DOCK2 is a RAC-directed guanine-nucleotide exchange factor enriched in hematopoietic cells. Its DHR2 catalytic region promotes nucleotide exchange, while interactions with ELMO proteins and membrane-associated signaling components regulate substrate access and cellular recruitment. DOCK2 links chemokine and antigen-receptor signals to actin remodeling, immune-cell migration and antigen uptake. Biallelic loss of function causes combined immunodeficiency with impaired cellular responses. Alternative transcripts encode a long catalytic product and a much shorter product whose biological activity remains unresolved.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0002277 myeloid dendritic cell activation involved in immune response | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse DOCK2 supports dendritic-cell antigen uptake and the associated immune-cell response. Reason: The literal donor is mouse Dock2 Q8C3J5. PMID:21892172 directly compares wild-type and Dock2-null bone-marrow-derived dendritic cells: uptake of soluble antigen and particles is reduced, and ectopic DOCK2 restores uptake in the low-Dock2 ASC-null background. These are positive functional observations, retained as a cell-type-specific role. The later addendum PMID:22905357 shows that low Dock2 expression occurs in only some ASC-null lines and leaves its cause unresolved; it limits the general ASC-to-Dock2 claim but explicitly retains the Dock2 loss/rescue observations. This ortholog annotation is not evidence that the experiments used human cells. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q8C3J5 SUPPORTS TRANSFER Current donor GOA retains the experimentally based dendritic-cell assertion; the original and its addendum were read separately. Context is mouse antigen uptake, not universal ASC regulation. ensembl:ENSMUSP00000090884 SUPPORTS TRANSFER Current donor GOA retains the experimentally based dendritic-cell assertion; the original and its addendum were read separately. Context is mouse antigen uptake, not universal ASC regulation. Supporting Evidence: PMID:21892172 Dock2-deficient DCs showed defective antigen uptake |
| GO:0002277 myeloid dendritic cell activation involved in immune response | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Mouse DOCK2 supports dendritic-cell antigen uptake and the associated immune-cell response. Reason: The literal donor is mouse Dock2 Q8C3J5. PMID:21892172 directly compares wild-type and Dock2-null bone-marrow-derived dendritic cells: uptake of soluble antigen and particles is reduced, and ectopic DOCK2 restores uptake in the low-Dock2 ASC-null background. These are positive functional observations, retained as a cell-type-specific role. The later addendum PMID:22905357 shows that low Dock2 expression occurs in only some ASC-null lines and leaves its cause unresolved; it limits the general ASC-to-Dock2 claim but explicitly retains the Dock2 loss/rescue observations. This ortholog annotation is not evidence that the experiments used human cells. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q8C3J5 SUPPORTS TRANSFER Current donor GOA retains the experimentally based dendritic-cell assertion; the original and its addendum were read separately. Context is mouse antigen uptake, not universal ASC regulation. |
| GO:0005085 guanyl-nucleotide exchange factor activity | IBA GO_REF:0000033 | ACCEPT | Summary: DOCK2 retains the ancestral guanine-nucleotide exchange activity. Reason: The PANTHER target leaf PTN002511203 descends from the exact IBD node PTN002902098. The literal IBD for GO:0005085 has experimental descendant support, including DOCK2 itself. Direct human DOCK2–ELMO1 exchange measurements independently corroborate the inherited activity. Target self-inclusion is legitimate experimental grounding, not circular evidence. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002902098 SUPPORTS TRANSFER The current family topology and exact GO:0005085 IBD were joined; target descent is verified. No target-specific catalytic loss is established. Supporting Evidence: |
| GO:0005085 guanyl-nucleotide exchange factor activity | IDA PMID:10559471 Non-adherent cell-specific expression of DOCK2, a member of ... | ACCEPT | Summary: The original human DOCK2 study reports Rac1 binding and activation. Reason: The complete cached abstract identifies human DOCK2/KIAA0209 and reports its Rac1-binding/activation result. The full Methods were not recovered, so no particular construct, purified reaction or splice product is assigned to this 1999 experiment. The curator-backed activity agrees with independently measured human DOCK2 nucleotide exchange in PMID:32651375. |
| GO:0005085 guanyl-nucleotide exchange factor activity | IDA PMID:32651375 Structure of the DOCK2-ELMO1 complex provides insights into ... | ACCEPT | Summary: Purified human DOCK2–ELMO1 directly promotes nucleotide exchange on RAC1. Reason: The original Methods specify human coding constructs expressed in High Five cells and a fluorescent nucleotide-release assay. ELMO1 deletion effects differ between the purified and cellular assays, but the measured molecular activity is exchange. The experiment does not establish equivalent activity of the 336-residue natural product. Supporting Evidence: |
| GO:0005085 guanyl-nucleotide exchange factor activity | IEA GO_REF:0000002 | ACCEPT | Summary: The DOCK-family and DHR2 mappings correctly identify nucleotide-exchange activity. Reason: IPR026791 and IPR026799 identify the DOCK family and its catalytic DHR2 region. Their exchange-function interpretation is independently established by direct human protein assays and a human catalytic-domain deposition. Domain-based support is not evidence that every alternative product retains the full catalytic module. Propagation Review Root cause: NO FAILURE CORE Sources checked: InterPro:IPR026791 SUPPORTS TRANSFER The exact current InterPro entries and GO mapping were read; their DHR2 GEF role matches direct human evidence. InterPro:IPR026799 SUPPORTS TRANSFER The exact current InterPro entries and GO mapping were read; their DHR2 GEF role matches direct human evidence. |
| GO:0005085 guanyl-nucleotide exchange factor activity | TAS Reactome:R-HSA-9014296 | ACCEPT | Summary: Reactome explicitly includes DOCK2 as a member of its RAC2 exchange-factor CandidateSet. Reason: The exact path is reaction 9014296, catalyst activity 9014402, CandidateSet 9014398, and its hasMember entity 200938, whose reference entity is human Q92608 residues 1–1830. The explicit hasMember relationship distinguishes this target from hasCandidate entries, but membership in this curated set does not itself constitute a direct DOCK2–RAC2 assay. The independent human T-cell-receptor study reports DOCK2-associated RAC2 activation. |
| GO:0005096 GTPase activator activity | IEA GO_REF:0000120 | REMOVE | Summary: The electronic GTPase-activator assignment conflates nucleotide exchange with GTP hydrolysis. Reason: Current GO:0005096 specifically increases the hydrolysis rate of a bound GTPase. Human DOCK2 instead catalyzes nucleotide exchange through DHR2. The exact IPR026799 record maps the domain to both GO:0005085 and GO:0005096 despite describing exchange; the mouse source also carries GO:0005096, while its PMID:12871644 abstract describes Rac activation and synapse phenotypes rather than a hydrolysis assay. The demonstrably inappropriate electronic activity is removed; valid exchange rows remain. This does not claim that the inaccessible mouse full text assayed a different gene. Propagation Review Root cause: SOURCE BAD Failure modes: ROLE CONFLATION Sources checked: UniProtKB:Q8C3J5 SOURCE BAD The imported combined inference reaches a GAP/hydrolysis term, whereas the target DHR2 mechanism is GEF-mediated exchange. The InterPro mapping itself includes the incompatible term; no experimental target hydrolysis is established. ensembl:ENSMUSP00000090884 SOURCE BAD The imported combined inference reaches a GAP/hydrolysis term, whereas the target DHR2 mechanism is GEF-mediated exchange. The InterPro mapping itself includes the incompatible term; no experimental target hydrolysis is established. InterPro:IPR026799 SOURCE BAD The imported combined inference reaches a GAP/hydrolysis term, whereas the target DHR2 mechanism is GEF-mediated exchange. The InterPro mapping itself includes the incompatible term; no experimental target hydrolysis is established. |
| GO:0005515 protein binding | IPI PMID:12134158 Unconventional Rac-GEF activity is mediated through the Dock... | MODIFY | Summary: The verified RAC1 interaction supports small GTPase binding. Reason: The exact MINT record retains DOCK2–RAC1 pull-down evidence and annotates a DOCK2 binding-associated region 1115–1680 with a COS-7 host. The canonical parent checksum does not make this a full-length reagent. The narrower small-GTPase-binding claim is supported by this literal pair and independent direct human DOCK2/RAC1 catalytic-complex evidence. The paper title foregrounding DOCK180 is not a misattribution. Proposed replacements: small GTPase binding |
| GO:0005515 protein binding | IPI PMID:15723800 A Steric-inhibition model for regulation of nucleotide excha... | MODIFY | Summary: The verified RAC1 interaction supports small GTPase binding. Reason: Two exact MINT records retain DOCK2–RAC1 pull-down evidence at Figure 2b. Their curator note explicitly says DOCK2 construct taxon was not specified; HEK293T is a host, not proof of human reagent origin. Independent direct human DOCK2/RAC1 evidence establishes the narrower target-level small-GTPase-binding activity. No inaccessible full-text detail or all-product equivalence is inferred. Proposed replacements: small GTPase binding |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: The verified PLSCR1 pair supports enzyme binding. Reason: The HI-II-14 records identify a positive DOCK2–PLSCR1 binary pair, including validated two-hybrid confirmation and matching reference-sequence checksums. PLSCR1 has experimentally supported catalytic functions, including nuclease activity, in its official record, meeting the enzyme class in GO:0019899. This supports enzyme binding without assigning PLSCR1 catalysis to DOCK2. The three records are related screening observations; native coexpression, stoichiometry and a physiological role for this pair remain unestablished. Proposed replacements: enzyme binding |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The positive O95273 binary association is retained outside the core. Reason: The exact HI-II-14 pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. CCNDBP1 is a cell-cycle regulator; inhibition of a cyclin/CDK complex does not make it a kinase or establish a transcription-machinery cofactor class for this pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The positive P26371 binary association is retained outside the core. Reason: The exact HI-II-14 pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: The verified TRIM23 pair supports ubiquitin protein ligase binding. Reason: The HI-II-14 records identify a positive DOCK2–TRIM23 binary pair, including validated two-hybrid confirmation and matching reference-sequence checksums. TRIM23 is an experimentally supported E3 ubiquitin ligase, meeting the partner class in GO:0031625. The refinement describes binding to that enzyme, not ubiquitination or ligase regulation by DOCK2. The related screening records do not establish native stoichiometry or a physiological pathway for this pair. Proposed replacements: ubiquitin protein ligase binding |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The positive P60410 binary association is retained outside the core. Reason: The exact HI-II-14 pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The positive P60411 binary association is retained outside the core. Reason: The exact HI-II-14 pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The positive P61978 binary association is retained outside the core. Reason: The exact HI-II-14 pair has 6 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. HNRNPK is an RNA-binding and context-dependent transcriptional regulator. This binary assay does not establish its sumoylated coactivator state or a transcriptional mechanism involving DOCK2. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The positive Q13137 binary association is retained outside the core. Reason: The exact HI-II-14 pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. CALCOCO2 is principally a xenophagy receptor; its reported possible actin/ruffle role does not establish a defined cytoskeletal-regulator recognition event here. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: The verified MTUS2 pair supports cytoskeletal regulatory protein binding. Reason: The HI-II-14 records identify a positive binary pair with sequence-matched 1369-residue MTUS2, including validated two-hybrid confirmation. This product retains the experimentally mapped MAPRE1/KIF2C interaction regions associated with microtubule regulation, supporting the cytoskeletal-regulatory partner class in GO:0005519. No microtubule-regulatory mechanism is assigned to DOCK2 through this pair. The distinct short HuRI product lacks those regions and is assessed separately; native coexpression and stoichiometry remain unestablished. Proposed replacements: cytoskeletal regulatory protein binding |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The positive Q5VWX1 binary association is retained outside the core. Reason: The exact HI-II-14 pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. KHDRBS2 is an RNA-binding/splicing regulator. Binding this protein does not establish RNA binding or splicing activity by DOCK2. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: The verified KRT40 pair supports cytoskeletal protein binding. Reason: HI-II-14 identifies a positive DOCK2–KRT40 binary pair, including validated two-hybrid confirmation and matching reference-sequence checksums. KRT40 is a keratin component of the intermediate-filament cytoskeleton; GO:0008092 describes binding to a cytoskeletal protein, supporting this narrower partner-class term. This does not assert binding to actin or to an assembled filament. Hair-associated expression limits physiological interpretation but does not negate the measured binary interaction; native DOCK2–KRT40 contact is not established. Proposed replacements: cytoskeletal protein binding |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The positive Q7Z3S9 binary association is retained outside the core. Reason: The exact HI-II-14 pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. NOTCH2NLA is a Notch-pathway modulator; the interaction does not establish DOCK2 as a Notch receptor ligand or a transcription factor. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The positive Q99750 binary association is retained outside the core. Reason: The exact HI-II-14 pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. MDFI can regulate transcription factors through cytoplasmic retention and other interactions. That does not establish the basal-transcription-machinery bridging role required by the checked transcription-coregulator-binding definition. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The positive Q9BYQ2 binary association is retained outside the core. Reason: The exact HI-II-14 pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The positive Q9BYQ4 binary association is retained outside the core. Reason: The exact HI-II-14 pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The positive Q9BYR5 binary association is retained outside the core. Reason: The exact HI-II-14 pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive A6NEM1 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. The GOLGA6L9 record separately annotates sufficient binding region 159–432. Its full parent sequence checksum does not establish a full-length reagent, and no specific catalytic or scaffold partner class was established. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive A8MQ03 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. CYSRT1 is a cornified-envelope protein with a proposed antimicrobial role; no more specific binding class was established. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive O75525 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. KHDRBS3 is an RNA-binding/splicing regulator. Binding this protein does not establish RNA binding or splicing activity by DOCK2. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The verified KRT34 pair supports cytoskeletal protein binding. Reason: HuRI identifies a positive DOCK2–KRT34 binary pair, including validated two-hybrid confirmation and matching reference-sequence checksums. KRT34 is a keratin component of the intermediate-filament cytoskeleton; GO:0008092 describes binding to a cytoskeletal protein, supporting this narrower partner-class term. This does not assert binding to actin or to an assembled filament. Hair-follicle expression limits physiological interpretation but does not negate the measured binary interaction; native DOCK2–KRT34 contact is not established. Proposed replacements: cytoskeletal protein binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive P0DPK4 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. NOTCH2NLC is a Notch-pathway modulator; the interaction does not establish DOCK2 as a Notch receptor ligand or a transcription factor. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The verified TGM1 pair supports enzyme binding. Reason: The HuRI records identify a positive DOCK2–TGM1 binary pair, including validated two-hybrid confirmation and matching reference-sequence checksums. TGM1 has experimentally supported transglutaminase activity, meeting the enzyme class in GO:0019899. This supports enzyme binding without assigning transglutaminase activity or skin-protein cross-linking to DOCK2. The related screening records do not establish native coexpression, stoichiometry or a cellular mechanism for this pair. Proposed replacements: enzyme binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive P26371 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The verified HOXA1 pair supports DNA-binding transcription factor binding. Reason: The HuRI records identify a positive DOCK2–HOXA1 binary pair, including validated two-hybrid confirmation and matching reference-sequence checksums. The official HOXA1 record establishes its sequence-specific DNA-binding transcription-factor class, matching GO:0140297. Binding this partner does not assign DNA binding or transcriptional regulation to DOCK2. Native coexpression, stoichiometry and a physiological role for the pair remain unestablished. Proposed replacements: DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive P60328 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: PMID:32296183 pairwise verification by quadruplicate retesting and sequence confirmation |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive P60409 binary association is retained outside the core. Reason: The exact HuRI pair has 5 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive P60410 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive P61978-2 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. The literal partner is sequence-matched HNRNPK isoform P61978-2. Its RNA-binding and context-dependent coactivator functions do not establish a specific regulatory state or mechanism in this assay. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive Q07627 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The verified KRT31 pair supports cytoskeletal protein binding. Reason: HuRI identifies a positive DOCK2–KRT31 binary pair, including validated two-hybrid confirmation and matching reference-sequence checksums. KRT31 is a keratin component of the intermediate-filament cytoskeleton; GO:0008092 describes binding to a cytoskeletal protein, supporting this narrower partner-class term. This does not assert binding to actin or to an assembled filament. Hair-cortex expression limits physiological interpretation but does not negate the measured binary interaction; native DOCK2–KRT31 contact is not established. Proposed replacements: cytoskeletal protein binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive Q5JR59-3 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. The literal 348-residue MTUS2 product Q5JR59-3 is sequence-verified. It deletes canonical residues 1–1021, including the mapped MAPRE1- and KIF2C-interaction regions. The full-length microtubule-regulatory class is not automatically assigned to this truncated product; this is not a claim that the product is biologically inactive. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive Q5VWX1 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. KHDRBS2 is an RNA-binding/splicing regulator. Binding this protein does not establish RNA binding or splicing activity by DOCK2. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The verified KRT40 pair supports cytoskeletal protein binding. Reason: HuRI identifies a positive DOCK2–KRT40 binary pair, including validated two-hybrid confirmation and matching reference-sequence checksums. KRT40 is a keratin component of the intermediate-filament cytoskeleton; GO:0008092 describes binding to a cytoskeletal protein, supporting this narrower partner-class term. This does not assert binding to actin or to an assembled filament. Hair-associated expression limits physiological interpretation but does not negate the measured binary interaction; native DOCK2–KRT40 contact is not established. Proposed replacements: cytoskeletal protein binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive Q6L8G8 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive Q6N022 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. The TENM4 record separately annotates sufficient binding region 663–2769. The parent checksum does not convert that fragment into a full-length receptor assay, and the pair does not define a DOCK2 signaling activity. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive Q8IUG1 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The verified PCSK5 pair supports protease binding. Reason: The HuRI records identify a positive DOCK2–PCSK5 binary pair, including validated two-hybrid confirmation and a checksum matching the literal 913-residue Q92824-2 product. This natural product retains the peptidase S8 domain and catalytic residues, supporting the protease-class partner required by GO:0002020. It is not an engineered catalytically inactive bait. Binding does not establish proteolytic maturation or activity during the assay, native secretory-pathway contact, or protease activity by DOCK2. Proposed replacements: protease binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive Q99750 binary association is retained outside the core. Reason: The exact HuRI pair has 5 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. MDFI can regulate transcription factors through cytoplasmic retention and other interactions. That does not establish the basal-transcription-machinery bridging role required by the checked transcription-coregulator-binding definition. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The verified CARD10 pair supports scaffold protein binding. Reason: The HuRI records identify a positive DOCK2–CARD10 binary pair, including validated two-hybrid confirmation and matching reference-sequence checksums. The official CARD10 record establishes its BCL10/EGFR-associated signaling-scaffold role, meeting the partner class in GO:0097110. Binding that scaffold does not assign scaffold activity or NF-kappa-B regulation to DOCK2. Native coexpression, stoichiometry and a physiological pathway for this pair remain unestablished. Proposed replacements: scaffold protein binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive Q9BYP8 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive Q9BYQ3 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive Q9BYR6 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive Q9BYR8 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. This keratin-associated protein forms part of the hair matrix around keratin filaments. It is not thereby an assembled intermediate filament or an independently established cytoskeletal regulator; those narrower binding terms would overstate the measured pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive Q9H8W4 binary association is retained outside the core. Reason: The exact HuRI pair has 3 curated positive two-hybrid records; their methods, partner identifiers and reference-sequence checksums were verified. Repeated records are not counted as independent physiological validations. These assays support a binary association but do not establish native stoichiometry, coexpression or a cellular mechanism. PLEKHF2 has a suggested endosomal-trafficking role, but the binding assay does not define a particular enzyme, scaffold or adaptor function for this pair. The project-specific positive-binding policy preserves the generic assertion when a justified narrower activity is not established. Supporting Evidence: |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-6798749 | UNDECIDED | Summary: The source-specific extracellular localization remains unresolved. Reason: The exact Reactome event output 6806312 has member 6806310, human Q92608 residues 1–1830 assigned to extracellular region. This verifies the curated model participant, but the primary DOCK2 fractionation/peptide row supporting the granule-exocytosis model was not recovered. The specific extracellular assertion therefore remains unresolved, rather than being accepted from set membership alone. Neither absent signal-peptide annotation nor DOCK2’s cytosolic function establishes contamination or disproves unconventional release. The original source assertion is preserved. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | MODIFY | Summary: The broad inherited cytoplasmic pool can be resolved to cytosol for DOCK2. Reason: The target descends from the exact cytoplasm IBD PTN002902098. Target-resolved Reactome member 200938 independently places full-length human DOCK2 in cytosol within its RAC2 exchange-factor role. Refine this broad source to that supported pool without claiming the ancestral assertion measured human cytosol or excluding membrane-associated pools. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN002902098 SUPPORTS TRANSFER Exact target descent and cytoplasm IBD are valid. The target-specific cytosol refinement comes from the checked human Reactome entity, not from greater resolution in the ancestral assertion. Proposed replacements: cytosol Supporting Evidence: Reactome:R-HSA-9014296 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-200952 | ACCEPT | Summary: The exact human DOCK2 entity supports the cytosolic functional pool. Reason: Reactome 200952 reaches input 200938 and output complex 200937, with human Q92608 residues 1–1830 and compartment GO:0005829. This verifies target membership rather than transferring a reaction-wide location. The Nef or RHOG context of individual reactions does not make the shared cytosolic location false or exclusive. Supporting Evidence: Reactome:R-HSA-200952 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9014296 | ACCEPT | Summary: The exact human DOCK2 entity supports the cytosolic functional pool. Reason: Reactome 9014296 reaches catalyst 9014402 → set 9014398 → member 200938, with human Q92608 residues 1–1830 and compartment GO:0005829. This verifies target membership rather than transferring a reaction-wide location. The Nef or RHOG context of individual reactions does not make the shared cytosolic location false or exclusive. Supporting Evidence: Reactome:R-HSA-9014296 |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9014449 | ACCEPT | Summary: The exact human DOCK2 entity supports the cytosolic functional pool. Reason: Reactome 9014449 reaches input set 9014451 → member 200938, with human Q92608 residues 1–1830 and compartment GO:0005829. This verifies target membership rather than transferring a reaction-wide location. The Nef or RHOG context of individual reactions does not make the shared cytosolic location false or exclusive. Supporting Evidence: Reactome:R-HSA-9014449 |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Human Jurkat colocalization supports a contextual cytoskeletal pool. Reason: The official subcellular-location mapping SL-0090 is backed by PMID:12393632, whose complete abstract explicitly reports DOCK2 colocalization with F-actin and CrkL in Jurkat cells. Retain this positive localization as contextual; colocalization does not demonstrate direct actin binding or structural incorporation into the cytoskeleton. Full target-specific Methods were not recovered. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB-SubCell:SL-0090 SUPPORTS TRANSFER The literal UniProt subcellular-location term and its original citation were traced; the human colocalization statement is explicit. Supporting Evidence: PMID:12393632 Colocalization of DOCK2 with Crk-like (CrkL) and F-actin |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The ancestral membrane-associated pool is retained alongside cytosolic function. Reason: DOCK2 descends from the exact plasma-membrane IBD PTN002902098, with experimental descendant grounding and no demonstrated target-specific loss. Retain this regulated membrane pool without treating the broad family assertion as a human imaging experiment or as exclusive localization. The core describes the independently target-resolved cytosolic exchange-factor pool. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002902098 SUPPORTS TRANSFER Exact plasma-membrane IBD and target descent are verified; a valid ancestral placement is not challenged solely because direct human imaging was not recovered. |
| GO:0007264 small GTPase-mediated signal transduction | IEA GO_REF:0000002 | MODIFY | Summary: DOCK2 performs the RAC-activation step within small-GTPase signaling. Reason: The InterPro mappings identify the correct signaling mechanism but are broad. Direct human DOCK2 nucleotide-exchange assays and receptor-triggered RAC1 defects support positive regulation of Rac protein signal transduction. This is a biologically specific regulatory-role refinement; the checked ontology traversal includes regulatory relations and is not claimed to be an is_a-only path. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: InterPro:IPR026791 SUPPORTS TRANSFER Both actual InterPro entries support a DOCK-family GEF signaling role. Human RAC specificity supports the narrower regulatory process. InterPro:IPR026799 SUPPORTS TRANSFER Both actual InterPro entries support a DOCK-family GEF signaling role. Human RAC specificity supports the narrower regulatory process. Proposed replacements: positive regulation of Rac protein signal transduction |
| GO:0007520 myoblast fusion | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The phylogenetically inherited myoblast-fusion role is retained contextually. Reason: The exact myoblast-fusion IBD PTN000594048 lies on the target lineage. Its experimental descendant grounding includes zebrafish dock1/dock5 and fly myoblast city, with corresponding current experimental GO records. No target-specific loss or incorrect node placement was established. Retain the curator judgment as a contextual inherited process, while not claiming a direct human DOCK2 myoblast-fusion assay or making muscle fusion the defining immune-cell function. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000594048 SUPPORTS TRANSFER The actual IBD, target descent and experimental donor records are verified. Current and seeded donor-list differences are preserved as snapshot differences, not rewritten or treated as loss. |
| GO:0012505 endomembrane system | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: The curated peripheral endomembrane pool is retained without greater compartment precision. Reason: The exact SL-0147 mapping follows the official UniProt endomembrane/peripheral-membrane annotation with PMID:12393632. The accessible original abstract verifies Jurkat F-actin/CrkL colocalization but does not resolve an individual endomembrane organelle. Retain the curated broad pool; do not infer ER lumen, secretion or a transmembrane topology. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB-SubCell:SL-0147 SUPPORTS TRANSFER The source subcellular-location record is present and traced. No more specific endomembrane compartment was established from the accessible source. Supporting Evidence: |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | KEEP AS NON CORE | Summary: The membrane-proteome detection is compatible with DOCK2 membrane association. Reason: PMID:19946888 surveys a membrane-enriched fraction of the human YTS NK-like cell line and explicitly notes that many detected proteins associate transiently with membranes. The target-specific supplementary row was not recovered. Retain the curator-backed broad membrane association, independently consistent with the official peripheral-membrane annotation and inherited membrane pool; do not claim an integral-membrane protein or identify a particular organelle from this screen. |
| GO:0016477 cell migration | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The conserved migration role is supported in human immune cells. Reason: The target descends from the cell-migration IBD PTN000594048. Mouse Dock1 and other experimental descendants ground that placement, while human DOCK2 deficiency independently impairs chemokine-directed T/B-cell migration. Retain the broad migration process as a cellular role downstream of the defining RAC-exchange activity; it does not imply identical migration behavior in every tissue. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000594048 SUPPORTS TRANSFER Actual node placement and current experimental donor records are verified, with independent human immune-cell evidence. No donor-count or self-circularity argument is used. Supporting Evidence: |
| GO:0030036 actin cytoskeleton organization | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: DOCK2-dependent RAC signaling organizes the actin cytoskeleton. Reason: The human T-cell receptor study reports RAC2 activation and the downstream cytoskeletal signaling context, and human DOCK2 deficiency impairs chemokine-triggered actin polymerization. This supports the cellular organization role through RAC activation; it is not evidence that DOCK2 directly nucleates or binds actin. The process is retained outside the narrowly defined exchange-factor core. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: InterPro:IPR026799 SUPPORTS TRANSFER The DHR2-domain mapping is consistent with the target’s experimentally supported RAC-to-actin signaling role. |
| GO:0030036 actin cytoskeleton organization | TAS PMID:12176041 DOCK2 mediates T cell receptor-induced activation of Rac2 an... | KEEP AS NON CORE | Summary: DOCK2-dependent RAC signaling organizes the actin cytoskeleton. Reason: The human T-cell receptor study reports RAC2 activation and the downstream cytoskeletal signaling context, and human DOCK2 deficiency impairs chemokine-triggered actin polymerization. This supports the cellular organization role through RAC activation; it is not evidence that DOCK2 directly nucleates or binds actin. The process is retained outside the narrowly defined exchange-factor core. |
| GO:0031267 small GTPase binding | IBA GO_REF:0000033 | ACCEPT | Summary: The inherited small-GTPase interaction is integral to nucleotide exchange. Reason: The exact IBD PTN002902098 for small GTPase binding is grounded in experimental DOCK-family evidence, including human DOCK4 Q8N1I0 with PMID:16464467. Target descent is verified, and independent human DOCK2/RAC1 complex and exchange assays corroborate the target activity. A single named experimental descendant is not weak or circular support. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002902098 SUPPORTS TRANSFER The actual GO:0031267 IBD, target lineage and current donor IDA record were joined; direct target complex evidence is independent corroboration. Supporting Evidence: |
| GO:0035580 specific granule lumen | TAS Reactome:R-HSA-6798749 | UNDECIDED | Summary: The source-specific granule-lumen localization remains unresolved. Reason: Reactome reaction input set 6799354 has member 6799558, human Q92608 residues 1–1830 assigned to specific granule lumen. The primary neutrophil survey abstract reports fractionation and mass spectrometry, but the DOCK2 measurement and evidence distinguishing lumen residence from surface association or co-fractionation were not recovered. The specific location is unresolved; model membership verifies the source claim without independently establishing topology. No contamination or biological impossibility is inferred from the lack of a conventional signal peptide. |
| GO:0042608 T cell receptor binding | IDA PMID:12176041 DOCK2 mediates T cell receptor-induced activation of Rac2 an... | KEEP AS NON CORE | Summary: DOCK2 association with the T-cell receptor complex is a contextual interaction. Reason: The complete PMID:12176041 abstract explicitly reports association with CD3zeta in human Jurkat cells, alongside RAC2 signaling. Retain the curator-backed receptor-complex binding claim without asserting a purified direct interface or equating receptor association with a second catalytic core. The inaccessible full Methods are not reconstructed from the abstract. Supporting Evidence: PMID:12176041 zeta subunit of the CD3 complex of T cell receptors in Jurkat cells |
| GO:0044351 macropinocytosis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse Dock2 loss and rescue support macropinocytosis. Reason: The literal mouse Q8C3J5 donor carries the experimental PMID:21892172 assertion. Its recovered original Figure 6 and Methods directly measure reduced uptake of soluble dextran, ovalbumin and Lucifer Yellow in Dock2-null bone-marrow-derived dendritic cells. This is positive process evidence, retained as a contextual immune-cell role. The addendum PMID:22905357 limits the proposed upstream ASC link to some mouse lines but explicitly preserves the DOCK2 loss/rescue findings. No direct human assay or universal ASC control is inferred. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q8C3J5 SUPPORTS TRANSFER The exact current mouse experimental source and original endpoints were checked. The correction limits the upstream ASC interpretation, not the observed Dock2-dependent uptake. ensembl:ENSMUSP00000090884 SUPPORTS TRANSFER The exact current mouse experimental source and original endpoints were checked. The correction limits the upstream ASC interpretation, not the observed Dock2-dependent uptake. |
| GO:0044351 macropinocytosis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Mouse Dock2 loss and rescue support macropinocytosis. Reason: The literal mouse Q8C3J5 donor carries the experimental PMID:21892172 assertion. Its recovered original Figure 6 and Methods directly measure reduced uptake of soluble dextran, ovalbumin and Lucifer Yellow in Dock2-null bone-marrow-derived dendritic cells. This is positive process evidence, retained as a contextual immune-cell role. The addendum PMID:22905357 limits the proposed upstream ASC link to some mouse lines but explicitly preserves the DOCK2 loss/rescue findings. No direct human assay or universal ASC control is inferred. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q8C3J5 SUPPORTS TRANSFER The exact current mouse experimental source and original endpoints were checked. The correction limits the upstream ASC interpretation, not the observed Dock2-dependent uptake. |
| GO:0050766 positive regulation of phagocytosis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse Dock2 loss and rescue support positive regulation of phagocytosis. Reason: The literal mouse Q8C3J5 donor carries the experimental PMID:21892172 assertion. Its recovered original Figure 6 and Methods directly measure reduced internalization of zymosan and polystyrene beads in Dock2-null bone-marrow-derived dendritic cells. This is positive process evidence, retained as a contextual immune-cell role. The addendum PMID:22905357 limits the proposed upstream ASC link to some mouse lines but explicitly preserves the DOCK2 loss/rescue findings. No direct human assay or universal ASC control is inferred. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q8C3J5 SUPPORTS TRANSFER The exact current mouse experimental source and original endpoints were checked. The correction limits the upstream ASC interpretation, not the observed Dock2-dependent uptake. ensembl:ENSMUSP00000090884 SUPPORTS TRANSFER The exact current mouse experimental source and original endpoints were checked. The correction limits the upstream ASC interpretation, not the observed Dock2-dependent uptake. |
| GO:0050766 positive regulation of phagocytosis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Mouse Dock2 loss and rescue support positive regulation of phagocytosis. Reason: The literal mouse Q8C3J5 donor carries the experimental PMID:21892172 assertion. Its recovered original Figure 6 and Methods directly measure reduced internalization of zymosan and polystyrene beads in Dock2-null bone-marrow-derived dendritic cells. This is positive process evidence, retained as a contextual immune-cell role. The addendum PMID:22905357 limits the proposed upstream ASC link to some mouse lines but explicitly preserves the DOCK2 loss/rescue findings. No direct human assay or universal ASC control is inferred. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q8C3J5 SUPPORTS TRANSFER The exact current mouse experimental source and original endpoints were checked. The correction limits the upstream ASC interpretation, not the observed Dock2-dependent uptake. |
| GO:0051056 regulation of small GTPase mediated signal transduction | TAS Reactome:R-HSA-9012999 | MODIFY | Summary: The broad RHO-cycle annotation can be resolved to positive RAC regulation. Reason: Reactome pathway 9012999 includes the RAC2 cycle 9013404 and reaction 9014296, whose catalytic member is human DOCK2. Direct exchange assays identify the positive activation step. Refine the broad regulation term to positive regulation of Rac protein signal transduction, preserving the same mechanistic role without adding a redundant NEW process. Proposed replacements: positive regulation of Rac protein signal transduction |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | UNDECIDED | Summary: The source-specific exosome detection could not be independently verified. Reason: The complete abstract describes highly purified B-cell exosomes and a 539-protein survey, but it does not identify DOCK2 or its measurement row. Publisher and supplementary recovery attempts returned access/error pages rather than the original target table. This limitation does not contradict the curator’s detection or establish contamination; retain the source assertion with an unresolved verdict rather than remove it from intracellular-function assumptions. Supporting Evidence: |
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