CSK2B_HUMAN
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 03-AUG-2022, entry version 188.
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; 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 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 [26]
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 [27]
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 [28]
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 [29]
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 [30]
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 [31]
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 [32]
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 [33]
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 [34]
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 [35]
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 -!- 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 {ECO:0000250, ECO:0000269|PubMed:10357806, ECO:0000269|PubMed:11239457,
CC ECO:0000269|PubMed:11298324, ECO:0000269|PubMed:11574463,
CC ECO:0000269|PubMed:11964394, ECO:0000269|PubMed:12393879,
CC ECO:0000269|PubMed:16818610}.
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; P68400: CSNK2A1; NbExp=27; IntAct=EBI-348169, EBI-347804;
CC P67870; P19784: CSNK2A2; NbExp=14; 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; A0A024R5S0: hCG_2003792; NbExp=3; IntAct=EBI-348169, EBI-10188461;
CC P67870; P09067: HOXB5; NbExp=3; IntAct=EBI-348169, EBI-3893317;
CC P67870; Q9C086: INO80B; NbExp=3; IntAct=EBI-348169, EBI-715611;
CC P67870; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-348169, EBI-14086479;
CC P67870; Q8NEJ9: NGDN; NbExp=3; IntAct=EBI-348169, EBI-9995414;
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; 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=3; IntAct=EBI-348169, EBI-395290;
CC P67870; Q99496: RNF2; NbExp=2; IntAct=EBI-348169, EBI-722416;
CC P67870; P51812: RPS6KA3; NbExp=4; IntAct=EBI-348169, EBI-1046616;
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: Arntl; 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 -!- 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}.
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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; 454.
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 IntAct; P67870; 271.
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 EPD; P67870; -.
DR jPOST; P67870; -.
DR MassIVE; P67870; -.
DR MaxQB; P67870; -.
DR PaxDb; P67870; -.
DR PeptideAtlas; P67870; -.
DR PRIDE; P67870; -.
DR ProteomicsDB; 57524; -.
DR Antibodypedia; 1045; 624 antibodies from 39 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 CTD; 1460; -.
DR DisGeNET; 1460; -.
DR GeneCards; CSNK2B; -.
DR HGNC; HGNC:2460; CSNK2B.
DR HPA; ENSG00000204435; Low tissue specificity.
DR MalaCards; CSNK2B; -.
DR MIM; 115441; gene.
DR MIM; 618732; phenotype.
DR neXtProt; NX_P67870; -.
DR OpenTargets; ENSG00000204435; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR PharmGKB; PA26960; -.
DR VEuPathDB; HostDB:ENSG00000204435; -.
DR eggNOG; KOG3092; Eukaryota.
DR GeneTree; ENSGT00390000003781; -.
DR HOGENOM; CLU_034027_3_3_1; -.
DR InParanoid; P67870; -.
DR OrthoDB; 1335521at2759; -.
DR PhylomeDB; P67870; -.
DR TreeFam; TF314462; -.
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 SignaLink; P67870; -.
DR SIGNOR; P67870; -.
DR BioGRID-ORCS; 1460; 707 hits in 1108 CRISPR screens.
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 93 other tissues.
DR ExpressionAtlas; P67870; baseline and differential.
DR Genevisible; P67870; HS.
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:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005956; C:protein kinase CK2 complex; IDA:CAFA.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
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: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:0018107; P:peptidyl-threonine phosphorylation; IDA:CAFA.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0065003; P:protein-containing complex assembly; NAS:BHF-UCL.
DR GO; GO:0051101; P:regulation of DNA binding; NAS:BHF-UCL.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1820.10; -; 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; PTHR11740; 1.
DR Pfam; PF01214; CK_II_beta; 1.
DR PRINTS; PR00472; CASNKINASEII.
DR SMART; SM01085; CK_II_beta; 1.
DR SUPFAM; SSF57798; SSF57798; 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; Phosphoprotein;
KW Reference proteome; 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 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; unknown pathological
FT significance; 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 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
