Reviewed,
UniProtKB/Swiss-Prot P70531 (EF2K_RAT)
Last modified
November 3, 2009.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Elongation factor 2 kinase EC=2.7.11.20 Alternative name(s): eEF-2 kinase Short name=eEF-2K Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase | ||
| 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 | 724 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | In vitro, it phosphorylates 2 adjacent threonine residues, 'Thr-57' and 'Thr-59', in the N-terminus of eukaryotic elongation factor-2. Binds calmodulin. |
| Catalytic activity | ATP + [elongation factor 2] = ADP + [elongation factor 2] phosphate. |
| Enzyme regulation | Undergoes calcium/calmodulin-dependent intramolecular autophosphorylation, and this results in it becoming partially calcium/calmodulin-independent. |
| Subunit structure | Monomer or homodimer Potential. |
| Tissue specificity | Mostly in skeletal muscle. |
| Post-translational modification | The N-terminus is blocked. |
| Sequence similarities | Belongs to the protein kinase superfamily. Alpha-type protein kinase family. Contains 1 alpha-type protein kinase domain. |
Ontologies
| Keywords | |
|---|---|
| Ligand | ATP-binding Calcium Calmodulin-binding Nucleotide-binding |
| Molecular function | Kinase Serine/threonine-protein kinase Transferase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion bindingInferred from electronic annotation. Source: UniProtKB-KW calmodulin bindingInferred from electronic annotation. Source: UniProtKB-KW elongation factor-2 kinase activity Ref.1Inferred from mutant phenotype. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 724 | 724 | Elongation factor 2 kinase | PRO_0000086938 | |||||
Regions | |||||||||
| Domain | 115 – 325 | 211 | Alpha-type protein kinase | ||||||
| Nucleotide binding | 295 – 301 | 7 | ATP By similarity | ||||||
| Region | 593 – 609 | 17 | Calmodulin-binding Potential | ||||||
| Region | 609 – 626 | 18 | Pseudosubstrate/autoinhibitory domain Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 18 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 27 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 29 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 31 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 70 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 134 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 347 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 444 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 469 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 473 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 476 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "Cloning and expression of cDNA encoding protein synthesis elongation factor-2 kinase." Redpath N.T., Price N.T., Proud C.G. J. Biol. Chem. 271:17547-17554(1996) [PubMed: 8663182] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Skeletal muscle. |
| [2] | "Identification of a new class of protein kinases represented by eukaryotic elongation factor-2 kinase." Ryazanov A.G., Ward M.D., Mendola C.E., Pavur K.S., Dorovkov M.V., Wiedmann M., Erdjument-Bromage H., Tempst P., Parmer T.G., Prostko C.R., Germino F.J., Hait W.N. Proc. Natl. Acad. Sci. U.S.A. 94:4884-4889(1997) [PubMed: 9144159] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: New England Deaconess Hospital. Tissue: Pheochromocytoma. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| X96426 mRNA. Translation: CAA65286.1. U93849 mRNA. Translation: AAB58272.1. | |
| IPI | IPI00189647. |
| RefSeq | NP_037079.1. |
| UniGene | Rn.10958 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P70531. |
PTM databases | |
| PhosphoSite | P70531. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000022726; ENSRNOP00000022726; ENSRNOG00000016448; Rattus norvegicus. [Genome view] |
| GeneID | 25435. |
| KEGG | rno:25435. |
| UCSC | BC061825. rat. |
Organism-specific databases | |
| CTD | 25435. |
| RGD | 2538. Eef2k. |
Phylogenomic databases | |
| HOVERGEN | P70531. |
| OMA | PKQVDIM. |
Enzyme and pathway databases | |
| BRENDA | 2.7.11.20. 248. |
Gene expression databases | |
| ArrayExpress | P70531. |
| Genevestigator | P70531. |
| GermOnline | ENSRNOG00000016448. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR017400. Elongation_factor_2_kinase. IPR004166. MHCK_EF2_kinase. IPR006597. Sel1-like. IPR011990. TPR-like_helical. [Graphical view] |
| Gene3D | G3DSA:1.25.40.10. TPR-like_helical. 1 hit. |
| Pfam | PF02816. Alpha_kinase. 1 hit. PF08238. Sel1. 3 hits. [Graphical view] |
| PIRSF | PIRSF038139. Elongation_factor_2_kinase. 1 hit. |
| SMART | SM00811. Alpha_kinase. 1 hit. [Graphical view] |
| PROSITE | PS51158. ALPHA_KINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 606641. |
Entry information
| Entry name | EF2K_RAT | ||||||||
| Accession | Primary (citable) accession number: P70531 Secondary accession number(s): O09089 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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