EEF2
entrez
1938
canonical
uniprot
P13639
canonical
ensembl
ENSG00000167658
resolver
ensp
ENSP00000307940
resolver
enst
ENST00000309311
resolver
genesymbol
EEF2
resolver
genesymbol_syn
EF2
resolver
hgnc
HGNC:3214
resolver
uniprot
A0A384N6H1
resolver
uniprot
B2RMP5
resolver
uniprot
D6W618
resolver
uniprot
Q58J86
resolver
uniprot_entry
EF2_HUMAN
resolver
uniprot_sec
A0A384N6H1
resolver
uniprot_sec
B2RMP5
resolver
uniprot_sec
D6W618
resolver
uniprot_sec
Q58J86
resolver
amino_acid_sequence
MVNFTVDQIRAIMDKKANIRNMSVIAHVDHGKSTLTDSLVCKAGIIASARAGETRFTDTRKDEQERCITIKSTAISLFYELSENDLNFIKQSKDGAGFLINLIDSPGHVDFSSEVTAALRVTDGALVVVDCVSGVCVQTETVLRQAIAERIKPVLMMNKMDRALLELQLEPEELYQTFQRIVENVNVIISTYGEGESGPMGNIMIDPVLGTVGFGSGLHGWAFTLKQFAEMYVAKFAAKGEGQLGPAERAKKVEDMMKKLWGDRYFDPANGKFSKSATSPEGKKLPRTFCQLILDPIFKVFDAIMNFKKEETAKLIEKLDIKLDSEDKDKEGKPLLKAVMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAMGIKSCDPKGPLMMYISKMVPTSDKGRFYAFGRVFSGLVSTGLKVRIMGPNYTPGKKEDLYLKPIQRTILMMGRYVEPIEDVPCGNIVGLVGVDQFLVKTGTITTFEHAHNMRVMKFSVSPVVRVAVEAKNPADLPKLVEGLKRLAKSDPMVQCIIEESGEHIIAGAGELHLEICLKDLEEDHACIPIKKSDPVVSYRETVSEESNVLCLSKSPNKHNRLYMKARPFPDGLAEDIDKGEVSARQELKQRARYLAEKYEWDVAEARKIWCFGPDGTGPNILTDITKGVQYLNEIKDSVVAGFQWATKEGALCEENMRGVRFDVHDVTLHADAIHRGGGQIIPTARRCLYASVLTAQPRLMEPIYLVEIQCPEQVVGGIYGVLNRKRGHVFEESQVAGTPMFVVKAYLPVNESFGFTADLRSNTGGQAFPQCVFDHWQILPGDPFDNSSRPSQVVAETRKRKGLKEGIPALDNFLDKL
uniprot
proteins
disease_involvement
DISEASE: Spinocerebellar ataxia 26 (SCA26) [MIM:609306]: 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. {ECO:0000269|PubMed:23001565}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
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). {ECO:0000269|PubMed:26593721}.
uniprot
proteins
mass_dalton
95338
uniprot
proteins
mutagenesis
MUTAGEN 595; /note="S->A: Strongly reduced phosphorylation at Thr-57."; /evidence="ECO:0000269|PubMed:23184662"; MUTAGEN 599; /note="H->P: Strongly reduced phosphorylation at Thr-57."; /evidence="ECO:0000269|PubMed:23184662"; MUTAGEN 715; /note="H->L,M,N,Q: Confers resistance to diphtheria toxin."; /evidence="ECO:0000269|PubMed:16901746
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:23184662, ECO:0000269|PubMed:24648518}.; PTM: Diphthamide is 2-[3-carboxyamido-3-(trimethyl-ammonio)propyl]histidine (By similarity). {ECO:0000250|UniProtKB:P05197}.; PTM: (Microbial infection) Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus arresting protein synthesis. {ECO:0000269|PubMed:16901746}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Proteolytically processed at two sites following phosphorylation by CSK. {ECO:0000269|PubMed:24648518}.; PTM: SUMOylated following phosphorylation by CSK, promotes proteolytic cleavage. {ECO:0000269|PubMed:24648518}.
uniprot
proteins
protein_family
Classic translation factor GTPase family
uniprot
proteins
protein_family
EF-G/EF-2 subfamily
uniprot
proteins
protein_family
TRAFAC class translation factor GTPase superfamily
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1596361
uniprot
proteins
pubmed
16139798
uniprot
proteins
pubmed
16901746
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19417104
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23001565
uniprot
proteins
pubmed
23184662
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23636399
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24648518
uniprot
proteins
pubmed
25064856
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25231979
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
2610926
uniprot
proteins
pubmed
26593721
uniprot
proteins
pubmed
27115996
uniprot
proteins
pubmed
2840927
uniprot
proteins
pubmed
30355441
uniprot
proteins
pubmed
32687489
uniprot
proteins
sequence_length
858
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25064856}. Nucleus {ECO:0000269|PubMed:24648518}. Note=Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product. {ECO:0000269|PubMed:24648518}.
uniprot
proteins