CSK2B_MOUSE
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 03-AUG-2022, entry version 152.
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, Pancreas,
RC 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 CD163. Also
CC component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H,
CC CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV
CC irradiation (By similarity). Interacts with DYNLT2. Interacts with
CC MUSK; mediates phosphorylation of MUSK by CK2. Interacts with FGF1;
CC this interaction is increased in the presence of FIBP, suggesting a
CC possible cooperative interaction between CSNKB and FIBP in binding to
CC FGF1 (By similarity). {ECO:0000250|UniProtKB:P67870}.
CC -!- INTERACTION:
CC P67871; Q9WTL8: Arntl; 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 -!- PTM: Phosphorylated by alpha subunit. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC {ECO:0000305}.
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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; 30.
DR CORUM; P67871; -.
DR DIP; DIP-35573N; -.
DR IntAct; P67871; 14.
DR MINT; P67871; -.
DR STRING; 10090.ENSMUSP00000025246; -.
DR ChEMBL; CHEMBL4095; -.
DR iPTMnet; P67871; -.
DR PhosphoSitePlus; P67871; -.
DR EPD; P67871; -.
DR jPOST; P67871; -.
DR MaxQB; P67871; -.
DR PaxDb; P67871; -.
DR PRIDE; P67871; -.
DR ProteomicsDB; 284137; -.
DR TopDownProteomics; P67871; -.
DR Antibodypedia; 1045; 624 antibodies from 39 providers.
DR DNASU; 13001; -.
DR Ensembl; ENSMUST00000025246; ENSMUSP00000025246; ENSMUSG00000024387.
DR Ensembl; ENSMUST00000173114; ENSMUSP00000134218; ENSMUSG00000024387.
DR GeneID; 13001; -.
DR KEGG; mmu:13001; -.
DR UCSC; uc008cfu.2; mouse.
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 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 75 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 257 other tissues.
DR ExpressionAtlas; P67871; baseline and differential.
DR Genevisible; P67871; MM.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031519; C:PcG protein complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0005956; C:protein kinase CK2 complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; 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: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:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; ISO:MGI.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
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 Acetylation; Isopeptide bond; Metal-binding; 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 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
