Relation Results

Summary

Name 43S_pre_initiation_complex
Primary ID SIGNOR-C453
Type complex
Formed by 40S cytosolic small ribosomal subunit, EIF3_complex, Ternary_GTP_eIF2_tRNA_complex, EIF1, EIF5
Relations 6
Pathways Initiation of Translation

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Type: Score: Layout: SPV 
0.20.7580.7580.650.20.2Ternary_GTP_eIF2_tRNA_complex43S_pre_initiation_complexEIF5EIF1EIF3_complex48S_initiation_complex40S cytosolic small ribosomal subunit

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Relations
Regulator
Mechanism
target
score ℹ
+ Ternary_GTP_eIF2_tRNA_complexform complex img/form-complex.png binding 43S_pre_initiation_complex 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-269159 Homo sapiens
pmid sentence
In eukaryotes, mRNA is recruited to the 43S pre-initiation complex (43S PIC), which consists of the 40S ribosomal subunit, translation initiation factors eIF1, eIF1A, eIF3, eIF5, and a ternary complex (TC) composed of eIF2, GTP and Met-tRNAiMet. 43S PIC binds to the 5′ end of the mRNA and scans along the 5′ untranslated region (5′UTR) in the 3′ direction to find the start codon (AUG) within the context of an optimal Kozak sequence. Start codon recognition stabilizes the 48S initiation complex (48S IC), initiates dissociation of eIF1, eIF1A, eIF2 and eIF5, and promotes recruitment of the 60S ribosomal subunit to form 80S IC ready to enter the elongation cycle of protein synthesis.
Publications: 1 Organism: Homo Sapiens
Pathways:Initiation of Translation
+ EIF5form complex img/form-complex.png binding 43S_pre_initiation_complex 0.758
Identifier Residue Sequence Organism Cell Line
SIGNOR-269163 Homo sapiens
pmid sentence
In eukaryotes, mRNA is recruited to the 43S pre-initiation complex (43S PIC), which consists of the 40S ribosomal subunit, translation initiation factors eIF1, eIF1A, eIF3, eIF5, and a ternary complex (TC) composed of eIF2, GTP and Met-tRNAiMet. 43S PIC binds to the 5′ end of the mRNA and scans along the 5′ untranslated region (5′UTR) in the 3′ direction to find the start codon (AUG) within the context of an optimal Kozak sequence. Start codon recognition stabilizes the 48S initiation complex (48S IC), initiates dissociation of eIF1, eIF1A, eIF2 and eIF5, and promotes recruitment of the 60S ribosomal subunit to form 80S IC ready to enter the elongation cycle of protein synthesis.
Publications: 1 Organism: Homo Sapiens
Pathways:Initiation of Translation
+ EIF1form complex img/form-complex.png binding 43S_pre_initiation_complex 0.758
Identifier Residue Sequence Organism Cell Line
SIGNOR-269161 Homo sapiens
pmid sentence
In eukaryotes, mRNA is recruited to the 43S pre-initiation complex (43S PIC), which consists of the 40S ribosomal subunit, translation initiation factors eIF1, eIF1A, eIF3, eIF5, and a ternary complex (TC) composed of eIF2, GTP and Met-tRNAiMet. 43S PIC binds to the 5′ end of the mRNA and scans along the 5′ untranslated region (5′UTR) in the 3′ direction to find the start codon (AUG) within the context of an optimal Kozak sequence. Start codon recognition stabilizes the 48S initiation complex (48S IC), initiates dissociation of eIF1, eIF1A, eIF2 and eIF5, and promotes recruitment of the 60S ribosomal subunit to form 80S IC ready to enter the elongation cycle of protein synthesis.
Publications: 1 Organism: Homo Sapiens
Pathways:Initiation of Translation
+ EIF3_complexform complex img/form-complex.png binding 43S_pre_initiation_complex 0.65
Identifier Residue Sequence Organism Cell Line
SIGNOR-269162 Homo sapiens
pmid sentence
In eukaryotes, mRNA is recruited to the 43S pre-initiation complex (43S PIC), which consists of the 40S ribosomal subunit, translation initiation factors eIF1, eIF1A, eIF3, eIF5, and a ternary complex (TC) composed of eIF2, GTP and Met-tRNAiMet. 43S PIC binds to the 5′ end of the mRNA and scans along the 5′ untranslated region (5′UTR) in the 3′ direction to find the start codon (AUG) within the context of an optimal Kozak sequence. Start codon recognition stabilizes the 48S initiation complex (48S IC), initiates dissociation of eIF1, eIF1A, eIF2 and eIF5, and promotes recruitment of the 60S ribosomal subunit to form 80S IC ready to enter the elongation cycle of protein synthesis.
Publications: 1 Organism: Homo Sapiens
Pathways:Initiation of Translation
+ 43S_pre_initiation_complexform complex img/form-complex.png binding 48S_initiation_complex 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-269167 Homo sapiens
pmid sentence
In eukaryotes, mRNA is recruited to the 43S pre-initiation complex (43S PIC), which consists of the 40S ribosomal subunit, translation initiation factors eIF1, eIF1A, eIF3, eIF5, and a ternary complex (TC) composed of eIF2, GTP and Met-tRNAiMet. 43S PIC binds to the 5′ end of the mRNA and scans along the 5′ untranslated region (5′UTR) in the 3′ direction to find the start codon (AUG) within the context of an optimal Kozak sequence. Start codon recognition stabilizes the 48S initiation complex (48S IC), initiates dissociation of eIF1, eIF1A, eIF2 and eIF5, and promotes recruitment of the 60S ribosomal subunit to form 80S IC ready to enter the elongation cycle of protein synthesis.
Publications: 1 Organism: Homo Sapiens
Pathways:Initiation of Translation
+ 40S cytosolic small ribosomal subunitform complex img/form-complex.png binding 43S_pre_initiation_complex 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-269160 Homo sapiens
pmid sentence
In eukaryotes, mRNA is recruited to the 43S pre-initiation complex (43S PIC), which consists of the 40S ribosomal subunit, translation initiation factors eIF1, eIF1A, eIF3, eIF5, and a ternary complex (TC) composed of eIF2, GTP and Met-tRNAiMet. 43S PIC binds to the 5′ end of the mRNA and scans along the 5′ untranslated region (5′UTR) in the 3′ direction to find the start codon (AUG) within the context of an optimal Kozak sequence. Start codon recognition stabilizes the 48S initiation complex (48S IC), initiates dissociation of eIF1, eIF1A, eIF2 and eIF5, and promotes recruitment of the 60S ribosomal subunit to form 80S IC ready to enter the elongation cycle of protein synthesis.
Publications: 1 Organism: Homo Sapiens
Pathways:Initiation of Translation
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