EIF5A

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0006414 translational elongation	IBA GO_REF:0000033	ACCEPT	Summary: eIF5A promotes translation elongation, particularly through ribosome-stalling motifs such as polyproline tracts. This phylogenetically inferred BP annotation captures the gene's core biological role. Reason: Strongly supported by UniProt function and experimental work across eukaryotes; this is the central biological process of eIF5A. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid
GO:0003746 translation elongation factor activity	IBA GO_REF:0000033	ACCEPT	Summary: eIF5A acts as a translation elongation factor, binding between the E and P sites of the ribosome to stimulate peptide-bond formation at difficult motifs. This is the core molecular function. Reason: Well established across eukaryotes and supported by UniProt; this is eIF5A's defining molecular activity (hypusine-dependent). Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Binds between the exit (E) and
GO:0003723 RNA binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: eIF5A contains an OB-fold and binds RNA (mRNA, and in vitro U6 snRNA / RRE). RNA binding is real but is a supporting activity subordinate to its ribosome-associated elongation function. Reason: RNA binding is documented but generic; the informative function is ribosome binding / elongation factor activity. Retained as a real but non-core capability. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt MRNA-BINDING
GO:0003746 translation elongation factor activity	IEA GO_REF:0000002	ACCEPT	Summary: InterPro-based electronic transfer of the elongation factor activity, redundant with and consistent with the IBA/ISS annotations for the same function. Reason: Correct molecular function, corroborated by stronger IBA and experimental evidence for eIF5A as an elongation factor. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Binds between the exit (E) and
GO:0005634 nucleus	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: Electronic (SubCell) nuclear localization, consistent with the experimentally documented hypusine/XPO4-dependent nuclear pool of eIF5A. Reason: A genuine but minor shuttling pool; the predominant site of action is the cytoplasmic ribosome. Retained as non-core nuclear localization. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Nuclear export of hypusinated protein is mediated by
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: Electronic (SubCell) cytoplasmic localization, the predominant compartment where eIF5A acts on translating ribosomes. Reason: Cytoplasm is eIF5A's primary site of action; corroborated by multiple experimental (EXP/IDA) annotations. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm
GO:0005789 endoplasmic reticulum membrane	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: eIF5A was detected as a peripheral protein on the cytoplasmic face of the ER membrane in early fractionation work. This is a peripheral/contextual localization, not its core compartment. Reason: Supported by a single early study (peripheral, cytoplasmic side); consistent with ribosome association at the ER but peripheral to the core cytosolic function. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Endoplasmic reticulum membrane
GO:0006414 translational elongation	IEA GO_REF:0000002	ACCEPT	Summary: InterPro-based electronic transfer of the elongation BP, redundant with the IBA/IMP annotations for the same process. Reason: Correct biological process; corroborated by stronger evidence. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt promotes translation elongation and
GO:0043022 ribosome binding	IEA GO_REF:0000002	ACCEPT	Summary: eIF5A binds the 80S ribosome (experimentally demonstrated), inserting between the E and P sites. Ribosome binding is the structural basis for its elongation factor activity. Reason: Experimentally validated 80S ribosome binding; central to and supporting the elongation factor mechanism. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Binds to 80S ribosomes PMID:27115996 Negative Cooperativity between eIF5A and eEF2 on Binding to the Ribosome.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	REMOVE	Summary: High-throughput Y2H interactome screen capturing eIF5A interactions, mostly with homeodomain/bZIP transcription factors (CRX, MEOX2, REL) plus DHPS. The bare protein binding term is uninformative. Reason: Bare GO:0005515 protein binding carries no functional information, so under the generic protein-binding policy this row is REMOVE. Removal does not mean the reported interaction is false; the summary and any supporting text keep it on record.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	REMOVE	Summary: HuRI binary interactome screen capturing eIF5A interactions (including SDCBP/syntenin and DHPS among many homeodomain TFs). Bare protein binding is uninformative. Reason: Bare GO:0005515 protein binding carries no functional information, so under the generic protein-binding policy this row is REMOVE. Removal does not mean the reported interaction is false; the summary and any supporting text keep it on record.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	MODIFY	Summary: BioPlex affinity-purification capturing the eIF5A-DOHH (Q9BU89) interaction. DOHH is the deoxyhypusine hydroxylase that completes hypusine synthesis, so this interaction is biologically meaningful, though the term itself is uninformative. Reason: Bare protein binding is uninformative. The WITH partner is DOHH (Q9BU89), an enzyme of the hypusination pathway acting on eIF5A; the specific enzyme-binding relationship is better captured by enzyme binding. UniProt records the curated DOHH interaction (PubMed:17213197). Proposed replacements: enzyme binding Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Interacts with DOHH PMID:17213197 Deoxyhypusine hydroxylase (DOHH) is a novel metalloenzyme that catalyzes the
GO:0005654 nucleoplasm	IDA GO_REF:0000052	KEEP AS NON CORE	Summary: HPA immunofluorescence places a pool of eIF5A in the nucleoplasm, consistent with the documented hypusine/XPO4-dependent shuttling pool. Reason: Genuine nuclear pool but peripheral to the cytoplasmic ribosome-associated core function. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt there was a dynamic shift in the localization from predominantly cytoplasmic to primarily nuclear under apoptotic inducing conditions PMID:12210765 eIF-5A was present in both the nucleus and cytoplasm
GO:0005829 cytosol	IDA GO_REF:0000052	ACCEPT	Summary: HPA immunofluorescence cytosolic localization, agreeing with eIF5A's predominant cytosolic ribosome-associated site of action. Reason: Direct evidence for cytosolic localization, consistent with the core function. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Hypusine modification promotes the nuclear export and cytoplasmic localization file:human/EIF5A/EIF5A-uniprot.txt Binds to 80S ribosomes (PubMed:27115996)
GO:0005634 nucleus	EXP PMID:10944119 Exportin 4: a mediator of a novel nuclear export pathway in ...	KEEP AS NON CORE	Summary: Experimental nuclear localization linked to XPO4/Ran-mediated nuclear export of hypusinated eIF5A. Reason: Genuine shuttling pool; non-core relative to cytoplasmic ribosome function. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Nuclear export of hypusinated protein is mediated by
GO:0005634 nucleus	EXP PMID:19379712 The effect of hypusine modification on the intracellular loc...	KEEP AS NON CORE	Summary: Experimental nuclear localization shown to depend on hypusine/acetylation status of eIF5A. Reason: Real but PTM-dependent shuttling pool; non-core. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Hypusine modification promotes the
GO:0005634 nucleus	EXP PMID:27306458 Structure of the exportin Xpo4 in complex with RanGTP and th...	KEEP AS NON CORE	Summary: Structural/biochemical study of XPO4-RanGTP-eIF5A export complex; nuclear annotation reflects the shuttling pool. Reason: Nuclear localization is part of XPO4-mediated shuttling; non-core relative to cytoplasmic translation. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Nuclear export of hypusinated protein is mediated by
GO:0005634 nucleus	EXP PMID:8253832 Eukaryotic initiation factor 5A is a cellular target of the ...	KEEP AS NON CORE	Summary: Nuclear localization in the context of eIF5A serving as an HIV-1 Rev cofactor for retroviral mRNA export. Reason: Nuclear pool tied to the Rev/Rex viral-cofactor context; non-core relative to translation elongation. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt essential for mRNA export of retroviral transcripts
GO:0005737 cytoplasm	EXP PMID:10944119 Exportin 4: a mediator of a novel nuclear export pathway in ...	ACCEPT	Summary: Experimental cytoplasmic localization, the predominant compartment for eIF5A. Reason: Cytoplasm is the core site of action; experimentally supported. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm
GO:0005737 cytoplasm	EXP PMID:19379712 The effect of hypusine modification on the intracellular loc...	ACCEPT	Summary: Experimental cytoplasmic localization; hypusination promotes the cytoplasmic pool. Reason: Consistent with the predominant cytoplasmic site of action. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Hypusine modification promotes the
GO:0005737 cytoplasm	EXP PMID:27306458 Structure of the exportin Xpo4 in complex with RanGTP and th...	ACCEPT	Summary: Cytoplasmic localization consistent with eIF5A's ribosome-associated function. Reason: Core compartment, experimentally supported. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm
GO:0005737 cytoplasm	EXP PMID:8660923 The subcellular distribution of eukaryotic translation initi...	ACCEPT	Summary: Early cell-fractionation study documenting cytoplasmic distribution of eIF5A. Reason: Core compartment, experimentally supported. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm
GO:0005789 endoplasmic reticulum membrane	EXP PMID:8660923 The subcellular distribution of eukaryotic translation initi...	KEEP AS NON CORE	Summary: Same fractionation study detecting eIF5A as a peripheral protein on the cytoplasmic face of the ER membrane. Reason: Peripheral membrane association (cytoplasmic side), consistent with ER-associated ribosomes; peripheral to the core function. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Endoplasmic reticulum membrane
GO:0006414 translational elongation	IMP PMID:29712776 eIF5A is required for autophagy by mediating ATG3 translatio...	ACCEPT	Summary: eIF5A is required for translation of ATG3 (at a difficult motif), thereby enabling autophagy. This is a specific, experimentally demonstrated example of eIF5A's elongation function. Reason: IMP evidence that eIF5A mediates ATG3 translation directly supports its role in translational elongation. Supporting Evidence: PMID:29712776 eIF5A is required for autophagy by mediating ATG3 translation. file:human/EIF5A/EIF5A-uniprot.txt is required for autophagy by assisting the ribosome in translating the ATG3 protein
GO:0033209 tumor necrosis factor-mediated signaling pathway	IDA PMID:17187778 Eukaryotic translation initiation factor 5A induces apoptosi...	KEEP AS NON CORE	Summary: eIF5A nuclear accumulation and apoptotic effects in response to TNF-alpha signaling. This is a context-dependent downstream role, not the core translation function. Reason: A genuine but pleiotropic stress/apoptosis-context role distinct from the core elongation function. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Also regulates TNF-mediated apoptosis
GO:0045944 positive regulation of transcription by RNA polymerase II	IMP PMID:15371445 A novel eIF5A complex functions as a regulator of p53 and p5...	MARK AS OVER ANNOTATED	Summary: Derived from a study where eIF5A (with SDCBP) regulates p53 and p53-dependent apoptosis. The transcriptional effect is an indirect downstream consequence, not a direct eIF5A transcription function. Reason: eIF5A is a translation factor, not a transcriptional regulator; the transcription effect here is indirect (via p53). Over-annotation of an indirect outcome. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt functions as a regulator of p53 and p53-dependent apoptosis
GO:0098586 cellular response to virus	IMP PMID:8596953 Inhibition of HIV-1 replication in lymphocytes by mutants of...	KEEP AS NON CORE	Summary: eIF5A serves as a cellular cofactor for HIV-1 Rev-mediated retroviral mRNA export. The "cellular response to virus" framing reflects this viral-cofactor role. Reason: A genuine microbial-infection cofactor role (Rev/Rex), but distinct from and non-core relative to translation elongation. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Cellular cofactor of human T-cell
GO:0098586 cellular response to virus	IMP PMID:9465063 Interaction of the HIV-1 rev cofactor eukaryotic initiation ...	KEEP AS NON CORE	Summary: eIF5A interaction with ribosomal protein L5 in the HIV-1 Rev cofactor context; same viral-cofactor role. Reason: Genuine Rev-cofactor / viral mRNA export role; non-core relative to translation. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt essential for mRNA export of retroviral transcripts
GO:1902255 positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator	IDA PMID:15371445 A novel eIF5A complex functions as a regulator of p53 and p5...	KEEP AS NON CORE	Summary: eIF5A, with SDCBP/syntenin, positively regulates p53-dependent apoptosis. A genuine context-dependent role, downstream of its translation function. Reason: Real but pleiotropic apoptosis-regulatory role; non-core relative to the elongation function. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt functions as a regulator of p53 and p53-dependent apoptosis
GO:0005829 cytosol	TAS Reactome:R-HSA-204617	ACCEPT	Summary: Reactome curated cytosolic localization (hypusine synthesis pathway), consistent with the core compartment. Reason: Correct cytosolic localization, agrees with experimental evidence. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Hypusine modification promotes the nuclear export and cytoplasmic localization
GO:0005829 cytosol	TAS Reactome:R-HSA-204647	ACCEPT	Summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations. Reason: Correct cytosolic localization. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Hypusine modification promotes the nuclear export and cytoplasmic localization
GO:0005829 cytosol	TAS Reactome:R-HSA-204662	ACCEPT	Summary: Reactome curated cytosolic localization, redundant with the other cytosol annotations. Reason: Correct cytosolic localization. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Hypusine modification promotes the nuclear export and cytoplasmic localization
GO:0016020 membrane	HDA PMID:19946888 Defining the membrane proteome of NK cells.	MARK AS OVER ANNOTATED	Summary: eIF5A appeared in a high-throughput membrane-proteome dataset of NK cells. This is a generic, non-specific localization likely reflecting ribosome/peripheral membrane association. Reason: Generic "membrane" from a high-throughput proteomics survey; uninformative and not a meaningful compartment assignment for a cytosolic translation factor. The survey itself notes that most identified species were only transiently membrane-associated; the specific curated membrane association is a peripheral ER-membrane pool. Supporting Evidence: PMID:19946888 The remaining species were largely involved in cellular processes and molecular functions that could be predicted to be transiently associated with membranes. file:human/EIF5A/EIF5A-uniprot.txt Endoplasmic reticulum membrane {ECO:0000269\|PubMed:8660923}; Peripheral membrane protein
GO:0003723 RNA binding	HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ...	KEEP AS NON CORE	Summary: eIF5A captured in an mRNA-interactome (RNA interactome capture) dataset, consistent with its RNA/mRNA-binding OB-fold and ribosome association. Reason: Real RNA-binding capability but generic; the informative function is ribosome binding / elongation factor activity. The mRNA-interactome capture assay detects RNA-bound proteins directly; this defers to the curator's reading of the full text for EIF5A. Supporting Evidence: PMID:22681889 We developed a photoreactive nucleotide-enhanced UV crosslinking and oligo(dT) purification approach to identify the mRNA-bound proteome using quantitative proteomics
GO:0003746 translation elongation factor activity	ISS GO_REF:0000024	ACCEPT	Summary: Sequence-similarity transfer of elongation factor activity from yeast eIF5A, consistent with the IBA/IEA annotations for the same core function. Reason: Correct core molecular function, supported by orthology and experimental data. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (PubMed:33547280)
GO:0045901 positive regulation of translational elongation	ISS GO_REF:0000024	ACCEPT	Summary: eIF5A positively regulates elongation, especially through stalling motifs. Captures the directionality of its core role. Reason: Consistent with eIF5A's documented elongation-promoting activity at polyproline and other difficult motifs. Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt specifically required for efficient translation of
GO:0017070 U6 snRNA binding	IDA PMID:9285100 Interaction of eukaryotic initiation factor 5A with the huma...	KEEP AS NON CORE	Summary: eIF5A binds U6 snRNA (and the HIV-1 RRE) in vitro in a hypusine-dependent manner. An isolated in vitro RNA-binding observation, peripheral to its core function. Reason: Single in vitro RNA-binding observation; a real but peripheral activity, not part of the core elongation role. Supporting Evidence: PMID:9285100 Preliminary studies also indicated that eIF-5A can bind to RNA such as U6 snRNA and that deoxyhypusine modification appears to be required for the binding.
GO:0005515 protein binding	IPI PMID:10381392 Nuclear pore localization and nucleocytoplasmic transport of...	REMOVE	Summary: Interaction with the export receptor CRM1 in the context of nucleocytoplasmic shuttling of eIF5A. Bare protein binding is uninformative. Reason: Bare GO:0005515 protein binding carries no functional information, so under the generic protein-binding policy this row is REMOVE. Removal does not mean the reported interaction is false; the summary and any supporting text keep it on record.
GO:0005515 protein binding	IPI PMID:10944119 Exportin 4: a mediator of a novel nuclear export pathway in ...	REMOVE	Summary: Interaction with the XPO4/RanGTP export machinery. The biologically meaningful relationship is eIF5A's export by XPO4; the bare term is uninformative. Reason: Bare GO:0005515 protein binding carries no functional information, so under the generic protein-binding policy this row is REMOVE. Removal does not mean the reported interaction is false; the summary and any supporting text keep it on record.
GO:0005515 protein binding	IPI PMID:15371445 A novel eIF5A complex functions as a regulator of p53 and p5...	REMOVE	Summary: Interaction with SDCBP/syntenin in the p53 apoptosis-regulation study. Bare protein binding is uninformative. Reason: Bare GO:0005515 protein binding carries no functional information, so under the generic protein-binding policy this row is REMOVE. Removal does not mean the reported interaction is false; the summary and any supporting text keep it on record.
GO:0005515 protein binding	IPI PMID:17213197 Specificity of the deoxyhypusine hydroxylase-eukaryotic tran...	MODIFY	Summary: Interaction with DOHH (deoxyhypusine hydroxylase), the enzyme that completes hypusine synthesis on eIF5A. Biologically meaningful enzyme-substrate binding. Reason: Bare protein binding is uninformative. The partner is the hypusination enzyme DOHH acting on eIF5A; enzyme binding is the appropriate specific term. Proposed replacements: enzyme binding Supporting Evidence: file:human/EIF5A/EIF5A-uniprot.txt Interacts with DOHH
GO:0005515 protein binding	IPI PMID:9442029 Identification of the eukaryotic initiation factor 5A as a r...	REMOVE	Summary: Interaction with tissue transglutaminase II reported as a retinoic-acid-stimulated binding partner. Isolated interaction; bare term is uninformative. Reason: Bare GO:0005515 protein binding carries no functional information, so under the generic protein-binding policy this row is REMOVE. Removal does not mean the reported interaction is false; the summary and any supporting text keep it on record.
GO:0005515 protein binding	IPI PMID:9465063 Interaction of the HIV-1 rev cofactor eukaryotic initiation ...	REMOVE	Summary: Interaction with ribosomal protein L5 in the HIV-1 Rev cofactor context. Bare protein binding is uninformative. Reason: Bare GO:0005515 protein binding carries no functional information, so under the generic protein-binding policy this row is REMOVE. Removal does not mean the reported interaction is false; the summary and any supporting text keep it on record.
GO:0005634 nucleus	IDA PMID:12210765 Subcellular localization of the hypusine-containing eukaryot...	KEEP AS NON CORE	Summary: Immunofluorescence/GFP localization showing a nuclear pool of hypusine-containing eIF5A. Reason: Genuine nuclear pool; non-core relative to the cytoplasmic ribosome function. Supporting Evidence: PMID:12210765 Immunofluorescent staining of the formaldehyde-fixed cells showed that eIF-5A was present in both the nucleus and cytoplasm.
GO:0005642 annulate lamellae	IDA PMID:12210765 Subcellular localization of the hypusine-containing eukaryot...	KEEP AS NON CORE	Summary: eIF5A detected at annulate lamellae (stacked nuclear-pore-containing ER membranes), consistent with its nuclear-pore/shuttling association. Reason: A specialized localization tied to nuclear pore/shuttling; peripheral to the core function. The abstract does not mention annulate lamellae; this defers to the curator's reading of the full text of this localization study. Supporting Evidence: PMID:12210765 we have determined the subcellular distribution of eIF-5A by indirect immunofluorescent staining and by direct visualization of green fluorescent protein tagged eIF-5A (GFP-eIF5A).
GO:0005643 nuclear pore	IDA PMID:10381392 Nuclear pore localization and nucleocytoplasmic transport of...	KEEP AS NON CORE	Summary: eIF5A localized to the nuclear pore, consistent with its CRM1/XPO4-mediated nucleocytoplasmic transport. Reason: Reflects transport through the nuclear pore; peripheral to the core cytoplasmic function. The part_of qualifier is questionable but the localization is real. Supporting Evidence: PMID:10381392 we used indirect immunofluorescence and immunogold electron microscopy to demonstrate that eIF-5A accumulates at nuclear pore-associated intranuclear filaments in mammalian cells and Xenopus oocytes.
GO:0005737 cytoplasm	IDA PMID:12210765 Subcellular localization of the hypusine-containing eukaryot...	ACCEPT	Summary: Direct immunofluorescence/GFP evidence for cytoplasmic localization, the predominant compartment. Reason: Core compartment, directly supported. Supporting Evidence: PMID:12210765 Immunofluorescent staining of the formaldehyde-fixed cells showed that eIF-5A was present in both the nucleus and cytoplasm.
GO:0003723 RNA binding	IDA PMID:15303967 Identification of mRNA that binds to eukaryotic initiation f...	KEEP AS NON CORE	Summary: Direct evidence that eIF5A binds specific mRNAs (affinity co-purification). A real RNA-binding activity supporting its ribosome-associated function. Reason: Genuine mRNA binding but generic; the informative function is ribosome binding / elongation factor activity. Supporting Evidence: PMID:15303967 Direct binding of the cloned RNA to eIF-5A could be demonstrated by electrophoretic mobility-shift assay.
GO:0005515 protein binding	IPI PMID:14622290 Identification and characterization of eukaryotic initiation...	REMOVE	Summary: Interaction reported during characterization of the paralog eIF5A-2. Bare protein binding is uninformative. Reason: Bare GO:0005515 protein binding carries no functional information, so under the generic protein-binding policy this row is REMOVE. Removal does not mean the reported interaction is false; the summary and any supporting text keep it on record.
GO:0005634 nucleus	IDA PMID:17187778 Eukaryotic translation initiation factor 5A induces apoptosi...	KEEP AS NON CORE	Summary: eIF5A nuclear accumulation in response to TNF-alpha (apoptosis context). Reason: Stimulus-dependent nuclear pool; non-core relative to cytoplasmic translation. Supporting Evidence: PMID:17187778 the protein is rapidly translocated from the cytoplasm to the nucleus by death receptor activation or following treatment with Actinomycin D.
GO:0005737 cytoplasm	IDA PMID:17187778 Eukaryotic translation initiation factor 5A induces apoptosi...	ACCEPT	Summary: Cytoplasmic localization of eIF5A (baseline) in the same TNF-alpha study. Reason: Core compartment, directly supported. Supporting Evidence: PMID:17187778 the protein is rapidly translocated from the cytoplasm to the nucleus by death receptor activation or following treatment with Actinomycin D.

Gene Description

Existing Annotations Review

Core Functions

Ribosome binding underlying its elongation activity; eIF5A binds 80S ribosomes and competes with eEF2, inserting between the E and P sites at the peptidyl transferase center.

References

Suggested Questions for Experts

Suggested Experiments

📚 Additional Documentation

Notes

Pn Notes

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