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Details on Person UniProt:P13639 EEF2

Class:Id	ReferenceGeneProduct:54178
_chainChangeLog	initiator methionine:1 added on Fri February 6 2015;chain:2-858 added on Fri February 6 2015;initiator methionine:1 for 54178 removed on Fri Nov 03 2023;initiator methionine: for 54178 added on Fri Nov 03 2023;initiator methionine: for 54178 removed on Fri Aug 15 2025;initiator methionine:1 for 54178 added on Fri Aug 15 2025
_displayName	UniProt:P13639 EEF2
_timestamp	2025-08-15 21:52:31
chain	initiator methionine:1 chain:2-858
checksum	78BD1710236C0D9C
comment	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).CATALYTIC ACTIVITY GTP + H2O = GDP + phosphate + H(+)SUBUNIT Binds to 80S ribosomes (PubMed:27115996, PubMed:30355441). Actively translating ribosomes show mutually exclusive binding of eIF5a (EIF5A or EIF5A2) and EEF2/eEF2 (PubMed:27115996). Interacts with SERBP1; interaction sequesters EEF2/eEF2 at the A-site of the ribosome, thereby blocking the interaction sites of the mRNA-tRNA complex, promoting ribosome stabilization and hibernation (PubMed:30355441). Interacts with HABP4; interaction takes place at the A-site of hibernating ribosomes and promotes ribosome stabilization (By similarity). Component of the mRNA surveillance SURF complex, at least composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8 and SMG9 (PubMed:19417104). Interacts with RBPMS2 (PubMed:25064856).INTERACTION Phosphorylation by CSK promotes cleavage and SUMOylation-dependent nuclear translocation of the C-terminal cleavage product.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.PTM Diphthamide is 2-[3-carboxyamido-3-(trimethyl-ammonio)propyl]histidine (By similarity).PTM (Microbial infection) Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus arresting protein synthesis.PTM ISGylated.PTM Proteolytically processed at two sites following phosphorylation by CSK.PTM SUMOylated following phosphorylation by CSK, promotes proteolytic cleavage.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.
description	recommendedName: Elongation factor 2 shortName: EF-2 ecNumber evidence="18"3.6.5.-
geneName	EEF2 EF2
identifier	P13639
isSequenceChanged	FALSE
keyword	3D-structure Acetylation ADP-ribosylation Cytoplasm Direct protein sequencing Disease variant Elongation factor GTP-binding Hydrolase Isopeptide bond Methylation Neurodegeneration Nucleotide-binding Nucleus Phosphoprotein Protein biosynthesis Proteomics identification Reference proteome Spinocerebellar ataxia Ubl conjugation
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9841277] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15
name	EEF2
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8957653] ENSEMBL:ENSG00000167658 EEF2 [Homo sapiens]
secondaryIdentifier	EF2_HUMAN A0A384N6H1 B2RMP5 D6W618 Q58J86
sequenceLength	858
species	[Species:48887] Homo sapiens
(referenceEntity)	[EntityWithAccessionedSequence:156901] EEF2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:165746] p-T56-EEF2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:5334764] ADP-ribo-EEF2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:5358472] nascent EEF2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:5358478] aminocarboxypropyl EEF2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:5358501] diphthine EEF2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:5367025] Me-diphthine EEF2 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:6801504] EEF2 [secretory granule lumen] [Homo sapiens] [EntityWithAccessionedSequence:6801513] EEF2 [ficolin-1-rich granule lumen] [Homo sapiens] [EntityWithAccessionedSequence:6801617] EEF2 [extracellular exosome] [Homo sapiens] List all 12 refering instances
(referenceSequence)	[ModifiedResidue:165748] O-phospho-L-threonine at 56 [ModifiedResidue:5334752] dipthamide at 715 [ModifiedResidue:5334778] N-tau-(ADP-ribosyl)diphthamide at 715 [GroupModifiedResidue:5358466] modified L-histidine residue (diphthine residue) at 715 [GroupModifiedResidue:5358500] modified L-histidine residue (2-(3-amino-3-carboxypropyl)-L-histidine zwitterion residue) at 715 [GroupModifiedResidue:5367018] modified L-histidine residue (diphthine methyl ester residue) at 715 [ModifiedResidue:8932236] N6,N6,N6-trimethyl-L-lysine at 525
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No pathways have been reviewed or authored by UniProt:P13639 EEF2 (54178)