CSK21_HUMAN
ID CSK21_HUMAN Reviewed; 391 AA.
AC P68400; B4DYS6; D3DVV8; P19138; P20426; Q14013; Q5U065;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Casein kinase II subunit alpha;
DE Short=CK II alpha;
DE EC=2.7.11.1 {ECO:0000269|PubMed:30699359};
GN Name=CSNK2A1; Synonyms=CK2A1;
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 [MRNA] (ISOFORM 1).
RX PubMed=2752008; DOI=10.1021/bi00435a066;
RA Meisner H., Heller-Harrison R., Buxton J., Czech M.P.;
RT "Molecular cloning of the human casein kinase II alpha subunit.";
RL Biochemistry 28:4072-4076(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2174700; DOI=10.1021/bi00488a034;
RA Lozeman F.J., Litchfield D.W., Piening C., Takio K., Walsh K.A.,
RA Krebs E.G.;
RT "Isolation and characterization of human cDNA clones encoding the alpha and
RT the alpha' subunits of casein kinase II.";
RL Biochemistry 29:8436-8447(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Muscle, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PHOSPHORYLATION AT THR-344; THR-360; SER-362 AND SER-370.
RX PubMed=7592773; DOI=10.1074/jbc.270.43.25872;
RA Bosc D.G., Slominski E., Sichler C., Litchfield D.W.;
RT "Phosphorylation of casein kinase II by p34cdc2. Identification of
RT phosphorylation sites using phosphorylation site mutants in vitro.";
RL J. Biol. Chem. 270:25872-25878(1995).
RN [11]
RP FUNCTION, AND INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=11239457; DOI=10.1016/s1097-2765(01)00176-9;
RA Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R.,
RA Lozano G., Zhao Y., Lu H.;
RT "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16,
RT and SSRP1.";
RL Mol. Cell 7:283-292(2001).
RN [12]
RP FUNCTION IN CELL CYCLE.
RX PubMed=11704824; DOI=10.1038/sj.onc.1204894;
RA Sayed M., Pelech S., Wong C., Marotta A., Salh B.;
RT "Protein kinase CK2 is involved in G2 arrest and apoptosis following
RT spindle damage in epithelial cells.";
RL Oncogene 20:6994-7005(2001).
RN [13]
RP INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=12393879; DOI=10.1074/jbc.m209820200;
RA Keller D.M., Lu H.;
RT "p53 serine 392 phosphorylation increases after UV through induction of the
RT assembly of the CK2.hSPT16.SSRP1 complex.";
RL J. Biol. Chem. 277:50206-50213(2002).
RN [14]
RP FUNCTION IN APOPTOSIS.
RX PubMed=16193064; DOI=10.1038/sj.emboj.7600827;
RA Shin S., Lee Y., Kim W., Ko H., Choi H., Kim K.;
RT "Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing
RT procaspase-8.";
RL EMBO J. 24:3532-3542(2005).
RN [15]
RP INTERACTION WITH RNPS1.
RX PubMed=15684395; DOI=10.1128/mcb.25.4.1446-1457.2005;
RA Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A.,
RA Suzuki H., Endo H., Kidd V.J., Mayeda A.;
RT "Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2
RT phosphorylation.";
RL Mol. Cell. Biol. 25:1446-1457(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP FUNCTION IN CELL CYCLE.
RX PubMed=19188443; DOI=10.1128/mcb.01563-08;
RA St-Denis N.A., Derksen D.R., Litchfield D.W.;
RT "Evidence for regulation of mitotic progression through temporal
RT phosphorylation and dephosphorylation of CK2alpha.";
RL Mol. Cell. Biol. 29:2068-2081(2009).
RN [18]
RP REVIEW ON FUNCTION.
RX PubMed=12631575; DOI=10.1096/fj.02-0473rev;
RA Meggio F., Pinna L.A.;
RT "One-thousand-and-one substrates of protein kinase CK2?";
RL FASEB J. 17:349-368(2003).
RN [19]
RP REVIEW ON STRUCTURE.
RX PubMed=19387553; DOI=10.1007/s00018-009-9149-8;
RA Niefind K., Raaf J., Issinger O.G.;
RT "Protein kinase CK2 in health and disease: Protein kinase CK2: from
RT structures to insights.";
RL Cell. Mol. Life Sci. 66:1800-1816(2009).
RN [20]
RP REVIEW ON FUNCTION.
RX PubMed=19387552; DOI=10.1007/s00018-009-9150-2;
RA St-Denis N.A., Litchfield D.W.;
RT "Protein kinase CK2 in health and disease: From birth to death: the role of
RT protein kinase CK2 in the regulation of cell proliferation and survival.";
RL Cell. Mol. Life Sci. 66:1817-1829(2009).
RN [21]
RP REVIEW ON FUNCTION.
RX PubMed=19387551; DOI=10.1007/s00018-009-9151-1;
RA Filhol O., Cochet C.;
RT "Protein kinase CK2 in health and disease: Cellular functions of protein
RT kinase CK2: a dynamic affair.";
RL Cell. Mol. Life Sci. 66:1830-1839(2009).
RN [22]
RP REVIEW ON FUNCTION IN REGULATION OF HSP90.
RX PubMed=19387550; DOI=10.1007/s00018-009-9152-0;
RA Miyata Y.;
RT "Protein kinase CK2 in health and disease: CK2: the kinase controlling the
RT Hsp90 chaperone machinery.";
RL Cell. Mol. Life Sci. 66:1840-1849(2009).
RN [23]
RP REVIEW ON FUNCTION IN WNT SIGNALING.
RX PubMed=19387549; DOI=10.1007/s00018-009-9153-z;
RA Dominguez I., Sonenshein G.E., Seldin D.C.;
RT "Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-
RT kappaB signaling: linking development and cancer.";
RL Cell. Mol. Life Sci. 66:1850-1857(2009).
RN [24]
RP INTERACTION WITH SNAI1.
RX PubMed=19923321; DOI=10.1091/mbc.e09-06-0504;
RA MacPherson M.R., Molina P., Souchelnytskyi S., Wernstedt C.,
RA Martin-Perez J., Portillo F., Cano A.;
RT "Phosphorylation of serine 11 and serine 92 as new positive regulators of
RT human Snail1 function: potential involvement of casein kinase-2 and the
RT cAMP-activated kinase protein kinase A.";
RL Mol. Biol. Cell 21:244-253(2010).
RN [25]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH PML.
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).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP FUNCTION, AND INTERACTION WITH PML.
RX PubMed=22406621; DOI=10.1158/0008-5472.can-11-3159;
RA Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A.,
RA Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J.,
RA Scaglioni P.P.;
RT "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its
RT oncogenic counterpart PML-RARA.";
RL Cancer Res. 72:2275-2284(2012).
RN [29]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=23123191; DOI=10.1016/j.bbamcr.2012.10.025;
RA Ampofo E., Sokolowsky T., Goetz C., Montenarh M.;
RT "Functional interaction of protein kinase CK2 and activating transcription
RT factor 4 (ATF4), a key player in the cellular stress response.";
RL Biochim. Biophys. Acta 1833:439-451(2013).
RN [30]
RP FUNCTION, INTERACTION WITH CCAR2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=24962073; DOI=10.1002/ijc.29043;
RA Bae J.S., Park S.H., Kim K.M., Kwon K.S., Kim C.Y., Lee H.K., Park B.H.,
RA Park H.S., Lee H., Moon W.S., Chung M.J., Sylvester K.G., Jang K.Y.;
RT "CK2alpha phosphorylates DBC1 and is involved in the progression of gastric
RT carcinoma and predicts poor survival of gastric carcinoma patients.";
RL Int. J. Cancer 136:797-809(2015).
RN [31]
RP INVOLVEMENT IN OCNDS, AND VARIANTS OCNDS GLN-47; SER-50; GLY-175 AND
RP ARG-198.
RX PubMed=27048600; DOI=10.1007/s00439-016-1661-y;
RA Okur V., Cho M.T., Henderson L., Retterer K., Schneider M., Sattler S.,
RA Niyazov D., Azage M., Smith S., Picker J., Lincoln S., Tarnopolsky M.,
RA Brady L., Bjornsson H.T., Applegate C., Dameron A., Willaert R., Baskin B.,
RA Juusola J., Chung W.K.;
RT "De novo mutations in CSNK2A1 are associated with neurodevelopmental
RT abnormalities and dysmorphic features.";
RL Hum. Genet. 135:699-705(2016).
RN [32]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30699359; DOI=10.1016/j.celrep.2019.01.018;
RA Sager R.A., Woodford M.R., Backe S.J., Makedon A.M., Baker-Williams A.J.,
RA DiGregorio B.T., Loiselle D.R., Haystead T.A., Zachara N.E., Prodromou C.,
RA Bourboulia D., Schmidt L.S., Linehan W.M., Bratslavsky G., Mollapour M.;
RT "Post-translational regulation of FNIP1 creates a rheostat for the
RT molecular chaperone Hsp90.";
RL Cell Rep. 26:1344-1356(2019).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337, AND SUBUNIT.
RX PubMed=11092945; DOI=10.1107/s0907444900013627;
RA Niefind K., Guerra B., Ermakowa I., Issinger O.G.;
RT "Crystallization and preliminary characterization of crystals of human
RT protein kinase CK2.";
RL Acta Crystallogr. D 56:1680-1684(2000).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337 IN COMPLEX WITH CSNK2B, AND
RP SUBUNIT.
RX PubMed=11574463; DOI=10.1093/emboj/20.19.5320;
RA Niefind K., Guerra B., Ermakowa I., Issinger O.G.;
RT "Crystal structure of human protein kinase CK2: insights into basic
RT properties of the CK2 holoenzyme.";
RL EMBO J. 20:5320-5331(2001).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-329.
RX PubMed=14646071; DOI=10.1107/s0907444903018900;
RA Pechkova E., Zanotti G., Nicolini C.;
RT "Three-dimensional atomic structure of a catalytic subunit mutant of human
RT protein kinase CK2.";
RL Acta Crystallogr. D 59:2133-2139(2003).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-335.
RX PubMed=12860116; DOI=10.1016/s0022-2836(03)00638-7;
RA Ermakova I., Boldyreff B., Issinger O.G., Niefind K.;
RT "Crystal structure of a C-terminal deletion mutant of human protein kinase
RT CK2 catalytic subunit.";
RL J. Mol. Biol. 330:925-934(2003).
CC -!- FUNCTION: 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 (PubMed:11239457, PubMed:11704824,
CC PubMed:16193064, PubMed:19188443, PubMed:20625391, PubMed:22406621,
CC PubMed:24962073). Regulates numerous cellular processes, such as cell
CC cycle progression, apoptosis and transcription, as well as viral
CC infection (PubMed:12631575, PubMed:19387552, PubMed:19387551). May act
CC as a regulatory node which integrates and coordinates numerous signals
CC leading to an appropriate cellular response (PubMed:12631575,
CC PubMed:19387552, PubMed:19387551). During mitosis, functions as a
CC component of the p53/TP53-dependent spindle assembly checkpoint (SAC)
CC that maintains cyclin-B-CDK1 activity and G2 arrest in response to
CC spindle damage (PubMed:11704824, PubMed:19188443). Also required for
CC p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53
CC following UV irradiation. Can also negatively regulate apoptosis
CC (PubMed:11239457). Phosphorylates the caspases CASP9 and CASP2 and the
CC apoptotic regulator NOL3 (PubMed:16193064). Phosphorylation protects
CC CASP9 from cleavage and activation by CASP8, and inhibits the
CC dimerization of CASP2 and activation of CASP8 (PubMed:16193064).
CC Regulates transcription by direct phosphorylation of RNA polymerases I,
CC II, III and IV. Also phosphorylates and regulates numerous
CC transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2,
CC ATF1, ATF4, SRF, MAX, JUN, FOS, MYC and MYB (PubMed:19387550,
CC PubMed:12631575, PubMed:19387552, PubMed:19387551, PubMed:23123191).
CC Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is
CC essential for chaperone function (PubMed:19387550). Mediates sequential
CC phosphorylation of FNIP1, promoting its gradual interaction with Hsp90,
CC leading to activate both kinase and non-kinase client proteins of Hsp90
CC (PubMed:30699359). Regulates Wnt signaling by phosphorylating CTNNB1
CC and the transcription factor LEF1 (PubMed:19387549). Acts as an
CC ectokinase that phosphorylates several extracellular proteins
CC (PubMed:19387550, PubMed:12631575, PubMed:19387552, PubMed:19387551).
CC During viral infection, phosphorylates various proteins involved in the
CC viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV
CC (PubMed:19387550, PubMed:12631575, PubMed:19387552, PubMed:19387551).
CC Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated
CC degradation (PubMed:20625391, PubMed:22406621). Plays an important role
CC in the circadian clock function by phosphorylating ARNTL/BMAL1 at 'Ser-
CC 90' which is pivotal for its interaction with CLOCK and which controls
CC CLOCK nuclear entry (By similarity). Phosphorylates CCAR2 at 'Thr-454'
CC in gastric carcinoma tissue (PubMed:24962073).
CC {ECO:0000250|UniProtKB:P19139, ECO:0000269|PubMed:11239457,
CC ECO:0000269|PubMed:11704824, ECO:0000269|PubMed:16193064,
CC ECO:0000269|PubMed:19188443, ECO:0000269|PubMed:20625391,
CC ECO:0000269|PubMed:22406621, ECO:0000269|PubMed:23123191,
CC ECO:0000269|PubMed:24962073, ECO:0000269|PubMed:30699359,
CC ECO:0000303|PubMed:12631575, ECO:0000303|PubMed:19387549,
CC ECO:0000303|PubMed:19387550, ECO:0000303|PubMed:19387551,
CC ECO:0000303|PubMed:19387552}.
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, ECO:0000269|PubMed:23123191,
CC ECO:0000269|PubMed:30699359};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:23123191, ECO:0000269|PubMed:30699359};
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 -!- ACTIVITY REGULATION: Constitutively active protein kinase whose
CC activity is not directly affected by phosphorylation. Seems to be
CC regulated by level of expression and localization.
CC -!- SUBUNIT: Heterotetramer composed of two catalytic subunits (alpha chain
CC and/or alpha' chain) and two regulatory subunits (beta chains). The
CC tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta
CC or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1
CC complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which
CC forms following UV irradiation. Interacts with RNPS1. Interacts with
CC SNAI1. Interacts with PML (isoform PML-12). Interacts with CCAR2.
CC {ECO:0000269|PubMed:11092945, ECO:0000269|PubMed:11239457,
CC ECO:0000269|PubMed:11574463, ECO:0000269|PubMed:12393879,
CC ECO:0000269|PubMed:15684395, ECO:0000269|PubMed:19923321,
CC ECO:0000269|PubMed:20625391, ECO:0000269|PubMed:22406621,
CC ECO:0000269|PubMed:24962073}.
CC -!- INTERACTION:
CC P68400; P78563: ADARB1; NbExp=3; IntAct=EBI-347804, EBI-2967304;
CC P68400; P05067: APP; NbExp=3; IntAct=EBI-347804, EBI-77613;
CC P68400; Q86V38: ATN1; NbExp=6; IntAct=EBI-347804, EBI-11954292;
CC P68400; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-347804, EBI-10181188;
CC P68400; P35226: BMI1; NbExp=2; IntAct=EBI-347804, EBI-2341576;
CC P68400; O00257-3: CBX4; NbExp=2; IntAct=EBI-347804, EBI-4392727;
CC P68400; Q8IYX3: CCDC116; NbExp=3; IntAct=EBI-347804, EBI-744311;
CC P68400; P68400: CSNK2A1; NbExp=4; IntAct=EBI-347804, EBI-347804;
CC P68400; P19784: CSNK2A2; NbExp=10; IntAct=EBI-347804, EBI-347451;
CC P68400; P67870: CSNK2B; NbExp=27; IntAct=EBI-347804, EBI-348169;
CC P68400; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-347804, EBI-12051833;
CC P68400; Q9GZR7: DDX24; NbExp=2; IntAct=EBI-347804, EBI-713081;
CC P68400; P35659: DEK; NbExp=2; IntAct=EBI-347804, EBI-301977;
CC P68400; Q92997: DVL3; NbExp=4; IntAct=EBI-347804, EBI-739789;
CC P68400; O75822: EIF3J; NbExp=3; IntAct=EBI-347804, EBI-366647;
CC P68400; Q8N9E0: FAM133A; NbExp=5; IntAct=EBI-347804, EBI-10268158;
CC P68400; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-347804, EBI-11977403;
CC P68400; Q9NW75-2: GPATCH2; NbExp=3; IntAct=EBI-347804, EBI-12068108;
CC P68400; Q9NWQ4-1: GPATCH2L; NbExp=6; IntAct=EBI-347804, EBI-11959863;
CC P68400; O15499: GSC2; NbExp=3; IntAct=EBI-347804, EBI-19954058;
CC P68400; Q13547: HDAC1; NbExp=3; IntAct=EBI-347804, EBI-301834;
CC P68400; P09017: HOXC4; NbExp=3; IntAct=EBI-347804, EBI-3923226;
CC P68400; A0A0C4DFT8: JADE2; NbExp=3; IntAct=EBI-347804, EBI-12094820;
CC P68400; Q14145: KEAP1; NbExp=3; IntAct=EBI-347804, EBI-751001;
CC P68400; Q5T7B8-2: KIF24; NbExp=3; IntAct=EBI-347804, EBI-10213781;
CC P68400; O60282: KIF5C; NbExp=4; IntAct=EBI-347804, EBI-717170;
CC P68400; Q92876: KLK6; NbExp=3; IntAct=EBI-347804, EBI-2432309;
CC P68400; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-347804, EBI-12039345;
CC P68400; Q68G74: LHX8; NbExp=3; IntAct=EBI-347804, EBI-8474075;
CC P68400; Q9NQ69: LHX9; NbExp=3; IntAct=EBI-347804, EBI-10175218;
CC P68400; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-347804, EBI-10178634;
CC P68400; P50221: MEOX1; NbExp=3; IntAct=EBI-347804, EBI-2864512;
CC P68400; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-347804, EBI-16439278;
CC P68400; Q9BU76: MMTAG2; NbExp=4; IntAct=EBI-347804, EBI-742459;
CC P68400; P23511: NFYA; NbExp=4; IntAct=EBI-347804, EBI-389739;
CC P68400; P23511-2: NFYA; NbExp=3; IntAct=EBI-347804, EBI-11061759;
CC P68400; Q02548: PAX5; NbExp=3; IntAct=EBI-347804, EBI-296331;
CC P68400; P26367: PAX6; NbExp=5; IntAct=EBI-347804, EBI-747278;
CC P68400; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-347804, EBI-2339674;
CC P68400; P78356-2: PIP4K2B; NbExp=3; IntAct=EBI-347804, EBI-11532361;
CC P68400; P29590: PML; NbExp=2; IntAct=EBI-347804, EBI-295890;
CC P68400; Q9H307: PNN; NbExp=2; IntAct=EBI-347804, EBI-681904;
CC P68400; P78424: POU6F2; NbExp=3; IntAct=EBI-347804, EBI-12029004;
CC P68400; O75400-2: PRPF40A; NbExp=2; IntAct=EBI-347804, EBI-5280197;
CC P68400; Q14498: RBM39; NbExp=3; IntAct=EBI-347804, EBI-395290;
CC P68400; Q04864-2: REL; NbExp=3; IntAct=EBI-347804, EBI-10829018;
CC P68400; Q6ZNA4: RNF111; NbExp=6; IntAct=EBI-347804, EBI-2129175;
CC P68400; Q99496: RNF2; NbExp=4; IntAct=EBI-347804, EBI-722416;
CC P68400; Q96EB6: SIRT1; NbExp=5; IntAct=EBI-347804, EBI-1802965;
CC P68400; Q92504: SLC39A7; NbExp=4; IntAct=EBI-347804, EBI-1051105;
CC P68400; O43623: SNAI2; NbExp=3; IntAct=EBI-347804, EBI-9876238;
CC P68400; P12931: SRC; NbExp=2; IntAct=EBI-347804, EBI-621482;
CC P68400; Q08945: SSRP1; NbExp=3; IntAct=EBI-347804, EBI-353771;
CC P68400; Q96MF2: STAC3; NbExp=7; IntAct=EBI-347804, EBI-745680;
CC P68400; O75683: SURF6; NbExp=2; IntAct=EBI-347804, EBI-2691252;
CC P68400; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-347804, EBI-11139477;
CC P68400; Q9NVV9: THAP1; NbExp=7; IntAct=EBI-347804, EBI-741515;
CC P68400; Q9Y2W1: THRAP3; NbExp=2; IntAct=EBI-347804, EBI-352039;
CC P68400; Q08117-2: TLE5; NbExp=3; IntAct=EBI-347804, EBI-11741437;
CC P68400; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-347804, EBI-725997;
CC P68400; Q9H2G4: TSPYL2; NbExp=4; IntAct=EBI-347804, EBI-947459;
CC P68400; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-347804, EBI-12272076;
CC P68400; Q8IYI8: ZNF440; NbExp=3; IntAct=EBI-347804, EBI-726439;
CC P68400; Q96NG5: ZNF558; NbExp=3; IntAct=EBI-347804, EBI-373363;
CC P68400; Q9BS34: ZNF670; NbExp=3; IntAct=EBI-347804, EBI-745276;
CC P68400; Q6NSZ9-2: ZSCAN25; NbExp=3; IntAct=EBI-347804, EBI-14650477;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23123191,
CC ECO:0000269|PubMed:24962073}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P68400-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P68400-2; Sequence=VSP_041925;
CC -!- TISSUE SPECIFICITY: Expressed in gastric carcinoma tissue and the
CC expression gradually increases with the progression of the carcinoma
CC (at protein level). {ECO:0000269|PubMed:24962073}.
CC -!- PTM: Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in
CC prophase and metaphase and dephosphorylated during anaphase.
CC Phosphorylation does not directly affect casein kinase 2 activity, but
CC may contribute to its regulation by forming binding sites for
CC interacting proteins and/or targeting it to different compartments.
CC {ECO:0000269|PubMed:7592773}.
CC -!- DISEASE: Okur-Chung neurodevelopmental syndrome (OCNDS) [MIM:617062]:
CC An autosomal dominant neurodevelopmental disorder characterized by
CC developmental delay, intellectual disability, behavioral problems,
CC hypotonia, speech problems, microcephaly, pachygyria and variable
CC dysmorphic features. {ECO:0000269|PubMed:27048600}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Can use both ATP and GTP as phosphoryl donors.
CC Phosphorylation by casein kinase 2 has been estimated to represent up
CC to one quarter of the eukaryotic phosphoproteome. Casein kinase 2 has
CC been found to be increased at protein level and up-regulated at the
CC level of enzyme activity in the majority of cancers. However, elevated
CC levels of casein kinase 2 are present in certain normal organs such as
CC brain and testes.
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; J02853; AAA56821.1; -; mRNA.
DR EMBL; M55265; AAA35503.1; -; mRNA.
DR EMBL; S53149; ABB72474.1; -; mRNA.
DR EMBL; X70251; CAA49758.1; -; Genomic_DNA.
DR EMBL; AK302583; BAG63838.1; -; mRNA.
DR EMBL; BT019792; AAV38595.1; -; mRNA.
DR EMBL; AB451279; BAG70093.1; -; mRNA.
DR EMBL; AL049761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10665.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10666.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10667.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10668.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10669.1; -; Genomic_DNA.
DR EMBL; BC011668; AAH11668.1; -; mRNA.
DR EMBL; BC053532; AAH53532.1; -; mRNA.
DR EMBL; BC071167; AAH71167.1; -; mRNA.
DR CCDS; CCDS13003.1; -. [P68400-1]
DR CCDS; CCDS13004.1; -. [P68400-2]
DR PIR; A30319; A30319.
DR RefSeq; NP_001886.1; NM_001895.3. [P68400-1]
DR RefSeq; NP_808227.1; NM_177559.2. [P68400-1]
DR RefSeq; NP_808228.1; NM_177560.2. [P68400-2]
DR PDB; 1JWH; X-ray; 3.10 A; A/B=1-337.
DR PDB; 1NA7; X-ray; 2.40 A; A=1-329.
DR PDB; 1PJK; X-ray; 2.50 A; A=2-335.
DR PDB; 2PVR; X-ray; 1.60 A; A=2-335.
DR PDB; 2ZJW; X-ray; 2.40 A; A=1-335.
DR PDB; 3AMY; X-ray; 2.30 A; A=1-335.
DR PDB; 3AT2; X-ray; 1.60 A; A=1-335.
DR PDB; 3AT3; X-ray; 2.60 A; A=1-335.
DR PDB; 3AT4; X-ray; 2.20 A; A=1-335.
DR PDB; 3AXW; X-ray; 2.50 A; A=1-335.
DR PDB; 3BQC; X-ray; 1.50 A; A=1-335.
DR PDB; 3C13; X-ray; 1.95 A; A=1-335.
DR PDB; 3FWQ; X-ray; 2.30 A; A/B=1-335.
DR PDB; 3H30; X-ray; 1.56 A; A/B=1-334.
DR PDB; 3JUH; X-ray; 1.66 A; A/B=1-335.
DR PDB; 3MB6; X-ray; 1.75 A; A=1-331.
DR PDB; 3MB7; X-ray; 1.65 A; A=1-331.
DR PDB; 3NGA; X-ray; 2.71 A; A/B=1-333.
DR PDB; 3NSZ; X-ray; 1.30 A; A=2-331.
DR PDB; 3OWJ; X-ray; 1.85 A; A=1-331.
DR PDB; 3OWK; X-ray; 1.80 A; A=1-331.
DR PDB; 3OWL; X-ray; 2.10 A; A=1-331.
DR PDB; 3PE1; X-ray; 1.60 A; A=1-337.
DR PDB; 3PE2; X-ray; 1.90 A; A=1-337.
DR PDB; 3PE4; X-ray; 1.95 A; B/D=340-352.
DR PDB; 3Q04; X-ray; 1.80 A; A=3-330.
DR PDB; 3Q9W; X-ray; 1.70 A; A=1-336.
DR PDB; 3Q9X; X-ray; 2.20 A; A/B=1-336.
DR PDB; 3Q9Y; X-ray; 1.80 A; A=1-336.
DR PDB; 3Q9Z; X-ray; 2.20 A; A/B=1-336.
DR PDB; 3QA0; X-ray; 2.50 A; A/B=1-336.
DR PDB; 3R0T; X-ray; 1.75 A; A=1-337.
DR PDB; 3RPS; X-ray; 2.30 A; A/B=1-335.
DR PDB; 3TAX; X-ray; 1.88 A; B/D=340-352.
DR PDB; 3U4U; X-ray; 2.20 A; A=1-333.
DR PDB; 3U87; X-ray; 2.90 A; A/B=1-325.
DR PDB; 3U9C; X-ray; 3.20 A; A/B=1-335.
DR PDB; 3W8L; X-ray; 2.40 A; A/B=1-335.
DR PDB; 3WAR; X-ray; 1.04 A; A=1-335.
DR PDB; 3WIK; X-ray; 2.00 A; A=1-335.
DR PDB; 3WIL; X-ray; 2.90 A; A=1-335.
DR PDB; 3WOW; X-ray; 2.50 A; A=1-335.
DR PDB; 4DGL; X-ray; 3.00 A; C/D=1-335.
DR PDB; 4FBX; X-ray; 2.33 A; A=1-335.
DR PDB; 4GRB; X-ray; 2.15 A; A=1-333.
DR PDB; 4GUB; X-ray; 2.20 A; A=1-333.
DR PDB; 4GYW; X-ray; 1.70 A; B/D=340-352.
DR PDB; 4GYY; X-ray; 1.85 A; B/D=340-352.
DR PDB; 4GZ3; X-ray; 1.90 A; B/D=340-352.
DR PDB; 4IB5; X-ray; 2.20 A; A/B/C=1-335.
DR PDB; 4KWP; X-ray; 1.25 A; A=1-336.
DR PDB; 4MD7; X-ray; 3.10 A; E/F/G/H=1-391.
DR PDB; 4MD8; X-ray; 3.30 A; E/F/G/H=1-391.
DR PDB; 4MD9; X-ray; 3.50 A; E/F/G/H/K/L/M/P=1-336.
DR PDB; 4NH1; X-ray; 3.30 A; A/B=1-335.
DR PDB; 4RLL; X-ray; 1.85 A; A=1-335.
DR PDB; 4UB7; X-ray; 2.10 A; A=1-335.
DR PDB; 4UBA; X-ray; 3.00 A; A/B=1-335.
DR PDB; 5B0X; X-ray; 2.30 A; A=1-335.
DR PDB; 5CLP; X-ray; 1.68 A; A/B=2-329.
DR PDB; 5CQU; X-ray; 2.35 A; A=1-335.
DR PDB; 5CQW; X-ray; 2.65 A; A/B=1-335.
DR PDB; 5CS6; X-ray; 1.88 A; A/B=2-329.
DR PDB; 5CSH; X-ray; 1.59 A; A/B=2-329.
DR PDB; 5CSP; X-ray; 1.50 A; A=2-329.
DR PDB; 5CSV; X-ray; 1.38 A; A=2-329.
DR PDB; 5CT0; X-ray; 2.01 A; A/B=2-329.
DR PDB; 5CTP; X-ray; 2.03 A; A/B=2-329.
DR PDB; 5CU0; X-ray; 2.18 A; A/B=2-329.
DR PDB; 5CU2; X-ray; 1.71 A; A/B=2-329.
DR PDB; 5CU3; X-ray; 1.79 A; A/B=2-329.
DR PDB; 5CU4; X-ray; 1.56 A; A=2-329.
DR PDB; 5CU6; X-ray; 1.36 A; A=2-329.
DR PDB; 5CVF; X-ray; 1.63 A; A=2-329.
DR PDB; 5CVG; X-ray; 1.25 A; A=2-329.
DR PDB; 5CVH; X-ray; 1.85 A; A/B=2-329.
DR PDB; 5CX9; X-ray; 1.73 A; A/B=2-329.
DR PDB; 5H8B; X-ray; 2.55 A; A/B=1-333.
DR PDB; 5H8E; X-ray; 2.15 A; A/B=1-333.
DR PDB; 5H8G; X-ray; 2.00 A; A=1-333.
DR PDB; 5HGV; X-ray; 2.05 A; B/D=340-352.
DR PDB; 5KU8; X-ray; 2.22 A; A/B=2-332.
DR PDB; 5KWH; X-ray; 2.12 A; A/B=1-333.
DR PDB; 5M44; X-ray; 2.71 A; A=1-335.
DR PDB; 5M4C; X-ray; 1.94 A; A=1-335.
DR PDB; 5M4F; X-ray; 1.52 A; A=1-335.
DR PDB; 5M4I; X-ray; 2.22 A; A=1-335.
DR PDB; 5MMF; X-ray; 1.99 A; A/B=2-329.
DR PDB; 5MMR; X-ray; 2.00 A; A/B=2-329.
DR PDB; 5MO5; X-ray; 2.04 A; A/B=2-329.
DR PDB; 5MO6; X-ray; 1.82 A; A/B=2-329.
DR PDB; 5MO7; X-ray; 2.15 A; A/B=2-329.
DR PDB; 5MO8; X-ray; 1.82 A; A/B=2-329.
DR PDB; 5MOD; X-ray; 2.08 A; A/B=2-329.
DR PDB; 5MOE; X-ray; 1.89 A; A/B=2-329.
DR PDB; 5MOH; X-ray; 1.38 A; A=2-329.
DR PDB; 5MOT; X-ray; 2.09 A; A=2-329.
DR PDB; 5MOV; X-ray; 2.20 A; A=3-327.
DR PDB; 5MOW; X-ray; 1.86 A; A/B=2-329.
DR PDB; 5MP8; X-ray; 1.92 A; A/B=2-329.
DR PDB; 5MPJ; X-ray; 2.14 A; A/B=2-329.
DR PDB; 5N1V; X-ray; 2.52 A; A/B=1-336.
DR PDB; 5N9K; X-ray; 1.64 A; A=1-335.
DR PDB; 5N9L; X-ray; 1.79 A; A=1-335.
DR PDB; 5N9N; X-ray; 1.84 A; A=1-335.
DR PDB; 5NQC; X-ray; 2.00 A; A=2-335.
DR PDB; 5OMY; X-ray; 1.95 A; A=1-391.
DR PDB; 5ONI; X-ray; 2.00 A; A/B=1-391.
DR PDB; 5OQU; X-ray; 2.32 A; A/B=2-329.
DR PDB; 5ORH; X-ray; 1.75 A; A/B=2-329.
DR PDB; 5ORJ; X-ray; 1.99 A; A/B=2-329.
DR PDB; 5ORK; X-ray; 2.14 A; A/B=2-329.
DR PDB; 5OS7; X-ray; 1.66 A; A/B=2-329.
DR PDB; 5OS8; X-ray; 1.55 A; A=2-329.
DR PDB; 5OSL; X-ray; 1.95 A; A=2-329.
DR PDB; 5OSP; X-ray; 1.91 A; A=2-329.
DR PDB; 5OSR; X-ray; 1.57 A; A=2-329.
DR PDB; 5OSU; X-ray; 1.63 A; A=2-329.
DR PDB; 5OSZ; X-ray; 2.00 A; A=2-329.
DR PDB; 5OT5; X-ray; 1.63 A; A/B=2-329.
DR PDB; 5OT6; X-ray; 1.94 A; A/B=2-329.
DR PDB; 5OTD; X-ray; 1.57 A; A/B=2-329.
DR PDB; 5OTH; X-ray; 1.69 A; A/B=2-329.
DR PDB; 5OTI; X-ray; 1.59 A; A=2-329.
DR PDB; 5OTL; X-ray; 1.57 A; A/B=2-329.
DR PDB; 5OTO; X-ray; 1.51 A; A/B=2-329.
DR PDB; 5OTP; X-ray; 1.57 A; A/B=2-329.
DR PDB; 5OTQ; X-ray; 1.38 A; A=2-329.
DR PDB; 5OTR; X-ray; 1.52 A; A=2-329.
DR PDB; 5OTS; X-ray; 1.90 A; A=2-329.
DR PDB; 5OTY; X-ray; 1.48 A; A=2-329.
DR PDB; 5OTZ; X-ray; 1.46 A; A=2-329.
DR PDB; 5OUE; X-ray; 2.01 A; A/B=2-329.
DR PDB; 5OUL; X-ray; 1.34 A; A=2-329.
DR PDB; 5OUM; X-ray; 2.05 A; A/B=2-329.
DR PDB; 5OUU; X-ray; 1.81 A; A/B=2-329.
DR PDB; 5OWH; X-ray; 2.30 A; A=1-335.
DR PDB; 5OWL; X-ray; 2.23 A; A/B=1-335.
DR PDB; 5OYF; X-ray; 1.54 A; A=2-329.
DR PDB; 5T1H; X-ray; 2.11 A; A/B=1-333.
DR PDB; 5VIE; X-ray; 2.60 A; B/D=339-352.
DR PDB; 5VIF; X-ray; 2.25 A; B=339-352.
DR PDB; 5ZN0; Other; 1.10 A; A=1-329.
DR PDB; 5ZN1; X-ray; 1.05 A; A=1-329.
DR PDB; 5ZN2; X-ray; 1.20 A; A=1-329.
DR PDB; 5ZN3; X-ray; 1.50 A; A=1-329.
DR PDB; 5ZN4; X-ray; 1.65 A; A=1-329.
DR PDB; 5ZN5; X-ray; 1.70 A; A=1-329.
DR PDB; 6A1C; X-ray; 1.68 A; A=1-335.
DR PDB; 6E37; X-ray; 2.53 A; B=339-352.
DR PDB; 6EHK; X-ray; 1.40 A; A=2-329.
DR PDB; 6EHU; X-ray; 1.95 A; A/B=2-329.
DR PDB; 6EII; X-ray; 1.94 A; A/B=2-329.
DR PDB; 6FVF; X-ray; 1.47 A; A=2-329.
DR PDB; 6FVG; X-ray; 1.60 A; A=2-329.
DR PDB; 6GIH; X-ray; 1.96 A; A=2-329.
DR PDB; 6GMD; X-ray; 1.66 A; A/B=2-329.
DR PDB; 6HBN; X-ray; 1.59 A; A/B=1-335.
DR PDB; 6HME; X-ray; 1.85 A; A/B=1-335.
DR PDB; 6HNW; X-ray; 2.00 A; A=1-336.
DR PDB; 6HNY; X-ray; 1.65 A; A=1-336.
DR PDB; 6HOP; X-ray; 1.55 A; A=1-336.
DR PDB; 6HOQ; X-ray; 1.55 A; A=1-336.
DR PDB; 6HOR; X-ray; 1.80 A; A=1-336.
DR PDB; 6HOT; X-ray; 1.50 A; A=1-336.
DR PDB; 6HOU; X-ray; 1.80 A; A=1-336.
DR PDB; 6JWA; X-ray; 1.78 A; A=1-335.
DR PDB; 6L1Z; X-ray; 1.91 A; A=1-335.
DR PDB; 6L21; X-ray; 2.05 A; A=1-335.
DR PDB; 6L22; X-ray; 2.12 A; A=1-335.
DR PDB; 6L23; X-ray; 1.97 A; A=1-335.
DR PDB; 6L24; X-ray; 2.40 A; A=1-335.
DR PDB; 6Q38; X-ray; 1.74 A; A=3-329.
DR PDB; 6Q4Q; X-ray; 1.45 A; A/B=3-329.
DR PDB; 6QY7; X-ray; 2.10 A; A/B=1-337.
DR PDB; 6RB1; X-ray; 1.50 A; A=1-336.
DR PDB; 6RCB; X-ray; 2.05 A; A=1-336.
DR PDB; 6RCM; X-ray; 1.70 A; A=1-336.
DR PDB; 6RFE; X-ray; 1.54 A; A=1-336.
DR PDB; 6RFF; X-ray; 1.80 A; A=1-336.
DR PDB; 6SPW; X-ray; 1.60 A; A=1-391.
DR PDB; 6SPX; X-ray; 1.99 A; A=1-335.
DR PDB; 6TEI; X-ray; 1.76 A; A/B=1-335.
DR PDB; 6TLL; X-ray; 1.88 A; A=1-391.
DR PDB; 6TLO; X-ray; 1.69 A; A=1-391.
DR PDB; 6TLP; X-ray; 1.93 A; A=1-391.
DR PDB; 6TLR; X-ray; 1.64 A; A=1-391.
DR PDB; 6TLS; X-ray; 1.46 A; A=1-391.
DR PDB; 6TLU; X-ray; 1.81 A; AAA=1-391.
DR PDB; 6TLV; X-ray; 1.67 A; A=1-391.
DR PDB; 6TLW; X-ray; 1.73 A; A=1-391.
DR PDB; 6YPG; X-ray; 1.51 A; A=2-329.
DR PDB; 6YPH; X-ray; 1.67 A; A/B=2-329.
DR PDB; 6YPJ; X-ray; 1.64 A; A=2-329.
DR PDB; 6YPK; X-ray; 1.79 A; A=2-329.
DR PDB; 6YPN; X-ray; 1.58 A; B=1-329.
DR PDB; 6YUL; X-ray; 2.40 A; AAA/GGG=1-391.
DR PDB; 6YUM; X-ray; 2.75 A; AAA/GGG=1-391.
DR PDB; 6YZH; X-ray; 1.19 A; A=3-329.
DR PDB; 6Z19; X-ray; 1.47 A; B=2-329.
DR PDB; 6Z83; X-ray; 2.17 A; AAA/BBB=1-337.
DR PDB; 6Z84; X-ray; 2.50 A; AAA/BBB=1-337.
DR PDB; 7A49; X-ray; 2.03 A; A/B=1-335.
DR PDB; 7A4B; X-ray; 2.06 A; A/B=1-335.
DR PDB; 7A4C; X-ray; 2.50 A; A/B=1-335.
DR PDB; 7AT5; X-ray; 1.77 A; A/B=1-335.
DR PDB; 7AY9; X-ray; 2.25 A; A/B=1-336.
DR PDB; 7AYA; X-ray; 2.45 A; A/B=1-336.
DR PDB; 7B8H; X-ray; 1.34 A; A=1-335.
DR PDB; 7B8I; X-ray; 2.55 A; A/B=1-335.
DR PDB; 7BU4; X-ray; 1.70 A; A=1-335.
DR PDB; 7L1X; X-ray; 1.80 A; A=2-335.
DR PDB; 7PSU; X-ray; 1.77 A; A/B=1-391.
DR PDBsum; 1JWH; -.
DR PDBsum; 1NA7; -.
DR PDBsum; 1PJK; -.
DR PDBsum; 2PVR; -.
DR PDBsum; 2ZJW; -.
DR PDBsum; 3AMY; -.
DR PDBsum; 3AT2; -.
DR PDBsum; 3AT3; -.
DR PDBsum; 3AT4; -.
DR PDBsum; 3AXW; -.
DR PDBsum; 3BQC; -.
DR PDBsum; 3C13; -.
DR PDBsum; 3FWQ; -.
DR PDBsum; 3H30; -.
DR PDBsum; 3JUH; -.
DR PDBsum; 3MB6; -.
DR PDBsum; 3MB7; -.
DR PDBsum; 3NGA; -.
DR PDBsum; 3NSZ; -.
DR PDBsum; 3OWJ; -.
DR PDBsum; 3OWK; -.
DR PDBsum; 3OWL; -.
DR PDBsum; 3PE1; -.
DR PDBsum; 3PE2; -.
DR PDBsum; 3PE4; -.
DR PDBsum; 3Q04; -.
DR PDBsum; 3Q9W; -.
DR PDBsum; 3Q9X; -.
DR PDBsum; 3Q9Y; -.
DR PDBsum; 3Q9Z; -.
DR PDBsum; 3QA0; -.
DR PDBsum; 3R0T; -.
DR PDBsum; 3RPS; -.
DR PDBsum; 3TAX; -.
DR PDBsum; 3U4U; -.
DR PDBsum; 3U87; -.
DR PDBsum; 3U9C; -.
DR PDBsum; 3W8L; -.
DR PDBsum; 3WAR; -.
DR PDBsum; 3WIK; -.
DR PDBsum; 3WIL; -.
DR PDBsum; 3WOW; -.
DR PDBsum; 4DGL; -.
DR PDBsum; 4FBX; -.
DR PDBsum; 4GRB; -.
DR PDBsum; 4GUB; -.
DR PDBsum; 4GYW; -.
DR PDBsum; 4GYY; -.
DR PDBsum; 4GZ3; -.
DR PDBsum; 4IB5; -.
DR PDBsum; 4KWP; -.
DR PDBsum; 4MD7; -.
DR PDBsum; 4MD8; -.
DR PDBsum; 4MD9; -.
DR PDBsum; 4NH1; -.
DR PDBsum; 4RLL; -.
DR PDBsum; 4UB7; -.
DR PDBsum; 4UBA; -.
DR PDBsum; 5B0X; -.
DR PDBsum; 5CLP; -.
DR PDBsum; 5CQU; -.
DR PDBsum; 5CQW; -.
DR PDBsum; 5CS6; -.
DR PDBsum; 5CSH; -.
DR PDBsum; 5CSP; -.
DR PDBsum; 5CSV; -.
DR PDBsum; 5CT0; -.
DR PDBsum; 5CTP; -.
DR PDBsum; 5CU0; -.
DR PDBsum; 5CU2; -.
DR PDBsum; 5CU3; -.
DR PDBsum; 5CU4; -.
DR PDBsum; 5CU6; -.
DR PDBsum; 5CVF; -.
DR PDBsum; 5CVG; -.
DR PDBsum; 5CVH; -.
DR PDBsum; 5CX9; -.
DR PDBsum; 5H8B; -.
DR PDBsum; 5H8E; -.
DR PDBsum; 5H8G; -.
DR PDBsum; 5HGV; -.
DR PDBsum; 5KU8; -.
DR PDBsum; 5KWH; -.
DR PDBsum; 5M44; -.
DR PDBsum; 5M4C; -.
DR PDBsum; 5M4F; -.
DR PDBsum; 5M4I; -.
DR PDBsum; 5MMF; -.
DR PDBsum; 5MMR; -.
DR PDBsum; 5MO5; -.
DR PDBsum; 5MO6; -.
DR PDBsum; 5MO7; -.
DR PDBsum; 5MO8; -.
DR PDBsum; 5MOD; -.
DR PDBsum; 5MOE; -.
DR PDBsum; 5MOH; -.
DR PDBsum; 5MOT; -.
DR PDBsum; 5MOV; -.
DR PDBsum; 5MOW; -.
DR PDBsum; 5MP8; -.
DR PDBsum; 5MPJ; -.
DR PDBsum; 5N1V; -.
DR PDBsum; 5N9K; -.
DR PDBsum; 5N9L; -.
DR PDBsum; 5N9N; -.
DR PDBsum; 5NQC; -.
DR PDBsum; 5OMY; -.
DR PDBsum; 5ONI; -.
DR PDBsum; 5OQU; -.
DR PDBsum; 5ORH; -.
DR PDBsum; 5ORJ; -.
DR PDBsum; 5ORK; -.
DR PDBsum; 5OS7; -.
DR PDBsum; 5OS8; -.
DR PDBsum; 5OSL; -.
DR PDBsum; 5OSP; -.
DR PDBsum; 5OSR; -.
DR PDBsum; 5OSU; -.
DR PDBsum; 5OSZ; -.
DR PDBsum; 5OT5; -.
DR PDBsum; 5OT6; -.
DR PDBsum; 5OTD; -.
DR PDBsum; 5OTH; -.
DR PDBsum; 5OTI; -.
DR PDBsum; 5OTL; -.
DR PDBsum; 5OTO; -.
DR PDBsum; 5OTP; -.
DR PDBsum; 5OTQ; -.
DR PDBsum; 5OTR; -.
DR PDBsum; 5OTS; -.
DR PDBsum; 5OTY; -.
DR PDBsum; 5OTZ; -.
DR PDBsum; 5OUE; -.
DR PDBsum; 5OUL; -.
DR PDBsum; 5OUM; -.
DR PDBsum; 5OUU; -.
DR PDBsum; 5OWH; -.
DR PDBsum; 5OWL; -.
DR PDBsum; 5OYF; -.
DR PDBsum; 5T1H; -.
DR PDBsum; 5VIE; -.
DR PDBsum; 5VIF; -.
DR PDBsum; 5ZN0; -.
DR PDBsum; 5ZN1; -.
DR PDBsum; 5ZN2; -.
DR PDBsum; 5ZN3; -.
DR PDBsum; 5ZN4; -.
DR PDBsum; 5ZN5; -.
DR PDBsum; 6A1C; -.
DR PDBsum; 6E37; -.
DR PDBsum; 6EHK; -.
DR PDBsum; 6EHU; -.
DR PDBsum; 6EII; -.
DR PDBsum; 6FVF; -.
DR PDBsum; 6FVG; -.
DR PDBsum; 6GIH; -.
DR PDBsum; 6GMD; -.
DR PDBsum; 6HBN; -.
DR PDBsum; 6HME; -.
DR PDBsum; 6HNW; -.
DR PDBsum; 6HNY; -.
DR PDBsum; 6HOP; -.
DR PDBsum; 6HOQ; -.
DR PDBsum; 6HOR; -.
DR PDBsum; 6HOT; -.
DR PDBsum; 6HOU; -.
DR PDBsum; 6JWA; -.
DR PDBsum; 6L1Z; -.
DR PDBsum; 6L21; -.
DR PDBsum; 6L22; -.
DR PDBsum; 6L23; -.
DR PDBsum; 6L24; -.
DR PDBsum; 6Q38; -.
DR PDBsum; 6Q4Q; -.
DR PDBsum; 6QY7; -.
DR PDBsum; 6RB1; -.
DR PDBsum; 6RCB; -.
DR PDBsum; 6RCM; -.
DR PDBsum; 6RFE; -.
DR PDBsum; 6RFF; -.
DR PDBsum; 6SPW; -.
DR PDBsum; 6SPX; -.
DR PDBsum; 6TEI; -.
DR PDBsum; 6TLL; -.
DR PDBsum; 6TLO; -.
DR PDBsum; 6TLP; -.
DR PDBsum; 6TLR; -.
DR PDBsum; 6TLS; -.
DR PDBsum; 6TLU; -.
DR PDBsum; 6TLV; -.
DR PDBsum; 6TLW; -.
DR PDBsum; 6YPG; -.
DR PDBsum; 6YPH; -.
DR PDBsum; 6YPJ; -.
DR PDBsum; 6YPK; -.
DR PDBsum; 6YPN; -.
DR PDBsum; 6YUL; -.
DR PDBsum; 6YUM; -.
DR PDBsum; 6YZH; -.
DR PDBsum; 6Z19; -.
DR PDBsum; 6Z83; -.
DR PDBsum; 6Z84; -.
DR PDBsum; 7A49; -.
DR PDBsum; 7A4B; -.
DR PDBsum; 7A4C; -.
DR PDBsum; 7AT5; -.
DR PDBsum; 7AY9; -.
DR PDBsum; 7AYA; -.
DR PDBsum; 7B8H; -.
DR PDBsum; 7B8I; -.
DR PDBsum; 7BU4; -.
DR PDBsum; 7L1X; -.
DR PDBsum; 7PSU; -.
DR AlphaFoldDB; P68400; -.
DR SMR; P68400; -.
DR BioGRID; 107841; 659.
DR ComplexPortal; CPX-2437; Casein kinase II complex, CSNK2A1-CNSK2A2 variant.
DR ComplexPortal; CPX-914; Casein kinase II complex, CSNK2A1 variant.
DR CORUM; P68400; -.
DR DIP; DIP-32682N; -.
DR IntAct; P68400; 406.
DR MINT; P68400; -.
DR STRING; 9606.ENSP00000217244; -.
DR BindingDB; P68400; -.
DR ChEMBL; CHEMBL3629; -.
DR DrugBank; DB01765; (5-hydroxyindolo[1,2-a]quinazolin-7-yl)acetic acid.
DR DrugBank; DB03035; 1,8-Di-Hydroxy-4-Nitro-Anthraquinone.
DR DrugBank; DB02170; 1,8-Di-Hydroxy-4-Nitro-Xanthen-9-One.
DR DrugBank; DB08338; 19-(cyclopropylamino)-4,6,7,15-tetrahydro-5H-16,1-(azenometheno)-10,14-(metheno)pyrazolo[4,3-o][1,3,9]triazacyclohexadecin-8(9H)-one.
DR DrugBank; DB08354; 2-(4-CHLOROBENZYLAMINO)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE.
DR DrugBank; DB08360; 2-(4-ETHYLPIPERAZIN-1-YL)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE.
DR DrugBank; DB08353; 2-(CYCLOHEXYLMETHYLAMINO)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE.
DR DrugBank; DB07802; 3,8-DIBROMO-7-HYDROXY-4-METHYL-2H-CHROMEN-2-ONE.
DR DrugBank; DB08345; 4-(2-(1H-IMIDAZOL-4-YL)ETHYLAMINO)-2-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE.
DR DrugBank; DB03924; 5,8-Di-Amino-1,4-Dihydroxy-Anthraquinone.
DR DrugBank; DB00171; ATP.
DR DrugBank; DB03127; Benzamidine.
DR DrugBank; DB08473; Dichlororibofuranosylbenzimidazole.
DR DrugBank; DB04719; DIMETHYL-(4,5,6,7-TETRABROMO-1H-BENZOIMIDAZOL-2-YL)-AMINE.
DR DrugBank; DB08846; Ellagic acid.
DR DrugBank; DB07715; Emodin.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB08340; N,N'-DIPHENYLPYRAZOLO[1,5-A][1,3,5]TRIAZINE-2,4-DIAMINE.
DR DrugBank; DB08362; N-(3-(8-CYANO-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZIN-2-YLAMINO)PHENYL)ACETAMIDE.
DR DrugBank; DB04721; N1,N2-ETHYLENE-2-METHYLAMINO-4,5,6,7-TETRABROMO-BENZIMIDAZOLE.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR DrugBank; DB04216; Quercetin.
DR DrugBank; DB08660; Quinalizarin.
DR DrugBank; DB02709; Resveratrol.
DR DrugBank; DB04720; S-METHYL-4,5,6,7-TETRABROMO-BENZIMIDAZOLE.
DR DrugBank; DB04462; Tetrabromo-2-Benzotriazole.
DR DrugCentral; P68400; -.
DR GuidetoPHARMACOLOGY; 1549; -.
DR MoonDB; P68400; Predicted.
DR GlyGen; P68400; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; P68400; -.
DR MetOSite; P68400; -.
DR PhosphoSitePlus; P68400; -.
DR SwissPalm; P68400; -.
DR BioMuta; CSNK2A1; -.
DR DMDM; 55977123; -.
DR EPD; P68400; -.
DR jPOST; P68400; -.
DR MassIVE; P68400; -.
DR MaxQB; P68400; -.
DR PaxDb; P68400; -.
DR PeptideAtlas; P68400; -.
DR PRIDE; P68400; -.
DR ProteomicsDB; 57536; -. [P68400-1]
DR ProteomicsDB; 57537; -. [P68400-2]
DR Antibodypedia; 6236; 759 antibodies from 42 providers.
DR DNASU; 1457; -.
DR Ensembl; ENST00000217244.9; ENSP00000217244.3; ENSG00000101266.19. [P68400-1]
DR Ensembl; ENST00000349736.10; ENSP00000339247.6; ENSG00000101266.19. [P68400-2]
DR Ensembl; ENST00000400217.7; ENSP00000383076.2; ENSG00000101266.19. [P68400-1]
DR Ensembl; ENST00000643660.1; ENSP00000495248.1; ENSG00000101266.19. [P68400-1]
DR Ensembl; ENST00000644003.1; ENSP00000495387.1; ENSG00000101266.19. [P68400-2]
DR Ensembl; ENST00000645623.1; ENSP00000495998.1; ENSG00000101266.19. [P68400-1]
DR Ensembl; ENST00000646305.1; ENSP00000495902.1; ENSG00000101266.19. [P68400-1]
DR Ensembl; ENST00000646477.1; ENSP00000495439.1; ENSG00000101266.19. [P68400-2]
DR Ensembl; ENST00000646561.1; ENSP00000496569.1; ENSG00000101266.19. [P68400-1]
DR Ensembl; ENST00000646814.1; ENSP00000495422.1; ENSG00000101266.19. [P68400-1]
DR Ensembl; ENST00000647348.1; ENSP00000495912.1; ENSG00000101266.19. [P68400-1]
DR GeneID; 1457; -.
DR KEGG; hsa:1457; -.
DR MANE-Select; ENST00000217244.9; ENSP00000217244.3; NM_177559.3; NP_808227.1.
DR UCSC; uc002wdw.2; human. [P68400-1]
DR CTD; 1457; -.
DR DisGeNET; 1457; -.
DR GeneCards; CSNK2A1; -.
DR HGNC; HGNC:2457; CSNK2A1.
DR HPA; ENSG00000101266; Low tissue specificity.
DR MalaCards; CSNK2A1; -.
DR MIM; 115440; gene.
DR MIM; 617062; phenotype.
DR neXtProt; NX_P68400; -.
DR OpenTargets; ENSG00000101266; -.
DR PharmGKB; PA26957; -.
DR VEuPathDB; HostDB:ENSG00000101266; -.
DR eggNOG; KOG0668; Eukaryota.
DR GeneTree; ENSGT00390000004215; -.
DR HOGENOM; CLU_000288_70_4_1; -.
DR InParanoid; P68400; -.
DR OMA; ACEKRPQ; -.
DR OrthoDB; 1098380at2759; -.
DR PhylomeDB; P68400; -.
DR TreeFam; TF300483; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; P68400; -.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR Reactome; R-HSA-201688; WNT mediated activation of DVL.
DR Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
DR Reactome; R-HSA-445144; Signal transduction by L1.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-HSA-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR SignaLink; P68400; -.
DR SIGNOR; P68400; -.
DR BioGRID-ORCS; 1457; 99 hits in 1087 CRISPR screens.
DR ChiTaRS; CSNK2A1; human.
DR EvolutionaryTrace; P68400; -.
DR GeneWiki; Casein_kinase_2,_alpha_1; -.
DR GenomeRNAi; 1457; -.
DR Pharos; P68400; Tchem.
DR PRO; PR:P68400; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P68400; protein.
DR Bgee; ENSG00000101266; Expressed in cortical plate and 201 other tissues.
DR ExpressionAtlas; P68400; baseline and differential.
DR Genevisible; P68400; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0005956; C:protein kinase CK2 complex; IDA:CAFA.
DR GO; GO:0016580; C:Sin3 complex; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051879; F:Hsp90 protein binding; TAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016301; F:kinase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0061077; P:chaperone-mediated protein folding; TAS:UniProtKB.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; TAS:ARUK-UCL.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IGI:ARUK-UCL.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:CAFA.
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:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:1905818; P:regulation of chromosome separation; IMP:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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 3D-structure; Alternative splicing; Apoptosis; ATP-binding;
KW Biological rhythms; Cell cycle; Disease variant; Intellectual disability;
KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase; Wnt signaling pathway.
FT CHAIN 1..391
FT /note="Casein kinase II subunit alpha"
FT /id="PRO_0000085883"
FT DOMAIN 39..324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 36..41
FT /note="Interaction with beta subunit"
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /note="Proton acceptor"
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 MOD_RES 344
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:7592773"
FT MOD_RES 360
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000269|PubMed:7592773"
FT MOD_RES 362
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:7592773"
FT MOD_RES 370
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:7592773,
FT ECO:0007744|PubMed:18691976"
FT VAR_SEQ 1..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041925"
FT VARIANT 47
FT /note="R -> Q (in OCNDS; dbSNP:rs869312845)"
FT /evidence="ECO:0000269|PubMed:27048600"
FT /id="VAR_077045"
FT VARIANT 50
FT /note="Y -> S (in OCNDS; dbSNP:rs869312849)"
FT /evidence="ECO:0000269|PubMed:27048600"
FT /id="VAR_077046"
FT VARIANT 175
FT /note="D -> G (in OCNDS; dbSNP:rs869312848)"
FT /evidence="ECO:0000269|PubMed:27048600"
FT /id="VAR_077047"
FT VARIANT 198
FT /note="K -> R (in OCNDS; dbSNP:rs869312840)"
FT /evidence="ECO:0000269|PubMed:27048600"
FT /id="VAR_077048"
FT CONFLICT 128
FT /note="L -> F (in Ref. 3; CAA49758)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="D -> G (in Ref. 3; CAA49758)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="S -> R (in Ref. 3; CAA49758)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="M -> V (in Ref. 3; CAA49758)"
FT /evidence="ECO:0000305"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:3WAR"
FT TURN 13..18
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:3WAR"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:6YZH"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3WAR"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:3WAR"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:3WAR"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:3WAR"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:3WAR"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:5CU6"
FT HELIX 75..88
FT /evidence="ECO:0007829|PDB:3WAR"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:3WAR"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:3WAR"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:3WAR"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:5CVG"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 130..149
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:3WAR"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3WAR"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:5ZN2"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 212..227
FT /evidence="ECO:0007829|PDB:3WAR"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:3WAR"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:3WAR"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:3WAR"
FT HELIX 325..331
FT /evidence="ECO:0007829|PDB:3WAR"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:1JWH"
SQ SEQUENCE 391 AA; 45144 MW; D3B6F5D13FF7422D CRC64;
MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY SEVFEAINIT
NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD
FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE
FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD
QLVRIAKVLG TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF
LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN MMSGISSVPT
PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ Q
