BioPAX pathway converted from "Metabolism of proteins" in the Reactome database.Metabolism of proteinsMetabolism of proteinsThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>TranslationTranslationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>tRNA AminoacylationtRNA AminoacylationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Cytosolic tRNA aminoacylationCytosolic tRNA aminoacylationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>3.6.1.1pyrophosphate + H2O => 2 orthophosphate [cytosolic]pyrophosphate + H2O => 2 orthophosphate [cytosolic]This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 1112941cytosolGO0005829diphosphoric acid [ChEBI:29888]diphosphoric acidReactomehttp://www.reactome.orgChEBI29888Reactome DB_ID: 293561water [ChEBI:15377]waterChEBI15377Reactome DB_ID: 293722hydrogenphosphate [ChEBI:43474]hydrogenphosphate[PO3(OH)](2-)HYDROGENPHOSPHATE IONhydrogen phosphate[P(OH)O3](2-)HPO4(2-)phosphateINORGANIC PHOSPHATE GROUPChEBI43474PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 10093376PPA1 dimer [cytosol]PPA1 dimerReactome DB_ID: 100933742UniProt:F1SUE3PPA1Sus scrofaNCBI Taxonomy9823UniProtF1SUE3Chain Coordinates1EQUAL289EQUALReactome Database ID Release 7510093376Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10093376ReactomeR-SSC-717261Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-71726.1GO0004427GO molecular functionReactome Database ID Release 7510093377Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10093377Reactome Database ID Release 7510093379Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10093379ReactomeR-SSC-717321Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-71732.1Cytosolic PPA1 (pyrophosphatase (inorganic) 1) catalyzes the hydrolysis of pyrophosphate to yield two molecules of orthophosphate. The enzyme, a homodimer, requires Mg++ for activity (Fisher et al. 1974; Pynes and Younathan 1967; Thuiller et al. 1978).656444Pubmed1978Purification and kinetic properties of human erythrocyte Mg2+-dependent inorganic pyrophosphataseThuillier, LBiochim Biophys Acta 524:198-2064130389Pubmed1974Studies on human erythrocyte inorganic pyrophosphatase.Fisher, RATurner, BMDorkin, HLHarris, HAnn Hum Genet 37:341-536022858Pubmed1967Purification and some properties of inorganic pyrophosphatase from human erythrocytesPynes, GDYounathan, ESJ Biol Chem 242:2119-23inferred by electronic annotationIEAGOIEAACTIVATIONReactome Database ID Release 75449940Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=449940ReactomeR-HSA-4499401Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-449940.1Reactome DB_ID: 29926magnesium(2+) [ChEBI:18420]magnesium(2+)ChEBI18420Reactome Database ID Release 7510184851Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10184851ReactomeR-SSC-3797161Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-379716.1GO0006418GO biological processCytosolic tRNA synthetases catalyze the reactions of tRNAs encoded in the nuclear genome, their cognate amino acids, and ATP to form aminoacyl-tRNAs, AMP, and pyrophosphate. Eight of the tRNA synthetases, those specific for arginine, aspartate, glutamate and proline, glutamine, isoleucine, leucine, lysine, and methionine, associate to form a complex with three accessory proteins. Each of the component synthetases is active in vitro as a purified protein; complex formation is thought to channel aminoacylated tRNAs more efficiently to the site of protein synthesis in mRNA:ribosome complexes (Quevillon et al. 1999; Wolfe et al. 2003, 2005).14500886Pubmed2003Isolation and characterization of human nuclear and cytosolic multisynthetase complexes and the intracellular distribution of p43/EMAPIIWolfe, CLWarrington, JADavis, SGreen, SNorcum, MTProtein Sci 12:2282-909878398Pubmed1999Macromolecular assemblage of aminoacyl-tRNA synthetases: identification of protein-protein interactions and characterization of a core proteinQuevillon, SRobinson, JCBerthonneau, ESiatecka, MMirande, MJ Mol Biol 285:183-9516169847Pubmed2005A three-dimensional working model of the multienzyme complex of aminoacyl-tRNA synthetases based on electron microscopic placements of tRNA and proteinsWolfe, CLWarrington, JATreadwell, LNorcum, MTJ Biol Chem 280:38870-8inferred by electronic annotationIEAGOIEAMitochondrial tRNA aminoacylationMitochondrial tRNA aminoacylationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>3.6.1.1pyrophosphate + H2O => 2 orthophosphate [mitochondrial]pyrophosphate + H2O => 2 orthophosphate [mitochondrial]This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 1594501mitochondrial matrixGO0005759Reactome DB_ID: 1135211Reactome DB_ID: 1135482PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 10123567PPA2 dimer [mitochondrial matrix]PPA2 dimerReactome DB_ID: 101235652UniProt:I3LFE8PPA2UniProtI3LFE833EQUAL334EQUALReactome Database ID Release 7510123567Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10123567ReactomeR-SSC-4499231Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-449923.1Reactome Database ID Release 7510123568Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10123568Reactome Database ID Release 7510123570Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10123570ReactomeR-SSC-4499371Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-449937.1Mitochondrial PPA2 (pyrophosphatase (inorganic) 2) catalyzes the hydrolysis of pyrophosphate to yield two molecules of orthophosphate. The enzyme requires Mg++ for activity (Curbo et al. 2006). The enzyme is inferred to be a homodimer by analogy to its cytosolic isoform.16300924Pubmed2006Human mitochondrial pyrophosphatase: cDNA cloning and analysis of the gene in patients with mtDNA depletion syndromesCurbo, SLagier-Tourenne, CCarrozzo, RPalenzuela, LLucioli, SHirano, MSantorelli, FArenas, JKarlsson, AJohansson, MGenomics 87:410-6inferred by electronic annotationIEAGOIEAACTIVATIONReactome Database ID Release 75210326Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=210326ReactomeR-HSA-2103262Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-210326.2Reactome DB_ID: 109496Reactome Database ID Release 7510186425Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10186425ReactomeR-SSC-3797261Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-379726.1Mitochondrial tRNA synthetases act in the mitochondrial matrix to catalyze the reactions of tRNAs encoded in the mitochondrial genome, their cognate amino acids, and ATP to form aminoacyl-tRNAs, AMP, and pyrophosphate (Schneider et al. 2000). The synthetase enzymes that catalyze these reactions are all encoded in the nuclear genome. In three cases, glycine, lysine, and glutamine, a single gene encodes two enzyme isoforms, one cytosolic and one mitochondrial. All other mitochondrial tRNA synthetases are encoded by genes different from the ones encoding the corresponding cytosolic enzymes.11121736Pubmed2000Mitochondrial tRNA import: are there distinct mechanisms?Schneider, AMarechal-Drouard, LTrends Cell Biol 10:509-13inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510184853Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10184853ReactomeR-SSC-3797241Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-379724.1tRNA synthetases catalyze the ligation of tRNAs to their cognate amino acids in an ATP-dependent manner. The reaction proceeds in two steps. First, amino acid and ATP form an aminoacyl adenylate molecule, releasing pyrophosphate. The aminoacyl adenylate remains associated with the synthetase enzyme where, in the second step it reacts with tRNA to form aminoacyl tRNA and AMP. The rapid hydrolysis of pyrophosphate makes these reactions essentially irreversible under physiological conditions (Fersht and Kaethner 1976a). Specificity of the tRNA charging reactions is achieved both by specific recognition of amino acid and tRNA substrates by the synthetase, and by an editing process in which incorrect aminoacyl adenylate molecules (e.g., valyl adenylate associated with isoleucyl tRNA synthetase) are hydrolyzed rather than conjugated to tRNAs in the second step of the reaction (Baldwin and Berg 1966a,b; Fersht and Kaethner 1976b). The tRNA synthetases can be divided into two structural classes based on conserved amino acid sequence features (Burnbaum and Schimmel 1991).<p>A single synthetase mediates the charging of all of the tRNA species specific for any one amino acid but, with three exceptions, glycine, lysine, and glutamine, the synthetase that catalyzes aminoacylation of mitochondrial tRNAs is encoded by a different gene than the one that acts on mitochondrial tRNAs. Both mitochondrial and cytosolic tRNA synthetase enzymes are encoded by genes in the nuclear genome.<p>A number of tRNA synthetases are known to have functions distinct from tRNA charging (reviewed by Park et al. 2005). Additionally, mutations in several of the tRNA synthetases, often affecting protein domains that are dispensable in vitro for aminoacyl tRNA synthesis, are associated with a diverse array of neurological and other diseases (Antonellis and Green 2008; Park et al. 2008). These findings raise interest into the role of these enzymes in human development and disease.<p> 5324172Pubmed1966Purification and properties of isoleucyl ribonucleic acid synthetase from Escherichia coliBaldwin, ANBerg, PJ Biol Chem 241:831-81894595Pubmed1991Structural relationships and the classification of aminoacyl-tRNA synthetasesBurbaum, JJSchimmel, PJ Biol Chem 266:16965-8182209Pubmed1976Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editingFersht, ARKaethner, MMBiochemistry 15:3342-65324173Pubmed1966Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetaseBaldwin, ANBerg, PJ Biol Chem 241:839-4518682559Pubmed2008Aminoacyl tRNA synthetases and their connections to diseasePark, SGSchimmel, PKim, SProc Natl Acad Sci U S A 105:11043-918767960Pubmed2008The role of aminoacyl-tRNA synthetases in genetic diseasesAntonellis, AnthonyGreen, EDAnnu Rev Genomics Hum Genet 9:87-107764868Pubmed1976Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthetases from Escherichia coli K12Fersht, ARKaethner, MMBiochemistry 15:818-2316125937Pubmed2005Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepersPark, SGEwalt, KLKim, STrends Biochem Sci 30:569-74inferred by electronic annotationIEAGOIEAEukaryotic Translation InitiationEukaryotic Translation InitiationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Cap-dependent Translation InitiationCap-dependent Translation InitiationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Formation of a pool of free 40S subunitsFormation of a pool of free 40S subunitsThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Release of 40S and 60S subunits from the 80S ribosome Release of 40S and 60S subunits from the 80S ribosome This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 10095039180S ribosome [cytosol]80S ribosomeReactome DB_ID: 10095037160S ribosomal complex [cytosol]60S ribosomal complexReactome DB_ID: 100948031UniProt:A0A287B3K6UniProtA0A287B3K61EQUAL196EQUALReactome DB_ID: 100948691UniProt:F2Z554RPL30UniProtF2Z5541EQUAL115EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100947611Homologues of RPL13A [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPL13A [cytosol]RPL13A [cytosol]RPL13A [cytosol]RPL13A [cytosol]RPL13A [cytosol]UniProtF1RU15UniProtF1RI01UniProtA0A287B236UniProtI3L8K3UniProtA0A287AYV7Reactome DB_ID: 100949451UniProt:A0A287A8T0RPL7UniProtA0A287A8T01EQUAL248EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100950251RPL36A,RPL36AL [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPL36A-HNRNPH2 [cytosol]UniProtA0A287AX39Reactome DB_ID: 100947191Ghost homologue of RPLP1 [cytosol]Ghost homologue of RPLP1Reactome DB_ID: 100948731UniProt:P62901RPL31UniProtP629011EQUAL125EQUALReactome DB_ID: 100948771UniProt:Q6QAT0RPL32UniProtQ6QAT02EQUAL135EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100948951Homologues of RPL34 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPL34 [cytosol]RPL34 [cytosol]RPL34 [cytosol]RPL34 [cytosol]UniProtA0A287BC35UniProtA0A286ZTM2UniProtA0A286ZN91UniProtA0A287AZ69Reactome DB_ID: 100947951UniProt:A0A287A764UniProtA0A287A7642EQUAL188EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100947871Homologues of RPL15 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPL15 [cytosol]RPL15 [cytosol]RPL15 [cytosol]RPL15 [cytosol]RPL15 [cytosol]UniProtA0A286ZLU9UniProtA0A286ZNS5UniProtI3LPJ2UniProtI3L623UniProtA0A287AAQ2Reactome DB_ID: 100949591Ghost homologue of 5.8S rRNA [cytosol]Ghost homologue of 5.8S rRNAConverted from EntitySet in ReactomeReactome DB_ID: 100948531Homologues of RPL27 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPL27 [cytosol]RPL27 [cytosol]UniProtA0A287A613UniProtA0A287ARE0Reactome DB_ID: 100948571UniProt:A0A287BLX6UniProtA0A287BLX62EQUAL148EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100947171Homologues of RPLP0 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPLP0 [cytosol]RPLP0 [cytosol]UniProtA0A287A934UniProtA0A287AEL4Reactome DB_ID: 100948651UniProt:Q95281RPL29UniProtQ952812EQUAL159EQUALReactome DB_ID: 100947311UniProt:A0A287BQI9UniProtA0A287BQI92EQUAL178EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100950151RPL3,RPL3L [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityReactome DB_ID: 100948991UniProt:Q29361RPL35UniProtQ293612EQUAL123EQUALReactome DB_ID: 100948611UniProt:A0A287AJT7RPL28UniProtA0A287AJT72EQUAL137EQUALReactome DB_ID: 100947231UniProt:F1RYZ0RPLP2UniProtF1RYZ01EQUAL115EQUALReactome DB_ID: 100947391UniProt:I3LSD3RPL13UniProtI3LSD31EQUAL211EQUALReactome DB_ID: 100949471Ghost homologue of RPL7A [cytosol]Ghost homologue of RPL7AConverted from EntitySet in ReactomeReactome DB_ID: 100948391Homologues of RPL23A [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPL23A [cytosol]RPL23A [cytosol]UniProtF2Z522UniProtA0A286ZL51Reactome DB_ID: 100949571Ghost homologue of 5S rRNA [cytosol]Ghost homologue of 5S rRNAReactome DB_ID: 100948431UniProt:A0A287A286UniProtA0A287A2861EQUAL157EQUALReactome DB_ID: 100949411UniProt:Q2YGT9UniProtQ2YGT92EQUAL288EQUALReactome DB_ID: 100947991UniProt:A0A287APR1RPL18AUniProtA0A287APR11EQUAL176EQUALReactome DB_ID: 100947271UniProt:F1RS60LOC100627129UniProtF1RS602EQUAL217EQUALReactome DB_ID: 100949251UniProt:F2Z568UniProtF2Z5682EQUAL70EQUALReactome DB_ID: 100949331Ghost homologue of RPL41 [cytosol]Ghost homologue of RPL41Converted from EntitySet in ReactomeReactome DB_ID: 100950351RPL39,RPL39L [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPL39 [cytosol]UniProtK7GP63Converted from EntitySet in ReactomeReactome DB_ID: 100950091RPL26,RPL26L1 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPL26 [cytosol]UniProtI3L7Y1Reactome DB_ID: 100949171UniProt:A0A287AX59UniProtA0A287AX592EQUAL97EQUALReactome DB_ID: 100949371UniProt:I3LS96UniProtI3LS962EQUAL297EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100948251Homologues of RPL21 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPL21 [cytosol]RPL21 [cytosol]RPL21 [cytosol]RPL21 [cytosol]RPL21 [cytosol]UniProtA0A287BH72UniProtA0A286ZR43UniProtA0A287BJC2UniProtA0A287AF12UniProtA0A287BBU4Converted from EntitySet in ReactomeReactome DB_ID: 100949991RPL22,RPL22L1 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPL22 [cytosol]UniProtP67985Converted from EntitySet in ReactomeReactome DB_ID: 100949891RPL10,RPL10L [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPL10 [cytosol]RPL10 [cytosol]RPL10 [cytosol]RPL10 [cytosol]RPL10 [cytosol]UniProtA0A287BNK6UniProtA0A287AEX9UniProtA0A287BCG0UniProtA0A286ZXC3UniProtA0A287AKX5Reactome DB_ID: 100949511UniProt:F2Z567RPL8UniProtF2Z5672EQUAL257EQUALReactome DB_ID: 100949131UniProt:A0A287A284UniProtA0A287A2842EQUAL105EQUALReactome DB_ID: 100949551UniProt:I3LP78UniProtI3LP781EQUAL192EQUALReactome DB_ID: 100949611Ghost homologue of 28S rRNA [cytosol]Ghost homologue of 28S rRNAReactome DB_ID: 100949311UniProt:P63053UniProtP6305377EQUAL128EQUALReactome DB_ID: 100947351UniProt:A0A287AJH8RPL12UniProtA0A287AJH81EQUAL165EQUALReactome DB_ID: 100949291UniProt:A0A287A9X4RPL4UniProtA0A287A9X42EQUAL427EQUALReactome DB_ID: 100947651UniProt:A0A286ZW72RPL14UniProtA0A286ZW722EQUAL215EQUALReactome DB_ID: 100948291UniProt:P62831RPL23UniProtP628311EQUAL140EQUALReactome DB_ID: 100947911UniProt:A0A287B386UniProtA0A287B3862EQUAL184EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100949091Homologues of RPL35A [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPL35A [cytosol]RPL35A [cytosol]UniProtA0A287A6D6UniProtA0A286ZQQ1Reactome DB_ID: 100949211UniProt:A0A287AME4RPL37AUniProtA0A287AME42EQUAL92EQUALReactome Database ID Release 7510095037Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10095037ReactomeR-SSC-724991Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72499.1Reactome DB_ID: 10094572140S ribosomal complex [cytosol]40S ribosomal complexReactome DB_ID: 100943421UniProt:F1RZ28UniProtF1RZ281EQUAL165EQUALReactome DB_ID: 100943461UniProt:F2Z4Y8RPS11UniProtF2Z4Y82EQUAL158EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100944801Homologues of RPS29 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPS29 [cytosol]RPS29 [cytosol]RPS29 [cytosol]RPS29 [cytosol]RPS29 [cytosol]UniProtI3LJY0UniProtA0A286ZUU5UniProtA0A286ZPL8UniProtF1SJZ7UniProtI3L8K5Reactome DB_ID: 100945201UniProt:A0A287A9Y6RPS7UniProtA0A287A9Y61EQUAL194EQUALReactome DB_ID: 100944541UniProt:A0A287AZA7RPS27AUniProtA0A287AZA777EQUAL156EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100943601Homologues of RPS13 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPS13 [cytosol]RPS13 [cytosol]UniProtI3L7A9UniProtA0A287AKU2Reactome DB_ID: 100943701UniProt:Q29201RPS16UniProtQ292012EQUAL146EQUALReactome DB_ID: 100944481UniProt:A0A287BH92UniProtA0A287BH921EQUAL125EQUALReactome DB_ID: 100945041Ghost homologue of FAU [cytosol]Ghost homologue of FAUReactome DB_ID: 100945261Ghost homologue of RPS9 [cytosol]Ghost homologue of RPS9Reactome DB_ID: 100944001UniProt:A0A287ADE6RPS15AUniProtA0A287ADE62EQUAL130EQUALReactome DB_ID: 100944041UniProt:I3LJ87RPS2UniProtI3LJ871EQUAL293EQUALReactome DB_ID: 100943741UniProt:Q6QAP7RPS17UniProtQ6QAP72EQUAL135EQUALReactome DB_ID: 100944581UniProt:Q6QAT1RPS28UniProtQ6QAT11EQUAL69EQUALReactome DB_ID: 100943661UniProt:P62844RPS15UniProtP628442EQUAL145EQUALReactome DB_ID: 100943621Ghost homologue of RPS14 [cytosol]Ghost homologue of RPS14Reactome DB_ID: 100944441UniProt:A0A287ACL6RPS24UniProtA0A287ACL61EQUAL133EQUALReactome DB_ID: 100945241UniProt:F2Z5F5RPS8UniProtF2Z5F52EQUAL208EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100945641RPS27,RPS27L [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPS27 [cytosol]UniProtA0A287BF06Reactome DB_ID: 100943781UniProt:P62272UniProtP622722EQUAL152EQUALReactome DB_ID: 100944521UniProt:A0A286ZJN3UniProtA0A286ZJN32EQUAL115EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100945521Homologues of RPSA [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPSA [cytosol]RPSA [cytosol]RPSA [cytosol]RPSA [cytosol]RPSA [cytosol]RPSA [cytosol]UniProtA0A287A252UniProtA0A287BE17UniProtA0A287BSF8UniProtI3LC48UniProtA0A287A7F1UniProtA0A287ALW1Reactome DB_ID: 100945081UniProt:F2Z5C7RPS3AUniProtF2Z5C72EQUAL264EQUALReactome DB_ID: 100945681UniProt:F1RQ91RPS4XUniProtF1RQ912EQUAL263EQUALReactome DB_ID: 100945541Ghost homologue of 18S rRNA [cytosol]Ghost homologue of 18S rRNAReactome DB_ID: 100943501UniProt:P46405RPS12UniProtP464052EQUAL132EQUALReactome DB_ID: 100945161UniProt:F2Z5Q6RPS6UniProtF2Z5Q61EQUAL249EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100944401Homologues of RPS23 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPS23 [cytosol]RPS23 [cytosol]RPS23 [cytosol]RPS23 [cytosol]RPS23 [cytosol]UniProtA0A286ZLV4UniProtA0A286ZS50UniProtA0A287AQL0UniProtI3LMI4UniProtA0A287BPZ3Reactome DB_ID: 100945121UniProt:A0A287AKC0RPS5UniProtA0A287AKC01EQUAL204EQUALReactome DB_ID: 100944081UniProt:A0A287BQP4RPS20UniProtA0A287BQP42EQUAL119EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100944181Homologues of RPS21 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPS21 [cytosol]RPS21 [cytosol]UniProtA0A287B4K2UniProtP63221Converted from EntitySet in ReactomeReactome DB_ID: 100945021Homologues of RPS3 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityRPS3 [cytosol]RPS3 [cytosol]RPS3 [cytosol]RPS3 [cytosol]RPS3 [cytosol]UniProtA0A287BHK7UniProtA0A286ZUY6UniProtA0A287BLJ0UniProtA0A287BK95UniProtA0A286ZUY4Converted from EntitySet in ReactomeReactome DB_ID: 100943961Homologues of RPS19 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityLOC100623742 [cytosol]RPS19 [cytosol]RPS19 [cytosol]RPS19 [cytosol]UniProtI3LQK3UniProtA0A287B7V4UniProtA0A287B1M2UniProtA0A287ASG4Reactome Database ID Release 7510094572Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094572ReactomeR-SSC-723921Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72392.1Reactome Database ID Release 7510095039Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10095039ReactomeR-SSC-725001Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72500.1Reactome DB_ID: 100946301UniProt:A0A287AKZ5EIF1AXUniProtA0A287AKZ51EQUAL144EQUALReactome DB_ID: 100950371Reactome DB_ID: 100945721Reactome DB_ID: 1009463011EQUAL144EQUALReactome Database ID Release 7510095057Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10095057ReactomeR-SSC-726731Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72673.180S monosomes dissociate into 40S and 60S ribosomal subunits. eIF1A promotes this dissociation.9780879696184ISBN2001Pathway and mechanism of initiation of protein synthesis.Hershey, John W BMerrick, William CTranslational Control of Gene Expression (Book): 33-88inferred by electronic annotationIEAGOIEAeIF3 and eIF1A bind to the 40S subuniteIF3 and eIF1A bind to the 40S subunitThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 1009463011EQUAL144EQUALReactome DB_ID: 100946261eIF3 subunits complex [cytosol]eIF3 subunits complexReactome DB_ID: 100946081UniProt:A0A286ZP85UniProtA0A286ZP851EQUAL913EQUALReactome DB_ID: 100946241UniProt:F1SGR0EIF3MUniProtF1SGR02EQUAL374EQUALReactome DB_ID: 100946201UniProt:A0A287AL05EIF3LUniProtA0A287AL052EQUAL564EQUALReactome DB_ID: 100946041UniProt:F1SKJ5EIF3DUniProtF1SKJ51EQUAL548EQUALReactome DB_ID: 100945921UniProt:M3TYC1EIF3BUniProtM3TYC11EQUAL814EQUALReactome DB_ID: 100946121UniProt:F1S1G0EIF3EUniProtF1S1G02EQUAL445EQUALReactome DB_ID: 100945961UniProt:A0A287BR32EIF3HUniProtA0A287BR321EQUAL352EQUALReactome DB_ID: 100945761UniProt:F1SN05EIF3JUniProtF1SN052EQUAL258EQUALReactome DB_ID: 100945881UniProt:A0A287ARI1EIF3FUniProtA0A287ARI12EQUAL357EQUALReactome DB_ID: 100946001UniProt:F1S4P6EIF3AUniProtF1S4P62EQUAL1382EQUALReactome DB_ID: 100945841UniProt:F1S3I3EIF3GUniProtF1S3I32EQUAL320EQUALReactome DB_ID: 100945801UniProt:F1SV90EIF3IUniProtF1SV901EQUAL325EQUALReactome DB_ID: 100946161UniProt:F1RI41EIF3KUniProtF1RI412EQUAL218EQUALReactome Database ID Release 7510094626Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094626ReactomeR-SSC-725551Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72555.1Reactome DB_ID: 100945721Reactome DB_ID: 10095059140S:eIF3:eIF1A [cytosol]40S:eIF3:eIF1AReactome DB_ID: 100945721Reactome DB_ID: 100946261Reactome DB_ID: 1009463011EQUAL144EQUALReactome Database ID Release 7510095059Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10095059ReactomeR-SSC-725701Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72570.1Reactome Database ID Release 7510095061Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10095061ReactomeR-SSC-726761Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72676.1eIF3 and eIF1A bind to the 40S ribosomal subunit. 6901506Pubmed1980The role of eIF-4C in protein synthesis initiation complex formation.Goumans, HThomas, AVerhoeven, AVoorma, HOBenne, RBiochim Biophys Acta 608:39-46641056Pubmed1978The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes.Benne, RHershey, John WJ Biol Chem 253:3078-87592399Pubmed1978Initiation of mammalian protein synthesis. II. The assembly of the initiation complex with purified initiation factors.Trachsel, HErni, BSchreier, MHStaehelin, TJ Mol Biol 116:755-67429297Pubmed1979Binding and release of radiolabeled eukaryotic initiation factors 2 and 3 during 80 S initiation complex formation.Peterson, DTMerrick, William CSafer, BJ Biol Chem 254:2509-1612493757Pubmed2003Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40 S preinitiation complex.Majumdar, RBandyopadhyay, AMaitra, UJ Biol Chem 278:6580-7inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510184883Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10184883ReactomeR-SSC-726891Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72689.1The 80S ribosome dissociates into free 40S (small) and 60S (large) ribosomal subunits. Each ribosomal subunit is constituted by several individual ribosomal proteins and rRNA.inferred by electronic annotationIEAGOIEAActivation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43SActivation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43SThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Release of eIF4E from the inactive eIF4E:4E-BP complex Release of eIF4E from the inactive eIF4E:4E-BP complex This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 100946941eIF4E:4E-BP [cytosol]eIF4E:4E-BPReactome DB_ID: 100946641UniProt:F1S0B9EIF4EUniProtF1S0B92EQUAL217EQUALReactome DB_ID: 100946921UniProt:I3L6D8EIF4EBP1UniProtI3L6D82EQUAL118EQUALReactome Database ID Release 7510094694Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094694ReactomeR-SSC-725811Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72581.1Reactome DB_ID: 1009466412EQUAL217EQUALReactome DB_ID: 1009469212EQUAL118EQUALReactome Database ID Release 7510094696Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094696ReactomeR-SSC-726221Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72622.1eIF4E gets released from the inactive eIF4E:4EBP complex. 7935836Pubmed1994Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function.Pause, ABelsham, GJGingras, ACDonzé, OLin, TALawrence, JCSonenberg, NahumNature 371:762-7inferred by electronic annotationIEAGOIEAFormation of the cap-binding eIF4F complexFormation of the cap-binding eIF4F complexThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 1009466412EQUAL217EQUALReactome DB_ID: 100946681UniProt:A0A287A1Z9UniProtA0A287A1Z91EQUAL1599EQUALReactome DB_ID: 100946601eIF4A subunits complex [cytosol]eIF4A subunits complexReactome DB_ID: 100946581UniProt:A6M930EIF4A2UniProtA6M9301EQUAL407EQUALReactome DB_ID: 100946541UniProt:A6M928EIF4A1UniProtA6M9282EQUAL406EQUALReactome Database ID Release 7510094660Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094660ReactomeR-SSC-725761Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72576.1Reactome DB_ID: 100946701eIF4F [cytosol]eIF4FReactome DB_ID: 1009466412EQUAL217EQUALReactome DB_ID: 1009466811EQUAL1599EQUALReactome DB_ID: 100946601Reactome Database ID Release 7510094670Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094670ReactomeR-SSC-725871Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72587.1Reactome Database ID Release 7510094698Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094698ReactomeR-SSC-726311Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72631.1eIF4A interacts with eIF4G, and eIF4E interacts with the amino-terminal domain of eIF4G to form the cap-binding complex eIF4F.8449919Pubmed1993The p46 subunit of eukaryotic initiation factor (eIF)-4F exchanges with eIF-4A.Yoder-Hill, JPause, ASonenberg, NahumMerrick, William CJ Biol Chem 268:5566-73inferred by electronic annotationIEAGOIEA3.6.4.13Cap-bound mRNA is activated by helicases Cap-bound mRNA is activated by helicases This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 100946741UniProt:A0A287BJS1UniProtA0A287BJS11EQUAL611EQUALReactome DB_ID: 100946781UniProt:I3LRD5EIF4HUniProtI3LRD52EQUAL248EQUALReactome DB_ID: 100947021eIF4F:mRNP [cytosol]eIF4F:mRNPReactome DB_ID: 100946701Reactome DB_ID: 100947001mRNP [cytosol]mRNPReactome DB_ID: 100946501Ghost homologue of mRNA [cytosol]Ghost homologue of mRNAReactome DB_ID: 725951RNA-binding protein in RNP (ribonucleoprotein) complexes [cytosol]RNA-binding protein in RNP (ribonucleoprotein) complexesReactome Database ID Release 7510094700Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094700ReactomeR-SSC-725961Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72596.1Reactome Database ID Release 7510094702Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094702ReactomeR-SSC-725971Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72597.1Reactome DB_ID: 100946601Reactome DB_ID: 1135921ATP(4-) [ChEBI:30616]ATP(4-)Adenosine 5'-triphosphateatpATPChEBI30616Reactome DB_ID: 100947041mRNA:eIF4F:eIF4B:eIF4H [cytosol]mRNA:eIF4F:eIF4B:eIF4HReactome DB_ID: 100946701Reactome DB_ID: 1009467411EQUAL611EQUALReactome DB_ID: 1009467812EQUAL248EQUALReactome DB_ID: 100946501Reactome Database ID Release 7510094704Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094704ReactomeR-SSC-725931Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72593.1Reactome DB_ID: 293701ADP(3-) [ChEBI:456216]ADP(3-)ADP trianion5&apos;-O-[(phosphonatooxy)phosphinato]adenosineADPChEBI456216Reactome DB_ID: 725951Reactome DB_ID: 100946601Reactome DB_ID: 293721PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 10094660GO0003724GO molecular functionReactome Database ID Release 7510094705Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094705Reactome Database ID Release 7510094707Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094707ReactomeR-SSC-726471Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72647.1The DEAD-box RNA helicase eIF4A, together with the RNA-binding proteins eIF4B or eIF4H, is thought to unwind RNA secondary structures near the 5'-end of the mRNA and in the presence of ATP. 6853548Pubmed1983New initiation factor activity required for globin mRNA translation.Grifo, JATahara, SMMorgan, MAShatkin, AJMerrick, William CJ Biol Chem 258:5804-10inferred by electronic annotationIEAGOIEATranslation initiation complex formationTranslation initiation complex formationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Formation of translation initiation complexes containing mRNA that does not circularizeFormation of translation initiation complexes containing mRNA that does not circularizeThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 10094648143S complex [cytosol]43S complexReactome DB_ID: 100946461ternary complex [cytosol]ternary complexReactome DB_ID: 100946441eIF2:GTP [cytosol]eIF2:GTPReactome DB_ID: 294381GTP [ChEBI:15996]GTPGuanosine 5'-triphosphateChEBI15996Reactome DB_ID: 100946421EIF2S1:EIF2S2:EIF2S3 [cytosol]EIF2S1:EIF2S2:EIF2S3Reactome DB_ID: 100946361UniProt:F1S4Y8EIF2S2UniProtF1S4Y82EQUAL333EQUALReactome DB_ID: 100946321Ghost homologue of EIF2S1 [cytosol]Ghost homologue of EIF2S1Reactome DB_ID: 100946401UniProt:F1SPY4LOC100624149UniProtF1SPY42EQUAL472EQUALReactome Database ID Release 7510094642Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094642ReactomeR-SSC-725151Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72515.1Reactome Database ID Release 7510094644Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094644ReactomeR-SSC-725311Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72531.1Reactome DB_ID: 723931Met-tRNAi [cytosol]Met-tRNAimethionyl initiator tRNAMet-tRNAffMet-tRNAReactome Database ID Release 7510094646Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094646ReactomeR-SSC-725321Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72532.1Reactome DB_ID: 100945721Reactome DB_ID: 100946261Reactome DB_ID: 1009463011EQUAL144EQUALReactome Database ID Release 7510094648Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094648ReactomeR-SSC-725711Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72571.1Reactome DB_ID: 100947041Reactome DB_ID: 1009463011EQUAL144EQUALReactome DB_ID: 1009463011EQUAL144EQUALReactome DB_ID: 10094680148S complex [cytosol]48S complexReactome DB_ID: 100946481Reactome DB_ID: 100946701Reactome DB_ID: 1009467411EQUAL611EQUALReactome DB_ID: 1009467812EQUAL248EQUALReactome DB_ID: 100946501Reactome Database ID Release 7510094680Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094680ReactomeR-SSC-725941Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72594.1Reactome Database ID Release 7510100483Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100483ReactomeR-SSC-1578491Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-157849.1The translation initiation complex forms when the 43S complex binds the mRNA that is associated with eIF4F, eIF4B and eIF4H. eIF4G in the eIF4F complex can directly contact eIF3 in the 43S complex. eIF1A is necessary for the formation of this complex.9732867Pubmed1999Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons.Pestova, TVBorukhov, SIHellen, CUNature 394:854-9inferred by electronic annotationIEAGOIEAFormation of translation initiation complexes yielding circularized Ceruloplasmin mRNA in a 'closed-loop' conformationFormation of translation initiation complexes yielding circularized Ceruloplasmin mRNA in a 'closed-loop' conformationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 100946481Reactome DB_ID: 1009463011EQUAL144EQUALReactome DB_ID: 101004041Ceruloplasmin mRNA:eIF4F:eIF4B:eIF4H [cytosol]Ceruloplasmin mRNA:eIF4F:eIF4B:eIF4HReactome DB_ID: 101004021Ghost homologue of Ceruloplasmin mRNA [cytosol]Ghost homologue of Ceruloplasmin mRNAReactome DB_ID: 100946701Reactome DB_ID: 1009467411EQUAL611EQUALReactome DB_ID: 1009467812EQUAL248EQUALReactome Database ID Release 7510100404Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100404ReactomeR-SSC-1568091Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156809.1Reactome DB_ID: 101004081UniProt:F2Z557PABPC1UniProtF2Z5571EQUAL636EQUALReactome DB_ID: 10100410143S: Ceruloplasmin mRNA:eIF4F:eIF4B:eIF4H:PABP [cytosol]43S: Ceruloplasmin mRNA:eIF4F:eIF4B:eIF4H:PABPReactome DB_ID: 101004021Reactome DB_ID: 100946481Reactome DB_ID: 100946701Reactome DB_ID: 1009467411EQUAL611EQUALReactome DB_ID: 1010040811EQUAL636EQUALReactome DB_ID: 1009467812EQUAL248EQUALReactome Database ID Release 7510100410Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100410ReactomeR-SSC-1568041Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156804.1Reactome DB_ID: 1009463011EQUAL144EQUALReactome Database ID Release 7510100412Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100412ReactomeR-SSC-1568081Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156808.1The precise order of events leading to the circularization of poly (A) mRNA during translation initiation is unknown. Here the association of PABP with the poly (A) mRNA and the association of PABP with eIF4F are represented as occuring simultaneously after formation of the initiation complex. However, it is also possible that these interactions occur during the formation of the translation initiation complex. The binding of eIF4F to the cap and binding of PABP to the poly (A) tail, for example, may occur at the same time. In fact, the eIF4G-PABP interaction helps eIF4F to bind tighter to the cap (Borman et al. 2000.) In addition, eIF4B and eIF4H bind more transiently to the mRNA and may not be part of an initial complex in which PABP has not yet touched eIF4G.9857202Pubmed1998A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translationImataka, HGradi, ASonenberg, NahumEMBO J 17:7480-911058101Pubmed2000Biochemical characterisation of cap-poly(A) synergy in rabbit reticulocyte lysates: the eIF4G-PABP interaction increases the functional affinity of eIF4E for the capped mRNA 5'-endBorman, AMMichel, YMKean, KMNucleic Acids Res 28:4068-75inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510185329Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10185329ReactomeR-SSC-726491Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72649.1The translation initiation complex forms when the 43S complex binds the mRNA that is associated with eIF4F, eIF4B and eIF4H. eIF4G in the eIF4F complex can directly contact eIF3 in the 43S complex. eIF1A is necessary for the formation of this complex.inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510184879Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10184879ReactomeR-SSC-726621Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72662.1The cap-binding complex is constituted by the initiation factors eIF4A, eIF4G and eIF4E. First, eIF4E must be released from the inactive eIF4E:4E-BP complex. Then eIF4A interacts with eIF4G, and eIF4E binds to the amino-terminal domain of eIF4G, resulting in the formation of the cap-binding complex eIF4F. eIF4A together with eIF4B or eIF4H is thought to unwind RNA secondary structures near the 5'-end of the mRNA. The translation initiation complex is formed when the 43S complex binds the cap-bound mRNA.inferred by electronic annotationIEAGOIEARibosomal scanning and start codon recognitionRibosomal scanning and start codon recognitionThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Ribosomal scanning Ribosomal scanning This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 100946801Reactome DB_ID: 1135921Reactome DB_ID: 293701Reactome DB_ID: 100946801Reactome DB_ID: 293721PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 72617eIF1 [cytosol]eIF1translation initiation factor 1eIF-1GO0003743GO molecular functionReactome Database ID Release 7572620Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=72620Reactome Database ID Release 7510094688Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094688ReactomeR-SSC-726211Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72621.1The mRNA-bound ribosomal complex moves along the 5'-untranslated region (5'-UTR) of the mRNA from its initial site to the initiation codon to form a 48S complex, in which the initiation codon (AUG) is base paired to the anticodon of the Met-tRNAi. It is not known whether eIF4A (or another ATPase, such as DED1) facilitates scanning by melting mRNA secondary structures or by actively propelling the ribosome.10364207Pubmed1999Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase.Iost, IDreyfus, MLinder, PJ Biol Chem 274:17677-839045610Pubmed1997Requirement of the DEAD-Box protein ded1p for messenger RNA translation.Chuang, RYWeaver, PLLiu, ZChang, THScience 275:1468-717000367Pubmed1981Evaluation of the "scanning model" for initiation of protein synthesis in eucaryotes.Kozak, MCell 22:7-88943342Pubmed1997Functional dissection of eukaryotic initiation factor 4F: the 4A subunit and the central domain of the 4G subunit are sufficient to mediate internal entry of 43S preinitiation complexes.Pestova, TVShatsky, INHellen, CUMol Cell Biol 16:6870-8inferred by electronic annotationIEAGOIEAACTIVATIONReactome Database ID Release 7572781Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=72781ReactomeR-HSA-727811Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-72781.1Reactome DB_ID: 113592Reactome Database ID Release 7510184873Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10184873ReactomeR-SSC-727021Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72702.1The 80S ribosome bound to the mRNA moves along the mRNA molecule from its initial site to the initiation codon and forms a 48S complex, in which the initiation codon is base paired to the anticodon of the Met-tRNAi. Proper recognition of the AUG initiation codon depends on base pairing with the anticodon of the Met-tRNAi and requires eIF1, eIF1A, eIF2 and eIF5.9780879696184ISBN2001Genetic approaches to translation initiation in Saccharomyces cerevisiae.Donahue, TFTranslational Control of Gene Expression (Book): 487-502inferred by electronic annotationIEAGOIEAGTP hydrolysis and joining of the 60S ribosomal subunitGTP hydrolysis and joining of the 60S ribosomal subunitThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>eIF5B:GTP is hydrolyzed and releasedeIF5B:GTP is hydrolyzed and releasedThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 10095047180S:Met-tRNAi:mRNA:eIF5B:GTP [cytosol]80S:Met-tRNAi:mRNA:eIF5B:GTPReactome DB_ID: 100950391Reactome DB_ID: 723931Reactome DB_ID: 100946501Reactome DB_ID: 100950451eIF5B:GTP [cytosol]eIF5B:GTPReactome DB_ID: 100950431UniProt:I3L8K4UniProtI3L8K41EQUAL1220EQUALReactome DB_ID: 294381Reactome Database ID Release 7510095045Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10095045ReactomeR-SSC-725031Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72503.1Reactome Database ID Release 7510095047Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10095047ReactomeR-SSC-725041Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72504.1Reactome DB_ID: 10095051180S:Met-tRNAi:mRNA [cytosol]80S:Met-tRNAi:mRNAReactome DB_ID: 100950391Reactome DB_ID: 723931Reactome DB_ID: 100946501Reactome Database ID Release 7510095051Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10095051ReactomeR-SSC-725051Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72505.1Reactome DB_ID: 100950491eIF5B:GDP [cytosol]eIF5B:GDPReactome DB_ID: 1009504311EQUAL1220EQUALReactome DB_ID: 294201GDP [ChEBI:17552]GDPGuanosine 5'-diphosphateGuanosine diphosphateChEBI17552Reactome Database ID Release 7510095049Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10095049ReactomeR-SSC-725021Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72502.1Reactome DB_ID: 293721Reactome Database ID Release 7510095053Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10095053ReactomeR-SSC-726711Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72671.1Once the 60S subunit joins the translation initiation complex, eIF5B hydrolyzes its GTP and is released from the now 80S monosome. The fully assembled 80s ribosome is now ready to start elongation of the polypeptide chain.1095581Pubmed1975Purification and characterization of homogeneous initiation factor M2A from rabbit reticulocytes.Merrick, William CKemper, WMAnderson, WFJ Biol Chem 250:5556-6210659855Pubmed2000The joining of ribosomal subunits in eukaryotes requires eIF5B.Pestova, TVLomakin, IBLee, JHChoi, SKDever, TEHellen, CUNature 403:332-5inferred by electronic annotationIEAGOIEAThe 60S subunit joins the translation initiation complex The 60S subunit joins the translation initiation complex This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 100950371Reactome DB_ID: 10094686140S:Met-tRNAi:mRNA [cytosol]40S:Met-tRNAi:mRNAReactome DB_ID: 723931Reactome DB_ID: 100945721Reactome DB_ID: 100946501Reactome Database ID Release 7510094686Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10094686ReactomeR-SSC-725081Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72508.1Reactome DB_ID: 100950451Reactome DB_ID: 100950471Reactome Database ID Release 7510095055Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10095055ReactomeR-SSC-726721Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72672.1Joining of the 60S subunit to form the 80S ribosome is catalyzed by the presence of GTP-bound eIF5B. 592398Pubmed1978Initiation of mammalian protein synthesis. I. Purification and characterization of seven initiation factors.Schreier, MHErni, BStaehelin, TJ Mol Biol 116:727-53inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510184881Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10184881ReactomeR-SSC-727061Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72706.1Hydrolysis of eIF2-GTP occurs after the Met-tRNAi has recognized the AUG. This reaction is catalyzed by eIF5 (or eIF5B) and is thought to cause dissociation of all other initiation factors and allow joining of the large 60S ribosomal subunit. The 60S subunit joins - a reaction catalyzed by eIF5 or eIF5B - resulting in a translation-competent 80S ribosome. Following 60S subunit joining, eIF5B hydrolyzes its GTP and is released from the 80S ribosome, which is now ready to start elongating the polypeptide chain.1856230Pubmed1991Function of eukaryotic initiation factor 5 in the formation of an 80 S ribosomal polypeptide chain initiation complex.Chakrabarti, AMaitra, UJ Biol Chem 266:14039-4511018020Pubmed2000A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo.Asano, KClayton, JShalev, AHinnebusch, Alan GGenes Dev 14:2534-46inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510184875Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10184875ReactomeR-SSC-727371Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72737.1Translation initiation is a complex process in which the Met-tRNAi initiator, 40S, and 60S ribosomal subunits are assembled by eukaryotic initiation factors (eIFs) into an 80S ribosome at the start codon of an mRNA. The basic mechanism for this process can be described as a series of five steps: 1) formation of a pool of free 40S subunits, 2) formation of the ternary complex (Met-tRNAi/eIF2/GTP), and subsequently, the 43S complex (comprising the 40S subunit, Met-tRNAi/eIF2/GTP, eIF3 and eIF1A), 3) activation of the mRNA upon binding of the cap-binding complex eIF4F, and factors eIF4A, eIF4B and eIF4H, with subsequent binding to the 43S complex, 4) ribosomal scanning and start codon recognition, and 5) GTP hydrolysis and joining of the 60S ribosomal subunit.inferred by electronic annotationIEAGOIEAL13a-mediated translational silencing of Ceruloplasmin expressionL13a-mediated translational silencing of Ceruloplasmin expressionThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Dissociation of L13a from the 60s ribosomal subunitDissociation of L13a from the 60s ribosomal subunitThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 100950371Converted from EntitySet in ReactomeReactome DB_ID: 100947611Reactome DB_ID: 10100435160s ribosomal complex lacking L13a subunit [cytosol]60s ribosomal complex lacking L13a subunitReactome DB_ID: 1009480311EQUAL196EQUALReactome DB_ID: 1009486911EQUAL115EQUALReactome DB_ID: 1009494511EQUAL248EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100950251Reactome DB_ID: 100947191Reactome DB_ID: 1009487311EQUAL125EQUALReactome DB_ID: 1009487712EQUAL135EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100948951Reactome DB_ID: 1009479512EQUAL188EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100947871Reactome DB_ID: 100949591Converted from EntitySet in ReactomeReactome DB_ID: 100948531Reactome DB_ID: 1009485712EQUAL148EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100947171Reactome DB_ID: 1009486512EQUAL159EQUALReactome DB_ID: 1009473112EQUAL178EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100950151Reactome DB_ID: 1009489912EQUAL123EQUALReactome DB_ID: 1009486112EQUAL137EQUALReactome DB_ID: 1009472311EQUAL115EQUALReactome DB_ID: 1009473911EQUAL211EQUALReactome DB_ID: 100949471Converted from EntitySet in ReactomeReactome DB_ID: 100948391Reactome DB_ID: 100949571Reactome DB_ID: 1009484311EQUAL157EQUALReactome DB_ID: 1009494112EQUAL288EQUALReactome DB_ID: 1009479911EQUAL176EQUALReactome DB_ID: 1009472712EQUAL217EQUALReactome DB_ID: 1009492512EQUAL70EQUALReactome DB_ID: 100949331Converted from EntitySet in ReactomeReactome DB_ID: 100950351Converted from EntitySet in ReactomeReactome DB_ID: 100950091Reactome DB_ID: 1009491712EQUAL97EQUALReactome DB_ID: 1009493712EQUAL297EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100948251Converted from EntitySet in ReactomeReactome DB_ID: 100949991Converted from EntitySet in ReactomeReactome DB_ID: 100949891Reactome DB_ID: 1009495112EQUAL257EQUALReactome DB_ID: 1009491312EQUAL105EQUALReactome DB_ID: 1009495511EQUAL192EQUALReactome DB_ID: 100949611Reactome DB_ID: 10094931177EQUAL128EQUALReactome DB_ID: 1009473511EQUAL165EQUALReactome DB_ID: 1009492912EQUAL427EQUALReactome DB_ID: 1009476512EQUAL215EQUALReactome DB_ID: 1009482911EQUAL140EQUALReactome DB_ID: 1009479112EQUAL184EQUALConverted from EntitySet in ReactomeReactome DB_ID: 100949091Reactome DB_ID: 1009492112EQUAL92EQUALReactome Database ID Release 7510100435Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100435ReactomeR-SSC-1568171Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156817.1Reactome Database ID Release 7510100437Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100437ReactomeR-SSC-1568261Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156826.1The L13a subunit of the 60s ribosome is phosphorylated about 16 hours after INF gamma induction by an unknown kinase. At this time, L13a is also released from the 60s subunit (Mazumder et al.,2003). It is unclear, however, whether phosphorylation occurs before or after the release of L13a. Here, phosphorylation is shown as occurring after release.14567916Pubmed2003Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational controlMazumder, BSampath, PSeshadri, VMaitra, RKDiCorleto, PEFox, PLCell 115:187-98inferred by electronic annotationIEAGOIEAAssociation of phospho-L13a with GAIT element of Ceruloplasmin mRNAAssociation of phospho-L13a with GAIT element of Ceruloplasmin mRNAThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Converted from EntitySet in ReactomeReactome DB_ID: 101004291Homologues of p-RPL13A [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityphospho-p-RPL13A [cytosol]phospho-p-RPL13A [cytosol]phospho-p-RPL13A [cytosol]phospho-p-RPL13A [cytosol]phospho-p-RPL13A [cytosol]Reactome DB_ID: 101004101Reactome DB_ID: 101004311phospho-L13a associated wth the 3' UTR GAIT element of ceruloplasmin mRNA within the translation initiation complex [cytosol]phospho-L13a associated wth the 3' UTR GAIT element of ceruloplasmin mRNA within the translation initiation complexReactome DB_ID: 101004101Converted from EntitySet in ReactomeReactome DB_ID: 101004291Reactome Database ID Release 7510100431Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100431ReactomeR-SSC-1568241Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156824.1Reactome Database ID Release 7510100433Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100433ReactomeR-SSC-1568231Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156823.1Although the mechanism through which L13a prevents translation initiation has not been determined, Mazumder et al. (2003) have described four alternatives. L13a could (1) inhibit the function of eIF4F, (2) block the recruitment of the 43S preinitiation complex, (3) prevent scanning of the 43S complex to the initiation codon, or 4) interfere with joining of the 60S ribosomal subunit.12588972Pubmed2003Transcript-selective translational silencing by gamma interferon is directed by a novel structural element in the ceruloplasmin mRNA 3' untranslated regionSampath, PMazumder, BSeshadri, VFox, PLMol Cell Biol 23:1509-19inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510185331Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10185331ReactomeR-SSC-1568271Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156827.1While circularization of mRNA during translation initiation is thought to contribute to an increase in the efficiency of translation, it also appears to provide a mechanism for translational silencing. This might be achieved by bringing inhibitory 3' UTR-binding proteins into a position in which they interfere either with the function of the translation initiation complex or with the assembly of the ribosome (Mazumder et al 2001). Translational silencing of Ceruloplasmin (Cp) occurs 16 hrs after its induction by INF-gamma (Mazumder et al., 1997). Although the mechanism by which silencing occurs has not yet been determined, this process is mediated by the L13a subunit of the 60s ribosome and thought to require circularization of the Cp mRNA (Sampath et al., 2003; Mazumder et al., 2001; Mazumder et al., 2003). Between 14 and 16 hrs after INF gamma induction, the L13a subunit of the 60s ribosome is phosphorylated and released from the 60s subunit. Phosphorylated L13a then associates with the GAIT element in the 3' UTR of the Cp mRNA inhibiting its translation.9257859Pubmed1997Induction of ceruloplasmin synthesis by IFN-gamma in human monocytic cellsMazumder, BMukhopadhyay, CKProk, ACathcart, MKFox, PLJ Immunol 159:1938-4411533233Pubmed2001Translational silencing of ceruloplasmin requires the essential elements of mRNA circularization: poly(A) tail, poly(A)-binding protein, and eukaryotic translation initiation factor 4GMazumder, BSeshadri, VImataka, HSonenberg, NahumFox, PLMol Cell Biol 21:6440-9inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510184877Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10184877ReactomeR-SSC-726131Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72613.1GO0006413GO biological processInitiation of translation in the majority of eukaryotic cellular mRNAs depends on the 5'-cap (m7GpppN) and involves ribosomal scanning of the 5' untranslated region (5'-UTR) for an initiating AUG start codon. Therefore, this mechanism is often called cap-dependent translation initiation. Proximity to the cap, as well as the nucleotides surrounding an AUG codon, influence the efficiency of the start site recognition during the scanning process. However, if the recognition site is poor enough, scanning ribosomal subunits will ignore and skip potential starting AUGs, a phenomenon called leaky scanning. Leaky scanning allows a single mRNA to encode several proteins that differ in their amino-termini. Merrick (2010) provides an overview of this process and hghlights several features of it that remain incompletely understood.<p>Several eukaryotic cell and viral mRNAs initiate translation by an alternative mechanism that involves internal initiation rather than ribosomal scanning. These mRNAs contain complex nucleotide sequences, called internal ribosomal entry sites, where ribosomes bind in a cap-independent manner and start translation at the closest downstream AUG codon.<br> Initiation on several viral and cellular mRNAs is cap-independent and is mediated by binding of the ribosome to internal ribosome entry site (IRES) elements. These elements are often found in characteristically long structured regions on the 5'-UTR of an mRNA that may or may not have regulatory upstream open reading frames (uORFs). Both of these features on the 5'-end of the mRNA hinder ribosomal scanning, and thus promote a cap-independent translation initiation mechanism. IRESs act as specific translational enhancers that allow translation initiation to occur in response to specific stimuli and under the control of different trans-acting factors, as for example when cap-dependent protein synthesis is shut off during viral infection. Such regulatory elements have been identified in the mRNAs of growth factors, protooncogenes, angiogenesis factors, and apoptosis regulators, which are translated under a variety of stress conditions, including hypoxia, serum deprivation, irradiation and apoptosis. Thus, cap-independent translational control might have evolved to regulate cellular responses in acute but transient stress conditions that would otherwise lead to cell death, while the same mechanism is of major importance for viral mRNAs to bypass the shutting-off of host protein synthesis after infection. Encephalomyocarditis virus (EMCV) and hepatitis C virus exemplify two distinct mechanisms of IRES-mediated initiation. In contrast to cap-dependent initiation, the eIF4A and eIF4G subunits of eIF4F bind immediately upstream of the EMCV initiation codon and promote binding of a 43S complex. Accordingly, EMCV initiation does not involve scanning and does not require eIF1, eIF1A, and the eIF4E subunit of eIF4F. Nonetheless, initiation on some EMCV-like IRESs requires additional non-canonical initiation factors, which alter IRES conformation and promote binding of eIF4A/eIF4G. Initiation on the hepatitis C virus IRES is simpler: a 43S complex containing only eIF2 and eIF3 binds directly to the initiation codon as a result of specific interaction of the IRES and the 40S subunit.20444697Pubmed2010Eukaryotic protein synthesis: still a mysteryMerrick, William CJ Biol Chem 285:21197-201inferred by electronic annotationIEAGOIEASRP-dependent cotranslational protein targeting to membraneSRP-dependent cotranslational protein targeting to membraneThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Nascent polypeptide:mRNA:ribosome complex binds signal recognition particle (SRP)Nascent polypeptide:mRNA:ribosome complex binds signal recognition particle (SRP)This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 101373091ribosome:mRNA:polypeptide+signal [cytosol]ribosome:mRNA:polypeptide+signalReactome DB_ID: 100950391Reactome DB_ID: 100946501Reactome DB_ID: 17993331nascent polypeptide with signal sequence [cytosol]nascent polypeptide with signal sequenceReactome Database ID Release 7510137309Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10137309ReactomeR-SSC-17993271Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-1799327.1Reactome DB_ID: 101373071Signal Recognition Particle [cytosol]Signal Recognition ParticleReactome DB_ID: 101372831UniProt:F1SS29SRP14UniProtF1SS292EQUAL136EQUALReactome DB_ID: 101372911UniProt:F2Z5M9SRP54UniProtF2Z5M91EQUAL504EQUALReactome DB_ID: 101373051Ghost homologue of 7SL RNA [cytosol]Ghost homologue of 7SL RNAReactome DB_ID: 101372991UniProt:A0A287AJ59SRP9UniProtA0A287AJ592EQUAL86EQUALReactome DB_ID: 101372951UniProt:F1RTV6SRP72UniProtF1RTV62EQUAL671EQUALReactome DB_ID: 101373031UniProt:F1RW08SRP68UniProtF1RW081EQUAL627EQUALReactome DB_ID: 101372871UniProt:F1RLG4SRP19UniProtF1RLG42EQUAL144EQUALReactome Database ID Release 7510137307Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10137307ReactomeR-SSC-2649321Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-264932.1Reactome DB_ID: 101373111SRP:polypeptide+signal:ribosome [cytosol]SRP:polypeptide+signal:ribosomeReactome DB_ID: 101373091Reactome DB_ID: 101373071Reactome Database ID Release 7510137311Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10137311ReactomeR-SSC-17993371Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-1799337.1Reactome Database ID Release 7510137313Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10137313ReactomeR-SSC-17993321Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-1799332.1The Ribosome Nascent Complex containing the ribosome and protruding signal peptide of preprolactin is bound by the Signal Recognition Particle Complex. Translation is paused during this step.12853463Pubmed2003Structure, function and evolution of the signal recognition particleNagai, KOubridge, CKuglstatter, AMenichelli, EIsel, CJovine, LEMBO J 22:3479-8516469117Pubmed2006Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stagesRömisch, KMiller, FWDobberstein, BHigh, SArthritis Res Ther 8:R3918455985Pubmed2008SRP keeps polypeptides translocation-competent by slowing translation to match limiting ER-targeting sitesLakkaraju, AKMary, CScherrer, AJohnson, AEStrub, KCell 133:440-51inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510186829Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10186829ReactomeR-SSC-17993391Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-1799339.1GO0006614GO biological processThe process for translation of a protein destined for the endoplasmic reticulum (ER) branches from the canonical cytoslic translation process at the point when a nascent polypeptide containing a hydrophobic signal sequence is exposed on the surface of the cytosolic ribosome:mRNA:peptide complex. The signal sequence mediates the interaction of this complex with a cytosolic signal recognition particle (SRP) to form a complex which in turn docks with an SRP receptor complex on the ER membrane. There the ribosome complex is transferred from the SRP complex to a translocon complex embedded in the ER membrane and reoriented so that the nascent polypeptide protrudes through a pore in the translocon into the ER lumen. Translation, which had been halted by SRP binding, now resumes, the signal peptide is cleaved from the polypeptide, and elongation proceeds, with the growing polypeptide oriented into the ER lumen.inferred by electronic annotationIEAGOIEAEukaryotic Translation ElongationEukaryotic Translation ElongationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Peptide chain elongationPeptide chain elongationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>GTP-binding activates eEF2GTP-binding activates eEF2This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 101004771UniProt:I3LII3EEF2UniProtI3LII3dipthamide at 715 (in Homo sapiens)715EQUALdipthamide2EQUAL858EQUALReactome DB_ID: 294381Reactome DB_ID: 101004791eEF2:GTP [cytosol]eEF2:GTPReactome DB_ID: 101004771dipthamide at 715 (in Homo sapiens)715EQUAL2EQUAL858EQUALReactome DB_ID: 294381Reactome Database ID Release 7510100479Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100479ReactomeR-SSC-1569161Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156916.1Reactome Database ID Release 7510100481Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100481ReactomeR-SSC-1569301Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156930.1At the beginning of this reaction, 1 molecule of 'eEF2', and 1 molecule of 'GTP' are present. At the end of this reaction, 1 molecule of 'eEF2:GTP' is present.<br><br> This reaction takes place in the 'cytosol' (Guillot et al. 2013).<br>8407925Pubmed1993GTP binding to elongation factor eEF-2 unmasks a tryptophan residue required for biological activityGuillot, DPenin, FDi Pietro, ASontag, BLavergne, J PReboud, J PJ. Biol. Chem. 268:20911-6inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510185335Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10185335ReactomeR-SSC-1569021Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156902.1The mechanism of a peptide bond requires the movement of three protons. First the deprotonation of the ammonium ion generates a reactive amine, allowing a nucleophilic attack on the carbonyl group. This is followed by the loss of a proton from the reaction intermediate, only to be taken up by the oxygen on the leaving group (from the end of the amino acid chain bound to the tRNA in the P-site). The peptide bond formation results in the net loss of one water molecule, leaving a deacylated-tRNA in the P-site, and a nascent polypeptide chain one amino acid larger in the A-site.<br>For the purpose of illustration, the figures used in the section show one amino acid being added to a peptidyl-tRNA with a growing peptide chain.<br>12297040Pubmed2002The path to perdition is paved with protonsGreen, RLorsch, JRCell 110:665-8inferred by electronic annotationIEAGOIEARegeneration of eEF1A:GTP by eEF1B activityRegeneration of eEF1A:GTP by eEF1B activityThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 101004631eEF1B complex [cytosol]eEF1B complexConverted from EntitySet in ReactomeReactome DB_ID: 101004611Homologues of EEF1G [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityEEF1G [cytosol]EEF1G [cytosol]UniProtA0A287A623UniProtF1RPW9Reactome DB_ID: 101004511UniProt:F1SEV8EEF1DUniProtF1SEV82EQUAL281EQUALReactome DB_ID: 101004471UniProt:F1SHD6EEF1B2UniProtF1SHD62EQUAL225EQUALReactome Database ID Release 7510100463Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100463ReactomeR-SSC-1569201Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156920.1Reactome DB_ID: 294381Reactome DB_ID: 101004671eEF1A:GDP [cytosol]eEF1A:GDPReactome DB_ID: 294201Reactome DB_ID: 101004411UniProt:A0A287AJQ9UniProtA0A287AJQ91EQUAL462EQUALReactome Database ID Release 7510100467Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100467ReactomeR-SSC-1569291Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156929.1Reactome DB_ID: 101004691eEF1B:GDP exchange complex [cytosol]eEF1B:GDP exchange complexReactome DB_ID: 101004631Reactome DB_ID: 294201Reactome Database ID Release 7510100469Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100469ReactomeR-SSC-1569171Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156917.1Reactome DB_ID: 101004431eEF1A:GTP [cytosol]eEF1A:GTPReactome DB_ID: 294381Reactome DB_ID: 1010044111EQUAL462EQUALReactome Database ID Release 7510100443Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100443ReactomeR-SSC-1569211Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156921.1PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 10100463GO0005085GO molecular functionReactome Database ID Release 7510100470Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100470Reactome Database ID Release 7510100472Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100472ReactomeR-SSC-1569131Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156913.1The eEF1B complex binds to eEF1A and regulates its activity by catalyzing the release of GDP. Subsequently, GTP is able to bind eEF1A allowing the formation of the ternary complex (eEF1A-GTP-aa-tRNA).In metazoans eEF1 protein family is composed of four subunits: eEF1A and eEF1B alpha, beta, and gamma (formerly EF-1alpha, EF-1beta, EF-1delta, and EF-1gamma, respectively). Both eEF1B alpha and eEF1B beta function as nucleotide exchange proteins. eEF1B gamma associates with eEF1B alpha and stimulates its exchange activity.<br>This process is illustrated below with a GTP molecule in white and eEF1A protein in yellow.The three subunits of eEF1B are also shown.3276514Pubmed1988Elongation factor 1 beta gamma from Artemia. Purification and properties of its subunits.Janssen, GMMoller, WEur J Biochem 171:119-292207149Pubmed1990Elongation factor 1 beta of artemia: localization of functional sites and homology to elongation factor 1 deltavan, Damme HTAmons, RKarssies, RTimmers, CJJanssen, GMMoller, WBiochim Biophys Acta 1050:241-710368288Pubmed1999The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coliPerez, JMSiegal, GKriek, JHard, KDijk, JCanters, GWMoller, WStructure Fold Des 7:217-26inferred by electronic annotationIEAGOIEAFormation of eEF1B complexFormation of eEF1B complexThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Converted from EntitySet in ReactomeReactome DB_ID: 101004611Reactome DB_ID: 1010045112EQUAL281EQUALReactome DB_ID: 1010044712EQUAL225EQUALReactome DB_ID: 101004631Reactome Database ID Release 7510100465Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10100465ReactomeR-SSC-1569101Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156910.1At the beginning of this reaction, 1 molecule of 'eEF1B alpha', 1 molecule of 'eEF1B gamma', and 1 molecule of 'eEF1B beta' are present. At the end of this reaction, 1 molecule of 'eEF1B complex' is present. This reaction takes place in the 'cytosol' (Veremieva et al. 2011). 20964681Pubmed2011Unbalanced expression of the translation complex eEF1 subunits in human cardioesophageal carcinomaVeremieva, MarinaKhoruzhenko, AntoninaZaicev, SergejNegrutskii, BorisEl'skaya, AnnaEur. J. Clin. Invest. 41:269-76inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510185333Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10185333ReactomeR-SSC-1568421Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-156842.1GO0006414GO biological processThe translation elongation cycle adds one amino acid at a time to a growing polypeptide according to the sequence of codons found in the mRNA. The next available codon on the mRNA is exposed in the aminoacyl-tRNA (aa-tRNA) binding site (A site) on the 30S subunit.<br>A: Ternary complexes of aa -tRNA:eEF1A:GTP enter the ribosome and enable the anticodon of the tRNA to make a codon/anticodon interaction with the A-site codon of the mRNA. B: Upon cognate recognition, the eEF1A:GTP is brought into the GTPase activating center of the ribosome, GTP is hydrolyzed and eEF1A:GDP leaves the ribosome. C: The peptidyl transferase center of ribosome catalyses the formation of a peptide bond between the incoming amino acid and the peptide found in the peptidyl-tRNA binding site (P site). D: In the pre-translocation state of the ribosome, the eEF2:GTP enters the ribosome, physically translocating the peptidyl-tRNA out of the A site to P site and leaves the ribosome eEF2:GDP. This action of eEF2:GTP accounts for the precise movement of the mRNA by 3 nucleotides.Consequently, deacylated tRNA is shifted to the E site. A ribosome associated ATPase activity is proposed to stimulate the release of deacylated tRNA from the E site subsequent to translocation (Elskaya et al., 1991). In this post-translocation state, the ribosome is now ready to receive a new ternary complex.<br>This process is illustrated below with: an amino acyl-tRNA with an amino acid, a peptidyl-tRNA with a growing peptide, a deacylated tRNA with an -OH, and a ribosome with A,P and E sites to accommodate these three forms of tRNA.9265629Pubmed1997Three tRNA binding sites in rabbit liver ribosomes and role of the intrinsic ATPase in 80S ribosomes from higher eukaryotesEl'skaya, AVOvcharenko, GVPalchevskii, SSPetrushenko, ZMTriana-Alonso, FJNierhaus, KHBiochemistry 36:10492-79780879696184ISBN2000The Protein Biosynthesis Elongation CycleMerrick, William CNyborg, JTranslational Control of Gene Expression (Book): 89-12715189156Pubmed2004The molecular mechanics of eukaryotic translationKapp, LDLorsch, JRAnnu Rev Biochem 73:657-704inferred by electronic annotationIEAGOIEAEukaryotic Translation TerminationEukaryotic Translation TerminationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>N6AMT1:TRMT112 transfers CH3 group from AdoMet to ETF1 dimerN6AMT1:TRMT112 transfers CH3 group from AdoMet to ETF1 dimerThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 712842S-adenosyl-L-methionine [ChEBI:15414]S-adenosyl-L-methionineChEBI15414Reactome DB_ID: 101688591ETF1 dimer:eRF3:GTP [cytosol]ETF1 dimer:eRF3:GTPReactome DB_ID: 101688551eRF3:GTP [cytosol]eRF3:GTPConverted from EntitySet in ReactomeReactome DB_ID: 101268911eRF3 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityGSPT1 [cytosol]GSPT2 [cytosol]UniProtI3LNK5UniProtF1RUJ9Reactome DB_ID: 294381Reactome Database ID Release 7510168855Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10168855ReactomeR-SSC-1433831Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-143383.1Reactome DB_ID: 101688571ETF1 dimer [cytosol]ETF1 dimerReactome DB_ID: 101268812UniProt:F2Z505ETF1UniProtF2Z5052EQUAL437EQUALReactome Database ID Release 7510168857Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10168857ReactomeR-SSC-68001391Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-6800139.1Reactome Database ID Release 7510168859Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10168859ReactomeR-SSC-68001321Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-6800132.1Reactome DB_ID: 712852S-adenosyl-L-homocysteine [ChEBI:16680]S-adenosyl-L-homocysteineChEBI16680Reactome DB_ID: 101688661Me-Q185-ETF1 dimer:eRF3:GTP [cytosol]Me-Q185-ETF1 dimer:eRF3:GTPReactome DB_ID: 101688641Me-Q185-ETF1 dimer [cytosol]Me-Q185-ETF1 dimerReactome DB_ID: 101688622N5-methyl-L-glutamine at 185 (in Homo sapiens)185EQUALN5-methyl-L-glutamine2EQUAL437EQUALReactome Database ID Release 7510168864Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10168864ReactomeR-SSC-68001311Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-6800131.1Reactome DB_ID: 101688551Reactome Database ID Release 7510168866Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10168866ReactomeR-SSC-68001541Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-6800154.1PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 10168876N6AMT1:TRMT112 [cytosol]N6AMT1:TRMT112Reactome DB_ID: 101688701UniProt:I3L8U7UniProtI3L8U71EQUAL214EQUALReactome DB_ID: 101688741UniProt:A0A287B938TRMT112UniProtA0A287B9381EQUAL125EQUALReactome Database ID Release 7510168876Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10168876ReactomeR-SSC-68001331Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-6800133.1GO0036009GO molecular functionReactome Database ID Release 7510168877Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10168877Reactome Database ID Release 7510168879Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10168879ReactomeR-SSC-68001381Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-6800138.1Class 1 release factors such as eukaryotic peptide chain release factor subunit 1 (ETF1) direct the termination of peptide translation in response to the termination codons UAA, UAG and UGA. ETF1 needs to be complexed with ERF3 in its GTP-bound form to be efficiently post-translationally methylated. HemK methyltransferase family member 2 (N6AMT1) is a heterodimeric methyltransferase that catalyses N5-methylation of ETF1 on glutamine 185 (Q185), using S-adenosyl L-methionine (AdoMet) as the methyl donor (Figaro et al. 2008). N6AMT1 forms a complex with multifunctional methyltransferase subunit TRM112-like protein (TRMT112)18539146Pubmed2008HemK2 protein, encoded on human chromosome 21, methylates translation termination factor eRF1Figaro, SabineScrima, NathalieBuckingham, Richard HHeurgué-Hamard, ValérieFEBS Lett. 582:2352-6inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510187377Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10187377ReactomeR-SSC-727641Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72764.1GO0006415GO biological processThe arrival of any of the three stop codons (UAA, UAG and UGA) into the ribosomal A-site triggers the binding of a release factor (RF) to the ribosome and subsequent polypeptide chain release. In eukaryotes, the RF is composed of two proteins, eRF1 and eRF3. eRF1 is responsible for the hydrolysis of the peptidyl-tRNA, while eRF3 provides a GTP-dependent function. The ribosome releases the mRNA and dissociates into its two complex subunits, which can reassemble on another molecule to begin a new round of protein synthesis. It should be noted that at present, there is no factor identified in eukaryotes that would be the functional equivalent of the bacterial ribosome release (or recycling) factor, RRF, that catalyzes dissociation of the ribosome from the mRNA following release of the polypeptide2684966Pubmed1989Molecular cloning and expression of ribosome releasing factorIchikawa, SKaji, AJ Biol Chem 264:20054-915314182Pubmed2004GTP hydrolysis by eRF3 facilitates stop codon decoding during eukaryotic translation terminationSalas-Marco, JBedwell, David MMol Cell Biol 24:7769-78inferred by electronic annotationIEAGOIEAMitochondrial translationMitochondrial translationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Mitochondrial translation elongationMitochondrial translation elongationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>55S ribosome with peptidyl-tRNA in A site binds GFM1:GTP55S ribosome with peptidyl-tRNA in A site binds GFM1:GTPThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 101555621mitochondrial inner membraneGO000574355S ribosome:mRNA:tRNA:peptidyl-tRNA at A-site [mitochondrial inner membrane]55S ribosome:mRNA:tRNA:peptidyl-tRNA at A-siteReactome DB_ID: 53682671mRNA [mitochondrial matrix]mRNAReactome DB_ID: 101555601Ghost homologue of fMet-tRNA(fMet) [mitochondrial matrix]Ghost homologue of fMet-tRNA(fMet)Reactome DB_ID: 53898361peptidyl-tRNA with elongated peptide [mitochondrial inner membrane]peptidyl-tRNA with elongated peptideReactome DB_ID: 10155558155S ribosome [mitochondrial inner membrane]55S ribosomeReactome DB_ID: 10155556139S ribosomal subunit [mitochondrial inner membrane]39S ribosomal subunitReactome DB_ID: 101554921UniProt:I3LGM5MRPL45UniProtI3LGM51EQUAL306EQUALReactome DB_ID: 101553961UniProt:F1RRN2MRPL2UniProtF1RRN261EQUAL305EQUALReactome DB_ID: 101555381UniProt:A0A286ZXA6GADD45GIP1UniProtA0A286ZXA61EQUAL222EQUALReactome DB_ID: 101555461Ghost homologue of MT-TV [mitochondrial matrix]Ghost homologue of MT-TVReactome DB_ID: 101553641UniProt:A0A287ARV8MRPL12UniProtA0A287ARV846EQUAL198EQUALReactome DB_ID: 101554201UniProt:F1RT79MRPL27UniProtF1RT791EQUAL148EQUALReactome DB_ID: 101554801UniProt:A0A287BQA1MRPL42UniProtA0A287BQA133EQUAL142EQUALReactome DB_ID: 101554881UniProt:F1SR64MRPL44UniProtF1SR6431EQUAL332EQUALReactome DB_ID: 101555121UniProt:I3L9H6MRPL50UniProtI3L9H61EQUAL158EQUALReactome DB_ID: 101555542UniProt:F1S9B6UniProtF1S9B61EQUAL435EQUALReactome DB_ID: 101554321UniProt:F1STE5MRPL30UniProtF1STE535EQUAL161EQUALReactome DB_ID: 101553841UniProt:F1RMQ4MRPL17UniProtF1RMQ49EQUAL175EQUALReactome DB_ID: 101554361UniProt:I3LTC4MRPL32UniProtI3LTC41EQUAL188EQUALReactome DB_ID: 101554401UniProt:A0A286ZU68MRPL33UniProtA0A286ZU681EQUAL65EQUALReactome DB_ID: 101555301UniProt:I3L9J0MRPL55UniProtI3L9J034EQUAL128EQUALReactome DB_ID: 101554841UniProt:F1S8U4MRPL43UniProtF1S8U41EQUAL215EQUALReactome DB_ID: 101553761UniProt:F1RSH0MRPL15UniProtF1RSH022EQUAL296EQUALReactome DB_ID: 101553721UniProt:A0A287BMZ6MRPL14UniProtA0A287BMZ631EQUAL145EQUALReactome DB_ID: 101555161UniProt:A0A287BE26UniProtA0A287BE2632EQUAL128EQUALReactome DB_ID: 101555201UniProt:F1S9B7UniProtF1S9B724EQUAL123EQUALReactome DB_ID: 101553601UniProt:F1RU54MRPL11UniProtF1RU541EQUAL192EQUALReactome DB_ID: 101554641UniProt:F1SHP6MRPL39UniProtF1SHP61EQUAL338EQUALReactome DB_ID: 101554481UniProt:A0A286ZLJ1MRPL35UniProtA0A286ZLJ11EQUAL188EQUALReactome DB_ID: 101554161UniProt:F1RHJ1MRPL24UniProtF1RHJ110EQUAL216EQUALReactome DB_ID: 101554681UniProt:A0A287B9C4UniProtA0A287B9C41EQUAL311EQUALReactome DB_ID: 101554601UniProt:F1RW03MRPL38UniProtF1RW0327EQUAL380EQUALReactome DB_ID: 101555501UniProt:A0A287BP93MRPL57UniProtA0A287BP931EQUAL102EQUALReactome DB_ID: 101553881UniProt:A0A0R4J8D5UniProtA0A0R4J8D51EQUAL180EQUALReactome DB_ID: 101554441UniProt:A0A287A119UniProtA0A287A1191EQUAL92EQUALReactome DB_ID: 101554121UniProt:A0A286ZZC6MRPL23UniProtA0A286ZZC61EQUAL153EQUALReactome DB_ID: 101554521UniProt:A0A287A731MRPL36UniProtA0A287A7311EQUAL103EQUALReactome DB_ID: 101554041UniProt:A0A287BAP6UniProtA0A287BAP640EQUAL205EQUALReactome DB_ID: 101555221Ghost homologue of MRPL53 [mitochondrial inner membrane]Ghost homologue of MRPL53Reactome DB_ID: 101555441UniProt:A0A286ZJR2MRPL58UniProtA0A286ZJR230EQUAL206EQUALReactome DB_ID: 101553801UniProt:F1RI89MRPL16UniProtF1RI8937EQUAL251EQUALReactome DB_ID: 101553681UniProt:K7GP19MRPL13UniProtK7GP191EQUAL178EQUALReactome DB_ID: 101554761UniProt:A0A287AWS0UniProtA0A287AWS014EQUAL137EQUALReactome DB_ID: 101555081UniProt:A0A0R4J8D6UniProtA0A0R4J8D61EQUAL166EQUALReactome DB_ID: 101553921UniProt:I3LNJ0UniProtI3LNJ01EQUAL292EQUALReactome DB_ID: 101554241UniProt:A0A0R4J8D7UniProtA0A0R4J8D756EQUAL256EQUALReactome DB_ID: 101555001UniProt:F1SGC7MRPL47UniProtF1SGC71EQUAL250EQUALReactome DB_ID: 101553561UniProt:F1RWJ0MRPL10UniProtF1RWJ029EQUAL261EQUALReactome DB_ID: 101553521UniProt:A0A287AAV8UniProtA0A287AAV851EQUAL325EQUALReactome DB_ID: 101554001UniProt:A0A286ZU56MRPL20UniProtA0A286ZU5646EQUAL149EQUALReactome DB_ID: 101555261UniProt:I3LN63MRPL54UniProtI3LN6315EQUAL138EQUALReactome DB_ID: 101555341UniProt:I3LR45MRPL9UniProtI3LR451EQUAL267EQUALReactome DB_ID: 101555041UniProt:F1SUS9UniProtF1SUS929EQUAL212EQUALReactome DB_ID: 101555401Ghost homologue of Mitochondrial 16S rRNA [mitochondrial matrix]Ghost homologue of Mitochondrial 16S rRNAReactome DB_ID: 101554081UniProt:A0A287AF90MRPL22UniProtA0A287AF9041EQUAL206EQUALReactome DB_ID: 101554721UniProt:A0A286ZP98UniProtA0A286ZP9847EQUAL206EQUALReactome DB_ID: 101554561UniProt:A0A287BIV6UniProtA0A287BIV630EQUAL423EQUALReactome DB_ID: 101554961UniProt:F1SRT0MRPL46UniProtF1SRT01EQUAL279EQUALReactome DB_ID: 101554281UniProt:A0A140UHW4MRPL3UniProtA0A140UHW41EQUAL348EQUALReactome Database ID Release 7510155556Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155556ReactomeR-SSC-53682331Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5368233.1Reactome DB_ID: 10155348128S ribosomal subunit [mitochondrial inner membrane]28S ribosomal subunitReactome DB_ID: 101552361UniProt:A0A287AQT5MRPS22UniProtA0A287AQT51EQUAL360EQUALReactome DB_ID: 101552141UniProt:A0A0M3KL52UniProtA0A0M3KL5230EQUAL138EQUALReactome DB_ID: 101552401UniProt:A0A287AEW3MRPS23UniProtA0A287AEW31EQUAL190EQUALReactome DB_ID: 101553461UniProt:F1RNA7ERAL1UniProtF1RNA744EQUAL437EQUALReactome DB_ID: 101552641UniProt:A0A286ZUX9UniProtA0A286ZUX91EQUAL439EQUALReactome DB_ID: 101552681UniProt:A0A287AR81MRPS31UniProtA0A287AR8166EQUAL395EQUALReactome DB_ID: 101553421UniProt:F1S001MRPS2UniProtF1S0011EQUAL296EQUALReactome DB_ID: 101552941UniProt:A0A287AC32UniProtA0A287AC321EQUAL430EQUALReactome DB_ID: 101553241UniProt:A0A287B3R8UniProtA0A287B3R81EQUAL199EQUALReactome DB_ID: 101552321UniProt:A0A286ZNB3MRPS21UniProtA0A286ZNB31EQUAL87EQUALReactome DB_ID: 101552481UniProt:A0A0M3KL55MRPS25UniProtA0A0M3KL551EQUAL173EQUALReactome DB_ID: 101552181UniProt:A0A0M3KL53MRPS14UniProtA0A0M3KL531EQUAL128EQUALReactome DB_ID: 101552441UniProt:A0A287ANU4MRPS24UniProtA0A287ANU436EQUAL167EQUALReactome DB_ID: 101552061UniProt:F1RUU2MRPS10UniProtF1RUU21EQUAL201EQUALReactome DB_ID: 101552801UniProt:F1SG95UniProtF1SG951EQUAL323EQUALReactome DB_ID: 101552981UniProt:I3LEJ9MRPS6UniProtI3LEJ92EQUAL125EQUALReactome DB_ID: 101553381Ghost homologue of Mitochondrial 12S rRNA [mitochondrial inner membrane]Ghost homologue of Mitochondrial 12S rRNAReactome DB_ID: 101553321UniProt:I3LS10DAP3UniProtI3LS1019EQUAL398EQUALReactome DB_ID: 101552101UniProt:A0A286ZJJ6MRPS11UniProtA0A286ZJJ61EQUAL194EQUALReactome DB_ID: 101552601UniProt:A0A0M3KL56MRPS28UniProtA0A0M3KL5672EQUAL187EQUALReactome DB_ID: 101552281UniProt:F1RIU0MRPS17UniProtF1RIU021EQUAL130EQUALReactome DB_ID: 101552221UniProt:A0A287AKS1MRPS15UniProtA0A287AKS158EQUAL257EQUALReactome DB_ID: 101552561UniProt:I3LK09MRPS27UniProtI3LK091EQUAL414EQUALConverted from EntitySet in ReactomeReactome DB_ID: 101552901Homologues of MRPS36 [mitochondrial inner membrane]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityMRPS36 [mitochondrial inner membrane]MRPS36 [mitochondrial inner membrane]UniProtA0A286ZSC0UniProtA0A287B719Reactome DB_ID: 101552241Ghost homologue of MRPS16 [mitochondrial inner membrane]Ghost homologue of MRPS16Reactome DB_ID: 101553361UniProt:K7GKS8PTCD3UniProtK7GKS838EQUAL689EQUALReactome DB_ID: 101553061UniProt:I3LU08MRPS9UniProtI3LU081EQUAL396EQUALReactome DB_ID: 101553281UniProt:F1SU49CHCHD1UniProtF1SU491EQUAL118EQUALConverted from EntitySet in ReactomeReactome DB_ID: 101553201MRPS18A,B,C [mitochondrial inner membrane]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityMRPS18B [mitochondrial inner membrane]MRPS18C [mitochondrial inner membrane]MRPS18A [mitochondrial inner membrane]UniProtQ767K8UniProtA0A0M3KL54UniProtF1RRH6Reactome DB_ID: 101552721UniProt:F1S8G3UniProtF1S8G32EQUAL106EQUALReactome DB_ID: 101552761UniProt:F1RG19UniProtF1RG192EQUAL218EQUALReactome DB_ID: 101552521UniProt:A0A287AY01GNRH2UniProtA0A287AY0128EQUAL205EQUALReactome DB_ID: 101553021UniProt:A0A286ZJ25MRPS7UniProtA0A286ZJ2538EQUAL242EQUALReactome Database ID Release 7510155348Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155348ReactomeR-SSC-53682391Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5368239.1Reactome Database ID Release 7510155558Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155558ReactomeR-SSC-53682771Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5368277.1Reactome Database ID Release 7510155562Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155562ReactomeR-SSC-53898431Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5389843.1Reactome DB_ID: 101555681GFM1:GTP [mitochondrial matrix]GFM1:GTPReactome DB_ID: 1135731Reactome DB_ID: 101555661UniProt:A0A287AM95GFM1UniProtA0A287AM9537EQUAL751EQUALReactome Database ID Release 7510155568Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155568ReactomeR-SSC-54192741Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419274.1Reactome DB_ID: 10155570155S ribosome:mRNA:tRNA:peptidyl-tRNA:GFM1:GTP [mitochondrial inner membrane]55S ribosome:mRNA:tRNA:peptidyl-tRNA:GFM1:GTPReactome DB_ID: 53682671Reactome DB_ID: 101555681Reactome DB_ID: 101555601Reactome DB_ID: 53898361Reactome DB_ID: 101555581Reactome Database ID Release 7510155570Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155570ReactomeR-SSC-54192671Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419267.1Reactome Database ID Release 7510155572Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155572ReactomeR-SSC-54192611Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419261.1GFMT1:GTP (EF-G1mt:GTP) binds ribosomes possessing a peptidyl-tRNA at the A site and an empty P site (Bhargava et al. 2004, Tsuboi et al. 2009, inferred from bovine homologs in Chung and Spremulli 1990).15358359Pubmed2004Expression and characterization of isoform 1 of human mitochondrial elongation factor GBhargava, KalpanaTempleton, PaulSpremulli, LLProtein Expr. Purif. 37:368-7619716793Pubmed2009EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesisTsuboi, MasafumiMorita, HiroyukiNozaki, YusukeAkama, KentaUeda, TIto, KoichiNierhaus, Knud HTakeuchi, NMol. Cell 35:502-102250005Pubmed1990Purification and characterization of elongation factor G from bovine liver mitochondriaChung, H KSpremulli, L LJ. Biol. Chem. 265:21000-4inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510187147Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10187147ReactomeR-SSC-53898401Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5389840.1GO0070125GO biological processTranslation elongation proceeds by cycles of aminoacyl-tRNAs binding, peptide bond formation, and displacement of deacylated tRNAs (reviewed in Christian and Spremulli 2012). In each cycle an aminoacyl-tRNA in a complex with TUFM:GTP (EF-Tu:GTP) binds a cognate codon at the A-site of the ribosome, GTP is hydrolyzed, and TUFM:GDP dissociates. The elongating polypeptide bonded to the tRNA at the P-site is transferred to the aminoacyl group at the A-site by peptide bond formation, leaving a deacylated tRNA at the P-site and the elongating polypeptide attached to the tRNA at the A-site. GFM1:GTP (EF-Gmt:GTP) binds, GTP is hydrolyzed, GFM1:GDP dissociates, and the ribosome translocates 3 nucleotides in the 3' direction, relocating the peptidyl-tRNA to the P-site and allowing another cycle to begin. Mitochondrial ribosomes associate with the inner membrane and polypeptides are co-translationally inserted into the membrane (reviewed in Ott and Herrmann 2010, Agrawal and Sharma 2012). TUFM:GDP is regenerated to TUFM:GTP by the guanine nucleotide exchange factor TSFM (EF-Ts, EF-TsMt).22959417Pubmed2012Structural aspects of mitochondrial translational apparatusAgrawal, Rajendra KSharma, Manjuli RCurr. Opin. Struct. Biol. 22:797-80322172991Pubmed2012Mechanism of protein biosynthesis in mammalian mitochondriaChristian, Brooke ESpremulli, LLBiochim. Biophys. Acta 1819:1035-5419962410Pubmed2010Co-translational membrane insertion of mitochondrially encoded proteinsOtt, MartinHerrmann, JMBiochim. Biophys. Acta 1803:767-75inferred by electronic annotationIEAGOIEAMitochondrial translation terminationMitochondrial translation terminationThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>MTRF1L (MTRF1a) or ICT1 binds stop codon in 55S ribosome:mRNA:peptidyl-tRNAMTRF1L (MTRF1a) or ICT1 binds stop codon in 55S ribosome:mRNA:peptidyl-tRNAThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 1135731Reactome DB_ID: 10155574155S ribosome:mRNA:peptidyl-tRNA at P-site [mitochondrial inner membrane]55S ribosome:mRNA:peptidyl-tRNA at P-siteReactome DB_ID: 53682671Reactome DB_ID: 53898361Reactome DB_ID: 101555581Reactome Database ID Release 7510155574Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155574ReactomeR-SSC-54192721Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419272.1Converted from EntitySet in ReactomeReactome DB_ID: 101555821MTRF1L, ICT1 [mitochondrial matrix]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityMTRF1L [mitochondrial matrix]MRPL58 [mitochondrial matrix]UniProtF1S7X5Reactome DB_ID: 10155584155S ribosome:mRNA:peptidyl-tRNA:MTRF1L:GTP [mitochondrial inner membrane]55S ribosome:mRNA:peptidyl-tRNA:MTRF1L:GTPReactome DB_ID: 1135731Reactome DB_ID: 53682671Reactome DB_ID: 53898361Reactome DB_ID: 101555581Converted from EntitySet in ReactomeReactome DB_ID: 101555821Reactome Database ID Release 7510155584Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155584ReactomeR-SSC-54192801Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419280.1Reactome Database ID Release 7510155586Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155586ReactomeR-SSC-54192641Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419264.1MTRF1L (mtRF1a) binds the stop codons UAA and UAG of the mRNA when they are in the A site of the ribosome (Soleimanpour-Lichaei 2007, Nozaki et al. 2008). (The UGA codon is recognized by the tryptophan tRNA in mitochondrial translation.) ICT1 can also bind standard stop codons in the A-site (inferred from pig mitochondrial ribosomes in Akabane et al. 2014). MTRF1 was also thought to play a role in translation termination by recognizing the unconventional termination codons AGA and AGG (Zhang and Spremulli 1998, Young et al. 2010) but frameshifting is now confirmed in the termination mechanism of these codons (Temperley et al. 2010). Structural features of MTRF1 have been reported suggesting it could recognize an empty A-site (Huynen et al. 2012) or UAA and UAG codons (Lind et al. 2013) however there is no direct experimental data to confirm these last two postulates.24352605Pubmed2013Codon-reading specificities of mitochondrial release factors and translation termination at non-standard stop codonsLind, ChristofferSund, JohanAqvist, JohanNat Commun 4:294018429816Pubmed2008HMRF1L is a human mitochondrial translation release factor involved in the decoding of the termination codons UAA and UAGNozaki, YusukeMatsunaga, NorikoIshizawa, ToshihiroUeda, TTakeuchi, NGenes Cells 13:429-389838146Pubmed1998Identification and cloning of human mitochondrial translational release factor 1 and the ribosome recycling factorZhang, YSpremulli, L LBiochim. Biophys. Acta 1443:245-5017803939Pubmed2007mtRF1a is a human mitochondrial translation release factor decoding the major termination codons UAA and UAGSoleimanpour-Lichaei, Hamid RezaKühl, IngeGaisne, MauricettePassos, Joao FWydro, MateuszRorbach, JoannaTemperley, RichardBonnefoy, NathalieTate, WarrenLightowlers, RobertChrzanowska-Lightowlers, Zofia M AMol. Cell 27:745-5720075246Pubmed2010Hungry codons promote frameshifting in human mitochondrial ribosomesTemperley, RichardRichter, RicardaDennerlein, SvenLightowlers, Robert NChrzanowska-Lightowlers, Zofia M AScience 327:30120421313Pubmed2010Bioinformatic, structural, and functional analyses support release factor-like MTRF1 as a protein able to decode nonstandard stop codons beginning with adenine in vertebrate mitochondriaYoung, David JEdgar, Christina DMurphy, JenniferFredebohm, JohannesPoole, Elizabeth STate, WPRNA 16:1146-5522569235Pubmed2012Structure based hypothesis of a mitochondrial ribosome rescue mechanismHuynen, Martijn ADuarte, IsabelChrzanowska-Lightowlers, Zofia M ANabuurs, Sander BBiol. Direct 7:14inferred by electronic annotationIEAGOIEA55S ribosome hydrolyzes peptidyl-tRNA bond and MTRF1L hydrolyzes GTP55S ribosome hydrolyzes peptidyl-tRNA bond and MTRF1L hydrolyzes GTPThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 101555841Reactome DB_ID: 10155590155S ribosome:mRNA:tRNA [mitochondrial inner membrane]55S ribosome:mRNA:tRNAReactome DB_ID: 53682671Reactome DB_ID: 101555881Ghost homologue of tRNA [mitochondrial matrix]Ghost homologue of tRNAReactome DB_ID: 101555581Reactome Database ID Release 7510155590Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155590ReactomeR-SSC-54192621Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419262.1Reactome DB_ID: 1135481Reactome DB_ID: 54192871polypeptide [mitochondrial inner membrane]polypeptideReactome DB_ID: 1135251Converted from EntitySet in ReactomeReactome DB_ID: 101555821Reactome Database ID Release 7510155592Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155592ReactomeR-SSC-54192711Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419271.1Binding of the MTRF1L (MTRF1a) termination factor triggers hydrolysis of the peptidyl-tRNA bond by the 39S subunit of the ribosome and release of the translated polypeptide (Soleimanpour-Lichaei et al. 2007, Nozaki et al. 2008, reviewed in Christian and Spremulli 2012). MTRF1L hydrolyzes GTP during the reaction. Stalled ribosomes are rescued by binding of an ICT1 protein in addition to the ICT1 subunit integrated in the 39S subunit (Richter et al. 2010, Akabane et al. 2014).20186120Pubmed2010A functional peptidyl-tRNA hydrolase, ICT1, has been recruited into the human mitochondrial ribosomeRichter, RicardaRorbach, JoannaPajak, AleksandraSmith, Paul MWessels, Hans JHuynen, Martijn ASmeitink, Jan ALightowlers, Robert NChrzanowska-Lightowlers, Zofia M AEMBO J. 29:1116-2525233460Pubmed2014Ribosome Rescue and Translation Termination at Non-Standard Stop Codons by ICT1 in Mammalian MitochondriaAkabane, ShioriUeda, TNierhaus, Knud HTakeuchi, NPLoS Genet. 10:e1004616inferred by electronic annotationIEAGOIEAMRRF binds 55S ribosome:mRNA:tRNAMRRF binds 55S ribosome:mRNA:tRNAThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 101555901Reactome DB_ID: 101556021UniProt:F1SLQ7UniProtF1SLQ756EQUAL262EQUALReactome DB_ID: 10155611155S ribosome:mRNA:tRNA:MRRF [mitochondrial inner membrane]55S ribosome:mRNA:tRNA:MRRFReactome DB_ID: 53682671Reactome DB_ID: 10155602156EQUAL262EQUALReactome DB_ID: 101555881Reactome DB_ID: 101555581Reactome Database ID Release 7510155611Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155611ReactomeR-SSC-54192751Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419275.1Reactome Database ID Release 7510155613Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155613ReactomeR-SSC-54192811Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419281.1The mitochondrial ribosome releasing factor MRRF (RRF) binds the 55S ribosome at the A-site after translation has been terminated by MTRF1L (MTRF1a) at a stop codon and the translated polypeptide has been hydrolyzed from the last tRNA, which remains in the P-site (Rorbach et al. 2008).18782833Pubmed2008The human mitochondrial ribosome recycling factor is essential for cell viabilityRorbach, JoannaRichter, RicardaWessels, Hans JWydro, MateuszPekalski, MarcinFarhoud, MurtadaKühl, IngeGaisne, MauricetteBonnefoy, NathalieSmeitink, Jan ALightowlers, Robert NChrzanowska-Lightowlers, Zofia M ANucleic Acids Res. 36:5787-99inferred by electronic annotationIEAGOIEA3.6.5.43.6.5.33.6.5.23.6.5.1Hydrolysis of GTP and dissociation of 28S and 39S subunitsHydrolysis of GTP and dissociation of 28S and 39S subunitsThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 10155604155S ribosome:MRRF:GFM2:GTP [mitochondrial inner membrane]55S ribosome:MRRF:GFM2:GTPReactome DB_ID: 101555981GFM2:GTP [mitochondrial matrix]GFM2:GTPReactome DB_ID: 1135731Reactome DB_ID: 101555961UniProt:A0A287AA55UniProtA0A287AA551EQUAL779EQUALReactome Database ID Release 7510155598Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155598ReactomeR-SSC-54192701Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419270.1Reactome DB_ID: 10155602156EQUAL262EQUALReactome DB_ID: 101555581Reactome Database ID Release 7510155604Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155604ReactomeR-SSC-54192821Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419282.1Reactome DB_ID: 101556061GFM2:GDP [mitochondrial matrix]GFM2:GDPReactome DB_ID: 1015559611EQUAL779EQUALReactome DB_ID: 1135251Reactome Database ID Release 7510155606Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155606ReactomeR-SSC-54192661Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419266.1Reactome DB_ID: 1135481Reactome DB_ID: 101555561Reactome DB_ID: 10155602156EQUAL262EQUALReactome DB_ID: 101553481PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 10155604GO0003924GO molecular functionReactome Database ID Release 7510155607Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155607Reactome Database ID Release 7510155609Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10155609ReactomeR-SSC-54192731Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419273.1When complexed with ribosomes GFM2 (EF-G2mt) hydrolyzes GTP and, together with MRRF, acts as a ribosome releasing factor by splitting 55S ribosomes into 28S and 39S subunits (Tsuboi et al. 2009). Though GTP is hydrolyzed during the reaction, hydrolysis is not necessary for splitting the 55S ribosome into 39S and 28S subunits, but is necessary for dissociation of GFM2 (as GFM2:GDP) and MRRF from the large ribosomal subunit after splitting (Tsuboi et al. 2009).inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510187151Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10187151ReactomeR-SSC-54192761Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5419276.1GO0070126GO biological processTranslation is terminated when MTRF1L:GTP (MTRF1a:GTP) recognizes a UAA or UAG termination codon in the mRNA at the A site of the ribosome (Soleimanpour-Lichaei et al. 2007, reviewed in Richter et al. 2010, Chrzanowska-Lightowlers et al. 2011. Christian and Spremulli 2012). GTP is hydrolyzed, and the aminoacyl bond between the translated polypeptide and the final tRNA at the P site is hydrolyzed by the 39S ribosomal subunit, releasing the translated polypeptide. MRRF (RRF) and GFM2:GTP (EF-G2mt:GTP) then act to release the remaining tRNA and mRNA from the ribosome and dissociate the 55S ribosome into 28S and 39S subunits.21118119Pubmed2010Translation termination in human mitochondrial ribosomesRichter, RicardaPajak, AleksandraDennerlein, SvenRozanska, AgataLightowlers, Robert NChrzanowska-Lightowlers, Zofia M ABiochem. Soc. Trans. 38:1523-621873426Pubmed2011Termination of protein synthesis in mammalian mitochondriaChrzanowska-Lightowlers, Zofia M APajak, AleksandraLightowlers, Robert NJ. Biol. Chem. 286:34479-85inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510187149Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10187149ReactomeR-SSC-53682871Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-5368287.1GO0032543GO biological processOf the roughly 1000 human mitochondrial proteins only 13 proteins, all of them hydrophobic inner membrane proteins that are components of the oxidative phosphorylation apparatus, are encoded in the mitochondrial genome and translated by mitoribosomes at the matrix face of the inner membrane (reviewed in Herrmann et al. 2012, Hallberg and Larsson 2014, Lightowlers et al. 2014). The remainder, including all proteins of the mitochondrial translation system, are encoded in the nucleus and imported from the cytosol into the mitochondrion. Translation in the mitochondrion reflects both the bacterial origin of the organelle and subsequent divergent evolution during symbiosis (reviewed in Huot et al. 2014, Richman et al. 2014). Human mitochondrial ribosomes have a low sedimentation coefficient of only 55S, but at 2.71 MDa they retain a similar mass to E. coli 70S particles. The 55S particles are protein-rich compared to both cytosolic ribosomes and eubacterial ribosomes. This is due to shorter mt-rRNAs, mitochondria-specific proteins, and numerous rearrangements in individual protein positions within the two ribosome subunits (inferred from bovine ribosomes in Sharma et al. 2003, Greber et al. 2014, Kaushal et al. 2014, reviewed in Agrawal and Sharma 2012).<br>Mitochondrial mRNAs have either no untranslated leader or short leaders of 1-3 nucleotides, with the exception of the 2 bicistronic transcripts, RNA7 and RNA14, which have overlapping orfs that encode ND4L/ND4 and ATP8/ATP6 respectively. Translation is believed to initiate with the mRNA binding the 28S subunit:MTIF3 (28S subunit:IF-3Mt, 28S subunit:IF2mt) complex together with MTIF2:GTP (IF-2Mt:GTP, IF2mt:GTP) at the matrix face of the inner membrane (reviewed in Christian and Spremulli 2012). MTIF3 can dissociate 55S particles in preparation for initiation, enhances formation of initiation complexes, and inhibits N-formylmethionine-tRNA (fMet-tRNA) binding to 28S subunits in the absence of mRNA. Binding of fMet-tRNA to the start codon of the mRNA results in a stable complex while absence of a start codon at the 5' end of the mRNA causes eventual dissociation of the mRNA from the 28S subunit. After recognition of a start codon, the 39S subunit then binds the stable complex, GTP is hydrolyzed, and the initiation factors MTIF3 and MTIF2:GDP dissociate.<br>Translation elongation then proceeds by cycles of aminoacyl-tRNAs binding, peptide bond formation, and displacement of deacylated tRNAs. In each cycle an aminoacyl-tRNA in a complex with TUFM:GTP (EF-Tu:GTP) binds at the A-site of the ribosome, GTP is hydrolyzed, and TUFM:GDP dissociates. The elongating polypeptide bonded to the tRNA at the P-site is transferred to the aminoacyl group at the A-site by peptide bond formation at the peptidyl transferase center, leaving a deacylated tRNA at the P-site and the elongating polypeptide attached to the tRNA at the A-site. The polypeptide is co-translationally inserted into the inner mitochondrial membrane via an interaction with OXA1L (Haque et al. 2010, reviewed in Ott and Hermann 2010). After peptide bond formation, GFM1:GTP (EF-Gmt:GTP) then binds the ribosome complex, GTP is hydrolyzed, GFM1:GDP dissociates, and the ribosome translocates 3 nucleotides in the 3' direction along the mRNA, relocating the polypeptide-tRNA to the P-site and allowing another cycle to begin. TUFM:GDP is regenerated to TUFM:GTP by the guanine nucleotide exchange factor TSFM (EF-Ts, EF-TsMt).<br>Translation is terminated when MTRF1L:GTP (MTRF1a:GTP) recognizes an UAA or UAG termination codon at the A-site of the ribosome (Tsuboi et al. 2009). GTP hydrolysis does not appear to be required. The tRNA-aminoacyl bond between the translated polypeptide and the final tRNA at the P-site is hydrolyzed by the 39S subunit, facilitating release of the polypeptide. MRRF (RRF) and GFM2:GTP (EF-G2mt:GTP) then act to release the remaining tRNA and mRNA from the ribosome and dissociate the 55S ribosome into 28S and 39S subunits.<br>Mutations have been identified in genes encoding mitochondrial ribosomal proteins and translation factors. These have been shown to be pathogenic, causing neurological and other diseases (reviewed in Koopman et al. 2013, Pearce et al. 2013).20601428Pubmed2010Properties of the C-terminal tail of human mitochondrial inner membrane protein Oxa1L and its interactions with mammalian mitochondrial ribosomesHaque, Md EmdadulElmore, Kevin BTripathy, AshutoshKoc, HasanKoc, Emine CSpremulli, LLJ. Biol. Chem. 285:28353-6224440477Pubmed2014Idiosyncrasies in decoding mitochondrial genomesHuot, Jonathan LEnkler, LudovicMegel, CyrilleKarim, LoukmaneLaporte, DaphnéBecker, Hubert DDuchêne, Anne-MarieSissler, MMarechal-Drouard, LBiochimie 100:95-10625088301Pubmed2014Making proteins in the powerhouseHällberg, B MartinLarsson, Nils-GöranCell Metab. 20:226-4023149385Pubmed2013OXPHOS mutations and neurodegenerationKoopman, Werner J HDistelmaier, FelixSmeitink, JAWillems, Peter H G MEMBO J. 32:9-2922729854Pubmed2012Biogenesis of mitochondrial proteinsHerrmann, JMLongen, SebastianWeckbecker, DanielDepuydt, MatthieuAdv. Exp. Med. Biol. 748:41-6424911204Pubmed2014Mitochondrial protein synthesis: figuring the fundamentals, complexities and complications, of mammalian mitochondrial translationLightowlers, Robert NRozanska, AgataChrzanowska-Lightowlers, Zofia M AFEBS Lett. 588:2496-50322986124Pubmed2013Mitochondrial diseases: translation mattersPearce, SarahNezich, Catherine LauraSpinazzola, AMol. Cell. Neurosci. 55:1-1224842111Pubmed2014Mitochondria: Unusual features of the mammalian mitoribosomeRichman, Tara RRackham, OliverFilipovska, AleksandraInt. J. Biochem. Cell Biol. 53:115-2023958563Pubmed2014Supernumerary proteins of mitochondrial ribosomesRackham, OliverFilipovska, AleksandraBiochim. Biophys. Acta 1840:1227-3224362565Pubmed2014Architecture of the large subunit of the mammalian mitochondrial ribosomeGreber, Basil JBoehringer, DanielLeitner, AlexanderBieri, PhilippVoigts-Hoffmann, FelixErzberger, Jan PLeibundgut, MarcAebersold, RuediBan, NenadNature 505:515-924799711Pubmed2014Cryo-EM structure of the small subunit of the mammalian mitochondrial ribosomeKaushal, Prem SSharma, Manjuli RBooth, Timothy MHaque, Emdadul MTung, Chang-ShungSanbonmatsu, Karissa YSpremulli, LLAgrawal, Rajendra KProc. Natl. Acad. Sci. U.S.A. 111:7284-9inferred by electronic annotationIEAGOIEAReactome Database ID Release 7510184855Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10184855ReactomeR-SSC-727661Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-72766.1GO0006412GO biological processProtein synthesis is accomplished through the process of translation of an mRNA sequence into a polypeptide chain. This process can be divided into three distinct stages: initiation, elongation and termination. During the initiation phase, the two subunits of the ribosome are brought together to the translation start site on the mRNA where the polypeptide chain is to begin. Extension of the polypeptide chain occurs when a specific aminoacyl-tRNA, as determined by the template mRNA, binds an elongating ribosome. The protein chain is released from the ribosome when any one of three stop codons in the relevant reading frame on the mRNA is reached. Individual reactions at each one of these stages are catalyzed by a number of initiation, elongation and release factors, respectively.<br>Proteins destined for the endoplasmic reticulum (ER) contain a short sequence of hydrophobic amino acid residues (approximately 20 residues) at their N-termini. Upon protrusion of the signal sequence from the translating ribosome, the signal sequence is bound by the cytosolic signal recognition particle (SRP), translation is temporarily halted, and the SRP:nascent peptide:ribosome complex then docks with a SRP receptor complex on the ER membrane. There the nascent peptide:ribosome complex is transferred from the SRP complex to a translocon complex embedded in the ER membrane and reoriented so that the nascent polypeptide protrudes through a pore in the translocon into the ER lumen. Translation now resumes, the signal peptide is cleaved from the polypeptide by signal peptidase as the signal peptide emerges into the ER, and elongation proceeds with the growing polypeptide oriented into the ER lumen.<br>The 13 proteins encoded by the mitochondrial genome are translated within the mitochondrion by mitochondrial ribosomes (mitoribosomes) at the matrix face of the inner mitochondrial membrane. Mitochondrial translation reflects both the bacterial origin of the organelle and subsequent divergent evolution during symbiosis. Mitoribosomes have shorter rRNAs, mitochondria-specific proteins, and rearranged protein positions. Mitochondrial mRNAs have either no untranslated leaders or very short untranslated leaders of 1-3 nucleotides. Translation begins with N-formylmethionine, as in bacteria, and continues with cycles of aminoacyl-tRNA:TUFM:GTP binding, GTP hydrolysis and dissociation of TUFM:GDP. All 13 proteins encoded by the mitochondrial genome are hydrophobic inner membrane proteins which are inserted cotranslationally into the membrane by an interaction with OXA1L. Translation is terminated when MTRF1L:GTP recognizes a UAA or UAG codon at the A-site of the mitoribosome. The translated polypeptide is released and MRRF and GFM2:GTP act to dissociate the 55S ribosome into 28S and 39S subunits.inferred by electronic annotationIEAGOIEAProtein foldingProtein foldingThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Chaperonin-mediated protein foldingChaperonin-mediated protein foldingThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Association of TriC/CCT with target proteins during biosynthesisAssociation of TriC/CCT with target proteins during biosynthesisThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Association of CCT/TriC with sphingosine kinase 1Association of CCT/TriC with sphingosine kinase 1This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 101188201CCT/TRiC:ADP [cytosol]CCT/TRiC:ADPReactome DB_ID: 101187861UniProt:F1SB63TCP1UniProtF1SB631EQUAL556EQUALReactome DB_ID: 101188081UniProt:I3LCA2UniProtI3LCA22EQUAL548EQUALReactome DB_ID: 101187981UniProt:I3LR32CCT5UniProtI3LR322EQUAL541EQUALReactome DB_ID: 101188021UniProt:D0G0C9CCT7UniProtD0G0C91EQUAL543EQUALReactome DB_ID: 101187901UniProt:D0G0C8CCT2UniProtD0G0C82EQUAL535EQUALConverted from EntitySet in ReactomeReactome DB_ID: 101188181CCT6 [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityCCT6A [cytosol]UniProtI3L9J4Reactome DB_ID: 293708Reactome DB_ID: 101187941UniProt:F1SQN1UniProtF1SQN12EQUAL539EQUALReactome DB_ID: 101188041Ghost homologue of CCT3 [cytosol]Ghost homologue of CCT3Reactome Database ID Release 7510118820Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10118820ReactomeR-SSC-3904551Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-390455.1Reactome DB_ID: 101187821UniProt:A0A287AP24UniProtA0A287AP241EQUAL384EQUALReactome DB_ID: 101188221CCT/TRiC:ADP:Sphingosine kinase 1 [cytosol]CCT/TRiC:ADP:Sphingosine kinase 1Reactome DB_ID: 101188201Reactome DB_ID: 1011878211EQUAL384EQUALReactome Database ID Release 7510118822Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10118822ReactomeR-SSC-3912561Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-391256.1Reactome Database ID Release 7510118824Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10118824ReactomeR-SSC-3912661Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-391266.1CCT/TRiC facilitates folding of newly translated SK1 into its mature active form (Zebol et al., 2008)18775504Pubmed2008The CCT/TRiC chaperonin is required for maturation of sphingosine kinase 1Zebol, JRHewitt, NMMoretti, PALynn, HELake, JALi, PVadas, MAWattenberg, BWPitson, SMInt J Biochem Cell Biolinferred by electronic annotationIEAGOIEAReactome Database ID Release 7510186193Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10186193ReactomeR-SSC-3904711Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-390471.1TRiC has broad recognition specificities, but in the cell it interacts with only a defined set of substrates (Yam et al. 2008). Many of its substrates that are targeted during biosynthesis are conserved between mammals and yeast (Yam et al. 2008).19011634Pubmed2008Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologiesYam, AYXia, YLin, HTBurlingame, AGerstein, MFrydman, JNat Struct Mol Biol 15:1255-62inferred by electronic annotationIEAGOIEACooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta foldingCooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta foldingThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>TRiC/CCT binds unfolded G-protein beta subunitTRiC/CCT binds unfolded G-protein beta subunitThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 101188201Converted from EntitySet in ReactomeReactome DB_ID: 100987341G-protein beta subunit [cytosol]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityGNB1 [cytosol]UniProtI3LSK5Reactome DB_ID: 101719771Unfolded G-protein beta subunit:CCT/TRiC:ADP [cytosol]Unfolded G-protein beta subunit:CCT/TRiC:ADPReactome DB_ID: 101188201Converted from EntitySet in ReactomeReactome DB_ID: 100987341Reactome Database ID Release 7510171977Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10171977ReactomeR-SSC-68142111Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-6814211.1Reactome Database ID Release 7510171979Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10171979ReactomeR-SSC-68141191Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-6814119.1The TRiC/CCT chaperonin complex binds nascent, unfolded, G-protein beta subunit (GNB1, GNB2, GNB3, GNB4 or GNB5) (Wells et al. 2006). G-beta reaches a near-native state in the folding cavity of TRiC, except that TRiC cannot mediate the folding of the seven-bladed beta propeller of the G-protein beta to a stable conformation (Plimpton et al. 2015).16702223Pubmed2006Role of the chaperonin CCT/TRiC complex in G protein betagamma-dimer assemblyWells, Christopher ADingus, JaneHildebrandt, John DJ. Biol. Chem. 281:20221-3225675501Pubmed2015Structures of the Gβ-CCT and PhLP1-Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assemblyPlimpton, Rebecca LCuellar, JorgeLai, Chun Wan JAoba, TakumaMakaju, AmanFranklin, SarahMathis, Andrew DPrince, John TCarrascosa, José LValpuesta, Jose MWillardson, Barry MProc. Natl. Acad. Sci. U.S.A. 112:2413-8inferred by electronic annotationIEAGOIEAATP binds G-protein beta associated TRiC/CCTATP binds G-protein beta associated TRiC/CCTThis event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Reactome DB_ID: 101719771Reactome DB_ID: 1135921Reactome DB_ID: 101719831Unfolded G-protein beta subunit:CCT/TRiC:ATP [cytosol]Unfolded G-protein beta subunit:CCT/TRiC:ATPConverted from EntitySet in ReactomeReactome DB_ID: 100987341Reactome DB_ID: 101719811CCT/TriC:ATP [cytosol]CCT/TriC:ATPReactome DB_ID: 1011878611EQUAL556EQUALReactome DB_ID: 1011880812EQUAL548EQUALReactome DB_ID: 1011879812EQUAL541EQUALReactome DB_ID: 1011880211EQUAL543EQUALReactome DB_ID: 1011879012EQUAL535EQUALConverted from EntitySet in ReactomeReactome DB_ID: 101188181Reactome DB_ID: 1011879412EQUAL539EQUALReactome DB_ID: 101188041Reactome DB_ID: 1135928Reactome Database ID Release 7510171981Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10171981ReactomeR-SSC-3904741Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-390474.1Reactome Database ID Release 7510171983Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10171983ReactomeR-SSC-88505451Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-8850545.1Reactome DB_ID: 293701Reactome Database ID Release 7510171999Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10171999ReactomeR-SSC-68141241Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-SSC-6814124.1Based on structural studies of the TRiC/CCT chaperonin complex, the exchange of ADP for ATP enables conformational change of the chaperonin complex needed for folding of substrate proteins. It is assumed that TRiC/CCT-mediated folding of the G-protein beta subunit follows this universal pattern of TRiC/CCT functioning (Melki et al. 1997).9153422Pubmed1997Cytoplasmic chaperonin containing TCP-1: structural and functional characterizationMelki, RBatelier, GSoulié, SWilliams RC, JrB