Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Casein kinase II subunit beta

Gene

Csnk2b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Participates in Wnt signaling. Plays a complex role in regulating the basal catalytic activity of the alpha subunit (By similarity).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi109 – 1091Zinc
Metal bindingi114 – 1141Zinc
Metal bindingi137 – 1371Zinc
Metal bindingi140 – 1401Zinc

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-201688. WNT mediated activation of DVL.
R-RNO-2514853. Condensation of Prometaphase Chromosomes.
R-RNO-445144. Signal transduction by L1.
R-RNO-6804756. Regulation of TP53 Activity through Phosphorylation.
R-RNO-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
Casein kinase II subunit beta
Short name:
CK II beta
Alternative name(s):
Phosvitin
Gene namesi
Name:Csnk2b
Synonyms:Ck2n
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi619978. Csnk2b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 215214Casein kinase II subunit betaPRO_0000068240Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei2 – 21Phosphoserine; by autocatalysisCurated
Modified residuei3 – 31Phosphoserine; by autocatalysisBy similarity
Modified residuei8 – 81PhosphoserineBy similarity
Modified residuei37 – 371PhosphothreonineBy similarity
Modified residuei69 – 691PhosphoserineBy similarity
Modified residuei209 – 2091PhosphoserineBy similarity
Modified residuei212 – 2121N6-acetyllysine; alternateBy similarity
Cross-linki212 – 212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity

Post-translational modificationi

Phosphorylated by alpha subunit. Also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP67874.
PRIDEiP67874.

PTM databases

iPTMnetiP67874.
PhosphoSiteiP67874.

Expressioni

Gene expression databases

ExpressionAtlasiP67874. baseline and differential.
GenevisibleiP67874. RN.

Interactioni

Subunit structurei

Tetramer composed of an alpha subunit, an alpha' subunit and two beta subunits. The beta subunit dimerization is mediated by zinc ions. Interacts with CD163 and TCTEX1D3. Also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation (By similarity). Interacts with MUSK; mediates phosphorylation of MUSK by CK2. Interacts with FGF1; this interaction is increased in the presence of FIBP, suggesting a possible cooperative interaction between CSNKB and FIBP in binding to FGF1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi249550. 6 interactions.
IntActiP67874. 2 interactions.
STRINGi10116.ENSRNOP00000001123.

Chemistry

BindingDBiP67874.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 157Combined sources
Helixi27 – 315Combined sources
Helixi33 – 353Combined sources
Turni37 – 426Combined sources
Helixi46 – 538Combined sources
Turni70 – 734Combined sources
Helixi74 – 8714Combined sources
Helixi91 – 10212Combined sources
Turni103 – 1064Combined sources
Helixi112 – 1143Combined sources
Beta strandi120 – 1223Combined sources
Beta strandi126 – 1305Combined sources
Beta strandi134 – 1374Combined sources
Turni138 – 1414Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi147 – 1493Combined sources
Helixi156 – 1583Combined sources
Helixi163 – 1686Combined sources
Helixi172 – 1743Combined sources
Beta strandi186 – 1916Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R6MX-ray3.10A/B1-215[»]
ProteinModelPortaliP67874.
SMRiP67874. Positions 7-207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP67874.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni188 – 1936Interaction with alpha subunit

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 6410Asp/Glu-rich (acidic)

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3092. Eukaryota.
COG5041. LUCA.
HOGENOMiHOG000039270.
HOVERGENiHBG051131.
InParanoidiP67874.
KOiK03115.
OMAiCEGHALL.
OrthoDBiEOG7GTT4V.
PhylomeDBiP67874.
TreeFamiTF314462.

Family and domain databases

Gene3Di1.10.1820.10. 1 hit.
2.20.25.20. 1 hit.
InterProiIPR016149. Casein_kin_II_reg-sub_a-hlx.
IPR016150. Casein_kin_II_reg-sub_b-sht.
IPR000704. Casein_kinase_II_reg-sub.
[Graphical view]
PANTHERiPTHR11740. PTHR11740. 1 hit.
PfamiPF01214. CK_II_beta. 1 hit.
[Graphical view]
PRINTSiPR00472. CASNKINASEII.
SMARTiSM01085. CK_II_beta. 1 hit.
[Graphical view]
SUPFAMiSSF57798. SSF57798. 1 hit.
PROSITEiPS01101. CK2_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P67874-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL
60 70 80 90 100
DMILDLEPDE ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK
110 120 130 140 150
YQQGDFGYCP RVYCENQPML PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR
160 170 180 190 200
HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA NQFVPRLYGF KIHPMAYQLQ
210
LQAASNFKSP VKTIR
Length:215
Mass (Da):24,942
Last modified:October 11, 2004 - v1
Checksum:iE465B1E699B0E0EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L15619 mRNA. Translation: AAA40928.1.
BX883045 Genomic DNA. Translation: CAE83994.1.
RefSeqiNP_001030315.1. NM_001035238.2.
NP_112283.1. NM_031021.3.
UniGeneiRn.137692.

Genome annotation databases

EnsembliENSRNOT00000001123; ENSRNOP00000001123; ENSRNOG00000000847.
ENSRNOT00000076528; ENSRNOP00000068429; ENSRNOG00000000847.
GeneIDi81650.
KEGGirno:81650.
UCSCiRGD:619978. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L15619 mRNA. Translation: AAA40928.1.
BX883045 Genomic DNA. Translation: CAE83994.1.
RefSeqiNP_001030315.1. NM_001035238.2.
NP_112283.1. NM_031021.3.
UniGeneiRn.137692.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R6MX-ray3.10A/B1-215[»]
ProteinModelPortaliP67874.
SMRiP67874. Positions 7-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249550. 6 interactions.
IntActiP67874. 2 interactions.
STRINGi10116.ENSRNOP00000001123.

Chemistry

BindingDBiP67874.

PTM databases

iPTMnetiP67874.
PhosphoSiteiP67874.

Proteomic databases

PaxDbiP67874.
PRIDEiP67874.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000001123; ENSRNOP00000001123; ENSRNOG00000000847.
ENSRNOT00000076528; ENSRNOP00000068429; ENSRNOG00000000847.
GeneIDi81650.
KEGGirno:81650.
UCSCiRGD:619978. rat.

Organism-specific databases

CTDi1460.
RGDi619978. Csnk2b.

Phylogenomic databases

eggNOGiKOG3092. Eukaryota.
COG5041. LUCA.
HOGENOMiHOG000039270.
HOVERGENiHBG051131.
InParanoidiP67874.
KOiK03115.
OMAiCEGHALL.
OrthoDBiEOG7GTT4V.
PhylomeDBiP67874.
TreeFamiTF314462.

Enzyme and pathway databases

ReactomeiR-RNO-201688. WNT mediated activation of DVL.
R-RNO-2514853. Condensation of Prometaphase Chromosomes.
R-RNO-445144. Signal transduction by L1.
R-RNO-6804756. Regulation of TP53 Activity through Phosphorylation.
R-RNO-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Miscellaneous databases

EvolutionaryTraceiP67874.
PROiP67874.

Gene expression databases

ExpressionAtlasiP67874. baseline and differential.
GenevisibleiP67874. RN.

Family and domain databases

Gene3Di1.10.1820.10. 1 hit.
2.20.25.20. 1 hit.
InterProiIPR016149. Casein_kin_II_reg-sub_a-hlx.
IPR016150. Casein_kin_II_reg-sub_b-sht.
IPR000704. Casein_kinase_II_reg-sub.
[Graphical view]
PANTHERiPTHR11740. PTHR11740. 1 hit.
PfamiPF01214. CK_II_beta. 1 hit.
[Graphical view]
PRINTSiPR00472. CASNKINASEII.
SMARTiSM01085. CK_II_beta. 1 hit.
[Graphical view]
SUPFAMiSSF57798. SSF57798. 1 hit.
PROSITEiPS01101. CK2_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of cDNAs encoding the alpha and beta subunits of rat casein kinase 2 (CK-2): investigation of molecular regulation of CK-2 by androgens in rat ventral prostate."
    Ahmed K., Davis A., Hanten J., Lambert D., McIvor R.S., Goueli S.A.
    Cell. Mol. Biol. Res. 39:451-462(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "The genomic sequence and comparative analysis of the rat major histocompatibility complex."
    Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.
    Genome Res. 14:631-639(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Casein kinase 2-dependent serine phosphorylation of MuSK regulates acetylcholine receptor aggregation at the neuromuscular junction."
    Cheusova T., Khan M.A., Schubert S.W., Gavin A.C., Buchou T., Jacob G., Sticht H., Allende J., Boldyreff B., Brenner H.R., Hashemolhosseini S.
    Genes Dev. 20:1800-1816(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MUSK, INTERACTION WITH MUSK.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Crystal structures of catalytic and regulatory subunits of rat protein kinase CK2."
    Zhou W., Qin X., Yan X., Xie X., Li L., Fang S., Long J., Adelman J., Tang W.-J., Shen Y.
    Chin. Sci. Bull. 54:220-226(2009)
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), SUBUNIT, ZINC-BINDING SITES.

Entry informationi

Entry nameiCSK2B_RAT
AccessioniPrimary (citable) accession number: P67874
Secondary accession number(s): P07312, P13862
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 6, 2016
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.