Eukaryotic translation initiation (Homo sapiens)

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1782, 18, 19, 23, 251416267, 15202631, 113, 8, 18, 253, 27292, 18, 257, 15101, 5, 111, 2, 18, 21, 24...4, 6, 18, 22, 25...cytosoleIF1RPS6 RPL27 RPS6 RPL34 RPS15 Ceruloplasmin mRNA RPS11 RPS4Y1 RPL34 RPS3A RPL5 RPS23 EIF3G RPL24 RPL6 RPS2 RPL12 RPL13A RPL10A EIF3J 18S rRNA RPL12 RPL35 RPL18 RPL10 RPS27L RPS14 GTP RPL32 EIF3J RPL7 RPL3 RPS20 RPL24 EIF3A RPS4X EIF4E Met-tRNAi RPL32 RPL19 RPS13 EIF2B2 FAU 28S rRNA EIF4EBP1RPL39L RPSA RPS15 RPL36A RPS2 RPL21 GTP RPS4Y2 EIF4A2 RPS27 RPS26 EIF3D RPS19 RPS13 RPS21 RPL7A EIF3M RPL7A EIF3L RPS26 80S ribosomeRPL29 RPS15A EIF3F RPLP0 GTPRPL29 RPS29 RPS6 RPL13ARPS16 RPSA RPS18 RPS3 RPL9 RPS15A RPS19 RPSA RPLP2 RPS4Y2 RPS25 RPL23 EIF3L RPS27L RPS27A(77-156) EIF3D RPL30 RPSA RPL41 RPS7 RPS23 EIF2S1:EIF2S2:EIF2S3RPS20 PiEIF3B RPS21 EIF3F RPS13 RPS10 eIF2:GTPRPL38 28S rRNA EIF3H RPL7 Ceruloplasmin mRNA EIF2B3 EIF2S1 80S:Met-tRNAi:mRNA:eIF5B:GTPEIF2S3 RPS13 RPL40 RPL11 FAU EIF3H 18S rRNA RPL28 RPL38 EIF4B EIF1AX L13a kinaseRPS4Y2 RPS3 RPLP2 RPS4Y1 RPL21 EIF3G RPS10 RPL22 RPS14 RPS19 RPS27 RPS4X 5.8S rRNA RPL23A phospho-L13aassociated wth the 3' UTR GAIT elementof ceruloplasminmRNA within thetranslationinitiation complexRPL39 Met-tRNAiRPL24 RPS24 EIF2S2 RPL12 RPS21 RPL13 RPL10 EIF3A RPL22L1 RPS16 EIF3H RPS5 EIF2S1 RPL39L EIF3I FAU RPL30 RPS2 EIF3H EIF2S2 RPL14 RPS28 RPL28 EIF3C RPS3 RPL10 RPS3A RPS9 EIF2S3 RPL39L EIF3F 5.8S rRNA RPS3A RPL26L1 PiEIF3D RPS26 EIF3A RPL37 RPS7 RPS14 RPS19 RPS6 EIF3E RPS17 RPL19 GTP RPLP0 RPS25 RNA-binding protein in RNP (ribonucleoprotein) complexes RPL3L EIF2S2 EIF3K eIF5B:GDPFAU ATPeIF4E:4E-BPRPS14 RPL40 18S rRNA RPS18 EIF3C 18S rRNA 18S rRNA RPS28 Met-tRNAi RPL37A RPL22 RPL26 p-RPL13A28S rRNA RPL21 EIF2S2 ADPRPS9 RPLP2 RPLP1 RPS15 RPS19 RPL40 EIF3E 5.8S rRNA EIF4A2 5S rRNA RPS24 GTP EIF2S3 eIF2B subunitscomplexRPS3 RPS3 RPS4Y2 RPS27L RPL36A RPS6 RPL31 EIF3M RPL18A EIF3J RPS27L RPS12 EIF4E RPL18A RPS8 RPS4Y2 EIF4A2 RPL3 EIF2S1 RPS15A RPS20 RPL34 GTP RPS27A(77-156) EIF3A EIF2S3 60s ribosomalcomplex lackingL13a subunitRPS7 5S rRNA RPL10L GTP RPL10A RPL32 RPS17 RPL37A RPS17 RPL10L EIF3G EIF2S2 EIF3E EIF4B EIF3J RPS9 RPL13A RPL27A EIF4EBP1 RPL12 RPL36A EIF3F 18S rRNA EIF4A2 RPS19 EIF3C RPS10 5.8S rRNA RPS15A EIF3L RPL10L RPS15 EIF2S1 RPS18 RPL28 RPL10 RPS15A EIF1AXEIF5B RPL17 RPS10 RPL37A RPS29 RPS20 RPS10 EIF2B2 EIF4H RPS27A(77-156) RPS17 RPS6 RPS23 RPL10A RPL36 RPLP0 EIF2B3 RPL18A RPS29 40S:eIF3:eIF1ARPS4Y1 40S ribosomalcomplexRPL26 18S rRNA RPS29 RPS24 RPL41 43S:CeruloplasminmRNA:eIF4F:eIF4B:eIF4H:PABPATPEIF4G1 RPL27 5.8S rRNA RPS4Y1 RPL3L EIF3B RPL35A eIF4A subunitscomplexMet-tRNAi EIF3K RPL37 RPL35 RPLP2 RPSA EIF1AXRPS5 RPLP1 RPS29 RPL30 RPS6 RPL39 EIF5B RPL13 RPS20 EIF5RPS6 RPL6 RPL23A RPS28 RPL10 EIF3A RPL35A RPS28 RPS11 RPL39 EIF3L RPS3A RPL21 RPS11 RPS11 RPS2 EIF3M RPL22L1 EIF3K RPL36 RPS6 RPL18 Ceruloplasmin mRNA RPL38 RPL13 RPL10L RPS27 RPS27A(77-156) RPS18 RPS21 RPS11 EIF4E RNA-binding protein in RNP (ribonucleoprotein) complexes EIF3A RPS10 EIF4G1 RPS4Y2 EIF4A2 60S ribosomalcomplexRPL12 RPS5 RPL36AL RPS18 RPL37 EIF2S3 RPL5 RPS10 EIF3F RPS12 eIF3 subunitscomplexRPL4 18S rRNA EIF1AX RPS4Y1 EIF3I RPS17 RPL41 RPS12 RPS3 RPS25 RPS8 RPL41 EIF3B RPL4 RPLP1 eIF5B:GTPRPL7 EIF2S2 RPS5 Met-tRNAi RPS11 EIF4H Ceruloplasmin mRNA RPL3 RPS4Y1 Met-tRNAi RPL19 RPL11 RPLP0 RPS15 EIF4HRPS25 EIF3H RPS28 EIF5B RPS26 RPL9 RPL10A RPL34 RPL23 EIF4B RPL7 EIF2B5 RPS26 RPS2 EIF4A1 RPL22 EIF4H RPS14 Ceruloplasmin mRNA RPL18 RPL8 EIF1AX RPS27L EIF3M RPS16 ATPRPS3A EIF4A2 eIF1RPL3L RPS24 RPS26 RPS27 EIF2S3 Met-tRNAi EIF3I RPL7A RPS10 RPS14 RPS17 RPL26L1 RPS9 RPL39L RNA-binding proteinin RNP(ribonucleoprotein)complexesEIF3E RPL35A EIF4E RPL36AL RPL5 RPL36AL RPL5 EIF1AXRPS29 RPS13 RPL23A Ceruloplasmin mRNA EIF3D RPS11 EIF4G1 EIF3J EIF4A1 RPS21 RPL17 EIF1AXRPS29 RPS2 EIF4G1 RPS15A RPL9 RPS6 EIF4G1 RPL31 28S rRNA eIF2:GTPRPL26L1 EIF3A EIF1AX mRNPRPL36A RPS23 RPS4Y2 RPS7 RPS4Y1 PiRPS5 RPS7 RPS9 RPS27A(77-156) 48S complex43S:mRNA:eIF4F:eIF4B:eIF4HRPS29 EIF3F RPL13 EIF4B RPS4Y2 RPL27A RPS12 RPS11 GDP EIF2S2 EIF3I RPL23A RPL22 RPS17 RPL23 RPS20 EIF4A1 GTPEIF4E RPS20 RPS21 RPS19 EIF4A1 RPL15 RPL27A RPS5 RPS5 RPL11 EIF4G1RPL22L1 RPS8 RPL24 EIF2S1 eIF4FRPS27A(77-156) RPL35 RPS9 RPS9 RPL14 EIF3C RPLP1 RPSA RPL37 RPL31 FAU RPS26 RPS2 RPS17 RPL27 RPL26 RPL28 RPS13 RPS5 GTP RPL17 RPL40 RPS27L RPS25 RPL14 Ceruloplasmin mRNA RPS4X RPS5 RPS3 EIF3D PABPC1 RPS13 EIF3C RPL15 EIF4G1 Ceruloplasmin mRNA RPS4X RPS25 RPL3L EIF2B1 EIF2S2 EIF4A2 EIF2S1 RPS7 Ceruloplasmin mRNA RPS25 FAU RPS19 RPL37A RPL3 RPS4Y1 EIF5EIF3L RPLP2 RPS17 Ceruloplasmin mRNA RPL31 RPL23A RPS4Y1 RPL14 RPS24 RPS4X GTP RPS15A RPL30 EIF4A1 EIF1AX EIF3K RPL29 RPL35 RPS27 RPS23 EIF2S1 RPS15A RPS23 RPL26L1 EIF2S3 PABPC1RPS27A(77-156) RPL6 RPS8 RPS26 RPL4 RPS7 RPS26 RPL32 RPL29 RPS7 RPS23 43S complexEIF3E RPL5 RPS4X RPL27A RPS16 RPS25 RPS27A(77-156) RPL23 RPS20 RPS16 EIF4A1 RPL4 RPL39 RPS26 RPS3 RPS27L RPS19 RPSA RPS27 RPL41 EIF3J RPS29 RPS3A RPS25 RPL11 RPL37 RPS28 ternary complexGTP RPS12 EIF2B1 RPL35 RPSA RPS8 EIF2S1 RPS3A RPS18 RPS14 RPS15 RPL36AL RPS12 eIF4F:mRNPRPS20 EIF3K EIF4EEIF3E RPS17 18S rRNA RPS3 RPS25 RPS18 RPS24 RPL8 RPS21 RPL4 EIF3B 5S rRNA RPS27A(77-156) RPS8 RPL23 RPL6 RPS24 EIF3G RPS28 RPS15 18S rRNA Met-tRNAi RPL15 RPL11 RPL6 EIF4A1 EIF3B GTP RPS27 RPS27 RPS4Y2 RPL17 RPL14 GDP RPL37A RPS21 RPL18A RPS3A RPL17 RPL18 EIF3F EIF4A2 EIF2B4 RPS8 PiRPS18 RPS9 RPS20 RPS13 EIF4B RPS15A RPS8 EIF3H RPL39L RPS27L RPS13 EIF3K EIF2S3 EIF1AX RPS19 28S rRNA RPS20 RPS16 RPS15 mRNA:eIF4F:eIF4B:eIF4HRPS2 CeruloplasminmRNA:eIF4F:eIF4B:eIF4HRPL28 EIF5RPL22 RPS18 EIF3M 40S:Met-tRNAi:mRNAEIF4BRPS4Y2 EIF3J EIF3D RPS15 RPS10 EIF2S1 RPL10A EIF3C RPS28 RPS12 RPL34 RPL15 GDP RPL7A EIF2S3 GDPRPS27L RPL18A FAU RPL27 RPS10 RPS3A RPL7 RPS26 RPS16 RPLP1 RPS27L EIF4A2 RPS3 RPL36A RPS18 RPS9 EIF2S2 EIF3M RPS14 RPL40 EIF2S2 RPL36AL 5S rRNA RPL8 RPS2 EIF4H RPS24 RPS12 RPL7A RPS4X EIF3L RPS4Y2 EIF2S3 RPS4Y1 RPS18 RPL26 RPLP0 RPSA RPS23 RPS12 EIF2S3 RPS23 ADPRPS9 RPL3 RPS16 EIF4E RPL15 RPS13 RPS9 EIF3B RPS10 RPS28 EIF3E RPL35A RPS21 eIF2:GDPRPS16 EIF3G RPL36 RPL13A EIF2S2 RPL36 RPS27 PABPC1 RPS17 RPL38 EIF4H RPS8 RPL30 RPL10L RPL26L1 EIF3I RPS27 RPS23 RPS24 RPS12 EIF3K EIF3D RPL19 RPS24 RPS11 RPS27 RPS27L EIF3I RPS4X EIF3M RPS14 RPS16 RPS15 RPS2 80S:Met-tRNAi:mRNARPS4Y1 RPL22L1 RPL35A EIF4B RPS2 RPS27A(77-156) RPS11 EIF2B4 FAU EIF4E RPL31 RPL38 RPS7 RPL39 RPS3 RPS15A EIF3L RPS23 EIF4A1 EIF3C RPL9 EIF4E RPS29 RPS4X eIF2:GDP: eIF2BEIF3G RPS15A EIF2S1 RPS7 RPSA RPS16 5S rRNA EIF3I FAU RPL8 EIF2B5 RPS24 RPL8 RPL3L RPS14 RPS8 RPS3A FAU RPS28 EIF3G RPS4X RPL24 Met-tRNAi RPS12 EIF4H RPS15 RPL29 RPS19 RPL13A EIF2S3 RPS29 EIF2S1 RPS5 RPS14 RPL21 RPL22L1 p-RPL13A RPL13 RPSA RPS7 EIF4G1 FAU RPL9 RPS6 EIF4E RPL27A RPS28 RPS5 RPL19 EIF3H RPL27 RPS27A(77-156) RPL36 RPS13 18S rRNA Met-tRNAi RPL26 RPS25 RPS21 EIF2S1 EIF4G1 RPS21 RPS8 EIF2S1:EIF2S2:EIF2S3RPL32 RPS3A RPS11 EIF2S2 EIF3B RPS4X RPL18 Ceruloplasmin mRNA EIF4A1 9, 129, 129, 129, 129, 12139, 129, 129, 129, 129, 12


Description

Initiation 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.

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.

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.

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Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 72613
Reactome-version 
Reactome version: 61

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Ontology Terms

 

Bibliography

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  1. Pause A, Belsham GJ, Gingras AC, Donzé O, Lin TA, Lawrence JC, Sonenberg N.; ''Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function.''; PubMed Europe PMC Scholia
  2. Sampath P, Mazumder B, Seshadri V, Fox PL.; ''Transcript-selective translational silencing by gamma interferon is directed by a novel structural element in the ceruloplasmin mRNA 3' untranslated region.''; PubMed Europe PMC Scholia
  3. Pestova TV, Borukhov SI, Hellen CU.; ''Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons.''; PubMed Europe PMC Scholia
  4. Mazumder B, Sampath P, Seshadri V, Maitra RK, DiCorleto PE, Fox PL.; ''Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control.''; PubMed Europe PMC Scholia
  5. Grifo JA, Tahara SM, Morgan MA, Shatkin AJ, Merrick WC.; ''New initiation factor activity required for globin mRNA translation.''; PubMed Europe PMC Scholia
  6. Safer B, Adams SL, Anderson WF, Merrick WC.; ''Binding of MET-TRNAf and GTP to homogeneous initiation factor MP.''; PubMed Europe PMC Scholia
  7. Pestova TV, Shatsky IN, Hellen CU.; ''Functional 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.''; PubMed Europe PMC Scholia
  8. Merrick WC.; ''Eukaryotic protein synthesis: still a mystery.''; PubMed Europe PMC Scholia
  9. Kozak M.; ''Evaluation of the "scanning model" for initiation of protein synthesis in eucaryotes.''; PubMed Europe PMC Scholia
  10. Chakrabarti A, Maitra U.; ''Function of eukaryotic initiation factor 5 in the formation of an 80 S ribosomal polypeptide chain initiation complex.''; PubMed Europe PMC Scholia
  11. Trachsel H, Erni B, Schreier MH, Staehelin T.; ''Initiation of mammalian protein synthesis. II. The assembly of the initiation complex with purified initiation factors.''; PubMed Europe PMC Scholia
  12. Rowlands AG, Panniers R, Henshaw EC.; ''The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2.''; PubMed Europe PMC Scholia
  13. Iost I, Dreyfus M, Linder P.; ''Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase.''; PubMed Europe PMC Scholia
  14. Benne R, Hershey JW.; ''The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes.''; PubMed Europe PMC Scholia
  15. Schreier MH, Erni B, Staehelin T.; ''Initiation of mammalian protein synthesis. I. Purification and characterization of seven initiation factors.''; PubMed Europe PMC Scholia
  16. Sonenberg N, Rupprecht KM, Hecht SM, Shatkin AJ.; ''Eukaryotic mRNA cap binding protein: purification by affinity chromatography on sepharose-coupled m7GDP.''; PubMed Europe PMC Scholia
  17. Dever TE, Wei CL, Benkowski LA, Browning K, Merrick WC, Hershey JW.; ''Determination of the amino acid sequence of rabbit, human, and wheat germ protein synthesis factor eIF-4C by cloning and chemical sequencing.''; PubMed Europe PMC Scholia
  18. Merrick WC, Kemper WM, Anderson WF.; ''Purification and characterization of homogeneous initiation factor M2A from rabbit reticulocytes.''; PubMed Europe PMC Scholia
  19. Asano K, Clayton J, Shalev A, Hinnebusch AG.; ''A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo.''; PubMed Europe PMC Scholia
  20. Peterson DT, Merrick WC, Safer B.; ''Binding and release of radiolabeled eukaryotic initiation factors 2 and 3 during 80 S initiation complex formation.''; PubMed Europe PMC Scholia
  21. Goumans H, Thomas A, Verhoeven A, Voorma HO, Benne R.; ''The role of eIF-4C in protein synthesis initiation complex formation.''; PubMed Europe PMC Scholia
  22. Imataka H, Gradi A, Sonenberg N.; ''A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation.''; PubMed Europe PMC Scholia
  23. Chuang RY, Weaver PL, Liu Z, Chang TH.; ''Requirement of the DEAD-Box protein ded1p for messenger RNA translation.''; PubMed Europe PMC Scholia
  24. Lahn BT, Page DC.; ''Functional coherence of the human Y chromosome.''; PubMed Europe PMC Scholia
  25. Yoder-Hill J, Pause A, Sonenberg N, Merrick WC.; ''The p46 subunit of eukaryotic initiation factor (eIF)-4F exchanges with eIF-4A.''; PubMed Europe PMC Scholia
  26. Pestova TV, Lomakin IB, Lee JH, Choi SK, Dever TE, Hellen CU.; ''The joining of ribosomal subunits in eukaryotes requires eIF5B.''; PubMed Europe PMC Scholia
  27. Damoc E, Fraser CS, Zhou M, Videler H, Mayeur GL, Hershey JW, Doudna JA, Robinson CV, Leary JA.; ''Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry.''; PubMed Europe PMC Scholia
  28. Majumdar R, Bandyopadhyay A, Maitra U.; ''Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40 S preinitiation complex.''; PubMed Europe PMC Scholia
  29. Dholakia JN, Wahba AJ.; ''Mechanism of the nucleotide exchange reaction in eukaryotic polypeptide chain initiation. Characterization of the guanine nucleotide exchange factor as a GTP-binding protein.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
128373view17:49, 3 February 2024Ash iyerFixing error (check)
128372view17:45, 3 February 2024Ash iyeridentifier added
128371view17:43, 3 February 2024Ash iyereif1 identifier added.
128323view00:28, 1 February 2024EweitzOntology Term : 'translation pathway' added !
117720view12:33, 22 May 2021EweitzModified title
114979view16:50, 25 January 2021ReactomeTeamReactome version 75
113423view11:49, 2 November 2020ReactomeTeamReactome version 74
112625view16:00, 9 October 2020ReactomeTeamReactome version 73
101541view11:40, 1 November 2018ReactomeTeamreactome version 66
101076view21:23, 31 October 2018ReactomeTeamreactome version 65
100606view19:57, 31 October 2018ReactomeTeamreactome version 64
100157view16:42, 31 October 2018ReactomeTeamreactome version 63
99707view15:11, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99288view12:46, 31 October 2018ReactomeTeamreactome version 62
93969view13:48, 16 August 2017ReactomeTeamreactome version 61
93568view11:27, 9 August 2017ReactomeTeamreactome version 61
86670view09:23, 11 July 2016ReactomeTeamreactome version 56
83337view10:49, 18 November 2015ReactomeTeamVersion54
76969view08:25, 17 July 2014ReactomeTeamFixed remaining interactions
76674view12:04, 16 July 2014ReactomeTeamFixed remaining interactions
76136view13:23, 11 June 2014AnweshaRe-fixing comment source
75707view11:05, 10 June 2014ReactomeTeamReactome 48 Update
75062view13:57, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74706view08:46, 30 April 2014ReactomeTeamReactome46
45250view18:36, 7 October 2011AlexanderPicoOntology Term : 'translation initiation pathway' added !
42035view21:51, 4 March 2011MaintBotAutomatic update
39838view05:52, 21 January 2011MaintBotNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
18S rRNA ProteinX03205 (EMBL)
28S rRNA ProteinM11167 (EMBL)
40S ribosomal complexComplexR-HSA-72392 (Reactome)
40S:Met-tRNAi:mRNAComplexR-HSA-72508 (Reactome)
40S:eIF3:eIF1AComplexR-HSA-72570 (Reactome)
43S complexComplexR-HSA-72571 (Reactome)
43S:

Ceruloplasmin

mRNA:eIF4F:eIF4B:eIF4H:PABP
ComplexR-HSA-156804 (Reactome)
43S:mRNA:eIF4F:eIF4B:eIF4HComplexR-HSA-72592 (Reactome)
48S complexComplexR-HSA-72594 (Reactome)
5.8S rRNA ProteinJ01866 (EMBL)
5S rRNA ProteinV00589 (EMBL)
60S ribosomal complexComplexR-HSA-72499 (Reactome)
60s ribosomal

complex lacking

L13a subunit
ComplexR-HSA-156817 (Reactome)
80S ribosomeComplexR-HSA-72500 (Reactome)
80S:Met-tRNAi:mRNA:eIF5B:GTPComplexR-HSA-72504 (Reactome)
80S:Met-tRNAi:mRNAComplexR-HSA-72505 (Reactome)
ADPMetaboliteCHEBI:16761 (ChEBI)
ATPMetaboliteCHEBI:15422 (ChEBI)
Ceruloplasmin mRNA:eIF4F:eIF4B:eIF4HComplexR-HSA-156809 (Reactome)
Ceruloplasmin mRNA ProteinM13699 (EMBL)
EIF1AX ProteinP47813 (Uniprot-TrEMBL)
EIF1AXProteinP47813 (Uniprot-TrEMBL)
EIF2B1 ProteinQ14232 (Uniprot-TrEMBL)
EIF2B2 ProteinP49770 (Uniprot-TrEMBL)
EIF2B3 ProteinQ9NR50 (Uniprot-TrEMBL)
EIF2B4 ProteinQ9UI10 (Uniprot-TrEMBL)
EIF2B5 ProteinQ13144 (Uniprot-TrEMBL)
EIF2S1 ProteinP05198 (Uniprot-TrEMBL)
EIF2S1:EIF2S2:EIF2S3ComplexR-HSA-72515 (Reactome)
EIF2S2 ProteinP20042 (Uniprot-TrEMBL)
EIF2S3 ProteinP41091 (Uniprot-TrEMBL)
EIF3A ProteinQ14152 (Uniprot-TrEMBL)
EIF3B ProteinP55884 (Uniprot-TrEMBL)
EIF3C ProteinQ99613 (Uniprot-TrEMBL)
EIF3D ProteinO15371 (Uniprot-TrEMBL)
EIF3E ProteinP60228 (Uniprot-TrEMBL)
EIF3F ProteinO00303 (Uniprot-TrEMBL)
EIF3G ProteinO75821 (Uniprot-TrEMBL)
EIF3H ProteinO15372 (Uniprot-TrEMBL)
EIF3I ProteinQ13347 (Uniprot-TrEMBL)
EIF3J ProteinO75822 (Uniprot-TrEMBL)
EIF3K ProteinQ9UBQ5 (Uniprot-TrEMBL)
EIF3L ProteinQ9Y262 (Uniprot-TrEMBL)
EIF3M ProteinQ7L2H7 (Uniprot-TrEMBL)
EIF4A1 ProteinP60842 (Uniprot-TrEMBL)
EIF4A2 ProteinQ14240 (Uniprot-TrEMBL)
EIF4B ProteinP23588 (Uniprot-TrEMBL)
EIF4BProteinP23588 (Uniprot-TrEMBL)
EIF4E ProteinP06730 (Uniprot-TrEMBL)
EIF4EBP1 ProteinQ13541 (Uniprot-TrEMBL)
EIF4EBP1ProteinQ13541 (Uniprot-TrEMBL)
EIF4EProteinP06730 (Uniprot-TrEMBL)
EIF4G1 ProteinQ04637 (Uniprot-TrEMBL)
EIF4G1ProteinQ04637 (Uniprot-TrEMBL)
EIF4H ProteinQ15056 (Uniprot-TrEMBL)
EIF4HProteinQ15056 (Uniprot-TrEMBL)
EIF5B ProteinO60841 (Uniprot-TrEMBL)
EIF5ProteinP55010 (Uniprot-TrEMBL)
FAU ProteinP62861 (Uniprot-TrEMBL)
GDP MetaboliteCHEBI:17552 (ChEBI)
GDPMetaboliteCHEBI:17552 (ChEBI)
GTP MetaboliteCHEBI:15996 (ChEBI)
GTPMetaboliteCHEBI:15996 (ChEBI)
L13a kinaseR-HSA-170641 (Reactome)
Met-tRNAi R-NUL-72393 (Reactome)
Met-tRNAiR-NUL-72393 (Reactome)
PABPC1 ProteinP11940 (Uniprot-TrEMBL)
PABPC1ProteinP11940 (Uniprot-TrEMBL)
PiMetaboliteCHEBI:18367 (ChEBI)
RNA-binding protein

in RNP (ribonucleoprotein)

complexes
R-NUL-72595 (Reactome)
RNA-binding protein in RNP (ribonucleoprotein) complexes R-NUL-72595 (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)
RPL13AProteinP40429 (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)
eIF1R-NUL-72617 (Reactome)
eIF2:GDP: eIF2BComplexR-HSA-72529 (Reactome)
eIF2:GDPComplexR-HSA-72530 (Reactome)
eIF2:GTPComplexR-HSA-72531 (Reactome)
eIF2B subunits complexComplexR-HSA-72526 (Reactome)
eIF3 subunits complexComplexR-HSA-72555 (Reactome)
eIF4A subunits complexComplexR-HSA-72576 (Reactome)
eIF4E:4E-BPComplexR-HSA-72581 (Reactome)
eIF4F:mRNPComplexR-HSA-72597 (Reactome)
eIF4FComplexR-HSA-72587 (Reactome)
eIF5B:GDPComplexR-HSA-72502 (Reactome)
eIF5B:GTPComplexR-HSA-72503 (Reactome)
mRNA:eIF4F:eIF4B:eIF4HComplexR-HSA-72593 (Reactome)
mRNPComplexR-HSA-72596 (Reactome)
p-RPL13A ProteinP40429 (Uniprot-TrEMBL)
p-RPL13AProteinP40429 (Uniprot-TrEMBL)
phospho-L13a

associated wth the 3' UTR GAIT element of ceruloplasmin mRNA within the translation

initiation complex
ComplexR-HSA-156824 (Reactome)
ternary complexComplexR-HSA-72532 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
40S ribosomal complexArrowR-HSA-72673 (Reactome)
40S ribosomal complexR-HSA-72676 (Reactome)
40S:Met-tRNAi:mRNAArrowR-HSA-72619 (Reactome)
40S:Met-tRNAi:mRNAR-HSA-72672 (Reactome)
40S:eIF3:eIF1AArrowR-HSA-72676 (Reactome)
40S:eIF3:eIF1AR-HSA-72691 (Reactome)
43S complexArrowR-HSA-72691 (Reactome)
43S complexR-HSA-156808 (Reactome)
43S complexR-HSA-157849 (Reactome)
43S:

Ceruloplasmin

mRNA:eIF4F:eIF4B:eIF4H:PABP
ArrowR-HSA-156808 (Reactome)
43S:

Ceruloplasmin

mRNA:eIF4F:eIF4B:eIF4H:PABP
R-HSA-156823 (Reactome)
43S:mRNA:eIF4F:eIF4B:eIF4HArrowR-HSA-157849 (Reactome)
43S:mRNA:eIF4F:eIF4B:eIF4HR-HSA-72621 (Reactome)
48S complexArrowR-HSA-72621 (Reactome)
48S complexArrowR-HSA-72697 (Reactome)
48S complexR-HSA-72619 (Reactome)
48S complexR-HSA-72697 (Reactome)
60S ribosomal complexArrowR-HSA-72673 (Reactome)
60S ribosomal complexR-HSA-156826 (Reactome)
60S ribosomal complexR-HSA-72672 (Reactome)
60s ribosomal

complex lacking

L13a subunit
ArrowR-HSA-156826 (Reactome)
80S ribosomeR-HSA-72673 (Reactome)
80S:Met-tRNAi:mRNA:eIF5B:GTPArrowR-HSA-72672 (Reactome)
80S:Met-tRNAi:mRNA:eIF5B:GTPR-HSA-72671 (Reactome)
80S:Met-tRNAi:mRNAArrowR-HSA-72671 (Reactome)
ADPArrowR-HSA-72621 (Reactome)
ADPArrowR-HSA-72647 (Reactome)
ATPArrowR-HSA-72621 (Reactome)
ATPR-HSA-72621 (Reactome)
ATPR-HSA-72647 (Reactome)
Ceruloplasmin mRNA:eIF4F:eIF4B:eIF4HR-HSA-156808 (Reactome)
EIF1AXArrowR-HSA-156808 (Reactome)
EIF1AXArrowR-HSA-157849 (Reactome)
EIF1AXArrowR-HSA-72619 (Reactome)
EIF1AXArrowR-HSA-72673 (Reactome)
EIF1AXArrowR-HSA-72697 (Reactome)
EIF1AXR-HSA-156808 (Reactome)
EIF1AXR-HSA-157849 (Reactome)
EIF1AXR-HSA-72673 (Reactome)
EIF1AXR-HSA-72676 (Reactome)
EIF1AXR-HSA-72697 (Reactome)
EIF2S1:EIF2S2:EIF2S3ArrowR-HSA-72697 (Reactome)
EIF2S1:EIF2S2:EIF2S3R-HSA-72663 (Reactome)
EIF2S1:EIF2S2:EIF2S3R-HSA-72697 (Reactome)
EIF4BArrowR-HSA-72619 (Reactome)
EIF4BR-HSA-72647 (Reactome)
EIF4Bmim-catalysisR-HSA-72647 (Reactome)
EIF4EArrowR-HSA-72619 (Reactome)
EIF4EArrowR-HSA-72622 (Reactome)
EIF4EBP1ArrowR-HSA-72622 (Reactome)
EIF4ER-HSA-72631 (Reactome)
EIF4G1ArrowR-HSA-72619 (Reactome)
EIF4G1R-HSA-72631 (Reactome)
EIF4HArrowR-HSA-72619 (Reactome)
EIF4HR-HSA-72647 (Reactome)
EIF4Hmim-catalysisR-HSA-72647 (Reactome)
EIF5ArrowR-HSA-72619 (Reactome)
EIF5ArrowR-HSA-72697 (Reactome)
EIF5R-HSA-72619 (Reactome)
EIF5R-HSA-72697 (Reactome)
GDPArrowR-HSA-72722 (Reactome)
GTPArrowR-HSA-72669 (Reactome)
GTPR-HSA-72663 (Reactome)
GTPR-HSA-72722 (Reactome)
L13a kinasemim-catalysisR-HSA-156832 (Reactome)
Met-tRNAiR-HSA-72669 (Reactome)
PABPC1R-HSA-156808 (Reactome)
PiArrowR-HSA-72619 (Reactome)
PiArrowR-HSA-72621 (Reactome)
PiArrowR-HSA-72647 (Reactome)
PiArrowR-HSA-72671 (Reactome)
R-HSA-156808 (Reactome) The 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.
R-HSA-156823 (Reactome) Although 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.
R-HSA-156826 (Reactome) The 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.
R-HSA-156832 (Reactome) The 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.
R-HSA-157849 (Reactome) The 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.
R-HSA-72619 (Reactome) Once the Met-tRNAi has recognized the AUG, eIF2-bound GTP is hydrolyzed. The 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. Release of the initiation factors from 40S leaves the Met-tRNAi in the ribosomal P-site base-paired to the start codon on the mRNA.
R-HSA-72621 (Reactome) The 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.
R-HSA-72622 (Reactome) eIF4E gets released from the inactive eIF4E:4EBP complex.
R-HSA-72631 (Reactome) eIF4A interacts with eIF4G, and eIF4E interacts with the amino-terminal domain of eIF4G to form the cap-binding complex eIF4F.
R-HSA-72635 (Reactome) The factor eIF4E within the eIF4F (cap-binding) complex directly binds the 5'-cap on eukaryotic mRNAs. Note that the mRNA is in complex with cytoplasmic proteins constituting an mRNP complex.
R-HSA-72647 (Reactome) The 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.
R-HSA-72663 (Reactome) Activation of eIF2 through direct binding of GTP.
R-HSA-72669 (Reactome) The ternary complex forms upon binding of the initiator methionyl-tRNA to the active eIF2:GTP complex.
R-HSA-72670 (Reactome) Inactive eIF2:GDP binds eIF2B to form an eIF2:GDP:eIF2B intermediate.
R-HSA-72671 (Reactome) Once 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.
R-HSA-72672 (Reactome) Joining of the 60S subunit to form the 80S ribosome is catalyzed by the presence of GTP-bound eIF5B.
R-HSA-72673 (Reactome) 80S monosomes dissociate into 40S and 60S ribosomal subunits. eIF1A promotes this dissociation.
R-HSA-72676 (Reactome) eIF3 and eIF1A bind to the 40S ribosomal subunit.
R-HSA-72691 (Reactome) The ternary complex (Met-tRNAi:eIF2:GTP) binds to the complex formed by the 40S subunit, eIF3 and eIF1A, to form the 43S complex. eIF1A promotes binding of the ternary complex to the 40S subunit within 43S. The initiator methionyl-tRNA from the ternary complex is positioned at the ribosomal P site.
R-HSA-72697 (Reactome) The AUG initiation codon in the mRNA is recognized by base pairing with the anticodon of the Met-tRNAi. This reaction requires eIF1, eIF1A, eIF2 and eIF5.
R-HSA-72722 (Reactome) eIF2B is a guanine nucleotide releasing factor that is required to cause GDP release so that a new GTP molecule can bind and activate eIF2, so that it can be reused.
RNA-binding protein

in RNP (ribonucleoprotein)

complexes
ArrowR-HSA-72647 (Reactome)
RPL13AArrowR-HSA-156826 (Reactome)
RPL13AR-HSA-156832 (Reactome)
eIF1ArrowR-HSA-72697 (Reactome)
eIF1R-HSA-72619 (Reactome)
eIF1R-HSA-72697 (Reactome)
eIF1mim-catalysisR-HSA-72621 (Reactome)
eIF1mim-catalysisR-HSA-72697 (Reactome)
eIF2:GDP: eIF2BArrowR-HSA-72670 (Reactome)
eIF2:GDP: eIF2BR-HSA-72722 (Reactome)
eIF2:GDPArrowR-HSA-72619 (Reactome)
eIF2:GDPR-HSA-72670 (Reactome)
eIF2:GTPArrowR-HSA-72663 (Reactome)
eIF2:GTPArrowR-HSA-72722 (Reactome)
eIF2:GTPR-HSA-72669 (Reactome)
eIF2B subunits complexArrowR-HSA-72722 (Reactome)
eIF2B subunits complexR-HSA-72670 (Reactome)
eIF2B subunits complexmim-catalysisR-HSA-72722 (Reactome)
eIF3 subunits complexArrowR-HSA-72619 (Reactome)
eIF3 subunits complexR-HSA-72676 (Reactome)
eIF4A subunits complexArrowR-HSA-72619 (Reactome)
eIF4A subunits complexArrowR-HSA-72647 (Reactome)
eIF4A subunits complexR-HSA-72631 (Reactome)
eIF4A subunits complexR-HSA-72647 (Reactome)
eIF4A subunits complexmim-catalysisR-HSA-72647 (Reactome)
eIF4E:4E-BPR-HSA-72622 (Reactome)
eIF4F:mRNPArrowR-HSA-72635 (Reactome)
eIF4F:mRNPR-HSA-72647 (Reactome)
eIF4FArrowR-HSA-72631 (Reactome)
eIF4FR-HSA-72635 (Reactome)
eIF5B:GDPArrowR-HSA-72671 (Reactome)
eIF5B:GTPR-HSA-72672 (Reactome)
mRNA:eIF4F:eIF4B:eIF4HArrowR-HSA-72647 (Reactome)
mRNA:eIF4F:eIF4B:eIF4HR-HSA-157849 (Reactome)
mRNPR-HSA-72635 (Reactome)
p-RPL13AArrowR-HSA-156832 (Reactome)
p-RPL13AR-HSA-156823 (Reactome)
phospho-L13a

associated wth the 3' UTR GAIT element of ceruloplasmin mRNA within the translation

initiation complex
ArrowR-HSA-156823 (Reactome)
ternary complexArrowR-HSA-72669 (Reactome)
ternary complexR-HSA-72691 (Reactome)

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