214; ENSMUSP00000148404; ENSMUSG00000046707.
GeneID; 13000; -.
KEGG; mmu:13000; -.
UCSC; uc009myk.2; mouse.
CTD; 1459; -.
MGI; MGI:88547; Csnk2a2.
eggNOG; KOG0668; Eukaryota.
eggNOG; ENOG410XNPP; LUCA.
GeneTree; ENSGT00390000004215; -.
HOGENOM; CLU_000288_70_4_1; -.
InParanoid; O54833; -.
KO; K03097; -.
OMA; KRPQEYW; -.
OrthoDB; 1098380at2759; -.
PhylomeDB; O54833; -.
TreeFam; TF300483; -.
BRENDA; 2.7.11.1; 3474.
Reactome; R-MMU-1483191; Synthesis of PC.
Reactome; R-MMU-201688; WNT mediated activation of DVL.
Reactome; R-MMU-2514853; Condensation of Prometaphase Chromosomes.
Reactome; R-MMU-445144; Signal transduction by L1.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
Reactome; R-MMU-8934903; Receptor Mediated Mitophagy.
Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
BioGRID-ORCS; 13000; 3 hits in 12 CRISPR screens.
ChiTaRS; Csnk2a2; mouse.
PRO; PR:O54833; -.
Proteomes; UP000000589; Chromosome 8.
RNAct; O54833; protein.
Bgee; ENSMUSG00000046707; Expressed in camera-type eye and 327 other tissues.
ExpressionAtlas; O54833; baseline and differential.
Genevisible; O54833; MM.
GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
GO; GO:0000785; C:chromatin; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0031519; C:PcG protein complex; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005956; C:protein kinase CK2 complex; TAS:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
GO; GO:1905818; P:regulation of chromosome separation; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; ATP-binding; Cell cycle; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transcription; Transcription regulation;
Transferase; Wnt signaling pathway.
CHAIN 1..350
/note="Casein kinase II subunit alpha'"
/id="PRO_0000085892"
DOMAIN 40..325
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 46..54
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
ACT_SITE 157
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10027"
BINDING 69
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 13
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P19784"
MOD_RES 18
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P19784"
MOD_RES 21
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P19784"
MOD_RES 97
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P19784"
MOD_RES 288
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P19784"
SEQUENCE 350 AA; 41215 MW; C5FA314617627F5B CRC64;
MPGPAAGSRA RVYAEVNSLR SREYWDYEAH VPSWGNQDDY QLVRKLGRGK YSEVFEAINI
TNNERVVVKI LKPVKKKKIK REVKILENLR GGTNIIKLID TVKDPVSKTP ALVFEYINNT
DFKQLYQILT DFDIRFYMYE LLKALDYCHS KGIMHRDVKP HNVMIDHQQK KLRLIDWGLA
EFYHPAQEYN VRVASRYFKG PELLVDYQMY DYSLDMWSLG CMLASMIFRK EPFFHGQDNY
DQLVRIAKVL GTDELYGYLK KYHIDLDPHF NDILGQHSRK RWENFIHSEN RHLVSPEALD
LLDKLLRYDH QQRLTAKEAM EHPYFYPVVK EQSQPCAENT VLSSGLTAAR


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