CSK2B_XENLA
ID CSK2B_XENLA Reviewed; 215 AA.
AC P28021; Q6DEB7;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Casein kinase II subunit beta;
DE Short=CK II beta;
DE AltName: Full=Phosvitin;
GN Name=csnk2b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=1544409; DOI=10.1016/0014-5793(92)80556-v;
RA Jedlicki A., Hinrichs M.V., Allende C., Allende J.E.;
RT "The cDNAs coding for the alpha- and beta-subunits of Xenopus laevis casein
RT kinase II.";
RL FEBS Lett. 297:280-284(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 1-178 IN COMPLEX WITH CDKN1A
RP PEPTIDE, AND ZINC-BINDING SITES.
RX PubMed=15388915; DOI=10.1107/s0907444904016750;
RA Bertrand L., Sayed M.F., Pei X.Y., Parisini E., Dhanaraj V.,
RA Bolanos-Garcia V.M., Allende J.E., Blundell T.L.;
RT "Structure of the regulatory subunit of CK2 in the presence of a p21WAF1
RT peptide demonstrates flexibility of the acidic loop.";
RL Acta Crystallogr. D 60:1698-1704(2004).
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. {ECO:0000250|UniProtKB:P67870,
CC 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. {ECO:0000250|UniProtKB:P67870}.
CC -!- INTERACTION:
CC P28021; B5TR11: PAPC; NbExp=3; IntAct=EBI-7614441, EBI-7614422;
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; X62376; CAA44239.1; -; mRNA.
DR EMBL; BC077212; AAH77212.1; -; mRNA.
DR PIR; S20405; S20405.
DR RefSeq; NP_001084126.1; NM_001090657.1.
DR RefSeq; XP_018085645.1; XM_018230156.1.
DR RefSeq; XP_018085646.1; XM_018230157.1.
DR RefSeq; XP_018085647.1; XM_018230158.1.
DR RefSeq; XP_018087419.1; XM_018231930.1.
DR PDB; 1RQF; X-ray; 2.89 A; A/B/D/E/G/H/J/K=1-178.
DR PDBsum; 1RQF; -.
DR AlphaFoldDB; P28021; -.
DR SMR; P28021; -.
DR BioGRID; 100645; 1.
DR IntAct; P28021; 1.
DR MINT; P28021; -.
DR DNASU; 399320; -.
DR GeneID; 108698568; -.
DR GeneID; 399320; -.
DR KEGG; xla:108698568; -.
DR KEGG; xla:399320; -.
DR CTD; 108698568; -.
DR CTD; 399320; -.
DR Xenbase; XB-GENE-17341072; csnk2b.L.
DR Xenbase; XB-GENE-865748; csnk2b.S.
DR OrthoDB; 1335521at2759; -.
DR EvolutionaryTrace; P28021; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 108698568; Expressed in testis and 19 other tissues.
DR GO; GO:0005956; C:protein kinase CK2 complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019887; F:protein kinase regulator activity; IEA:InterPro.
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; Metal-binding; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway; Zinc.
FT CHAIN 1..215
FT /note="Casein kinase II subunit beta"
FT /id="PRO_0000068242"
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 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="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000305"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:1RQF"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:1RQF"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1RQF"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1RQF"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:1RQF"
FT HELIX 69..87
FT /evidence="ECO:0007829|PDB:1RQF"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:1RQF"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:1RQF"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:1RQF"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1RQF"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1RQF"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1RQF"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:1RQF"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1RQF"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:1RQF"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1RQF"
SQ SEQUENCE 215 AA; 24960 MW; E46371E699B0E0EC CRC64;
MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE
ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML
PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA
NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTMR
