EIF3J (eukaryotic translation initiation factor 3 subunit J) is a cytoplasmic accessory subunit of the 13-subunit eIF-3 complex, the largest eukaryotic translation initiation factor. eIF-3 associates with the 40S ribosomal subunit and orchestrates several steps of cap-dependent translation initiation, promoting recruitment of eIF-1, eIF-1A, the eIF-2-GTP-Met-tRNAi ternary complex and eIF-5 to form the 43S pre-initiation complex, stimulating mRNA recruitment and scanning to the AUG start codon, and contributing to disassembly/recycling of post-termination ribosomal complexes while preventing premature 40S-60S subunit joining. EIF3J is a loosely associated, sub-stoichiometric ("labile") subunit that docks onto the complex through EIF3B; it positions near the 40S mRNA entry channel/decoding region and is required for stable binding of eIF-3 (and its subcomplexes) to the 40S subunit, thereby modulating mRNA loading and 40S availability. It is a non-catalytic accessory factor (its initiation-factor activity is contributed in the context of the assembled complex) and is phosphorylated in a serum-stimulation-dependent manner.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
|
GO:0005852
eukaryotic translation initiation factor 3 complex
|
IBA
GO_REF:0000033 |
ACCEPT |
Summary: EIF3J is a (labile) subunit of the eIF-3 complex, well supported across eukaryotes and by direct human evidence. This is the core cellular-component annotation.
Reason: EIF3J is documented as a component of the 13-subunit eIF-3 complex, binding via EIF3B; the IBA is corroborated by IDA/IPI evidence.
Supporting Evidence:
file:human/EIF3J/EIF3J-uniprot.txt
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex
|
|
GO:0001732
formation of cytoplasmic translation initiation complex
|
IEA
GO_REF:0000104 |
ACCEPT |
Summary: As part of eIF-3, EIF3J participates in assembly of the 43S/48S translation initiation complexes on the 40S subunit. A genuine core process annotation.
Reason: eIF-3 facilitates recruitment of initiation factors and ternary complex to form the 43S PIC; EIF3J contributes to this assembly.
Supporting Evidence:
file:human/EIF3J/EIF3J-uniprot.txt
facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to
|
|
GO:0002183
cytoplasmic translational initiation
|
IEA
GO_REF:0000104 |
ACCEPT |
Summary: EIF3J participates in cytoplasmic translation initiation as an eIF-3 subunit. This is the core biological process.
Reason: eIF-3 is required for several steps in initiation of protein synthesis; this is EIF3J's central biological role.
Supporting Evidence:
file:human/EIF3J/EIF3J-uniprot.txt
required for several steps in the initiation of protein synthesis
|
|
GO:0003743
translation initiation factor activity
|
IEA
GO_REF:0000120 |
ACCEPT |
Summary: EIF3J contributes translation initiation factor activity as an accessory subunit of eIF-3. The activity is exerted in the context of the assembled complex rather than by EIF3J alone.
Reason: The core molecular function of EIF3J is translation initiation factor activity via the eIF-3 complex; note the curated experimental annotations use the contributes_to qualifier, reflecting its accessory role.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0003743 translation initiation factor activity molecular_function ECO:0000501 IEA
|
|
GO:0005737
cytoplasm
|
IEA
GO_REF:0000120 |
ACCEPT |
Summary: EIF3J is cytoplasmic, consistent with its role in cytoplasmic translation initiation.
Reason: Cytoplasm is the documented subcellular location and the site of translation initiation.
Supporting Evidence:
file:human/EIF3J/EIF3J-uniprot.txt
SUBCELLULAR LOCATION: Cytoplasm
|
|
GO:0005852
eukaryotic translation initiation factor 3 complex
|
IEA
GO_REF:0000120 |
ACCEPT |
Summary: Electronic transfer of eIF-3 complex membership, redundant with the IBA/IDA/IPI evidence.
Reason: Correct core cellular component, corroborated by stronger evidence.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005852 eukaryotic translation initiation factor 3 complex cellular_component ECO:0000501 IEA
|
|
GO:0016282
eukaryotic 43S preinitiation complex
|
IEA
GO_REF:0000104 |
KEEP AS NON CORE |
Summary: Via eIF-3, EIF3J is part of the transient 43S pre-initiation complex on the 40S subunit. A genuine but transient assembly intermediate.
Reason: The 43S PIC is a transient initiation intermediate that contains eIF-3; a real but non-core localization relative to the stable eIF-3 complex membership.
Supporting Evidence:
file:human/EIF3J/EIF3J-uniprot.txt
to form the 43S pre-initiation complex (43S PIC)
|
|
GO:0033290
eukaryotic 48S preinitiation complex
|
IEA
GO_REF:0000104 |
KEEP AS NON CORE |
Summary: Via eIF-3, EIF3J is part of the transient 48S pre-initiation complex (after mRNA recruitment and start-codon scanning). A transient assembly intermediate.
Reason: The 48S PIC is a transient initiation intermediate; real but non-core relative to stable eIF-3 complex membership.
Supporting Evidence:
file:human/EIF3J/EIF3J-uniprot.txt
stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for
|
|
GO:0005515
protein binding
|
IPI
PMID:14688252 The j-subunit of human translation initiation factor eIF3 is... |
KEEP AS NON CORE |
Summary: Interaction with EIF3B (P55884), the subunit through which EIF3J docks onto eIF-3; this study shows EIF3J is required for stable binding of eIF-3 to 40S subunits. Deep-research synthesis further localizes EIF3J binding to the 40S near the mRNA entry channel and A-site, where it binds anti-cooperatively with mRNA and acts as a gatekeeper for mRNA accommodation. Bare protein binding is uninformative, but the interaction is biologically central.
Reason: Records the functionally important EIF3J-EIF3B interaction, but the term is uninformative; the informative function (eIF-3 membership and 40S/mRNA-entry-channel binding) is captured by complex/initiation annotations and core_functions.
Supporting Evidence:
PMID:14688252
j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro
file:human/EIF3J/EIF3J-deep-research-falcon.md
Binds the 40S small subunit near the mRNA entry channel and A-site; competes anti-cooperatively with accommodated mRNA
|
|
GO:0005515
protein binding
|
IPI
PMID:16932749 p97/DAP5 is a ribosome-associated factor that facilitates pr... |
KEEP AS NON CORE |
Summary: Interaction reported in a study of the ribosome-associated factor p97/DAP5. Bare protein binding is uninformative.
Reason: Records a real interaction but uninformative term; not core to EIF3J's function.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:16932749 UniProtKB:Q04637
|
|
GO:0005515
protein binding
|
IPI
PMID:18628297 Human DDX3 functions in translation and interacts with the t... |
KEEP AS NON CORE |
Summary: Interaction with EIF4G1 (Q04637) in a study of DDX3 in translation and eIF3. Bare protein binding is uninformative.
Reason: Records a real translation-related interaction but uninformative term; not core.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:18628297 UniProtKB:P55884
|
|
GO:0005515
protein binding
|
IPI
PMID:22113938 A bead-based approach for large-scale identification of in v... |
KEEP AS NON CORE |
Summary: Interaction with the casein kinase 2 catalytic subunit CSNK2A1 (P68400) from a kinase-substrate screen; consistent with EIF3J being phosphorylated. Bare protein binding is uninformative.
Reason: Records a kinase-substrate interaction (EIF3J is phosphorylated) but uninformative term; not a core function.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:22113938 UniProtKB:P68400
|
|
GO:0005515
protein binding
|
IPI
PMID:25852190 Integrative analysis of kinase networks in TRAIL-induced apo... |
KEEP AS NON CORE |
Summary: Interaction with CSNK2A1 (P68400) from a kinase-network apoptosis study. Bare protein binding is uninformative.
Reason: Records a kinase interaction but uninformative term; not core.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:25852190 UniProtKB:P68400
|
|
GO:0005515
protein binding
|
IPI
PMID:32296183 A reference map of the human binary protein interactome. |
KEEP AS NON CORE |
Summary: HuRI binary interactome capturing an EIF3J-ABCE1 (P61221) interaction. ABCE1 is the ribosome-recycling ATPase; deep-research synthesis indicates EIF3J specifically (not merely the eIF-3 holo-complex) functionally couples to ABCE1/RLI1 and enhances post-termination ribosome recycling, so this interaction is biologically meaningful even though the bare term is uninformative.
Reason: Records a recycling-relevant interaction (ABCE1) with EIF3J-subunit-specific functional support in the recycling literature, but the term itself is uninformative; the recycling role is captured at the complex level.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:32296183 UniProtKB:P61221
file:human/EIF3J/EIF3J-deep-research-falcon.md
physically/ functionally associates with ABCE1/RLI1, the ATPase required for post-termination ribosome recycling
|
|
GO:0005515
protein binding
|
IPI
PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... |
KEEP AS NON CORE |
Summary: Interaction with CSNK2A1 (P68400) from a kinase-interaction-network study. Bare protein binding is uninformative.
Reason: Records a kinase interaction but uninformative term; not core.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:32707033 UniProtKB:P68400
|
|
GO:0005515
protein binding
|
IPI
PMID:32911434 A functionally defined high-density NRF2 interactome reveals... |
KEEP AS NON CORE |
Summary: Interaction with NFE2L2/NRF2 (Q16236) from an NRF2-interactome screen. Bare protein binding is uninformative and likely peripheral.
Reason: Records a real interaction but uninformative term and peripheral to translation initiation; not core.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:32911434 UniProtKB:Q16236
|
|
GO:0005515
protein binding
|
IPI
PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... |
KEEP AS NON CORE |
Summary: BioPlex affinity-purification capturing an EIF3J-CSNK2A1 (P68400) interaction. Bare protein binding is uninformative.
Reason: Records a kinase interaction but uninformative term; not core.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:33961781 UniProtKB:P68400
|
|
GO:0005515
protein binding
|
IPI
PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... |
KEEP AS NON CORE |
Summary: OpenCell endogenous-tagging interactome capturing EIF3J interactions with EIF3B (P55884) and ABCE1 (P61221), consistent with eIF-3 docking and recycling roles. Bare protein binding is uninformative.
Reason: Records biologically consistent interactions (EIF3B, ABCE1) but uninformative term; captured by complex/initiation annotations.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:35271311 UniProtKB:P55884
|
|
GO:0042802
identical protein binding
|
IPI
PMID:32296183 A reference map of the human binary protein interactome. |
KEEP AS NON CORE |
Summary: EIF3J self-interaction reported in the HuRI binary interactome (consistent with the EIF3J-EIF3J IntAct entry). A real homotypic interaction but not a core function.
Reason: Records a self-interaction; not part of the core translation-initiation function.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0042802 identical protein binding molecular_function ECO:0000353 IPI PMID:32296183 UniProtKB:O75822
|
|
GO:0001732
formation of cytoplasmic translation initiation complex
|
NAS
PMID:16920360 eIF3: a versatile scaffold for translation initiation comple... |
ACCEPT |
Summary: Author statement (eIF3 review) that eIF-3 serves as a scaffold for assembly of translation initiation complexes; EIF3J participates as a subunit.
Reason: Consistent with eIF-3's documented role in initiation-complex assembly; core process for EIF3J as a subunit.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0001732 formation of cytoplasmic translation initiation complex biological_process ECO:0005547 NAS PMID:16920360
|
|
GO:0005852
eukaryotic translation initiation factor 3 complex
|
IPI
PMID:17322308 Structural characterization of the human eukaryotic initiati... |
ACCEPT |
Summary: Direct (ComplexPortal/MS) evidence placing EIF3J in the eIF-3 complex. Core cellular component.
Reason: Mass-spectrometry characterization of human eIF-3 confirms EIF3J as a component.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005852 eukaryotic translation initiation factor 3 complex cellular_component ECO:0000353 IPI PMID:17322308
|
|
GO:0005829
cytosol
|
TAS
Reactome:R-HSA-156808 |
ACCEPT |
Summary: Reactome curated cytosolic localization for translation-initiation reactions.
Reason: Correct cytosolic localization, consistent with the cytoplasmic site of action.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-156808
|
|
GO:0005829
cytosol
|
TAS
Reactome:R-HSA-156823 |
ACCEPT |
Summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
Reason: Correct cytosolic localization.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-156823
|
|
GO:0005829
cytosol
|
TAS
Reactome:R-HSA-157849 |
ACCEPT |
Summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
Reason: Correct cytosolic localization.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-157849
|
|
GO:0005829
cytosol
|
TAS
Reactome:R-HSA-72619 |
ACCEPT |
Summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
Reason: Correct cytosolic localization.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-72619
|
|
GO:0005829
cytosol
|
TAS
Reactome:R-HSA-72621 |
ACCEPT |
Summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
Reason: Correct cytosolic localization.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-72621
|
|
GO:0005829
cytosol
|
TAS
Reactome:R-HSA-72676 |
ACCEPT |
Summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
Reason: Correct cytosolic localization.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-72676
|
|
GO:0005829
cytosol
|
TAS
Reactome:R-HSA-72691 |
ACCEPT |
Summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
Reason: Correct cytosolic localization.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-72691
|
|
GO:0005829
cytosol
|
TAS
Reactome:R-HSA-72697 |
ACCEPT |
Summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
Reason: Correct cytosolic localization.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-72697
|
|
GO:0003743
translation initiation factor activity
|
IC
PMID:17322308 Structural characterization of the human eukaryotic initiati... |
ACCEPT |
Summary: Curator-inferred (from eIF-3 complex membership) that EIF3J contributes to translation initiation factor activity. The contributes_to qualifier correctly reflects its accessory role within the complex.
Reason: This is the core molecular function annotation for EIF3J, appropriately qualified as contributes_to for a non-catalytic accessory subunit.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0003743 translation initiation factor activity molecular_function ECO:0000305 IC PMID:17322308
|
|
GO:0003743
translation initiation factor activity
|
IC
PMID:18599441 Mass spectrometry reveals modularity and a complete subunit ... |
ACCEPT |
Summary: Curator-inferred translation initiation factor activity from eIF-3 complex membership (subunit interaction map study). Redundant with the other IC annotation.
Reason: Core molecular function, appropriately qualified contributes_to.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0003743 translation initiation factor activity molecular_function ECO:0000305 IC PMID:18599441
|
|
GO:0005852
eukaryotic translation initiation factor 3 complex
|
IDA
PMID:17322308 Structural characterization of the human eukaryotic initiati... |
ACCEPT |
Summary: Direct MS-based evidence for EIF3J as an eIF-3 component. Core cellular component.
Reason: Directly demonstrated eIF-3 complex membership.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005852 eukaryotic translation initiation factor 3 complex cellular_component ECO:0000314 IDA PMID:17322308
|
|
GO:0005852
eukaryotic translation initiation factor 3 complex
|
IDA
PMID:18599441 Mass spectrometry reveals modularity and a complete subunit ... |
ACCEPT |
Summary: Direct MS-based evidence for EIF3J as an eIF-3 component (subunit interaction map). Core cellular component.
Reason: Directly demonstrated eIF-3 complex membership.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0005852 eukaryotic translation initiation factor 3 complex cellular_component ECO:0000314 IDA PMID:18599441
|
|
GO:0006413
translational initiation
|
IC
PMID:17322308 Structural characterization of the human eukaryotic initiati... |
ACCEPT |
Summary: Curator-inferred involvement in translational initiation from eIF-3 membership. Core biological process.
Reason: EIF3J participates in translation initiation as an eIF-3 subunit.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0006413 translational initiation biological_process ECO:0000305 IC PMID:17322308
|
|
GO:0006413
translational initiation
|
IC
PMID:18599441 Mass spectrometry reveals modularity and a complete subunit ... |
ACCEPT |
Summary: Curator-inferred involvement in translational initiation from eIF-3 membership. Redundant with the other IC annotation.
Reason: Core biological process for EIF3J as an eIF-3 subunit.
Supporting Evidence:
file:human/EIF3J/EIF3J-goa.tsv
GO:0006413 translational initiation biological_process ECO:0000305 IC PMID:18599441
|
Q: Does human EIF3J have a distinct, separable role in 40S ribosome recycling/availability (post-termination) versus initiation, as suggested by yeast Hcr1?
Q: How does the sub-stoichiometric/labile association of EIF3J with eIF-3 regulate switching between mRNA-entry-channel occupancy and mRNA loading?
Q: What is the functional consequence of serum-stimulated phosphorylation of EIF3J for its association with eIF-3 and selective mRNA translation?
Experiment: Selective EIF3J depletion/rescue with ribosome profiling and 40S/80S subunit-availability assays to dissect its contribution to initiation versus post-termination recycling.
Experiment: Cryo-EM of 40S-eIF-3 complexes with and without EIF3J to define its occupancy of the mRNA entry channel and effect on mRNA accommodation.
Experiment: Phosphomutant (phospho-null/phospho-mimetic) EIF3J variants to test how serum-stimulated phosphorylation modulates eIF-3 binding and translational output.
The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
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Extensive review of recent and foundational literature confirms the correct targeting of the human gene EIF3J. EIF3J encodes the eukaryotic translation initiation factor 3 subunit J (eIF3j), as annotated in UniProt O75822, and matches the provided protein/domain description. All reviewed sources describe its role within the human eIF3 system; ambiguous alternative gene/protein symbols were not detected in retrieved authoritative literature (wagner2016humaneif3band pages 1-2, valasek2017embracedbyeif3 pages 1-2).
eIF3j is a non-enzymatic, ribosome-associated translation factor classified as a peripheral, substoichiometric member of the eIF3 multiprotein complex. Unlike core eIF3 subunitsโwhich form the PCI/MPN octamer or "yeast-like core"โeIF3j associates transiently with the eIF3 complex and the small (40S) ribosomal subunit (wagner2016humaneif3band pages 1-2). It is best described as an eIF3-associated factor rather than a bona fide core subunit (valasek2017embracedbyeif3 pages 1-2, valasek2017embracedbyeif3 pages 3-4, sokabe2017ahelicaseindependentactivity pages 1-1).
Domain Structure: Human eIF3j comprises an N-terminal region mediating interaction with the RRM domain of eIF3b (the core scaffolding subunit), and a C-terminal region required for specific regulatory activity (notably, inhibition of circular RNA translation) (valasek2017embracedbyeif3 pages 3-4, song2022eif3jinhibitstranslation pages 1-2).
Primary Function: eIF3j regulates translation initiation, ribosome recycling, and selected non-canonical translation processes, without direct enzymatic activity or substrate specificity.
EIF3J is predominantly cytoplasmic, consistent with its roles in mRNA translation (initiation and recycling) on cytoplasmic ribosomes. There is no significant evidence for nuclear or mitochondrial localization in humans (duan2023eif3mrnaselectivity pages 1-2, sokabe2017ahelicaseindependentactivity pages 1-1).
The following table comprehensively summarizes specific findings, pathways, features, and structural insights, prioritized by publication year and experimental authority:
| Aspect | Key finding for human EIF3J/eIF3j | Evidence/details | Recent relevance (2022-2024) | Source / year / URL |
|---|---|---|---|---|
| Gene/protein identity | EIF3J encodes human eukaryotic translation initiation factor 3 subunit J (eIF3j), an eIF3-associated translation factor rather than a stable core eIF3 subunit | Reviews and assembly studies distinguish mammalian eIF3 as a 12-subunit complex and describe eIF3j as loosely associated/substoichiometric, often treated as an eIF3-associated factor rather than a bona fide core subunit (wagner2016humaneif3band pages 1-2, valasek2017embracedbyeif3 pages 1-2) | Still the prevailing model used in current eIF3 literature and structural studies | Wagner et al., 2016, Nucleic Acids Research, https://doi.org/10.1093/nar/gkw972 ; Valรกลกek et al., 2017, Nucleic Acids Research, https://doi.org/10.1093/nar/gkx805 |
| Primary molecular function | Non-catalytic ribosome-associated translation factor that modulates mRNA recruitment, translation initiation complex dynamics, and ribosome recycling | No enzymatic activity is described; instead, eIF3j acts through protein- and ribosome-binding interactions that alter 40S/mRNA/factor configurations (sokabe2017ahelicaseindependentactivity pages 1-1, young2022rebirthofthe pages 3-4) | Current understanding emphasizes regulatory rather than catalytic function | Sokabe & Fraser, 2017, PNAS, https://doi.org/10.1073/pnas.1620426114 ; Young & Guydosh, 2022, BioEssays, https://doi.org/10.1002/bies.202100269 |
| Subunit association within eIF3 system | eIF3j is substoichiometric and transiently associated with holo-eIF3 | eIF3j binds the eIF3b RRM and is not required for the stable PCI/MPN octamer or yeast-like core assembly; this supports its classification as peripheral/associated (wagner2016humaneif3band pages 1-2, valasek2017embracedbyeif3 pages 3-4) | Important for interpreting modern cryo-EM structures, which typically focus on core eIF3 architecture | Wagner et al., 2016, https://doi.org/10.1093/nar/gkw972 ; Valรกลกek et al., 2017, https://doi.org/10.1093/nar/gkx805 |
| Domain architecture | Contains an eIF3j-specific domain and functionally important N- and C-terminal regions; the N-terminus mediates factor interactions and the C-terminus contributes to RNA-regulatory functions | Structural review cites NMR information for the interaction of human eIF3j residues 35-69 with human eIF3b RRM; 2022 circRNA work found the C-terminus essential for inhibitory activity on circRNA translation (valasek2017embracedbyeif3 pages 3-4, song2022eif3jinhibitstranslation pages 1-2) | The C-terminal regulatory role gained new attention in 2022 | Valรกลกek et al., 2017, https://doi.org/10.1093/nar/gkx805 ; Song et al., 2022, Nucleic Acids Research, https://doi.org/10.1093/nar/gkac980 |
| Direct interaction partner(s) | Interacts with eIF3b and functionally couples to eIF3 and ABCE1/RLI1 | Human eIF3j N-terminal peptide contacts eIF3b RRM; ribosome recycling literature and review evidence indicate physical/functional interplay with ABCE1 and eIF3 on post-termination ribosomes (valasek2017embracedbyeif3 pages 3-4, young2022rebirthofthe pages 3-4) | These interactions underpin newer models of initiation-recycling continuity | Valรกลกek et al., 2017, https://doi.org/10.1093/nar/gkx805 ; Young & Guydosh, 2022, https://doi.org/10.1002/bies.202100269 |
| Ribosome binding site | Binds the 40S small subunit near the mRNA entry channel and A-site; competes anti-cooperatively with accommodated mRNA | Reconstituted human systems show high-affinity binding of eIF3j to the 43S PIC/40S and a marked reduction in affinity after mRNA recruitment; this is interpreted as reporting mRNA accommodation into the decoding site/entry channel (sokabe2017ahelicaseindependentactivity pages 1-1) | Remains a key mechanistic framework for understanding eIF3j action in human initiation | Sokabe & Fraser, 2017, https://doi.org/10.1073/pnas.1620426114 |
| Role in cap-dependent initiation | Regulates an early step of mRNA recruitment to the 43S PIC and is displaced as mRNA becomes fully accommodated | Human reconstitution experiments indicate that eIF4F/eIF4A/eIF4B-dependent mRNA recruitment lowers eIF3j affinity for the 43S PIC; short RNAs that do not extend into the entry channel fail to displace eIF3j (sokabe2017ahelicaseindependentactivity pages 1-1) | Supports the current view that eIF3j marks and/or gates mRNA entry into the 40S channel | Sokabe & Fraser, 2017, https://doi.org/10.1073/pnas.1620426114 |
| Dependence on eIF4A/ATP during initiation | Full reduction in eIF3j affinity during mRNA recruitment requires ATP-dependent but unwinding-independent eIF4A activity | This suggests eIF3j senses a regulated conformational transition of the human 43S PIC rather than only RNA helicase action (sokabe2017ahelicaseindependentactivity pages 1-1) | Conceptually reinforced by 2024 human 48S structures showing factor-rich organization around entry and exit channels | Sokabe & Fraser, 2017, https://doi.org/10.1073/pnas.1620426114 ; Querido et al., 2024, Nature Structural & Molecular Biology, https://doi.org/10.1038/s41594-023-01196-0 |
| Role in ribosome recycling | Promotes efficient post-termination recycling, especially by enhancing ABCE1/RLI1-mediated subunit splitting and/or subsequent 40S recycling transitions | Reviews summarize yeast/human evidence that eIF3j improves ABCE1/RLI1 recycling efficiency, binds when one ABCE1 nucleotide-binding site is partially open, and may help control post-splitting 40S states (young2022rebirthofthe pages 3-4, young2022rebirthofthe pages 4-6) | Ribosome recycling remains one of the most important non-initiation functions ascribed to eIF3j in recent synthesis articles | Young & Guydosh, 2022, https://doi.org/10.1002/bies.202100269 |
| Site of action in recycling | Cytoplasmic post-termination 80S/40S ribosome complexes | Reconstituted and structural/review evidence places eIF3j on ribosomal complexes after termination, participating with ABCE1 and canonical initiation/recycling factors on the small subunit (young2022rebirthofthe pages 3-4, young2022rebirthofthe pages 4-6) | Helps explain functional continuity between recycling and re-initiation-capable 40S states | Young & Guydosh, 2022, https://doi.org/10.1002/bies.202100269 |
| Role in translation termination fidelity / readthrough | eIF3j has been linked to stop-codon decoding outcomes via the broader eIF3 network; loss of eIF3j/HCR1 increased readthrough in yeast models | Review of foundational work notes that eIF3 and eIF3j associate with terminating ribosomes and influence stop-codon readthrough/termination dynamics, though much mechanistic evidence comes from yeast systems (valasek2017embracedbyeif3 pages 10-11, valasek2017embracedbyeif3 pages 11-12) | Useful as evolutionary/mechanistic context, but less directly established for human EIF3J than initiation/recycling roles | Valรกลกek et al., 2017, https://doi.org/10.1093/nar/gkx805 |
| Role in circular RNA translation | eIF3j can act as a negative regulator of a subset of circRNA translation by promoting eIF3 dissociation from circRNA templates | In a 2022 systematic screen, eIF3j was the strongest inhibitor among tested eIFs; binding of eIF3j to circSfl promoted dissociation of eIF3, and the eIF3j C-terminus plus a circRNA UTR regulon were required (song2022eif3jinhibitstranslation pages 1-2, song2022eif3jinhibitstranslation pages 4-5) | One of the clearest newly described regulatory activities relevant to 2022-2024 literature | Song et al., 2022, https://doi.org/10.1093/nar/gkac980 ; Hwang & Kim, 2024 review, https://doi.org/10.1038/s12276-024-01220-3 |
| Subcellular localization | Predominantly cytoplasmic site of action, consistent with roles in mRNA translation, ribosome binding, and ribosome recycling | eIF3 subunits in mammalian cells show predominantly cytoplasmic localization, and eIF3j functions are consistently described on cytoplasmic 40S/43S/80S complexes rather than nuclear pathways (duan2023eif3mrnaselectivity pages 1-2, sokabe2017ahelicaseindependentactivity pages 1-1) | No strong evidence in the retrieved set for a primary non-cytoplasmic human EIF3J role | Duan et al., 2023, The EMBO Journal, https://doi.org/10.15252/embj.2022112362 ; Sokabe & Fraser, 2017, https://doi.org/10.1073/pnas.1620426114 |
| Structural context in modern human initiation complexes | Modern 48S cryo-EM maps emphasize eIF3 architecture at both mRNA entry and exit sides of the 40S, providing context for eIF3jโs gatekeeping position even when eIF3j itself is not the focus of the map | Human 48S structure shows eIF3 octamer/core plus peripheral subunits surrounding the mRNA path and a second eIF4A at the entry site, supporting a framework in which entry-channel factors such as eIF3j regulate mRNA accommodation (querido2024thestructureof pages 1-2) | Important 2024 context for integrating older eIF3j biochemical data with current structural models | Querido et al., 2024, https://doi.org/10.1038/s41594-023-01196-0 |
| Viral/pathogen interface relevance | eIF3j-binding surfaces on the 40S entry region are functionally important enough to be targeted or competed by pathogens/viral factors | SARS-CoV-2 Nsp1 was proposed to compete with eIF3j for 40S binding and weaken eIF3 association; this supports the biological importance of eIF3jโs 40S interface (yuan2020nonstructuralprotein1 pages 1-7) | Highlights translational control interfaces relevant to infection biology | Yuan et al., 2020, Molecular Cell, https://doi.org/10.1016/j.molcel.2020.10.034 |
| Human tissue expression pattern | EIF3J transcript abundance varies across human tissues rather than being uniformly invariant | Transcriptomic survey identified relative tissue differences, including lower expression in ovary and higher expression in brain/liver/testis-related comparisons (young2022rebirthofthe pages 1-3) | Provides recent systems-level context, although not direct functional proof | Anisimova et al., 2023, International Journal of Molecular Sciences, https://doi.org/10.3390/ijms24098361 |
| Current consensus summary | Human EIF3J/eIF3j is best annotated as a peripheral, non-enzymatic 40S/eIF3-associated regulator that helps coordinate mRNA entry, initiation-complex remodeling, and ribosome recycling, with emerging transcript-selective inhibitory functions on circRNA translation | This synthesis is supported by assembly studies, structural reviews, biochemical reconstitution, recycling reviews, and newer circRNA-focused work (wagner2016humaneif3band pages 1-2, valasek2017embracedbyeif3 pages 1-2, sokabe2017ahelicaseindependentactivity pages 1-1, young2022rebirthofthe pages 4-6, song2022eif3jinhibitstranslation pages 1-2) | Most robust experimentally supported functions remain in cytoplasmic translation control rather than signaling or catalysis | Wagner et al., 2016, https://doi.org/10.1093/nar/gkw972 ; Valรกลกek et al., 2017, https://doi.org/10.1093/nar/gkx805 ; Sokabe & Fraser, 2017, https://doi.org/10.1073/pnas.1620426114 ; Young & Guydosh, 2022, https://doi.org/10.1002/bies.202100269 ; Song et al., 2022, https://doi.org/10.1093/nar/gkac980 |
Table: This table summarizes the main experimentally supported functions and structural features of human EIF3J/eIF3j, emphasizing its 40S/eIF3-associated roles in translation initiation and ribosome recycling. It also highlights newer findings from 2022-2024, including selective inhibition of circRNA translation and modern structural context.
Leading-edge research now highlights eIF3j as a selective, modular regulator within cytoplasmic translation, best conceptualized as a non-catalytic RNAโprotein remodeling factor. Its physiological impacts are most apparent at the level of core protein synthesis, ribosome recycling efficiency, and context-dependent translation inhibition (such as for circular RNA translation). Emerging evidence supports a model where eIF3j integrates mRNA fate at the interface of ribosome structure, eIF3 complex status, and cellular stress/adaptation signals.
EIF3J (eIF3j) serves as a regulatory hub for cytoplasmic ribosomes, linking translation efficiency and selectivity at both initiation and recycling stages, with recently discovered control over circular RNA translation. Continued structural, genetic, and single-molecule studies will likely further clarify its roles in disease, adaptation, and metabolic stress responses.
References
(wagner2016humaneif3band pages 1-2): Susan Wagner, Anna Herrmannovรก, Darina ล ikrovรก, and Leoลก Shivaya Valรกลกek. Human eif3b and eif3a serve as the nucleation core for the assembly of eif3 into two interconnected modules: the yeast-like core and the octamer. Nucleic Acids Research, 44:10772-10788, Oct 2016. URL: https://doi.org/10.1093/nar/gkw972, doi:10.1093/nar/gkw972. This article has 107 citations and is from a highest quality peer-reviewed journal.
(valasek2017embracedbyeif3 pages 1-2): Leoลก Shivaya Valรกลกek, Jakub Zeman, Susan Wagner, Petra Beznoskovรก, Zuzana Pavlรญkovรก, Mahabub Pasha Mohammad, Vladislava Hronovรก, Anna Herrmannovรก, Yaser Hashem, and Stanislava Guniลกovรก. Embraced by eif3: structural and functional insights into the roles of eif3 across the translation cycle. Nucleic Acids Research, 45:10948-10968, Sep 2017. URL: https://doi.org/10.1093/nar/gkx805, doi:10.1093/nar/gkx805. This article has 181 citations and is from a highest quality peer-reviewed journal.
(valasek2017embracedbyeif3 pages 3-4): Leoลก Shivaya Valรกลกek, Jakub Zeman, Susan Wagner, Petra Beznoskovรก, Zuzana Pavlรญkovรก, Mahabub Pasha Mohammad, Vladislava Hronovรก, Anna Herrmannovรก, Yaser Hashem, and Stanislava Guniลกovรก. Embraced by eif3: structural and functional insights into the roles of eif3 across the translation cycle. Nucleic Acids Research, 45:10948-10968, Sep 2017. URL: https://doi.org/10.1093/nar/gkx805, doi:10.1093/nar/gkx805. This article has 181 citations and is from a highest quality peer-reviewed journal.
(sokabe2017ahelicaseindependentactivity pages 1-1): Masaaki Sokabe and Christopher S. Fraser. A helicase-independent activity of eif4a in promoting mrna recruitment to the human ribosome. Proceedings of the National Academy of Sciences, 114:6304-6309, May 2017. URL: https://doi.org/10.1073/pnas.1620426114, doi:10.1073/pnas.1620426114. This article has 104 citations and is from a highest quality peer-reviewed journal.
(song2022eif3jinhibitstranslation pages 1-2): Zhenxing Song, Jiamei Lin, Rui Su, Yu Ji, Ruirui Jia, Shi Li, Ge Shan, and Chuan Huang. Eif3j inhibits translation of a subset of circular rnas in eukaryotic cells. Nucleic Acids Research, 50:11529-11549, Nov 2022. URL: https://doi.org/10.1093/nar/gkac980, doi:10.1093/nar/gkac980. This article has 36 citations and is from a highest quality peer-reviewed journal.
(young2022rebirthofthe pages 3-4): David J. Young and Nicholas R. Guydosh. Rebirth of the translational machinery: the importance of recycling ribosomes. BioEssays, Feb 2022. URL: https://doi.org/10.1002/bies.202100269, doi:10.1002/bies.202100269. This article has 32 citations and is from a peer-reviewed journal.
(young2022rebirthofthe pages 4-6): David J. Young and Nicholas R. Guydosh. Rebirth of the translational machinery: the importance of recycling ribosomes. BioEssays, Feb 2022. URL: https://doi.org/10.1002/bies.202100269, doi:10.1002/bies.202100269. This article has 32 citations and is from a peer-reviewed journal.
(song2022eif3jinhibitstranslation pages 4-5): Zhenxing Song, Jiamei Lin, Rui Su, Yu Ji, Ruirui Jia, Shi Li, Ge Shan, and Chuan Huang. Eif3j inhibits translation of a subset of circular rnas in eukaryotic cells. Nucleic Acids Research, 50:11529-11549, Nov 2022. URL: https://doi.org/10.1093/nar/gkac980, doi:10.1093/nar/gkac980. This article has 36 citations and is from a highest quality peer-reviewed journal.
(hwang2024molecularmechanismsof pages 1-2): Hyun Jung Hwang and Yoon Ki Kim. Molecular mechanisms of circular rna translation. Experimental & Molecular Medicine, 56:1272-1280, Jun 2024. URL: https://doi.org/10.1038/s12276-024-01220-3, doi:10.1038/s12276-024-01220-3. This article has 153 citations and is from a peer-reviewed journal.
(duan2023eif3mrnaselectivity pages 1-2): Haoran Duan, Siqiong Zhang, Yoram Zarai, Rupert รllinger, Yanmeng Wu, Li Sun, Cheng Hu, Yaohui He, Guiyou Tian, Roland Rad, Xiangquan Kong, Yabin Cheng, Tamir Tuller, and Dieter A Wolf. Eif3 mrna selectivity profiling reveals eif3k as a cancerโrelevant regulator of ribosome content. The EMBO Journal, May 2023. URL: https://doi.org/10.15252/embj.2022112362, doi:10.15252/embj.2022112362. This article has 28 citations.
(valasek2017embracedbyeif3 pages 10-11): Leoลก Shivaya Valรกลกek, Jakub Zeman, Susan Wagner, Petra Beznoskovรก, Zuzana Pavlรญkovรก, Mahabub Pasha Mohammad, Vladislava Hronovรก, Anna Herrmannovรก, Yaser Hashem, and Stanislava Guniลกovรก. Embraced by eif3: structural and functional insights into the roles of eif3 across the translation cycle. Nucleic Acids Research, 45:10948-10968, Sep 2017. URL: https://doi.org/10.1093/nar/gkx805, doi:10.1093/nar/gkx805. This article has 181 citations and is from a highest quality peer-reviewed journal.
(valasek2017embracedbyeif3 pages 11-12): Leoลก Shivaya Valรกลกek, Jakub Zeman, Susan Wagner, Petra Beznoskovรก, Zuzana Pavlรญkovรก, Mahabub Pasha Mohammad, Vladislava Hronovรก, Anna Herrmannovรก, Yaser Hashem, and Stanislava Guniลกovรก. Embraced by eif3: structural and functional insights into the roles of eif3 across the translation cycle. Nucleic Acids Research, 45:10948-10968, Sep 2017. URL: https://doi.org/10.1093/nar/gkx805, doi:10.1093/nar/gkx805. This article has 181 citations and is from a highest quality peer-reviewed journal.
(she2023translationalfidelityscreens pages 1-2): Richard She, Jingchuan Luo, and Jonathan S Weissman. Translational fidelity screens in mammalian cells reveal eif3 and eif4g2 as regulators of start codon selectivity. Nucleic Acids Research, 51:6355-6369, May 2023. URL: https://doi.org/10.1093/nar/gkad329, doi:10.1093/nar/gkad329. This article has 26 citations and is from a highest quality peer-reviewed journal.
(querido2024thestructureof pages 1-2): Jailson Brito Querido, Masaaki Sokabe, Irene Dรญaz-Lรณpez, Yuliya Gordiyenko, Christopher S. Fraser, and V. Ramakrishnan. The structure of a human translation initiation complex reveals two independent roles for the helicase eif4a. Nature Structural & Molecular Biology, 31:455-464, Dec 2024. URL: https://doi.org/10.1038/s41594-023-01196-0, doi:10.1038/s41594-023-01196-0. This article has 108 citations and is from a highest quality peer-reviewed journal.
(young2022rebirthofthe pages 1-3): David J. Young and Nicholas R. Guydosh. Rebirth of the translational machinery: the importance of recycling ribosomes. BioEssays, Feb 2022. URL: https://doi.org/10.1002/bies.202100269, doi:10.1002/bies.202100269. This article has 32 citations and is from a peer-reviewed journal.
(yuan2020nonstructuralprotein1 pages 1-7): Shuai Yuan, Lei Peng, Jonathan J. Park, Yingxia Hu, Swapnil C. Devarkar, Matthew B. Dong, Shenping Wu, Sidi Chen, Ivan Lomakin, and Yong Xiong. Nonstructural protein 1 of sars-cov-2 is a potent pathogenicity factor redirecting host protein synthesis machinery toward viral rna. Molecular Cell, 80:1055-1066.e6, Aug 2020. URL: https://doi.org/10.1016/j.molcel.2020.10.034, doi:10.1016/j.molcel.2020.10.034. This article has 210 citations and is from a highest quality peer-reviewed journal.
UniProt O75822 (EIF3J_HUMAN), eukaryotic translation initiation factor 3 subunit J. Cytoplasm.
EIF3J is a subunit of the 13-subunit eukaryotic translation initiation factor 3 (eIF-3) complex.
- UniProt FUNCTION: "Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis [PMID:25849773, PMID:27462815]. 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 pre-initiation complex (43S PIC)."
- The eIF-3 complex "is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation." (UniProt) โ this is the ribosome-recycling / 40S-availability role.
*-deep-research*.md file found in this gene directory.new_to_goa. EIF3J's recycling role is real but is a recycling/40S-availability function, not protein quality control / misfolded-chain surveillance; GO:0006515 (protein QC for misfolded/incompletely synthesized proteins) mischaracterizes it and over-reaches. A ribosome-recycling/disassembly process term (e.g. GO:0032790 ribosome disassembly) would be more defensible than GO:0006515 if any RQC-row term is projected.Translation|Cytosolic translation|Translation initiation|eIF3 complex and Translation|Cytosolic translation|Ribosome-associated QC|other RQC processes ; PN-node mapping: initiation type โ GO:0005852 eIF3 complex (mapped); initiation group โ GO:0006413 translational initiation (mapped); RQC group โ GO:0006515 protein QC (mapped, new_to_goa); RQC type no_mapping.new_to_goa. EIF3J's recycling role is real but is a recycling/40S-availability function, not protein quality control / misfolded-chain surveillance; GO:0006515 (protein QC for misfolded/incompletely synthesized proteins) mischaracterizes it and over-reaches. A ribosome-recycling/disassembly process term (e.g. GO:0032790 ribosome disassembly) would be more defensible than GO:0006515 if any RQC-row term is projected.Ribosome-associated QC group โ GO:0006515 is too broad/mischaracterizing for EIF3J (a recycling accessory, not a QC factor); recommend not projecting GO:0006515 here.This file is generated from the current PROTEOSTASIS phase-1 dossier and local gene-review artifacts. Edit the source review, PN mapping, or dossier rather than this generated note when correcting the underlying curation.
id: O75822
gene_symbol: EIF3J
product_type: PROTEIN
status: COMPLETE
taxon:
id: NCBITaxon:9606
label: Homo sapiens
description: EIF3J (eukaryotic translation initiation factor 3 subunit J) is a cytoplasmic accessory subunit of the 13-subunit eIF-3 complex, the largest eukaryotic translation initiation factor. eIF-3 associates with the 40S ribosomal subunit and orchestrates several steps of cap-dependent translation initiation, promoting recruitment of eIF-1, eIF-1A, the eIF-2-GTP-Met-tRNAi ternary complex and eIF-5 to form the 43S pre-initiation complex, stimulating mRNA recruitment and scanning to the AUG start codon, and contributing to disassembly/recycling of post-termination ribosomal complexes while preventing premature 40S-60S subunit joining. EIF3J is a loosely associated, sub-stoichiometric ("labile") subunit that docks onto the complex through EIF3B; it positions near the 40S mRNA entry channel/decoding region and is required for stable binding of eIF-3 (and its subcomplexes) to the 40S subunit, thereby modulating mRNA loading and 40S availability. It is a non-catalytic accessory factor (its initiation-factor activity is contributed in the context of the assembled complex) and is phosphorylated in a serum-stimulation-dependent manner.
alternative_products:
- name: '1'
id: O75822-1
- name: '2'
id: O75822-2
sequence_note: VSP_054593
- name: '3'
id: O75822-3
sequence_note: VSP_054776
existing_annotations:
- term:
id: GO:0005852
label: eukaryotic translation initiation factor 3 complex
evidence_type: IBA
original_reference_id: GO_REF:0000033
qualifier: part_of
review:
summary: EIF3J is a (labile) subunit of the eIF-3 complex, well supported across eukaryotes and by direct human evidence. This is the core cellular-component annotation.
action: ACCEPT
reason: EIF3J is documented as a component of the 13-subunit eIF-3 complex, binding via EIF3B; the IBA is corroborated by IDA/IPI evidence.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-uniprot.txt
supporting_text: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex
- term:
id: GO:0001732
label: formation of cytoplasmic translation initiation complex
evidence_type: IEA
original_reference_id: GO_REF:0000104
qualifier: involved_in
review:
summary: As part of eIF-3, EIF3J participates in assembly of the 43S/48S translation initiation complexes on the 40S subunit. A genuine core process annotation.
action: ACCEPT
reason: eIF-3 facilitates recruitment of initiation factors and ternary complex to form the 43S PIC; EIF3J contributes to this assembly.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-uniprot.txt
supporting_text: facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to
- term:
id: GO:0002183
label: cytoplasmic translational initiation
evidence_type: IEA
original_reference_id: GO_REF:0000104
qualifier: involved_in
review:
summary: EIF3J participates in cytoplasmic translation initiation as an eIF-3 subunit. This is the core biological process.
action: ACCEPT
reason: eIF-3 is required for several steps in initiation of protein synthesis; this is EIF3J's central biological role.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-uniprot.txt
supporting_text: required for several steps in the initiation of protein synthesis
- term:
id: GO:0003743
label: translation initiation factor activity
evidence_type: IEA
original_reference_id: GO_REF:0000120
qualifier: enables
review:
summary: EIF3J contributes translation initiation factor activity as an accessory subunit of eIF-3. The activity is exerted in the context of the assembled complex rather than by EIF3J alone.
action: ACCEPT
reason: The core molecular function of EIF3J is translation initiation factor activity via the eIF-3 complex; note the curated experimental annotations use the contributes_to qualifier, reflecting its accessory role.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0003743 translation initiation factor activity molecular_function ECO:0000501 IEA
- term:
id: GO:0005737
label: cytoplasm
evidence_type: IEA
original_reference_id: GO_REF:0000120
qualifier: located_in
review:
summary: EIF3J is cytoplasmic, consistent with its role in cytoplasmic translation initiation.
action: ACCEPT
reason: Cytoplasm is the documented subcellular location and the site of translation initiation.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-uniprot.txt
supporting_text: 'SUBCELLULAR LOCATION: Cytoplasm'
- term:
id: GO:0005852
label: eukaryotic translation initiation factor 3 complex
evidence_type: IEA
original_reference_id: GO_REF:0000120
qualifier: part_of
review:
summary: Electronic transfer of eIF-3 complex membership, redundant with the IBA/IDA/IPI evidence.
action: ACCEPT
reason: Correct core cellular component, corroborated by stronger evidence.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005852 eukaryotic translation initiation factor 3 complex cellular_component ECO:0000501 IEA
- term:
id: GO:0016282
label: eukaryotic 43S preinitiation complex
evidence_type: IEA
original_reference_id: GO_REF:0000104
qualifier: part_of
review:
summary: Via eIF-3, EIF3J is part of the transient 43S pre-initiation complex on the 40S subunit. A genuine but transient assembly intermediate.
action: KEEP_AS_NON_CORE
reason: The 43S PIC is a transient initiation intermediate that contains eIF-3; a real but non-core localization relative to the stable eIF-3 complex membership.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-uniprot.txt
supporting_text: to form the 43S pre-initiation complex (43S PIC)
- term:
id: GO:0033290
label: eukaryotic 48S preinitiation complex
evidence_type: IEA
original_reference_id: GO_REF:0000104
qualifier: part_of
review:
summary: Via eIF-3, EIF3J is part of the transient 48S pre-initiation complex (after mRNA recruitment and start-codon scanning). A transient assembly intermediate.
action: KEEP_AS_NON_CORE
reason: The 48S PIC is a transient initiation intermediate; real but non-core relative to stable eIF-3 complex membership.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-uniprot.txt
supporting_text: stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:14688252
qualifier: enables
review:
summary: Interaction with EIF3B (P55884), the subunit through which EIF3J docks onto eIF-3; this study shows EIF3J is required for stable binding of eIF-3 to 40S subunits. Deep-research synthesis further localizes EIF3J binding to the 40S near the mRNA entry channel and A-site, where it binds anti-cooperatively with mRNA and acts as a gatekeeper for mRNA accommodation. Bare protein binding is uninformative, but the interaction is biologically central.
action: KEEP_AS_NON_CORE
reason: Records the functionally important EIF3J-EIF3B interaction, but the term is uninformative; the informative function (eIF-3 membership and 40S/mRNA-entry-channel binding) is captured by complex/initiation annotations and core_functions.
supported_by:
- reference_id: PMID:14688252
supporting_text: j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro
- reference_id: file:human/EIF3J/EIF3J-deep-research-falcon.md
supporting_text: Binds the 40S small subunit near the mRNA entry channel and A-site; competes anti-cooperatively with accommodated mRNA
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:16932749
qualifier: enables
review:
summary: Interaction reported in a study of the ribosome-associated factor p97/DAP5. Bare protein binding is uninformative.
action: KEEP_AS_NON_CORE
reason: Records a real interaction but uninformative term; not core to EIF3J's function.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:16932749 UniProtKB:Q04637
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:18628297
qualifier: enables
review:
summary: Interaction with EIF4G1 (Q04637) in a study of DDX3 in translation and eIF3. Bare protein binding is uninformative.
action: KEEP_AS_NON_CORE
reason: Records a real translation-related interaction but uninformative term; not core.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:18628297 UniProtKB:P55884
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:22113938
qualifier: enables
review:
summary: Interaction with the casein kinase 2 catalytic subunit CSNK2A1 (P68400) from a kinase-substrate screen; consistent with EIF3J being phosphorylated. Bare protein binding is uninformative.
action: KEEP_AS_NON_CORE
reason: Records a kinase-substrate interaction (EIF3J is phosphorylated) but uninformative term; not a core function.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:22113938 UniProtKB:P68400
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:25852190
qualifier: enables
review:
summary: Interaction with CSNK2A1 (P68400) from a kinase-network apoptosis study. Bare protein binding is uninformative.
action: KEEP_AS_NON_CORE
reason: Records a kinase interaction but uninformative term; not core.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:25852190 UniProtKB:P68400
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:32296183
qualifier: enables
review:
summary: HuRI binary interactome capturing an EIF3J-ABCE1 (P61221) interaction. ABCE1 is the ribosome-recycling ATPase; deep-research synthesis indicates EIF3J specifically (not merely the eIF-3 holo-complex) functionally couples to ABCE1/RLI1 and enhances post-termination ribosome recycling, so this interaction is biologically meaningful even though the bare term is uninformative.
action: KEEP_AS_NON_CORE
reason: Records a recycling-relevant interaction (ABCE1) with EIF3J-subunit-specific functional support in the recycling literature, but the term itself is uninformative; the recycling role is captured at the complex level.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:32296183 UniProtKB:P61221
- reference_id: file:human/EIF3J/EIF3J-deep-research-falcon.md
supporting_text: physically/ functionally associates with ABCE1/RLI1, the ATPase required for post-termination ribosome recycling
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:32707033
qualifier: enables
review:
summary: Interaction with CSNK2A1 (P68400) from a kinase-interaction-network study. Bare protein binding is uninformative.
action: KEEP_AS_NON_CORE
reason: Records a kinase interaction but uninformative term; not core.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:32707033 UniProtKB:P68400
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:32911434
qualifier: enables
review:
summary: Interaction with NFE2L2/NRF2 (Q16236) from an NRF2-interactome screen. Bare protein binding is uninformative and likely peripheral.
action: KEEP_AS_NON_CORE
reason: Records a real interaction but uninformative term and peripheral to translation initiation; not core.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:32911434 UniProtKB:Q16236
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:33961781
qualifier: enables
review:
summary: BioPlex affinity-purification capturing an EIF3J-CSNK2A1 (P68400) interaction. Bare protein binding is uninformative.
action: KEEP_AS_NON_CORE
reason: Records a kinase interaction but uninformative term; not core.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:33961781 UniProtKB:P68400
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:35271311
qualifier: enables
review:
summary: OpenCell endogenous-tagging interactome capturing EIF3J interactions with EIF3B (P55884) and ABCE1 (P61221), consistent with eIF-3 docking and recycling roles. Bare protein binding is uninformative.
action: KEEP_AS_NON_CORE
reason: Records biologically consistent interactions (EIF3B, ABCE1) but uninformative term; captured by complex/initiation annotations.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005515 protein binding molecular_function ECO:0000353 IPI PMID:35271311 UniProtKB:P55884
- term:
id: GO:0042802
label: identical protein binding
evidence_type: IPI
original_reference_id: PMID:32296183
qualifier: enables
review:
summary: EIF3J self-interaction reported in the HuRI binary interactome (consistent with the EIF3J-EIF3J IntAct entry). A real homotypic interaction but not a core function.
action: KEEP_AS_NON_CORE
reason: Records a self-interaction; not part of the core translation-initiation function.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0042802 identical protein binding molecular_function ECO:0000353 IPI PMID:32296183 UniProtKB:O75822
- term:
id: GO:0001732
label: formation of cytoplasmic translation initiation complex
evidence_type: NAS
original_reference_id: PMID:16920360
qualifier: involved_in
review:
summary: Author statement (eIF3 review) that eIF-3 serves as a scaffold for assembly of translation initiation complexes; EIF3J participates as a subunit.
action: ACCEPT
reason: Consistent with eIF-3's documented role in initiation-complex assembly; core process for EIF3J as a subunit.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0001732 formation of cytoplasmic translation initiation complex biological_process ECO:0005547 NAS PMID:16920360
- term:
id: GO:0005852
label: eukaryotic translation initiation factor 3 complex
evidence_type: IPI
original_reference_id: PMID:17322308
qualifier: part_of
review:
summary: Direct (ComplexPortal/MS) evidence placing EIF3J in the eIF-3 complex. Core cellular component.
action: ACCEPT
reason: Mass-spectrometry characterization of human eIF-3 confirms EIF3J as a component.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005852 eukaryotic translation initiation factor 3 complex cellular_component ECO:0000353 IPI PMID:17322308
- term:
id: GO:0005829
label: cytosol
evidence_type: TAS
original_reference_id: Reactome:R-HSA-156808
qualifier: located_in
review:
summary: Reactome curated cytosolic localization for translation-initiation reactions.
action: ACCEPT
reason: Correct cytosolic localization, consistent with the cytoplasmic site of action.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-156808
- term:
id: GO:0005829
label: cytosol
evidence_type: TAS
original_reference_id: Reactome:R-HSA-156823
qualifier: located_in
review:
summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
action: ACCEPT
reason: Correct cytosolic localization.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-156823
- term:
id: GO:0005829
label: cytosol
evidence_type: TAS
original_reference_id: Reactome:R-HSA-157849
qualifier: located_in
review:
summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
action: ACCEPT
reason: Correct cytosolic localization.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-157849
- term:
id: GO:0005829
label: cytosol
evidence_type: TAS
original_reference_id: Reactome:R-HSA-72619
qualifier: located_in
review:
summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
action: ACCEPT
reason: Correct cytosolic localization.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-72619
- term:
id: GO:0005829
label: cytosol
evidence_type: TAS
original_reference_id: Reactome:R-HSA-72621
qualifier: located_in
review:
summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
action: ACCEPT
reason: Correct cytosolic localization.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-72621
- term:
id: GO:0005829
label: cytosol
evidence_type: TAS
original_reference_id: Reactome:R-HSA-72676
qualifier: located_in
review:
summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
action: ACCEPT
reason: Correct cytosolic localization.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-72676
- term:
id: GO:0005829
label: cytosol
evidence_type: TAS
original_reference_id: Reactome:R-HSA-72691
qualifier: located_in
review:
summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
action: ACCEPT
reason: Correct cytosolic localization.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-72691
- term:
id: GO:0005829
label: cytosol
evidence_type: TAS
original_reference_id: Reactome:R-HSA-72697
qualifier: located_in
review:
summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations.
action: ACCEPT
reason: Correct cytosolic localization.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005829 cytosol cellular_component ECO:0000304 TAS Reactome:R-HSA-72697
- term:
id: GO:0003743
label: translation initiation factor activity
evidence_type: IC
original_reference_id: PMID:17322308
qualifier: contributes_to
review:
summary: Curator-inferred (from eIF-3 complex membership) that EIF3J contributes to translation initiation factor activity. The contributes_to qualifier correctly reflects its accessory role within the complex.
action: ACCEPT
reason: This is the core molecular function annotation for EIF3J, appropriately qualified as contributes_to for a non-catalytic accessory subunit.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0003743 translation initiation factor activity molecular_function ECO:0000305 IC PMID:17322308
- term:
id: GO:0003743
label: translation initiation factor activity
evidence_type: IC
original_reference_id: PMID:18599441
qualifier: contributes_to
review:
summary: Curator-inferred translation initiation factor activity from eIF-3 complex membership (subunit interaction map study). Redundant with the other IC annotation.
action: ACCEPT
reason: Core molecular function, appropriately qualified contributes_to.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0003743 translation initiation factor activity molecular_function ECO:0000305 IC PMID:18599441
- term:
id: GO:0005852
label: eukaryotic translation initiation factor 3 complex
evidence_type: IDA
original_reference_id: PMID:17322308
qualifier: part_of
review:
summary: Direct MS-based evidence for EIF3J as an eIF-3 component. Core cellular component.
action: ACCEPT
reason: Directly demonstrated eIF-3 complex membership.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005852 eukaryotic translation initiation factor 3 complex cellular_component ECO:0000314 IDA PMID:17322308
- term:
id: GO:0005852
label: eukaryotic translation initiation factor 3 complex
evidence_type: IDA
original_reference_id: PMID:18599441
qualifier: part_of
review:
summary: Direct MS-based evidence for EIF3J as an eIF-3 component (subunit interaction map). Core cellular component.
action: ACCEPT
reason: Directly demonstrated eIF-3 complex membership.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0005852 eukaryotic translation initiation factor 3 complex cellular_component ECO:0000314 IDA PMID:18599441
- term:
id: GO:0006413
label: translational initiation
evidence_type: IC
original_reference_id: PMID:17322308
qualifier: involved_in
review:
summary: Curator-inferred involvement in translational initiation from eIF-3 membership. Core biological process.
action: ACCEPT
reason: EIF3J participates in translation initiation as an eIF-3 subunit.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0006413 translational initiation biological_process ECO:0000305 IC PMID:17322308
- term:
id: GO:0006413
label: translational initiation
evidence_type: IC
original_reference_id: PMID:18599441
qualifier: involved_in
review:
summary: Curator-inferred involvement in translational initiation from eIF-3 membership. Redundant with the other IC annotation.
action: ACCEPT
reason: Core biological process for EIF3J as an eIF-3 subunit.
supported_by:
- reference_id: file:human/EIF3J/EIF3J-goa.tsv
supporting_text: GO:0006413 translational initiation biological_process ECO:0000305 IC PMID:18599441
references:
- id: GO_REF:0000033
title: Annotation inferences using phylogenetic trees.
findings: []
- id: GO_REF:0000104
title: Automatic annotation of UniProtKB entries based on UniRule rules.
findings: []
- id: GO_REF:0000120
title: Combined Automated Annotation using Multiple IEA Methods.
findings: []
- id: PMID:14688252
title: The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro.
reference_review:
relevance: HIGH
correctness: VERIFIED
review_notes: "Cached publications/PMID_14688252.md title matches YAML; directly establishes
EIF3J's core function โ required for stable binding of eIF-3 (and subcomplexes) to 40S
ribosomal subunits. This is the primary experimental support cited in core_functions."
findings:
- statement: EIF3J (the j-subunit) is required for stable binding of eIF-3 and its subcomplexes to 40S ribosomal subunits.
reference_section_type: RESULTS
- id: PMID:16920360
title: 'eIF3: a versatile scaffold for translation initiation complexes.'
findings:
- statement: eIF-3 acts as a scaffold for assembly of translation initiation complexes.
reference_section_type: RESULTS
- id: PMID:16932749
title: p97/DAP5 is a ribosome-associated factor that facilitates protein synthesis and cell proliferation by modulating the synthesis of cell cycle proteins.
findings: []
- id: PMID:17322308
title: Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry.
findings:
- statement: Mass-spectrometry characterization of human eIF-3 confirms EIF3J as a subunit of the complex.
reference_section_type: RESULTS
- id: PMID:18599441
title: Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3.
findings:
- statement: Subunit interaction map of eIF-3 places EIF3J as a labile subunit binding via EIF3B.
reference_section_type: RESULTS
- id: PMID:18628297
title: Human DDX3 functions in translation and interacts with the translation initiation factor eIF3.
findings: []
- id: PMID:22113938
title: A bead-based approach for large-scale identification of in vitro kinase substrates.
findings: []
- id: PMID:25852190
title: Integrative analysis of kinase networks in TRAIL-induced apoptosis provides a source of potential targets for combination therapy.
findings: []
- id: PMID:32296183
title: A reference map of the human binary protein interactome.
findings: []
- id: PMID:32707033
title: Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases.
findings: []
- id: PMID:32911434
title: A functionally defined high-density NRF2 interactome reveals new conditional regulators of ARE transactivation.
findings: []
- id: PMID:33961781
title: Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
findings: []
- id: PMID:35271311
title: 'OpenCell: Endogenous tagging for the cartography of human cellular organization.'
findings: []
- id: PMID:25849773
title: eIF3 targets cell-proliferation messenger RNAs for translational activation or repression.
findings:
- statement: eIF-3 selectively targets a subset of cell-proliferation mRNAs for translational activation or repression via stem-loop binding.
reference_section_type: RESULTS
- id: PMID:27462815
title: eIF3d is an mRNA cap-binding protein that is required for specialized translation initiation.
findings:
- statement: eIF-3 (via eIF3d) mediates specialized cap-dependent translation initiation.
reference_section_type: RESULTS
- id: Reactome:R-HSA-156808
title: Reactome translation-initiation reaction (cytosolic).
findings: []
- id: Reactome:R-HSA-156823
title: Reactome translation-initiation reaction (cytosolic).
findings: []
- id: Reactome:R-HSA-157849
title: Reactome translation-initiation reaction (cytosolic).
findings: []
- id: Reactome:R-HSA-72619
title: Reactome translation-initiation reaction (cytosolic).
findings: []
- id: Reactome:R-HSA-72621
title: Reactome translation-initiation reaction (cytosolic).
findings: []
- id: Reactome:R-HSA-72676
title: Reactome translation-initiation reaction (cytosolic).
findings: []
- id: Reactome:R-HSA-72691
title: Reactome translation-initiation reaction (cytosolic).
findings: []
- id: Reactome:R-HSA-72697
title: Reactome translation-initiation reaction (cytosolic).
findings: []
- id: file:human/EIF3J/EIF3J-deep-research-falcon.md
title: Falcon deep research report for EIF3J
reference_review:
relevance: HIGH
correctness: UNVERIFIED
review_notes: "LLM-synthesized deep-research report (Edison/falcon); citations are author-year
keys to reviews/primary papers, not independently re-verified here, hence UNVERIFIED.
EIF3J-SUBUNIT-SPECIFIC claims that are well-anchored to primary literature and used below:
(1) eIF3j binds the human 40S near the mRNA entry channel and A-site, anti-cooperatively with
mRNA, acting as a gatekeeper for mRNA accommodation and being displaced upon mRNA recruitment
in an ATP-dependent, helicase-independent manner (Sokabe & Fraser 2017, PNAS); (2) eIF3j
functionally couples to ABCE1/RLI1 and enhances post-termination ribosome recycling (Young &
Guydosh 2022, BioEssays); (3) eIF3j N-terminus contacts the eIF3b RRM (NMR) and its C-terminus
mediates transcript-selective inhibition of a subset of circRNA translation (Song et al. 2022).
DISTINGUISH from eIF3 HOLO-COMPLEX inference: the report repeatedly attributes whole-eIF3
functions (43S/48S PIC formation, cap-dependent initiation, mRNA scanning, start-codon
selectivity, NF-kB/IFN crosstalk) to the complex; these are NOT EIF3J-subunit-specific and were
not used to strengthen subunit-level annotations. The eIF3j-specific, biochemically grounded
roles are the mRNA-entry-channel/A-site gatekeeping and the ABCE1-coupled recycling role."
findings:
- statement: eIF3j binds the human 40S near the mRNA entry channel and A-site (anti-cooperatively with mRNA) as a gatekeeper for mRNA accommodation, and is displaced upon mRNA recruitment; it also functionally couples to ABCE1/RLI1 to enhance post-termination ribosome recycling.
reference_section_type: RESULTS
- id: file:human/EIF3J/EIF3J-uniprot.txt
title: UniProt entry O75822 (EIF3J_HUMAN), Eukaryotic translation initiation factor 3 subunit J.
findings:
- statement: EIF3J is a labile/loosely-associated subunit of the eIF-3 complex that binds via EIF3B; eIF-3 associates with the 40S subunit, drives 43S/48S pre-initiation complex formation, mRNA recruitment and scanning, and post-termination ribosome recycling; cytoplasmic; phosphorylated upon serum stimulation.
reference_section_type: OTHER
core_functions:
- description: Accessory (labile) subunit of the eIF-3 complex that contributes translation initiation factor activity, helping eIF-3 assemble the 43S/48S pre-initiation complexes on the 40S ribosomal subunit and recruit/scan mRNA during cap-dependent translation initiation.
molecular_function:
id: GO:0003743
label: translation initiation factor activity
in_complex:
id: GO:0005852
label: eukaryotic translation initiation factor 3 complex
locations:
- id: GO:0005737
label: cytoplasm
supported_by:
- reference_id: file:human/EIF3J/EIF3J-uniprot.txt
supporting_text: required for several steps in the initiation of protein synthesis
- reference_id: PMID:14688252
supporting_text: j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro
- description: Structural component of the eIF-3 complex; EIF3J docks onto eIF-3 through EIF3B and is required for stable association of eIF-3 with the 40S ribosomal subunit, positioning near the mRNA entry channel and modulating mRNA loading and 40S availability (including in ribosome recycling).
molecular_function:
id: GO:0003743
label: translation initiation factor activity
locations:
- id: GO:0005737
label: cytoplasm
supported_by:
- reference_id: file:human/EIF3J/EIF3J-uniprot.txt
supporting_text: EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B
- reference_id: file:human/EIF3J/EIF3J-deep-research-falcon.md
supporting_text: Binds the 40S small subunit near the mRNA entry channel and A-site; competes anti-cooperatively with accommodated mRNA
in_complex:
id: GO:0005852
label: eukaryotic translation initiation factor 3 complex
proposed_new_terms: []
suggested_questions:
- question: Does human EIF3J have a distinct, separable role in 40S ribosome recycling/availability (post-termination) versus initiation, as suggested by yeast Hcr1?
- question: How does the sub-stoichiometric/labile association of EIF3J with eIF-3 regulate switching between mRNA-entry-channel occupancy and mRNA loading?
- question: What is the functional consequence of serum-stimulated phosphorylation of EIF3J for its association with eIF-3 and selective mRNA translation?
suggested_experiments:
- description: Selective EIF3J depletion/rescue with ribosome profiling and 40S/80S subunit-availability assays to dissect its contribution to initiation versus post-termination recycling.
- description: Cryo-EM of 40S-eIF-3 complexes with and without EIF3J to define its occupancy of the mRNA entry channel and effect on mRNA accommodation.
- description: Phosphomutant (phospho-null/phospho-mimetic) EIF3J variants to test how serum-stimulated phosphorylation modulates eIF-3 binding and translational output.