CSK23_HUMAN
ID CSK23_HUMAN Reviewed; 391 AA.
AC Q8NEV1;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Casein kinase II subunit alpha 3;
DE Short=CK II alpha 3;
DE EC=2.7.11.1;
DE AltName: Full=Casein kinase II alpha 1 polypeptide pseudogene;
GN Name=CSNK2A3; Synonyms=CSNK2A1P;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1610905; DOI=10.1016/0167-4781(92)90083-c;
RA Wirkner U., Voss H., Lichter P., Weitz S., Ansorge W., Pyerin W.;
RT "Human casein kinase II subunit alpha: sequence of a processed (pseudo)gene
RT and its localization on chromosome 11.";
RL Biochim. Biophys. Acta 1131:220-222(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8420794; DOI=10.1016/0014-5793(93)81197-8;
RA Devilat I., Carvallo P.;
RT "Structure and sequence of an intronless gene for human casein kinase II-
RT alpha subunit.";
RL FEBS Lett. 316:114-118(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Platelet;
RX PubMed=12102635; DOI=10.1021/bi025791r;
RA Singh L.S., Kalafatis M.;
RT "Sequencing of full-length cDNA encoding the alpha and beta subunits of
RT human casein kinase II from human platelets and megakaryocytic cells.
RT Expression of the casein kinase IIalpha intronless gene in a megakaryocytic
RT cell line.";
RL Biochemistry 41:8935-8940(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PML, VARIANT THR-133, AND
RP TISSUE SPECIFICITY.
RX PubMed=20625391; DOI=10.1371/journal.pone.0011418;
RA Hung M.S., Lin Y.C., Mao J.H., Kim I.J., Xu Z., Yang C.T., Jablons D.M.,
RA You L.;
RT "Functional polymorphism of the CK2alpha intronless gene plays oncogenic
RT roles in lung cancer.";
RL PLoS ONE 5:E11418-E11418(2010).
CC -!- FUNCTION: Probable catalytic subunit of a constitutively active
CC serine/threonine-protein kinase complex that phosphorylates a large
CC number of substrates containing acidic residues C-terminal to the
CC phosphorylated serine or threonine. Amplification-dependent oncogene;
CC promotes cell proliferation and tumorigenesis by down-regulating
CC expression of the tumor suppressor protein, PML. May play a role in the
CC pathogenesis of the lung cancer development and progression.
CC {ECO:0000269|PubMed:20625391}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:20625391};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:20625391};
CC -!- SUBUNIT: Heterotetramer composed of two catalytic subunits (alpha chain
CC and/or alpha' chain) and two regulatory subunits (beta chains) (By
CC similarity). Interacts with PML. {ECO:0000250,
CC ECO:0000269|PubMed:20625391}.
CC -!- TISSUE SPECIFICITY: Detected in blood platelets and megakaryocyte cell
CC lines. Poorly expressed in lung. Highly expressed in lung tumor
CC tissues. {ECO:0000269|PubMed:12102635, ECO:0000269|PubMed:20625391}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X64692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY112721; AAM52224.1; -; mRNA.
DR EMBL; CH471064; EAW68546.1; -; Genomic_DNA.
DR RefSeq; NP_001243615.1; NM_001256686.1.
DR AlphaFoldDB; Q8NEV1; -.
DR SMR; Q8NEV1; -.
DR BioGRID; 129460; 18.
DR IntAct; Q8NEV1; 9.
DR STRING; 9606.ENSP00000473553; -.
DR BindingDB; Q8NEV1; -.
DR ChEMBL; CHEMBL3832943; -.
DR iPTMnet; Q8NEV1; -.
DR PhosphoSitePlus; Q8NEV1; -.
DR BioMuta; CSNK2A3; -.
DR EPD; Q8NEV1; -.
DR jPOST; Q8NEV1; -.
DR MassIVE; Q8NEV1; -.
DR MaxQB; Q8NEV1; -.
DR PeptideAtlas; Q8NEV1; -.
DR PRIDE; Q8NEV1; -.
DR Antibodypedia; 72367; 16 antibodies from 5 providers.
DR DNASU; 283106; -.
DR Ensembl; ENST00000528848.3; ENSP00000473553.1; ENSG00000254598.3.
DR GeneID; 283106; -.
DR KEGG; hsa:283106; -.
DR MANE-Select; ENST00000528848.3; ENSP00000473553.1; NM_001256686.2; NP_001243615.1.
DR UCSC; uc001mjp.4; human.
DR CTD; 283106; -.
DR DisGeNET; 283106; -.
DR GeneCards; CSNK2A3; -.
DR HGNC; HGNC:2458; CSNK2A3.
DR HPA; ENSG00000254598; Low tissue specificity.
DR neXtProt; NX_Q8NEV1; -.
DR OpenTargets; ENSG00000254598; -.
DR VEuPathDB; HostDB:ENSG00000254598; -.
DR eggNOG; KOG0668; Eukaryota.
DR GeneTree; ENSGT00390000004215; -.
DR HOGENOM; CLU_000288_70_4_1; -.
DR InParanoid; Q8NEV1; -.
DR OrthoDB; 1301576at2759; -.
DR PhylomeDB; Q8NEV1; -.
DR PathwayCommons; Q8NEV1; -.
DR SignaLink; Q8NEV1; -.
DR SIGNOR; Q8NEV1; -.
DR BioGRID-ORCS; 283106; 36 hits in 1029 CRISPR screens.
DR GenomeRNAi; 283106; -.
DR Pharos; Q8NEV1; Tdark.
DR PRO; PR:Q8NEV1; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8NEV1; protein.
DR Bgee; ENSG00000254598; Expressed in calcaneal tendon and 54 other tissues.
DR Genevisible; Q8NEV1; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005956; C:protein kinase CK2 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR CDD; cd14132; STKc_CK2_alpha; 1.
DR InterPro; IPR045216; CK2_alpha.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24054; PTHR24054; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Proto-oncogene;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..391
FT /note="Casein kinase II subunit alpha 3"
FT /id="PRO_0000422194"
FT DOMAIN 39..324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 45..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VARIANT 133
FT /note="I -> T (in a lung carcinoma sample; somatic
FT mutation; shows greater kinase activity, provides a cell
FT growth advantage and increases its interaction with the PML
FT tumor suppressor protein and PML degradation;
FT dbSNP:rs2071460)"
FT /evidence="ECO:0000269|PubMed:20625391"
FT /id="VAR_069225"
FT CONFLICT 128
FT /note="L -> F (in Ref. 1; X64692, 3; AAM52224 and 5;
FT EAW68546)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="R -> S (in Ref. 1; X64692, 3; AAM52224 and 5;
FT EAW68546)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="R -> H (in Ref. 1; X64692)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="F -> V (in Ref. 1; X64692, 3; AAM52224 and 5;
FT EAW68546)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="S -> R (in Ref. 1; X64692, 3; AAM52224 and 5;
FT EAW68546)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="Missing (in Ref. 1; X64692)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="T -> A (in Ref. 1; X64692, 3; AAM52224 and 5;
FT EAW68546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 391 AA; 45220 MW; D0FA2E3EACB5A064 CRC64;
MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY SEVFEAINIT
NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD
FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE
FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWRLGC MLASMIFRKE PFFHGRDNYD
QLVRIAKFLG TEDLYGYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF
LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN VMSGISSVPT
PSPLGPLAGS PVIAAANPLG MPVPAATGAQ Q
