DBP5

id: P20449
gene_symbol: DBP5
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:559292
  label: Saccharomyces cerevisiae
description: 'DBP5 is an essential DEAD-box RNA helicase that functions as a key factor
  in mRNA nuclear export. It acts at the cytoplasmic face of the nuclear pore complex
  where it remodels mRNP complexes and facilitates mRNA release. The protein is activated
  by interaction with Gle1 and inositol hexakisphosphate (InsP6) at the NPC. Beyond
  its primary role in mRNA export, DBP5 also participates in tRNA export and has secondary
  roles in translation termination.'
existing_annotations:
  - term:
      id: GO:0003724
      label: RNA helicase activity
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      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.
      action: ACCEPT
      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.
      supported_by:
        - reference_id: PMID:9564047
          supporting_text: "It is shown here that Dbp5p is an ATP-dependent RNA helicase
            required for polyadenylated [poly(A)+] RNA export."
        - reference_id: PMID:9564048
          supporting_text: "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."
  - term:
      id: GO:0003729
      label: mRNA binding
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      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.
      action: KEEP_AS_NON_CORE
      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.
      supported_by:
        - reference_id: PMID:9564047
          supporting_text: "It is shown here that Dbp5p is an ATP-dependent RNA helicase
            required for polyadenylated [poly(A)+] RNA export."
        - reference_id: PMID:9564047
          supporting_text: "Dbp5p may play a role in unloading or remodeling messenger
            RNA particles (mRNPs) upon arrival in the cytoplasm"
  - term:
      id: GO:0005634
      label: nucleus
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: DBP5 localizes to the nucleus and specifically to the nuclear 
        pore complex region. The IBA annotation reflects this well-documented 
        subcellular localization pattern.
      action: ACCEPT
      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.
      supported_by:
        - reference_id: PMID:9564048
          supporting_text: "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)."
  - term:
      id: GO:0010494
      label: cytoplasmic stress granule
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      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.
      action: KEEP_AS_NON_CORE
      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.
      supported_by:
        - reference_id: PMID:27251550
          supporting_text: "Defects in THO/TREX-2 function cause accumulation of novel
            cytoplasmic mRNP granules"
  - term:
      id: GO:0016973
      label: poly(A)+ mRNA export from nucleus
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      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.
      action: ACCEPT
      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.
      supported_by:
        - reference_id: PMID:9564047
          supporting_text: "Dbp5p is an ATP-dependent RNA helicase required for polyadenylated
            [poly(A)+] RNA export."
        - reference_id: PMID:9564048
          supporting_text: "In rat8 mutant strains, cells displayed rapid, synchronous
            accumulation of poly(A)+ RNA in nuclei when shifted to the non-permissive
            temperature."
  - term:
      id: GO:0000166
      label: nucleotide binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      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.
      action: KEEP_AS_NON_CORE
      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.
  - term:
      id: GO:0003676
      label: nucleic acid binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    review:
      summary: DBP5 binds nucleic acid (RNA) as part of its helicase mechanism. 
        The InterPro mapping is appropriate for this conserved domain property.
      action: KEEP_AS_NON_CORE
      reason: This is a parent term of RNA binding and is appropriate but 
        redundant with more specific annotations. RNA binding subsumes this 
        annotation.
  - term:
      id: GO:0003723
      label: RNA binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: DBP5 binds RNA as substrate for helicase activity. This is 
        documented from domain analysis and experimental evidence.
      action: KEEP_AS_NON_CORE
      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.
  - term:
      id: GO:0003724
      label: RNA helicase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    review:
      summary: DBP5 helicase activity is correctly inferred from domain 
        annotation and sequence homology. This IEA annotation duplicates the IBA
        and IDA annotations already present.
      action: ACCEPT
      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.
  - term:
      id: GO:0004386
      label: helicase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: DBP5 is a helicase with nucleic acid unwinding activity. This is 
        a parent term to RNA helicase activity.
      action: ACCEPT
      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.
  - term:
      id: GO:0005524
      label: ATP binding
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    review:
      summary: DBP5 contains a DEAD box domain with ATP binding site. This 
        binding is essential for the helicase mechanism.
      action: ACCEPT
      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.
  - term:
      id: GO:0005643
      label: nuclear pore
    evidence_type: IEA
    original_reference_id: GO_REF:0000044
    review:
      summary: DBP5 is associated with the nuclear pore complex, specifically on
        the cytoplasmic face. The subcellular location annotation is 
        appropriate.
      action: ACCEPT
      reason: DBP5 is indeed a component of the nuclear pore export machinery. 
        The annotation correctly represents the structural context where the 
        protein operates.
  - term:
      id: GO:0005737
      label: cytoplasm
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    review:
      summary: DBP5 localizes primarily to the cytoplasm, where it resides both 
        diffusely and at the nuclear pore complex.
      action: ACCEPT
      reason: Appropriate subcellular localization annotation confirmed by 
        experimental data. The cytoplasmic localization is essential for its 
        mRNA export function.
  - term:
      id: GO:0010467
      label: gene expression
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    review:
      summary: DBP5 contributes to gene expression by facilitating mRNA export, 
        which is downstream of transcription and essential for protein 
        synthesis.
      action: MARK_AS_OVER_ANNOTATED
      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.
  - term:
      id: GO:0015031
      label: protein transport
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: DBP5 is annotated as protein transport based on general transport
        keywords. However, DBP5 specifically transports RNA, not proteins.
      action: REMOVE
      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.
  - term:
      id: GO:0016787
      label: hydrolase activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: DBP5 is an ATP-dependent enzyme with ATP hydrolysis activity as 
        part of its catalytic mechanism. This parent term is appropriate.
      action: ACCEPT
      reason: Hydrolase activity is the correct parent classification for 
        ATP-dependent enzymes including helicases. This annotation accurately 
        represents the enzymatic class.
  - term:
      id: GO:0016887
      label: ATP hydrolysis activity
    evidence_type: IEA
    original_reference_id: GO_REF:0000116
    review:
      summary: DBP5 catalyzes ATP hydrolysis coupled to RNA unwinding. The Rhea 
        mapping appropriately captures this catalytic activity.
      action: ACCEPT
      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.
  - term:
      id: GO:0031965
      label: nuclear membrane
    evidence_type: IEA
    original_reference_id: GO_REF:0000044
    review:
      summary: DBP5 associates with the nuclear pore complex, which is embedded 
        in the nuclear membrane. The localization annotation is appropriate.
      action: ACCEPT
      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.
  - term:
      id: GO:0051028
      label: mRNA transport
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: DBP5 functions in mRNA transport from nucleus to cytoplasm. This 
        process term appropriately captures DBP5's role in mRNA export.
      action: ACCEPT
      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.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:15619606
    review:
      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.
      action: REMOVE
      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.
      supported_by:
        - reference_id: PMID:15619606
          supporting_text: 2004 Dec 24. Physical and genetic interactions link 
            the yeast protein Zds1p with mRNA nuclear export.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:16554755
    review:
      summary: Protein binding annotation from large-scale yeast protein 
        interaction study. While interactions are documented, the generic nature
        of the annotation is not informative.
      action: REMOVE
      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.
      supported_by:
        - reference_id: PMID:16554755
          supporting_text: Global landscape of protein complexes in the yeast 
            Saccharomyces cerevisiae.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:19805289
    review:
      summary: DBP5 interacts with Gle1p, its primary regulatory partner. This 
        interaction is essential for DBP5 activation and mRNA export function.
      action: REMOVE
      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).
      supported_by:
        - reference_id: PMID:19805289
          supporting_text: Structure of the C-terminus of the mRNA export factor
            Dbp5 reveals the interaction surface for the ATPase activator Gle1.
  - term:
      id: GO:0005515
      label: protein binding
    evidence_type: IPI
    original_reference_id: PMID:21441902
    review:
      summary: Protein binding annotation from study of DEAD-box ATPase 
        activation mechanism. The specific partners are nucleoporins and Gle1p 
        involved in mRNA export.
      action: REMOVE
      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.
      supported_by:
        - reference_id: PMID:21441902
          supporting_text: A conserved mechanism of DEAD-box ATPase activation 
            by nucleoporins and InsP6 in mRNA export.
  - term:
      id: GO:0006409
      label: tRNA export from nucleus
    evidence_type: IDA
    original_reference_id: PMID:31453808
    review:
      summary: Recent evidence demonstrates that DBP5 has a function in tRNA 
        export from the nucleus, in addition to its well-characterized mRNA 
        export role. This represents an additional RNA export function beyond 
        poly(A)+ mRNA.
      action: KEEP_AS_NON_CORE
      reason: While the evidence is solid, tRNA export represents a secondary 
        and more recently discovered function of DBP5 compared to mRNA export. 
        The protein's primary and essential function is mRNA export. tRNA export
        may represent an ancillary function or a substrate promiscuity of the 
        mRNA export machinery.
      supported_by:
        - reference_id: PMID:31453808
          supporting_text: "A nuclear role for the DEAD-box protein Dbp5 in tRNA export."
  - term:
      id: GO:0003724
      label: RNA helicase activity
    evidence_type: IDA
    original_reference_id: PMID:9564047
    review:
      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.
      action: ACCEPT
      reason: Multiple evidence codes for the same well-established function are
        appropriate. This IDA annotation provides direct experimental 
        confirmation of the helicase activity.
      supported_by:
        - reference_id: PMID:9564047
          supporting_text: "Dbp5p is an ATP-dependent RNA helicase required for polyadenylated
            [poly(A)+] RNA export."
  - term:
      id: GO:0010494
      label: cytoplasmic stress granule
    evidence_type: IDA
    original_reference_id: PMID:27251550
    review:
      summary: Experimental data shows DBP5 localizes to cytoplasmic stress 
        granule-like structures under conditions of defective mRNA export.
      action: KEEP_AS_NON_CORE
      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.
      supported_by:
        - reference_id: PMID:27251550
          supporting_text: Defects in THO/TREX-2 function cause accumulation of 
            novel cytoplasmic mRNP granules that can be cleared by autophagy.
  - term:
      id: GO:0016973
      label: poly(A)+ mRNA export from nucleus
    evidence_type: IMP
    original_reference_id: PMID:27385342
    review:
      summary: Experimental mutation and phenotypic analysis shows DBP5 is 
        directly involved in mRNA export. Multiple IMP and IDA annotations 
        confirm this core function.
      action: ACCEPT
      reason: This is a primary core function confirmed by multiple experimental
        methods. IMP annotations appropriately reflect the loss-of-function 
        phenotype of DBP5 mutations.
      supported_by:
        - reference_id: PMID:27385342
          supporting_text: "Altered RNA processing and export lead to retention of
            mRNAs near transcription sites and nuclear pore complexes or within the
            nucleolus."
  - term:
      id: GO:0000822
      label: inositol hexakisphosphate binding
    evidence_type: IDA
    original_reference_id: PMID:16783363
    review:
      summary: DBP5 directly binds inositol hexakisphosphate (InsP6), an 
        essential cofactor that activates its ATPase activity at the nuclear 
        pore complex.
      action: ACCEPT
      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.
      supported_by:
        - reference_id: PMID:16783363
          supporting_text: "We now propose that Dbp5 activation at NPCs requires Gle1
            and InsP6."
  - term:
      id: GO:0005634
      label: nucleus
    evidence_type: IDA
    original_reference_id: PMID:15280434
    review:
      summary: DBP5 localizes to the nucleus and undergoes stress-dependent 
        relocalization to nuclear regions under ethanol stress.
      action: ACCEPT
      reason: Appropriate experimental confirmation of nuclear localization. 
        While DBP5 is primarily cytoplasmic, it does associate with nuclear 
        structures, particularly under stress conditions.
      supported_by:
        - reference_id: PMID:15280434
          supporting_text: 'Jul 27. Stress response in yeast mRNA export factor: reversible
            changes in Rat8p localization are caused by ethanol stress but not heat
            shock.'
  - term:
      id: GO:0005737
      label: cytoplasm
    evidence_type: IDA
    original_reference_id: PMID:10610322
    review:
      summary: DBP5 is predominantly localized to the cytoplasm and is 
        concentrated around the nuclear envelope at the cytoplasmic face of the 
        nuclear pore complex.
      action: ACCEPT
      reason: The primary subcellular localization of DBP5 is cytoplasmic. This 
        annotation appropriately reflects the experimental localization data.
      supported_by:
        - reference_id: PMID:10610322
          supporting_text: "immunoelectron microscopy localizations indicate that
            Gle1p, Rip1p and Rat8p/Dbp5p are present on the NPC cytoplasmic fibrils"
  - term:
      id: GO:0005737
      label: cytoplasm
    evidence_type: IDA
    original_reference_id: PMID:15280434
    review:
      summary: DBP5 cytoplasmic localization confirmed under stress conditions. 
        Redundant with other cytoplasm annotations but provides 
        condition-specific evidence.
      action: ACCEPT
      reason: Multiple lines of evidence confirm cytoplasmic localization under 
        different conditions. Retention of redundant annotations is acceptable.
      supported_by:
        - reference_id: PMID:15280434
          supporting_text: 'Jul 27. Stress response in yeast mRNA export factor: reversible
            changes in Rat8p localization are caused by ethanol stress but not heat
            shock.'
  - term:
      id: GO:0005737
      label: cytoplasm
    evidence_type: IDA
    original_reference_id: PMID:9564048
    review:
      summary: DBP5 is located in the cytoplasm, concentrated in the perinuclear
        region.
      action: ACCEPT
      reason: Multiple evidence codes for the same subcellular localization 
        reflect convergent experimental evidence from independent studies.
      supported_by:
        - reference_id: PMID:9564048
          supporting_text: "Dbp5p/Rat8p is located within the cytoplasm and concentrated
            in the perinuclear region."
  - term:
      id: GO:0005934
      label: cellular bud tip
    evidence_type: IDA
    original_reference_id: PMID:19198597
    review:
      summary: DBP5 localizes to the cellular bud tip, possibly involved in 
        directing mRNA and/or translation during mitosis.
      action: KEEP_AS_NON_CORE
      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.
      supported_by:
        - reference_id: PMID:19198597
          supporting_text: Nuclear transport factor directs localization of 
            protein synthesis during mitosis.
  - term:
      id: GO:0006406
      label: mRNA export from nucleus
    evidence_type: IMP
    original_reference_id: PMID:9564048
    review:
      summary: Experimental mutation phenotype shows DBP5 is essential for mRNA 
        export from the nucleus. IMP annotation reflects the loss-of-function 
        phenotype.
      action: ACCEPT
      reason: This is a primary core function confirmed by classical 
        loss-of-function experiments. The IMP annotation appropriately 
        represents the mutant phenotype.
      supported_by:
        - reference_id: PMID:9564048
          supporting_text: "In rat8 mutant strains, cells displayed rapid, synchronous
            accumulation of poly(A)+ RNA in nuclei when shifted to the non-permissive
            temperature."
  - term:
      id: GO:0006415
      label: translational termination
    evidence_type: IGI
    original_reference_id: PMID:17272721
    review:
      summary: DBP5 shows genetic interaction with translation termination 
        factors eRF1 and eRF3, indicating a role in translation termination 
        beyond mRNA export.
      action: KEEP_AS_NON_CORE
      reason: While the genetic interactions are documented, translation 
        termination appears to be a secondary function of DBP5. The primary and 
        essential function is mRNA export. Translation termination interactions 
        may represent pleiotropy or indirect effects.
      supported_by:
        - reference_id: PMID:17272721
          supporting_text: "Dbp5 interacts genetically with both release factors and
            the polyadenlyate-binding protein Pab1."
  - term:
      id: GO:0006415
      label: translational termination
    evidence_type: IPI
    original_reference_id: PMID:17272721
    review:
      summary: DBP5 shows direct physical interaction with eRF1, a translation 
        termination factor. The interaction is specifically detected and 
        characterized.
      action: KEEP_AS_NON_CORE
      reason: While the physical interaction with eRF1 is documented, 
        translation termination remains a secondary function. The protein's 
        essential function is mRNA export, not translation termination.
      supported_by:
        - reference_id: PMID:17272721
          supporting_text: The DEAD-box RNA helicase Dbp5 functions in 
            translation termination.
  - term:
      id: GO:0008186
      label: ATP-dependent activity, acting on RNA
    evidence_type: IDA
    original_reference_id: PMID:19805289
    review:
      summary: DBP5 is directly shown to have ATP-dependent RNA-modifying 
        activity. This reflects the core catalytic function of the helicase.
      action: ACCEPT
      reason: This annotation appropriately characterizes the ATP-dependent 
        catalytic activity of DBP5 acting on RNA. It is both informative and 
        accurate.
      supported_by:
        - reference_id: PMID:19805289
          supporting_text: "Structure of the C-terminus of the mRNA export factor
            Dbp5 reveals the interaction surface for the ATPase activator Gle1."
  - term:
      id: GO:0044614
      label: nuclear pore cytoplasmic filaments
    evidence_type: IDA
    original_reference_id: PMID:10610322
    review:
      summary: DBP5 is experimentally localized to the cytoplasmic filaments of 
        the nuclear pore complex, where it functions in mRNA remodeling.
      action: ACCEPT
      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.
      supported_by:
        - reference_id: PMID:10610322
          supporting_text: "immunoelectron microscopy localizations indicate that
            Gle1p, Rip1p and Rat8p/Dbp5p are present on the NPC cytoplasmic fibrils"
core_functions:
  - molecular_function:
      id: GO:0003724
      label: RNA helicase activity
    directly_involved_in:
      - id: GO:0006406
        label: mRNA export from nucleus
      - id: GO:0016973
        label: poly(A)+ mRNA export from nucleus
    locations:
      - id: GO:0044614
        label: nuclear pore cytoplasmic filaments
    description: DBP5 catalyzes ATP-dependent RNA unwinding (helicase activity) 
      as a core function, operating at the cytoplasmic filaments of the nuclear 
      pore complex where it remodels mRNP complexes to facilitate mRNA export. 
      The protein is a key component of the terminal step of mRNA export, where 
      it removes mRNA-binding proteins and remodels the mRNP to allow passage 
      through the NPC.
    supported_by:
      - reference_id: PMID:9564047
        supporting_text: "Dbp5p is an ATP-dependent RNA helicase required for polyadenylated
          [poly(A)+] RNA export."
      - reference_id: PMID:9564048
        supporting_text: "In rat8 mutant strains, cells displayed rapid, synchronous
          accumulation of poly(A)+ RNA in nuclei when shifted to the non-permissive
          temperature."
      - reference_id: PMID:10610322
        supporting_text: "immunoelectron microscopy localizations indicate that Gle1p,
          Rip1p and Rat8p/Dbp5p are present on the NPC cytoplasmic fibrils"
  - molecular_function:
      id: GO:0000822
      label: inositol hexakisphosphate binding
    directly_involved_in:
      - id: GO:0016973
        label: poly(A)+ mRNA export from nucleus
    locations:
      - id: GO:0044614
        label: nuclear pore cytoplasmic filaments
    in_complex:
      id: GO:0005643
      label: nuclear pore
    description: 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.
    supported_by:
      - reference_id: PMID:16783363
        supporting_text: "We now propose that Dbp5 activation at NPCs requires Gle1
          and InsP6."
      - reference_id: PMID:21441902
        supporting_text: "A conserved mechanism of DEAD-box ATPase activation by nucleoporins
          and InsP6 in mRNA export."
references:
  - id: GO_REF:0000002
    title: Gene Ontology annotation through association of InterPro records with
      GO terms
    findings: []
  - id: GO_REF:0000033
    title: Annotation inferences using phylogenetic trees
    findings: []
  - id: GO_REF:0000043
    title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword 
      mapping
    findings: []
  - id: GO_REF:0000044
    title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular 
      Location vocabulary mapping, accompanied by conservative changes to GO 
      terms applied by UniProt
    findings: []
  - id: GO_REF:0000116
    title: Automatic Gene Ontology annotation based on Rhea mapping
    findings: []
  - id: GO_REF:0000117
    title: Electronic Gene Ontology annotations created by ARBA machine learning
      models
    findings: []
  - id: GO_REF:0000120
    title: Combined Automated Annotation using Multiple IEA Methods
    findings: []
  - id: PMID:10610322
    title: The RNA export factor Gle1p is located on the cytoplasmic fibrils of 
      the NPC and physically interacts with the FG-nucleoporin Rip1p, the 
      DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p.
    findings: []
  - id: PMID:15280434
    title: 'Stress response in yeast mRNA export factor: reversible changes in Rat8p
      localization are caused by ethanol stress but not heat shock.'
    findings: []
  - id: PMID:15619606
    title: Physical and genetic interactions link the yeast protein Zds1p with 
      mRNA nuclear export.
    findings: []
  - id: PMID:16554755
    title: Global landscape of protein complexes in the yeast Saccharomyces 
      cerevisiae.
    findings: []
  - id: PMID:16783363
    title: Inositol hexakisphosphate and Gle1 activate the DEAD-box protein Dbp5
      for nuclear mRNA export.
    findings: []
  - id: PMID:17272721
    title: The DEAD-box RNA helicase Dbp5 functions in translation termination.
    findings: []
  - id: PMID:19198597
    title: Nuclear transport factor directs localization of protein synthesis 
      during mitosis.
    findings: []
  - id: PMID:19805289
    title: Structure of the C-terminus of the mRNA export factor Dbp5 reveals 
      the interaction surface for the ATPase activator Gle1.
    findings: []
  - id: PMID:21441902
    title: A conserved mechanism of DEAD-box ATPase activation by nucleoporins 
      and InsP6 in mRNA export.
    findings: []
  - id: PMID:27251550
    title: Defects in THO/TREX-2 function cause accumulation of novel 
      cytoplasmic mRNP granules that can be cleared by autophagy.
    findings: []
  - id: PMID:27385342
    title: Altered RNA processing and export lead to retention of mRNAs near 
      transcription sites and nuclear pore complexes or within the nucleolus.
    findings: []
  - id: PMID:31453808
    title: A nuclear role for the DEAD-box protein Dbp5 in tRNA export.
    findings: []
  - id: PMID:9564047
    title: Dbp5p, a cytosolic RNA helicase, is required for poly(A)+ RNA export.
    findings: []
  - id: PMID:9564048
    title: Dbp5p/Rat8p is a yeast nuclear pore-associated DEAD-box protein 
      essential for RNA export.
    findings: []