P67874 (CSK2B_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 61.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Casein kinase II subunit beta Short name=CK II beta Alternative name(s): Phosvitin | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 215 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Participates in Wnt signaling. Plays a complex role in regulating the basal catalytic activity of the alpha subunit By similarity. Ref.3 |
| Subunit structure | 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. Ref.3 Ref.4 |
| Post-translational modification | 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. Ref.3 |
| Sequence similarities | Belongs to the casein kinase 2 subunit beta family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Wnt signaling pathway |
| Ligand | Metal-binding Zinc |
| PTM | Acetylation Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | I-kappaB kinase/NF-kappaB cascade Traceable author statement. Source: RGD Wnt receptor signaling pathwayInferred from electronic annotation. Source: UniProtKB-KW positive regulation of Wnt receptor signaling pathwayTraceable author statement. Source: RGD |
| Cellular component | protein kinase CK2 complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | protein kinase regulator activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 215 | 215 | Casein kinase II subunit beta | PRO_0000068240 | ||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||
| Region | 188 – 193 | 6 | Interaction with alpha subunit | |||||||||||||||||||||||||||||||||||||
| Compositional bias | 55 – 64 | 10 | Asp/Glu-rich (acidic) | |||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||
| Metal binding | 109 | 1 | Zinc | |||||||||||||||||||||||||||||||||||||
| Metal binding | 114 | 1 | Zinc | |||||||||||||||||||||||||||||||||||||
| Metal binding | 137 | 1 | Zinc | |||||||||||||||||||||||||||||||||||||
| Metal binding | 140 | 1 | Zinc | |||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | Phosphoserine; by autocatalysis Probable | |||||||||||||||||||||||||||||||||||||
| Modified residue | 3 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||||||||||||
| Modified residue | 4 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||||||||||||
| Modified residue | 8 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||||||||||||
| Modified residue | 69 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||||||||||||
| Modified residue | 145 | 1 | Phosphothreonine By similarity | |||||||||||||||||||||||||||||||||||||
| Modified residue | 197 | 1 | Phosphotyrosine By similarity | |||||||||||||||||||||||||||||||||||||
| Modified residue | 205 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||||||||||||
| Modified residue | 209 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||||||||||||
| Modified residue | 212 | 1 | N6-acetyllysine By similarity | |||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||
| Helix | 9 – 13 | 5 | ||||||||||||||||||||||||||||||||||||||
| Helix | 27 – 31 | 5 | ||||||||||||||||||||||||||||||||||||||
| Helix | 33 – 35 | 3 | ||||||||||||||||||||||||||||||||||||||
| Turn | 40 – 42 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 46 – 53 | 8 | ||||||||||||||||||||||||||||||||||||||
| Turn | 70 – 73 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 74 – 79 | 6 | ||||||||||||||||||||||||||||||||||||||
| Helix | 83 – 87 | 5 | ||||||||||||||||||||||||||||||||||||||
| Helix | 95 – 102 | 8 | ||||||||||||||||||||||||||||||||||||||
| Helix | 112 – 114 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 120 – 122 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 134 – 137 | 4 | ||||||||||||||||||||||||||||||||||||||
| Turn | 138 – 141 | 4 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 142 – 144 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 147 – 149 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 164 – 168 | 5 | ||||||||||||||||||||||||||||||||||||||
| Helix | 172 – 174 | 3 | ||||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [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: 8173590] [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: 15060004] [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: 16818610] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MUSK, INTERACTION WITH MUSK. |
| [4] | "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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | L15619 mRNA. Translation: AAA40928.1. BX883045 Genomic DNA. Translation: CAE83994.1. | ||||||||||||
| IPI | IPI00205531. | ||||||||||||
| RefSeq | NP_001030315.1. NM_001035238.2. NP_112283.1. NM_031021.3. | ||||||||||||
| UniGene | Rn.137692. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P67874. | ||||||||||||
| SMR | P67874. Positions 2-205. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | P67874. 1 interaction. | ||||||||||||
| STRING | P67874. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | P67874. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | P67874. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSRNOT00000001123; ENSRNOP00000001123; ENSRNOG00000000847. | ||||||||||||
| GeneID | 81650. | ||||||||||||
| KEGG | rno:81650. | ||||||||||||
| UCSC | NM_031021. rat. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 1460. | ||||||||||||
| RGD | 619978. Csnk2b. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | maNOG15317. | ||||||||||||
| HOVERGEN | HBG051131. | ||||||||||||
| InParanoid | P67874. | ||||||||||||
| OMA | TNQFVPR. | ||||||||||||
| OrthoDB | EOG4FBHTQ. | ||||||||||||
| PhylomeDB | P67874. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | P67874. | ||||||||||||
| Genevestigator | P67874. | ||||||||||||
| GermOnline | ENSRNOG00000000847. Rattus norvegicus. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR016149. Casein_kin_II_reg-sub_a-hlx. IPR016150. Casein_kin_II_reg-sub_b-sht. IPR000704. Casein_kinase_II_reg-sub. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:1.10.1820.10. Casein_kin_II_reg-sub_a-hlx. 1 hit. G3DSA:2.20.25.20. Casein_kin_II_reg-sub_b-sht. 1 hit. | ||||||||||||
| KO | K03115. | ||||||||||||
| PANTHER | PTHR11740. CAS_kinase_II. 1 hit. | ||||||||||||
| Pfam | PF01214. CK_II_beta. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00472. CASNKINASEII. | ||||||||||||
| SMART | SM01085. CK_II_beta. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF57798. Casein_kinase_II_reg-sub. 1 hit. | ||||||||||||
| PROSITE | PS01101. CK2_BETA. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| NextBio | 615182. | ||||||||||||
Entry information
| Entry name | CSK2B_RAT | ||||||||
| Accession | Primary (citable) accession number: P67874 Secondary accession number(s): P07312, P13862 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with