Mitochondrial translational release factor 1

Mitochondrial translational release factor 1, also known as MTRF1 is a human gene.^[5][6]

MTRF1
Identifiers
Aliases	MTRF1, MRF1, MTTRF1, RF1, mitochondrial translational release factor 1, mitochondrial translation release factor 1
External IDs	OMIM: 604601; MGI: 2384815; HomoloGene: 20903; GeneCards: MTRF1; OMA:MTRF1 - orthologs
Gene location (Human) Chr. Chromosome 13 (human)[1] Band 13q14.11 Start 41,216,369 bp[1] End 41,263,577 bp[1]
Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14|14 D3 Start 79,635,212 bp[2] End 79,661,027 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas rectum right adrenal gland right adrenal cortex gallbladder left adrenal gland granulocyte testicle left adrenal cortex body of stomach Top expressed in left ventricle interventricular septum quadriceps femoris muscle primary oocyte muscle tissue proximal tubule muscle of thigh skeletal muscle tissue right kidney ovary More reference expression data BioGPS n/a
Gene ontology Molecular function translation release factor activity translation release factor activity, codon specific ribosome binding Cellular component mitochondrion cytoplasm Biological process translational termination regulation of translational termination protein biosynthesis mitochondrial translational termination Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9617 211253 Ensembl ENSG00000120662 ENSMUSG00000022022 UniProt O75570 Q8N6Z2 Q8K126 RefSeq (mRNA) NM_004294 NM_001354073 NM_001354074 NM_001354076 NM_145960 RefSeq (protein) NP_004285 NP_001341002 NP_001341003 NP_001341005 NP_666072 Location (UCSC) Chr 13: 41.22 – 41.26 Mb Chr 14: 79.64 – 79.66 Mb PubMed search [3] [4]
Wikidata
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The protein encoded by this gene directs the termination of translation in response to the peptide chain termination codons. Initially thought to have a role in the termination of mitochondria protein synthesis. mtRF1 has been hypothesized to recognize non-standard stop codons AGA and AGG in vertebrates. Alternatively, based on detailed 3D modelling, it has been proposed to recognize stalled ribosomes in which a tRNA is still bound to the peptide chain, but in which the A-site of the ribosome is empty.