Full text data of CSNK2A1
CSNK2A1
(CK2A1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Casein kinase II subunit alpha; CK II alpha; 2.7.11.1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Casein kinase II subunit alpha; CK II alpha; 2.7.11.1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P68400
ID CSK21_HUMAN Reviewed; 391 AA.
AC P68400; B4DYS6; D3DVV8; P19138; P20426; Q14013; Q5U065;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-NOV-2004, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Casein kinase II subunit alpha;
DE Short=CK II alpha;
DE EC=2.7.11.1;
GN Name=CSNK2A1; Synonyms=CK2A1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2752008; DOI=10.1021/bi00435a066;
RA Meisner H., Heller-Harrison R., Buxton J., Czech M.P.;
RT "Molecular cloning of the human casein kinase II alpha subunit.";
RL Biochemistry 28:4072-4076(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2174700; DOI=10.1021/bi00488a034;
RA Lozeman F.J., Litchfield D.W., Piening C., Takio K., Walsh K.A.,
RA Krebs E.G.;
RT "Isolation and characterization of human cDNA clones encoding the
RT alpha and the alpha' subunits of casein kinase II.";
RL Biochemistry 29:8436-8447(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=8420794; DOI=10.1016/0014-5793(93)81197-8;
RA Devilat I., Carvallo P.;
RT "Structure and sequence of an intronless gene for human casein kinase
RT II-alpha subunit.";
RL FEBS Lett. 316:114-118(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Muscle, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PHOSPHORYLATION AT THR-344; THR-360; SER-362 AND SER-370.
RX PubMed=7592773; DOI=10.1074/jbc.270.43.25872;
RA Bosc D.G., Slominski E., Sichler C., Litchfield D.W.;
RT "Phosphorylation of casein kinase II by p34cdc2. Identification of
RT phosphorylation sites using phosphorylation site mutants in vitro.";
RL J. Biol. Chem. 270:25872-25878(1995).
RN [11]
RP FUNCTION, AND INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=11239457; DOI=10.1016/S1097-2765(01)00176-9;
RA Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H.,
RA Goodman R., Lozano G., Zhao Y., Lu H.;
RT "A DNA damage-induced p53 serine 392 kinase complex contains CK2,
RT hSpt16, and SSRP1.";
RL Mol. Cell 7:283-292(2001).
RN [12]
RP FUNCTION IN CELL CYCLE.
RX PubMed=11704824; DOI=10.1038/sj.onc.1204894;
RA Sayed M., Pelech S., Wong C., Marotta A., Salh B.;
RT "Protein kinase CK2 is involved in G2 arrest and apoptosis following
RT spindle damage in epithelial cells.";
RL Oncogene 20:6994-7005(2001).
RN [13]
RP INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=12393879; DOI=10.1074/jbc.M209820200;
RA Keller D.M., Lu H.;
RT "p53 serine 392 phosphorylation increases after UV through induction
RT of the assembly of the CK2.hSPT16.SSRP1 complex.";
RL J. Biol. Chem. 277:50206-50213(2002).
RN [14]
RP FUNCTION IN APOPTOSIS.
RX PubMed=16193064; DOI=10.1038/sj.emboj.7600827;
RA Shin S., Lee Y., Kim W., Ko H., Choi H., Kim K.;
RT "Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by
RT processing procaspase-8.";
RL EMBO J. 24:3532-3542(2005).
RN [15]
RP INTERACTION WITH RNPS1.
RX PubMed=15684395; DOI=10.1128/MCB.25.4.1446-1457.2005;
RA Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A.,
RA Suzuki H., Endo H., Kidd V.J., Mayeda A.;
RT "Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2
RT phosphorylation.";
RL Mol. Cell. Biol. 25:1446-1457(2005).
RN [16]
RP FUNCTION IN CELL CYCLE.
RX PubMed=19188443; DOI=10.1128/MCB.01563-08;
RA St-Denis N.A., Derksen D.R., Litchfield D.W.;
RT "Evidence for regulation of mitotic progression through temporal
RT phosphorylation and dephosphorylation of CK2alpha.";
RL Mol. Cell. Biol. 29:2068-2081(2009).
RN [17]
RP REVIEW ON FUNCTION.
RX PubMed=12631575; DOI=10.1096/fj.02-0473rev;
RA Meggio F., Pinna L.A.;
RT "One-thousand-and-one substrates of protein kinase CK2?";
RL FASEB J. 17:349-368(2003).
RN [18]
RP REVIEW ON STRUCTURE.
RX PubMed=19387553; DOI=10.1007/s00018-009-9149-8;
RA Niefind K., Raaf J., Issinger O.G.;
RT "Protein kinase CK2 in health and disease: Protein kinase CK2: from
RT structures to insights.";
RL Cell. Mol. Life Sci. 66:1800-1816(2009).
RN [19]
RP REVIEW ON FUNCTION.
RX PubMed=19387552; DOI=10.1007/s00018-009-9150-2;
RA St-Denis N.A., Litchfield D.W.;
RT "Protein kinase CK2 in health and disease: From birth to death: the
RT role of protein kinase CK2 in the regulation of cell proliferation and
RT survival.";
RL Cell. Mol. Life Sci. 66:1817-1829(2009).
RN [20]
RP REVIEW ON FUNCTION.
RX PubMed=19387551; DOI=10.1007/s00018-009-9151-1;
RA Filhol O., Cochet C.;
RT "Protein kinase CK2 in health and disease: Cellular functions of
RT protein kinase CK2: a dynamic affair.";
RL Cell. Mol. Life Sci. 66:1830-1839(2009).
RN [21]
RP REVIEW ON FUNCTION IN REGULATION OF HSP90.
RX PubMed=19387550; DOI=10.1007/s00018-009-9152-0;
RA Miyata Y.;
RT "Protein kinase CK2 in health and disease: CK2: the kinase controlling
RT the Hsp90 chaperone machinery.";
RL Cell. Mol. Life Sci. 66:1840-1849(2009).
RN [22]
RP REVIEW ON FUNCTION IN WNT SIGNALING.
RX PubMed=19387549; DOI=10.1007/s00018-009-9153-z;
RA Dominguez I., Sonenshein G.E., Seldin D.C.;
RT "Protein kinase CK2 in health and disease: CK2 and its role in Wnt and
RT NF-kappaB signaling: linking development and cancer.";
RL Cell. Mol. Life Sci. 66:1850-1857(2009).
RN [23]
RP INTERACTION WITH SNAI1.
RX PubMed=19923321; DOI=10.1091/mbc.E09-06-0504;
RA MacPherson M.R., Molina P., Souchelnytskyi S., Wernstedt C.,
RA Martin-Perez J., Portillo F., Cano A.;
RT "Phosphorylation of serine 11 and serine 92 as new positive regulators
RT of human Snail1 function: potential involvement of casein kinase-2 and
RT the cAMP-activated kinase protein kinase A.";
RL Mol. Biol. Cell 21:244-253(2010).
RN [24]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH PML.
RX PubMed=20625391; DOI=10.1371/journal.pone.0011418;
RA Hung M.S., Lin Y.C., Mao J.H., Kim I.J., Xu Z., Yang C.T.,
RA Jablons D.M., You L.;
RT "Functional polymorphism of the CK2alpha intronless gene plays
RT oncogenic roles in lung cancer.";
RL PLoS ONE 5:E11418-E11418(2010).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP FUNCTION, AND INTERACTION WITH PML.
RX PubMed=22406621; DOI=10.1158/0008-5472.CAN-11-3159;
RA Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A.,
RA Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J.,
RA Scaglioni P.P.;
RT "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its
RT oncogenic counterpart PML-RARA.";
RL Cancer Res. 72:2275-2284(2012).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337, AND SUBUNIT.
RX PubMed=11092945; DOI=10.1107/S0907444900013627;
RA Niefind K., Guerra B., Ermakowa I., Issinger O.G.;
RT "Crystallization and preliminary characterization of crystals of human
RT protein kinase CK2.";
RL Acta Crystallogr. D 56:1680-1684(2000).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337 IN COMPLEX WITH CSNK2B,
RP AND SUBUNIT.
RX PubMed=11574463; DOI=10.1093/emboj/20.19.5320;
RA Niefind K., Guerra B., Ermakowa I., Issinger O.G.;
RT "Crystal structure of human protein kinase CK2: insights into basic
RT properties of the CK2 holoenzyme.";
RL EMBO J. 20:5320-5331(2001).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-329.
RX PubMed=14646071; DOI=10.1107/S0907444903018900;
RA Pechkova E., Zanotti G., Nicolini C.;
RT "Three-dimensional atomic structure of a catalytic subunit mutant of
RT human protein kinase CK2.";
RL Acta Crystallogr. D 59:2133-2139(2003).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-335.
RX PubMed=12860116; DOI=10.1016/S0022-2836(03)00638-7;
RA Ermakova I., Boldyreff B., Issinger O.G., Niefind K.;
RT "Crystal structure of a C-terminal deletion mutant of human protein
RT kinase CK2 catalytic subunit.";
RL J. Mol. Biol. 330:925-934(2003).
CC -!- FUNCTION: Catalytic subunit of a constitutively active
CC serine/threonine-protein kinase complex that phosphorylates a
CC large number of substrates containing acidic residues C-terminal
CC to the phosphorylated serine or threonine. Regulates numerous
CC cellular processes, such as cell cycle progression, apoptosis and
CC transcription, as well as viral infection. May act as a regulatory
CC node which integrates and coordinates numerous signals leading to
CC an appropriate cellular response. During mitosis, functions as a
CC component of the p53/TP53-dependent spindle assembly checkpoint
CC (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in
CC response to spindle damage. Also required for p53/TP53-mediated
CC apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV
CC irradiation. Can also negatively regulate apoptosis.
CC Phosphorylates the caspases CASP9 and CASP2 and the apoptotic
CC regulator NOL3. Phosphorylation protects CASP9 from cleavage and
CC activation by CASP8, and inhibits the dimerization of CASP2 and
CC activation of CASP8. Regulates transcription by direct
CC phosphorylation of RNA polymerases I, II, III and IV. Also
CC phosphorylates and regulates numerous transcription factors
CC including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX,
CC JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones
CC FKBP4 and CDC37, which is essential for chaperone function.
CC Regulates Wnt signaling by phosphorylating CTNNB1 and the
CC transcription factor LEF1. Acts as an ectokinase that
CC phosphorylates several extracellular proteins. During viral
CC infection, phosphorylates various proteins involved in the viral
CC life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.
CC Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-
CC mediated degradation.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- ENZYME REGULATION: Constitutively active protein kinase whose
CC activity is not directly affected by phosphorylation. Seems to be
CC regulated by level of expression and localization.
CC -!- SUBUNIT: Heterotetramer composed of two catalytic subunits (alpha
CC chain and/or alpha' chain) and two regulatory subunits (beta
CC chains). The tetramer can exist as a combination of 2 alpha/2
CC beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also
CC part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H,
CC CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation.
CC Interacts with RNPS1. Interacts with SNAI1. Interacts with PML
CC (isoform PML-12).
CC -!- INTERACTION:
CC O00257-3:CBX4; NbExp=2; IntAct=EBI-347804, EBI-4392727;
CC P19784:CSNK2A2; NbExp=3; IntAct=EBI-347804, EBI-347451;
CC P67870:CSNK2B; NbExp=13; IntAct=EBI-347804, EBI-348169;
CC Q13547:HDAC1; NbExp=2; IntAct=EBI-347804, EBI-301834;
CC O60282:KIF5C; NbExp=4; IntAct=EBI-347804, EBI-717170;
CC P29590:PML; NbExp=2; IntAct=EBI-347804, EBI-295890;
CC Q96EB6:SIRT1; NbExp=4; IntAct=EBI-347804, EBI-1802965;
CC Q92504:SLC39A7; NbExp=4; IntAct=EBI-347804, EBI-1051105;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P68400-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P68400-2; Sequence=VSP_041925;
CC -!- PTM: Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by
CC CDK1 in prophase and metaphase and dephosphorylated during
CC anaphase. Phosphorylation does not directly affect casein kinase 2
CC activity, but may contribute to its regulation by forming binding
CC sites for interacting proteins and/or targeting it to different
CC compartments.
CC -!- MISCELLANEOUS: Can use both ATP and GTP as phosphoryl donors.
CC Phosphorylation by casein kinase 2 has been estimated to represent
CC up to one quarter of the eukaryotic phosphoproteome. Casein kinase
CC 2 has been found to be increased at protein level and up-regulated
CC at the level of enzyme activity in the majority of cancers.
CC However, elevated levels of casein kinase 2 are present in certain
CC normal organs such as brain and testes.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC protein kinase family. CK2 subfamily.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
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DR EMBL; J02853; AAA56821.1; -; mRNA.
DR EMBL; M55265; AAA35503.1; -; mRNA.
DR EMBL; S53149; ABB72474.1; -; mRNA.
DR EMBL; X70251; CAA49758.1; -; Genomic_DNA.
DR EMBL; AK302583; BAG63838.1; -; mRNA.
DR EMBL; BT019792; AAV38595.1; -; mRNA.
DR EMBL; AB451279; BAG70093.1; -; mRNA.
DR EMBL; AL049761; CAB65624.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10665.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10666.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10667.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10668.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10669.1; -; Genomic_DNA.
DR EMBL; BC011668; AAH11668.1; -; mRNA.
DR EMBL; BC053532; AAH53532.1; -; mRNA.
DR EMBL; BC071167; AAH71167.1; -; mRNA.
DR PIR; A30319; A30319.
DR RefSeq; NP_001886.1; NM_001895.3.
DR RefSeq; NP_808227.1; NM_177559.2.
DR RefSeq; NP_808228.1; NM_177560.2.
DR UniGene; Hs.644056; -.
DR UniGene; Hs.654675; -.
DR UniGene; Hs.741126; -.
DR PDB; 1JWH; X-ray; 3.10 A; A/B=1-337.
DR PDB; 1NA7; X-ray; 2.40 A; A=1-329.
DR PDB; 1PJK; X-ray; 2.50 A; A=2-335.
DR PDB; 2PVR; X-ray; 1.60 A; A=2-335.
DR PDB; 2ZJW; X-ray; 2.40 A; A=1-335.
DR PDB; 3AMY; X-ray; 2.30 A; A=1-335.
DR PDB; 3AT2; X-ray; 1.60 A; A=1-335.
DR PDB; 3AT3; X-ray; 2.60 A; A=1-335.
DR PDB; 3AT4; X-ray; 2.20 A; A=1-335.
DR PDB; 3AXW; X-ray; 2.50 A; A=1-335.
DR PDB; 3BQC; X-ray; 1.50 A; A=1-335.
DR PDB; 3C13; X-ray; 1.95 A; A=1-335.
DR PDB; 3FWQ; X-ray; 2.30 A; A/B=1-335.
DR PDB; 3H30; X-ray; 1.56 A; A/B=1-334.
DR PDB; 3JUH; X-ray; 1.66 A; A/B=1-335.
DR PDB; 3MB6; X-ray; 1.75 A; A=1-331.
DR PDB; 3MB7; X-ray; 1.65 A; A=1-331.
DR PDB; 3NGA; X-ray; 2.71 A; A/B=1-333.
DR PDB; 3NSZ; X-ray; 1.30 A; A=2-331.
DR PDB; 3OWJ; X-ray; 1.85 A; A=1-331.
DR PDB; 3OWK; X-ray; 1.80 A; A=1-331.
DR PDB; 3OWL; X-ray; 2.10 A; A=1-331.
DR PDB; 3PE1; X-ray; 1.60 A; A=1-337.
DR PDB; 3PE2; X-ray; 1.90 A; A=1-337.
DR PDB; 3PE4; X-ray; 1.95 A; B/D=340-352.
DR PDB; 3Q04; X-ray; 1.80 A; A=3-330.
DR PDB; 3Q9W; X-ray; 1.70 A; A=1-336.
DR PDB; 3Q9X; X-ray; 2.20 A; A/B=1-336.
DR PDB; 3Q9Y; X-ray; 1.80 A; A=1-336.
DR PDB; 3Q9Z; X-ray; 2.20 A; A/B=1-336.
DR PDB; 3QA0; X-ray; 2.50 A; A/B=1-336.
DR PDB; 3R0T; X-ray; 1.75 A; A=1-337.
DR PDB; 3RPS; X-ray; 2.30 A; A/B=1-335.
DR PDB; 3TAX; X-ray; 1.88 A; B/D=340-352.
DR PDB; 3U4U; X-ray; 2.20 A; A=1-333.
DR PDB; 3U87; X-ray; 2.90 A; A/B=1-329.
DR PDB; 3U9C; X-ray; 3.20 A; A/B=1-335.
DR PDB; 3W8L; X-ray; 2.40 A; A/B=1-335.
DR PDB; 3WAR; X-ray; 1.04 A; A=1-335.
DR PDB; 4DGL; X-ray; 3.00 A; C/D=1-335.
DR PDB; 4FBX; X-ray; 2.33 A; A=1-335.
DR PDB; 4GRB; X-ray; 2.15 A; A=1-333.
DR PDB; 4GUB; X-ray; 2.20 A; A=1-333.
DR PDB; 4GYW; X-ray; 1.70 A; B/D=340-352.
DR PDB; 4GYY; X-ray; 1.85 A; B/D=340-352.
DR PDB; 4GZ3; X-ray; 1.90 A; B/D=340-352.
DR PDB; 4IB5; X-ray; 2.20 A; A/B/C=1-335.
DR PDB; 4MD7; X-ray; 3.10 A; E/F/G/H=1-391.
DR PDB; 4MD8; X-ray; 3.30 A; E/F/G/H=1-391.
DR PDB; 4MD9; X-ray; 3.50 A; E/F/G/H/K/L/M/P=1-336.
DR PDBsum; 1JWH; -.
DR PDBsum; 1NA7; -.
DR PDBsum; 1PJK; -.
DR PDBsum; 2PVR; -.
DR PDBsum; 2ZJW; -.
DR PDBsum; 3AMY; -.
DR PDBsum; 3AT2; -.
DR PDBsum; 3AT3; -.
DR PDBsum; 3AT4; -.
DR PDBsum; 3AXW; -.
DR PDBsum; 3BQC; -.
DR PDBsum; 3C13; -.
DR PDBsum; 3FWQ; -.
DR PDBsum; 3H30; -.
DR PDBsum; 3JUH; -.
DR PDBsum; 3MB6; -.
DR PDBsum; 3MB7; -.
DR PDBsum; 3NGA; -.
DR PDBsum; 3NSZ; -.
DR PDBsum; 3OWJ; -.
DR PDBsum; 3OWK; -.
DR PDBsum; 3OWL; -.
DR PDBsum; 3PE1; -.
DR PDBsum; 3PE2; -.
DR PDBsum; 3PE4; -.
DR PDBsum; 3Q04; -.
DR PDBsum; 3Q9W; -.
DR PDBsum; 3Q9X; -.
DR PDBsum; 3Q9Y; -.
DR PDBsum; 3Q9Z; -.
DR PDBsum; 3QA0; -.
DR PDBsum; 3R0T; -.
DR PDBsum; 3RPS; -.
DR PDBsum; 3TAX; -.
DR PDBsum; 3U4U; -.
DR PDBsum; 3U87; -.
DR PDBsum; 3U9C; -.
DR PDBsum; 3W8L; -.
DR PDBsum; 3WAR; -.
DR PDBsum; 4DGL; -.
DR PDBsum; 4FBX; -.
DR PDBsum; 4GRB; -.
DR PDBsum; 4GUB; -.
DR PDBsum; 4GYW; -.
DR PDBsum; 4GYY; -.
DR PDBsum; 4GZ3; -.
DR PDBsum; 4IB5; -.
DR PDBsum; 4MD7; -.
DR PDBsum; 4MD8; -.
DR PDBsum; 4MD9; -.
DR ProteinModelPortal; P68400; -.
DR SMR; P68400; 2-359.
DR DIP; DIP-32682N; -.
DR IntAct; P68400; 213.
DR MINT; MINT-142347; -.
DR STRING; 9606.ENSP00000217244; -.
DR BindingDB; P68400; -.
DR ChEMBL; CHEMBL3629; -.
DR GuidetoPHARMACOLOGY; 1549; -.
DR PhosphoSite; P68400; -.
DR DMDM; 55977123; -.
DR PaxDb; P68400; -.
DR PRIDE; P68400; -.
DR DNASU; 1457; -.
DR Ensembl; ENST00000217244; ENSP00000217244; ENSG00000101266.
DR Ensembl; ENST00000349736; ENSP00000339247; ENSG00000101266.
DR Ensembl; ENST00000400217; ENSP00000383076; ENSG00000101266.
DR GeneID; 1457; -.
DR KEGG; hsa:1457; -.
DR UCSC; uc002wdw.1; human.
DR CTD; 1457; -.
DR GeneCards; GC20M000459; -.
DR HGNC; HGNC:2457; CSNK2A1.
DR HPA; CAB020680; -.
DR MIM; 115440; gene.
DR neXtProt; NX_P68400; -.
DR PharmGKB; PA26957; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000233021; -.
DR HOVERGEN; HBG107282; -.
DR KO; K03097; -.
DR OMA; NNTDFRS; -.
DR OrthoDB; EOG7QG446; -.
DR PhylomeDB; P68400; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR SignaLink; P68400; -.
DR ChiTaRS; CSNK2A1; human.
DR EvolutionaryTrace; P68400; -.
DR GeneWiki; Casein_kinase_2,_alpha_1; -.
DR GenomeRNAi; 1457; -.
DR NextBio; 5989; -.
DR PMAP-CutDB; B4DYS6; -.
DR PRO; PR:P68400; -.
DR ArrayExpress; P68400; -.
DR Bgee; P68400; -.
DR CleanEx; HS_CSNK2A1; -.
DR Genevestigator; P68400; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016581; C:NuRD complex; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0016580; C:Sin3 complex; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051879; F:Hsp90 protein binding; TAS:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0061077; P:chaperone-mediated protein folding; TAS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR GO; GO:0071174; P:mitotic spindle checkpoint; IMP:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; ATP-binding;
KW Cell cycle; Complete proteome; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transcription; Transcription regulation; Transferase;
KW Wnt signaling pathway.
FT CHAIN 1 391 Casein kinase II subunit alpha.
FT /FTId=PRO_0000085883.
FT DOMAIN 39 324 Protein kinase.
FT NP_BIND 45 53 ATP (By similarity).
FT REGION 36 41 Interaction with beta subunit (By
FT similarity).
FT ACT_SITE 156 156 Proton acceptor.
FT BINDING 68 68 ATP (By similarity).
FT MOD_RES 344 344 Phosphothreonine; by CDK1.
FT MOD_RES 360 360 Phosphothreonine; by CDK1.
FT MOD_RES 362 362 Phosphoserine; by CDK1.
FT MOD_RES 370 370 Phosphoserine; by CDK1.
FT VAR_SEQ 1 136 Missing (in isoform 2).
FT /FTId=VSP_041925.
FT CONFLICT 128 128 L -> F (in Ref. 3; CAA49758).
FT CONFLICT 256 256 D -> G (in Ref. 3; CAA49758).
FT CONFLICT 287 287 S -> R (in Ref. 3; CAA49758).
FT CONFLICT 351 351 M -> V (in Ref. 3; CAA49758).
FT STRAND 10 12
FT TURN 13 18
FT HELIX 21 24
FT HELIX 26 28
FT HELIX 36 38
FT STRAND 39 47
FT STRAND 49 58
FT TURN 59 61
FT STRAND 64 70
FT HELIX 75 88
FT STRAND 97 102
FT TURN 104 106
FT STRAND 109 114
FT HELIX 121 124
FT HELIX 125 127
FT HELIX 130 149
FT HELIX 159 161
FT STRAND 162 165
FT TURN 166 169
FT STRAND 170 173
FT HELIX 176 178
FT HELIX 195 197
FT HELIX 200 203
FT HELIX 212 227
FT STRAND 230 233
FT HELIX 238 249
FT HELIX 251 260
FT HELIX 269 273
FT HELIX 281 284
FT TURN 287 289
FT HELIX 290 292
FT HELIX 295 302
FT HELIX 309 311
FT HELIX 315 319
FT HELIX 322 324
FT HELIX 327 329
FT STRAND 333 335
SQ SEQUENCE 391 AA; 45144 MW; D3B6F5D13FF7422D CRC64;
MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY SEVFEAINIT
NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD
FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE
FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD
QLVRIAKVLG TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF
LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN MMSGISSVPT
PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ Q
//
ID CSK21_HUMAN Reviewed; 391 AA.
AC P68400; B4DYS6; D3DVV8; P19138; P20426; Q14013; Q5U065;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-NOV-2004, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Casein kinase II subunit alpha;
DE Short=CK II alpha;
DE EC=2.7.11.1;
GN Name=CSNK2A1; Synonyms=CK2A1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2752008; DOI=10.1021/bi00435a066;
RA Meisner H., Heller-Harrison R., Buxton J., Czech M.P.;
RT "Molecular cloning of the human casein kinase II alpha subunit.";
RL Biochemistry 28:4072-4076(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2174700; DOI=10.1021/bi00488a034;
RA Lozeman F.J., Litchfield D.W., Piening C., Takio K., Walsh K.A.,
RA Krebs E.G.;
RT "Isolation and characterization of human cDNA clones encoding the
RT alpha and the alpha' subunits of casein kinase II.";
RL Biochemistry 29:8436-8447(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=8420794; DOI=10.1016/0014-5793(93)81197-8;
RA Devilat I., Carvallo P.;
RT "Structure and sequence of an intronless gene for human casein kinase
RT II-alpha subunit.";
RL FEBS Lett. 316:114-118(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Muscle, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PHOSPHORYLATION AT THR-344; THR-360; SER-362 AND SER-370.
RX PubMed=7592773; DOI=10.1074/jbc.270.43.25872;
RA Bosc D.G., Slominski E., Sichler C., Litchfield D.W.;
RT "Phosphorylation of casein kinase II by p34cdc2. Identification of
RT phosphorylation sites using phosphorylation site mutants in vitro.";
RL J. Biol. Chem. 270:25872-25878(1995).
RN [11]
RP FUNCTION, AND INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=11239457; DOI=10.1016/S1097-2765(01)00176-9;
RA Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H.,
RA Goodman R., Lozano G., Zhao Y., Lu H.;
RT "A DNA damage-induced p53 serine 392 kinase complex contains CK2,
RT hSpt16, and SSRP1.";
RL Mol. Cell 7:283-292(2001).
RN [12]
RP FUNCTION IN CELL CYCLE.
RX PubMed=11704824; DOI=10.1038/sj.onc.1204894;
RA Sayed M., Pelech S., Wong C., Marotta A., Salh B.;
RT "Protein kinase CK2 is involved in G2 arrest and apoptosis following
RT spindle damage in epithelial cells.";
RL Oncogene 20:6994-7005(2001).
RN [13]
RP INTERACTION WITH SSRP1 AND SUPT16H.
RX PubMed=12393879; DOI=10.1074/jbc.M209820200;
RA Keller D.M., Lu H.;
RT "p53 serine 392 phosphorylation increases after UV through induction
RT of the assembly of the CK2.hSPT16.SSRP1 complex.";
RL J. Biol. Chem. 277:50206-50213(2002).
RN [14]
RP FUNCTION IN APOPTOSIS.
RX PubMed=16193064; DOI=10.1038/sj.emboj.7600827;
RA Shin S., Lee Y., Kim W., Ko H., Choi H., Kim K.;
RT "Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by
RT processing procaspase-8.";
RL EMBO J. 24:3532-3542(2005).
RN [15]
RP INTERACTION WITH RNPS1.
RX PubMed=15684395; DOI=10.1128/MCB.25.4.1446-1457.2005;
RA Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A.,
RA Suzuki H., Endo H., Kidd V.J., Mayeda A.;
RT "Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2
RT phosphorylation.";
RL Mol. Cell. Biol. 25:1446-1457(2005).
RN [16]
RP FUNCTION IN CELL CYCLE.
RX PubMed=19188443; DOI=10.1128/MCB.01563-08;
RA St-Denis N.A., Derksen D.R., Litchfield D.W.;
RT "Evidence for regulation of mitotic progression through temporal
RT phosphorylation and dephosphorylation of CK2alpha.";
RL Mol. Cell. Biol. 29:2068-2081(2009).
RN [17]
RP REVIEW ON FUNCTION.
RX PubMed=12631575; DOI=10.1096/fj.02-0473rev;
RA Meggio F., Pinna L.A.;
RT "One-thousand-and-one substrates of protein kinase CK2?";
RL FASEB J. 17:349-368(2003).
RN [18]
RP REVIEW ON STRUCTURE.
RX PubMed=19387553; DOI=10.1007/s00018-009-9149-8;
RA Niefind K., Raaf J., Issinger O.G.;
RT "Protein kinase CK2 in health and disease: Protein kinase CK2: from
RT structures to insights.";
RL Cell. Mol. Life Sci. 66:1800-1816(2009).
RN [19]
RP REVIEW ON FUNCTION.
RX PubMed=19387552; DOI=10.1007/s00018-009-9150-2;
RA St-Denis N.A., Litchfield D.W.;
RT "Protein kinase CK2 in health and disease: From birth to death: the
RT role of protein kinase CK2 in the regulation of cell proliferation and
RT survival.";
RL Cell. Mol. Life Sci. 66:1817-1829(2009).
RN [20]
RP REVIEW ON FUNCTION.
RX PubMed=19387551; DOI=10.1007/s00018-009-9151-1;
RA Filhol O., Cochet C.;
RT "Protein kinase CK2 in health and disease: Cellular functions of
RT protein kinase CK2: a dynamic affair.";
RL Cell. Mol. Life Sci. 66:1830-1839(2009).
RN [21]
RP REVIEW ON FUNCTION IN REGULATION OF HSP90.
RX PubMed=19387550; DOI=10.1007/s00018-009-9152-0;
RA Miyata Y.;
RT "Protein kinase CK2 in health and disease: CK2: the kinase controlling
RT the Hsp90 chaperone machinery.";
RL Cell. Mol. Life Sci. 66:1840-1849(2009).
RN [22]
RP REVIEW ON FUNCTION IN WNT SIGNALING.
RX PubMed=19387549; DOI=10.1007/s00018-009-9153-z;
RA Dominguez I., Sonenshein G.E., Seldin D.C.;
RT "Protein kinase CK2 in health and disease: CK2 and its role in Wnt and
RT NF-kappaB signaling: linking development and cancer.";
RL Cell. Mol. Life Sci. 66:1850-1857(2009).
RN [23]
RP INTERACTION WITH SNAI1.
RX PubMed=19923321; DOI=10.1091/mbc.E09-06-0504;
RA MacPherson M.R., Molina P., Souchelnytskyi S., Wernstedt C.,
RA Martin-Perez J., Portillo F., Cano A.;
RT "Phosphorylation of serine 11 and serine 92 as new positive regulators
RT of human Snail1 function: potential involvement of casein kinase-2 and
RT the cAMP-activated kinase protein kinase A.";
RL Mol. Biol. Cell 21:244-253(2010).
RN [24]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH PML.
RX PubMed=20625391; DOI=10.1371/journal.pone.0011418;
RA Hung M.S., Lin Y.C., Mao J.H., Kim I.J., Xu Z., Yang C.T.,
RA Jablons D.M., You L.;
RT "Functional polymorphism of the CK2alpha intronless gene plays
RT oncogenic roles in lung cancer.";
RL PLoS ONE 5:E11418-E11418(2010).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [26]
RP FUNCTION, AND INTERACTION WITH PML.
RX PubMed=22406621; DOI=10.1158/0008-5472.CAN-11-3159;
RA Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A.,
RA Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J.,
RA Scaglioni P.P.;
RT "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its
RT oncogenic counterpart PML-RARA.";
RL Cancer Res. 72:2275-2284(2012).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337, AND SUBUNIT.
RX PubMed=11092945; DOI=10.1107/S0907444900013627;
RA Niefind K., Guerra B., Ermakowa I., Issinger O.G.;
RT "Crystallization and preliminary characterization of crystals of human
RT protein kinase CK2.";
RL Acta Crystallogr. D 56:1680-1684(2000).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337 IN COMPLEX WITH CSNK2B,
RP AND SUBUNIT.
RX PubMed=11574463; DOI=10.1093/emboj/20.19.5320;
RA Niefind K., Guerra B., Ermakowa I., Issinger O.G.;
RT "Crystal structure of human protein kinase CK2: insights into basic
RT properties of the CK2 holoenzyme.";
RL EMBO J. 20:5320-5331(2001).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-329.
RX PubMed=14646071; DOI=10.1107/S0907444903018900;
RA Pechkova E., Zanotti G., Nicolini C.;
RT "Three-dimensional atomic structure of a catalytic subunit mutant of
RT human protein kinase CK2.";
RL Acta Crystallogr. D 59:2133-2139(2003).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-335.
RX PubMed=12860116; DOI=10.1016/S0022-2836(03)00638-7;
RA Ermakova I., Boldyreff B., Issinger O.G., Niefind K.;
RT "Crystal structure of a C-terminal deletion mutant of human protein
RT kinase CK2 catalytic subunit.";
RL J. Mol. Biol. 330:925-934(2003).
CC -!- FUNCTION: Catalytic subunit of a constitutively active
CC serine/threonine-protein kinase complex that phosphorylates a
CC large number of substrates containing acidic residues C-terminal
CC to the phosphorylated serine or threonine. Regulates numerous
CC cellular processes, such as cell cycle progression, apoptosis and
CC transcription, as well as viral infection. May act as a regulatory
CC node which integrates and coordinates numerous signals leading to
CC an appropriate cellular response. During mitosis, functions as a
CC component of the p53/TP53-dependent spindle assembly checkpoint
CC (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in
CC response to spindle damage. Also required for p53/TP53-mediated
CC apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV
CC irradiation. Can also negatively regulate apoptosis.
CC Phosphorylates the caspases CASP9 and CASP2 and the apoptotic
CC regulator NOL3. Phosphorylation protects CASP9 from cleavage and
CC activation by CASP8, and inhibits the dimerization of CASP2 and
CC activation of CASP8. Regulates transcription by direct
CC phosphorylation of RNA polymerases I, II, III and IV. Also
CC phosphorylates and regulates numerous transcription factors
CC including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX,
CC JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones
CC FKBP4 and CDC37, which is essential for chaperone function.
CC Regulates Wnt signaling by phosphorylating CTNNB1 and the
CC transcription factor LEF1. Acts as an ectokinase that
CC phosphorylates several extracellular proteins. During viral
CC infection, phosphorylates various proteins involved in the viral
CC life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.
CC Phosphorylates PML at 'Ser-565' and primes it for ubiquitin-
CC mediated degradation.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- ENZYME REGULATION: Constitutively active protein kinase whose
CC activity is not directly affected by phosphorylation. Seems to be
CC regulated by level of expression and localization.
CC -!- SUBUNIT: Heterotetramer composed of two catalytic subunits (alpha
CC chain and/or alpha' chain) and two regulatory subunits (beta
CC chains). The tetramer can exist as a combination of 2 alpha/2
CC beta, 2 alpha'/2 beta or 1 alpha/1 alpha'/2 beta subunits. Also
CC part of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H,
CC CSNK2A1, CSNK2A2 and CSNK2B, which forms following UV irradiation.
CC Interacts with RNPS1. Interacts with SNAI1. Interacts with PML
CC (isoform PML-12).
CC -!- INTERACTION:
CC O00257-3:CBX4; NbExp=2; IntAct=EBI-347804, EBI-4392727;
CC P19784:CSNK2A2; NbExp=3; IntAct=EBI-347804, EBI-347451;
CC P67870:CSNK2B; NbExp=13; IntAct=EBI-347804, EBI-348169;
CC Q13547:HDAC1; NbExp=2; IntAct=EBI-347804, EBI-301834;
CC O60282:KIF5C; NbExp=4; IntAct=EBI-347804, EBI-717170;
CC P29590:PML; NbExp=2; IntAct=EBI-347804, EBI-295890;
CC Q96EB6:SIRT1; NbExp=4; IntAct=EBI-347804, EBI-1802965;
CC Q92504:SLC39A7; NbExp=4; IntAct=EBI-347804, EBI-1051105;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P68400-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P68400-2; Sequence=VSP_041925;
CC -!- PTM: Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by
CC CDK1 in prophase and metaphase and dephosphorylated during
CC anaphase. Phosphorylation does not directly affect casein kinase 2
CC activity, but may contribute to its regulation by forming binding
CC sites for interacting proteins and/or targeting it to different
CC compartments.
CC -!- MISCELLANEOUS: Can use both ATP and GTP as phosphoryl donors.
CC Phosphorylation by casein kinase 2 has been estimated to represent
CC up to one quarter of the eukaryotic phosphoproteome. Casein kinase
CC 2 has been found to be increased at protein level and up-regulated
CC at the level of enzyme activity in the majority of cancers.
CC However, elevated levels of casein kinase 2 are present in certain
CC normal organs such as brain and testes.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC protein kinase family. CK2 subfamily.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
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DR EMBL; J02853; AAA56821.1; -; mRNA.
DR EMBL; M55265; AAA35503.1; -; mRNA.
DR EMBL; S53149; ABB72474.1; -; mRNA.
DR EMBL; X70251; CAA49758.1; -; Genomic_DNA.
DR EMBL; AK302583; BAG63838.1; -; mRNA.
DR EMBL; BT019792; AAV38595.1; -; mRNA.
DR EMBL; AB451279; BAG70093.1; -; mRNA.
DR EMBL; AL049761; CAB65624.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10665.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10666.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10667.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10668.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10669.1; -; Genomic_DNA.
DR EMBL; BC011668; AAH11668.1; -; mRNA.
DR EMBL; BC053532; AAH53532.1; -; mRNA.
DR EMBL; BC071167; AAH71167.1; -; mRNA.
DR PIR; A30319; A30319.
DR RefSeq; NP_001886.1; NM_001895.3.
DR RefSeq; NP_808227.1; NM_177559.2.
DR RefSeq; NP_808228.1; NM_177560.2.
DR UniGene; Hs.644056; -.
DR UniGene; Hs.654675; -.
DR UniGene; Hs.741126; -.
DR PDB; 1JWH; X-ray; 3.10 A; A/B=1-337.
DR PDB; 1NA7; X-ray; 2.40 A; A=1-329.
DR PDB; 1PJK; X-ray; 2.50 A; A=2-335.
DR PDB; 2PVR; X-ray; 1.60 A; A=2-335.
DR PDB; 2ZJW; X-ray; 2.40 A; A=1-335.
DR PDB; 3AMY; X-ray; 2.30 A; A=1-335.
DR PDB; 3AT2; X-ray; 1.60 A; A=1-335.
DR PDB; 3AT3; X-ray; 2.60 A; A=1-335.
DR PDB; 3AT4; X-ray; 2.20 A; A=1-335.
DR PDB; 3AXW; X-ray; 2.50 A; A=1-335.
DR PDB; 3BQC; X-ray; 1.50 A; A=1-335.
DR PDB; 3C13; X-ray; 1.95 A; A=1-335.
DR PDB; 3FWQ; X-ray; 2.30 A; A/B=1-335.
DR PDB; 3H30; X-ray; 1.56 A; A/B=1-334.
DR PDB; 3JUH; X-ray; 1.66 A; A/B=1-335.
DR PDB; 3MB6; X-ray; 1.75 A; A=1-331.
DR PDB; 3MB7; X-ray; 1.65 A; A=1-331.
DR PDB; 3NGA; X-ray; 2.71 A; A/B=1-333.
DR PDB; 3NSZ; X-ray; 1.30 A; A=2-331.
DR PDB; 3OWJ; X-ray; 1.85 A; A=1-331.
DR PDB; 3OWK; X-ray; 1.80 A; A=1-331.
DR PDB; 3OWL; X-ray; 2.10 A; A=1-331.
DR PDB; 3PE1; X-ray; 1.60 A; A=1-337.
DR PDB; 3PE2; X-ray; 1.90 A; A=1-337.
DR PDB; 3PE4; X-ray; 1.95 A; B/D=340-352.
DR PDB; 3Q04; X-ray; 1.80 A; A=3-330.
DR PDB; 3Q9W; X-ray; 1.70 A; A=1-336.
DR PDB; 3Q9X; X-ray; 2.20 A; A/B=1-336.
DR PDB; 3Q9Y; X-ray; 1.80 A; A=1-336.
DR PDB; 3Q9Z; X-ray; 2.20 A; A/B=1-336.
DR PDB; 3QA0; X-ray; 2.50 A; A/B=1-336.
DR PDB; 3R0T; X-ray; 1.75 A; A=1-337.
DR PDB; 3RPS; X-ray; 2.30 A; A/B=1-335.
DR PDB; 3TAX; X-ray; 1.88 A; B/D=340-352.
DR PDB; 3U4U; X-ray; 2.20 A; A=1-333.
DR PDB; 3U87; X-ray; 2.90 A; A/B=1-329.
DR PDB; 3U9C; X-ray; 3.20 A; A/B=1-335.
DR PDB; 3W8L; X-ray; 2.40 A; A/B=1-335.
DR PDB; 3WAR; X-ray; 1.04 A; A=1-335.
DR PDB; 4DGL; X-ray; 3.00 A; C/D=1-335.
DR PDB; 4FBX; X-ray; 2.33 A; A=1-335.
DR PDB; 4GRB; X-ray; 2.15 A; A=1-333.
DR PDB; 4GUB; X-ray; 2.20 A; A=1-333.
DR PDB; 4GYW; X-ray; 1.70 A; B/D=340-352.
DR PDB; 4GYY; X-ray; 1.85 A; B/D=340-352.
DR PDB; 4GZ3; X-ray; 1.90 A; B/D=340-352.
DR PDB; 4IB5; X-ray; 2.20 A; A/B/C=1-335.
DR PDB; 4MD7; X-ray; 3.10 A; E/F/G/H=1-391.
DR PDB; 4MD8; X-ray; 3.30 A; E/F/G/H=1-391.
DR PDB; 4MD9; X-ray; 3.50 A; E/F/G/H/K/L/M/P=1-336.
DR PDBsum; 1JWH; -.
DR PDBsum; 1NA7; -.
DR PDBsum; 1PJK; -.
DR PDBsum; 2PVR; -.
DR PDBsum; 2ZJW; -.
DR PDBsum; 3AMY; -.
DR PDBsum; 3AT2; -.
DR PDBsum; 3AT3; -.
DR PDBsum; 3AT4; -.
DR PDBsum; 3AXW; -.
DR PDBsum; 3BQC; -.
DR PDBsum; 3C13; -.
DR PDBsum; 3FWQ; -.
DR PDBsum; 3H30; -.
DR PDBsum; 3JUH; -.
DR PDBsum; 3MB6; -.
DR PDBsum; 3MB7; -.
DR PDBsum; 3NGA; -.
DR PDBsum; 3NSZ; -.
DR PDBsum; 3OWJ; -.
DR PDBsum; 3OWK; -.
DR PDBsum; 3OWL; -.
DR PDBsum; 3PE1; -.
DR PDBsum; 3PE2; -.
DR PDBsum; 3PE4; -.
DR PDBsum; 3Q04; -.
DR PDBsum; 3Q9W; -.
DR PDBsum; 3Q9X; -.
DR PDBsum; 3Q9Y; -.
DR PDBsum; 3Q9Z; -.
DR PDBsum; 3QA0; -.
DR PDBsum; 3R0T; -.
DR PDBsum; 3RPS; -.
DR PDBsum; 3TAX; -.
DR PDBsum; 3U4U; -.
DR PDBsum; 3U87; -.
DR PDBsum; 3U9C; -.
DR PDBsum; 3W8L; -.
DR PDBsum; 3WAR; -.
DR PDBsum; 4DGL; -.
DR PDBsum; 4FBX; -.
DR PDBsum; 4GRB; -.
DR PDBsum; 4GUB; -.
DR PDBsum; 4GYW; -.
DR PDBsum; 4GYY; -.
DR PDBsum; 4GZ3; -.
DR PDBsum; 4IB5; -.
DR PDBsum; 4MD7; -.
DR PDBsum; 4MD8; -.
DR PDBsum; 4MD9; -.
DR ProteinModelPortal; P68400; -.
DR SMR; P68400; 2-359.
DR DIP; DIP-32682N; -.
DR IntAct; P68400; 213.
DR MINT; MINT-142347; -.
DR STRING; 9606.ENSP00000217244; -.
DR BindingDB; P68400; -.
DR ChEMBL; CHEMBL3629; -.
DR GuidetoPHARMACOLOGY; 1549; -.
DR PhosphoSite; P68400; -.
DR DMDM; 55977123; -.
DR PaxDb; P68400; -.
DR PRIDE; P68400; -.
DR DNASU; 1457; -.
DR Ensembl; ENST00000217244; ENSP00000217244; ENSG00000101266.
DR Ensembl; ENST00000349736; ENSP00000339247; ENSG00000101266.
DR Ensembl; ENST00000400217; ENSP00000383076; ENSG00000101266.
DR GeneID; 1457; -.
DR KEGG; hsa:1457; -.
DR UCSC; uc002wdw.1; human.
DR CTD; 1457; -.
DR GeneCards; GC20M000459; -.
DR HGNC; HGNC:2457; CSNK2A1.
DR HPA; CAB020680; -.
DR MIM; 115440; gene.
DR neXtProt; NX_P68400; -.
DR PharmGKB; PA26957; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000233021; -.
DR HOVERGEN; HBG107282; -.
DR KO; K03097; -.
DR OMA; NNTDFRS; -.
DR OrthoDB; EOG7QG446; -.
DR PhylomeDB; P68400; -.
DR Reactome; REACT_111045; Developmental Biology.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_21300; Mitotic M-M/G1 phases.
DR SignaLink; P68400; -.
DR ChiTaRS; CSNK2A1; human.
DR EvolutionaryTrace; P68400; -.
DR GeneWiki; Casein_kinase_2,_alpha_1; -.
DR GenomeRNAi; 1457; -.
DR NextBio; 5989; -.
DR PMAP-CutDB; B4DYS6; -.
DR PRO; PR:P68400; -.
DR ArrayExpress; P68400; -.
DR Bgee; P68400; -.
DR CleanEx; HS_CSNK2A1; -.
DR Genevestigator; P68400; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016581; C:NuRD complex; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0016580; C:Sin3 complex; IDA:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051879; F:Hsp90 protein binding; TAS:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR GO; GO:0061077; P:chaperone-mediated protein folding; TAS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome.
DR GO; GO:0071174; P:mitotic spindle checkpoint; IMP:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; ATP-binding;
KW Cell cycle; Complete proteome; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transcription; Transcription regulation; Transferase;
KW Wnt signaling pathway.
FT CHAIN 1 391 Casein kinase II subunit alpha.
FT /FTId=PRO_0000085883.
FT DOMAIN 39 324 Protein kinase.
FT NP_BIND 45 53 ATP (By similarity).
FT REGION 36 41 Interaction with beta subunit (By
FT similarity).
FT ACT_SITE 156 156 Proton acceptor.
FT BINDING 68 68 ATP (By similarity).
FT MOD_RES 344 344 Phosphothreonine; by CDK1.
FT MOD_RES 360 360 Phosphothreonine; by CDK1.
FT MOD_RES 362 362 Phosphoserine; by CDK1.
FT MOD_RES 370 370 Phosphoserine; by CDK1.
FT VAR_SEQ 1 136 Missing (in isoform 2).
FT /FTId=VSP_041925.
FT CONFLICT 128 128 L -> F (in Ref. 3; CAA49758).
FT CONFLICT 256 256 D -> G (in Ref. 3; CAA49758).
FT CONFLICT 287 287 S -> R (in Ref. 3; CAA49758).
FT CONFLICT 351 351 M -> V (in Ref. 3; CAA49758).
FT STRAND 10 12
FT TURN 13 18
FT HELIX 21 24
FT HELIX 26 28
FT HELIX 36 38
FT STRAND 39 47
FT STRAND 49 58
FT TURN 59 61
FT STRAND 64 70
FT HELIX 75 88
FT STRAND 97 102
FT TURN 104 106
FT STRAND 109 114
FT HELIX 121 124
FT HELIX 125 127
FT HELIX 130 149
FT HELIX 159 161
FT STRAND 162 165
FT TURN 166 169
FT STRAND 170 173
FT HELIX 176 178
FT HELIX 195 197
FT HELIX 200 203
FT HELIX 212 227
FT STRAND 230 233
FT HELIX 238 249
FT HELIX 251 260
FT HELIX 269 273
FT HELIX 281 284
FT TURN 287 289
FT HELIX 290 292
FT HELIX 295 302
FT HELIX 309 311
FT HELIX 315 319
FT HELIX 322 324
FT HELIX 327 329
FT STRAND 333 335
SQ SEQUENCE 391 AA; 45144 MW; D3B6F5D13FF7422D CRC64;
MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY SEVFEAINIT
NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD
FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE
FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD
QLVRIAKVLG TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF
LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN MMSGISSVPT
PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ Q
//
MIM
115440
*RECORD*
*FIELD* NO
115440
*FIELD* TI
*115440 CASEIN KINASE II, ALPHA-1; CSNK2A1
;;CASEIN KINASE II, ALPHA SUBUNIT; CK2A1
read more*FIELD* TX
CLONING
Casein kinase II is a serine/threonine kinase that phosphorylates acidic
protein such as casein. It has a tetrameric a(2)/b(2) structure. The
alpha subunit of molecular mass 40 kD possesses catalytic activity,
whereas the beta subunit (115441), molecular mass 25 kD, is
autophosphorylated in vitro. Meisner et al. (1989) reported the
identification and nucleotide sequencing of a complete human cDNA for
the alpha subunit. Using the full-length cDNA probe, Meisner et al.
(1989) found 2 bands with restriction enzymes that have no recognition
sites within the cDNA and 3 to 6 bands with enzymes having single
internal sites. These results were considered consistent with the
existence of 2 genes encoding alpha subunits. See 115442.
GENE STRUCTURE
Wirkner et al. (1994) demonstrated that the CSNK2A1 gene contains 8
exons whose sequences comprise bases 102 to 824 of the coding region of
the human casein kinase II alpha subunit. Three of the 9 introns are
located at positions corresponding to those of the homologous gene in
the nematode Caenorhabditis elegans. The introns contain 8 complete and
8 incomplete Alu repeats.
GENE FUNCTION
Phosphorylation of the human p53 protein (191170) at ser392 is
responsive to ultraviolet (UV) but not gamma irradiation. Keller et al.
(2001) identified and purified a mammalian UV-activated protein kinase
complex that phosphorylates ser392 in vitro. This kinase complex
contains CK2 and the chromatin transcriptional elongation factor FACT, a
heterodimer of SPT16 (605012) and SSRP1 (604328). In vitro studies
showed that FACT alters the specificity of CK2 in the complex such that
it selectively phosphorylates p53 over other substrates, including
casein. In addition, phosphorylation by the kinase complex was found to
enhance p53 activity. These results provided a potential mechanism for
p53 activation by UV irradiation.
Doray et al. (2002) demonstrated that the Golgi-localized,
gamma-ear-containing adenosine diphosphate ribosylation factor-binding
proteins (GGA1, 606004 and GGA3, 606006) and the coat protein adaptor
protein-1 (AP-1) complex (see AP1G2, 603534) colocalize in
clathrin-coated buds of the trans-Golgi networks of mouse L cells and
human HeLa cells. Binding studies revealed a direct interaction between
the hinge domains of the GGAs and the gamma-ear domain of AP-1. Further,
AP-1 contained bound casein kinase-2 that phosphorylated GGA1 and GGA3,
thereby causing autoinhibition. Doray et al. (2002) demonstrated that
this autoinhibition could induce the directed transfer of mannose
6-phosphate receptors (see 154540) from the GGAs to AP-1. Mannose
6-phosphate receptors that were defective in binding to GGAs were poorly
incorporated into adaptor protein complex containing clathrin coated
vesicles. Thus, Doray et al. (2002) concluded that GGAs and the AP-1
complex interact to package mannose 6-phosphate receptors into
AP-1-containing coated vesicles.
Lin et al. (2002) identified a Drosophila circadian mutant, Timekeeper
(Tik), that behaved in a dominant manner. Tik homozygotes do not live to
adulthood, and heterozygotes have a circadian rhythm lengthened by about
3 hours. Lin et al. (2002) showed that the catalytic subunit of
Drosophila casein kinase-2 (CK2-alpha) is expressed predominantly in the
cytoplasm of key circadian pacemaker neurons. CK2-alpha mutant flies
showed lengthened circadian period, decreased CK2 activity, and delayed
nuclear entry of Per (see 602260). Lin et al. (2002) suggested that
these are probably direct, as CK2-alpha specifically phosphorylates Per
in vitro. Lin et al. (2002) proposed that CK2 is an evolutionary link
between the divergent circadian systems of animals, plants, and fungi.
Loizou et al. (2004) showed that CK2 phosphorylates the scaffold protein
XRCC1 (194360) and thereby enables the assembly and activity of DNA
single-strand break repair protein complexes in vitro and at sites of
chromosome breakage. Inhibition of XRCC1 phosphorylation by mutation of
the CK2 phosphorylation sites or by preventing CK2 activity using a
highly specific inhibitor ablated the rapid repair of cellular DNA
single-strand breaks by XRCC1. These data identified a direct role for
CK2 in the repair of chromosome DNA strand breaks and in maintaining
genetic integrity.
Downstream core promoter elements (DPE) are regulatory sequences that
add diversity to the promoter architecture of RNA polymerase
II-transcribed genes. Despite a functional correlation between the
presence of TFIID (313650) and DPE, Lewis et al. (2005) found that TFIID
was insufficient for DPE-specific transcription in HeLa cells. Using a
functional transcription assay coupled with conventional biochemistry,
they found that protein kinase CK2, in conjunction with the coactivator
PC4 (600503), established DPE-specific transcription.
MAPPING
By segregation analysis of rodent-human somatic cell hybrids and
chromosomal in situ hybridization, Yang-Feng et al. (1991) identified 2
loci for the alpha subunit of casein kinase II: 11p15.5-p.15.4 and
20p13. Whether one of these is a pseudogene remained to be determined.
Boldyreff et al. (1992) likewise found 2 assignments by in situ
hybridization: 11pter-p15.1 and 20p13. Only the locus on chromosome 11
was confirmed by somatic cell hybrid analysis, based on the presence of
a CK2A1-specific 20-kb fragment. However, Wirkner et al. (1992)
demonstrated that the sequence that maps to 11p15 by in situ
hybridization has the characteristics of a processed pseudogene.
By fluorescence in situ hybridization using an 18.9-kb genomic clone
representing the central portion of the gene, Wirkner et al. (1994)
mapped CSNK2A1 to 20p13. Using the genomic clone, no hybridization
signal was obtained in 11p15 as had previously been the case when the
cDNA was used as probe (Yang-Feng et al., 1991).
*FIELD* RF
1. Boldyreff, B.; Klett, C.; Gottert, E.; Geurts van Kessel, A.; Hameister,
H.; Issinger, O.-G.: Assignment of casein kinase 2 alpha sequences
to two different human chromosomes. Hum. Genet. 89: 79-82, 1992.
2. Doray, B.; Ghosh, P.; Griffith, J.; Geuze, H. J.; Kornfeld, S.
: Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi
network. Science 297: 1700-1703, 2002.
3. 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. Molec.
Cell 7: 283-292, 2001.
4. Lewis, B. A.; Sims, R. J., III; Lane, W. S.; Reinberg, D.: Functional
characterization of core promoter elements: DPE-specific transcription
requires the protein kinase CK2 and the PC4 coactivator. Molec. Cell 18:
471-481, 2005.
5. Lin, J.-M.; Kilman, V. L.; Keegan, K.; Paddock, B.; Emery-Le, M.;
Rosbash, M.; Allada, R.: A role for casein kinase 2-alpha in the
Drosophila circadian clock. Nature 420: 816-820, 2002.
6. Loizou, J. I.; El-Khamisy, S. F.; Zlatanou, A.; Moore, D. J.; Chan,
D. W.; Qin, J.; Sarno, S.; Meggio, F.; Pinna, L. A.; Caldecott, K.
W.: The protein kinase CK2 facilitates repair of chromosomal DNA
single-strand breaks. Cell 117: 17-28, 2004.
7. 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. Note: Erratum: Biochemistry 28: 7138 only, 1989.
8. Wirkner, U.; Voss, H.; Lichter, P.; Ansorge, W.; Pyerin, W.: The
human gene (CSNK2A1) coding for the casein kinase II subunit alpha
is located on chromosome 20 and contains tandemly arranged Alu repeats. Genomics 19:
257-265, 1994.
9. Wirkner, U.; Voss, H.; Lichter, P.; Weitz, S.; Ansorge, W.; Pyerin,
W.: Human casein kinase II subunit alpha: sequence of a processed
(pseudo)gene and its localization on chromosome 11. Biochim. Biophys.
Acta 1131: 220-222, 1992.
10. Yang-Feng, T. L.; Zheng, K.; Kopatz, I.; Naiman, T.; Canaani,
D.: Mapping of the human casein kinase II catalytic subunit genes:
two loci carrying the homologous sequences for the alpha subunit. Nucleic
Acids Res. 19: 7125-7129, 1991.
*FIELD* CN
Patricia A. Hartz - updated: 6/24/2005
Stylianos E. Antonarakis - updated: 4/13/2004
Ada Hamosh - updated: 11/25/2002
Ada Hamosh - updated: 10/23/2002
Stylianos E. Antonarakis - updated: 3/12/2001
*FIELD* CD
Victor A. McKusick: 6/12/1989
*FIELD* ED
carol: 03/19/2013
carol: 3/19/2013
mgross: 6/24/2005
mgross: 4/13/2004
mgross: 9/18/2003
alopez: 12/19/2002
alopez: 12/3/2002
terry: 11/25/2002
alopez: 10/23/2002
mgross: 3/12/2001
psherman: 10/22/1999
dkim: 6/30/1998
mark: 1/19/1998
mark: 10/16/1996
carol: 4/12/1994
carol: 10/8/1992
carol: 6/11/1992
carol: 3/25/1992
supermim: 3/16/1992
carol: 1/2/1991
*RECORD*
*FIELD* NO
115440
*FIELD* TI
*115440 CASEIN KINASE II, ALPHA-1; CSNK2A1
;;CASEIN KINASE II, ALPHA SUBUNIT; CK2A1
read more*FIELD* TX
CLONING
Casein kinase II is a serine/threonine kinase that phosphorylates acidic
protein such as casein. It has a tetrameric a(2)/b(2) structure. The
alpha subunit of molecular mass 40 kD possesses catalytic activity,
whereas the beta subunit (115441), molecular mass 25 kD, is
autophosphorylated in vitro. Meisner et al. (1989) reported the
identification and nucleotide sequencing of a complete human cDNA for
the alpha subunit. Using the full-length cDNA probe, Meisner et al.
(1989) found 2 bands with restriction enzymes that have no recognition
sites within the cDNA and 3 to 6 bands with enzymes having single
internal sites. These results were considered consistent with the
existence of 2 genes encoding alpha subunits. See 115442.
GENE STRUCTURE
Wirkner et al. (1994) demonstrated that the CSNK2A1 gene contains 8
exons whose sequences comprise bases 102 to 824 of the coding region of
the human casein kinase II alpha subunit. Three of the 9 introns are
located at positions corresponding to those of the homologous gene in
the nematode Caenorhabditis elegans. The introns contain 8 complete and
8 incomplete Alu repeats.
GENE FUNCTION
Phosphorylation of the human p53 protein (191170) at ser392 is
responsive to ultraviolet (UV) but not gamma irradiation. Keller et al.
(2001) identified and purified a mammalian UV-activated protein kinase
complex that phosphorylates ser392 in vitro. This kinase complex
contains CK2 and the chromatin transcriptional elongation factor FACT, a
heterodimer of SPT16 (605012) and SSRP1 (604328). In vitro studies
showed that FACT alters the specificity of CK2 in the complex such that
it selectively phosphorylates p53 over other substrates, including
casein. In addition, phosphorylation by the kinase complex was found to
enhance p53 activity. These results provided a potential mechanism for
p53 activation by UV irradiation.
Doray et al. (2002) demonstrated that the Golgi-localized,
gamma-ear-containing adenosine diphosphate ribosylation factor-binding
proteins (GGA1, 606004 and GGA3, 606006) and the coat protein adaptor
protein-1 (AP-1) complex (see AP1G2, 603534) colocalize in
clathrin-coated buds of the trans-Golgi networks of mouse L cells and
human HeLa cells. Binding studies revealed a direct interaction between
the hinge domains of the GGAs and the gamma-ear domain of AP-1. Further,
AP-1 contained bound casein kinase-2 that phosphorylated GGA1 and GGA3,
thereby causing autoinhibition. Doray et al. (2002) demonstrated that
this autoinhibition could induce the directed transfer of mannose
6-phosphate receptors (see 154540) from the GGAs to AP-1. Mannose
6-phosphate receptors that were defective in binding to GGAs were poorly
incorporated into adaptor protein complex containing clathrin coated
vesicles. Thus, Doray et al. (2002) concluded that GGAs and the AP-1
complex interact to package mannose 6-phosphate receptors into
AP-1-containing coated vesicles.
Lin et al. (2002) identified a Drosophila circadian mutant, Timekeeper
(Tik), that behaved in a dominant manner. Tik homozygotes do not live to
adulthood, and heterozygotes have a circadian rhythm lengthened by about
3 hours. Lin et al. (2002) showed that the catalytic subunit of
Drosophila casein kinase-2 (CK2-alpha) is expressed predominantly in the
cytoplasm of key circadian pacemaker neurons. CK2-alpha mutant flies
showed lengthened circadian period, decreased CK2 activity, and delayed
nuclear entry of Per (see 602260). Lin et al. (2002) suggested that
these are probably direct, as CK2-alpha specifically phosphorylates Per
in vitro. Lin et al. (2002) proposed that CK2 is an evolutionary link
between the divergent circadian systems of animals, plants, and fungi.
Loizou et al. (2004) showed that CK2 phosphorylates the scaffold protein
XRCC1 (194360) and thereby enables the assembly and activity of DNA
single-strand break repair protein complexes in vitro and at sites of
chromosome breakage. Inhibition of XRCC1 phosphorylation by mutation of
the CK2 phosphorylation sites or by preventing CK2 activity using a
highly specific inhibitor ablated the rapid repair of cellular DNA
single-strand breaks by XRCC1. These data identified a direct role for
CK2 in the repair of chromosome DNA strand breaks and in maintaining
genetic integrity.
Downstream core promoter elements (DPE) are regulatory sequences that
add diversity to the promoter architecture of RNA polymerase
II-transcribed genes. Despite a functional correlation between the
presence of TFIID (313650) and DPE, Lewis et al. (2005) found that TFIID
was insufficient for DPE-specific transcription in HeLa cells. Using a
functional transcription assay coupled with conventional biochemistry,
they found that protein kinase CK2, in conjunction with the coactivator
PC4 (600503), established DPE-specific transcription.
MAPPING
By segregation analysis of rodent-human somatic cell hybrids and
chromosomal in situ hybridization, Yang-Feng et al. (1991) identified 2
loci for the alpha subunit of casein kinase II: 11p15.5-p.15.4 and
20p13. Whether one of these is a pseudogene remained to be determined.
Boldyreff et al. (1992) likewise found 2 assignments by in situ
hybridization: 11pter-p15.1 and 20p13. Only the locus on chromosome 11
was confirmed by somatic cell hybrid analysis, based on the presence of
a CK2A1-specific 20-kb fragment. However, Wirkner et al. (1992)
demonstrated that the sequence that maps to 11p15 by in situ
hybridization has the characteristics of a processed pseudogene.
By fluorescence in situ hybridization using an 18.9-kb genomic clone
representing the central portion of the gene, Wirkner et al. (1994)
mapped CSNK2A1 to 20p13. Using the genomic clone, no hybridization
signal was obtained in 11p15 as had previously been the case when the
cDNA was used as probe (Yang-Feng et al., 1991).
*FIELD* RF
1. Boldyreff, B.; Klett, C.; Gottert, E.; Geurts van Kessel, A.; Hameister,
H.; Issinger, O.-G.: Assignment of casein kinase 2 alpha sequences
to two different human chromosomes. Hum. Genet. 89: 79-82, 1992.
2. Doray, B.; Ghosh, P.; Griffith, J.; Geuze, H. J.; Kornfeld, S.
: Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi
network. Science 297: 1700-1703, 2002.
3. 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. Molec.
Cell 7: 283-292, 2001.
4. Lewis, B. A.; Sims, R. J., III; Lane, W. S.; Reinberg, D.: Functional
characterization of core promoter elements: DPE-specific transcription
requires the protein kinase CK2 and the PC4 coactivator. Molec. Cell 18:
471-481, 2005.
5. Lin, J.-M.; Kilman, V. L.; Keegan, K.; Paddock, B.; Emery-Le, M.;
Rosbash, M.; Allada, R.: A role for casein kinase 2-alpha in the
Drosophila circadian clock. Nature 420: 816-820, 2002.
6. Loizou, J. I.; El-Khamisy, S. F.; Zlatanou, A.; Moore, D. J.; Chan,
D. W.; Qin, J.; Sarno, S.; Meggio, F.; Pinna, L. A.; Caldecott, K.
W.: The protein kinase CK2 facilitates repair of chromosomal DNA
single-strand breaks. Cell 117: 17-28, 2004.
7. 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. Note: Erratum: Biochemistry 28: 7138 only, 1989.
8. Wirkner, U.; Voss, H.; Lichter, P.; Ansorge, W.; Pyerin, W.: The
human gene (CSNK2A1) coding for the casein kinase II subunit alpha
is located on chromosome 20 and contains tandemly arranged Alu repeats. Genomics 19:
257-265, 1994.
9. Wirkner, U.; Voss, H.; Lichter, P.; Weitz, S.; Ansorge, W.; Pyerin,
W.: Human casein kinase II subunit alpha: sequence of a processed
(pseudo)gene and its localization on chromosome 11. Biochim. Biophys.
Acta 1131: 220-222, 1992.
10. Yang-Feng, T. L.; Zheng, K.; Kopatz, I.; Naiman, T.; Canaani,
D.: Mapping of the human casein kinase II catalytic subunit genes:
two loci carrying the homologous sequences for the alpha subunit. Nucleic
Acids Res. 19: 7125-7129, 1991.
*FIELD* CN
Patricia A. Hartz - updated: 6/24/2005
Stylianos E. Antonarakis - updated: 4/13/2004
Ada Hamosh - updated: 11/25/2002
Ada Hamosh - updated: 10/23/2002
Stylianos E. Antonarakis - updated: 3/12/2001
*FIELD* CD
Victor A. McKusick: 6/12/1989
*FIELD* ED
carol: 03/19/2013
carol: 3/19/2013
mgross: 6/24/2005
mgross: 4/13/2004
mgross: 9/18/2003
alopez: 12/19/2002
alopez: 12/3/2002
terry: 11/25/2002
alopez: 10/23/2002
mgross: 3/12/2001
psherman: 10/22/1999
dkim: 6/30/1998
mark: 1/19/1998
mark: 10/16/1996
carol: 4/12/1994
carol: 10/8/1992
carol: 6/11/1992
carol: 3/25/1992
supermim: 3/16/1992
carol: 1/2/1991