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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.
22-NOV-2017, entry version 159.
RecName: Full=Casein kinase II subunit alpha;
Short=CK II alpha;
EC=2.7.11.1;
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, 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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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. Regulates numerous
cellular processes, such as cell cycle progression, apoptosis and
transcription, as well as viral infection. May act as a regulatory
node which integrates and coordinates numerous signals leading to
an appropriate cellular response. During mitosis, functions as a
component of the p53/TP53-dependent spindle assembly checkpoint
(SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in
response to spindle damage. Also required for p53/TP53-mediated
apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV
irradiation. Can also negatively regulate apoptosis.
Phosphorylates the caspases CASP9 and CASP2 and the apoptotic
regulator NOL3. Phosphorylation protects CASP9 from cleavage and
activation by CASP8, and inhibits the dimerization of CASP2 and
activation of CASP8. Regulates transcription by direct
phosphorylation of RNA polymerases I, II, III and IV. Also
phosphorylates and regulates numerous transcription factors
including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX,
JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones
FKBP4 and CDC37, which is essential for chaperone function.
Regulates Wnt signaling by phosphorylating CTNNB1 and the
transcription factor LEF1. Acts as an ectokinase that
phosphorylates several extracellular proteins. During viral
infection, phosphorylates various proteins involved in the viral
life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.
Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-
mediated degradation. 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 (PubMed:11239457, PubMed:11704824, PubMed:16193064,
PubMed:19188443, PubMed:20625391, PubMed:22406621). Phosphorylates
CCAR2 at 'Thr-454' in gastric carcinoma tissue (PubMed:24962073).
{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:24962073}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:20625391}.
-!- ENZYME 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:
Self; NbExp=3; IntAct=EBI-347804, EBI-347804;
O00257-3:CBX4; NbExp=2; IntAct=EBI-347804, EBI-4392727;
P19784:CSNK2A2; NbExp=7; IntAct=EBI-347804, EBI-347451;
P67870:CSNK2B; NbExp=20; IntAct=EBI-347804, EBI-348169;
O75822:EIF3J; NbExp=2; IntAct=EBI-347804, EBI-366647;
Q13547:HDAC1; NbExp=2; IntAct=EBI-347804, EBI-301834;
A0A0C4DFT8:JADE2; NbExp=4; IntAct=EBI-347804, EBI-12094820;
Q5T7B8-2:KIF24; NbExp=4; IntAct=EBI-347804, EBI-10213781;
O60282:KIF5C; NbExp=4; IntAct=EBI-347804, EBI-717170;
P43364-2:MAGEA11; NbExp=3; IntAct=EBI-347804, EBI-10178634;
P50222:MEOX2; NbExp=4; IntAct=EBI-347804, EBI-748397;
P23511:NFYA; NbExp=3; IntAct=EBI-347804, EBI-389739;
P29590:PML; NbExp=2; IntAct=EBI-347804, EBI-295890;
Q6ZNA4:RNF111; NbExp=4; IntAct=EBI-347804, EBI-2129175;
Q99496:RNF2; NbExp=3; IntAct=EBI-347804, EBI-722416;
Q96EB6:SIRT1; NbExp=5; IntAct=EBI-347804, EBI-1802965;
Q92504:SLC39A7; NbExp=4; IntAct=EBI-347804, EBI-1051105;
Q08945:SSRP1; NbExp=2; IntAct=EBI-347804, EBI-353771;
Q96MF2:STAC3; NbExp=5; IntAct=EBI-347804, EBI-745680;
O75683:SURF6; NbExp=2; IntAct=EBI-347804, EBI-2691252;
Q9NVV9:THAP1; NbExp=5; IntAct=EBI-347804, EBI-741515;
P04637:TP53; NbExp=2; IntAct=EBI-347804, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus {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]
UniGene; Hs.644056; -.
UniGene; Hs.654675; -.
UniGene; Hs.741126; -.
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; 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; 5NQC; X-ray; 2.00 A; A=2-335.
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; 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; 5NQC; -.
ProteinModelPortal; P68400; -.
SMR; P68400; -.
BioGrid; 107841; 461.
CORUM; P68400; -.
DIP; DIP-32682N; -.
IntAct; P68400; 285.
MINT; MINT-142347; -.
STRING; 9606.ENSP00000217244; -.
BindingDB; P68400; -.
ChEMBL; CHEMBL3629; -.
DrugBank; DB03127; Benzamidine.
DrugBank; DB08846; Ellagic Acid.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB02709; Resveratrol.
DrugBank; DB04462; Tetrabromo-2-Benzotriazole.
GuidetoPHARMACOLOGY; 1549; -.
iPTMnet; P68400; -.
PhosphoSitePlus; P68400; -.
SwissPalm; P68400; -.
BioMuta; CSNK2A1; -.
DMDM; 55977123; -.
EPD; P68400; -.
MaxQB; P68400; -.
PaxDb; P68400; -.
PeptideAtlas; P68400; -.
PRIDE; P68400; -.
DNASU; 1457; -.
Ensembl; ENST00000217244; ENSP00000217244; ENSG00000101266. [P68400-1]
Ensembl; ENST00000349736; ENSP00000339247; ENSG00000101266. [P68400-1]
Ensembl; ENST00000400217; ENSP00000383076; ENSG00000101266. [P68400-2]
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; CAB020680; -.
HPA; CAB069395; -.
HPA; HPA059206; -.
MalaCards; CSNK2A1; -.
MIM; 115440; gene.
MIM; 617062; phenotype.
neXtProt; NX_P68400; -.
OpenTargets; ENSG00000101266; -.
PharmGKB; PA26957; -.
eggNOG; KOG0668; Eukaryota.
eggNOG; ENOG410XNPP; LUCA.
GeneTree; ENSGT00390000004215; -.
HOGENOM; HOG000233021; -.
HOVERGEN; HBG107282; -.
InParanoid; P68400; -.
KO; K03097; -.
OMA; NNTDFRS; -.
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; -.
ChiTaRS; CSNK2A1; human.
EvolutionaryTrace; P68400; -.
GeneWiki; Casein_kinase_2,_alpha_1; -.
GenomeRNAi; 1457; -.
PMAP-CutDB; B4DYS6; -.
PRO; PR:P68400; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101266; -.
CleanEx; HS_CSNK2A1; -.
ExpressionAtlas; P68400; baseline and differential.
Genevisible; P68400; HS.
GO; GO:0000785; C:chromatin; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
GO; GO:0005956; C:protein kinase CK2 complex; IDA:CAFA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
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:0019888; F:protein phosphatase regulator activity; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0061077; P:chaperone-mediated protein folding; TAS:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP: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 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:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0006457; P:protein folding; TAS:Reactome.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:1905818; P:regulation of chromosome separation; IMP:UniProtKB.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; Complete proteome; 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 Casein kinase II subunit alpha.
/FTId=PRO_0000085883.
DOMAIN 39 324 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 45 53 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 36 41 Interaction with beta subunit.
{ECO:0000250}.
ACT_SITE 156 156 Proton acceptor.
BINDING 68 68 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 344 344 Phosphothreonine; by CDK1.
{ECO:0000269|PubMed:7592773}.
MOD_RES 360 360 Phosphothreonine; by CDK1.
{ECO:0000269|PubMed:7592773}.
MOD_RES 362 362 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:7592773}.
MOD_RES 370 370 Phosphoserine; by CDK1.
{ECO:0000244|PubMed:18691976,
ECO:0000269|PubMed:7592773}.
VAR_SEQ 1 136 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041925.
VARIANT 47 47 R -> Q (in OCNDS; dbSNP:rs869312845).
{ECO:0000269|PubMed:27048600}.
/FTId=VAR_077045.
VARIANT 50 50 Y -> S (in OCNDS; dbSNP:rs869312849).
{ECO:0000269|PubMed:27048600}.
/FTId=VAR_077046.
VARIANT 175 175 D -> G (in OCNDS; dbSNP:rs869312848).
{ECO:0000269|PubMed:27048600}.
/FTId=VAR_077047.
VARIANT 198 198 K -> R (in OCNDS; dbSNP:rs869312840).
{ECO:0000269|PubMed:27048600}.
/FTId=VAR_077048.
CONFLICT 128 128 L -> F (in Ref. 3; CAA49758).
{ECO:0000305}.
CONFLICT 256 256 D -> G (in Ref. 3; CAA49758).
{ECO:0000305}.
CONFLICT 287 287 S -> R (in Ref. 3; CAA49758).
{ECO:0000305}.
CONFLICT 351 351 M -> V (in Ref. 3; CAA49758).
{ECO:0000305}.
STRAND 10 12 {ECO:0000244|PDB:3WAR}.
TURN 13 18 {ECO:0000244|PDB:3WAR}.
HELIX 21 24 {ECO:0000244|PDB:3WAR}.
HELIX 26 28 {ECO:0000244|PDB:3WAR}.
HELIX 36 38 {ECO:0000244|PDB:3WAR}.
STRAND 39 47 {ECO:0000244|PDB:3WAR}.
STRAND 49 58 {ECO:0000244|PDB:3WAR}.
TURN 59 61 {ECO:0000244|PDB:3WAR}.
STRAND 64 70 {ECO:0000244|PDB:3WAR}.
TURN 72 74 {ECO:0000244|PDB:5CU6}.
HELIX 75 88 {ECO:0000244|PDB:3WAR}.
STRAND 97 102 {ECO:0000244|PDB:3WAR}.
TURN 104 106 {ECO:0000244|PDB:3WAR}.
STRAND 107 114 {ECO:0000244|PDB:3WAR}.
TURN 118 120 {ECO:0000244|PDB:5CVG}.
HELIX 121 124 {ECO:0000244|PDB:3WAR}.
HELIX 125 127 {ECO:0000244|PDB:3WAR}.
HELIX 130 149 {ECO:0000244|PDB:3WAR}.
HELIX 159 161 {ECO:0000244|PDB:3WAR}.
STRAND 162 165 {ECO:0000244|PDB:3WAR}.
HELIX 166 168 {ECO:0000244|PDB:3WAR}.
STRAND 170 173 {ECO:0000244|PDB:3WAR}.
HELIX 176 178 {ECO:0000244|PDB:5CVG}.
HELIX 195 197 {ECO:0000244|PDB:3WAR}.
HELIX 200 203 {ECO:0000244|PDB:3WAR}.
HELIX 212 227 {ECO:0000244|PDB:3WAR}.
STRAND 230 233 {ECO:0000244|PDB:3WAR}.
HELIX 238 249 {ECO:0000244|PDB:3WAR}.
HELIX 251 261 {ECO:0000244|PDB:3WAR}.
HELIX 267 269 {ECO:0000244|PDB:3WAR}.
TURN 270 272 {ECO:0000244|PDB:3WAR}.
HELIX 281 284 {ECO:0000244|PDB:3WAR}.
TURN 287 289 {ECO:0000244|PDB:3WAR}.
HELIX 290 292 {ECO:0000244|PDB:3WAR}.
HELIX 295 304 {ECO:0000244|PDB:3WAR}.
HELIX 309 311 {ECO:0000244|PDB:3WAR}.
HELIX 315 318 {ECO:0000244|PDB:3WAR}.
HELIX 322 324 {ECO:0000244|PDB:3WAR}.
HELIX 325 331 {ECO:0000244|PDB:3WAR}.
STRAND 333 335 {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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