ID CSK2B_BOVIN Reviewed; 215 AA.
AC P67868; P07312; P13862; Q2YDL2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, 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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 4-213.
RC TISSUE=Lung;
RX PubMed=3299375; DOI=10.1073/pnas.84.14.4851;
RA Takio K., Kuenzel E.A., Walsh K.A., Krebs E.G.;
RT "Amino acid sequence of the beta subunit of bovine lung casein kinase II.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4851-4855(1987).
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 (By similarity).
CC Participates in Wnt signaling (By similarity).
CC {ECO:0000250|UniProtKB:P67870, ECO:0000250|UniProtKB:P67871}.
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 -!- 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 -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC {ECO:0000305}.
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DR EMBL; BC110170; AAI10171.1; -; mRNA.
DR PIR; A25828; A25828.
DR RefSeq; NP_001039919.1; NM_001046454.1.
DR AlphaFoldDB; P67868; -.
DR SMR; P67868; -.
DR BioGRID; 195802; 6.
DR CORUM; P67868; -.
DR DIP; DIP-12N; -.
DR IntAct; P67868; 1.
DR STRING; 9913.ENSBTAP00000042926; -.
DR ChEMBL; CHEMBL3988628; -.
DR PaxDb; 9913-ENSBTAP00000042926; -.
DR Ensembl; ENSBTAT00000045545.2; ENSBTAP00000042926.1; ENSBTAG00000008837.4.
DR GeneID; 539235; -.
DR KEGG; bta:539235; -.
DR CTD; 1460; -.
DR VEuPathDB; HostDB:ENSBTAG00000008837; -.
DR VGNC; VGNC:53965; CSNK2B.
DR eggNOG; KOG3092; Eukaryota.
DR GeneTree; ENSGT00390000003781; -.
DR HOGENOM; CLU_034027_3_3_1; -.
DR InParanoid; P67868; -.
DR OMA; DADFGRC; -.
DR TreeFam; TF314462; -.
DR Reactome; R-BTA-1483191; Synthesis of PC.
DR Reactome; R-BTA-201688; WNT mediated activation of DVL.
DR Reactome; R-BTA-2514853; Condensation of Prometaphase Chromosomes.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-BTA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-BTA-8934903; Receptor Mediated Mitophagy.
DR Reactome; R-BTA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-BTA-8948751; Regulation of PTEN stability and activity.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000008837; Expressed in spermatid and 104 other cell types or tissues.
DR ExpressionAtlas; P67868; baseline and differential.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031519; C:PcG protein complex; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
DR GO; GO:0005956; C:protein kinase CK2 complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; IEA:Ensembl.
DR GO; GO:0061154; P:endothelial tube morphogenesis; IEA:Ensembl.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:1903901; P:negative regulation of viral life cycle; IEA:Ensembl.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0046719; P:regulation by virus of viral protein levels in host cell; IMP:AgBase.
DR GO; GO:0042325; P:regulation of phosphorylation; IDA:AgBase.
DR GO; GO:0050792; P:regulation of viral process; IMP:AgBase.
DR GO; GO:0075342; P:symbiont-mediated disruption of host cell PML body; IEA:Ensembl.
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.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation;
KW 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_0000068235"
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"
FT CONFLICT 5
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
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
//
