ID CSK2B_MOUSE Reviewed; 215 AA. AC P67871; P07312; P13862; Q3TTJ7; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 161. DE RecName: Full=Casein kinase II subunit beta; DE Short=CK II beta; DE AltName: Full=Phosvitin; GN Name=Csnk2b; Synonyms=Ck2n; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/cJ; RX PubMed=2362816; DOI=10.1093/nar/18.12.3639; RA Kopatz I., Naiman T., Eli D., Canaani D.; RT "The nucleotide sequence of the mouse cDNA encoding the beta subunit of RT casein kinase II."; RL Nucleic Acids Res. 18:3639-3639(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2015307; DOI=10.1016/0167-4781(91)90140-h; RA Boldyreff B., Piontek K., Schmidt-Spaniol I., Issinger O.-J.; RT "The beta subunit of casein kinase II: cloning of cDNAs from murine and RT porcine origin and expression of the porcine sequence as a fusion RT protein."; RL Biochim. Biophys. Acta 1088:439-441(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/6 X CBA; TISSUE=Spleen; RX PubMed=8530080; DOI=10.1006/geno.1995.1239; RA Boldyreff B., Issinger O.G.; RT "Structure of the gene encoding the murine protein kinase CK2 beta RT subunit."; RL Genomics 29:253-256(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=129; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Kidney, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Mammary tumor; 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 [7] RP FUNCTION IN WNT SIGNALING. RX PubMed=10806215; DOI=10.1074/jbc.m909107199; RA Song D.H., Sussman D.J., Seldin D.C.; RT "Endogenous protein kinase CK2 participates in Wnt signaling in mammary RT epithelial cells."; RL J. Biol. Chem. 275:23790-23797(2000). RN [8] RP INTERACTION WITH DYNLT2. RX PubMed=12849985; DOI=10.1016/s0006-291x(03)01118-5; RA Bai X., Xu X., Zhang F., Shu H.-B., Chan E.D.; RT "The protein of a new gene, Tctex4, interacts with protein kinase CK2beta RT subunit and is highly expressed in mouse testis."; RL Biochem. Biophys. Res. Commun. 307:86-91(2003). RN [9] 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). 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:16818610). CC Participates in Wnt signaling (PubMed:10806215). CC {ECO:0000269|PubMed:10806215, 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 (By CC similarity). Interacts (via KSSR motif) with ARK2N. Interacts with JUN CC and ARK2N; mediates the interaction between ARK2N and JUN (By CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P67870}. CC -!- INTERACTION: CC P67871; Q9WTL8: Bmal1; NbExp=8; IntAct=EBI-348179, EBI-644534; CC P67871; P97784: Cry1; NbExp=4; IntAct=EBI-348179, EBI-1266607; CC P67871; Q9R194: Cry2; NbExp=3; IntAct=EBI-348179, EBI-1266619; CC P67871; Q60737: Csnk2a1; NbExp=5; IntAct=EBI-348179, EBI-771698; CC P67871; P11985-2: Dynlt2; NbExp=2; IntAct=EBI-348179, EBI-1781298; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P67870}. CC -!- DOMAIN: The KSSR motif is part of a protein interaction pocket that CC mediates interaction with cellular and viral proteins. CC {ECO:0000250|UniProtKB:P67870}. CC -!- PTM: Phosphorylated by alpha subunit. {ECO:0000250}. 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; X52959; CAA37132.1; -; mRNA. DR EMBL; X56502; CAA39857.1; -; mRNA. DR EMBL; X80685; CAA56700.1; -; Genomic_DNA. DR EMBL; AF109719; AAF03911.1; -; Genomic_DNA. DR EMBL; AK002903; BAB22445.1; -; mRNA. DR EMBL; AK010730; BAB27147.1; -; mRNA. DR EMBL; AK012369; BAB28193.1; -; mRNA. DR EMBL; AK146186; BAE26962.1; -; mRNA. DR EMBL; AK161330; BAE36328.1; -; mRNA. DR EMBL; BC003775; AAH03775.1; -; mRNA. DR CCDS; CCDS28684.1; -. DR PIR; S14724; S14724. DR RefSeq; NP_001290374.1; NM_001303445.1. DR RefSeq; NP_034105.1; NM_009975.3. DR AlphaFoldDB; P67871; -. DR SMR; P67871; -. DR BioGRID; 198947; 31. DR CORUM; P67871; -. DR DIP; DIP-35573N; -. DR IntAct; P67871; 14. DR MINT; P67871; -. DR STRING; 10090.ENSMUSP00000134673; -. DR ChEMBL; CHEMBL4095; -. DR GlyGen; P67871; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P67871; -. DR PhosphoSitePlus; P67871; -. DR SwissPalm; P67871; -. DR EPD; P67871; -. DR jPOST; P67871; -. DR MaxQB; P67871; -. DR PaxDb; 10090-ENSMUSP00000025246; -. DR ProteomicsDB; 284137; -. DR Pumba; P67871; -. DR TopDownProteomics; P67871; -. DR Antibodypedia; 1045; 699 antibodies from 39 providers. DR DNASU; 13001; -. DR Ensembl; ENSMUST00000025246.13; ENSMUSP00000025246.7; ENSMUSG00000024387.14. DR Ensembl; ENSMUST00000173114.8; ENSMUSP00000134218.2; ENSMUSG00000024387.14. DR GeneID; 13001; -. DR KEGG; mmu:13001; -. DR UCSC; uc008cfu.2; mouse. DR AGR; MGI:88548; -. DR CTD; 1460; -. DR MGI; MGI:88548; Csnk2b. DR VEuPathDB; HostDB:ENSMUSG00000024387; -. DR eggNOG; KOG3092; Eukaryota. DR GeneTree; ENSGT00390000003781; -. DR InParanoid; P67871; -. DR OMA; DADFGRC; -. DR OrthoDB; 5485421at2759; -. DR PhylomeDB; P67871; -. DR TreeFam; TF314462; -. DR Reactome; R-MMU-1483191; Synthesis of PC. DR Reactome; R-MMU-201688; WNT mediated activation of DVL. DR Reactome; R-MMU-2514853; Condensation of Prometaphase Chromosomes. DR Reactome; R-MMU-445144; Signal transduction by L1. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding. DR Reactome; R-MMU-8934903; Receptor Mediated Mitophagy. DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known. DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity. DR BioGRID-ORCS; 13001; 28 hits in 79 CRISPR screens. DR ChiTaRS; Csnk2b; mouse. DR PRO; PR:P67871; -. DR Proteomes; UP000000589; Chromosome 17. DR RNAct; P67871; Protein. DR Bgee; ENSMUSG00000024387; Expressed in spermatid and 260 other cell types or tissues. DR ExpressionAtlas; P67871; baseline and differential. DR GO; GO:0042995; C:cell projection; ISO:MGI. DR GO; GO:0000785; C:chromatin; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016363; C:nuclear matrix; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0016605; C:PML body; ISO:MGI. DR GO; GO:0005956; C:protein kinase CK2 complex; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI. DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:MGI. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI. DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI. DR GO; GO:0033211; P:adiponectin-activated signaling pathway; ISO:MGI. DR GO; GO:0061154; P:endothelial tube morphogenesis; ISO:MGI. DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:MGI. DR GO; GO:1903901; P:negative regulation of viral life cycle; ISO:MGI. DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; ISO:MGI. DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISO:MGI. DR GO; GO:0075342; P:symbiont-mediated disruption of host cell PML body; ISO:MGI. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. 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. DR Genevisible; P67871; MM. PE 1: Evidence at protein level; KW Acetylation; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Ubl conjugation; Wnt signaling pathway; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P67870" FT CHAIN 2..215 FT /note="Casein kinase II subunit beta" FT /id="PRO_0000068237" 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:0000250|UniProtKB:P67870" FT BINDING 109 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 114 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 137 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P67870" FT MOD_RES 2 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P67870, ECO:0000305" FT MOD_RES 3 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P67870" FT MOD_RES 8 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P67870" FT MOD_RES 37 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P67870" FT MOD_RES 69 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P67870" FT MOD_RES 209 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P67870" FT MOD_RES 212 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P67870" FT CROSSLNK 212 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P67870" 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 //