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CSK2B_RABIT
ID   CSK2B_RABIT             Reviewed;         215 AA.
AC   P67873; P07312; P13862;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Casein kinase II subunit beta;
DE            Short=CK II beta;
DE   AltName: Full=Phosvitin;
GN   Name=CSNK2B; Synonyms=CK2N;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8444352; DOI=10.1016/0378-1119(93)90407-t;
RA   Gupta S.K., Singh J.P.;
RT   "PCR cloning and sequence of two cDNAs encoding the alpha and beta subunits
RT   of rabbit casein kinase-II.";
RL   Gene 124:287-290(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New Zealand white;
RA   Gupta S.K., Rothfuss K.J., Singh J.P.;
RT   "PCR cloning and sequence of two cDNAs encoding the alpha and beta subunit
RT   of rabbit casein kinase-II.";
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
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. 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; S56242; AAB25555.1; -; mRNA.
DR   EMBL; M98450; AAA91892.1; -; mRNA.
DR   PIR; JN0556; JN0556.
DR   RefSeq; NP_001153755.1; NM_001160283.1.
DR   AlphaFoldDB; P67873; -.
DR   SMR; P67873; -.
DR   BioGRID; 1172791; 1.
DR   STRING; 9986.ENSOCUP00000017566; -.
DR   Ensembl; ENSOCUT00000023439; ENSOCUP00000017566; ENSOCUG00000023483.
DR   GeneID; 100301531; -.
DR   KEGG; ocu:100301531; -.
DR   CTD; 1460; -.
DR   eggNOG; KOG3092; Eukaryota.
DR   GeneTree; ENSGT00390000003781; -.
DR   HOGENOM; CLU_034027_3_3_1; -.
DR   InParanoid; P67873; -.
DR   OMA; DADFGRC; -.
DR   OrthoDB; 1335521at2759; -.
DR   Proteomes; UP000001811; Chromosome 12.
DR   Bgee; ENSOCUG00000023483; Expressed in testis and 15 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   2: Evidence at transcript 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_0000068239"
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
 
 
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