CSK2B_RAT
ID CSK2B_RAT Reviewed; 215 AA.
AC P67874; P07312; P13862;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Casein kinase II subunit beta;
DE Short=CK II beta;
DE AltName: Full=Phosvitin;
GN Name=Csnk2b; Synonyms=Ck2n;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8173590;
RA Ahmed K., Davis A., Hanten J., Lambert D., McIvor R.S., Goueli S.A.;
RT "Cloning of cDNAs encoding the alpha and beta subunits of rat casein kinase
RT 2 (CK-2): investigation of molecular regulation of CK-2 by androgens in rat
RT ventral prostate.";
RL Cell. Mol. Biol. Res. 39:451-462(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
RN [3]
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), SUBUNIT, AND ZINC-BINDING SITES.
RX DOI=10.1007/S11434-008-0580-2;
RA Zhou W., Qin X., Yan X., Xie X., Li L., Fang S., Long J., Adelman J.,
RA Tang W.-J., Shen Y.;
RT "Crystal structures of catalytic and regulatory subunits of rat protein
RT kinase CK2.";
RL Chin. Sci. Bull. 54:220-226(2009).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P67871, 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 -!- PTM: Phosphorylated by alpha subunit. 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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC {ECO:0000305}.
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DR EMBL; L15619; AAA40928.1; -; mRNA.
DR EMBL; BX883045; CAE83994.1; -; Genomic_DNA.
DR RefSeq; NP_001030315.1; NM_001035238.2.
DR RefSeq; NP_112283.1; NM_031021.3.
DR PDB; 2R6M; X-ray; 3.10 A; A/B=1-215.
DR PDBsum; 2R6M; -.
DR AlphaFoldDB; P67874; -.
DR SMR; P67874; -.
DR BioGRID; 249550; 9.
DR IntAct; P67874; 3.
DR MINT; P67874; -.
DR STRING; 10116.ENSRNOP00000001123; -.
DR BindingDB; P67874; -.
DR ChEMBL; CHEMBL3988629; -.
DR iPTMnet; P67874; -.
DR PhosphoSitePlus; P67874; -.
DR SwissPalm; P67874; -.
DR jPOST; P67874; -.
DR PaxDb; P67874; -.
DR PRIDE; P67874; -.
DR GeneID; 81650; -.
DR KEGG; rno:81650; -.
DR UCSC; RGD:619978; rat.
DR CTD; 1460; -.
DR RGD; 619978; Csnk2b.
DR VEuPathDB; HostDB:ENSRNOG00000000847; -.
DR eggNOG; KOG3092; Eukaryota.
DR HOGENOM; CLU_034027_3_3_1; -.
DR InParanoid; P67874; -.
DR OMA; DADFGRC; -.
DR OrthoDB; 1335521at2759; -.
DR PhylomeDB; P67874; -.
DR TreeFam; TF314462; -.
DR Reactome; R-RNO-1483191; Synthesis of PC.
DR Reactome; R-RNO-201688; WNT mediated activation of DVL.
DR Reactome; R-RNO-2514853; Condensation of Prometaphase Chromosomes.
DR Reactome; R-RNO-445144; Signal transduction by L1.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-RNO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-RNO-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-RNO-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-RNO-8948751; Regulation of PTEN stability and activity.
DR EvolutionaryTrace; P67874; -.
DR PRO; PR:P67874; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000847; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; P67874; baseline and differential.
DR Genevisible; P67874; RN.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0000785; C:chromatin; IDA:RGD.
DR GO; GO:0005929; C:cilium; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; EXP:SynGO.
DR GO; GO:0016363; C:nuclear matrix; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0005956; C:protein kinase CK2 complex; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; EXP:SynGO.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; ISO:RGD.
DR GO; GO:0061154; P:endothelial tube morphogenesis; ISO:RGD.
DR GO; GO:0097421; P:liver regeneration; IEP:RGD.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISO:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; ISO:RGD.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:RGD.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; EXP:SynGO.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
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; 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_0000068240"
FT REGION 188..193
FT /note="Interaction with alpha subunit"
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: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"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:2R6M"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:2R6M"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:2R6M"
FT TURN 37..42
FT /evidence="ECO:0007829|PDB:2R6M"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:2R6M"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:2R6M"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:2R6M"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:2R6M"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:2R6M"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2R6M"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2R6M"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2R6M"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2R6M"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:2R6M"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2R6M"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:2R6M"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2R6M"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:2R6M"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:2R6M"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2R6M"
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
