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Details on Person UniProt:P49411 TUFM
| Class:Id | ReferenceGeneProduct:54206 |
|---|---|
| _chainChangeLog | transit peptide:1-43 added on Sat February 7 2015;chain:44-452 added on Sat February 7 2015;transit peptide:1-43 for 54206 removed on Fri February 24 2023;chain:44-452 for 54206 removed on Fri February 24 2023;transit peptide:1-46 for 54206 added on Fri February 24 2023;chain:47-455 for 54206 added on Fri February 24 2023 |
| _displayName | UniProt:P49411 TUFM |
| _timestamp | 2026-02-20 21:48:47 |
| chain | transit peptide:1-46 chain:47-455 |
| checksum | 58CAE59637766D3D |
| comment | FUNCTION GTP hydrolase that promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Participates in mitochondrial translation (By similarity). Also plays a role in the regulation of autophagy and innate immunity (PubMed:22749352, PubMed:28407488). Recruits ATG5-ATG12 and NLRX1 at mitochondria and serves as a checkpoint of the RIGI-MAVS pathway (PubMed:28407488). In turn, inhibits RLR-mediated type I interferon while promoting autophagy (PubMed:22749352).CATALYTIC ACTIVITY GTP + H2O = GDP + phosphate + H(+)PATHWAY Protein biosynthesis; polypeptide chain elongation.SUBUNIT Interacts with NLRX1 (PubMed:22749352). Interacts with ATG16L1 (PubMed:22749352).SUBUNIT (Microbial infection) Interacts with human parainfluenza virus 3 matrix protein; this interaction inhibits RLR-mediated type I interferon production while promoting autophagy.SUBUNIT (Microbial infection) Interacts with Hantaan hantavirus glycoprotein N; this interaction contributes to the virus-induced degradation of mitochondria by autophagy, which leads to degradation of MAVS and inhibition of type I interferon (IFN) responses.INTERACTION 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-Tu/EF-1A subfamily.SEQUENCE CAUTION Truncated N-terminus.SEQUENCE CAUTION Truncated N-terminus. |
| description | recommendedName: Elongation factor Tu, mitochondrial shortName: EF-Tu ecNumber evidence="2"3.6.5.3 alternativeName: P43 |
| geneName | TUFM |
| identifier | P49411 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Direct protein sequencing Disease variant Elongation factor GTP-binding Host-virus interaction Hydrolase Magnesium Metal-binding Mitochondrion Nucleotide-binding Phosphoprotein Primary mitochondrial disease Protein biosynthesis Proteomics identification Reference proteome Transit peptide |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9948485] Weiser, Joel, 2025-05-21 [InstanceEdit:9983091] Weiser, Joel, 2026-02-20 |
| name | TUFM |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:9001733] ENSEMBL:ENSG00000178952 TUFM [Homo sapiens] |
| secondaryIdentifier | EFTU_HUMAN O15276 |
| sequenceLength | 455 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:5389846] TUFM [mitochondrial matrix] [Homo sapiens] [EntityWithAccessionedSequence:9754777] TUFM [mitochondrial outer membrane] [Homo sapiens] |
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No pathways have been reviewed or authored by UniProt:P49411 TUFM (54206)
