Eukaryotic translation elongation (Homo sapiens)

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ArcPathVisio Brace Ellipse EndoplasmicReticulum GolgiApparatus HexagonPathVisio MimDegradation Mitochondria Octagon PentagonPathVisio Rectangle RoundedRectangle SarcoplasmicReticulum TriangleEquilateralEast TrianglePathVisio none cytosolEEF1B2Elongation complexwith growingpeptide chaineEF1A:GTPEEF1A1-like proteinsEEF2eEF1A:GTP:aminoacyl-tRNA complex80S:aminoacyltRNA:mRNA:eEF1A:GTPeEF2:GDPeEF2:GTPAminoacyl-tRNA80S:Met-tRNAi:mRNA:aminoacyl-tRNA80SRibosome:mRNA:peptidyl-tRNA with elongating peptideEEF1A1eEF1B:GDP exchangecomplexPiGTPPi80S ribosomeeEF1B complexGTPEEF1G80S:Met-tRNAi:mRNAeEF1A:GDPEEF1DRPL7Gln-tRNA(Gln)RPL35RPS11RPS24Ala-tRNA(Ala)RPS20RPS18RPL10ARPL27RPS4Y2RPL34Met-tRNAi18S rRNARPS10Arg-tRNA(Arg)RPS27Asn-tRNA(Asn)RPL26L1RPS4Y1RPL28RPL40RPL26RPS6Tyr-tRNA(Tyr)5.8S rRNARPL36ARPS16RPL19RPS15RPL3LRPL36ALRPL24RPS21Phe-tRNA(Phe)RPL9RPL23ARPL37Cys-tRNA(Cys)28S rRNARPL3Pro-tRNA(Pro)RPS9RPL18ARPLP1RPL12RPL39LLys-tRNA(Lys)RPS8RPL32Leu-tRNA(Leu)RPS27LRPS3RPL6Ser-tRNA(Ser)RPLP0RPL29RPS15ARPL31RPL37AMet-tRNA(Met)RPL38RPL36RPL27AVal-tRNA(Val)RPS2RPS19Asp-tRNA(Asp)RPL22RPL8RPS7RPL13ARPS29RPL4Thr-tRNA(Thr)RPL13RPS3ARPL5Gly-tRNA(Gly)Trp-tRNA(Trp)RPS13RPS25RPL10RPS5RPL15RPS4XRPS12RPL39His-tRNA(His)Glu-tRNA(Glu)RPL10LRPL21RPL11RPS23Ile-tRNA(Ile)RPLP2RPL17RPS28RPL7ARPS27A(77-156)RPL30RPL35ARPS17RPL23mRNARPL14RPL22L1FAURPS26RPL41RPL185S rRNARPS14RPSARPL36RPL18RPS25RPS13RPL3LRPL29RPLP0RPS4XRPL22RPL27RPLP2RPL10RPL12FAURPS14RPL30RPS11RPL27ARPL36ARPS12RPS20RPS27LRPL23ARPS10RPL39RPS6RPLP1RPL10ARPL38RPS19mRNARPL21RPSARPL31RPL10LRPL28RPL11RPL26L1RPL32RPL8RPL37ARPL15RPS9RPS24RPS15ARPS18peptidyl-tRNA with elongated peptideRPL7ARPS4Y1RPL3RPS28RPL26RPL9RPS29RPS265S rRNARPL39LRPS17RPL4RPS8RPL245.8S rRNARPL19RPS27RPL23RPL35A28S rRNARPL14RPL18ARPL37RPL17RPS16RPL7RPL36ALRPS3RPS4Y2RPS21RPL22L1RPL13RPL6RPL13ARPS5RPL35RPS3ARPL41RPS15RPS2RPL5RPS27A(77-156)RPL40RPL3418S rRNARPS23RPS7EEF2GTPRPLP0RPS24RPL39RPS6RPL26L1RPL5RPL3L5S rRNARPL10LFAURPL26RPL15RPS16RPS14RPL18ARPL36ARPL7ARPL415.8S rRNARPS7RPL37RPL27peptidyl-tRNA with elongated peptideRPS12RPS3RPL36ALRPL22L1RPL7RPS19RPS10RPS9RPL10RPL11RPL24RPL14RPSARPL39LRPL32RPS2RPLP1RPS26RPL4RPL3RPL38RPS11RPS20RPS15RPL13RPS4XRPL27ARPL28RPS18RPS15ARPS8RPS27LRPL40RPL31RPL23A28S rRNARPL12RPS4Y1RPS27RPL10ARPL35RPL29RPS5RPS13RPL22RPS4Y2RPS29RPL618S rRNARPS17RPS23RPS25RPS3ARPL34RPL30RPL23RPS21RPS27A(77-156)RPL36mRNARPL18RPL35ARPL8RPL37ARPS28RPL19RPL9RPL17RPL13ARPL21RPLP2EEF1A1GTPEEF1A2EEF1A1P5EEF1A1EEF1GEEF1B2EEF1DRPL35ARPLP0RPL30RPL31RPS11RPS4Y2Met-tRNAiRPS6RPS27A(77-156)RPL10LRPL12RPL26L1RPL22L1RPS27L5S rRNARPL10A18S rRNARPL14RPL9RPL4RPL13ARPL18RPS15RPL21RPLP1RPL36ARPL23RPS26RPL3LRPS8RPL13RPS20RPL39LRPL36RPL19RPS21RPL37RPLP2RPL22RPL75.8S rRNARPL24RPL8RPL5RPS18RPS12RPL28RPL38RPS3RPL39RPS24RPS7RPL37A28S rRNARPL7ARPL35RPS23RPS29RPS14RPL26RPS25RPL3RPS17RPL23ARPL17RPS4XRPL27ARPL41RPS13RPS16RPS9RPS3ARPL18ARPL29RPSARPS28RPS19RPL27RPL34RPL11RPL32mRNARPL40RPL15RPL6RPS2RPS10RPS27RPS15ARPS5RPL36ALRPS4Y1RPL10FAUAla-tRNA(Ala)Arg-tRNA(Arg)Pro-tRNA(Pro)Ser-tRNA(Ser)Ile-tRNA(Ile)Phe-tRNA(Phe)Cys-tRNA(Cys)Lys-tRNA(Lys)Asp-tRNA(Asp)His-tRNA(His)Trp-tRNA(Trp)Val-tRNA(Val)Gly-tRNA(Gly)Tyr-tRNA(Tyr)Glu-tRNA(Glu)Asn-tRNA(Asn)GTPEEF1A1Leu-tRNA(Leu)Gln-tRNA(Gln)Thr-tRNA(Thr)Met-tRNA(Met)EEF2GDPTrp-tRNA(Trp)Gln-tRNA(Gln)RPS9Ala-tRNA(Ala)RPL40RPS19RPL22RPS4XRPS13RPL12RPL18ARPL11RPL35RPL29Leu-tRNA(Leu)RPS27LRPL215S rRNAIle-tRNA(Ile)RPS16RPL13ARPL36RPLP2RPL39LMet-tRNAiRPSARPL3LRPS17Cys-tRNA(Cys)RPL10A5.8S rRNARPS27A(77-156)RPL34GTPRPL31RPS8RPS10Arg-tRNA(Arg)RPS24RPS20RPL4RPL35ARPL7RPL23RPL26L1Tyr-tRNA(Tyr)RPS2Gly-tRNA(Gly)18S rRNARPS11Asp-tRNA(Asp)RPL19RPL23APro-tRNA(Pro)RPL6RPS2828S rRNAVal-tRNA(Val)RPL41RPL17RPS21RPS4Y2RPL39RPL36ALRPL13RPL37RPL8RPS5RPS6RPL5RPL37ARPL10LAsn-tRNA(Asn)RPL22L1RPS14RPL32Glu-tRNA(Glu)RPL14RPL27Phe-tRNA(Phe)RPL24EEF1A1RPL3RPL36ARPLP0RPS26RPS7RPS27RPL10Thr-tRNA(Thr)RPL27AmRNARPL38RPS23RPS3RPL28RPS15RPL18RPL26RPS12RPL7ARPS4Y1Ser-tRNA(Ser)RPLP1His-tRNA(His)RPS15AFAUMet-tRNA(Met)RPS3ARPS18RPL30Lys-tRNA(Lys)RPS29RPL9RPS25RPL15Asp-tRNA(Asp)Gly-tRNA(Gly)Cys-tRNA(Cys)Thr-tRNA(Thr)Leu-tRNA(Leu)Phe-tRNA(Phe)Asn-tRNA(Asn)Gln-tRNA(Gln)His-tRNA(His)Lys-tRNA(Lys)Tyr-tRNA(Tyr)Ser-tRNA(Ser)Ile-tRNA(Ile)Glu-tRNA(Glu)Arg-tRNA(Arg)Trp-tRNA(Trp)Val-tRNA(Val)Ala-tRNA(Ala)Met-tRNA(Met)Pro-tRNA(Pro)EEF1DEEF1GGDPEEF1B2RPS28RPL38RPL14RPL18RPS4Y1RPL39LRPS24RPS25RPS4Y2RPS29RPS3RPS18RPL36ARPS9RPL26L1RPL36RPL12RPS19RPL19RPL35ARPL13RPL95.8S rRNARPL11RPL3RPL26RPL5RPL24RPL2928S rRNARPL34RPL15RPL21RPL27RPS27A(77-156)RPS5RPS15RPL3LRPS16RPL13ARPS6RPS17RPS15ARPS26RPL18ARPL10L5S rRNARPS20RPL23RPL23ARPL35RPL36ALRPL6RPS8RPL8RPL7ARPL27ARPL28RPL40RPL37RPS14RPS13RPSARPS11RPS2RPL39RPL30RPS23RPS10RPL31RPS21RPS3AFAURPL37ARPS27LRPL7RPL10RPL10ARPLP0RPLP1RPS27RPL41RPLP2RPL22RPL4RPS4XRPL22L1RPL32RPS7RPS12RPL1718S rRNAEEF1A1GDPName: Eukaryotic translation elongationOrganism: Homo sapiens


Description

The 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.
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.
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. View original pathway at Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 156842
Reactome-version 
Reactome version: 75
Reactome Author 
Reactome Author: Gopinathrao, G

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Bibliography

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  1. Carvalho MD, Carvalho JF, Merrick WC.; ''Biological characterization of various forms of elongation factor 1 from rabbit reticulocytes.''; PubMed Europe PMC Scholia
  2. Pérez JM, Siegal G, Kriek J, Hård K, Dijk J, Canters GW, Möller W.; ''The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli.''; PubMed Europe PMC Scholia
  3. Van Ness BG, Howard JB, Bodley JW.; ''ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-amino acid and its hydrolysis products.''; PubMed Europe PMC Scholia
  4. Veremieva M, Khoruzhenko A, Zaicev S, Negrutskii B, El'skaya A.; ''Unbalanced expression of the translation complex eEF1 subunits in human cardioesophageal carcinoma.''; PubMed Europe PMC Scholia
  5. Guillot D, Penin F, Di Pietro A, Sontag B, Lavergne JP, Reboud JP.; ''GTP binding to elongation factor eEF-2 unmasks a tryptophan residue required for biological activity.''; PubMed Europe PMC Scholia
  6. Van Ness BG, Howard JB, Bodley JW.; ''ADP-ribosylation of elongation factor 2 by diphtheria toxin. NMR spectra and proposed structures of ribosyl-diphthamide and its hydrolysis products.''; PubMed Europe PMC Scholia
  7. Kapp LD, Lorsch JR.; ''The molecular mechanics of eukaryotic translation.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
117719view12:33, 22 May 2021EweitzModified title
114891
Reactome
view16:40, 25 January 2021ReactomeTeamReactome version 75
113337view11:41, 2 November 2020ReactomeTeamReactome version 74
112548view15:51, 9 October 2020ReactomeTeamReactome version 73
101462view11:32, 1 November 2018ReactomeTeamreactome version 66
101000view21:12, 31 October 2018ReactomeTeamreactome version 65
100536view19:46, 31 October 2018ReactomeTeamreactome version 64
100083view16:30, 31 October 2018ReactomeTeamreactome version 63
99634view15:02, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99240view12:44, 31 October 2018ReactomeTeamreactome version 62
93857view13:41, 16 August 2017ReactomeTeamreactome version 61
93420view11:23, 9 August 2017ReactomeTeamreactome version 61
86508view09:19, 11 July 2016ReactomeTeamreactome version 56
83399view11:07, 18 November 2015ReactomeTeamVersion54
81592view13:08, 21 August 2015ReactomeTeamVersion53
77053view08:35, 17 July 2014ReactomeTeamFixed remaining interactions
76758view12:11, 16 July 2014ReactomeTeamFixed remaining interactions
76083view10:14, 11 June 2014ReactomeTeamRe-fixing comment source
75793view11:32, 10 June 2014ReactomeTeamReactome 48 Update
75143view14:09, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74790view08:52, 30 April 2014ReactomeTeamReactome46
69032view17:50, 8 July 2013MaintBotUpdated to 2013 gpml schema
45249view18:35, 7 October 2011AlexanderPicoOntology Term : 'translation elongation pathway' added !
42034view21:51, 4 March 2011MaintBotAutomatic update
39837view05:52, 21 January 2011MaintBotNew pathway

External references

DataNodes

View all...
Name  ↓Type  ↓Database reference  ↓Comment  ↓
18S rRNA ProteinX03205 (EMBL)
28S rRNA ProteinM11167 (EMBL)
5.8S rRNA ProteinJ01866 (EMBL)
5S rRNA ProteinV00589 (EMBL)
80S Ribosome:mRNA:peptidyl-tRNA with elongating peptideComplexR-HSA-141952 (Reactome)
80S ribosomeComplexR-HSA-72500 (Reactome)
80S:Met-tRNAi:mRNA:aminoacyl-tRNAComplexR-HSA-72506 (Reactome)
80S:Met-tRNAi:mRNAComplexR-HSA-72505 (Reactome)
80S:aminoacyl tRNA:mRNA:eEF1A:GTPComplexR-HSA-156903 (Reactome)
Ala-tRNA(Ala) R-HSA-379700 (Reactome)
Aminoacyl-tRNAComplexR-HSA-37001 (Reactome)
Arg-tRNA(Arg) R-HSA-379720 (Reactome)
Asn-tRNA(Asn) R-HSA-379728 (Reactome)
Asp-tRNA(Asp) R-HSA-379707 (Reactome)
Cys-tRNA(Cys) R-HSA-379719 (Reactome)
EEF1A1 ProteinP68104 (Uniprot-TrEMBL)
EEF1A1-like proteinsComplexR-HSA-3907260 (Reactome) This CandidateSet contains sequences identified by William Pearson's analysis of Reactome catalyst entities. Catalyst entity sequences were used to identify analagous sequences that shared overall homology and active site homology. Sequences in this Candidate set were identified in an April 24, 2012 analysis.
EEF1A1P5 ProteinQ5VTE0 (Uniprot-TrEMBL)
EEF1A1ProteinP68104 (Uniprot-TrEMBL)
EEF1A2 ProteinQ05639 (Uniprot-TrEMBL)
EEF1B2 ProteinP24534 (Uniprot-TrEMBL)
EEF1B2ProteinP24534 (Uniprot-TrEMBL)
EEF1D ProteinP29692 (Uniprot-TrEMBL)
EEF1DProteinP29692 (Uniprot-TrEMBL)
EEF1G ProteinP26641 (Uniprot-TrEMBL)
EEF1GProteinP26641 (Uniprot-TrEMBL)
EEF2 ProteinP13639 (Uniprot-TrEMBL)
EEF2ProteinP13639 (Uniprot-TrEMBL)
Elongation complex

with growing

peptide chain
ComplexR-HSA-156927 (Reactome)
FAU ProteinP62861 (Uniprot-TrEMBL)
GDP MetaboliteCHEBI:17552 (ChEBI)
GTP MetaboliteCHEBI:15996 (ChEBI)
GTPMetaboliteCHEBI:15996 (ChEBI)
Gln-tRNA(Gln) R-HSA-379772 (Reactome)
Glu-tRNA(Glu) R-HSA-379751 (Reactome)
Gly-tRNA(Gly) R-HSA-379784 (Reactome)
His-tRNA(His) R-HSA-379786 (Reactome)
Ile-tRNA(Ile) R-HSA-379787 (Reactome)
Leu-tRNA(Leu) R-HSA-379757 (Reactome)
Lys-tRNA(Lys) R-HSA-379736 (Reactome)
Met-tRNA(Met) R-HSA-379794 (Reactome)
Met-tRNAi R-ALL-72393 (Reactome)
Phe-tRNA(Phe) R-HSA-379792 (Reactome)
PiMetaboliteCHEBI:43474 (ChEBI)
Pro-tRNA(Pro) R-HSA-379746 (Reactome)
RPL10 ProteinP27635 (Uniprot-TrEMBL)
RPL10A ProteinP62906 (Uniprot-TrEMBL)
RPL10L ProteinQ96L21 (Uniprot-TrEMBL)
RPL11 ProteinP62913 (Uniprot-TrEMBL)
RPL12 ProteinP30050 (Uniprot-TrEMBL)
RPL13 ProteinP26373 (Uniprot-TrEMBL)
RPL13A ProteinP40429 (Uniprot-TrEMBL)
RPL14 ProteinP50914 (Uniprot-TrEMBL)
RPL15 ProteinP61313 (Uniprot-TrEMBL)
RPL17 ProteinP18621 (Uniprot-TrEMBL)
RPL18 ProteinQ07020 (Uniprot-TrEMBL)
RPL18A ProteinQ02543 (Uniprot-TrEMBL)
RPL19 ProteinP84098 (Uniprot-TrEMBL)
RPL21 ProteinP46778 (Uniprot-TrEMBL)
RPL22 ProteinP35268 (Uniprot-TrEMBL)
RPL22L1 ProteinQ6P5R6 (Uniprot-TrEMBL)
RPL23 ProteinP62829 (Uniprot-TrEMBL)
RPL23A ProteinP62750 (Uniprot-TrEMBL)
RPL24 ProteinP83731 (Uniprot-TrEMBL)
RPL26 ProteinP61254 (Uniprot-TrEMBL)
RPL26L1 ProteinQ9UNX3 (Uniprot-TrEMBL)
RPL27 ProteinP61353 (Uniprot-TrEMBL)
RPL27A ProteinP46776 (Uniprot-TrEMBL)
RPL28 ProteinP46779 (Uniprot-TrEMBL)
RPL29 ProteinP47914 (Uniprot-TrEMBL)
RPL3 ProteinP39023 (Uniprot-TrEMBL)
RPL30 ProteinP62888 (Uniprot-TrEMBL)
RPL31 ProteinP62899 (Uniprot-TrEMBL)
RPL32 ProteinP62910 (Uniprot-TrEMBL)
RPL34 ProteinP49207 (Uniprot-TrEMBL)
RPL35 ProteinP42766 (Uniprot-TrEMBL)
RPL35A ProteinP18077 (Uniprot-TrEMBL)
RPL36 ProteinQ9Y3U8 (Uniprot-TrEMBL)
RPL36A ProteinP83881 (Uniprot-TrEMBL)
RPL36AL ProteinQ969Q0 (Uniprot-TrEMBL)
RPL37 ProteinP61927 (Uniprot-TrEMBL)
RPL37A ProteinP61513 (Uniprot-TrEMBL)
RPL38 ProteinP63173 (Uniprot-TrEMBL)
RPL39 ProteinP62891 (Uniprot-TrEMBL)
RPL39L ProteinQ96EH5 (Uniprot-TrEMBL)
RPL3L ProteinQ92901 (Uniprot-TrEMBL)
RPL4 ProteinP36578 (Uniprot-TrEMBL)
RPL40 ProteinP62987 (Uniprot-TrEMBL)
RPL41 ProteinP62945 (Uniprot-TrEMBL)
RPL5 ProteinP46777 (Uniprot-TrEMBL)
RPL6 ProteinQ02878 (Uniprot-TrEMBL)
RPL7 ProteinP18124 (Uniprot-TrEMBL)
RPL7A ProteinP62424 (Uniprot-TrEMBL)
RPL8 ProteinP62917 (Uniprot-TrEMBL)
RPL9 ProteinP32969 (Uniprot-TrEMBL)
RPLP0 ProteinP05388 (Uniprot-TrEMBL)
RPLP1 ProteinP05386 (Uniprot-TrEMBL)
RPLP2 ProteinP05387 (Uniprot-TrEMBL)
RPS10 ProteinP46783 (Uniprot-TrEMBL)
RPS11 ProteinP62280 (Uniprot-TrEMBL)
RPS12 ProteinP25398 (Uniprot-TrEMBL)
RPS13 ProteinP62277 (Uniprot-TrEMBL)
RPS14 ProteinP62263 (Uniprot-TrEMBL)
RPS15 ProteinP62841 (Uniprot-TrEMBL)
RPS15A ProteinP62244 (Uniprot-TrEMBL)
RPS16 ProteinP62249 (Uniprot-TrEMBL)
RPS17 ProteinP08708 (Uniprot-TrEMBL)
RPS18 ProteinP62269 (Uniprot-TrEMBL)
RPS19 ProteinP39019 (Uniprot-TrEMBL)
RPS2 ProteinP15880 (Uniprot-TrEMBL)
RPS20 ProteinP60866 (Uniprot-TrEMBL)
RPS21 ProteinP63220 (Uniprot-TrEMBL)
RPS23 ProteinP62266 (Uniprot-TrEMBL)
RPS24 ProteinP62847 (Uniprot-TrEMBL)
RPS25 ProteinP62851 (Uniprot-TrEMBL)
RPS26 ProteinP62854 (Uniprot-TrEMBL)
RPS27 ProteinP42677 (Uniprot-TrEMBL)
RPS27A(77-156) ProteinP62979 (Uniprot-TrEMBL)
RPS27L ProteinQ71UM5 (Uniprot-TrEMBL)
RPS28 ProteinP62857 (Uniprot-TrEMBL)
RPS29 ProteinP62273 (Uniprot-TrEMBL)
RPS3 ProteinP23396 (Uniprot-TrEMBL)
RPS3A ProteinP61247 (Uniprot-TrEMBL)
RPS4X ProteinP62701 (Uniprot-TrEMBL)
RPS4Y1 ProteinP22090 (Uniprot-TrEMBL)
RPS4Y2 ProteinQ8TD47 (Uniprot-TrEMBL)
RPS5 ProteinP46782 (Uniprot-TrEMBL)
RPS6 ProteinP62753 (Uniprot-TrEMBL)
RPS7 ProteinP62081 (Uniprot-TrEMBL)
RPS8 ProteinP62241 (Uniprot-TrEMBL)
RPS9 ProteinP46781 (Uniprot-TrEMBL)
RPSA ProteinP08865 (Uniprot-TrEMBL)
Ser-tRNA(Ser) R-HSA-379738 (Reactome)
Thr-tRNA(Thr) R-HSA-379783 (Reactome)
Trp-tRNA(Trp) R-HSA-379765 (Reactome)
Tyr-tRNA(Tyr) R-HSA-379785 (Reactome)
Val-tRNA(Val) R-HSA-379790 (Reactome)
eEF1A:GDPComplexR-HSA-156929 (Reactome)
eEF1A:GTP:aminoacyl-tRNA complexComplexR-HSA-156911 (Reactome)
eEF1A:GTPComplexR-HSA-156921 (Reactome)
eEF1B complexComplexR-HSA-156920 (Reactome)
eEF1B:GDP exchange complexComplexR-HSA-156917 (Reactome)
eEF2:GDPComplexR-HSA-156922 (Reactome)
eEF2:GTPComplexR-HSA-156916 (Reactome)
mRNA R-HSA-72323 (Reactome)
peptidyl-tRNA with elongated peptide R-ALL-141678 (Reactome)

Annotated Interactions

View all...
Source  ↓Target  ↓Type  ↓Database reference  ↓Comment  ↓
80S Ribosome:mRNA:peptidyl-tRNA with elongating peptideArrowR-HSA-156915 (Reactome)
80S ribosomemim-catalysisR-HSA-156912 (Reactome)
80S ribosomemim-catalysisR-HSA-156923 (Reactome)
80S:Met-tRNAi:mRNA:aminoacyl-tRNAArrowR-HSA-156923 (Reactome)
80S:Met-tRNAi:mRNA:aminoacyl-tRNAR-HSA-156912 (Reactome)
80S:Met-tRNAi:mRNAR-HSA-156907 (Reactome)
80S:aminoacyl tRNA:mRNA:eEF1A:GTPArrowR-HSA-156907 (Reactome)
80S:aminoacyl tRNA:mRNA:eEF1A:GTPR-HSA-156923 (Reactome)
Aminoacyl-tRNAR-HSA-156908 (Reactome)
EEF1A1-like proteinsmim-catalysisR-HSA-156909 (Reactome)
EEF1A1R-HSA-156909 (Reactome)
EEF1B2R-HSA-156910 (Reactome)
EEF1DR-HSA-156910 (Reactome)
EEF1GR-HSA-156910 (Reactome)
EEF2R-HSA-156930 (Reactome)
Elongation complex

with growing

peptide chain
ArrowR-HSA-156912 (Reactome)
Elongation complex

with growing

peptide chain
R-HSA-156915 (Reactome)
GTPR-HSA-156909 (Reactome)
GTPR-HSA-156913 (Reactome)
GTPR-HSA-156930 (Reactome)
PiArrowR-HSA-156915 (Reactome)
PiArrowR-HSA-156923 (Reactome)
R-HSA-156907 (Reactome) Once the correct codon-anticodon match occurs between the mRNA and aa-tRNA, the decoding event triggers GTP hydrolysis on eEF1A. The resulting conformational change releases the aa-tRNA to the A-site, and GDP bound form eEF1A is released from the ribosome.
Insight into the mechanics of this system has been obtained from earlier works with rabbit reticulocytes and the E.coli system.
This process is illustrated below with: an amino acyl-tRNA with an amino acid, a peptidyl-tRNA with a growing peptide and a ribosome with A,P and E sites to accommodate these two forms of tRNA.
R-HSA-156908 (Reactome) The binding of eEF1A:GTP to aminoacyl tRNA (aa-tRNA) results in the formation of a ternary complex (eEF1A:GTP:aa-tRNA). Human eEF1A and rabbit eEF1A are 100% identical, and prokaryotic homologue of eEF1A (EF-Tu) shows 59% identity in the GTP-binding domain.This process is illustrated below with: a GTP molecule in white and eEF1A protein in yellow.
R-HSA-156909 (Reactome) The cycle of elongation starts with an empty ribosomal A-site and the peptidyl-tRNA in the P-site. eEF1A is activated by GTP binding and allows for the subsequent binding of aminoacyl-tRNA (aa-tRNA).This process is illustrated below with a GTP molecule in white and eEF1A protein in yellow.
R-HSA-156910 (Reactome) At 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).

R-HSA-156912 (Reactome) The A- and P-sites of the ribosome positions the aa-tRNA and peptidyl-tRNA such that a nucleophilic attack can occur between the amine group of the A-site aa-tRNA and the carbonyl group of the growing peptide chain on the P-site tRNA, resulting in the formation of a peptide bond. The carboxyl end of the peptide chain is uncoupled from the tRNA molecule in the P-site and forms a new peptide bond with the amino acid that is in the A-site.
This process is illustrated below with: 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.
R-HSA-156913 (Reactome) The 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.
This process is illustrated below with a GTP molecule in white and eEF1A protein in yellow.The three subunits of eEF1B are also shown.
R-HSA-156915 (Reactome) Following peptide bond formation, GTP-bound eEF2 catalyzes the translocation of the deacylated tRNA in the P-site and the peptidyl-tRNA in the A-site (the pre-translocation state) into the E- and P- sites (the post-translocation state), respectively. Thus, the mRNA advances by three bases to expose the next codon in the A-site. After translocation, GDP-bound eEF2 leaves the ribosome to allow another round of elongation. eEF2 is reactivated by the release of GDP and binds GTP for subsequent rounds.
This process is illustrated below with 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 is also shown.
R-HSA-156923 (Reactome) Once the correct codon-anticodon match occurs between the mRNA and aa-tRNA, the decoding event triggers GTP hydrolysis on eEF1A. The resulting conformational change releases the aa-tRNA to the A-site, and GDP bound form of eEF1A is released from the ribosome.
This process is illustrated below with: an amino acyl-tRNA with an amino acid,a peptidyl-tRNA with a growing peptide and a ribosome with A,P and E sites to accommodate these two forms of tRNA.
R-HSA-156930 (Reactome) At 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.

This reaction takes place in the 'cytosol' (Guillot et al. 2013).

eEF1A:GDPArrowR-HSA-156915 (Reactome)
eEF1A:GDPArrowR-HSA-156923 (Reactome)
eEF1A:GDPR-HSA-156913 (Reactome)
eEF1A:GTP:aminoacyl-tRNA complexArrowR-HSA-156908 (Reactome)
eEF1A:GTP:aminoacyl-tRNA complexR-HSA-156907 (Reactome)
eEF1A:GTP:aminoacyl-tRNA complexR-HSA-156915 (Reactome)
eEF1A:GTPArrowR-HSA-156909 (Reactome)
eEF1A:GTPArrowR-HSA-156913 (Reactome)
eEF1A:GTPR-HSA-156908 (Reactome)
eEF1B complexArrowR-HSA-156910 (Reactome)
eEF1B complexR-HSA-156913 (Reactome)
eEF1B complexmim-catalysisR-HSA-156913 (Reactome)
eEF1B:GDP exchange complexArrowR-HSA-156913 (Reactome)
eEF2:GDPArrowR-HSA-156915 (Reactome)
eEF2:GTPArrowR-HSA-156930 (Reactome)
eEF2:GTPR-HSA-156915 (Reactome)
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