Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts with RNF139; the interaction leads to protein translation inhibitions in a ubiquitination-dependent manner.
Function:
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of posttermination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation.
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
4.
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L.
,
Schick M.
,
Neubert P.
,
Schatten R.
,
Henze S.
,
Korn B.
Submitted (2004-06) to the EMBL/GenBank/DDBJ databases
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
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Cited for: INTERACTION WITH RPS6KB1;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX;CHARACTERIZATION OF THE EIF-3 COMPLEX;CLEAVAGE OF INITIATOR METHIONINE;ACETYLATION AT ALA-2;PHOSPHORYLATION AT SER-258;MASS SPECTROMETRY
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-238;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX;CHARACTERIZATION OF THE EIF-3 COMPLEX;MASS SPECTROMETRY;INTERACTION WITH EIF3B; EIF3H AND EIF3M
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Cited for: FUNCTION AS A DEUBIQUITINATING ENZYME;CATALYTIC ACTIVITY;INTERACTION WITH DTX1
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
Vaild Sequence:
