ID CSK2B_HUMAN Reviewed; 215 AA. AC P67870; B0UXA9; P07312; P13862; Q4VX47; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 28-JAN-2026, entry version 205. DE RecName: Full=Casein kinase II subunit beta; DE Short=CK II beta; DE AltName: Full=Phosvitin; DE AltName: Full=Protein G5a; GN Name=CSNK2B {ECO:0000312|HGNC:HGNC:2460}; Synonyms=CK2N, G5A; 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]. RX PubMed=2666134; DOI=10.1111/j.1432-1033.1989.tb14917.x; RA Jakobi R., Voss H., Pyerin W.; RT "Human phosvitin/casein kinase type II. Molecular cloning and sequencing of RT full-length cDNA encoding subunit beta."; RL Eur. J. Biochem. 183:227-233(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1694965; DOI=10.1016/0921-8777(90)90036-5; RA Teitz T., Eli D., Penner M., Bakhanashvili M., Naiman T., Timme T.L., RA Wood C.M., Moses R.E., Canaani D.; RT "Expression of the cDNA for the beta subunit of human casein kinase II RT confers partial UV resistance on xeroderma pigmentosum cells."; RL Mutat. Res. 236:85-97(1990). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2513884; DOI=10.1021/bi00449a014; RA Heller-Harrison R.A., Meisner H., Czech M.P.; RT "Cloning and characterization of a cDNA encoding the beta subunit of human RT casein kinase II."; RL Biochemistry 28:9053-9058(1989). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1856204; DOI=10.1016/s0021-9258(18)92756-0; RA Voss A., Wirkner U., Jacobi R., Hewitt N., Schwager C., Zimmermann J., RA Ansorge W., Pyerin W.; RT "Structure of the gene encoding human casein kinase II subunit beta."; RL J. Biol. Chem. 266:13706-13711(1991). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=12102635; DOI=10.1021/bi025791r; RA Singh L.S., Kalafatis M.; RT "Sequencing of full-length cDNA encoding the alpha and beta subunits of RT human casein kinase II from human platelets and megakaryocytic cells. RT Expression of the casein kinase IIalpha intronless gene in a megakaryocytic RT cell line."; RL Biochemistry 41:8935-8940(2002). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14656967; DOI=10.1101/gr.1736803; RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., RA Hood L.; RT "Analysis of the gene-dense major histocompatibility complex class III RT region and its comparison to mouse."; RL Genome Res. 13:2621-2636(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Shiina S., Tamiya G., Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [14] RP PHOSPHORYLATION. RX PubMed=2300566; DOI=10.1073/pnas.87.2.821; RA Ackerman P., Glover C.V., Osheroff N.; RT "Stimulation of casein kinase II by epidermal growth factor: relationship RT between the physiological activity of the kinase and the phosphorylation RT state of its beta subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 87:821-825(1990). RN [15] RP INTERACTION WITH CD163. RX PubMed=11298324; RX DOI=10.1002/1521-4141(200104)31:4<999::aid-immu999>3.0.co;2-r; RA Ritter M., Buechler C., Kapinsky M., Schmitz G.; RT "Interaction of CD163 with the regulatory subunit of casein kinase II RT (CKII) and dependence of CD163 signaling on CKII and protein kinase C."; RL Eur. J. Immunol. 31:999-1009(2001). RN [16] 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 [17] RP INTERACTION WITH FGF1. RX PubMed=11964394; DOI=10.1074/jbc.m112193200; RA Skjerpen C.S., Wesche J., Olsnes S.; RT "Identification of ribosome-binding protein p34 as an intracellular protein RT that binds acidic fibroblast growth factor."; RL J. Biol. Chem. 277:23864-23871(2002). RN [18] 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 [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [20] RP FUNCTION IN PHOSPHORYLATION OF MUSK, AND INTERACTION WITH MUSK. RX PubMed=16818610; DOI=10.1101/gad.375206; RA Cheusova T., Khan M.A., Schubert S.W., Gavin A.C., Buchou T., Jacob G., RA Sticht H., Allende J., Boldyreff B., Brenner H.R., Hashemolhosseini S.; RT "Casein kinase 2-dependent serine phosphorylation of MuSK regulates RT acetylcholine receptor aggregation at the neuromuscular junction."; RL Genes Dev. 20:1800-1816(2006). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-69 AND SER-209, AND RP IDENTIFICATION BY 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 [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-209, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [25] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EPSTEIN-BARR VIRUS RP EBNA1 (MICROBIAL INFECTION). RX PubMed=20719947; DOI=10.1128/jvi.01183-10; RA Sivachandran N., Cao J.Y., Frappier L.; RT "Epstein-Barr virus nuclear antigen 1 Hijacks the host kinase CK2 to RT disrupt PML nuclear bodies."; RL J. Virol. 84:11113-11123(2010). RN [26] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-209, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-209, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND SER-209, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [31] RP INTERACTION WITH ARK2N, INTERACTION WITH EPSTEIN-BARR VIRUS EBNA1 RP (MICROBIAL INFECTION), AND MUTAGENESIS OF 147-LYS--ARG-150. RX PubMed=24216761; DOI=10.1128/mcb.00968-13; RA Cao J.Y., Shire K., Landry C., Gish G.D., Pawson T., Frappier L.; RT "Identification of a novel protein interaction motif in the regulatory RT subunit of casein kinase 2."; RL Mol. Cell. Biol. 34:246-258(2014). RN [32] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-212, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [33] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [34] RP INVOLVEMENT IN POBINDS. RX PubMed=28585349; DOI=10.1002/humu.23270; RA Poirier K., Hubert L., Viot G., Rio M., Billuart P., Besmond C., RA Bienvenu T.; RT "CSNK2B splice site mutations in patients cause intellectual disability RT with or without myoclonic epilepsy."; RL Hum. Mutat. 38:932-941(2017). RN [35] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH JUN AND ARKN2, AND RP SUBCELLULAR LOCATION. RX PubMed=31341047; DOI=10.1128/jvi.00989-19; RA Siddiqi U.Z., Vaidya A.S., Li X., Marcon E., Tsao S.W., Greenblatt J., RA Frappier L.; RT "Identification of ARKL1 as a Negative Regulator of Epstein-Barr Virus RT Reactivation."; RL J. Virol. 93:0-0(2019). RN [36] RP INVOLVEMENT IN POBINDS, AND VARIANTS POBINDS 5-GLU--ARG-215 DEL; CYS-86; RP PRO-111; GLY-137; PHE-137 AND ARG-187. RX PubMed=31784560; DOI=10.1038/s41598-019-53484-9; RA Li J., Gao K., Cai S., Liu Y., Wang Y., Huang S., Zha J., Hu W., Yu S., RA Yang Z., Xie H., Yan H., Wang J., Wu Y., Jiang Y.; RT "Germline de novo variants in CSNK2B in Chinese patients with epilepsy."; RL Sci. Rep. 9:17909-17909(2019). RN [37] RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-182, SUBUNIT, AND ZINC-BINDING RP SITES. RX PubMed=10357806; DOI=10.1093/emboj/18.11.2930; RA Chantalat L., Leroy D., Filhol O., Nueda A., Benitez M.J., Chambaz E.M., RA Cochet C., Dideberg O.; RT "Crystal structure of the human protein kinase CK2 regulatory subunit RT reveals its zinc finger-mediated dimerization."; RL EMBO J. 18:2930-2940(1999). RN [38] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CSNK2A1, ZINC-BINDING RP SITES, SUBUNIT, AND PHOSPHORYLATION AT SER-2 AND SER-3. 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). CC -!- FUNCTION: Regulatory subunit of casein kinase II/CK2. As part of the CC kinase complex regulates the basal catalytic activity of the alpha CC subunit a constitutively active serine/threonine-protein kinase that CC phosphorylates a large number of substrates containing acidic residues CC C-terminal to the phosphorylated serine or threonine (PubMed:11239457, CC PubMed:16818610). Participates in Wnt signaling (By similarity). CC {ECO:0000250|UniProtKB:P67871, ECO:0000269|PubMed:11239457, CC ECO:0000269|PubMed:16818610}. CC -!- FUNCTION: (Microbial infection) Upon infection with Epstein-Barr virus CC (EBV), the interaction with viral EBNA1 increases the association of CC CK2 with PML proteins, which increases PML phosphorylation by CK2, CC triggering the polyubiquitylation and degradation of PML CC (PubMed:20719947, PubMed:24216761). Seems to also suppress EBV CC reactivation by mediating ARK2N and JUN at the Z promoter which CC inhibits BZLF1 transcrition (PubMed:31341047). CC {ECO:0000269|PubMed:20719947, ECO:0000269|PubMed:24216761, CC ECO:0000269|PubMed:31341047}. CC -!- SUBUNIT: Casein kinase II/CK2 is a tetramer composed of an alpha CC subunit, an alpha' subunit and two beta subunits. The beta subunit CC dimerization is mediated by zinc ions. Interacts with DYNLT2 (By CC similarity). Interacts with CD163. Also a component of a CK2-SPT16- CC SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, CC the complex associating following UV irradiation. Interacts with MUSK; CC mediates phosphorylation of MUSK by CK2. Interacts with FGF1; this CC interaction is increased in the presence of FIBP, suggesting a possible CC cooperative interaction between CSNKB and FIBP in binding to FGF1. CC Interacts (via KSSR motif) with ARK2N (PubMed:24216761). Interacts with CC JUN and ARK2N; mediates the interaction between ARK2N and JUN CC (PubMed:31341047). {ECO:0000250, ECO:0000269|PubMed:10357806, CC ECO:0000269|PubMed:11239457, ECO:0000269|PubMed:11298324, CC ECO:0000269|PubMed:11574463, ECO:0000269|PubMed:11964394, CC ECO:0000269|PubMed:12393879, ECO:0000269|PubMed:16818610, CC ECO:0000269|PubMed:24216761, ECO:0000269|PubMed:31341047}. CC -!- SUBUNIT: (Microbial infection) Interacts (via KSSR motif) with Epstein- CC Barr virus EBNA1; the interaction requires phosphorylation of EBNA1, is CC independent and simultaneous to EBNA1 interaction with USP7 as well as CC necessary for PML nuclear bodies disruption by EBNA1. EBNA1, USP7 and CC CSNK2B form a ternary complex. {ECO:0000269|PubMed:24216761}. CC -!- INTERACTION: CC P67870; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-348169, EBI-11524452; CC P67870; O00555: CACNA1A; NbExp=2; IntAct=EBI-348169, EBI-766279; CC P67870; O00257-3: CBX4; NbExp=2; IntAct=EBI-348169, EBI-4392727; CC P67870; P07199: CENPB; NbExp=3; IntAct=EBI-348169, EBI-949451; CC P67870; O14757: CHEK1; NbExp=3; IntAct=EBI-348169, EBI-974488; CC P67870; P68400: CSNK2A1; NbExp=34; IntAct=EBI-348169, EBI-347804; CC P67870; P19784: CSNK2A2; NbExp=19; IntAct=EBI-348169, EBI-347451; CC P67870; P67870: CSNK2B; NbExp=7; IntAct=EBI-348169, EBI-348169; CC P67870; P01037: CST1; NbExp=3; IntAct=EBI-348169, EBI-1056240; CC P67870; Q9NVL1-2: FAM86C1P; NbExp=3; IntAct=EBI-348169, EBI-12845222; CC P67870; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-348169, EBI-7251368; CC P67870; P09067: HOXB5; NbExp=3; IntAct=EBI-348169, EBI-3893317; CC P67870; Q9C086: INO80B; NbExp=3; IntAct=EBI-348169, EBI-715611; CC P67870; Q96EZ8: MCRS1; NbExp=2; IntAct=EBI-348169, EBI-348259; CC P67870; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-348169, EBI-14086479; CC P67870; Q8NEJ9: NGDN; NbExp=3; IntAct=EBI-348169, EBI-9995414; CC P67870; O60551: NMT2; NbExp=3; IntAct=EBI-348169, EBI-3920273; CC P67870; Q16656-4: NRF1; NbExp=3; IntAct=EBI-348169, EBI-11742836; CC P67870; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-348169, EBI-741158; CC P67870; Q6VY07: PACS1; NbExp=3; IntAct=EBI-348169, EBI-2555014; CC P67870; Q9P1Y6: PHRF1; NbExp=4; IntAct=EBI-348169, EBI-3937171; CC P67870; Q9BSJ6: PIMREG; NbExp=3; IntAct=EBI-348169, EBI-2568609; CC P67870; Q9NZH5-2: PTTG2; NbExp=3; IntAct=EBI-348169, EBI-17630019; CC P67870; Q14498: RBM39; NbExp=4; IntAct=EBI-348169, EBI-395290; CC P67870; Q99496: RNF2; NbExp=6; IntAct=EBI-348169, EBI-722416; CC P67870; Q15287: RNPS1; NbExp=2; IntAct=EBI-348169, EBI-395959; CC P67870; Q15349: RPS6KA2; NbExp=4; IntAct=EBI-348169, EBI-1384149; CC P67870; P51812: RPS6KA3; NbExp=8; IntAct=EBI-348169, EBI-1046616; CC P67870; O75582: RPS6KA5; NbExp=3; IntAct=EBI-348169, EBI-73869; CC P67870; Q8WU57: SELI; NbExp=3; IntAct=EBI-348169, EBI-751012; CC P67870; Q96EB6: SIRT1; NbExp=5; IntAct=EBI-348169, EBI-1802965; CC P67870; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-348169, EBI-11952651; CC P67870; O43711: TLX3; NbExp=3; IntAct=EBI-348169, EBI-3939165; CC P67870; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-348169, EBI-2130429; CC P67870; Q12792: TWF1; NbExp=3; IntAct=EBI-348169, EBI-1056675; CC P67870; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-348169, EBI-12040603; CC P67870; P17023: ZNF19; NbExp=3; IntAct=EBI-348169, EBI-12884200; CC P67870; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-348169, EBI-11741890; CC P67870; Q9WTL8: Bmal1; Xeno; NbExp=4; IntAct=EBI-348169, EBI-644534; CC P67870; Q9JK25: Clip1; Xeno; NbExp=2; IntAct=EBI-348169, EBI-908338; CC P67870; O08785: Clock; Xeno; NbExp=2; IntAct=EBI-348169, EBI-79859; CC P67870; P97784: Cry1; Xeno; NbExp=2; IntAct=EBI-348169, EBI-1266607; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31341047}. CC -!- DOMAIN: The KSSR motif is part of a protein interaction pocket that CC mediates interaction with cellular and viral proteins. CC {ECO:0000269|PubMed:24216761}. CC -!- PTM: Phosphorylated by alpha subunit. {ECO:0000269|PubMed:11574463, CC ECO:0000269|PubMed:2300566}. CC -!- DISEASE: Poirier-Bienvenu neurodevelopmental syndrome (POBINDS) CC [MIM:618732]: An autosomal dominant neurodevelopmental disorder CC characterized by onset of seizures in infancy, developmental delay, CC impaired intellectual development, and poor or absent speech. CC {ECO:0000269|PubMed:28585349, ECO:0000269|PubMed:31784560}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family. CC {ECO:0000305}. 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; X16937; CAA34811.1; -; mRNA. DR EMBL; X16312; CAA34379.1; -; mRNA. DR EMBL; M30448; AAA52123.1; -; mRNA. DR EMBL; X57152; CAA40442.1; -; Genomic_DNA. DR EMBL; AY113186; AAM50092.1; -; mRNA. DR EMBL; CR541699; CAG46500.1; -; mRNA. DR EMBL; AF129756; AAD18081.1; -; Genomic_DNA. DR EMBL; BA000025; BAB63386.1; -; Genomic_DNA. DR EMBL; DQ314868; ABC40727.1; -; Genomic_DNA. DR EMBL; AK311860; BAG34801.1; -; mRNA. DR EMBL; AL662899; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL670886; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL805934; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX511262; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR354443; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753842; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759761; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03473.1; -; Genomic_DNA. DR EMBL; BC112017; AAI12018.1; -; mRNA. DR EMBL; BC112019; AAI12020.1; -; mRNA. DR CCDS; CCDS4712.1; -. DR PIR; A39459; A39459. DR RefSeq; NP_001269314.1; NM_001282385.1. DR RefSeq; NP_001311.3; NM_001320.6. DR PDB; 1DS5; X-ray; 3.16 A; E/F/G/H=181-203. DR PDB; 1JWH; X-ray; 3.10 A; C/D=1-215. DR PDB; 1QF8; X-ray; 1.74 A; A/B=1-182. DR PDB; 3EED; X-ray; 2.80 A; A/B=1-193. DR PDB; 4DGL; X-ray; 3.00 A; A/B=1-215. DR PDB; 4MD7; X-ray; 3.10 A; A/B/C/D=1-215. DR PDB; 4MD8; X-ray; 3.30 A; A/B/C/D=1-215. DR PDB; 4MD9; X-ray; 3.50 A; A/B/C/D/I/J/N/O=1-215. DR PDB; 4NH1; X-ray; 3.30 A; C/D=1-215. DR PDB; 6Q38; X-ray; 1.74 A; C=186-193. DR PDBsum; 1DS5; -. DR PDBsum; 1JWH; -. DR PDBsum; 1QF8; -. DR PDBsum; 3EED; -. DR PDBsum; 4DGL; -. DR PDBsum; 4MD7; -. DR PDBsum; 4MD8; -. DR PDBsum; 4MD9; -. DR PDBsum; 4NH1; -. DR PDBsum; 6Q38; -. DR AlphaFoldDB; P67870; -. DR SMR; P67870; -. DR BioGRID; 107843; 631. DR ComplexPortal; CPX-2428; Casein kinase II complex, CSNK2A2 variant. DR ComplexPortal; CPX-2437; Casein kinase II complex, CSNK2A1-CNSK2A2 variant. DR ComplexPortal; CPX-914; Casein kinase II complex, CSNK2A1 variant. DR CORUM; P67870; -. DR DIP; DIP-131N; -. DR FunCoup; P67870; 3553. DR IntAct; P67870; 511. DR MINT; P67870; -. DR STRING; 9606.ENSP00000365042; -. DR BindingDB; P67870; -. DR ChEMBL; CHEMBL2358; -. DR DrugBank; DB00171; ATP. DR DrugBank; DB04216; Quercetin. DR MoonDB; P67870; Predicted. DR GlyGen; P67870; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P67870; -. DR MetOSite; P67870; -. DR PhosphoSitePlus; P67870; -. DR SwissPalm; P67870; -. DR BioMuta; CSNK2B; -. DR DMDM; 54037520; -. DR jPOST; P67870; -. DR MassIVE; P67870; -. DR PaxDb; 9606-ENSP00000365042; -. DR PeptideAtlas; P67870; -. DR ProteomicsDB; 57524; -. DR Pumba; P67870; -. DR Antibodypedia; 1045; 625 antibodies from 41 providers. DR DNASU; 1460; -. DR Ensembl; ENST00000375865.6; ENSP00000365025.2; ENSG00000204435.15. DR Ensembl; ENST00000375866.2; ENSP00000365026.2; ENSG00000204435.15. DR Ensembl; ENST00000375882.7; ENSP00000365042.3; ENSG00000204435.15. DR Ensembl; ENST00000383427.6; ENSP00000372919.2; ENSG00000206406.9. DR Ensembl; ENST00000383433.8; ENSP00000372925.4; ENSG00000206406.9. DR Ensembl; ENST00000400110.5; ENSP00000382980.1; ENSG00000206406.9. DR Ensembl; ENST00000412802.5; ENSP00000413469.1; ENSG00000224774.7. DR Ensembl; ENST00000418230.5; ENSP00000411322.1; ENSG00000228875.8. DR Ensembl; ENST00000422567.6; ENSP00000407018.2; ENSG00000224398.7. DR Ensembl; ENST00000429633.5; ENSP00000409510.1; ENSG00000230700.11. DR Ensembl; ENST00000431476.5; ENSP00000394855.1; ENSG00000224398.7. DR Ensembl; ENST00000436169.5; ENSP00000412520.1; ENSG00000224398.7. DR Ensembl; ENST00000443673.6; ENSP00000400188.2; ENSG00000230700.11. DR Ensembl; ENST00000448596.1; ENSP00000391038.1; ENSG00000232960.12. DR Ensembl; ENST00000451917.6; ENSP00000415303.2; ENSG00000224774.7. DR Ensembl; ENST00000452985.6; ENSP00000415237.2; ENSG00000228875.8. DR Ensembl; ENST00000453234.5; ENSP00000395275.1; ENSG00000224774.7. DR Ensembl; ENST00000454382.6; ENSP00000390900.2; ENSG00000232960.12. DR Ensembl; ENST00000454511.5; ENSP00000393756.1; ENSG00000232960.12. DR Ensembl; ENST00000455161.1; ENSP00000407379.1; ENSG00000230700.11. DR Ensembl; ENST00000458330.5; ENSP00000410802.1; ENSG00000228875.8. DR GeneID; 1460; -. DR KEGG; hsa:1460; -. DR MANE-Select; ENST00000375882.7; ENSP00000365042.3; NM_001320.7; NP_001311.3. DR UCSC; uc003nvr.3; human. DR AGR; HGNC:2460; -. DR ClinPGx; PA26960; -. DR CTD; 1460; -. DR DisGeNET; 1460; -. DR GeneCards; CSNK2B; -. DR GeneReviews; CSNK2B; -. DR HGNC; HGNC:2460; CSNK2B. DR HPA; ENSG00000204435; Low tissue specificity. DR MalaCards; CSNK2B; -. DR MIM; 115441; gene. DR MIM; 618732; phenotype. DR OpenTargets; ENSG00000204435; -. DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability. DR Orphanet; 689397; Poirier-Bienvenu neurodevelopmental syndrome. DR VEuPathDB; HostDB:ENSG00000204435; -. DR eggNOG; KOG3092; Eukaryota. DR GeneTree; ENSGT00390000003781; -. DR HOGENOM; CLU_034027_3_3_1; -. DR InParanoid; P67870; -. DR OrthoDB; 3971593at2759; -. DR PAN-GO; P67870; 4 GO annotations based on evolutionary models. DR PhylomeDB; P67870; -. DR PathwayCommons; P67870; -. 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-6798695; Neutrophil degranulation. 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 Reactome; R-HSA-9768727; Regulation of CDH1 posttranslational processing and trafficking to plasma membrane. DR Reactome; R-HSA-9828806; Maturation of hRSV A proteins. DR Reactome; R-HSA-9931529; Phosphorylation and nuclear translocation of BMAL1 (ARNTL) and CLOCK. DR Reactome; R-HSA-9931530; Phosphorylation and nuclear translocation of the CRY:PER:kinase complex. DR SignaLink; P67870; -. DR SIGNOR; P67870; -. DR Agora; ENSG00000204435; -. DR BioGRID-ORCS; 1460; 737 hits in 1197 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR ChiTaRS; CSNK2B; human. DR EvolutionaryTrace; P67870; -. DR GeneWiki; CSNK2B; -. DR GenomeRNAi; 1460; -. DR Pharos; P67870; Tbio. DR PRO; PR:P67870; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P67870; protein. DR Bgee; ENSG00000204435; Expressed in left testis and 95 other cell types or tissues. DR ExpressionAtlas; P67870; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:UniProt. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0033011; C:perinuclear theca; IDA:HPA. DR GO; GO:0016605; C:PML body; IDA:UniProt. DR GO; GO:0005956; C:protein kinase CK2 complex; IDA:CAFA. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:0120238; C:sperm glycocalyx; IDA:HPA. DR GO; GO:0097225; C:sperm midpiece; IDA:HPA. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:CAFA. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProt. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL. DR GO; GO:0033211; P:adiponectin-activated signaling pathway; IDA:BHF-UCL. DR GO; GO:0061154; P:endothelial tube morphogenesis; IMP:BHF-UCL. DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL. DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:BHF-UCL. DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:ARUK-UCL. DR GO; GO:1903901; P:negative regulation of viral life cycle; IDA:UniProt. DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IDA:BHF-UCL. DR GO; GO:0065003; P:protein-containing complex assembly; NAS:BHF-UCL. DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB. 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 FunFam; 1.10.1820.10:FF:000001; Casein kinase II subunit beta; 1. DR FunFam; 2.20.25.20:FF:000002; Casein kinase II subunit beta; 1. DR Gene3D; 2.20.25.20; -; 1. DR Gene3D; 1.10.1820.10; protein kinase ck2 holoenzyme, chain C, domain 1; 1. DR InterPro; IPR016149; Casein_kin_II_reg-sub_N. DR InterPro; IPR035991; Casein_kinase_II_beta-like. DR InterPro; IPR000704; Casein_kinase_II_reg-sub. DR PANTHER; PTHR11740; CASEIN KINASE II SUBUNIT BETA; 1. DR PANTHER; PTHR11740:SF0; CASEIN KINASE II SUBUNIT BETA; 1. DR Pfam; PF01214; CK_II_beta; 1. DR PRINTS; PR00472; CASNKINASEII. DR SMART; SM01085; CK_II_beta; 1. DR SUPFAM; SSF57798; Casein kinase II beta subunit; 1. DR PROSITE; PS01101; CK2_BETA; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Disease variant; Epilepsy; KW Intellectual disability; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; KW Ubl conjugation; Wnt signaling pathway; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT CHAIN 2..215 FT /note="Casein kinase II subunit beta" FT /id="PRO_0000068236" FT REGION 188..193 FT /note="Interaction with alpha subunit" FT /evidence="ECO:0000250" FT MOTIF 147..150 FT /note="KSSR motif" FT /evidence="ECO:0000269|PubMed:24216761" FT BINDING 109 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 114 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 137 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:19369195, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 2 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:11574463" FT MOD_RES 3 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000269|PubMed:11574463" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 37 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 69 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 212 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 212 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25755297" FT VARIANT 5..215 FT /note="Missing (in POBINDS; associated in cis with C-86)" FT /evidence="ECO:0000269|PubMed:31784560" FT /id="VAR_083650" FT VARIANT 86 FT /note="R -> C (in POBINDS; uncertain significance; FT associated in cis with 5-E--R-215 del)" FT /evidence="ECO:0000269|PubMed:31784560" FT /id="VAR_083651" FT VARIANT 111 FT /note="R -> P (in POBINDS)" FT /evidence="ECO:0000269|PubMed:31784560" FT /id="VAR_083652" FT VARIANT 137 FT /note="C -> F (in POBINDS)" FT /evidence="ECO:0000269|PubMed:31784560" FT /id="VAR_083653" FT VARIANT 137 FT /note="C -> G (in POBINDS)" FT /evidence="ECO:0000269|PubMed:31784560" FT /id="VAR_083654" FT VARIANT 187 FT /note="L -> R (in POBINDS)" FT /evidence="ECO:0000269|PubMed:31784560" FT /id="VAR_083655" FT MUTAGEN 147..150 FT /note="KSSR->AAAA: No effect on interaction alpha subunit FT CSNK2A1. Loss on interaction with ARK2N and Epstein-Barr FT virus EBNA1." FT /evidence="ECO:0000269|PubMed:24216761" FT CONFLICT 194 FT /note="P -> A (in Ref. 3; AAA52123)" FT /evidence="ECO:0000305" FT HELIX 9..15 FT /evidence="ECO:0007829|PDB:1QF8" FT TURN 17..20 FT /evidence="ECO:0007829|PDB:1JWH" FT HELIX 27..31 FT /evidence="ECO:0007829|PDB:1QF8" FT HELIX 33..36 FT /evidence="ECO:0007829|PDB:1QF8" FT HELIX 39..41 FT /evidence="ECO:0007829|PDB:1QF8" FT STRAND 43..45 FT /evidence="ECO:0007829|PDB:4DGL" FT HELIX 46..53 FT /evidence="ECO:0007829|PDB:1QF8" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:4NH1" FT HELIX 67..87 FT /evidence="ECO:0007829|PDB:1QF8" FT HELIX 91..102 FT /evidence="ECO:0007829|PDB:1QF8" FT TURN 103..106 FT /evidence="ECO:0007829|PDB:1QF8" FT HELIX 112..114 FT /evidence="ECO:0007829|PDB:1QF8" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:1QF8" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:1QF8" FT TURN 138..140 FT /evidence="ECO:0007829|PDB:1QF8" FT STRAND 142..144 FT /evidence="ECO:0007829|PDB:3EED" FT HELIX 149..151 FT /evidence="ECO:0007829|PDB:1QF8" FT STRAND 152..155 FT /evidence="ECO:0007829|PDB:4MD7" FT HELIX 156..158 FT /evidence="ECO:0007829|PDB:1QF8" FT TURN 159..162 FT /evidence="ECO:0007829|PDB:4DGL" FT HELIX 163..170 FT /evidence="ECO:0007829|PDB:1QF8" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:1QF8" FT STRAND 187..189 FT /evidence="ECO:0007829|PDB:4MD9" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:4DGL" FT HELIX 195..198 FT /evidence="ECO:0007829|PDB:4DGL" FT TURN 199..201 FT /evidence="ECO:0007829|PDB:4DGL" FT HELIX 202..205 FT /evidence="ECO:0007829|PDB:4DGL" SQ SEQUENCE 215 AA; 24942 MW; E465B1E699B0E0EC CRC64; MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTIR //