ID CSK21_HUMAN Reviewed; 391 AA. AC P68400; B4DYS6; D3DVV8; P19138; P20426; Q14013; Q5U065; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 27-MAR-2024, entry version 203. DE RecName: Full=Casein kinase II subunit alpha; DE Short=CK II alpha; DE EC=2.7.11.1 {ECO:0000269|PubMed:20545769, ECO:0000269|PubMed:22017874, ECO:0000269|PubMed:22325354, ECO:0000269|PubMed:30699359, ECO:0000269|PubMed:31439799}; GN Name=CSNK2A1; Synonyms=CK2A1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2752008; DOI=10.1021/bi00435a066; RA Meisner H., Heller-Harrison R., Buxton J., Czech M.P.; RT "Molecular cloning of the human casein kinase II alpha subunit."; RL Biochemistry 28:4072-4076(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2174700; DOI=10.1021/bi00488a034; RA Lozeman F.J., Litchfield D.W., Piening C., Takio K., Walsh K.A., RA Krebs E.G.; RT "Isolation and characterization of human cDNA clones encoding the alpha and RT the alpha' subunits of casein kinase II."; RL Biochemistry 29:8436-8447(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RX PubMed=8420794; DOI=10.1016/0014-5793(93)81197-8; RA Devilat I., Carvallo P.; RT "Structure and sequence of an intronless gene for human casein kinase II- RT alpha subunit."; RL FEBS Lett. 316:114-118(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, Muscle, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PHOSPHORYLATION AT THR-344; THR-360; SER-362 AND SER-370. RX PubMed=7592773; DOI=10.1074/jbc.270.43.25872; RA Bosc D.G., Slominski E., Sichler C., Litchfield D.W.; RT "Phosphorylation of casein kinase II by p34cdc2. Identification of RT phosphorylation sites using phosphorylation site mutants in vitro."; RL J. Biol. Chem. 270:25872-25878(1995). RN [11] RP FUNCTION, AND INTERACTION WITH SSRP1 AND SUPT16H. RX PubMed=11239457; DOI=10.1016/s1097-2765(01)00176-9; RA Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., RA Lozano G., Zhao Y., Lu H.; RT "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, RT and SSRP1."; RL Mol. Cell 7:283-292(2001). RN [12] RP FUNCTION IN CELL CYCLE. RX PubMed=11704824; DOI=10.1038/sj.onc.1204894; RA Sayed M., Pelech S., Wong C., Marotta A., Salh B.; RT "Protein kinase CK2 is involved in G2 arrest and apoptosis following RT spindle damage in epithelial cells."; RL Oncogene 20:6994-7005(2001). RN [13] RP INTERACTION WITH SSRP1 AND SUPT16H. RX PubMed=12393879; DOI=10.1074/jbc.m209820200; RA Keller D.M., Lu H.; RT "p53 serine 392 phosphorylation increases after UV through induction of the RT assembly of the CK2.hSPT16.SSRP1 complex."; RL J. Biol. Chem. 277:50206-50213(2002). RN [14] RP FUNCTION IN APOPTOSIS. RX PubMed=16193064; DOI=10.1038/sj.emboj.7600827; RA Shin S., Lee Y., Kim W., Ko H., Choi H., Kim K.; RT "Caspase-2 primes cancer cells for TRAIL-mediated apoptosis by processing RT procaspase-8."; RL EMBO J. 24:3532-3542(2005). RN [15] RP INTERACTION WITH RNPS1. RX PubMed=15684395; DOI=10.1128/mcb.25.4.1446-1457.2005; RA Trembley J.H., Tatsumi S., Sakashita E., Loyer P., Slaughter C.A., RA Suzuki H., Endo H., Kidd V.J., Mayeda A.; RT "Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 RT phosphorylation."; RL Mol. Cell. Biol. 25:1446-1457(2005). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [17] RP FUNCTION IN CELL CYCLE. RX PubMed=19188443; DOI=10.1128/mcb.01563-08; RA St-Denis N.A., Derksen D.R., Litchfield D.W.; RT "Evidence for regulation of mitotic progression through temporal RT phosphorylation and dephosphorylation of CK2alpha."; RL Mol. Cell. Biol. 29:2068-2081(2009). RN [18] RP REVIEW ON FUNCTION. RX PubMed=12631575; DOI=10.1096/fj.02-0473rev; RA Meggio F., Pinna L.A.; RT "One-thousand-and-one substrates of protein kinase CK2?"; RL FASEB J. 17:349-368(2003). RN [19] RP REVIEW ON STRUCTURE. RX PubMed=19387553; DOI=10.1007/s00018-009-9149-8; RA Niefind K., Raaf J., Issinger O.G.; RT "Protein kinase CK2 in health and disease: Protein kinase CK2: from RT structures to insights."; RL Cell. Mol. Life Sci. 66:1800-1816(2009). RN [20] RP REVIEW ON FUNCTION. RX PubMed=19387552; DOI=10.1007/s00018-009-9150-2; RA St-Denis N.A., Litchfield D.W.; RT "Protein kinase CK2 in health and disease: From birth to death: the role of RT protein kinase CK2 in the regulation of cell proliferation and survival."; RL Cell. Mol. Life Sci. 66:1817-1829(2009). RN [21] RP REVIEW ON FUNCTION. RX PubMed=19387551; DOI=10.1007/s00018-009-9151-1; RA Filhol O., Cochet C.; RT "Protein kinase CK2 in health and disease: Cellular functions of protein RT kinase CK2: a dynamic affair."; RL Cell. Mol. Life Sci. 66:1830-1839(2009). RN [22] RP REVIEW ON FUNCTION IN REGULATION OF HSP90. RX PubMed=19387550; DOI=10.1007/s00018-009-9152-0; RA Miyata Y.; RT "Protein kinase CK2 in health and disease: CK2: the kinase controlling the RT Hsp90 chaperone machinery."; RL Cell. Mol. Life Sci. 66:1840-1849(2009). RN [23] RP REVIEW ON FUNCTION IN WNT SIGNALING. RX PubMed=19387549; DOI=10.1007/s00018-009-9153-z; RA Dominguez I., Sonenshein G.E., Seldin D.C.; RT "Protein kinase CK2 in health and disease: CK2 and its role in Wnt and NF- RT kappaB signaling: linking development and cancer."; RL Cell. Mol. Life Sci. 66:1850-1857(2009). RN [24] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20545769; DOI=10.1111/j.1365-2443.2010.01418.x; RA Takeishi Y., Ohashi E., Ogawa K., Masai H., Obuse C., Tsurimoto T.; RT "Casein kinase 2-dependent phosphorylation of human Rad9 mediates the RT interaction between human Rad9-Hus1-Rad1 complex and TopBP1."; RL Genes Cells 15:761-771(2010). RN [25] RP INTERACTION WITH SNAI1. RX PubMed=19923321; DOI=10.1091/mbc.e09-06-0504; RA MacPherson M.R., Molina P., Souchelnytskyi S., Wernstedt C., RA Martin-Perez J., Portillo F., Cano A.; RT "Phosphorylation of serine 11 and serine 92 as new positive regulators of RT human Snail1 function: potential involvement of casein kinase-2 and the RT cAMP-activated kinase protein kinase A."; RL Mol. Biol. Cell 21:244-253(2010). RN [26] RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH PML. RX PubMed=20625391; DOI=10.1371/journal.pone.0011418; RA Hung M.S., Lin Y.C., Mao J.H., Kim I.J., Xu Z., Yang C.T., Jablons D.M., RA You L.; RT "Functional polymorphism of the CK2alpha intronless gene plays oncogenic RT roles in lung cancer."; RL PLoS ONE 5:E11418-E11418(2010). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [29] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=21482717; DOI=10.1083/jcb.201010026; RA Wang J., Gong Z., Chen J.; RT "MDC1 collaborates with TopBP1 in DNA replication checkpoint control."; RL J. Cell Biol. 193:267-273(2011). RN [30] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=22017874; DOI=10.1016/j.molcel.2011.07.039; RA Matsumoto G., Wada K., Okuno M., Kurosawa M., Nukina N.; RT "Serine 403 phosphorylation of p62/SQSTM1 regulates selective autophagic RT clearance of ubiquitinated proteins."; RL Mol. Cell 44:279-289(2011). RN [31] 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 [32] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=22325354; DOI=10.1016/j.molcel.2011.12.028; RA Yata K., Lloyd J., Maslen S., Bleuyard J.Y., Skehel M., Smerdon S.J., RA Esashi F.; RT "Plk1 and CK2 act in concert to regulate Rad51 during DNA double strand RT break repair."; RL Mol. Cell 45:371-383(2012). RN [33] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=22184066; DOI=10.1128/mcb.06466-11; RA Riman S., Rizkallah R., Kassardjian A., Alexander K.E., Luescher B., RA Hurt M.M.; RT "Phosphorylation of the transcription factor YY1 by CK2alpha prevents RT cleavage by caspase 7 during apoptosis."; RL Mol. Cell. Biol. 32:797-807(2012). RN [34] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=23123191; DOI=10.1016/j.bbamcr.2012.10.025; RA Ampofo E., Sokolowsky T., Goetz C., Montenarh M.; RT "Functional interaction of protein kinase CK2 and activating transcription RT factor 4 (ATF4), a key player in the cellular stress response."; RL Biochim. Biophys. Acta 1833:439-451(2013). RN [35] RP FUNCTION, INTERACTION WITH CCAR2, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=24962073; DOI=10.1002/ijc.29043; RA Bae J.S., Park S.H., Kim K.M., Kwon K.S., Kim C.Y., Lee H.K., Park B.H., RA Park H.S., Lee H., Moon W.S., Chung M.J., Sylvester K.G., Jang K.Y.; RT "CK2alpha phosphorylates DBC1 and is involved in the progression of gastric RT carcinoma and predicts poor survival of gastric carcinoma patients."; RL Int. J. Cancer 136:797-809(2015). RN [36] RP INVOLVEMENT IN OCNDS, AND VARIANTS OCNDS GLN-47; SER-50; GLY-175 AND RP ARG-198. RX PubMed=27048600; DOI=10.1007/s00439-016-1661-y; RA Okur V., Cho M.T., Henderson L., Retterer K., Schneider M., Sattler S., RA Niyazov D., Azage M., Smith S., Picker J., Lincoln S., Tarnopolsky M., RA Brady L., Bjornsson H.T., Applegate C., Dameron A., Willaert R., Baskin B., RA Juusola J., Chung W.K.; RT "De novo mutations in CSNK2A1 are associated with neurodevelopmental RT abnormalities and dysmorphic features."; RL Hum. Genet. 135:699-705(2016). RN [37] RP FUNCTION. RX PubMed=26811421; DOI=10.1083/jcb.201507042; RA Moudry P., Watanabe K., Wolanin K.M., Bartkova J., Wassing I.E., RA Watanabe S., Strauss R., Troelsgaard Pedersen R., Oestergaard V.H., RA Lisby M., Andujar-Sanchez M., Maya-Mendoza A., Esashi F., Lukas J., RA Bartek J.; RT "TOPBP1 regulates RAD51 phosphorylation and chromatin loading and RT determines PARP inhibitor sensitivity."; RL J. Cell Biol. 212:281-288(2016). RN [38] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=30699359; DOI=10.1016/j.celrep.2019.01.018; RA Sager R.A., Woodford M.R., Backe S.J., Makedon A.M., Baker-Williams A.J., RA DiGregorio B.T., Loiselle D.R., Haystead T.A., Zachara N.E., Prodromou C., RA Bourboulia D., Schmidt L.S., Linehan W.M., Bratslavsky G., Mollapour M.; RT "Post-translational regulation of FNIP1 creates a rheostat for the RT molecular chaperone Hsp90."; RL Cell Rep. 26:1344-1356(2019). RN [39] RP FUNCTION. RX PubMed=30765518; DOI=10.1073/pnas.1814385116; RA Tsang B., Arsenault J., Vernon R.M., Lin H., Sonenberg N., Wang L.Y., RA Bah A., Forman-Kay J.D.; RT "Phosphoregulated FMRP phase separation models activity-dependent RT translation through bidirectional control of mRNA granule formation."; RL Proc. Natl. Acad. Sci. U.S.A. 116:4218-4227(2019). RN [40] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=30898438; DOI=10.1016/j.molcel.2019.02.014; RA Leimbacher P.A., Jones S.E., Shorrocks A.K., de Marco Zompit M., Day M., RA Blaauwendraad J., Bundschuh D., Bonham S., Fischer R., Fink D., RA Kessler B.M., Oliver A.W., Pearl L.H., Blackford A.N., Stucki M.; RT "MDC1 interacts with TOPBP1 to maintain chromosomal stability during RT mitosis."; RL Mol. Cell 74:571-583(2019). RN [41] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=31439799; DOI=10.1126/science.aax4240; RA Kim T.H., Tsang B., Vernon R.M., Sonenberg N., Kay L.E., Forman-Kay J.D.; RT "Phospho-dependent phase separation of FMRP and CAPRIN1 recapitulates RT regulation of translation and deadenylation."; RL Science 365:825-829(2019). RN [42] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=35597237; DOI=10.1016/j.molcel.2022.04.031; RA Zhao J., Tian S., Guo Q., Bao K., Yu G., Wang X., Shen X., Zhang J., RA Chen J., Yang Y., Liu L., Li X., Hao J., Yang N., Liu Z., Ai D., Yang J., RA Zhu Y., Yao Z., Ma S., Zhang K., Shi L.; RT "A PARylation-phosphorylation cascade promotes TOPBP1 loading and RPA-RAD51 RT exchange in homologous recombination."; RL Mol. Cell 82:2571-2587(2022). RN [43] 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 [44] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-337 IN COMPLEX WITH CSNK2B, AND RP SUBUNIT. RX PubMed=11574463; DOI=10.1093/emboj/20.19.5320; RA Niefind K., Guerra B., Ermakowa I., Issinger O.G.; RT "Crystal structure of human protein kinase CK2: insights into basic RT properties of the CK2 holoenzyme."; RL EMBO J. 20:5320-5331(2001). RN [45] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-329. RX PubMed=14646071; DOI=10.1107/s0907444903018900; RA Pechkova E., Zanotti G., Nicolini C.; RT "Three-dimensional atomic structure of a catalytic subunit mutant of human RT protein kinase CK2."; RL Acta Crystallogr. D 59:2133-2139(2003). RN [46] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-335. RX PubMed=12860116; DOI=10.1016/s0022-2836(03)00638-7; RA Ermakova I., Boldyreff B., Issinger O.G., Niefind K.; RT "Crystal structure of a C-terminal deletion mutant of human protein kinase RT CK2 catalytic subunit."; RL J. Mol. Biol. 330:925-934(2003). CC -!- FUNCTION: Catalytic subunit of a constitutively active CC serine/threonine-protein kinase complex that phosphorylates a large CC number of substrates containing acidic residues C-terminal to the CC phosphorylated serine or threonine (PubMed:11239457, PubMed:11704824, CC PubMed:16193064, PubMed:19188443, PubMed:20545769, PubMed:20625391, CC PubMed:22017874, PubMed:22406621, PubMed:24962073, PubMed:30898438, CC PubMed:31439799). Regulates numerous cellular processes, such as cell CC cycle progression, apoptosis and transcription, as well as viral CC infection (PubMed:12631575, PubMed:19387552, PubMed:19387551). May act CC as a regulatory node which integrates and coordinates numerous signals CC leading to an appropriate cellular response (PubMed:12631575, CC PubMed:19387552, PubMed:19387551). During mitosis, functions as a CC component of the p53/TP53-dependent spindle assembly checkpoint (SAC) CC that maintains cyclin-B-CDK1 activity and G2 arrest in response to CC spindle damage (PubMed:11704824, PubMed:19188443). Also required for CC p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 CC following UV irradiation (PubMed:11239457). Phosphorylates a number of CC DNA repair proteins in response to DNA damage, such as MDC1, RAD9A, CC RAD51 and HTATSF1, promoting their recruitment to DNA damage sites CC (PubMed:20545769, PubMed:21482717, PubMed:22325354, PubMed:26811421, CC PubMed:30898438, PubMed:35597237). Can also negatively regulate CC apoptosis (PubMed:16193064, PubMed:22184066). Phosphorylates the CC caspases CASP9 and CASP2 and the apoptotic regulator NOL3 CC (PubMed:16193064). Phosphorylation protects CASP9 from cleavage and CC activation by CASP8, and inhibits the dimerization of CASP2 and CC activation of CASP8 (PubMed:16193064). Phosphorylates YY1, protecting CC YY1 from cleavage by CASP7 during apoptosis (PubMed:22184066). CC Regulates transcription by direct phosphorylation of RNA polymerases I, CC II, III and IV (PubMed:19387550, PubMed:12631575, PubMed:19387552, CC PubMed:19387551, PubMed:23123191). Also phosphorylates and regulates CC numerous transcription factors including NF-kappa-B, STAT1, CREB1, CC IRF1, IRF2, ATF1, ATF4, SRF, MAX, JUN, FOS, MYC and MYB CC (PubMed:19387550, PubMed:12631575, PubMed:19387552, PubMed:19387551, CC PubMed:23123191). Phosphorylates Hsp90 and its co-chaperones FKBP4 and CC CDC37, which is essential for chaperone function (PubMed:19387550). CC Mediates sequential phosphorylation of FNIP1, promoting its gradual CC interaction with Hsp90, leading to activate both kinase and non-kinase CC client proteins of Hsp90 (PubMed:30699359). Regulates Wnt signaling by CC phosphorylating CTNNB1 and the transcription factor LEF1 CC (PubMed:19387549). Acts as an ectokinase that phosphorylates several CC extracellular proteins (PubMed:19387550, PubMed:12631575, CC PubMed:19387552, PubMed:19387551). During viral infection, CC phosphorylates various proteins involved in the viral life cycles of CC EBV, HSV, HBV, HCV, HIV, CMV and HPV (PubMed:19387550, PubMed:12631575, CC PubMed:19387552, PubMed:19387551). Phosphorylates PML at 'Ser-565' and CC primes it for ubiquitin-mediated degradation (PubMed:20625391, CC PubMed:22406621). Plays an important role in the circadian clock CC function by phosphorylating BMAL1 at 'Ser-90' which is pivotal for its CC interaction with CLOCK and which controls CLOCK nuclear entry (By CC similarity). Phosphorylates CCAR2 at 'Thr-454' in gastric carcinoma CC tissue (PubMed:24962073). Phosphorylates FMR1, promoting FMR1-dependent CC formation of a membraneless compartment (PubMed:30765518, CC PubMed:31439799). {ECO:0000250|UniProtKB:P19139, CC ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:11704824, CC ECO:0000269|PubMed:16193064, ECO:0000269|PubMed:19188443, CC ECO:0000269|PubMed:20545769, ECO:0000269|PubMed:20625391, CC ECO:0000269|PubMed:21482717, ECO:0000269|PubMed:22017874, CC ECO:0000269|PubMed:22184066, ECO:0000269|PubMed:22325354, CC ECO:0000269|PubMed:22406621, ECO:0000269|PubMed:23123191, CC ECO:0000269|PubMed:24962073, ECO:0000269|PubMed:26811421, CC ECO:0000269|PubMed:30699359, ECO:0000269|PubMed:30765518, CC ECO:0000269|PubMed:30898438, ECO:0000269|PubMed:31439799, CC ECO:0000269|PubMed:35597237, ECO:0000303|PubMed:12631575, CC ECO:0000303|PubMed:19387549, ECO:0000303|PubMed:19387550, CC ECO:0000303|PubMed:19387551, ECO:0000303|PubMed:19387552}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC Evidence={ECO:0000269|PubMed:20545769, ECO:0000269|PubMed:20625391, CC ECO:0000269|PubMed:21482717, ECO:0000269|PubMed:22017874, CC ECO:0000269|PubMed:22184066, ECO:0000269|PubMed:23123191, CC ECO:0000269|PubMed:30699359, ECO:0000269|PubMed:30898438, CC ECO:0000269|PubMed:31439799}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000269|PubMed:20545769, ECO:0000269|PubMed:21482717, CC ECO:0000269|PubMed:23123191, ECO:0000269|PubMed:30699359, CC ECO:0000269|PubMed:30898438, ECO:0000269|PubMed:31439799, CC ECO:0000269|PubMed:35597237}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:20625391, CC ECO:0000269|PubMed:22325354, ECO:0000269|PubMed:31439799}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; CC Evidence={ECO:0000269|PubMed:31439799}; CC -!- ACTIVITY REGULATION: Constitutively active protein kinase whose CC activity is not directly affected by phosphorylation. Seems to be CC regulated by level of expression and localization. CC -!- SUBUNIT: Heterotetramer composed of two catalytic subunits (alpha chain CC and/or alpha' chain) and two regulatory subunits (beta chains). The CC tetramer can exist as a combination of 2 alpha/2 beta, 2 alpha'/2 beta CC or 1 alpha/1 alpha'/2 beta subunits. Also part of a CK2-SPT16-SSRP1 CC complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, which CC forms following UV irradiation. Interacts with RNPS1. Interacts with CC SNAI1. Interacts with PML (isoform PML-12). Interacts with CCAR2. CC {ECO:0000269|PubMed:11092945, ECO:0000269|PubMed:11239457, CC ECO:0000269|PubMed:11574463, ECO:0000269|PubMed:12393879, CC ECO:0000269|PubMed:15684395, ECO:0000269|PubMed:19923321, CC ECO:0000269|PubMed:20625391, ECO:0000269|PubMed:22406621, CC ECO:0000269|PubMed:24962073}. CC -!- INTERACTION: CC P68400; P78563: ADARB1; NbExp=3; IntAct=EBI-347804, EBI-2967304; CC P68400; P05067: APP; NbExp=3; IntAct=EBI-347804, EBI-77613; CC P68400; Q86V38: ATN1; NbExp=6; IntAct=EBI-347804, EBI-11954292; CC P68400; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-347804, EBI-10181188; CC P68400; P35226: BMI1; NbExp=2; IntAct=EBI-347804, EBI-2341576; CC P68400; O00257-3: CBX4; NbExp=2; IntAct=EBI-347804, EBI-4392727; CC P68400; Q8IYX3: CCDC116; NbExp=3; IntAct=EBI-347804, EBI-744311; CC P68400; P68400: CSNK2A1; NbExp=4; IntAct=EBI-347804, EBI-347804; CC P68400; P19784: CSNK2A2; NbExp=10; IntAct=EBI-347804, EBI-347451; CC P68400; P67870: CSNK2B; NbExp=27; IntAct=EBI-347804, EBI-348169; CC P68400; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-347804, EBI-12051833; CC P68400; Q9GZR7: DDX24; NbExp=2; IntAct=EBI-347804, EBI-713081; CC P68400; P35659: DEK; NbExp=2; IntAct=EBI-347804, EBI-301977; CC P68400; Q92997: DVL3; NbExp=4; IntAct=EBI-347804, EBI-739789; CC P68400; O75822: EIF3J; NbExp=3; IntAct=EBI-347804, EBI-366647; CC P68400; Q8N9E0: FAM133A; NbExp=5; IntAct=EBI-347804, EBI-10268158; CC P68400; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-347804, EBI-11977403; CC P68400; Q9NW75-2: GPATCH2; NbExp=3; IntAct=EBI-347804, EBI-12068108; CC P68400; Q9NWQ4-1: GPATCH2L; NbExp=6; IntAct=EBI-347804, EBI-11959863; CC P68400; O15499: GSC2; NbExp=3; IntAct=EBI-347804, EBI-19954058; CC P68400; Q13547: HDAC1; NbExp=3; IntAct=EBI-347804, EBI-301834; CC P68400; P09017: HOXC4; NbExp=3; IntAct=EBI-347804, EBI-3923226; CC P68400; A0A0C4DFT8: JADE2; NbExp=3; IntAct=EBI-347804, EBI-12094820; CC P68400; Q14145: KEAP1; NbExp=3; IntAct=EBI-347804, EBI-751001; CC P68400; Q5T7B8-2: KIF24; NbExp=3; IntAct=EBI-347804, EBI-10213781; CC P68400; O60282: KIF5C; NbExp=4; IntAct=EBI-347804, EBI-717170; CC P68400; Q92876: KLK6; NbExp=3; IntAct=EBI-347804, EBI-2432309; CC P68400; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-347804, EBI-12039345; CC P68400; Q68G74: LHX8; NbExp=3; IntAct=EBI-347804, EBI-8474075; CC P68400; Q9NQ69: LHX9; NbExp=3; IntAct=EBI-347804, EBI-10175218; CC P68400; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-347804, EBI-10178634; CC P68400; P50221: MEOX1; NbExp=3; IntAct=EBI-347804, EBI-2864512; CC P68400; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-347804, EBI-16439278; CC P68400; Q9BU76: MMTAG2; NbExp=4; IntAct=EBI-347804, EBI-742459; CC P68400; P23511: NFYA; NbExp=4; IntAct=EBI-347804, EBI-389739; CC P68400; P23511-2: NFYA; NbExp=3; IntAct=EBI-347804, EBI-11061759; CC P68400; Q02548: PAX5; NbExp=3; IntAct=EBI-347804, EBI-296331; CC P68400; P26367: PAX6; NbExp=5; IntAct=EBI-347804, EBI-747278; CC P68400; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-347804, EBI-2339674; CC P68400; P78356-2: PIP4K2B; NbExp=3; IntAct=EBI-347804, EBI-11532361; CC P68400; P29590: PML; NbExp=2; IntAct=EBI-347804, EBI-295890; CC P68400; Q9H307: PNN; NbExp=2; IntAct=EBI-347804, EBI-681904; CC P68400; P78424: POU6F2; NbExp=3; IntAct=EBI-347804, EBI-12029004; CC P68400; O75400-2: PRPF40A; NbExp=2; IntAct=EBI-347804, EBI-5280197; CC P68400; Q14498: RBM39; NbExp=3; IntAct=EBI-347804, EBI-395290; CC P68400; Q04864-2: REL; NbExp=3; IntAct=EBI-347804, EBI-10829018; CC P68400; Q6ZNA4: RNF111; NbExp=6; IntAct=EBI-347804, EBI-2129175; CC P68400; Q99496: RNF2; NbExp=4; IntAct=EBI-347804, EBI-722416; CC P68400; Q96EB6: SIRT1; NbExp=5; IntAct=EBI-347804, EBI-1802965; CC P68400; Q92504: SLC39A7; NbExp=4; IntAct=EBI-347804, EBI-1051105; CC P68400; O43623: SNAI2; NbExp=3; IntAct=EBI-347804, EBI-9876238; CC P68400; P12931: SRC; NbExp=2; IntAct=EBI-347804, EBI-621482; CC P68400; Q08945: SSRP1; NbExp=3; IntAct=EBI-347804, EBI-353771; CC P68400; Q96MF2: STAC3; NbExp=7; IntAct=EBI-347804, EBI-745680; CC P68400; O75683: SURF6; NbExp=2; IntAct=EBI-347804, EBI-2691252; CC P68400; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-347804, EBI-11139477; CC P68400; Q9NVV9: THAP1; NbExp=7; IntAct=EBI-347804, EBI-741515; CC P68400; Q9Y2W1: THRAP3; NbExp=2; IntAct=EBI-347804, EBI-352039; CC P68400; Q08117-2: TLE5; NbExp=3; IntAct=EBI-347804, EBI-11741437; CC P68400; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-347804, EBI-725997; CC P68400; Q9H2G4: TSPYL2; NbExp=4; IntAct=EBI-347804, EBI-947459; CC P68400; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-347804, EBI-12272076; CC P68400; Q8IYI8: ZNF440; NbExp=3; IntAct=EBI-347804, EBI-726439; CC P68400; Q96NG5: ZNF558; NbExp=3; IntAct=EBI-347804, EBI-373363; CC P68400; Q9BS34: ZNF670; NbExp=3; IntAct=EBI-347804, EBI-745276; CC P68400; Q6NSZ9-2: ZSCAN25; NbExp=3; IntAct=EBI-347804, EBI-14650477; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23123191, CC ECO:0000269|PubMed:24962073}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P68400-1; Sequence=Displayed; CC Name=2; CC IsoId=P68400-2; Sequence=VSP_041925; CC -!- TISSUE SPECIFICITY: Expressed in gastric carcinoma tissue and the CC expression gradually increases with the progression of the carcinoma CC (at protein level). {ECO:0000269|PubMed:24962073}. CC -!- PTM: Phosphorylated at Thr-344, Thr-360, Ser-362 and Ser-370 by CDK1 in CC prophase and metaphase and dephosphorylated during anaphase. CC Phosphorylation does not directly affect casein kinase 2 activity, but CC may contribute to its regulation by forming binding sites for CC interacting proteins and/or targeting it to different compartments. CC {ECO:0000269|PubMed:7592773}. CC -!- DISEASE: Okur-Chung neurodevelopmental syndrome (OCNDS) [MIM:617062]: CC An autosomal dominant neurodevelopmental disorder characterized by CC developmental delay, intellectual disability, behavioral problems, CC hypotonia, speech problems, microcephaly, pachygyria and variable CC dysmorphic features. {ECO:0000269|PubMed:27048600}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Can use both ATP and GTP as phosphoryl donors. CC Phosphorylation by casein kinase 2 has been estimated to represent up CC to one quarter of the eukaryotic phosphoproteome. Casein kinase 2 has CC been found to be increased at protein level and up-regulated at the CC level of enzyme activity in the majority of cancers. However, elevated CC levels of casein kinase 2 are present in certain normal organs such as CC brain and testes. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. CK2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J02853; AAA56821.1; -; mRNA. DR EMBL; M55265; AAA35503.1; -; mRNA. DR EMBL; S53149; ABB72474.1; -; mRNA. DR EMBL; X70251; CAA49758.1; -; Genomic_DNA. DR EMBL; AK302583; BAG63838.1; -; mRNA. DR EMBL; BT019792; AAV38595.1; -; mRNA. DR EMBL; AB451279; BAG70093.1; -; mRNA. DR EMBL; AL049761; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10665.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10666.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10667.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10668.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10669.1; -; Genomic_DNA. DR EMBL; BC011668; AAH11668.1; -; mRNA. DR EMBL; BC053532; AAH53532.1; -; mRNA. DR EMBL; BC071167; AAH71167.1; -; mRNA. DR CCDS; CCDS13003.1; -. [P68400-1] DR CCDS; CCDS13004.1; -. [P68400-2] DR PIR; A30319; A30319. DR RefSeq; NP_001886.1; NM_001895.3. [P68400-1] DR RefSeq; NP_808227.1; NM_177559.2. [P68400-1] DR RefSeq; NP_808228.1; NM_177560.2. [P68400-2] DR PDB; 1JWH; X-ray; 3.10 A; A/B=1-337. DR PDB; 1NA7; X-ray; 2.40 A; A=1-329. DR PDB; 1PJK; X-ray; 2.50 A; A=2-335. DR PDB; 2PVR; X-ray; 1.60 A; A=2-335. DR PDB; 2ZJW; X-ray; 2.40 A; A=1-335. DR PDB; 3AMY; X-ray; 2.30 A; A=1-335. DR PDB; 3AT2; X-ray; 1.60 A; A=1-335. DR PDB; 3AT3; X-ray; 2.60 A; A=1-335. DR PDB; 3AT4; X-ray; 2.20 A; A=1-335. DR PDB; 3AXW; X-ray; 2.50 A; A=1-335. DR PDB; 3BQC; X-ray; 1.50 A; A=1-335. DR PDB; 3C13; X-ray; 1.95 A; A=1-335. DR PDB; 3FWQ; X-ray; 2.30 A; A/B=1-335. DR PDB; 3H30; X-ray; 1.56 A; A/B=1-334. DR PDB; 3JUH; X-ray; 1.66 A; A/B=1-335. DR PDB; 3MB6; X-ray; 1.75 A; A=1-331. DR PDB; 3MB7; X-ray; 1.65 A; A=1-331. DR PDB; 3NGA; X-ray; 2.71 A; A/B=1-333. DR PDB; 3NSZ; X-ray; 1.30 A; A=2-331. DR PDB; 3OWJ; X-ray; 1.85 A; A=1-331. DR PDB; 3OWK; X-ray; 1.80 A; A=1-331. DR PDB; 3OWL; X-ray; 2.10 A; A=1-331. DR PDB; 3PE1; X-ray; 1.60 A; A=1-337. DR PDB; 3PE2; X-ray; 1.90 A; A=1-337. DR PDB; 3PE4; X-ray; 1.95 A; B/D=340-352. DR PDB; 3Q04; X-ray; 1.80 A; A=3-330. DR PDB; 3Q9W; X-ray; 1.70 A; A=1-336. DR PDB; 3Q9X; X-ray; 2.20 A; A/B=1-336. DR PDB; 3Q9Y; X-ray; 1.80 A; A=1-336. DR PDB; 3Q9Z; X-ray; 2.20 A; A/B=1-336. DR PDB; 3QA0; X-ray; 2.50 A; A/B=1-336. DR PDB; 3R0T; X-ray; 1.75 A; A=1-337. DR PDB; 3RPS; X-ray; 2.30 A; A/B=1-335. DR PDB; 3TAX; X-ray; 1.88 A; B/D=340-352. DR PDB; 3U4U; X-ray; 2.20 A; A=1-333. DR PDB; 3U87; X-ray; 2.90 A; A/B=1-325. DR PDB; 3U9C; X-ray; 3.20 A; A/B=1-335. DR PDB; 3W8L; X-ray; 2.40 A; A/B=1-335. DR PDB; 3WAR; X-ray; 1.04 A; A=1-335. DR PDB; 3WIK; X-ray; 2.00 A; A=1-335. DR PDB; 3WIL; X-ray; 2.90 A; A=1-335. DR PDB; 3WOW; X-ray; 2.50 A; A=1-335. DR PDB; 4DGL; X-ray; 3.00 A; C/D=1-335. DR PDB; 4FBX; X-ray; 2.33 A; A=1-335. DR PDB; 4GRB; X-ray; 2.15 A; A=1-333. DR PDB; 4GUB; X-ray; 2.20 A; A=1-333. DR PDB; 4GYW; X-ray; 1.70 A; B/D=340-352. DR PDB; 4GYY; X-ray; 1.85 A; B/D=340-352. DR PDB; 4GZ3; X-ray; 1.90 A; B/D=340-352. DR PDB; 4IB5; X-ray; 2.20 A; A/B/C=1-335. DR PDB; 4KWP; X-ray; 1.25 A; A=1-336. DR PDB; 4MD7; X-ray; 3.10 A; E/F/G/H=1-391. DR PDB; 4MD8; X-ray; 3.30 A; E/F/G/H=1-391. DR PDB; 4MD9; X-ray; 3.50 A; E/F/G/H/K/L/M/P=1-336. DR PDB; 4NH1; X-ray; 3.30 A; A/B=1-335. DR PDB; 4RLL; X-ray; 1.85 A; A=1-335. DR PDB; 4UB7; X-ray; 2.10 A; A=1-335. DR PDB; 4UBA; X-ray; 3.00 A; A/B=1-335. DR PDB; 5B0X; X-ray; 2.30 A; A=1-335. DR PDB; 5CLP; X-ray; 1.68 A; A/B=2-329. DR PDB; 5CQU; X-ray; 2.35 A; A=1-335. DR PDB; 5CQW; X-ray; 2.65 A; A/B=1-335. DR PDB; 5CS6; X-ray; 1.88 A; A/B=2-329. DR PDB; 5CSH; X-ray; 1.59 A; A/B=2-329. DR PDB; 5CSP; X-ray; 1.50 A; A=2-329. DR PDB; 5CSV; X-ray; 1.38 A; A=2-329. DR PDB; 5CT0; X-ray; 2.01 A; A/B=2-329. DR PDB; 5CTP; X-ray; 2.03 A; A/B=2-329. DR PDB; 5CU0; X-ray; 2.18 A; A/B=2-329. DR PDB; 5CU2; X-ray; 1.71 A; A/B=2-329. DR PDB; 5CU3; X-ray; 1.79 A; A/B=2-329. DR PDB; 5CU4; X-ray; 1.56 A; A=2-329. DR PDB; 5CU6; X-ray; 1.36 A; A=2-329. DR PDB; 5CVF; X-ray; 1.63 A; A=2-329. DR PDB; 5CVG; X-ray; 1.25 A; A=2-329. DR PDB; 5CVH; X-ray; 1.85 A; A/B=2-329. DR PDB; 5CX9; X-ray; 1.73 A; A/B=2-329. DR PDB; 5H8B; X-ray; 2.55 A; A/B=1-333. DR PDB; 5H8E; X-ray; 2.15 A; A/B=1-333. DR PDB; 5H8G; X-ray; 2.00 A; A=1-333. DR PDB; 5HGV; X-ray; 2.05 A; B/D=340-352. DR PDB; 5KU8; X-ray; 2.22 A; A/B=2-332. DR PDB; 5KWH; X-ray; 2.12 A; A/B=1-333. DR PDB; 5M44; X-ray; 2.71 A; A=1-335. DR PDB; 5M4C; X-ray; 1.94 A; A=1-335. DR PDB; 5M4F; X-ray; 1.52 A; A=1-335. DR PDB; 5M4I; X-ray; 2.22 A; A=1-335. DR PDB; 5MMF; X-ray; 1.99 A; A/B=2-329. DR PDB; 5MMR; X-ray; 2.00 A; A/B=2-329. DR PDB; 5MO5; X-ray; 2.04 A; A/B=2-329. DR PDB; 5MO6; X-ray; 1.82 A; A/B=2-329. DR PDB; 5MO7; X-ray; 2.15 A; A/B=2-329. DR PDB; 5MO8; X-ray; 1.82 A; A/B=2-329. DR PDB; 5MOD; X-ray; 2.08 A; A/B=2-329. DR PDB; 5MOE; X-ray; 1.89 A; A/B=2-329. DR PDB; 5MOH; X-ray; 1.38 A; A=2-329. DR PDB; 5MOT; X-ray; 2.09 A; A=2-329. DR PDB; 5MOV; X-ray; 2.20 A; A=3-327. DR PDB; 5MOW; X-ray; 1.86 A; A/B=2-329. DR PDB; 5MP8; X-ray; 1.92 A; A/B=2-329. DR PDB; 5MPJ; X-ray; 2.14 A; A/B=2-329. DR PDB; 5N1V; X-ray; 2.52 A; A/B=1-336. DR PDB; 5N9K; X-ray; 1.64 A; A=1-335. DR PDB; 5N9L; X-ray; 1.79 A; A=1-335. DR PDB; 5N9N; X-ray; 1.84 A; A=1-335. DR PDB; 5NQC; X-ray; 2.00 A; A=2-335. DR PDB; 5OMY; X-ray; 1.95 A; A=1-391. DR PDB; 5ONI; X-ray; 2.00 A; A/B=1-391. DR PDB; 5OQU; X-ray; 2.32 A; A/B=2-329. DR PDB; 5ORH; X-ray; 1.75 A; A/B=2-329. DR PDB; 5ORJ; X-ray; 1.99 A; A/B=2-329. DR PDB; 5ORK; X-ray; 2.14 A; A/B=2-329. DR PDB; 5OS7; X-ray; 1.66 A; A/B=2-329. DR PDB; 5OS8; X-ray; 1.55 A; A=2-329. DR PDB; 5OSL; X-ray; 1.95 A; A=2-329. DR PDB; 5OSP; X-ray; 1.91 A; A=2-329. DR PDB; 5OSR; X-ray; 1.57 A; A=2-329. DR PDB; 5OSU; X-ray; 1.63 A; A=2-329. DR PDB; 5OSZ; X-ray; 2.00 A; A=2-329. DR PDB; 5OT5; X-ray; 1.63 A; A/B=2-329. DR PDB; 5OT6; X-ray; 1.94 A; A/B=2-329. DR PDB; 5OTD; X-ray; 1.57 A; A/B=2-329. DR PDB; 5OTH; X-ray; 1.69 A; A/B=2-329. DR PDB; 5OTI; X-ray; 1.59 A; A=2-329. DR PDB; 5OTL; X-ray; 1.57 A; A/B=2-329. DR PDB; 5OTO; X-ray; 1.51 A; A/B=2-329. DR PDB; 5OTP; X-ray; 1.57 A; A/B=2-329. DR PDB; 5OTQ; X-ray; 1.38 A; A=2-329. DR PDB; 5OTR; X-ray; 1.52 A; A=2-329. DR PDB; 5OTS; X-ray; 1.90 A; A=2-329. DR PDB; 5OTY; X-ray; 1.48 A; A=2-329. DR PDB; 5OTZ; X-ray; 1.46 A; A=2-329. DR PDB; 5OUE; X-ray; 2.01 A; A/B=2-329. DR PDB; 5OUL; X-ray; 1.34 A; A=2-329. DR PDB; 5OUM; X-ray; 2.05 A; A/B=2-329. DR PDB; 5OUU; X-ray; 1.81 A; A/B=2-329. DR PDB; 5OWH; X-ray; 2.30 A; A=1-335. DR PDB; 5OWL; X-ray; 2.23 A; A/B=1-335. DR PDB; 5OYF; X-ray; 1.54 A; A=2-329. DR PDB; 5T1H; X-ray; 2.11 A; A/B=1-333. DR PDB; 5VIE; X-ray; 2.60 A; B/D=339-352. DR PDB; 5VIF; X-ray; 2.25 A; B=339-352. DR PDB; 5ZN0; Other; 1.10 A; A=1-329. DR PDB; 5ZN1; X-ray; 1.05 A; A=1-329. DR PDB; 5ZN2; X-ray; 1.20 A; A=1-329. DR PDB; 5ZN3; X-ray; 1.50 A; A=1-329. DR PDB; 5ZN4; X-ray; 1.65 A; A=1-329. DR PDB; 5ZN5; X-ray; 1.70 A; A=1-329. DR PDB; 6A1C; X-ray; 1.68 A; A=1-335. DR PDB; 6E37; X-ray; 2.53 A; B=339-352. DR PDB; 6EHK; X-ray; 1.40 A; A=2-329. DR PDB; 6EHU; X-ray; 1.95 A; A/B=2-329. DR PDB; 6EII; X-ray; 1.94 A; A/B=2-329. DR PDB; 6FVF; X-ray; 1.47 A; A=2-329. DR PDB; 6FVG; X-ray; 1.60 A; A=2-329. DR PDB; 6GIH; X-ray; 1.96 A; A=2-329. DR PDB; 6GMD; X-ray; 1.66 A; A/B=2-329. DR PDB; 6HBN; X-ray; 1.59 A; A/B=1-335. DR PDB; 6HME; X-ray; 1.85 A; A/B=1-335. DR PDB; 6HNW; X-ray; 2.00 A; A=1-336. DR PDB; 6HNY; X-ray; 1.65 A; A=1-336. DR PDB; 6HOP; X-ray; 1.55 A; A=1-336. DR PDB; 6HOQ; X-ray; 1.55 A; A=1-336. DR PDB; 6HOR; X-ray; 1.80 A; A=1-336. DR PDB; 6HOT; X-ray; 1.50 A; A=1-336. DR PDB; 6HOU; X-ray; 1.80 A; A=1-336. DR PDB; 6JWA; X-ray; 1.78 A; A=1-335. DR PDB; 6L1Z; X-ray; 1.91 A; A=1-335. DR PDB; 6L21; X-ray; 2.05 A; A=1-335. DR PDB; 6L22; X-ray; 2.12 A; A=1-335. DR PDB; 6L23; X-ray; 1.97 A; A=1-335. DR PDB; 6L24; X-ray; 2.40 A; A=1-335. DR PDB; 6Q38; X-ray; 1.74 A; A=3-329. DR PDB; 6Q4Q; X-ray; 1.45 A; A/B=3-329. DR PDB; 6QY7; X-ray; 2.10 A; A/B=1-337. DR PDB; 6RB1; X-ray; 1.50 A; A=1-336. DR PDB; 6RCB; X-ray; 2.05 A; A=1-336. DR PDB; 6RCM; X-ray; 1.70 A; A=1-336. DR PDB; 6RFE; X-ray; 1.54 A; A=1-336. DR PDB; 6RFF; X-ray; 1.80 A; A=1-336. DR PDB; 6SPW; X-ray; 1.60 A; A=1-391. DR PDB; 6SPX; X-ray; 1.99 A; A=1-335. DR PDB; 6TEI; X-ray; 1.76 A; A/B=1-335. DR PDB; 6TLL; X-ray; 1.88 A; A=1-391. DR PDB; 6TLO; X-ray; 1.69 A; A=1-391. DR PDB; 6TLP; X-ray; 1.93 A; A=1-391. DR PDB; 6TLR; X-ray; 1.64 A; A=1-391. DR PDB; 6TLS; X-ray; 1.46 A; A=1-391. DR PDB; 6TLU; X-ray; 1.81 A; AAA=1-391. DR PDB; 6TLV; X-ray; 1.67 A; A=1-391. DR PDB; 6TLW; X-ray; 1.73 A; A=1-391. DR PDB; 6YPG; X-ray; 1.51 A; A=2-329. DR PDB; 6YPH; X-ray; 1.67 A; A/B=2-329. DR PDB; 6YPJ; X-ray; 1.64 A; A=2-329. DR PDB; 6YPK; X-ray; 1.79 A; A=2-329. DR PDB; 6YPN; X-ray; 1.58 A; B=1-329. DR PDB; 6YUL; X-ray; 2.40 A; AAA/GGG=1-391. DR PDB; 6YUM; X-ray; 2.75 A; AAA/GGG=1-391. DR PDB; 6YZH; X-ray; 1.19 A; A=3-329. DR PDB; 6Z19; X-ray; 1.47 A; B=2-329. DR PDB; 6Z83; X-ray; 2.17 A; AAA/BBB=1-337. DR PDB; 6Z84; X-ray; 2.50 A; AAA/BBB=1-337. DR PDB; 7A49; X-ray; 2.03 A; A/B=1-335. DR PDB; 7A4B; X-ray; 2.06 A; A/B=1-335. DR PDB; 7A4C; X-ray; 2.50 A; A/B=1-335. DR PDB; 7A4Q; X-ray; 1.42 A; A=3-329. DR PDB; 7AT5; X-ray; 1.77 A; A/B=1-335. DR PDB; 7AY9; X-ray; 2.25 A; A/B=1-336. DR PDB; 7AYA; X-ray; 2.45 A; A/B=1-336. DR PDB; 7B8H; X-ray; 1.34 A; A=1-335. DR PDB; 7B8I; X-ray; 2.55 A; A/B=1-335. DR PDB; 7BU4; X-ray; 1.70 A; A=1-335. DR PDB; 7L1X; X-ray; 1.80 A; A=2-335. DR PDB; 7PSU; X-ray; 1.77 A; A/B=1-391. DR PDB; 7QGB; X-ray; 2.58 A; A=1-391. DR PDB; 7QGC; X-ray; 2.55 A; A=1-391. DR PDB; 7QGD; X-ray; 2.30 A; A=1-391. DR PDB; 7QGE; X-ray; 2.27 A; A=1-391. DR PDB; 7QUX; X-ray; 1.48 A; A=2-329. DR PDB; 7X4H; X-ray; 1.77 A; A=1-335. DR PDB; 7Z39; X-ray; 1.60 A; A=2-329. DR PDB; 7ZWE; X-ray; 1.47 A; A=3-329. DR PDB; 7ZWG; X-ray; 1.31 A; A=2-329. DR PDB; 7ZY0; X-ray; 1.44 A; A=2-329. DR PDB; 7ZY2; X-ray; 1.51 A; A=2-329. DR PDB; 7ZY5; X-ray; 1.82 A; A/B=2-329. DR PDB; 7ZY8; X-ray; 1.85 A; A/B=2-329. DR PDB; 7ZYD; X-ray; 1.40 A; A=2-329. DR PDB; 7ZYK; X-ray; 1.31 A; A=2-329. DR PDB; 7ZYO; X-ray; 1.58 A; A=2-329. DR PDB; 7ZYR; X-ray; 1.85 A; A=2-329. DR PDB; 8AE7; X-ray; 1.28 A; A=2-329. DR PDB; 8AEC; X-ray; 1.09 A; A=2-329. DR PDB; 8AEK; X-ray; 1.65 A; A=2-329. DR PDB; 8AEM; X-ray; 1.60 A; A=2-329. DR PDB; 8BGC; X-ray; 2.80 A; A/B=1-337. DR PDB; 8P05; X-ray; 2.45 A; A/B=1-337. DR PDB; 8P07; X-ray; 2.40 A; A/B=1-337. DR PDBsum; 1JWH; -. DR PDBsum; 1NA7; -. DR PDBsum; 1PJK; -. DR PDBsum; 2PVR; -. DR PDBsum; 2ZJW; -. DR PDBsum; 3AMY; -. DR PDBsum; 3AT2; -. DR PDBsum; 3AT3; -. DR PDBsum; 3AT4; -. DR PDBsum; 3AXW; -. DR PDBsum; 3BQC; -. DR PDBsum; 3C13; -. DR PDBsum; 3FWQ; -. DR PDBsum; 3H30; -. DR PDBsum; 3JUH; -. DR PDBsum; 3MB6; -. DR PDBsum; 3MB7; -. DR PDBsum; 3NGA; -. DR PDBsum; 3NSZ; -. DR PDBsum; 3OWJ; -. DR PDBsum; 3OWK; -. DR PDBsum; 3OWL; -. DR PDBsum; 3PE1; -. DR PDBsum; 3PE2; -. DR PDBsum; 3PE4; -. DR PDBsum; 3Q04; -. DR PDBsum; 3Q9W; -. DR PDBsum; 3Q9X; -. DR PDBsum; 3Q9Y; -. DR PDBsum; 3Q9Z; -. DR PDBsum; 3QA0; -. DR PDBsum; 3R0T; -. DR PDBsum; 3RPS; -. DR PDBsum; 3TAX; -. DR PDBsum; 3U4U; -. DR PDBsum; 3U87; -. DR PDBsum; 3U9C; -. DR PDBsum; 3W8L; -. DR PDBsum; 3WAR; -. DR PDBsum; 3WIK; -. DR PDBsum; 3WIL; -. DR PDBsum; 3WOW; -. DR PDBsum; 4DGL; -. DR PDBsum; 4FBX; -. DR PDBsum; 4GRB; -. DR PDBsum; 4GUB; -. DR PDBsum; 4GYW; -. DR PDBsum; 4GYY; -. DR PDBsum; 4GZ3; -. DR PDBsum; 4IB5; -. DR PDBsum; 4KWP; -. DR PDBsum; 4MD7; -. DR PDBsum; 4MD8; -. DR PDBsum; 4MD9; -. DR PDBsum; 4NH1; -. DR PDBsum; 4RLL; -. DR PDBsum; 4UB7; -. DR PDBsum; 4UBA; -. DR PDBsum; 5B0X; -. DR PDBsum; 5CLP; -. DR PDBsum; 5CQU; -. DR PDBsum; 5CQW; -. DR PDBsum; 5CS6; -. DR PDBsum; 5CSH; -. DR PDBsum; 5CSP; -. DR PDBsum; 5CSV; -. DR PDBsum; 5CT0; -. DR PDBsum; 5CTP; -. DR PDBsum; 5CU0; -. DR PDBsum; 5CU2; -. DR PDBsum; 5CU3; -. DR PDBsum; 5CU4; -. DR PDBsum; 5CU6; -. DR PDBsum; 5CVF; -. DR PDBsum; 5CVG; -. DR PDBsum; 5CVH; -. DR PDBsum; 5CX9; -. DR PDBsum; 5H8B; -. DR PDBsum; 5H8E; -. DR PDBsum; 5H8G; -. DR PDBsum; 5HGV; -. DR PDBsum; 5KU8; -. DR PDBsum; 5KWH; -. DR PDBsum; 5M44; -. DR PDBsum; 5M4C; -. DR PDBsum; 5M4F; -. DR PDBsum; 5M4I; -. DR PDBsum; 5MMF; -. DR PDBsum; 5MMR; -. DR PDBsum; 5MO5; -. DR PDBsum; 5MO6; -. DR PDBsum; 5MO7; -. DR PDBsum; 5MO8; -. DR PDBsum; 5MOD; -. DR PDBsum; 5MOE; -. DR PDBsum; 5MOH; -. DR PDBsum; 5MOT; -. DR PDBsum; 5MOV; -. DR PDBsum; 5MOW; -. DR PDBsum; 5MP8; -. DR PDBsum; 5MPJ; -. DR PDBsum; 5N1V; -. DR PDBsum; 5N9K; -. DR PDBsum; 5N9L; -. DR PDBsum; 5N9N; -. DR PDBsum; 5NQC; -. DR PDBsum; 5OMY; -. DR PDBsum; 5ONI; -. DR PDBsum; 5OQU; -. DR PDBsum; 5ORH; -. DR PDBsum; 5ORJ; -. DR PDBsum; 5ORK; -. DR PDBsum; 5OS7; -. DR PDBsum; 5OS8; -. DR PDBsum; 5OSL; -. DR PDBsum; 5OSP; -. DR PDBsum; 5OSR; -. DR PDBsum; 5OSU; -. DR PDBsum; 5OSZ; -. DR PDBsum; 5OT5; -. DR PDBsum; 5OT6; -. DR PDBsum; 5OTD; -. DR PDBsum; 5OTH; -. DR PDBsum; 5OTI; -. DR PDBsum; 5OTL; -. DR PDBsum; 5OTO; -. DR PDBsum; 5OTP; -. DR PDBsum; 5OTQ; -. DR PDBsum; 5OTR; -. DR PDBsum; 5OTS; -. DR PDBsum; 5OTY; -. DR PDBsum; 5OTZ; -. DR PDBsum; 5OUE; -. DR PDBsum; 5OUL; -. DR PDBsum; 5OUM; -. DR PDBsum; 5OUU; -. DR PDBsum; 5OWH; -. DR PDBsum; 5OWL; -. DR PDBsum; 5OYF; -. DR PDBsum; 5T1H; -. DR PDBsum; 5VIE; -. DR PDBsum; 5VIF; -. DR PDBsum; 5ZN0; -. DR PDBsum; 5ZN1; -. DR PDBsum; 5ZN2; -. DR PDBsum; 5ZN3; -. DR PDBsum; 5ZN4; -. DR PDBsum; 5ZN5; -. DR PDBsum; 6A1C; -. DR PDBsum; 6E37; -. DR PDBsum; 6EHK; -. DR PDBsum; 6EHU; -. DR PDBsum; 6EII; -. DR PDBsum; 6FVF; -. DR PDBsum; 6FVG; -. DR PDBsum; 6GIH; -. DR PDBsum; 6GMD; -. DR PDBsum; 6HBN; -. DR PDBsum; 6HME; -. DR PDBsum; 6HNW; -. DR PDBsum; 6HNY; -. DR PDBsum; 6HOP; -. DR PDBsum; 6HOQ; -. DR PDBsum; 6HOR; -. DR PDBsum; 6HOT; -. DR PDBsum; 6HOU; -. DR PDBsum; 6JWA; -. DR PDBsum; 6L1Z; -. DR PDBsum; 6L21; -. DR PDBsum; 6L22; -. DR PDBsum; 6L23; -. DR PDBsum; 6L24; -. DR PDBsum; 6Q38; -. DR PDBsum; 6Q4Q; -. DR PDBsum; 6QY7; -. DR PDBsum; 6RB1; -. DR PDBsum; 6RCB; -. DR PDBsum; 6RCM; -. DR PDBsum; 6RFE; -. DR PDBsum; 6RFF; -. DR PDBsum; 6SPW; -. DR PDBsum; 6SPX; -. DR PDBsum; 6TEI; -. DR PDBsum; 6TLL; -. DR PDBsum; 6TLO; -. DR PDBsum; 6TLP; -. DR PDBsum; 6TLR; -. DR PDBsum; 6TLS; -. DR PDBsum; 6TLU; -. DR PDBsum; 6TLV; -. DR PDBsum; 6TLW; -. DR PDBsum; 6YPG; -. DR PDBsum; 6YPH; -. DR PDBsum; 6YPJ; -. DR PDBsum; 6YPK; -. DR PDBsum; 6YPN; -. DR PDBsum; 6YUL; -. DR PDBsum; 6YUM; -. DR PDBsum; 6YZH; -. DR PDBsum; 6Z19; -. DR PDBsum; 6Z83; -. DR PDBsum; 6Z84; -. DR PDBsum; 7A49; -. DR PDBsum; 7A4B; -. DR PDBsum; 7A4C; -. DR PDBsum; 7A4Q; -. DR PDBsum; 7AT5; -. DR PDBsum; 7AY9; -. DR PDBsum; 7AYA; -. DR PDBsum; 7B8H; -. DR PDBsum; 7B8I; -. DR PDBsum; 7BU4; -. DR PDBsum; 7L1X; -. DR PDBsum; 7PSU; -. DR PDBsum; 7QGB; -. DR PDBsum; 7QGC; -. DR PDBsum; 7QGD; -. DR PDBsum; 7QGE; -. DR PDBsum; 7QUX; -. DR PDBsum; 7X4H; -. DR PDBsum; 7Z39; -. DR PDBsum; 7ZWE; -. DR PDBsum; 7ZWG; -. DR PDBsum; 7ZY0; -. DR PDBsum; 7ZY2; -. DR PDBsum; 7ZY5; -. DR PDBsum; 7ZY8; -. DR PDBsum; 7ZYD; -. DR PDBsum; 7ZYK; -. DR PDBsum; 7ZYO; -. DR PDBsum; 7ZYR; -. DR PDBsum; 8AE7; -. DR PDBsum; 8AEC; -. DR PDBsum; 8AEK; -. DR PDBsum; 8AEM; -. DR PDBsum; 8BGC; -. DR PDBsum; 8P05; -. DR PDBsum; 8P07; -. DR AlphaFoldDB; P68400; -. DR SASBDB; P68400; -. DR SMR; P68400; -. DR BioGRID; 107841; 898. DR ComplexPortal; CPX-2437; Casein kinase II complex, CSNK2A1-CNSK2A2 variant. DR ComplexPortal; CPX-914; Casein kinase II complex, CSNK2A1 variant. DR CORUM; P68400; -. DR DIP; DIP-32682N; -. DR IntAct; P68400; 410. DR MINT; P68400; -. DR STRING; 9606.ENSP00000217244; -. DR BindingDB; P68400; -. DR ChEMBL; CHEMBL3629; -. DR DrugBank; DB01765; (5-hydroxyindolo[1,2-a]quinazolin-7-yl)acetic acid. DR DrugBank; DB03035; 1,8-Di-Hydroxy-4-Nitro-Anthraquinone. DR DrugBank; DB02170; 1,8-Di-Hydroxy-4-Nitro-Xanthen-9-One. DR DrugBank; DB08338; 19-(cyclopropylamino)-4,6,7,15-tetrahydro-5H-16,1-(azenometheno)-10,14-(metheno)pyrazolo[4,3-o][1,3,9]triazacyclohexadecin-8(9H)-one. DR DrugBank; DB08354; 2-(4-CHLOROBENZYLAMINO)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE. DR DrugBank; DB08360; 2-(4-ETHYLPIPERAZIN-1-YL)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE. DR DrugBank; DB08353; 2-(CYCLOHEXYLMETHYLAMINO)-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE. DR DrugBank; DB07802; 3,8-DIBROMO-7-HYDROXY-4-METHYL-2H-CHROMEN-2-ONE. DR DrugBank; DB08345; 4-(2-(1H-IMIDAZOL-4-YL)ETHYLAMINO)-2-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE. DR DrugBank; DB03924; 5,8-Di-Amino-1,4-Dihydroxy-Anthraquinone. DR DrugBank; DB00171; ATP. DR DrugBank; DB03127; Benzamidine. DR DrugBank; DB08473; Dichlororibofuranosylbenzimidazole. DR DrugBank; DB04719; DIMETHYL-(4,5,6,7-TETRABROMO-1H-BENZOIMIDAZOL-2-YL)-AMINE. DR DrugBank; DB08846; Ellagic acid. DR DrugBank; DB07715; Emodin. DR DrugBank; DB12010; Fostamatinib. DR DrugBank; DB08340; N,N'-DIPHENYLPYRAZOLO[1,5-A][1,3,5]TRIAZINE-2,4-DIAMINE. DR DrugBank; DB08362; N-(3-(8-CYANO-4-(PHENYLAMINO)PYRAZOLO[1,5-A][1,3,5]TRIAZIN-2-YLAMINO)PHENYL)ACETAMIDE. DR DrugBank; DB04721; N1,N2-ETHYLENE-2-METHYLAMINO-4,5,6,7-TETRABROMO-BENZIMIDAZOLE. DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester. DR DrugBank; DB04216; Quercetin. DR DrugBank; DB08660; Quinalizarin. DR DrugBank; DB02709; Resveratrol. DR DrugBank; DB04720; S-METHYL-4,5,6,7-TETRABROMO-BENZIMIDAZOLE. DR DrugBank; DB04462; Tetrabromo-2-Benzotriazole. DR DrugCentral; P68400; -. DR GuidetoPHARMACOLOGY; 1549; -. DR MoonDB; P68400; Predicted. DR GlyCosmos; P68400; 3 sites, 1 glycan. DR GlyGen; P68400; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P68400; -. DR MetOSite; P68400; -. DR PhosphoSitePlus; P68400; -. DR SwissPalm; P68400; -. DR BioMuta; CSNK2A1; -. DR DMDM; 55977123; -. DR EPD; P68400; -. DR jPOST; P68400; -. DR MassIVE; P68400; -. DR MaxQB; P68400; -. DR PaxDb; 9606-ENSP00000217244; -. DR PeptideAtlas; P68400; -. DR ProteomicsDB; 57536; -. [P68400-1] DR ProteomicsDB; 57537; -. [P68400-2] DR Pumba; P68400; -. DR Antibodypedia; 6236; 830 antibodies from 42 providers. DR DNASU; 1457; -. DR Ensembl; ENST00000217244.9; ENSP00000217244.3; ENSG00000101266.19. [P68400-1] DR Ensembl; ENST00000349736.10; ENSP00000339247.6; ENSG00000101266.19. [P68400-2] DR Ensembl; ENST00000400217.7; ENSP00000383076.2; ENSG00000101266.19. [P68400-1] DR Ensembl; ENST00000643660.1; ENSP00000495248.1; ENSG00000101266.19. [P68400-1] DR Ensembl; ENST00000644003.1; ENSP00000495387.1; ENSG00000101266.19. [P68400-2] DR Ensembl; ENST00000645623.1; ENSP00000495998.1; ENSG00000101266.19. [P68400-1] DR Ensembl; ENST00000646305.1; ENSP00000495902.1; ENSG00000101266.19. [P68400-1] DR Ensembl; ENST00000646477.1; ENSP00000495439.1; ENSG00000101266.19. [P68400-2] DR Ensembl; ENST00000646561.1; ENSP00000496569.1; ENSG00000101266.19. [P68400-1] DR Ensembl; ENST00000646814.1; ENSP00000495422.1; ENSG00000101266.19. [P68400-1] DR Ensembl; ENST00000647348.1; ENSP00000495912.1; ENSG00000101266.19. [P68400-1] DR GeneID; 1457; -. DR KEGG; hsa:1457; -. DR MANE-Select; ENST00000217244.9; ENSP00000217244.3; NM_177559.3; NP_808227.1. DR UCSC; uc002wdw.2; human. [P68400-1] DR AGR; HGNC:2457; -. DR CTD; 1457; -. DR DisGeNET; 1457; -. DR GeneCards; CSNK2A1; -. DR GeneReviews; CSNK2A1; -. DR HGNC; HGNC:2457; CSNK2A1. DR HPA; ENSG00000101266; Low tissue specificity. DR MalaCards; CSNK2A1; -. DR MIM; 115440; gene. DR MIM; 617062; phenotype. DR neXtProt; NX_P68400; -. DR OpenTargets; ENSG00000101266; -. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR PharmGKB; PA26957; -. DR VEuPathDB; HostDB:ENSG00000101266; -. DR eggNOG; KOG0668; Eukaryota. DR GeneTree; ENSGT00390000004215; -. DR HOGENOM; CLU_000288_70_4_1; -. DR InParanoid; P68400; -. DR OMA; KSWHSFV; -. DR OrthoDB; 5472858at2759; -. DR PhylomeDB; P68400; -. DR TreeFam; TF300483; -. DR BRENDA; 2.7.11.1; 2681. DR PathwayCommons; P68400; -. DR Reactome; R-HSA-1483191; Synthesis of PC. DR Reactome; R-HSA-201688; WNT mediated activation of DVL. DR Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes. DR Reactome; R-HSA-445144; Signal transduction by L1. DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR Reactome; R-HSA-8934903; Receptor Mediated Mitophagy. DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known. DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity. DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway. DR SignaLink; P68400; -. DR SIGNOR; P68400; -. DR BioGRID-ORCS; 1457; 103 hits in 1169 CRISPR screens. DR ChiTaRS; CSNK2A1; human. DR EvolutionaryTrace; P68400; -. DR GeneWiki; Casein_kinase_2,_alpha_1; -. DR GenomeRNAi; 1457; -. DR Pharos; P68400; Tchem. DR PRO; PR:P68400; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P68400; Protein. DR Bgee; ENSG00000101266; Expressed in cortical plate and 203 other cell types or tissues. DR ExpressionAtlas; P68400; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0016605; C:PML body; IDA:UniProt. DR GO; GO:0005956; C:protein kinase CK2 complex; IDA:CAFA. DR GO; GO:0070822; C:Sin3-type complex; IDA:BHF-UCL. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0051879; F:Hsp90 protein binding; TAS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0016301; F:kinase activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0061077; P:chaperone-mediated protein folding; TAS:UniProtKB. DR GO; GO:0006974; P:DNA damage response; IDA:UniProt. DR GO; GO:0006302; P:double-strand break repair; IDA:UniProtKB. DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; TAS:ARUK-UCL. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB. DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProt. DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IGI:ARUK-UCL. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB. DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:CAFA. DR GO; GO:1905337; P:positive regulation of aggrephagy; IDA:UniProtKB. DR GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB. DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; IDA:UniProt. DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central. DR GO; GO:1905818; P:regulation of chromosome separation; IMP:UniProtKB. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0075342; P:symbiont-mediated disruption of host cell PML body; IDA:UniProt. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR CDD; cd14132; STKc_CK2_alpha; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR045216; CK2_alpha. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24054; CASEIN KINASE II SUBUNIT ALPHA; 1. DR PANTHER; PTHR24054:SF16; CASEIN KINASE II SUBUNIT ALPHA-RELATED; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P68400; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; ATP-binding; KW Biological rhythms; Cell cycle; Disease variant; Intellectual disability; KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transcription; Transcription regulation; KW Transferase; Wnt signaling pathway. FT CHAIN 1..391 FT /note="Casein kinase II subunit alpha" FT /id="PRO_0000085883" FT DOMAIN 39..324 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 36..41 FT /note="Interaction with beta subunit" FT /evidence="ECO:0000250" FT ACT_SITE 156 FT /note="Proton acceptor" FT BINDING 45..53 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 68 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 344 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000269|PubMed:7592773" FT MOD_RES 360 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000269|PubMed:7592773" FT MOD_RES 362 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:7592773" FT MOD_RES 370 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:7592773, FT ECO:0007744|PubMed:18691976" FT VAR_SEQ 1..136 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041925" FT VARIANT 47 FT /note="R -> Q (in OCNDS; dbSNP:rs869312845)" FT /evidence="ECO:0000269|PubMed:27048600" FT /id="VAR_077045" FT VARIANT 50 FT /note="Y -> S (in OCNDS; dbSNP:rs869312849)" FT /evidence="ECO:0000269|PubMed:27048600" FT /id="VAR_077046" FT VARIANT 175 FT /note="D -> G (in OCNDS; dbSNP:rs869312848)" FT /evidence="ECO:0000269|PubMed:27048600" FT /id="VAR_077047" FT VARIANT 198 FT /note="K -> R (in OCNDS; dbSNP:rs869312840)" FT /evidence="ECO:0000269|PubMed:27048600" FT /id="VAR_077048" FT CONFLICT 128 FT /note="L -> F (in Ref. 3; CAA49758)" FT /evidence="ECO:0000305" FT CONFLICT 256 FT /note="D -> G (in Ref. 3; CAA49758)" FT /evidence="ECO:0000305" FT CONFLICT 287 FT /note="S -> R (in Ref. 3; CAA49758)" FT /evidence="ECO:0000305" FT CONFLICT 351 FT /note="M -> V (in Ref. 3; CAA49758)" FT /evidence="ECO:0000305" FT STRAND 10..12 FT /evidence="ECO:0007829|PDB:3WAR" FT TURN 13..18 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 21..24 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:3WAR" FT STRAND 29..32 FT /evidence="ECO:0007829|PDB:6YZH" FT HELIX 36..38 FT /evidence="ECO:0007829|PDB:3WAR" FT STRAND 39..47 FT /evidence="ECO:0007829|PDB:3WAR" FT STRAND 49..58 FT /evidence="ECO:0007829|PDB:3WAR" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:3WAR" FT STRAND 64..70 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:7ZYK" FT HELIX 75..88 FT /evidence="ECO:0007829|PDB:3WAR" FT STRAND 97..102 FT /evidence="ECO:0007829|PDB:3WAR" FT TURN 104..106 FT /evidence="ECO:0007829|PDB:3WAR" FT STRAND 107..114 FT /evidence="ECO:0007829|PDB:3WAR" FT TURN 118..120 FT /evidence="ECO:0007829|PDB:5CVG" FT HELIX 121..124 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 125..127 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 130..149 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 159..161 FT /evidence="ECO:0007829|PDB:3WAR" FT STRAND 162..165 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 166..168 FT /evidence="ECO:0007829|PDB:3WAR" FT STRAND 170..173 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:5ZN2" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 200..203 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 212..227 FT /evidence="ECO:0007829|PDB:3WAR" FT STRAND 230..233 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 238..249 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 251..261 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:3WAR" FT TURN 270..272 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 281..284 FT /evidence="ECO:0007829|PDB:3WAR" FT TURN 287..289 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 290..292 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 295..304 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 315..318 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:3WAR" FT HELIX 325..331 FT /evidence="ECO:0007829|PDB:3WAR" FT STRAND 333..335 FT /evidence="ECO:0007829|PDB:1JWH" SQ SEQUENCE 391 AA; 45144 MW; D3B6F5D13FF7422D CRC64; MSGPVPSRAR VYTDVNTHRP REYWDYESHV VEWGNQDDYQ LVRKLGRGKY SEVFEAINIT NNEKVVVKIL KPVKKKKIKR EIKILENLRG GPNIITLADI VKDPVSRTPA LVFEHVNNTD FKQLYQTLTD YDIRFYMYEI LKALDYCHSM GIMHRDVKPH NVMIDHEHRK LRLIDWGLAE FYHPGQEYNV RVASRYFKGP ELLVDYQMYD YSLDMWSLGC MLASMIFRKE PFFHGHDNYD QLVRIAKVLG TEDLYDYIDK YNIELDPRFN DILGRHSRKR WERFVHSENQ HLVSPEALDF LDKLLRYDHQ SRLTAREAME HPYFYTVVKD QARMGSSSMP GGSTPVSSAN MMSGISSVPT PSPLGPLAGS PVIAAANPLG MPVPAAAGAQ Q //