EEF2 phospho T56
Function
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (PubMed:26593721). During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively (PubMed:26593721). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (PubMed:26593721).
Involvement in disease
Spinocerebellar ataxia 26
SCA26
A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
Phosphorylation by EF-2 kinase completely inactivates EF-2; it requires prior phosphorylation by CDK2 at Ser-595 during mitotic prometaphase. Phosphorylation by CSK promotes SUMOylation, proteolytic cleavage, and nuclear translocation if the C-terminal fragment.
Diphthamide is 2-[3-carboxyamido-3-(trimethyl-ammonio)propyl]histidine (By similarity).
(Microbial infection) Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus arresting protein synthesis.
ISGylated.
Proteolytically processed at two sites following phosphorylation by CSK.
SUMOylated following phosphorylation by CSK, promotes proteolytic cleavage.
Sequence Similarities
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
Cellular localization
- Cytoplasm
- Nucleus
- Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product.
Alternative names
EF2, EEF2, Elongation factor 2, EF-2