DBP5

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0003724 RNA helicase activity	IBA GO_REF:0000033	ACCEPT	Summary: DBP5 is a well-characterized DEAD-box RNA helicase with demonstrated ATP-dependent RNA unwinding activity. The IBA annotation is supported by extensive experimental evidence from multiple species, representing a core molecular function conserved across eukaryotes. Reason: This is a core function of DBP5. The DEAD-box helicase family is defined by this activity. The protein contains the diagnostic DEAD box motif and Q motif characteristic of this helicase class. IBA reflects legitimate phylogenetic inference of this conserved catalytic domain function. Supporting Evidence: PMID:9564047 It is shown here that Dbp5p is an ATP-dependent RNA helicase required for polyadenylated [poly(A)+] RNA export. PMID:9564048 Dbp5p/Rat8p, a previously uncharacterized member of the DEAD-box family of proteins, is closely related to eukaryotic initiation factor 4A(eIF4A) an RNA helicase essential for protein synthesis initiation. file:yeast/DBP5/DBP5-deep-research-falcon.md Dbp5 is a DEAD-box RNA helicase-family protein whose core activity is RNA-dependent ATP hydrolysis coupled to nucleotide-state–dependent conformational cycling, enabling binding and remodeling of RNA–protein complexes (RNPs) rather than long-range processive duplex unwinding. In the export context, this remodeling function is often described as an RNPase activity acting on messenger RNPs at the NPC
GO:0003729 mRNA binding	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: DBP5 binds mRNA as part of its catalytic mechanism for helicase activity. However, this annotation is overly generic for a protein whose function is specifically remodeling mRNP complexes. The binding represents a means to the mechanistic end of mRNA remodeling and export, not a separate function. Reason: While DBP5 does bind mRNA, describing this as a separate function obscures the more informative molecular mechanism. DBP5 binds mRNA transiently as substrate for ATP-dependent unwinding during the mRNA export process. The IBA annotation is technically correct but less informative than the actual catalytic function (RNA helicase activity). This should not be listed as a core function alongside the helicase activity, as it is subsidiary to that activity. Supporting Evidence: PMID:9564047 It is shown here that Dbp5p is an ATP-dependent RNA helicase required for polyadenylated [poly(A)+] RNA export. PMID:9564047 Dbp5p may play a role in unloading or remodeling messenger RNA particles (mRNPs) upon arrival in the cytoplasm
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: DBP5 localizes to the nucleus and specifically to the nuclear pore complex region. The IBA annotation reflects this well-documented subcellular localization pattern. Reason: While DBP5 is primarily cytoplasmic, it does accumulate at the nuclear pore complex on the cytoplasmic side and transiently associates with nuclear structures. The IBA annotation is appropriate for phylogenetic inference of documented subcellular localization. Supporting Evidence: PMID:9564048 Dbp5p/Rat8p is located within the cytoplasm and concentrated in the perinuclear region. Analysis of the distribution of Dbp5p/Rat8p in yeast strains where nuclear pore complexes are tightly clustered indicated that a fraction of this protein associates with nuclear pore complexes (NPCs).
GO:0010494 cytoplasmic stress granule	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: DBP5 has been observed in cytoplasmic stress granules, which is consistent with the protein's broader role in mRNA remodeling and processing. This represents a secondary cellular role. Reason: DBP5's presence in stress granules represents a stress-response localization of the protein rather than a core catalytic function. This is a conditional, non-essential aspect of DBP5 biology. The protein's primary function is mRNA export, with stress granule association being a secondary phenomenon. Supporting Evidence: PMID:27251550 Defects in THO/TREX-2 function cause accumulation of novel cytoplasmic mRNP granules
GO:0016973 poly(A)+ mRNA export from nucleus	IBA GO_REF:0000033	ACCEPT	Summary: DBP5 is a key factor in mRNA export from the nucleus. The poly(A)+ specificity reflects the well-characterized role of DBP5 in the export of mature, polyadenylated mRNAs. The IBA annotation appropriately represents this core function. Reason: This is a primary core function of DBP5. Extensive experimental evidence demonstrates that DBP5 is essential for mRNA export, specifically acting on poly(A)+ mRNAs at the cytoplasmic face of the nuclear pore complex. The phylogenetic inference is appropriate for this conserved and well-documented function. Supporting Evidence: PMID:9564047 Dbp5p is an ATP-dependent RNA helicase required for polyadenylated [poly(A)+] RNA export. PMID:9564048 In rat8 mutant strains, cells displayed rapid, synchronous accumulation of poly(A)+ RNA in nuclei when shifted to the non-permissive temperature. file:yeast/DBP5/DBP5-deep-research-falcon.md The mechanistic focus is on Dbp5-driven removal of export-associated factors such as Mex67–Mtr2 (major mRNA export receptor) and Nab2 (poly(A) RNA-binding/export factor), thereby enforcing directionality and enabling cytoplasmic fate decisions file:yeast/DBP5/DBP5-deep-research-falcon.md Directionality is established at the cytoplasmic NPC face, where Dbp5 activity promotes dissociation of export factors from the mRNP so that the particle cannot re-enter the nucleus using the same export-binding interactions
GO:0000166 nucleotide binding	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: DBP5 is an ATP-dependent enzyme that requires nucleotide binding for catalytic activity. This is a predictable annotation based on the helicase domain and ATP-binding motifs. Reason: While technically correct, nucleotide binding is a subsidiary property of ATP-dependent enzymes. This is less informative than the actual ATP binding term and should not be emphasized as a core function.
GO:0003676 nucleic acid binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: DBP5 binds nucleic acid (RNA) as part of its helicase mechanism. The InterPro mapping is appropriate for this conserved domain property. Reason: This is a parent term of RNA binding and is appropriate but redundant with more specific annotations. RNA binding subsumes this annotation.
GO:0003723 RNA binding	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: DBP5 binds RNA as substrate for helicase activity. This is documented from domain analysis and experimental evidence. Reason: RNA binding is a mechanistic property subsidiary to the primary helicase activity. Should not be listed as a core function separately from the catalytic activity.
GO:0003724 RNA helicase activity	IEA GO_REF:0000120	ACCEPT	Summary: DBP5 helicase activity is correctly inferred from domain annotation and sequence homology. This IEA annotation duplicates the IBA and IDA annotations already present. Reason: While redundant with IBA and IDA annotations for the same term, this IEA annotation is correct and appropriately supported by InterPro mapping. Multiple evidence codes for the same well-established function is acceptable in GO.
GO:0004386 helicase activity	IEA GO_REF:0000043	ACCEPT	Summary: DBP5 is a helicase with nucleic acid unwinding activity. This is a parent term to RNA helicase activity. Reason: This is a correct characterization of DBP5 as a helicase. While more general than RNA helicase activity, it appropriately represents the broader catalytic class.
GO:0005524 ATP binding	IEA GO_REF:0000120	ACCEPT	Summary: DBP5 contains a DEAD box domain with ATP binding site. This binding is essential for the helicase mechanism. Reason: ATP binding is a core mechanistic feature of DEAD-box helicases and is well-documented in the protein structure and function. This is appropriate to retain.
GO:0005643 nuclear pore	IEA GO_REF:0000044	ACCEPT	Summary: DBP5 is associated with the nuclear pore complex, specifically on the cytoplasmic face. The subcellular location annotation is appropriate. Reason: DBP5 is indeed a component of the nuclear pore export machinery. The annotation correctly represents the structural context where the protein operates.
GO:0005737 cytoplasm	IEA GO_REF:0000120	ACCEPT	Summary: DBP5 localizes primarily to the cytoplasm, where it resides both diffusely and at the nuclear pore complex. Reason: Appropriate subcellular localization annotation confirmed by experimental data. The cytoplasmic localization is essential for its mRNA export function.
GO:0010467 gene expression	IEA GO_REF:0000117	MARK AS OVER ANNOTATED	Summary: DBP5 contributes to gene expression by facilitating mRNA export, which is downstream of transcription and essential for protein synthesis. Reason: While DBP5 is involved in the post-transcriptional steps of gene expression, this annotation is overly broad and generic. DBP5 is not directly involved in transcription, translation initiation, or other early gene expression steps. The term obscures the specific mRNA export function.
GO:0015031 protein transport	IEA GO_REF:0000043	REMOVE	Summary: DBP5 is annotated as protein transport based on general transport keywords. However, DBP5 specifically transports RNA, not proteins. Reason: This annotation is mechanistically incorrect. DBP5 facilitates mRNA transport, not protein transport. The mRNA is transported as an mRNP complex, but the cargo is RNA, not protein. This should be removed in favor of more accurate mRNA transport annotations.
GO:0016787 hydrolase activity	IEA GO_REF:0000043	ACCEPT	Summary: DBP5 is an ATP-dependent enzyme with ATP hydrolysis activity as part of its catalytic mechanism. This parent term is appropriate. Reason: Hydrolase activity is the correct parent classification for ATP-dependent enzymes including helicases. This annotation accurately represents the enzymatic class.
GO:0016887 ATP hydrolysis activity	IEA GO_REF:0000116	ACCEPT	Summary: DBP5 catalyzes ATP hydrolysis coupled to RNA unwinding. The Rhea mapping appropriately captures this catalytic activity. Reason: This accurately represents the ATP hydrolysis catalytic activity. DEAD-box helicases use ATP hydrolysis to power RNA unwinding, making this annotation both appropriate and informative.
GO:0031965 nuclear membrane	IEA GO_REF:0000044	ACCEPT	Summary: DBP5 associates with the nuclear pore complex, which is embedded in the nuclear membrane. The localization annotation is appropriate. Reason: The nuclear membrane is the structural context where the nuclear pore complex resides. DBP5 peripheral association with the nuclear pore complex on the cytoplasmic face makes this annotation appropriate.
GO:0051028 mRNA transport	IEA GO_REF:0000043	ACCEPT	Summary: DBP5 functions in mRNA transport from nucleus to cytoplasm. This process term appropriately captures DBP5's role in mRNA export. Reason: mRNA transport is an appropriate process annotation for DBP5. While more general than the specific poly(A)+ mRNA export annotation, it correctly characterizes the biological process.
GO:0005515 protein binding	IPI PMID:15619606 Physical and genetic interactions link the yeast protein Zds...	REMOVE	Summary: DBP5 physically interacts with multiple protein partners including Zds1p and Gfd1p (Ymr255p). These protein-protein interactions are documented by experimental methods. However, generic protein binding term is uninformative. Reason: While the protein binding is documented, this annotation is overly generic and uninformative. The specific binding partners (Zds1p, Gfd1p) are known and documented in UniProt. Rather than generic protein binding, the annotations should focus on the functional roles of these interactions in mRNA export and complex assembly. Generic protein binding terms should be avoided per GO best practices. Supporting Evidence: PMID:15619606 2004 Dec 24. Physical and genetic interactions link the yeast protein Zds1p with mRNA nuclear export.
GO:0005515 protein binding	IPI PMID:16554755 Global landscape of protein complexes in the yeast Saccharom...	REMOVE	Summary: Protein binding annotation from large-scale yeast protein interaction study. While interactions are documented, the generic nature of the annotation is not informative. Reason: Generic protein binding annotations are not recommended per GO guidelines. Large-scale interaction studies should be represented at the level of specific, named binding partners and their functional roles. Supporting Evidence: PMID:16554755 Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.
GO:0005515 protein binding	IPI PMID:19805289 Structure of the C-terminus of the mRNA export factor Dbp5 r...	REMOVE	Summary: DBP5 interacts with Gle1p, its primary regulatory partner. This interaction is essential for DBP5 activation and mRNA export function. Reason: While the Gle1p interaction is critical, generic protein binding obscures this specific and important interaction. This would be better represented as a specific protein binding annotation for Gle1p, or better yet, as the functional consequence (activation by Gle1p and InsP6). Supporting Evidence: PMID:19805289 Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1.
GO:0005515 protein binding	IPI PMID:21441902 A conserved mechanism of DEAD-box ATPase activation by nucle...	REMOVE	Summary: Protein binding annotation from study of DEAD-box ATPase activation mechanism. The specific partners are nucleoporins and Gle1p involved in mRNA export. Reason: The generic protein binding term obscures the mechanistic importance of these interactions. While interactions are documented, they should be represented through their functional roles in mRNA export rather than as generic protein binding. Supporting Evidence: PMID:21441902 A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 in mRNA export.
GO:0006409 tRNA export from nucleus	IDA PMID:31453808 A nuclear role for the DEAD-box protein Dbp5 in tRNA export.	KEEP AS NON CORE	Summary: Evidence demonstrates that DBP5 has a function in tRNA export from the nucleus, in addition to its well-characterized mRNA export role. Falcon deep research (Rajan et al. 2024, eLife) adds biochemical and genetic detail: Dbp5 directly binds tRNA (Kd ~130-150 nM), but tRNA/dsRNA alone does not stimulate its ATPase; instead tRNA synergizes with Gle1/InsP6 to fully activate Dbp5, and Dbp5 acts in a Los1-independent pathway. This is a well-supported additional RNA export function rather than mere substrate promiscuity. Reason: The evidence for tRNA export is solid and now mechanistically defined, but it represents a secondary function relative to the protein's primary and essential role in bulk poly(A)+ mRNA export. Dbp5 binds structured tRNA directly and is activated via the same Gle1/InsP6 module used for mRNA export, operating in a pathway parallel to and independent of the canonical exporter Los1. Retained as non-core because mRNA export, not tRNA export, defines the essential function. Supporting Evidence: PMID:31453808 A nuclear role for the DEAD-box protein Dbp5 in tRNA export. file:yeast/DBP5/DBP5-deep-research-falcon.md Dbp5 binds tRNA in vitro with Kd ~150 nM (Phe tRNA) and ~130 nM (mixed tRNA) (Rajan et al., eLife 2024-01, https://doi.org/10.7554/elife.89835). file:yeast/DBP5/DBP5-deep-research-falcon.md tRNA (or dsRNA poly(I:C)) alone does not stimulate Dbp5 ATPase activity, unlike a typical ssRNA activator (poly(A)). However, tRNA/dsRNA synergizes with Gle1/InsP6 to fully activate Dbp5, reaching ~1.03 ± 0.04 ATP/s (mixed tRNA with Gle1/InsP6) comparable to ssRNA activation (~1.11 ± 0.07 ATP/s) file:yeast/DBP5/DBP5-deep-research-falcon.md Rajan et al. (eLife 2024-01) provide genetic and biochemical evidence that Dbp5 functions in tRNA export in a pathway parallel to canonical exporters:
GO:0003724 RNA helicase activity	IDA PMID:9564047 Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RN...	ACCEPT	Summary: Experimental evidence directly demonstrates DBP5 RNA helicase activity. The IDA annotation with PMID:9564047 is redundant with the IBA and IEA annotations for the same term, but provides direct experimental confirmation. Reason: Multiple evidence codes for the same well-established function are appropriate. This IDA annotation provides direct experimental confirmation of the helicase activity. Supporting Evidence: PMID:9564047 Dbp5p is an ATP-dependent RNA helicase required for polyadenylated [poly(A)+] RNA export.
GO:0010494 cytoplasmic stress granule	IDA PMID:27251550 Defects in THO/TREX-2 function cause accumulation of novel c...	KEEP AS NON CORE	Summary: Experimental data shows DBP5 localizes to cytoplasmic stress granule-like structures under conditions of defective mRNA export. Reason: This annotation represents a secondary, conditional localization. DBP5 stress granule accumulation occurs in response to mRNA export defects, not as a primary cellular function. Should be marked as non-core. Supporting Evidence: PMID:27251550 Defects in THO/TREX-2 function cause accumulation of novel cytoplasmic mRNP granules that can be cleared by autophagy.
GO:0016973 poly(A)+ mRNA export from nucleus	IMP PMID:27385342 Altered RNA processing and export lead to retention of mRNAs...	ACCEPT	Summary: Experimental mutation and phenotypic analysis shows DBP5 is directly involved in mRNA export. Multiple IMP and IDA annotations confirm this core function. Reason: This is a primary core function confirmed by multiple experimental methods. IMP annotations appropriately reflect the loss-of-function phenotype of DBP5 mutations. Supporting Evidence: PMID:27385342 Altered RNA processing and export lead to retention of mRNAs near transcription sites and nuclear pore complexes or within the nucleolus.
GO:0000822 inositol hexakisphosphate binding	IDA PMID:16783363 Inositol hexakisphosphate and Gle1 activate the DEAD-box pro...	ACCEPT	Summary: DBP5 directly binds inositol hexakisphosphate (InsP6), an essential cofactor that activates its ATPase activity at the nuclear pore complex. Reason: This represents a specific, mechanistically important ligand binding interaction. InsP6 is a cofactor required for DBP5 activation in mRNA export. The annotation appropriately represents this catalytic requirement. Supporting Evidence: PMID:16783363 We now propose that Dbp5 activation at NPCs requires Gle1 and InsP6. file:yeast/DBP5/DBP5-deep-research-falcon.md Alcázar-Román et al. (JBC 2010-05-28, https://doi.org/10.1074/jbc.M109.082370) describe Gle1 and IP6 as essential for mRNA export by activating Dbp5 ATPase and promoting localized mRNP remodeling and directionality; they also report that the same module is required for proper translation termination
GO:0005634 nucleus	IDA PMID:15280434 Stress response in yeast mRNA export factor: reversible chan...	ACCEPT	Summary: DBP5 localizes to the nucleus and undergoes stress-dependent relocalization to nuclear regions under ethanol stress. Reason: Appropriate experimental confirmation of nuclear localization. While DBP5 is primarily cytoplasmic, it does associate with nuclear structures, particularly under stress conditions. Supporting Evidence: PMID:15280434 Jul 27. Stress response in yeast mRNA export factor: reversible changes in Rat8p localization are caused by ethanol stress but not heat shock.
GO:0005737 cytoplasm	IDA PMID:10610322 The RNA export factor Gle1p is located on the cytoplasmic fi...	ACCEPT	Summary: DBP5 is predominantly localized to the cytoplasm and is concentrated around the nuclear envelope at the cytoplasmic face of the nuclear pore complex. Reason: The primary subcellular localization of DBP5 is cytoplasmic. This annotation appropriately reflects the experimental localization data. Supporting Evidence: PMID:10610322 immunoelectron microscopy localizations indicate that Gle1p, Rip1p and Rat8p/Dbp5p are present on the NPC cytoplasmic fibrils
GO:0005737 cytoplasm	IDA PMID:15280434 Stress response in yeast mRNA export factor: reversible chan...	ACCEPT	Summary: DBP5 cytoplasmic localization confirmed under stress conditions. Redundant with other cytoplasm annotations but provides condition-specific evidence. Reason: Multiple lines of evidence confirm cytoplasmic localization under different conditions. Retention of redundant annotations is acceptable. Supporting Evidence: PMID:15280434 Jul 27. Stress response in yeast mRNA export factor: reversible changes in Rat8p localization are caused by ethanol stress but not heat shock.
GO:0005737 cytoplasm	IDA PMID:9564048 Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box prot...	ACCEPT	Summary: DBP5 is located in the cytoplasm, concentrated in the perinuclear region. Reason: Multiple evidence codes for the same subcellular localization reflect convergent experimental evidence from independent studies. Supporting Evidence: PMID:9564048 Dbp5p/Rat8p is located within the cytoplasm and concentrated in the perinuclear region.
GO:0005934 cellular bud tip	IDA PMID:19198597 Nuclear transport factor directs localization of protein syn...	KEEP AS NON CORE	Summary: DBP5 localizes to the cellular bud tip, possibly involved in directing mRNA and/or translation during mitosis. Reason: While localization to bud tip is documented, this represents a specialized, conditional cellular location related to cell division. This is a secondary, non-essential aspect of DBP5 cellular distribution. Supporting Evidence: PMID:19198597 Nuclear transport factor directs localization of protein synthesis during mitosis.
GO:0006406 mRNA export from nucleus	IMP PMID:9564048 Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box prot...	ACCEPT	Summary: Experimental mutation phenotype shows DBP5 is essential for mRNA export from the nucleus. IMP annotation reflects the loss-of-function phenotype. Reason: This is a primary core function confirmed by classical loss-of-function experiments. The IMP annotation appropriately represents the mutant phenotype. Supporting Evidence: PMID:9564048 In rat8 mutant strains, cells displayed rapid, synchronous accumulation of poly(A)+ RNA in nuclei when shifted to the non-permissive temperature.
GO:0006415 translational termination	IGI PMID:17272721 The DEAD-box RNA helicase Dbp5 functions in translation term...	KEEP AS NON CORE	Summary: DBP5 shows genetic interaction with translation termination factors eRF1 and eRF3, indicating a role in translation termination beyond mRNA export. Falcon deep research (Querl & Krebber 2023 review) supports a defined mechanism in which Dbp5 delivers eRF1 to terminating ribosomes and prevents premature eRF1-eRF3 interactions, thereby reducing readthrough. The same Gle1/InsP6 activation module that supports mRNA export is also required for proper translation termination. Reason: The genetic interactions are documented, and falcon deep research indicates this is a direct, mechanistically defined coupled function rather than mere pleiotropy or an indirect consequence of mRNA export defects: Dbp5 is proposed to deliver eRF1 to terminating ribosomes and prevent premature eRF1-eRF3 association. It is retained as non-core because the essential, defining function of Dbp5 is bulk mRNA export at the NPC, with translation termination being one of several downstream gene-expression steps that Dbp5 couples. Supporting Evidence: PMID:17272721 Dbp5 interacts genetically with both release factors and the polyadenlyate-binding protein Pab1. file:yeast/DBP5/DBP5-deep-research-falcon.md Querl & Krebber (Biological Chemistry, published online 2023-07-13, https://doi.org/10.1515/hsz-2023-0130) review evidence that Dbp5 functions in translation termination, including a mechanistic model where Dbp5 delivers eRF1 to terminating ribosomes and prevents premature eRF1–eRF3 interactions, thereby reducing readthrough file:yeast/DBP5/DBP5-deep-research-falcon.md Alcázar-Román et al. (JBC 2010-05-28, https://doi.org/10.1074/jbc.M109.082370) describe Gle1 and IP6 as essential for mRNA export by activating Dbp5 ATPase and promoting localized mRNP remodeling and directionality; they also report that the same module is required for proper translation termination
GO:0006415 translational termination	IPI PMID:17272721 The DEAD-box RNA helicase Dbp5 functions in translation term...	KEEP AS NON CORE	Summary: DBP5 shows direct physical interaction with eRF1, a translation termination factor. The interaction is specifically detected and characterized. Falcon deep research supports a model in which Dbp5 delivers eRF1 to terminating ribosomes and prevents premature eRF1-eRF3 interactions, reducing stop-codon readthrough. Reason: The physical interaction with eRF1 is documented and falcon deep research places it in a defined mechanistic model (Dbp5 delivers eRF1 and prevents premature eRF1-eRF3 association). Translation termination is retained as non-core because the protein's essential, defining function is bulk mRNA export at the nuclear pore complex; translation termination is one of the coupled downstream gene-expression steps. Supporting Evidence: PMID:17272721 The DEAD-box RNA helicase Dbp5 functions in translation termination. file:yeast/DBP5/DBP5-deep-research-falcon.md Querl & Krebber (Biological Chemistry, published online 2023-07-13, https://doi.org/10.1515/hsz-2023-0130) review evidence that Dbp5 functions in translation termination, including a mechanistic model where Dbp5 delivers eRF1 to terminating ribosomes and prevents premature eRF1–eRF3 interactions, thereby reducing readthrough
GO:0008186 ATP-dependent activity, acting on RNA	IDA PMID:19805289 Structure of the C-terminus of the mRNA export factor Dbp5 r...	ACCEPT	Summary: DBP5 is directly shown to have ATP-dependent RNA-modifying activity. This reflects the core catalytic function of the helicase. Reason: This annotation appropriately characterizes the ATP-dependent catalytic activity of DBP5 acting on RNA. It is both informative and accurate. Supporting Evidence: PMID:19805289 Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1.
GO:0044614 nuclear pore cytoplasmic filaments	IDA PMID:10610322 The RNA export factor Gle1p is located on the cytoplasmic fi...	ACCEPT	Summary: DBP5 is experimentally localized to the cytoplasmic filaments of the nuclear pore complex, where it functions in mRNA remodeling. Reason: This annotation accurately represents the specific subcellular microlocalization of DBP5 within the NPC structure. It provides important detail about where the mRNA export activity occurs. Supporting Evidence: PMID:10610322 immunoelectron microscopy localizations indicate that Gle1p, Rip1p and Rat8p/Dbp5p are present on the NPC cytoplasmic fibrils file:yeast/DBP5/DBP5-deep-research-falcon.md Dbp5 is enriched at the nuclear rim and is a key factor on the cytoplasmic face/cytoplasmic fibrils of the NPC, where terminal export remodeling is executed file:yeast/DBP5/DBP5-deep-research-falcon.md Dbp5 association with NPCs is highly dynamic, with ~0.8 s average residence time reported by FRAP in yeast

Gene Description

Existing Annotations Review

Core Functions

DBP5 binds inositol hexakisphosphate (InsP6) as a critical cofactor for activation at the nuclear pore complex. InsP6 binding is mediated by the nucleoporin Gle1 and is essential for efficient mRNA export. This interaction provides spatial and mechanistic control of DBP5 ATPase activity.

References

Deep Research

Falcon

📄 View Raw YAML