CSK2B_BOVIN
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 03-AUG-2022, entry version 127.
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 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. {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; P67868; -.
DR PRIDE; P67868; -.
DR Ensembl; ENSBTAT00000045545; ENSBTAP00000042926; ENSBTAG00000008837.
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 OrthoDB; 1335521at2759; -.
DR TreeFam; TF314462; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000008837; Expressed in spermatid and 104 other tissues.
DR ExpressionAtlas; P67868; baseline and differential.
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: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: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:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
DR GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; 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:0080163; P:regulation of protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0050792; P:regulation of viral process; IMP:AgBase.
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; Direct protein sequencing; Isopeptide bond; Metal-binding;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Wnt signaling pathway;
KW 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 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
