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

 CSK21_HUMAN             Reviewed;         391 AA.
P68400; B4DYS6; D3DVV8; P19138; P20426; Q14013; Q5U065;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 1.
17-JUN-2020, entry version 184.
RecName: Full=Casein kinase II subunit alpha;
Short=CK II alpha;
EC=2.7.11.1 {ECO:0000269|PubMed:30699359};
Name=CSNK2A1; Synonyms=CK2A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2752008; DOI=10.1021/bi00435a066;
Meisner H., Heller-Harrison R., Buxton J., Czech M.P.;
"Molecular cloning of the human casein kinase II alpha subunit.";
Biochemistry 28:4072-4076(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2174700; DOI=10.1021/bi00488a034;
Lozeman F.J., Litchfield D.W., Piening C., Takio K., Walsh K.A.,
Krebs E.G.;
"Isolation and characterization of human cDNA clones encoding the alpha and
the alpha' subunits of casein kinase II.";
Biochemistry 29:8436-8447(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=8420794; DOI=10.1016/0014-5793(93)81197-8;
Devilat I., Carvallo P.;
"Structure and sequence of an intronless gene for human casein kinase II-
alpha subunit.";
FEBS Lett. 316:114-118(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
Nomura N.;
"Human protein factory for converting the transcriptome into an in vitro-
expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, Muscle, and Uterus;
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).
[10]
PHOSPHORYLATION AT THR-344; THR-360; SER-362 AND SER-370.
PubMed=7592773; DOI=10.1074/jbc.270.43.25872;
Bosc D.G., Slominski E., Sichler C., Litchfield D.W.;
"Phosphorylation of casein kinase II by p34cdc2. Identification of
phosphorylation sites using phosphorylation site mutants in vitro.";
J. Biol. Chem. 270:25872-25878(1995).
[11]
FUNCTION, AND INTERACTION WITH SSRP1 AND SUPT16H.
PubMed=11239457; DOI=10.1016/s1097-2765(01)00176-9;
Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R.,
Lozano G., Zhao Y., Lu H.;
"A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16,
and SSRP1.";
Mol. Cell 7:283-292(2001).
[12]
FUNCTION IN CELL CYCLE.
PubMed=11704824; DOI=10.1038/sj.onc.1204894;
Sayed M., Pelech S., Wong C., Marotta A., Salh B.;
"Protein kinase CK2 is involved in G2 arrest and apoptosis following
spindle damage in epithelial cells.";
Oncogene 20:6994-7005(2001).
[13]
INTERACTION WITH SSRP1 AND SUPT16H.
PubMed=12393879; DOI=10.1074/jbc.m209820200;
Keller D.M., Lu H.;
"p53 serine 392 phosphorylation increases after UV through induction of the
assembly of the CK2.hSPT16.SSRP1 complex.";
J. Biol. Chem. 277:50206-50213(2002).
[14]
FUNCTION IN APOPTOSIS.
PubMed=16193064; DOI=10.1038/sj.emboj.7600827;
Shin S., Lee Y., Kim W., Ko H., Choi H., Kim K.;
"Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing
procaspase-8.";
EMBO J. 24:3532-3542(2005).
[15]
INTERACTION WITH RNPS1.
PubMed=15684395; DOI=10.1128/mcb.25.4.1446-1457.2005;
Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A.,
Suzuki H., Endo H., Kidd V.J., Mayeda A.;
"Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2
phosphorylation.";
Mol. Cell. Biol. 25:1446-1457(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
FUNCTION IN CELL CYCLE.
PubMed=19188443; DOI=10.1128/mcb.01563-08;
St-Denis N.A., Derksen D.R., Litchfield D.W.;
"Evidence for regulation of mitotic progression through temporal
phosphorylation and dephosphorylation of CK2alpha.";
Mol. Cell. Biol. 29:2068-2081(2009).
[18]
REVIEW ON FUNCTION.
PubMed=12631575; DOI=10.1096/fj.02-0473rev;
Meggio F., Pinna L.A.;
"One-thousand-and-one substrates of protein kinase CK2?";
FASEB J. 17:349-368(2003).
[19]
REVIEW ON STRUCTURE.
PubMed=19387553; DOI=10.1007/s00018-009-9149-8;
Niefind K., Raaf J., Issinger O.G.;
"Protein kinase CK2 in health and disease: Protein kinase CK2: from
structures to insights.";
Cell. Mol. Life Sci. 66:1800-1816(2009).
[20]
REVIEW ON FUNCTION.
PubMed=19387552; DOI=10.1007/s00018-009-9150-2;
St-Denis N.A., Litchfield D.W.;
"Protein kinase CK2 in health and disease: From birth to death: the role of
protein kinase CK2 in the regulation of cell proliferation and survival.";
Cell. Mol. Life Sci. 66:1817-1829(2009).
[21]
REVIEW ON FUNCTION.
PubMed=19387551; DOI=10.1007/s00018-009-9151-1;
Filhol O., Cochet C.;
"Protein kinase CK2 in health and disease: Cellular functions of protein
kinase CK2: a dynamic affair.";
Cell. Mol. Life Sci. 66:1830-1839(2009).
[22]
REVIEW ON FUNCTION IN REGULATION OF HSP90.
PubMed=19387550; DOI=10.1007/s00018-009-9152-0;
Miyata Y.;
"Protein kinase CK2 in health and disease: CK2: the kinase controlling the
Hsp90 chaperone machinery.";
Cell. Mol. Life Sci. 66:1840-1849(2009).
[23]
REVIEW ON FUNCTION IN WNT SIGNALING.
PubMed=19387549; DOI=10.1007/s00018-009-9153-z;
Dominguez I., Sonenshein G.E., Seldin D.C.;
"Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF-
kappaB signaling: linking development and cancer.";
Cell. Mol. Life Sci. 66:1850-1857(2009).
[24]
INTERACTION WITH SNAI1.
PubMed=19923321; DOI=10.1091/mbc.e09-06-0504;
MacPherson M.R., Molina P., Souchelnytskyi S., Wernstedt C.,
Martin-Perez J., Portillo F., Cano A.;
"Phosphorylation of serine 11 and serine 92 as new positive regulators of
human Snail1 function: potential involvement of casein kinase-2 and the
cAMP-activated kinase protein kinase A.";
Mol. Biol. Cell 21:244-253(2010).
[25]
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH PML.
PubMed=20625391; DOI=10.1371/journal.pone.0011418;
Hung M.S., Lin Y.C., Mao J.H., Kim I.J., Xu Z., Yang C.T., Jablons D.M.,
You L.;
"Functional polymorphism of the CK2alpha intronless gene plays oncogenic
roles in lung cancer.";
PLoS ONE 5:E11418-E11418(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
FUNCTION, AND INTERACTION WITH PML.
PubMed=22406621; DOI=10.1158/0008-5472.can-11-3159;
Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A.,
Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J.,
Scaglioni P.P.;
"The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its
oncogenic counterpart PML-RARA.";
Cancer Res. 72:2275-2284(2012).
[29]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=23123191; DOI=10.1016/j.bbamcr.2012.10.025;
Ampofo E., Sokolowsky T., Goetz C., Montenarh M.;
"Functional interaction of protein kinase CK2 and activating transcription
factor 4 (ATF4), a key player in the cellular stress response.";
Biochim. Biophys. Acta 1833:439-451(2013).
[30]
FUNCTION, INTERACTION WITH CCAR2, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=24962073; DOI=10.1002/ijc.29043;
Bae J.S., Park S.H., Kim K.M., Kwon K.S., Kim C.Y., Lee H.K., Park B.H.,
Park H.S., Lee H., Moon W.S., Chung M.J., Sylvester K.G., Jang K.Y.;
"CK2alpha phosphorylates DBC1 and is involved in the progression of gastric
carcinoma and predicts poor survival of gastric carcinoma patients.";
Int. J. Cancer 136:797-809(2015).
[31]
INVOLVEMENT IN OCNDS, AND VARIANTS OCNDS GLN-47; SER-50; GLY-175 AND
ARG-198.
PubMed=27048600; DOI=10.1007/s00439-016-1661-y;
Okur V., Cho M.T., Henderson L., Retterer K., Schneider M., Sattler S.,
Niyazov D., Azage M., Smith S., Picker J., Lincoln S., Tarnopolsky M.,
Brady L., Bjornsson H.T., Applegate C., Dameron A., Willaert R., Baskin B.,
Juusola J., Chung W.K.;
"De novo mutations in CSNK2A1 are associated with neurodevelopmental
abnormalities and dysmorphic features.";
Hum. Genet. 135:699-705(2016).
[32]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=30699359; DOI=10.1016/j.celrep.2019.01.018;
Sager R.A., Woodford M.R., Backe S.J., Makedon A.M., Baker-Williams A.J.,
DiGregorio B.T., Loiselle D.R., Haystead T.A., Zachara N.E., Prodromou C.,
Bourboulia D., Schmidt L.S., Linehan W.M., Bratslavsky G., Mollapour M.;
"Post-translational regulation of FNIP1 creates a rheostat for the
molecular chaperone Hsp90.";
Cell Rep. 26:1344-1356(2019).
[33]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337, AND SUBUNIT.
PubMed=11092945; DOI=10.1107/s0907444900013627;
Niefind K., Guerra B., Ermakowa I., Issinger O.G.;
"Crystallization and preliminary characterization of crystals of human
protein kinase CK2.";
Acta Crystallogr. D 56:1680-1684(2000).
[34]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337 IN COMPLEX WITH CSNK2B, AND
SUBUNIT.
PubMed=11574463; DOI=10.1093/emboj/20.19.5320;
Niefind K., Guerra B., Ermakowa I., Issinger O.G.;
"Crystal structure of human protein kinase CK2: insights into basic
properties of the CK2 holoenzyme.";
EMBO J. 20:5320-5331(2001).
[35]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-329.
PubMed=14646071; DOI=10.1107/s0907444903018900;
Pechkova E., Zanotti G., Nicolini C.;
"Three-dimensional atomic structure of a catalytic subunit mutant of human
protein kinase CK2.";
Acta Crystallogr. D 59:2133-2139(2003).
[36]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-335.
PubMed=12860116; DOI=10.1016/s0022-2836(03)00638-7;
Ermakova I., Boldyreff B., Issinger O.G., Niefind K.;
"Crystal structure of a C-terminal deletion mutant of human protein kinase
CK2 catalytic subunit.";
J. Mol. Biol. 330:925-934(2003).
-!- 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 (PubMed:11239457, PubMed:11704824,
PubMed:16193064, PubMed:19188443, PubMed:20625391, PubMed:22406621,
PubMed:24962073). Regulates numerous cellular processes, such as cell
cycle progression, apoptosis and transcription, as well as viral
infection (PubMed:12631575, PubMed:19387552, PubMed:19387551). May act
as a regulatory node which integrates and coordinates numerous signals
leading to an appropriate cellular response (PubMed:12631575,
PubMed:19387552, PubMed:19387551). 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 (PubMed:11704824, PubMed:19188443). Also required for
p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53
following UV irradiation. Can also negatively regulate apoptosis
(PubMed:11239457). Phosphorylates the caspases CASP9 and CASP2 and the
apoptotic regulator NOL3 (PubMed:16193064). Phosphorylation protects
CASP9 from cleavage and activation by CASP8, and inhibits the
dimerization of CASP2 and activation of CASP8 (PubMed:16193064).
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, ATF4, SRF, MAX, JUN, FOS, MYC and MYB (PubMed:19387550,
PubMed:12631575, PubMed:19387552, PubMed:19387551, PubMed:23123191).
Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is
essential for chaperone function (PubMed:19387550). Mediates sequential
phosphorylation of FNIP1, promoting its gradual interaction with Hsp90,
leading to activate both kinase and non-kinase client proteins of Hsp90
(PubMed:30699359). Regulates Wnt signaling by phosphorylating CTNNB1
and the transcription factor LEF1 (PubMed:19387549). Acts as an
ectokinase that phosphorylates several extracellular proteins
(PubMed:19387550, PubMed:12631575, PubMed:19387552, PubMed:19387551).
During viral infection, phosphorylates various proteins involved in the
viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV
(PubMed:19387550, PubMed:12631575, PubMed:19387552, PubMed:19387551).
Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-mediated
degradation (PubMed:20625391, PubMed:22406621). 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 (By similarity). Phosphorylates CCAR2 at 'Thr-454'
in gastric carcinoma tissue (PubMed:24962073).
{ECO:0000250|UniProtKB:P19139, ECO:0000269|PubMed:11239457,
ECO:0000269|PubMed:11704824, ECO:0000269|PubMed:16193064,
ECO:0000269|PubMed:19188443, ECO:0000269|PubMed:20625391,
ECO:0000269|PubMed:22406621, ECO:0000269|PubMed:23123191,
ECO:0000269|PubMed:24962073, ECO:0000269|PubMed:30699359,
ECO:0000303|PubMed:12631575, ECO:0000303|PubMed:19387549,
ECO:0000303|PubMed:19387550, ECO:0000303|PubMed:19387551,
ECO:0000303|PubMed:19387552}.
-!- 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;
Evidence={ECO:0000269|PubMed:20625391, ECO:0000269|PubMed:23123191,
ECO:0000269|PubMed:30699359};
PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
Evidence={ECO:0000269|PubMed:23123191, ECO:0000269|PubMed:30699359};
-!- 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; Evidence={ECO:0000269|PubMed:20625391};
-!- ACTIVITY REGULATION: Constitutively active protein kinase whose
activity is not directly affected by phosphorylation. Seems to be
regulated by level of expression and localization.
-!- 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. Interacts with
SNAI1. Interacts with PML (isoform PML-12). Interacts with CCAR2.
{ECO:0000269|PubMed:11092945, ECO:0000269|PubMed:11239457,
ECO:0000269|PubMed:11574463, ECO:0000269|PubMed:12393879,
ECO:0000269|PubMed:15684395, ECO:0000269|PubMed:19923321,
ECO:0000269|PubMed:20625391, ECO:0000269|PubMed:22406621,
ECO:0000269|PubMed:24962073}.
-!- INTERACTION:
P68400; Q86V38: ATN1; NbExp=3; IntAct=EBI-347804, EBI-11954292;
P68400; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-347804, EBI-10181188;
P68400; O00257-3: CBX4; NbExp=2; IntAct=EBI-347804, EBI-4392727;
P68400; Q8IYX3: CCDC116; NbExp=3; IntAct=EBI-347804, EBI-744311;
P68400; P68400: CSNK2A1; NbExp=4; IntAct=EBI-347804, EBI-347804;
P68400; P19784: CSNK2A2; NbExp=8; IntAct=EBI-347804, EBI-347451;
P68400; P67870: CSNK2B; NbExp=25; IntAct=EBI-347804, EBI-348169;
P68400; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-347804, EBI-12051833;
P68400; Q92997: DVL3; NbExp=4; IntAct=EBI-347804, EBI-739789;
P68400; O75822: EIF3J; NbExp=2; IntAct=EBI-347804, EBI-366647;
P68400; Q8N9E0: FAM133A; NbExp=5; IntAct=EBI-347804, EBI-10268158;
P68400; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-347804, EBI-11977403;
P68400; Q9NW75-2: GPATCH2; NbExp=3; IntAct=EBI-347804, EBI-12068108;
P68400; Q9NWQ4-1: GPATCH2L; NbExp=6; IntAct=EBI-347804, EBI-11959863;
P68400; O15499: GSC2; NbExp=3; IntAct=EBI-347804, EBI-19954058;
P68400; Q13547: HDAC1; NbExp=2; IntAct=EBI-347804, EBI-301834;
P68400; P09017: HOXC4; NbExp=3; IntAct=EBI-347804, EBI-3923226;
P68400; A0A0C4DFT8: JADE2; NbExp=3; IntAct=EBI-347804, EBI-12094820;
P68400; Q14145: KEAP1; NbExp=3; IntAct=EBI-347804, EBI-751001;
P68400; Q5T7B8-2: KIF24; NbExp=3; IntAct=EBI-347804, EBI-10213781;
P68400; O60282: KIF5C; NbExp=4; IntAct=EBI-347804, EBI-717170;
P68400; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-347804, EBI-12039345;
P68400; Q68G74: LHX8; NbExp=3; IntAct=EBI-347804, EBI-8474075;
P68400; Q9NQ69: LHX9; NbExp=3; IntAct=EBI-347804, EBI-10175218;
P68400; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-347804, EBI-10178634;
P68400; P50221: MEOX1; NbExp=3; IntAct=EBI-347804, EBI-2864512;
P68400; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-347804, EBI-16439278;
P68400; Q9BU76: MMTAG2; NbExp=3; IntAct=EBI-347804, EBI-742459;
P68400; P23511: NFYA; NbExp=4; IntAct=EBI-347804, EBI-389739;
P68400; P23511-2: NFYA; NbExp=3; IntAct=EBI-347804, EBI-11061759;
P68400; Q02548: PAX5; NbExp=3; IntAct=EBI-347804, EBI-296331;
P68400; P26367: PAX6; NbExp=5; IntAct=EBI-347804, EBI-747278;
P68400; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-347804, EBI-2339674;
P68400; P78356-2: PIP4K2B; NbExp=3; IntAct=EBI-347804, EBI-11532361;
P68400; P29590: PML; NbExp=2; IntAct=EBI-347804, EBI-295890;
P68400; P78424: POU6F2; NbExp=3; IntAct=EBI-347804, EBI-12029004;
P68400; O75400-2: PRPF40A; NbExp=2; IntAct=EBI-347804, EBI-5280197;
P68400; Q14498: RBM39; NbExp=3; IntAct=EBI-347804, EBI-395290;
P68400; Q04864-2: REL; NbExp=3; IntAct=EBI-347804, EBI-10829018;
P68400; Q6ZNA4: RNF111; NbExp=5; IntAct=EBI-347804, EBI-2129175;
P68400; Q99496: RNF2; NbExp=3; IntAct=EBI-347804, EBI-722416;
P68400; Q96EB6: SIRT1; NbExp=5; IntAct=EBI-347804, EBI-1802965;
P68400; Q92504: SLC39A7; NbExp=4; IntAct=EBI-347804, EBI-1051105;
P68400; O43623: SNAI2; NbExp=3; IntAct=EBI-347804, EBI-9876238;
P68400; P12931: SRC; NbExp=2; IntAct=EBI-347804, EBI-621482;
P68400; Q08945: SSRP1; NbExp=3; IntAct=EBI-347804, EBI-353771;
P68400; Q96MF2: STAC3; NbExp=7; IntAct=EBI-347804, EBI-745680;
P68400; O75683: SURF6; NbExp=2; IntAct=EBI-347804, EBI-2691252;
P68400; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-347804, EBI-11139477;
P68400; Q9NVV9: THAP1; NbExp=7; IntAct=EBI-347804, EBI-741515;
P68400; Q08117-2: TLE5; NbExp=3; IntAct=EBI-347804, EBI-11741437;
P68400; P04637: TP53; NbExp=2; IntAct=EBI-347804, EBI-366083;
P68400; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-347804, EBI-725997;
P68400; Q9H2G4: TSPYL2; NbExp=3; IntAct=EBI-347804, EBI-947459;
P68400; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-347804, EBI-12272076;
P68400; Q8IYI8: ZNF440; NbExp=3; IntAct=EBI-347804, EBI-726439;
P68400; Q96NG5: ZNF558; NbExp=3; IntAct=EBI-347804, EBI-373363;
P68400; Q9BS34: ZNF670; NbExp=3; IntAct=EBI-347804, EBI-745276;
P68400; Q6NSZ9-2: ZSCAN25; NbExp=3; IntAct=EBI-347804, EBI-14650477;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23123191,
ECO:0000269|PubMed:24962073}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P68400-1; Sequence=Displayed;
Name=2;
IsoId=P68400-2; Sequence=VSP_041925;
-!- TISSUE SPECIFICITY: Expressed in gastric carcinoma tissue and the
expression gradually increases with the progression of the carcinoma
(at protein level). {ECO:0000269|PubMed:24962073}.
-!- PTM: 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.
{ECO:0000269|PubMed:7592773}.
-!- DISEASE: Okur-Chung neurodevelopmental syndrome (OCNDS) [MIM:617062]:
An autosomal dominant neurodevelopmental disorder characterized by
developmental delay, intellectual disability, behavioral problems,
hypotonia, speech problems, microcephaly, pachygyria and variable
dysmorphic features. {ECO:0000269|PubMed:27048600}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- 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. Casein kinase 2 has
been found to be increased at protein level and up-regulated at the
level of enzyme activity in the majority of cancers. However, elevated
levels of casein kinase 2 are present in certain normal organs such as
brain and testes.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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EMBL; J02853; AAA56821.1; -; mRNA.
EMBL; M55265; AAA35503.1; -; mRNA.
EMBL; S53149; ABB72474.1; -; mRNA.
EMBL; X70251; CAA49758.1; -; Genomic_DNA.
EMBL; AK302583; BAG63838.1; -; mRNA.
EMBL; BT019792; AAV38595.1; -; mRNA.
EMBL; AB451279; BAG70093.1; -; mRNA.
EMBL; AL049761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471133; EAX10665.1; -; Genomic_DNA.
EMBL; CH471133; EAX10666.1; -; Genomic_DNA.
EMBL; CH471133; EAX10667.1; -; Genomic_DNA.
EMBL; CH471133; EAX10668.1; -; Genomic_DNA.
EMBL; CH471133; EAX10669.1; -; Genomic_DNA.
EMBL; BC011668; AAH11668.1; -; mRNA.
EMBL; BC053532; AAH53532.1; -; mRNA.
EMBL; BC071167; AAH71167.1; -; mRNA.
CCDS; CCDS13003.1; -. [P68400-1]
CCDS; CCDS13004.1; -. [P68400-2]
PIR; A30319; A30319.
RefSeq; NP_001886.1; NM_001895.3. [P68400-1]
RefSeq; NP_808227.1; NM_177559.2. [P68400-1]
RefSeq; NP_808228.1; NM_177560.2. [P68400-2]
PDB; 1JWH; X-ray; 3.10 A; A/B=1-337.
PDB; 1NA7; X-ray; 2.40 A; A=1-329.
PDB; 1PJK; X-ray; 2.50 A; A=2-335.
PDB; 2PVR; X-ray; 1.60 A; A=2-335.
PDB; 2ZJW; X-ray; 2.40 A; A=1-335.
PDB; 3AMY; X-ray; 2.30 A; A=1-335.
PDB; 3AT2; X-ray; 1.60 A; A=1-335.
PDB; 3AT3; X-ray; 2.60 A; A=1-335.
PDB; 3AT4; X-ray; 2.20 A; A=1-335.
PDB; 3AXW; X-ray; 2.50 A; A=1-335.
PDB; 3BQC; X-ray; 1.50 A; A=1-335.
PDB; 3C13; X-ray; 1.95 A; A=1-335.
PDB; 3FWQ; X-ray; 2.30 A; A/B=1-335.
PDB; 3H30; X-ray; 1.56 A; A/B=1-334.
PDB; 3JUH; X-ray; 1.66 A; A/B=1-335.
PDB; 3MB6; X-ray; 1.75 A; A=1-331.
PDB; 3MB7; X-ray; 1.65 A; A=1-331.
PDB; 3NGA; X-ray; 2.71 A; A/B=1-333.
PDB; 3NSZ; X-ray; 1.30 A; A=2-331.
PDB; 3OWJ; X-ray; 1.85 A; A=1-331.
PDB; 3OWK; X-ray; 1.80 A; A=1-331.
PDB; 3OWL; X-ray; 2.10 A; A=1-331.
PDB; 3PE1; X-ray; 1.60 A; A=1-337.
PDB; 3PE2; X-ray; 1.90 A; A=1-337.
PDB; 3PE4; X-ray; 1.95 A; B/D=340-352.
PDB; 3Q04; X-ray; 1.80 A; A=3-330.
PDB; 3Q9W; X-ray; 1.70 A; A=1-336.
PDB; 3Q9X; X-ray; 2.20 A; A/B=1-336.
PDB; 3Q9Y; X-ray; 1.80 A; A=1-336.
PDB; 3Q9Z; X-ray; 2.20 A; A/B=1-336.
PDB; 3QA0; X-ray; 2.50 A; A/B=1-336.
PDB; 3R0T; X-ray; 1.75 A; A=1-337.
PDB; 3RPS; X-ray; 2.30 A; A/B=1-335.
PDB; 3TAX; X-ray; 1.88 A; B/D=340-352.
PDB; 3U4U; X-ray; 2.20 A; A=1-333.
PDB; 3U87; X-ray; 2.90 A; A/B=1-325.
PDB; 3U9C; X-ray; 3.20 A; A/B=1-335.
PDB; 3W8L; X-ray; 2.40 A; A/B=1-335.
PDB; 3WAR; X-ray; 1.04 A; A=1-335.
PDB; 3WIK; X-ray; 2.00 A; A=1-335.
PDB; 3WIL; X-ray; 2.90 A; A=1-335.
PDB; 3WOW; X-ray; 2.50 A; A=1-335.
PDB; 4DGL; X-ray; 3.00 A; C/D=1-335.
PDB; 4FBX; X-ray; 2.33 A; A=1-335.
PDB; 4GRB; X-ray; 2.15 A; A=1-333.
PDB; 4GUB; X-ray; 2.20 A; A=1-333.
PDB; 4GYW; X-ray; 1.70 A; B/D=340-352.
PDB; 4GYY; X-ray; 1.85 A; B/D=340-352.
PDB; 4GZ3; X-ray; 1.90 A; B/D=340-352.
PDB; 4IB5; X-ray; 2.20 A; A/B/C=1-335.
PDB; 4KWP; X-ray; 1.25 A; A=1-336.
PDB; 4MD7; X-ray; 3.10 A; E/F/G/H=1-391.
PDB; 4MD8; X-ray; 3.30 A; E/F/G/H=1-391.
PDB; 4MD9; X-ray; 3.50 A; E/F/G/H/K/L/M/P=1-336.
PDB; 4NH1; X-ray; 3.30 A; A/B=1-335.
PDB; 4RLL; X-ray; 1.85 A; A=1-335.
PDB; 4UB7; X-ray; 2.10 A; A=1-335.
PDB; 4UBA; X-ray; 3.00 A; A/B=1-335.
PDB; 5B0X; X-ray; 2.30 A; A=1-335.
PDB; 5CLP; X-ray; 1.68 A; A/B=2-329.
PDB; 5CQU; X-ray; 2.35 A; A=1-335.
PDB; 5CQW; X-ray; 2.65 A; A/B=1-335.
PDB; 5CS6; X-ray; 1.88 A; A/B=2-329.
PDB; 5CSH; X-ray; 1.59 A; A/B=2-329.
PDB; 5CSP; X-ray; 1.50 A; A=2-329.
PDB; 5CSV; X-ray; 1.38 A; A=2-329.
PDB; 5CT0; X-ray; 2.01 A; A/B=2-329.
PDB; 5CTP; X-ray; 2.03 A; A/B=2-329.
PDB; 5CU0; X-ray; 2.18 A; A/B=2-329.
PDB; 5CU2; X-ray; 1.71 A; A/B=2-329.
PDB; 5CU3; X-ray; 1.79 A; A/B=2-329.
PDB; 5CU4; X-ray; 1.56 A; A=2-329.
PDB; 5CU6; X-ray; 1.36 A; A=2-329.
PDB; 5CVF; X-ray; 1.63 A; A=2-329.
PDB; 5CVG; X-ray; 1.25 A; A=2-329.
PDB; 5CVH; X-ray; 1.85 A; A/B=2-329.
PDB; 5CX9; X-ray; 1.73 A; A/B=2-329.
PDB; 5H8B; X-ray; 2.55 A; A/B=1-333.
PDB; 5H8E; X-ray; 2.15 A; A/B=1-333.
PDB; 5H8G; X-ray; 2.00 A; A=1-333.
PDB; 5HGV; X-ray; 2.05 A; B/D=340-352.
PDB; 5KU8; X-ray; 2.22 A; A/B=2-332.
PDB; 5KWH; X-ray; 2.12 A; A/B=1-333.
PDB; 5M44; X-ray; 2.71 A; A=1-335.
PDB; 5M4C; X-ray; 1.94 A; A=1-335.
PDB; 5M4F; X-ray; 1.52 A; A=1-335.
PDB; 5M4I; X-ray; 2.22 A; A=1-335.
PDB; 5MMF; X-ray; 1.99 A; A/B=2-329.
PDB; 5MMR; X-ray; 2.00 A; A/B=2-329.
PDB; 5MO5; X-ray; 2.04 A; A/B=2-329.
PDB; 5MO6; X-ray; 1.82 A; A/B=2-329.
PDB; 5MO7; X-ray; 2.15 A; A/B=2-329.
PDB; 5MO8; X-ray; 1.82 A; A/B=2-329.
PDB; 5MOD; X-ray; 2.08 A; A/B=2-329.
PDB; 5MOE; X-ray; 1.89 A; A/B=2-329.
PDB; 5MOH; X-ray; 1.38 A; A=2-329.
PDB; 5MOT; X-ray; 2.09 A; A=2-329.
PDB; 5MOV; X-ray; 2.20 A; A=3-327.
PDB; 5MOW; X-ray; 1.86 A; A/B=2-329.
PDB; 5MP8; X-ray; 1.92 A; A/B=2-329.
PDB; 5MPJ; X-ray; 2.14 A; A/B=2-329.
PDB; 5N1V; X-ray; 2.52 A; A/B=1-336.
PDB; 5N9K; X-ray; 1.64 A; A=1-335.
PDB; 5N9L; X-ray; 1.79 A; A=1-335.
PDB; 5N9N; X-ray; 1.84 A; A=1-335.
PDB; 5NQC; X-ray; 2.00 A; A=2-335.
PDB; 5OMY; X-ray; 1.95 A; A=1-391.
PDB; 5ONI; X-ray; 2.00 A; A/B=1-391.
PDB; 5OQU; X-ray; 2.32 A; A/B=2-329.
PDB; 5ORH; X-ray; 1.75 A; A/B=2-329.
PDB; 5ORJ; X-ray; 1.99 A; A/B=2-329.
PDB; 5ORK; X-ray; 2.14 A; A/B=2-329.
PDB; 5OS7; X-ray; 1.66 A; A/B=2-329.
PDB; 5OS8; X-ray; 1.55 A; A=2-329.
PDB; 5OSL; X-ray; 1.95 A; A=2-329.
PDB; 5OSP; X-ray; 1.91 A; A=2-329.
PDB; 5OSR; X-ray; 1.57 A; A=2-329.
PDB; 5OSU; X-ray; 1.63 A; A=2-329.
PDB; 5OSZ; X-ray; 2.00 A; A=2-329.
PDB; 5OT5; X-ray; 1.63 A; A/B=2-329.
PDB; 5OT6; X-ray; 1.94 A; A/B=2-329.
PDB; 5OTD; X-ray; 1.57 A; A/B=2-329.
PDB; 5OTH; X-ray; 1.69 A; A/B=2-329.
PDB; 5OTI; X-ray; 1.59 A; A=2-329.
PDB; 5OTL; X-ray; 1.57 A; A/B=2-329.
PDB; 5OTO; X-ray; 1.51 A; A/B=2-329.
PDB; 5OTP; X-ray; 1.57 A; A/B=2-329.
PDB; 5OTQ; X-ray; 1.38 A; A=2-329.
PDB; 5OTR; X-ray; 1.52 A; A=2-329.
PDB; 5OTS; X-ray; 1.90 A; A=2-329.
PDB; 5OTY; X-ray; 1.48 A; A=2-329.
PDB; 5OTZ; X-ray; 1.46 A; A=2-329.
PDB; 5OUE; X-ray; 2.01 A; A/B=2-329.
PDB; 5OUL; X-ray; 1.34 A; A=2-329.
PDB; 5OUM; X-ray; 2.05 A; A/B=2-329.
PDB; 5OUU; X-ray; 1.81 A; A/B=2-329.
PDB; 5OWH; X-ray; 2.30 A; A=1-335.
PDB; 5OWL; X-ray; 2.23 A; A/B=1-335.
PDB; 5OYF; X-ray; 1.54 A; A=2-329.
PDB; 5T1H; X-ray; 2.11 A; A/B=1-333.
PDB; 5VIE; X-ray; 2.60 A; B/D=339-352.
PDB; 5VIF; X-ray; 2.25 A; B=339-352.
PDB; 5ZN0; Other; 1.10 A; A=1-329.
PDB; 5ZN1; X-ray; 1.05 A; A=1-329.
PDB; 5ZN2; X-ray; 1.20 A; A=1-329.
PDB; 5ZN3; X-ray; 1.50 A; A=1-329.
PDB; 5ZN4; X-ray; 1.65 A; A=1-329.
PDB; 5ZN5; X-ray; 1.70 A; A=1-329.
PDB; 6A1C; X-ray; 1.68 A; A=1-335.
PDB; 6E37; X-ray; 2.53 A; B=339-352.
PDB; 6EHK; X-ray; 1.40 A; A=2-329.
PDB; 6EHU; X-ray; 1.95 A; A/B=2-329.
PDB; 6EII; X-ray; 1.94 A; A/B=2-329.
PDB; 6FVF; X-ray; 1.47 A; A=2-329.
PDB; 6FVG; X-ray; 1.60 A; A=2-329.
PDB; 6GIH; X-ray; 1.96 A; A=2-329.
PDB; 6GMD; X-ray; 1.66 A; A/B=2-329.
PDB; 6HBN; X-ray; 1.59 A; A/B=1-335.
PDB; 6HME; X-ray; 1.85 A; A/B=1-335.
PDB; 6HNW; X-ray; 2.00 A; A=1-336.
PDB; 6HNY; X-ray; 1.65 A; A=1-336.
PDB; 6HOP; X-ray; 1.55 A; A=1-336.
PDB; 6HOQ; X-ray; 1.55 A; A=1-336.
PDB; 6HOR; X-ray; 1.80 A; A=1-336.
PDB; 6HOT; X-ray; 1.50 A; A=1-336.
PDB; 6HOU; X-ray; 1.80 A; A=1-336.
PDB; 6JWA; X-ray; 1.78 A; A=1-335.
PDB; 6L1Z; X-ray; 1.91 A; A=1-335.
PDB; 6L21; X-ray; 2.05 A; A=1-335.
PDB; 6L22; X-ray; 2.12 A; A=1-335.
PDB; 6L24; X-ray; 2.40 A; A=1-335.
PDB; 6Q38; X-ray; 1.74 A; A=3-329.
PDB; 6Q4Q; X-ray; 1.45 A; A/B=3-329.
PDB; 6QY7; X-ray; 2.10 A; A/B=1-337.
PDB; 6SPW; X-ray; 1.60 A; A=1-391.
PDB; 6SPX; X-ray; 1.99 A; A=1-335.
PDBsum; 1JWH; -.
PDBsum; 1NA7; -.
PDBsum; 1PJK; -.
PDBsum; 2PVR; -.
PDBsum; 2ZJW; -.
PDBsum; 3AMY; -.
PDBsum; 3AT2; -.
PDBsum; 3AT3; -.
PDBsum; 3AT4; -.
PDBsum; 3AXW; -.
PDBsum; 3BQC; -.
PDBsum; 3C13; -.
PDBsum; 3FWQ; -.
PDBsum; 3H30; -.
PDBsum; 3JUH; -.
PDBsum; 3MB6; -.
PDBsum; 3MB7; -.
PDBsum; 3NGA; -.
PDBsum; 3NSZ; -.
PDBsum; 3OWJ; -.
PDBsum; 3OWK; -.
PDBsum; 3OWL; -.
PDBsum; 3PE1; -.
PDBsum; 3PE2; -.
PDBsum; 3PE4; -.
PDBsum; 3Q04; -.
PDBsum; 3Q9W; -.
PDBsum; 3Q9X; -.
PDBsum; 3Q9Y; -.
PDBsum; 3Q9Z; -.
PDBsum; 3QA0; -.
PDBsum; 3R0T; -.
PDBsum; 3RPS; -.
PDBsum; 3TAX; -.
PDBsum; 3U4U; -.
PDBsum; 3U87; -.
PDBsum; 3U9C; -.
PDBsum; 3W8L; -.
PDBsum; 3WAR; -.
PDBsum; 3WIK; -.
PDBsum; 3WIL; -.
PDBsum; 3WOW; -.
PDBsum; 4DGL; -.
PDBsum; 4FBX; -.
PDBsum; 4GRB; -.
PDBsum; 4GUB; -.
PDBsum; 4GYW; -.
PDBsum; 4GYY; -.
PDBsum; 4GZ3; -.
PDBsum; 4IB5; -.
PDBsum; 4KWP; -.
PDBsum; 4MD7; -.
PDBsum; 4MD8; -.
PDBsum; 4MD9; -.
PDBsum; 4NH1; -.
PDBsum; 4RLL; -.
PDBsum; 4UB7; -.
PDBsum; 4UBA; -.
PDBsum; 5B0X; -.
PDBsum; 5CLP; -.
PDBsum; 5CQU; -.
PDBsum; 5CQW; -.
PDBsum; 5CS6; -.
PDBsum; 5CSH; -.
PDBsum; 5CSP; -.
PDBsum; 5CSV; -.
PDBsum; 5CT0; -.
PDBsum; 5CTP; -.
PDBsum; 5CU0; -.
PDBsum; 5CU2; -.
PDBsum; 5CU3; -.
PDBsum; 5CU4; -.
PDBsum; 5CU6; -.
PDBsum; 5CVF; -.
PDBsum; 5CVG; -.
PDBsum; 5CVH; -.
PDBsum; 5CX9; -.
PDBsum; 5H8B; -.
PDBsum; 5H8E; -.
PDBsum; 5H8G; -.
PDBsum; 5HGV; -.
PDBsum; 5KU8; -.
PDBsum; 5KWH; -.
PDBsum; 5M44; -.
PDBsum; 5M4C; -.
PDBsum; 5M4F; -.
PDBsum; 5M4I; -.
PDBsum; 5MMF; -.
PDBsum; 5MMR; -.
PDBsum; 5MO5; -.
PDBsum; 5MO6; -.
PDBsum; 5MO7; -.
PDBsum; 5MO8; -.
PDBsum; 5MOD; -.
PDBsum; 5MOE; -.
PDBsum; 5MOH; -.
PDBsum; 5MOT; -.
PDBsum; 5MOV; -.
PDBsum; 5MOW; -.
PDBsum; 5MP8; -.
PDBsum; 5MPJ; -.
PDBsum; 5N1V; -.
PDBsum; 5N9K; -.
PDBsum; 5N9L; -.
PDBsum; 5N9N; -.
PDBsum; 5NQC; -.
PDBsum; 5OMY; -.
PDBsum; 5ONI; -.
PDBsum; 5OQU; -.
PDBsum; 5ORH; -.
PDBsum; 5ORJ; -.
PDBsum; 5ORK; -.
PDBsum; 5OS7; -.
PDBsum; 5OS8; -.
PDBsum; 5OSL; -.
PDBsum; 5OSP; -.
PDBsum; 5OSR; -.
PDBsum; 5OSU; -.
PDBsum; 5OSZ; -.
PDBsum; 5OT5; -.
PDBsum; 5OT6; -.
PDBsum; 5OTD; -.
PDBsum; 5OTH; -.
PDBsum; 5OTI; -.
PDBsum; 5OTL; -.
PDBsum; 5OTO; -.
PDBsum; 5OTP; -.
PDBsum; 5OTQ; -.
PDBsum; 5OTR; -.
PDBsum; 5OTS; -.
PDBsum; 5OTY; -.
PDBsum; 5OTZ; -.
PDBsum; 5OUE; -.
PDBsum; 5OUL; -.
PDBsum; 5OUM; -.
PDBsum; 5OUU; -.
PDBsum; 5OWH; -.
PDBsum; 5OWL; -.
PDBsum; 5OYF; -.
PDBsum; 5T1H; -.
PDBsum; 5VIE; -.
PDBsum; 5VIF; -.
PDBsum; 5ZN0; -.
PDBsum; 5ZN1; -.
PDBsum; 5ZN2; -.
PDBsum; 5ZN3; -.
PDBsum; 5ZN4; -.
PDBsum; 5ZN5; -.
PDBsum; 6A1C; -.
PDBsum; 6E37; -.
PDBsum; 6EHK; -.
PDBsum; 6EHU; -.
PDBsum; 6EII; -.
PDBsum; 6FVF; -.
PDBsum; 6FVG; -.
PDBsum; 6GIH; -.
PDBsum; 6GMD; -.
PDBsum; 6HBN; -.
PDBsum; 6HME; -.
PDBsum; 6HNW; -.
PDBsum; 6HNY; -.
PDBsum; 6HOP; -.
PDBsum; 6HOQ; -.
PDBsum; 6HOR; -.
PDBsum; 6HOT; -.
PDBsum; 6HOU; -.
PDBsum; 6JWA; -.
PDBsum; 6L1Z; -.
PDBsum; 6L21; -.
PDBsum; 6L22; -.
PDBsum; 6L24; -.
PDBsum; 6Q38; -.
PDBsum; 6Q4Q; -.
PDBsum; 6QY7; -.
PDBsum; 6SPW; -.
PDBsum; 6SPX; -.
SMR; P68400; -.
BioGRID; 107841; 519.
CORUM; P68400; -.
DIP; DIP-32682N; -.
IntAct; P68400; 353.
MINT; P68400; -.
STRING; 9606.ENSP00000217244; -.
BindingDB; P68400; -.
ChEMBL; CHEMBL3629; -.
DrugBank; DB01765; (5-Oxo-5,6-Dihydro-Indolo[1,2-a]Quinazolin-7-Yl)-Acetic Acid.
DrugBank; DB08660; 1,2,5,8-tetrahydroxyanthracene-9,10-dione.
DrugBank; DB03035; 1,8-Di-Hydroxy-4-Nitro-Anthraquinone.
DrugBank; DB02170; 1,8-Di-Hydroxy-4-Nitro-Xanthen-9-One.
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.
DrugBank; DB08354; 2-(4-CHLOROBENZYLAMINO)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE.
DrugBank; DB08360; 2-(4-ETHYLPIPERAZIN-1-YL)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE.
DrugBank; DB08353; 2-(CYCLOHEXYLMETHYLAMINO)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE.
DrugBank; DB07802; 3,8-DIBROMO-7-HYDROXY-4-METHYL-2H-CHROMEN-2-ONE.
DrugBank; DB08345; 4-(2-(1H-IMIDAZOL-4-YL)ETHYLAMINO)-2-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE.
DrugBank; DB08473; 5,6-dichloro-1-beta-D-ribofuranosyl-1H-benzimidazole.
DrugBank; DB03924; 5,8-Di-Amino-1,4-Dihydroxy-Anthraquinone.
DrugBank; DB00171; ATP.
DrugBank; DB03127; Benzamidine.
DrugBank; DB04719; DIMETHYL-(4,5,6,7-TETRABROMO-1H-BENZOIMIDAZOL-2-YL)-AMINE.
DrugBank; DB08846; Ellagic acid.
DrugBank; DB07715; Emodin.
DrugBank; DB12010; Fostamatinib.
DrugBank; DB08340; N,N'-DIPHENYLPYRAZOLO[1,5-A][1,3,5]TRIAZINE-2,4-DIAMINE.
DrugBank; DB08362; N-(3-(8-CYANO-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZIN-2-YLAMINO)PHENYL)ACETAMIDE.
DrugBank; DB04721; N1,N2-ETHYLENE-2-METHYLAMINO-4,5,6,7-TETRABROMO-BENZIMIDAZOLE.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB04216; Quercetin.
DrugBank; DB02709; Resveratrol.
DrugBank; DB04720; S-METHYL-4,5,6,7-TETRABROMO-BENZIMIDAZOLE.
DrugBank; DB04462; Tetrabromo-2-Benzotriazole.
DrugCentral; P68400; -.
GuidetoPHARMACOLOGY; 1549; -.
MoonDB; P68400; Predicted.
iPTMnet; P68400; -.
MetOSite; P68400; -.
PhosphoSitePlus; P68400; -.
SwissPalm; P68400; -.
BioMuta; CSNK2A1; -.
DMDM; 55977123; -.
EPD; P68400; -.
jPOST; P68400; -.
MassIVE; P68400; -.
MaxQB; P68400; -.
PaxDb; P68400; -.
PeptideAtlas; P68400; -.
PRIDE; P68400; -.
ProteomicsDB; 57536; -. [P68400-1]
ProteomicsDB; 57537; -. [P68400-2]
Antibodypedia; 6236; 705 antibodies.
DNASU; 1457; -.
Ensembl; ENST00000217244; ENSP00000217244; ENSG00000101266. [P68400-1]
Ensembl; ENST00000349736; ENSP00000339247; ENSG00000101266. [P68400-2]
Ensembl; ENST00000400217; ENSP00000383076; ENSG00000101266. [P68400-1]
Ensembl; ENST00000643660; ENSP00000495248; ENSG00000101266. [P68400-1]
Ensembl; ENST00000644003; ENSP00000495387; ENSG00000101266. [P68400-2]
Ensembl; ENST00000645623; ENSP00000495998; ENSG00000101266. [P68400-1]
Ensembl; ENST00000646305; ENSP00000495902; ENSG00000101266. [P68400-1]
Ensembl; ENST00000646477; ENSP00000495439; ENSG00000101266. [P68400-2]
Ensembl; ENST00000646561; ENSP00000496569; ENSG00000101266. [P68400-1]
Ensembl; ENST00000646814; ENSP00000495422; ENSG00000101266. [P68400-1]
Ensembl; ENST00000647348; ENSP00000495912; ENSG00000101266. [P68400-1]
GeneID; 1457; -.
KEGG; hsa:1457; -.
UCSC; uc002wdw.2; human. [P68400-1]
CTD; 1457; -.
DisGeNET; 1457; -.
EuPathDB; HostDB:ENSG00000101266.16; -.
GeneCards; CSNK2A1; -.
HGNC; HGNC:2457; CSNK2A1.
HPA; ENSG00000101266; Low tissue specificity.
MalaCards; CSNK2A1; -.
MIM; 115440; gene.
MIM; 617062; phenotype.
neXtProt; NX_P68400; -.
OpenTargets; ENSG00000101266; -.
PharmGKB; PA26957; -.
eggNOG; KOG0668; Eukaryota.
eggNOG; ENOG410XNPP; LUCA.
GeneTree; ENSGT00390000004215; -.
HOGENOM; CLU_000288_70_4_1; -.
InParanoid; P68400; -.
KO; K03097; -.
OMA; WHSFINA; -.
OrthoDB; 1098380at2759; -.
PhylomeDB; P68400; -.
TreeFam; TF300483; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-1483191; Synthesis of PC.
Reactome; R-HSA-201688; WNT mediated activation of DVL.
Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
Reactome; R-HSA-8934903; Receptor Mediated Mitophagy.
Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
SignaLink; P68400; -.
SIGNOR; P68400; -.
BioGRID-ORCS; 1457; 77 hits in 819 CRISPR screens.
ChiTaRS; CSNK2A1; human.
EvolutionaryTrace; P68400; -.
GeneWiki; Casein_kinase_2,_alpha_1; -.
GenomeRNAi; 1457; -.
Pharos; P68400; Tchem.
PRO; PR:P68400; -.
Proteomes; UP000005640; Chromosome 20.
RNAct; P68400; protein.
Bgee; ENSG00000101266; Expressed in kidney and 230 other tissues.
ExpressionAtlas; P68400; baseline and differential.
Genevisible; P68400; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016581; C:NuRD complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
GO; GO:0005956; C:protein kinase CK2 complex; IDA:CAFA.
GO; GO:0016580; C:Sin3 complex; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051879; F:Hsp90 protein binding; TAS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016301; F:kinase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0061077; P:chaperone-mediated protein folding; TAS:UniProtKB.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; TAS:ARUK-UCL.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IGI:ARUK-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:CAFA.
GO; GO:0006656; P:phosphatidylcholine biosynthetic process; TAS:Reactome.
GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0006457; P:protein folding; TAS:Reactome.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
GO; GO:1905818; P:regulation of chromosome separation; IMP:UniProtKB.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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;
3D-structure; Alternative splicing; Apoptosis; ATP-binding;
Biological rhythms; Cell cycle; Disease mutation; Kinase;
Mental retardation; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Transcription; Transcription regulation; Transferase;
Wnt signaling pathway.
CHAIN 1..391
/note="Casein kinase II subunit alpha"
/id="PRO_0000085883"
DOMAIN 39..324
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 45..53
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
REGION 36..41
/note="Interaction with beta subunit"
/evidence="ECO:0000250"
ACT_SITE 156
/note="Proton acceptor"
BINDING 68
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
MOD_RES 344
/note="Phosphothreonine; by CDK1"
/evidence="ECO:0000269|PubMed:7592773"
MOD_RES 360
/note="Phosphothreonine; by CDK1"
/evidence="ECO:0000269|PubMed:7592773"
MOD_RES 362
/note="Phosphoserine; by CDK1"
/evidence="ECO:0000269|PubMed:7592773"
MOD_RES 370
/note="Phosphoserine; by CDK1"
/evidence="ECO:0000244|PubMed:18691976,
ECO:0000269|PubMed:7592773"
VAR_SEQ 1..136
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:14702039"
/id="VSP_041925"
VARIANT 47
/note="R -> Q (in OCNDS; dbSNP:rs869312845)"
/evidence="ECO:0000269|PubMed:27048600"
/id="VAR_077045"
VARIANT 50
/note="Y -> S (in OCNDS; dbSNP:rs869312849)"
/evidence="ECO:0000269|PubMed:27048600"
/id="VAR_077046"
VARIANT 175
/note="D -> G (in OCNDS; dbSNP:rs869312848)"
/evidence="ECO:0000269|PubMed:27048600"
/id="VAR_077047"
VARIANT 198
/note="K -> R (in OCNDS; dbSNP:rs869312840)"
/evidence="ECO:0000269|PubMed:27048600"
/id="VAR_077048"
CONFLICT 128
/note="L -> F (in Ref. 3; CAA49758)"
/evidence="ECO:0000305"
CONFLICT 256
/note="D -> G (in Ref. 3; CAA49758)"
/evidence="ECO:0000305"
CONFLICT 287
/note="S -> R (in Ref. 3; CAA49758)"
/evidence="ECO:0000305"
CONFLICT 351
/note="M -> V (in Ref. 3; CAA49758)"
/evidence="ECO:0000305"
STRAND 10..12
/evidence="ECO:0000244|PDB:3WAR"
TURN 13..18
/evidence="ECO:0000244|PDB:3WAR"
HELIX 21..24
/evidence="ECO:0000244|PDB:3WAR"
HELIX 26..28
/evidence="ECO:0000244|PDB:3WAR"
HELIX 36..38
/evidence="ECO:0000244|PDB:3WAR"
STRAND 39..47
/evidence="ECO:0000244|PDB:3WAR"
STRAND 49..58
/evidence="ECO:0000244|PDB:3WAR"
TURN 59..61
/evidence="ECO:0000244|PDB:3WAR"
STRAND 64..70
/evidence="ECO:0000244|PDB:3WAR"
TURN 72..74
/evidence="ECO:0000244|PDB:5CU6"
HELIX 75..88
/evidence="ECO:0000244|PDB:3WAR"
STRAND 97..102
/evidence="ECO:0000244|PDB:3WAR"
TURN 104..106
/evidence="ECO:0000244|PDB:3WAR"
STRAND 107..114
/evidence="ECO:0000244|PDB:3WAR"
TURN 118..120
/evidence="ECO:0000244|PDB:5CVG"
HELIX 121..124
/evidence="ECO:0000244|PDB:3WAR"
HELIX 125..127
/evidence="ECO:0000244|PDB:3WAR"
HELIX 130..149
/evidence="ECO:0000244|PDB:3WAR"
HELIX 159..161
/evidence="ECO:0000244|PDB:3WAR"
STRAND 162..165
/evidence="ECO:0000244|PDB:3WAR"
HELIX 166..168
/evidence="ECO:0000244|PDB:3WAR"
STRAND 170..173
/evidence="ECO:0000244|PDB:3WAR"
HELIX 176..178
/evidence="ECO:0000244|PDB:5ZN2"
HELIX 195..197
/evidence="ECO:0000244|PDB:3WAR"
HELIX 200..203
/evidence="ECO:0000244|PDB:3WAR"
HELIX 212..227
/evidence="ECO:0000244|PDB:3WAR"
STRAND 230..233
/evidence="ECO:0000244|PDB:3WAR"
HELIX 238..249
/evidence="ECO:0000244|PDB:3WAR"
HELIX 251..261
/evidence="ECO:0000244|PDB:3WAR"
HELIX 267..269
/evidence="ECO:0000244|PDB:3WAR"
TURN 270..272
/evidence="ECO:0000244|PDB:3WAR"
HELIX 281..284
/evidence="ECO:0000244|PDB:3WAR"
TURN 287..289
/evidence="ECO:0000244|PDB:3WAR"
HELIX 290..292
/evidence="ECO:0000244|PDB:3WAR"
HELIX 295..304
/evidence="ECO:0000244|PDB:3WAR"
HELIX 309..311
/evidence="ECO:0000244|PDB:3WAR"
HELIX 315..318
/evidence="ECO:0000244|PDB:3WAR"
HELIX 322..324
/evidence="ECO:0000244|PDB:3WAR"
HELIX 325..331
/evidence="ECO:0000244|PDB:3WAR"
STRAND 333..335
/evidence="ECO:0000244|PDB:1JWH"
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


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EIAAB29519 Homo sapiens,Human,Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha,Phosphoinositide 3-kinase-C2-alpha,PI3K-C2-alpha,PIK3C2A,PtdIns-3-kinase C2 subunit alpha
EIAAB29518 Cpk,Cpk-m,Mouse,Mus musculus,p170,Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha,Phosphoinositide 3-kinase-C2-alpha,PI3K-C2-alpha,Pik3c2a,PtdIns-3-kinase C2 subunit alpha
EIAAB09580 Casein kinase II subunit alpha',CK II alpha',Csnk2a2,Mouse,Mus musculus
EIAAB09575 Casein kinase II subunit alpha,CK II alpha,Csnk2a1,Rat,Rattus norvegicus
EIAAB09578 Bos taurus,Bovine,Casein kinase II subunit alpha',CK II alpha',CSNK2A2
EIAAB09576 Bos taurus,Bovine,Casein kinase II subunit alpha,CK II alpha,CK2A1,CSNK2A1
EIAAB09573 Casein kinase II subunit alpha,CK II alpha,Ckiia,Csnk2a1,Mouse,Mus musculus
EIAAB09577 Casein kinase II subunit alpha,CK II alpha,CSNK2A1,Oryctolagus cuniculus,Rabbit
EIAAB09579 Casein kinase II subunit alpha',CK II alpha',CK2A2,CSNK2A2,Homo sapiens,Human
EIAAB09574 Casein kinase II subunit alpha,CK II alpha,CK2A1,CSNK2A1,Homo sapiens,Human
E0655h ELISA kit Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,CAMK2A,CAMKA,CaMK-II subunit alpha,Homo sapiens,Human,KIAA0968 96T
U0655h CLIA Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,CAMK2A,CAMKA,CaMK-II subunit alpha,Homo sapiens,Human,KIAA0968 96T
E0655h ELISA Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,CAMK2A,CAMKA,CaMK-II subunit alpha,Homo sapiens,Human,KIAA0968 96T
ABD-019 anti-hCK2, alpha-subunit anti-human casein kinase 2, alpha-subunit murine, monoclonal 100
E0655m ELISA kit Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,Camk2a,CaMK-II subunit alpha,Mouse,Mus musculus 96T
U0655m CLIA Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,Camk2a,CaMK-II subunit alpha,Mouse,Mus musculus 96T
E0655r ELISA kit Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,Camk2a,CaMK-II subunit alpha,Rat,Rattus norvegicus 96T
E0655r ELISA Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,Camk2a,CaMK-II subunit alpha,Rat,Rattus norvegicus 96T
E0655m ELISA Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,Camk2a,CaMK-II subunit alpha,Mouse,Mus musculus 96T
U0655r CLIA Calcium_calmodulin-dependent protein kinase type II subunit alpha,CaM kinase II subunit alpha,Camk2a,CaMK-II subunit alpha,Rat,Rattus norvegicus 96T
OBT1784 Casein kinase 2 (CKIIa), alpha 1 polypeptide encoded within exon 11, alpha prime subunit, CSNK2A1, Rabbit anti_Human, Mouse; WB_IP 0.1 mg.
18-783-75638 RABBIT ANTI CaMKII - CALCIUM_CALMODULIN-DEPENDENT KINASE II; EC 2.7.11.17; CaM-kinase II alpha chain; CaM kinase II subunit alpha; CaMK-II subunit alpha Polyclonal 0.05 mg
Pathways :
WP32: Translation Factors
WP1655: Geraniol degradation
WP1614: 1- and 2-Methylnaphthalene degradation
WP1566: Citrate cycle (TCA cycle)
WP1584: Type II diabetes mellitus
WP1003: Ovarian Infertility Genes
WP457: TNF-alpha NF-kB Signaling Pathway
WP1163: TNF-alpha NF-kB Signaling Pathway
WP622: Long-Day Flowering Time Pathway
WP246: TNF-alpha NF-kB Signaling Pathway
WP1225: estrogen signalling
WP885: Ovarian Infertility Genes
WP1434: Osteopontin Signaling
WP1963: The effect of Glucocorticoids on target gene expression
WP263: Ovarian Infertility Genes
WP1531: Vitamin D synthesis
WP215: noncanonical wnt pathway
WP1571: EBV LMP1 signaling
WP433: tRNA Synthetases
WP1120: Ovarian Infertility Genes
WP566: canonical wnt - zebrafish
WP1618: alpha-Linolenic acid metabolism
WP244: Alpha 6 Beta 4 signaling pathway
WP1224: EBV LMP1 signaling
WP1835: Interferon alpha/beta signaling

Related Genes :
[CSNK2A1 CK2A1] Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1)
[CSNK2A3 CSNK2A1P] Casein kinase II subunit alpha 3 (CK II alpha 3) (EC 2.7.11.1) (Casein kinase II alpha 1 polypeptide pseudogene)
[CSNK2A2 CK2A2] Casein kinase II subunit alpha' (CK II alpha') (EC 2.7.11.1)
[cka1 orb5 SPAC23C11.11] Casein kinase II subunit alpha (CK II subunit alpha) (EC 2.7.11.1)
[Csnk2a1] Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1)
[Csnk2a1 Ckiia] Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1)
[CSNK2A1 CK2A1] Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1)
[Csnk2a2] Casein kinase II subunit alpha' (CK II alpha') (EC 2.7.11.1)
[cka ck-1b 5C2.270 NCU03124] Casein kinase II subunit alpha (CK II subunit alpha) (EC 2.7.11.1)
[hchA A9819_11910 ACN81_03425 AML35_08765 AW059_23935 BANRA_00208 BANRA_00433 BANRA_02614 BHF46_18455 BMA87_25350 BMT91_24760 BON76_21885 BvCmsC61A_00149 BvCmsKSNP120_04693 BvCmsKSP026_03873 BvCmsKSP076_04891 C7B08_25495 C9Z39_20510 CR538_10415 D3Y67_22910 D4023_08350 D9G42_11130 D9I97_22010 D9J11_25195 D9J52_16665 DJ503_24045 DLX40_18195 DM267_05215 DN627_18690 DP258_02540 DQE91_25240 EC3234A_36c00010 EC382_21100 ECTO6_01955 EHH55_07135 FORC82_1921 FV293_07100 GHR40_13690 GKE15_01795 GKE22_01795 GKE24_01795 GKE26_01795 GKE29_19015 GKE31_01795 GKE39_01795 GKE46_01795 GKE58_00235 GKE60_01795 GKE64_01795 GKE77_01800 GKE87_19180 GKE93_04790 GKF00_12775 GKF03_06100 GKF74_23075 GKF86_23585 GKF89_24720 GKG12_21690 GP700_02420 GP720_02430 GP727_01495 GP912_03195 NCTC12650_02300 NCTC8500_02249 NCTC9117_02637 NCTC9969_02156 SAMEA3472108_01151 SAMEA3484427_04795 SAMEA3484429_02051 SAMEA3752557_05476 SAMEA3752559_04333] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.124) (Maillard deglycase)
[CkIalpha CKI CG2028] Casein kinase I isoform alpha (CKI-alpha) (DmCK1) (EC 2.7.11.1)
[nnrD nnrE BHS81_24940 BMA87_06210 BON75_25135 BUE81_24185 BW690_00535 C5P01_11605 C9114_00800 C9141_20385 C9160_20005 C9201_17640 C9Z03_11025 C9Z39_09990 CF006_04810 CG692_00180 CI641_014360 CI693_12780 COD46_22200 CWS33_03515 D2185_07770 D3821_07085 D3O91_01535 D3Y67_00680 D4011_02210 D4638_06395 D6W00_07670 D6X63_00505 D7W70_13040 D8Y65_09515 D9D20_08295 D9D44_05795 D9G29_02235 D9H68_15720 D9H94_06330 D9I18_04405 D9J11_13510 D9J52_05810 D9J63_13405 DAH30_09295 DAH34_17710 DAH37_06235 DEN89_23315 DEO04_15015 DK132_00975 DL292_04305 DL326_12595 DLU82_19955 DM973_03315 DMC44_08050 DMY83_06260 DNW42_15620 DOY22_05310 DOY61_22135 DQE91_09055 DT034_15395 E0I42_01095 E2119_06500 E5P22_06605 E5S42_20000 EA213_12050 EAI42_08035 EAI42_19730 EAI46_08330 ED307_02425 EEP23_07485 EH186_16255 EI021_09655 EI041_04975 EIZ86_02830 EL75_3998 EL79_4176 EL80_4091 ELT20_09170 EPT01_09990 EXX24_09350 EXX78_19455 F1E13_09470 F1E19_03510 FQ022_21765 FQR64_20885 FRV13_14670 FV293_00830 GHR40_02625 GKF89_03420 GNZ03_04915 GP654_08840 GP689_08305 GQE30_17865 GQE34_01730 GQE51_12505 GQE64_09140 GQL64_02225 GRW80_01300 RK56_012375] Bifunctional NAD(P)H-hydrate repair enzyme (Nicotinamide nucleotide repair protein) [Includes: ADP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.136) (ADP-dependent NAD(P)HX dehydratase); NAD(P)H-hydrate epimerase (EC 5.1.99.6)]
[CSNK2A1] Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1)
[hchA A8C65_13880 A9R57_25255 AMK83_16550 AWB10_10580 AWG90_013200 B7C53_22525 B9M99_11580 B9T59_01945 BJJ90_15205 BMT49_12710 BON65_01250 BON66_15955 BON86_06490 BON95_14610 BUE81_10670 BvCms12BK_01457 BvCms28BK_04168 BvCmsHHP001_02632 BvCmsKKP061_00566 BvCmsKSP045_04450 BvCmsKSP058_03204 BvCmsKSP067_02879 BvCmsNSP006_03750 BvCmsNSP007_03329 BvCmsNSP047_03567 BvCmsSINP011_04162 BW690_17225 BZL69_29425 C2U48_24800 C5715_19445 C5N07_21380 C6669_19295 C7B06_02290 C7B07_03930 C9Z23_21970 C9Z37_00915 C9Z43_06360 C9Z78_05610 CDC27_10055 CDL37_00765 CI693_17820 CI694_25210 CIG45_02340 COD46_23180 CQP61_17160 CRD98_26150 D2188_01360 D4628_09465 D6T98_10515 D6X36_17295 D9D20_21030 D9D43_06110 D9G29_20785 D9G69_01560 D9H68_20750 D9H70_25730 D9I87_15275 D9J58_04360 D9S45_22925 DEN89_24995 DEO04_05510 DL705_18425 DL800_09215 DLU50_17670 DLW88_16170 DLY44_04800 DND16_20085 DNR35_16895 DQE83_22775 DQP61_11280 DTL43_21780 DTZ20_09315 DU321_04440 DXT73_20690 E2134_24005 E2135_17195 E2855_02503 E2863_02392 E4K55_17625 E4K61_03800 E5P22_21380 E5S46_06650 EA213_19000 EA225_13320 EAX79_27320 EC95NR1_00961 ED648_25045 EG796_17135 EHD79_18540 EI028_00085 ELT20_21515 ELV08_24970 EPT01_11070 EQ825_23250 ERS085379_01273 ERS085386_05041 ExPECSC019_03873 ExPECSC038_01920 EXX71_02385 EXX78_21815 EYD11_09165 F7F11_20115 F7F18_11615 F7F29_22635 FNJ83_13175 FQ915_04255 FQR64_09390 FQZ46_21375 FWK02_18105 FZ043_14730 GIY13_02485 GNZ00_15670 GNZ02_11235 GNZ03_00440 GP712_09450 GQE64_12165 GQL64_10635 GQM17_02800 HmCmsJML079_02678 HMPREF3040_01583 HW43_13705 NCTC10082_04431 NCTC10418_03071 NCTC10767_03558 NCTC10974_02300 NCTC11022_01867 NCTC11126_04427 NCTC11181_05650 NCTC12950_02263 NCTC13216_04667 NCTC8985_00529 NCTC9111_05933 NCTC9703_00277 PGD_01271 PU06_24500 SAMEA3472043_00447 SAMEA3472055_03589 SAMEA3472056_01268 SAMEA3472070_00654 SAMEA3472080_04213 SAMEA3472090_03376 SAMEA3472110_00060 SAMEA3472112_00448 SAMEA3752372_00752 UN91_23615 WQ89_10695] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.124) (Maillard deglycase)
[hmpA hmp A6V01_10200 A8C65_03855 A9R57_17040 ACN002_2592 ACN68_11055 ACN81_26320 ACU57_10360 ACU90_01485 AM270_07210 AM464_04560 AML07_10430 APZ14_05505 AUQ13_13215 AUS26_21665 AW106_11070 AWB10_06910 BANRA_01097 BANRA_03418 BANRA_04525 BB545_05760 BHS81_15570 BHS87_14445 BJJ90_06510 BK292_20760 BK296_24730 BMA87_03660 BMT91_09730 BN17_18391 BOH76_09290 BON63_10755 BON69_13990 BON71_13675 BON75_17540 BUE81_08005 BvCms12BK_01774 BvCms2454_04468 BvCmsHHP001_04806 BvCmsHHP019_04806 BvCmsHHP056_01828 BvCmsKSP026_04305 BvCmsNSP072_00267 BvCmsOUP014_02948 BvCmsSIP019_03821 BvCmsSIP044_05092 BVL39_14050 BW690_11150 BZL31_13550 C2U48_21325 C5N07_10115 C5P01_05560 C7235_06805 C9098_02900 C9114_06110 C9141_01855 C9160_04920 C9201_01350 C9306_06605 C9E25_16695 C9Z03_13455 C9Z37_03155 C9Z39_18350 C9Z89_02035 CF006_16010 CI641_005655 CI693_09205 CI694_19335 CIG45_08585 CJU64_15040 CMR93_17935 CO706_10650 COD30_01045 COD46_11500 CRM83_27495 CWS33_10010 D2184_18725 D2185_06690 D3821_11445 D3O91_03570 D3Y67_23905 D4638_14775 D5H35_00985 D6004_00980 D6W00_02395 D7W70_06755 D9610_05050 D9C99_14310 D9D44_02510 D9E19_04690 D9F87_12905 D9G29_09320 D9G69_17680 D9H68_00985 D9I18_09865 D9I97_07905 D9J11_04290 D9J44_00060 D9J63_02360 D9K48_25840 D9S45_04285 D9Z28_05540 DAH18_00220 DAH32_12610 DAH34_18605 DAH37_19275 DEN89_09990 DEO04_07795 DIV22_11300 DJ503_18890 DK132_08375 DL292_04635 DL326_03510 DL479_01320 DL530_01200 DL545_07245 DL800_19195 DLU67_05700 DLU82_05745 DLW60_01510 DLY41_10965 DLY44_09805 DM155_03210 DM267_09015 DM296_18085 DM382_04695 DM973_01355 DN808_02505 DNC98_15250 DNI21_11200 DNX19_14815 DOY61_05325 DP265_12450 DP277_03620 DQE91_09215 DQF36_02795 DQF71_00500 DQF72_12760 DS143_00500 DT034_06375 DTL43_01910 DVB38_05460 DXT69_13075 DXT71_19935 E0I42_02095 E0K84_11045 E2119_10050 E2127_03890 E2128_10370 E2129_06190 E2134_09855 E2135_00930 E2855_03303 E2863_03210 E4K60_01585 E4K61_07850 E5P22_05385 E5P28_04540 E5S47_00200 EA213_03875 EAI42_06330 EAM59_02405 EAN70_01040 EB476_05175 EBA46_07820 EBM08_03540 EC1094V2_1116 EC3234A_44c01590 EC95NR1_01777 ECTO6_01279 ED307_10115 ED600_07770 EEP23_02350 EG599_00985 EG808_01365 EH186_03630 EH412_02350 EHH55_21860 EHJ36_02425 EI021_12090 EI028_07810 EI032_05735 EI041_00200 EIZ86_09040 EIZ93_07130 EKI52_21980 ELT20_16535 ELV08_03290 ELY05_02130 EPT01_18845 ERS085365_01518 ERS085374_00038 ERS085416_03760 ERS139211_00868 ERS150873_01392 ERS150876_00857 EXX71_04790 EXX78_07615 EYD11_06210 EYY78_04395 F1E19_02170 F7F00_00975 F7F23_03720 F7F26_02345 FORC82_1263 FQ022_12130 FQR64_06320 FRV13_24300 FV293_03855 FWK02_18305 FZ043_18225 GHR40_10735 GII67_02720 GKF74_16560 GKF86_17785 GKF89_05425 GKG12_07770 GP654_15220 GP666_02550 GP689_11980 GP935_11615 GP946_10005 GP950_14040 GQE22_07390 GQE34_03495 GQE42_05370 GQE64_06950 GQE93_09845 GQM06_13725 GQM09_02790 GQM17_07930 GRW42_07130 GRW80_05725 HmCms184_00603 HmCmsJML079_04829 HW43_17160 NCTC10963_01285 NCTC11022_02631 NCTC11181_03552 NCTC12650_01586 NCTC13148_02382 NCTC8500_01411 NCTC8960_04037 NCTC8985_06124 NCTC9036_01390 NCTC9058_00631 NCTC9062_01812 NCTC9073_04581 NCTC9706_04593 NCTC9962_00729 PGD_00684 PU06_05410 RG28_09110 RK56_022045 SAMEA3472043_01058 SAMEA3472044_03009 SAMEA3472070_00042 SAMEA3472080_01630 SAMEA3484427_00463 SAMEA3484429_00572 SAMEA3752553_02327 SAMEA3752557_00946 SAMEA3753097_02775 SK85_02808 WQ89_05840] Flavohemoprotein (Flavohemoglobin) (Hemoglobin-like protein) (Nitric oxide dioxygenase) (NO oxygenase) (NOD) (EC 1.14.12.17)
[Eif2ak2 Pkr Prkr Tik] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[CSNK1D HCKID] Casein kinase I isoform delta (CKI-delta) (CKId) (EC 2.7.11.1) (Tau-protein kinase CSNK1D) (EC 2.7.11.26)
[MAPK14 CSBP CSBP1 CSBP2 CSPB1 MXI2 SAPK2A] Mitogen-activated protein kinase 14 (MAP kinase 14) (MAPK 14) (EC 2.7.11.24) (Cytokine suppressive anti-inflammatory drug-binding protein) (CSAID-binding protein) (CSBP) (MAP kinase MXI2) (MAX-interacting protein 2) (Mitogen-activated protein kinase p38 alpha) (MAP kinase p38 alpha) (Stress-activated protein kinase 2a) (SAPK2a)
[CKB2 YOR039W OR26.32] Casein kinase II subunit beta' (CK II beta')
[HD16 CKI EL1 Os03g0793500 LOC_Os03g57940 OsJ_12923 OSJNBb0060J21.12] Casein kinase 1-like protein HD16 (EC 2.7.11.1) (Os03g0793500 protein) (Protein EARLY FLOWERING 1) (Protein HEADING DATE 16)
[FAM20C DMP4] Extracellular serine/threonine protein kinase FAM20C (EC 2.7.11.1) (Dentin matrix protein 4) (DMP-4) (Golgi casein kinase) (Golgi-enriched fraction casein kinase) (GEF-CK)
[PRKAA1 AMPK1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)
[Prkaa1 Ampk1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)
[Csnk1d Hckid] Casein kinase I isoform delta (CKI-delta) (EC 2.7.11.1) (Tau-protein kinase CSNK1D) (EC 2.7.11.26)
[hchA AM465_15370 AWF59_019055 AZZ83_004235 B9N33_26475 BFD68_20845 C7B02_06890 C9Z28_17130 CCZ14_26645 CCZ17_22700 CRJUMX01_1140054 CRT43_11430 CUB99_23505 D3C88_02905 D3P02_16265 D9D33_15385 D9D94_15735 D9E49_19020 D9I20_10460 D9J46_03345 DJ487_18960 DJ492_13470 DL251_00505 DL979_00380 DMC44_18755 DMZ50_24495 DNR41_00375 DS966_16070 DU333_03260 DW236_02290 E0L04_20335 EA159_21345 EA167_21075 EA189_00370 EA191_21560 EA198_02280 EA200_00370 EA203_21510 EA222_02305 EA232_20265 EA233_11705 EA242_17410 EA245_13290 EA429_05770 EA435_21775 EA834_21700 ECTO124_02024 EGT48_04930 ELT23_21030 ELT33_08025 ELT34_19745 ELU82_24705 ELU96_05025 ELV13_26065 ELX79_15035 ELX83_25640 ELY23_20490 ELY24_19085 ELY50_24510 EPS76_06485 EPS91_17475 EPS94_00505 ERS085406_02591 EWK56_00075 ExPECSC065_02714 EYX99_25670 FNJ67_10775 FV295_16190 GFU40_00360 GFU45_09680 GFU47_04835 GJ638_18410 GKE92_23545 GKF28_00040 GKF34_00055 GKF47_00040 GKG08_13460 GKG09_11990 GKG11_12245 GKG22_12830 GKG29_13740 GQE47_24120 GQN33_12435 GQS26_09145 NCTC10766_03778 NCTC7928_05955 NCTC8450_02317 NCTC9007_02951 NCTC9075_02834 SY51_11150 U12A_02105 U14A_02105] Protein/nucleic acid deglycase HchA (EC 3.1.2.-) (EC 3.5.1.124) (Maillard deglycase)
[Prkaa1] 5'-AMP-activated protein kinase catalytic subunit alpha-1 (AMPK subunit alpha-1) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31) (Tau-protein kinase PRKAA1) (EC 2.7.11.26)
[PIK3CA] Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform (PI3-kinase subunit alpha) (PI3K-alpha) (PI3Kalpha) (PtdIns-3-kinase subunit alpha) (EC 2.7.1.153) (Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit alpha) (PtdIns-3-kinase subunit p110-alpha) (p110alpha) (Phosphoinositide-3-kinase catalytic alpha polypeptide) (Serine/threonine protein kinase PIK3CA) (EC 2.7.11.1)
[pyrG A6592_02570 A6V01_01290 A9P13_05400 A9R57_06965 A9X72_05250 AC067_22330 AC789_1c31020 ACN002_2797 ACN68_00955 ACN81_20385 ACU57_24415 ACU90_23015 AJ318_22735 AM270_00945 AM446_06950 AM464_05605 AM465_10605 AML07_12460 AML35_05300 APT94_17890 APU18_18535 APZ14_09290 ARC77_10140 AU473_08010 AUQ13_17535 AUS26_15660 AW059_10675 AW106_00665 AWB10_05845 AWE53_025360 AWF59_014510 AWG78_018325 AWG90_017920 AWP75_20610 AZZ83_003241 B6V57_15035 B7C53_10055 B9M99_21725 B9N33_09475 B9T59_19685 BANRA_01301 BANRA_03509 BANRA_03630 BANRA_04324 BB545_13920 BE963_03670 BEN53_16995 BFD68_17190 BHF03_06455 BHF46_05050 BHJ80_19590 BHS81_16640 BHS87_15735 BIQ87_15835 BIU72_09520 BIZ41_16885 BJJ90_05265 BK248_12970 BK292_23205 BK296_17745 BK334_11935 BK373_15870 BK375_10085 BK383_11680 BMA87_05450 BMT49_17330 BMT91_11105 BN17_26661 BOH76_24715 BON63_19880 BON65_10470 BON66_19055 BON69_14990 BON71_18475 BON75_14060 BON76_10430 BON83_26590 BON86_03420 BON87_20865 BON91_20235 BON92_09140 BON96_25385 BTQ04_11510 BTQ06_23845 BUE81_06975 BvCms12BK_05148 BvCms2454_02052 BvCms35BK_01272 BvCmsC61A_01055 BvCmsHHP001_01156 BvCmsHHP019_01127 BvCmsHHP056_01979 BvCmsKKP036_03980 BvCmsKKP061_04391 BvCmsKSNP073_04203 BvCmsKSNP081_03790 BvCmsKSNP120_03969 BvCmsKSP011_02434 BvCmsKSP024_03358 BvCmsKSP026_00102 BvCmsKSP045_02208 BvCmsKSP058_00862 BvCmsKSP067_03640 BvCmsKSP076_05173 BvCmsNSNP036_03047 BvCmsNSP007_01096 BvCmsNSP047_01557 BvCmsNSP072_00181 BvCmsOUP014_01917 BvCmsSINP011_00512 BvCmsSINP022_00781 BvCmsSIP019_01766 BvCmsSIP044_01614 BVL39_12970 BW690_04975 BWI89_25410 BWP17_05185 BXT93_24405 BZL31_00820 BZL69_02125 C2M16_17770 C2U48_20025 C4K41_05275 C4M78_00835 C5715_23540 C5N07_06155 C5P01_05005 C5P44_09340 C6669_14670 C6B13_03370 C7235_05745 C7B02_19400 C7B06_11630 C7B07_14530 C7B08_01430 C7B18_14945 C9098_13720 C9114_10610 C9141_08815 C9160_11785 C9162_15350 C9201_02025 C9306_10515 C9E25_03325 C9E67_05815 C9Z03_03520 C9Z23_09225 C9Z37_12455 C9Z39_03205 C9Z43_07790 C9Z69_03200 C9Z70_05405 C9Z78_15545 C9Z89_02595 CA593_12975 CCZ14_04445 CCZ17_10850 CDC27_14650 CDL37_13440 CF006_02945 CG692_07005 CI641_006865 CI693_01450 CI694_13655 CIG45_04935 CJU63_16170 CJU64_16425 CMR93_10525 CO706_11780 COD30_01795 COD46_07095 CQP61_06810 CR538_05495 CR539_18815 CRE06_03485 CRJUMX01_160005 CRM83_26360 CRT43_16405 CRX46_18850 CSB64_15850 CT146_00680 CUB99_19065 CV83915_03339 CVH05_06295 CWM24_00790 CWS33_03125 D0X26_06660 D2184_01135 D2185_02785 D2188_08435 D3821_11140 D3M98_14175 D3O91_13425 D3P01_10795 D3P02_18650 D3Y67_06430 D4011_20680 D4023_03535 D4074_08165 D4636_12345 D4638_15660 D4660_07760 D4718_06700 D4L91_10970 D4M06_10805 D4U49_02065 D4U85_13910 D4V08_11640 D5H35_06960 D5I97_07085 D6004_06600 D6C36_08560 D6D43_15090 D6T60_21710 D6W00_05605 D6X63_06250 D6X76_00665 D7K33_11370 D7K63_03745 D7K66_09735 D7W70_08720 D7Y10_03025 D7Z75_00480 D8Y65_06395 D9610_06925 D9C99_02870 D9D20_04450 D9D33_19300 D9D43_17525 D9D44_11660 D9D94_19995 D9E13_19660 D9E19_06295 D9E35_20180 D9E73_07150 D9F17_11720 D9F32_18535 D9F87_14880 D9G11_05335 D9G29_07695 D9G42_05640 D9G48_11875 D9G69_15675 D9G95_24305 D9H36_19535 D9H53_12755 D9H68_17340 D9H70_12195 D9H94_16855 D9I18_10690 D9I20_00375 D9I87_07250 D9I88_14405 D9I97_09750 D9J03_22055 D9J11_17735 D9J44_16360 D9J46_14445 D9J52_13520 D9J58_10595 D9J60_10045 D9J63_04880 D9J78_14800 D9K02_13530 D9K48_23835 D9K54_13555 D9L89_10810 D9L99_02095 D9S45_05925 D9X77_06065 D9X97_06540 D9Z28_07585 DAH18_08260 DAH26_03580 DAH30_04675 DAH32_02015 DAH34_11000 DAH37_01335 DAH43_05325 DB359_08835 DBQ99_06250 DD762_13665 DEN89_06185 DEN97_03935 DEO04_02940 DEO19_03715 DIV22_29760 DJ487_00440 DJ492_07250 DJ503_09945 DL251_04515 DL257_11915 DL292_16405 DL326_19010 DL455_11645 DL479_12200 DL530_03985 DL545_05995 DL800_20505 DL979_18970 DLT82_09290 DLU67_11100 DLU82_08170 DLW60_06590 DLW88_08740 DLX38_01400 DLX40_17180 DLY41_21435 DLY44_20595 DM102_10625 DM129_10705 DM155_07315 DM267_14905 DM272_03810 DM280_20210 DM382_13710 DM820_02080 DM962_00445 DM973_18825 DMI04_14240 DMI53_07435 DMO02_14990 DMY83_10765 DMZ50_15435 DN627_17365 DN660_13250 DN700_02075 DN703_12685 DN808_12120 DNB37_12630 DNC98_03960 DND16_10185 DND79_12465 DNI21_05695 DNJ62_04410 DNK12_06795 DNR35_10760 DNR41_08670 DNX19_04715 DNX30_08935 DOE35_02030 DOM23_03020 DOS18_12055 DOT81_13135 DOU81_11955 DOY22_19570 DOY56_02000 DOY61_03145 DOY67_13090 DP258_16075 DP265_17025 DP277_11440 DQE83_04685 DQE91_10495 DQF36_14860 DQF71_04970 DQF72_16505 DQG35_07980 DQO13_13250 DRP48_13490 DRW19_11765 DS143_05250 DS721_02825 DS732_20695 DS966_06010 DT034_02885 DTL43_09355 DTL90_02675 DTM10_03745 DTM45_13530 DTZ20_19385 DU309_08860 DU321_06150 DU333_12515 DVB38_02710 DW236_13020 DWB25_05920 DXT69_20555 DXT71_17355 DXT73_08070 DXX80_007370 E0I42_10500 E0K84_20120 E0L04_10915 E0L12_01040 E2112_20720 E2114_10485 E2115_08690 E2119_13595 E2127_11355 E2128_06395 E2129_11320 E2134_08140 E2135_07675 E2148_10650 E2855_03617 E2863_03463 E4K55_04550 E4K60_10640 E4K61_15140 E5P22_15685 E5P28_02240 E5P37_16160 E5S42_03270 E5S46_13510 E5S47_04995 E5S58_00660 E5S61_16625 EA159_15255 EA167_16290 EA189_08455 EA191_15960 EA198_05390 EA200_09530 EA203_16215 EA213_04170 EA214_11185 EA218_13120 EA223_08230 EA225_01145 EA231_20080 EA232_13255 EA233_00965 EA242_06320 EA245_06985 EA250_17410 EA410_00760 EA429_04715 EA434_00760 EA435_11325 EA834_09100 EAI42_07155 EAI46_14335 EAI52_12500 EAM59_05115 EAN70_01890 EB476_14050 EB509_19080 EB510_16355 EB515_03490 EBA46_07975 EBA84_02290 EBJ06_02570 EBM08_02305 EC1094V2_904 EC3234A_48c00890 EC3426_03921 EC382_15705 EC95NR1_02021 ECONIH1_15890 ECs3640 ECTO124_01152 ECTO6_01068 ED225_00710 ED307_10820 ED600_14885 ED607_09825 ED611_00710 ED648_01520 ED903_09700 ED944_03505 EEA45_12675 EEP23_14050 EF082_18470 EF173_03685 EG075_13145 EG599_01830 EG808_06220 EGC26_11055 EGT48_09620 EGU87_12650 EH186_13570 EH412_03190 EHD45_02185 EHD63_08185 EHD79_13870 EHH55_20810 EHJ36_03270 EHJ66_02550 EHV81_04065 EHV90_01500 EHW09_03455 EHX09_18045 EI021_14555 EI028_04155 EI032_03990 EI041_16020 EIA08_07275 EIA21_04795 EIZ86_12185 EIZ93_11190 EJ366_03305 EJC75_12775 EKI52_20580 EL75_0914 EL79_0915 EL80_0918 ELT20_14390 ELT23_08310 ELT33_11340 ELT34_08915 ELT48_15890 ELT49_03005 ELT58_07520 ELU82_04890 ELU85_05750 ELU96_10810 ELV08_21905 ELV13_07545 ELV15_07575 ELV24_11300 ELV28_16420 ELX79_10280 ELX83_17325 ELY05_07495 ELY23_11490 ELY24_07925 ELY50_05380 EO241_20205 EPS91_16285 EPS94_11415 EPT01_17055 EPU41_15765 EQ820_17285 EQ823_14605 EQ825_07980 EQ830_01100 ERL57_14345 ERS085365_02427 ERS085366_03042 ERS085374_03279 ERS085386_03410 ERS085416_02898 ERS139211_02072 ERS150873_02003 ERS150876_01467 EST51_05505 EVY14_17325 EWK56_05345 ExPECSC019_02242 ExPECSC038_01963 ExPECSC065_01289 EXX06_06960 EXX13_05855 EXX23_03700 EXX24_19085 EXX53_03685 EXX55_06445 EXX71_16235 EXX78_11575 EXX87_15385 EYD11_05205 EYX82_06265 EYX99_17285 EYY27_21685 EYY34_09650 EYY78_11015 F1E13_12850 F1E19_13585 F7F00_02940 F7F11_01115 F7F23_00665 F7F26_03065 F7G01_03890 F7G03_02700 F9059_06090 F9Z74_18200 FAF34_010195 FE846_02780 FKO60_03565 FNJ67_06370 FNJ69_12285 FNJ83_17875 FORC82_1067 FQ022_17605 FQR64_05280 FQU83_07080 FQZ46_00480 FRV13_23300 FTV93_23860 FV293_15850 FV295_08510 FV438_15285 FY127_14515 FZ043_19260 GFU40_06320 GFU47_11920 GHR40_09615 GII67_05930 GII91_14310 GIY13_16875 GJ11_18025 GJ638_02750 GJD97_05060 GKE15_03135 GKE22_09005 GKE24_03125 GKE26_03130 GKE29_04180 GKE31_03095 GKE39_03150 GKE46_11750 GKE58_03040 GKE60_03095 GKE64_07540 GKE77_03100 GKE87_04995 GKE92_01660 GKE93_03620 GKF03_04460 GKF28_13940 GKF34_13235 GKF47_13220 GKF74_07795 GKF86_09815 GKF89_09790 GKG08_07710 GKG09_07960 GKG11_08165 GKG12_00975 GKG22_07970 GKG29_08010 GN312_04475 GNZ00_00805 GNZ02_06270 GNZ03_13180 GP654_05220 GP661_15475 GP664_04220 GP666_07425 GP689_01920 GP700_13945 GP712_05420 GP720_12915 GP727_17550 GP912_17995 GP935_06995 GP946_10500 GP950_03155 GQE22_17855 GQE30_14975 GQE34_06655 GQE42_09295 GQE47_08060 GQE51_07155 GQE58_08185 GQE64_12560 GQE68_19320 GQE88_19580 GQE93_00635 GQL64_00935 GQM06_06780 GQM09_04835 GQM13_07125 GQM17_05020 GQN16_02715 GQN33_06080 GQS26_09385 GRW42_02075 GRW80_15480 HmCms169_01730 HmCms184_04776 HmCmsJML074_04422 HmCmsJML079_03779 HmCmsJML146_01816 HmCmsJML204_00525 HMPREF3040_01161 HW43_18180 MJ49_17095 MS6198_30910 MS8345_02965 NCTC10082_03473 NCTC10090_04050 NCTC10418_01701 NCTC10764_00296 NCTC10766_00690 NCTC10767_02309 NCTC10963_01055 NCTC10974_01288 NCTC11022_02860 NCTC11112_00121 NCTC11181_03277 NCTC12650_01316 NCTC12950_01251 NCTC13127_01436 NCTC13216_00824 NCTC13846_01212 NCTC7927_01209 NCTC8500_01090 NCTC8960_03783 NCTC9007_03892 NCTC9036_01135 NCTC9044_00576 NCTC9045_01221 NCTC9050_04166 NCTC9058_00847 NCTC9062_02131 NCTC9075_01630 NCTC9077_01409 NCTC9081_05851 NCTC9117_01609 NCTC9119_01271 NCTC9434_01004 NCTC9702_01298 NCTC9706_03296 NCTC9777_02704 NCTC9969_01292 PGD_04325 PU06_02080 RG28_07675 RK56_023165 SAMEA3472043_01265 SAMEA3472044_02272 SAMEA3472047_00339 SAMEA3472056_05455 SAMEA3472070_01673 SAMEA3472080_03155 SAMEA3472090_00131 SAMEA3472108_00527 SAMEA3472110_03462 SAMEA3472112_03722 SAMEA3472114_02432 SAMEA3472147_03296 SAMEA3484427_03298 SAMEA3484429_03415 SAMEA3484434_01581 SAMEA3485101_02257 SAMEA3485113_02257 SAMEA3752372_03639 SAMEA3752553_01510 SAMEA3752557_03040 SAMEA3752559_02995 SAMEA3752620_01282 SAMEA3753064_02287 SAMEA3753097_02219 SAMEA3753164_01192 SAMEA3753290_02847 SAMEA3753300_01107 SK85_03024 SY51_15605 U12A_02895 U14A_02898 UC41_20365 UN91_03645 WQ89_10170 WR15_06090 YDC107_1339] CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase)
[PRKAA2 AMPK AMPK2] 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)
[Prkaa2 Ampk Ampk2] 5'-AMP-activated protein kinase catalytic subunit alpha-2 (AMPK subunit alpha-2) (EC 2.7.11.1) (Acetyl-CoA carboxylase kinase) (ACACA kinase) (EC 2.7.11.27) (Hydroxymethylglutaryl-CoA reductase kinase) (HMGCR kinase) (EC 2.7.11.31)

Bibliography :
[32254052] Crystal structure of Arabidopsis thaliana casein kinase 2 α1.
[32103024] Structure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1.
[31779225] Protein Kinase CK2 Subunits Differentially Perturb the Adhesion and Migration of GN11 Cells: A Model of Immature Migrating Neurons.
[31583500] Protein kinase CK2 is involved in zinc homeostasis in breast and prostate cancer cells.
[31268746] Protein kinase CK2 subunits exert specific and coordinated functions in skeletal muscle differentiation and fusogenic activity.
[31091289] Activity of CK2α protein kinase is required for efficient replication of some HPV types.
[30883733] TET1 reprograms the epithelial ovarian cancer epigenome and reveals casein kinase 2α as a therapeutic target.
[30834696] A proteomics analysis of CK2β C2C12 cells provides novel insights into the biological functions of the non-catalytic β subunit.
[30689946] 2-Aminothiazole Derivatives as Selective Allosteric Modulators of the Protein Kinase CK2. 2. Structure-Based Optimization and Investigation of Effects Specific to the Allosteric Mode of Action.
[30607803] Up-Regulation of the Alpha Prime Subunit of Protein Kinase CK2 as a Marker of Fast Proliferation in GL261 Cultured Cells.