SYK is a cytoplasmic non-receptor protein tyrosine kinase with tandem SH2 domains that recognize phosphorylated immune-receptor signaling motifs. Receptor recruitment and autophosphorylation activate SYK, which phosphorylates adaptor and enzyme substrates and also supplies docking interfaces for sustained signaling complexes. It is central to B-cell antigen-receptor, Fc-receptor, C-type lectin and integrin-linked signaling. Context-dependent roles extend to myeloid cytokine responses, platelet activation, receptor trafficking, microglial lipid responses and epithelial signaling. SYK can also phosphorylate Ikaros on serine residues in a defined regulatory context. Its effects on cytokines, adhesion and cell survival depend on receptor, cell type and stimulation, rather than having one universal sign.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001775 cell activation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse donor PMID:19136564 tests Dectin-1-dependent dendritic-cell activation and its signaling effectors. Reason: The mouse donor PMID:19136564 tests Dectin-1-dependent dendritic-cell activation and its signaling effectors. Human Dectin-1/SYK inhibition in PMID:19358895 independently supports activation in immune cells. Cell activation is as broad as these multiple cellular outputs warrant, and is retained as contextual biology rather than made the defining molecular function. |
| GO:0001775 cell activation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The mouse donor PMID:19136564 tests Dectin-1-dependent dendritic-cell activation and its signaling effectors. Reason: The mouse donor PMID:19136564 tests Dectin-1-dependent dendritic-cell activation and its signaling effectors. Human Dectin-1/SYK inhibition in PMID:19358895 independently supports activation in immune cells. Cell activation is as broad as these multiple cellular outputs warrant, and is retained as contextual biology rather than made the defining molecular function. |
| GO:0001784 phosphotyrosine residue binding | IPI PMID:20624904 Tarp regulates early Chlamydia-induced host cell survival th... | ACCEPT | Summary: The original phosphopeptide-array study tests human SH2-domain binding to phosphorylated Chlamydia Tarp; its title emphasizes SHC1 but does not exclude SYK from the array. Reason: The original phosphopeptide-array study tests human SH2-domain binding to phosphorylated Chlamydia Tarp; its title emphasizes SHC1 but does not exclude SYK from the array. Independent purified ITAM binding and the SYK tandem-SH2 crystal structure directly establish phosphotyrosine recognition. Preserve the bacterial-effector partner without claiming that the SHC1 survival experiments were performed on SYK. The preserved original source is PMID:20624904. |
| GO:0001945 lymph vessel development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The source mouse knockout study PMID:12522250 demonstrates defective bloodβlymphatic separation and hematopoietic dependence, not a requirement for SYK expression in every endothelial cell. Reason: The source mouse knockout study PMID:12522250 demonstrates defective bloodβlymphatic separation and hematopoietic dependence, not a requirement for SYK expression in every endothelial cell. Retain the human orthology-based vascular-development role with that source-specific cellular boundary; a conserved immune kinase does not by itself prove native human endothelial action. Supporting Evidence: |
| GO:0001945 lymph vessel development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The source mouse knockout study PMID:12522250 demonstrates defective bloodβlymphatic separation and hematopoietic dependence, not a requirement for SYK expression in every endothelial cell. Reason: The source mouse knockout study PMID:12522250 demonstrates defective bloodβlymphatic separation and hematopoietic dependence, not a requirement for SYK expression in every endothelial cell. Retain the human orthology-based vascular-development role with that source-specific cellular boundary; a conserved immune kinase does not by itself prove native human endothelial action. Supporting Evidence: |
| GO:0002092 positive regulation of receptor internalization | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse studies identify SYKβPLCgamma2 signaling in CD14-dependent TLR4 endocytosis (PMID:22078883) and SYK-dependent CD36 internalization (PMID:23395392). Reason: Native mouse studies identify SYKβPLCgamma2 signaling in CD14-dependent TLR4 endocytosis (PMID:22078883) and SYK-dependent CD36 internalization (PMID:23395392). These support conserved receptor-trafficking and associated interferon responses in human as orthology inferences, not direct human experiments for every receptor. IFN effects depend on cell type and stimulus, as the dendritic-cell results in PMID:26708990 show. |
| GO:0002223 stimulatory C-type lectin receptor signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: SYK transmits signals from stimulatory C-type lectin receptors through phosphorylated receptor/adaptor motifs to downstream enzymes. Reason: SYK transmits signals from stimulatory C-type lectin receptors through phosphorylated receptor/adaptor motifs to downstream enzymes. Human dendritic-cell inhibitor experiments in PMID:19358895 and native mouse Dectin-1 studies independently support the catalytic signaling role. The BCR is not its only receptor context. |
| GO:0002223 stimulatory C-type lectin receptor signaling pathway | ISS GO_REF:0000024 | ACCEPT | Summary: SYK transmits signals from stimulatory C-type lectin receptors through phosphorylated receptor/adaptor motifs to downstream enzymes. Reason: SYK transmits signals from stimulatory C-type lectin receptors through phosphorylated receptor/adaptor motifs to downstream enzymes. Human dendritic-cell inhibitor experiments in PMID:19358895 and native mouse Dectin-1 studies independently support the catalytic signaling role. The BCR is not its only receptor context. |
| GO:0002223 stimulatory C-type lectin receptor signaling pathway | TAS Reactome:R-HSA-5621481 | ACCEPT | Summary: SYK transmits signals from stimulatory C-type lectin receptors through phosphorylated receptor/adaptor motifs to downstream enzymes. Reason: SYK transmits signals from stimulatory C-type lectin receptors through phosphorylated receptor/adaptor motifs to downstream enzymes. Human dendritic-cell inhibitor experiments in PMID:19358895 and native mouse Dectin-1 studies independently support the catalytic signaling role. The BCR is not its only receptor context. |
| GO:0002250 adaptive immune response | IBA GO_REF:0000033 | ACCEPT | Summary: SYK directly couples antigen-receptor phosphorylation to downstream signaling, with human BCR enzyme studies and native chicken DT40/BLNK experiments corroborating the PTN002815343 ancestral adaptive-immune assertion. Reason: SYK directly couples antigen-receptor phosphorylation to downstream signaling, with human BCR enzyme studies and native chicken DT40/BLNK experiments corroborating the PTN002815343 ancestral adaptive-immune assertion. The node is not judged by donor count, and chicken-host reconstitution is not silently relabeled as human native physiology. |
| GO:0002250 adaptive immune response | ISS GO_REF:0000024 | ACCEPT | Summary: SYK directly couples antigen-receptor phosphorylation to downstream signaling, with human BCR enzyme studies and native chicken DT40/BLNK experiments corroborating the PTN002815343 ancestral adaptive-immune assertion. Reason: SYK directly couples antigen-receptor phosphorylation to downstream signaling, with human BCR enzyme studies and native chicken DT40/BLNK experiments corroborating the PTN002815343 ancestral adaptive-immune assertion. The node is not judged by donor count, and chicken-host reconstitution is not silently relabeled as human native physiology. |
| GO:0002281 macrophage activation involved in immune response | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The PTN002815343 and mouse transfers concern integrin-linked activation of myeloid cells. Reason: The PTN002815343 and mouse transfers concern integrin-linked activation of myeloid cells. Native mouse deletion/reconstitution in PMID:17086186 establishes DAP12/FcRgamma ITAM-dependent SYK signaling; human neutrophil CD18 association and chemotaxis in PMID:12885943 provide independent human corroboration. Retain these cell-type-specific outputs outside the kinase core. |
| GO:0002281 macrophage activation involved in immune response | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The PTN002815343 and mouse transfers concern integrin-linked activation of myeloid cells. Reason: The PTN002815343 and mouse transfers concern integrin-linked activation of myeloid cells. Native mouse deletion/reconstitution in PMID:17086186 establishes DAP12/FcRgamma ITAM-dependent SYK signaling; human neutrophil CD18 association and chemotaxis in PMID:12885943 provide independent human corroboration. Retain these cell-type-specific outputs outside the kinase core. |
| GO:0002281 macrophage activation involved in immune response | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The PTN002815343 and mouse transfers concern integrin-linked activation of myeloid cells. Reason: The PTN002815343 and mouse transfers concern integrin-linked activation of myeloid cells. Native mouse deletion/reconstitution in PMID:17086186 establishes DAP12/FcRgamma ITAM-dependent SYK signaling; human neutrophil CD18 association and chemotaxis in PMID:12885943 provide independent human corroboration. Retain these cell-type-specific outputs outside the kinase core. |
| GO:0002283 neutrophil activation involved in immune response | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The PTN002815343 and mouse transfers concern integrin-linked activation of myeloid cells. Reason: The PTN002815343 and mouse transfers concern integrin-linked activation of myeloid cells. Native mouse deletion/reconstitution in PMID:17086186 establishes DAP12/FcRgamma ITAM-dependent SYK signaling; human neutrophil CD18 association and chemotaxis in PMID:12885943 provide independent human corroboration. Retain these cell-type-specific outputs outside the kinase core. |
| GO:0002283 neutrophil activation involved in immune response | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The PTN002815343 and mouse transfers concern integrin-linked activation of myeloid cells. Reason: The PTN002815343 and mouse transfers concern integrin-linked activation of myeloid cells. Native mouse deletion/reconstitution in PMID:17086186 establishes DAP12/FcRgamma ITAM-dependent SYK signaling; human neutrophil CD18 association and chemotaxis in PMID:12885943 provide independent human corroboration. Retain these cell-type-specific outputs outside the kinase core. |
| GO:0002283 neutrophil activation involved in immune response | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The PTN002815343 and mouse transfers concern integrin-linked activation of myeloid cells. Reason: The PTN002815343 and mouse transfers concern integrin-linked activation of myeloid cells. Native mouse deletion/reconstitution in PMID:17086186 establishes DAP12/FcRgamma ITAM-dependent SYK signaling; human neutrophil CD18 association and chemotaxis in PMID:12885943 provide independent human corroboration. Retain these cell-type-specific outputs outside the kinase core. |
| GO:0002366 leukocyte activation involved in immune response | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: SYK participates catalytically in innate leukocyte receptor responses, including Dectin-1-dependent cytokine signaling and integrin-dependent antimicrobial functions. Reason: SYK participates catalytically in innate leukocyte receptor responses, including Dectin-1-dependent cytokine signaling and integrin-dependent antimicrobial functions. Native mouse genetics and human dendritic-cell perturbation support these broad immune-context claims; they are not evidence that every immune output has the same direction. |
| GO:0002366 leukocyte activation involved in immune response | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: SYK participates catalytically in innate leukocyte receptor responses, including Dectin-1-dependent cytokine signaling and integrin-dependent antimicrobial functions. Reason: SYK participates catalytically in innate leukocyte receptor responses, including Dectin-1-dependent cytokine signaling and integrin-dependent antimicrobial functions. Native mouse genetics and human dendritic-cell perturbation support these broad immune-context claims; they are not evidence that every immune output has the same direction. |
| GO:0002554 serotonin secretion by platelet | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Reason: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Human platelet SYK association/activation and GPVI studies independently support conserved platelet signaling. Retain the specified output as a contextual inference, without asserting that SYK synthesizes serotonin/arachidonate or controls every platelet agonist. |
| GO:0002554 serotonin secretion by platelet | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Reason: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Human platelet SYK association/activation and GPVI studies independently support conserved platelet signaling. Retain the specified output as a contextual inference, without asserting that SYK synthesizes serotonin/arachidonate or controls every platelet agonist. |
| GO:0002752 cell surface pattern recognition receptor signaling pathway | IMP PMID:19358895 Dectin-1 is required for human dendritic cells to initiate i... | ACCEPT | Summary: SYK transmits signals from stimulatory C-type lectin receptors through phosphorylated receptor/adaptor motifs to downstream enzymes. Reason: SYK transmits signals from stimulatory C-type lectin receptors through phosphorylated receptor/adaptor motifs to downstream enzymes. Human dendritic-cell inhibitor experiments in PMID:19358895 and native mouse Dectin-1 studies independently support the catalytic signaling role. The BCR is not its only receptor context. The preserved original source is PMID:19358895. |
| GO:0002862 negative regulation of inflammatory response to antigenic stimulus | TAS Reactome:R-HSA-9664323 | KEEP AS NON CORE | Summary: The Reactome negative inflammatory-response branch is compatible with inhibitory immune-receptor signaling and with source-specific opposing SYK effects in TLR pathways. Reason: The original Reactome FCGR3A-mediated IL10 synthesis pathway supports a context-specific anti-inflammatory output of immune-receptor signaling. SYK executes proximal phosphorylation in this cytokine-producing route, rather than acting as IL10 itself. PMID:23962979 independently illustrates opposing, stimulus-specific SYK effects in TLR pathways; it is corroboration of context dependence, not an experiment on the FCGR3A branch. Retain negative inflammatory regulation as non-core, not a universal anti-inflammatory function. |
| GO:0004672 protein kinase activity | IDA PMID:18818202 Molecular mechanism of the Syk activation switch. | MODIFY | Summary: SYK is principally a non-receptor tyrosine kinase, established by purified full-length human enzyme and native B-cell autophosphorylation. Reason: SYK is principally a non-receptor tyrosine kinase, established by purified full-length human enzyme and native B-cell autophosphorylation. Direct Ikaros serine phosphorylation in PMID:23071339 also supports a contextual serine/threonine kinase activity; refine the broad kinase claim to both supported classes rather than erase that chemistry. These activities are already represented in this review. The preserved original source is PMID:18818202. Proposed replacements: non-membrane spanning protein tyrosine kinase activity protein serine/threonine kinase activity |
| GO:0004672 protein kinase activity | IEA GO_REF:0000002 | MODIFY | Summary: SYK is principally a non-receptor tyrosine kinase, established by purified full-length human enzyme and native B-cell autophosphorylation. Reason: SYK is principally a non-receptor tyrosine kinase, established by purified full-length human enzyme and native B-cell autophosphorylation. Direct Ikaros serine phosphorylation in PMID:23071339 also supports a contextual serine/threonine kinase activity; refine the broad kinase claim to both supported classes rather than erase that chemistry. These activities are already represented in this review. Proposed replacements: non-membrane spanning protein tyrosine kinase activity protein serine/threonine kinase activity |
| GO:0004672 protein kinase activity | NAS PMID:12885943 A role for Syk-kinase in the control of the binding cycle of... | MODIFY | Summary: SYK is principally a non-receptor tyrosine kinase, established by purified full-length human enzyme and native B-cell autophosphorylation. Reason: SYK is principally a non-receptor tyrosine kinase, established by purified full-length human enzyme and native B-cell autophosphorylation. Direct Ikaros serine phosphorylation in PMID:23071339 also supports a contextual serine/threonine kinase activity; refine the broad kinase claim to both supported classes rather than erase that chemistry. These activities are already represented in this review. The preserved original source is PMID:12885943. Proposed replacements: non-membrane spanning protein tyrosine kinase activity protein serine/threonine kinase activity |
| GO:0004674 protein serine/threonine kinase activity | IDA PMID:23071339 Serine phosphorylation by SYK is critical for nuclear locali... | KEEP AS NON CORE | Summary: PMID:23071339 directly tests purified recombinant SYK phosphorylation of Ikaros, with phospho-amino-acid analysis and mass spectrometry, and native human-cell knockdown supports regulation of Ikaros. Reason: PMID:23071339 directly tests purified recombinant SYK phosphorylation of Ikaros, with phospho-amino-acid analysis and mass spectrometry, and native human-cell knockdown supports regulation of Ikaros. The mapped mouse Ikaros S358/S361 correspond to human S361/S364; this is genuine serine phosphorylation by SYK, not merely activation of a downstream serine kinase. Retain this contextual chemistry alongside its principal tyrosine kinase function. The preserved original source is PMID:23071339. Supporting Evidence: url:https://pmc.ncbi.nlm.nih.gov/articles/PMC3497833/ Phospho amino acid analysis of the SYK-phosphorylated MBP-IK1 band showed S-phosphorylation. |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:10648173 Purification and characterization of human Syk produced usin... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:10648173. |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:17993265 Kit- and Fc epsilonRI-induced differential phosphorylation o... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:17993265. |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:18818202 Molecular mechanism of the Syk activation switch. | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:18818202. |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:22041900 Phospholipase CΞ³2 (PLCΞ³2) is key component in Dectin-2 signa... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:22041900. |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:8629002 Activation of BTK by a phosphorylation mechanism initiated b... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:8629002. |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:8657103 Phospholipase C-gamma1 interacts with conserved phosphotyros... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:8657103. |
| GO:0004713 protein tyrosine kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:23071339 Serine phosphorylation by SYK is critical for nuclear locali... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:23071339. |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:34634301 Tyrosine phosphorylation of DEPTOR functions as a molecular ... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:34634301. |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:39694035 MYO1F positions cGAS on the plasma membrane to ensure full a... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:39694035. |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:40980882 TLR9 signaling requires ligand-induced phosphorylation of tw... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:40980882. |
| GO:0004713 protein tyrosine kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004713 protein tyrosine kinase activity | IMP PMID:33782605 Gain-of-function variants in SYK cause immune dysregulation ... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:33782605. |
| GO:0004713 protein tyrosine kinase activity | ISS GO_REF:0000024 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004713 protein tyrosine kinase activity | NAS PMID:28386764 Roles of tau protein in health and disease. | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:28386764. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-2029453 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-2395412 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-2395801 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-2396594 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-2424484 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-2424486 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-2424487 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-429449 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-434836 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-HSA-9666425 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004715 non-membrane spanning protein tyrosine kinase activity | IDA PMID:11606584 Tyrosine residues in phospholipase Cgamma 2 essential for th... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:11606584. |
| GO:0004715 non-membrane spanning protein tyrosine kinase activity | IDA PMID:8163536 Molecular cloning of human Syk. A B cell protein-tyrosine ki... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:8163536. |
| GO:0004715 non-membrane spanning protein tyrosine kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0004715 non-membrane spanning protein tyrosine kinase activity | IGI PMID:14656219 Glycoproteins VI and Ib-IX-V stimulate tyrosine phosphorylat... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:14656219. |
| GO:0004715 non-membrane spanning protein tyrosine kinase activity | IMP PMID:15509800 Mechanism of B-cell receptor-induced phosphorylation and act... | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. The preserved original source is PMID:15509800. |
| GO:0004715 non-membrane spanning protein tyrosine kinase activity | TAS Reactome:R-HSA-453200 | ACCEPT | Summary: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Reason: Human SYK catalyzes ATP-dependent protein tyrosine phosphorylation. Purified full-length enzyme in PMID:10648173 and native human B-cell enzyme in PMID:8163536 establish the reaction independently of domain/ancestral mappings. PMID:18818202 directly distinguishes ITAM binding and autophosphorylation as activation mechanisms. Membrane recruitment is peripheral and does not confer receptor-spanning topology; the varied original substrate/pathway citations retain their own assay contexts. |
| GO:0005102 signaling receptor binding | IPI PMID:31145836 Physical proximity and functional cooperation of glycoprotei... | ACCEPT | Summary: SYK binds signaling receptors or their phosphorylated signaling chains through SH2-mediated recognition, established independently by CD3/ITAM and IL15RA binding. Reason: SYK binds signaling receptors or their phosphorylated signaling chains through SH2-mediated recognition, established independently by CD3/ITAM and IL15RA binding. The original GPVI/GP130 platelet paper establishes pathway proximity but its accessible abstract does not resolve the exact GPVIβSYK pair assay. Retain the supported general receptor-binding claim without mislabeling that abstract as an isolated binary GPVI-binding measurement. The preserved original source is PMID:31145836. |
| GO:0005178 integrin binding | IPI PMID:12885943 A role for Syk-kinase in the control of the binding cycle of... | KEEP AS NON CORE | Summary: PMID:12885943 directly reports Syk coprecipitation with CD18 in activated human neutrophils. Reason: PMID:12885943 directly reports Syk coprecipitation with CD18 in activated human neutrophils. Retain this integrin association in its adhesion-cycle context; co-immunoprecipitation does not require an isolated binary complex and inhibition has different effects on attachment and migration. The preserved original source is PMID:12885943. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:11940607 Coordinate interactions of Csk, Src, and Syk kinases with [a... | MODIFY | Summary: The original PMID:11940607 directly shows activation-dependent SYK association with platelet integrin alphaIIbbeta3. Reason: The original PMID:11940607 directly shows activation-dependent SYK association with platelet integrin alphaIIbbeta3. Refine bare protein binding to integrin binding, already represented in the review; this preserves the actual partner class without assuming constitutive association or an isolated binary interface. The preserved original source is PMID:11940607. Proposed replacements: integrin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12051764 SPAP2, an Ig family receptor containing both ITIMs and ITAMs... | MODIFY | Summary: The preserved Q96P31 partner is FCRL3/SPAP2. Reason: The preserved Q96P31 partner is FCRL3/SPAP2. PMID:12051764 directly maps phosphotyrosine-dependent recruitment of SYK, and curated human UniProt independently corroborates the same receptor association. Refine to phosphotyrosine residue binding; the FCRL3 chimeric-receptor inhibition study is not evidence that SYK itself has phosphatase activity. The preserved original source is PMID:12051764. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: file:human/SYK/SYK-uniprot.txt Interacts with FCRL3 |
| GO:0005515 protein binding | IPI PMID:15536084 Molecular basis for a direct interaction between the Syk pro... | MODIFY | Summary: The preserved partner P06239 is LCK. Reason: The preserved partner P06239 is LCK. PMID:8798676 directly identifies the LCK SH2 interaction with phosphorylated SYK; refine to protein tyrosine kinase binding and SH2 domain binding. PMID:15536084 foregrounds p85 binding and does not expose the exact LCK experiment in its abstract, so the independent LCK paper grounds the refinement without a wrong-gene allegation. The preserved original source is PMID:15536084. Proposed replacements: protein tyrosine kinase binding SH2 domain binding |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | UNDECIDED | Summary: PMID:16273093 measures human SH2/PTB domains against ErbB phosphopeptides, but the accessible abstract does not expose the exact SYK-domain/partner peptide entry for this preserved EGFR/ERBB2/ERBB3 pair. Reason: PMID:16273093 measures human SH2/PTB domains against ErbB phosphopeptides, but the accessible abstract does not expose the exact SYK-domain/partner peptide entry for this preserved EGFR/ERBB2/ERBB3 pair. The measured domain-array design is credible, yet affinity and pair identity cannot be reconstructed from the available source. Retain uncertainty rather than invent a particular physiological receptor interaction from the generic screen description. The preserved original source is PMID:16273093. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | UNDECIDED | Summary: PMID:16273093 measures human SH2/PTB domains against ErbB phosphopeptides, but the accessible abstract does not expose the exact SYK-domain/partner peptide entry for this preserved EGFR/ERBB2/ERBB3 pair. Reason: PMID:16273093 measures human SH2/PTB domains against ErbB phosphopeptides, but the accessible abstract does not expose the exact SYK-domain/partner peptide entry for this preserved EGFR/ERBB2/ERBB3 pair. The measured domain-array design is credible, yet affinity and pair identity cannot be reconstructed from the available source. Retain uncertainty rather than invent a particular physiological receptor interaction from the generic screen description. The preserved original source is PMID:16273093. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece... | UNDECIDED | Summary: PMID:16273093 measures human SH2/PTB domains against ErbB phosphopeptides, but the accessible abstract does not expose the exact SYK-domain/partner peptide entry for this preserved EGFR/ERBB2/ERBB3 pair. Reason: PMID:16273093 measures human SH2/PTB domains against ErbB phosphopeptides, but the accessible abstract does not expose the exact SYK-domain/partner peptide entry for this preserved EGFR/ERBB2/ERBB3 pair. The measured domain-array design is credible, yet affinity and pair identity cannot be reconstructed from the available source. Retain uncertainty rather than invent a particular physiological receptor interaction from the generic screen description. The preserved original source is PMID:16273093. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18273061 Structural basis for a novel intrapeptidyl H-bond and revers... | MODIFY | Summary: Full PMID:18273061 directly resolves c-CBL TKB recognition of phosphorylated SYK peptide with mutational/binding validation. Reason: Full PMID:18273061 directly resolves c-CBL TKB recognition of phosphorylated SYK peptide with mutational/binding validation. Refine to ubiquitin protein ligase binding; SYK supplies the phosphopeptide recognized by CBL and does not acquire CBL ubiquitin ligase activity. The preserved original source is PMID:18273061. Proposed replacements: ubiquitin protein ligase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19843936 FCRL3, an autoimmune susceptibility gene, has inhibitory pot... | MODIFY | Summary: The preserved Q96P31 partner is FCRL3/SPAP2. Reason: The preserved Q96P31 partner is FCRL3/SPAP2. PMID:12051764 directly maps phosphotyrosine-dependent recruitment of SYK, and curated human UniProt independently corroborates the same receptor association. Refine to phosphotyrosine residue binding; the FCRL3 chimeric-receptor inhibition study is not evidence that SYK itself has phosphatase activity. The preserved original source is PMID:19843936. Proposed replacements: phosphotyrosine residue binding Supporting Evidence: file:human/SYK/SYK-uniprot.txt Interacts with FCRL3 |
| GO:0005515 protein binding | IPI PMID:20133729 STAT3 is a substrate of SYK tyrosine kinase in B-lineage leu... | MODIFY | Summary: The preserved partner P40763 is STAT3, a DNA-binding transcription factor. Reason: The preserved partner P40763 is STAT3, a DNA-binding transcription factor. PMID:20133729 directly reports human SYKβSTAT3 association and phosphorylation during oxidative stress, independently corroborating the interactome entries. Refine bare binding to DNA-binding transcription factor binding without implying that every screen used the same stress condition or that SYK binds DNA. The preserved original source is PMID:20133729. Proposed replacements: DNA-binding transcription factor binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20585042 A novel histidine tyrosine phosphatase, TULA-2, associates w... | MODIFY | Summary: PMID:20585042 directly establishes SYK association with the histidine tyrosine phosphatase TULA2/UBASH3B in human and murine platelets. Reason: PMID:20585042 directly establishes SYK association with the histidine tyrosine phosphatase TULA2/UBASH3B in human and murine platelets. Refine the bare interaction to phosphatase binding, already represented here; the phosphatase catalysis belongs to TULA2, not SYK. The preserved original source is PMID:20585042. Proposed replacements: phosphatase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20713593 A novel interaction between FlnA and Syk regulates platelet ... | MODIFY | Summary: Full PMID:20713593 maps SYK binding to repeat5 of the cytoskeletal scaffold filamin A and links this interaction to platelet receptor signaling. Reason: Full PMID:20713593 maps SYK binding to repeat5 of the cytoskeletal scaffold filamin A and links this interaction to platelet receptor signaling. Scaffold protein binding captures the partnerβs organizational role without falsely assigning actin-binding activity to SYK or equating a mouse platelet knockout with every human domain assay. The preserved original source is PMID:20713593. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21044950 Genome-wide YFP fluorescence complementation screen identifi... | UNDECIDED | Summary: The full PMID:21044950 main text describes a fluorescence-complementation telomere interactome, but the exact SYKβTERF2/P54274 supplemental pair and construct conditions were not reconstructed. Reason: The full PMID:21044950 main text describes a fluorescence-complementation telomere interactome, but the exact SYKβTERF2/P54274 supplemental pair and construct conditions were not reconstructed. Retain this specific screen claim as unresolved; telomeric DNA binding by TERF2 does not make it a sequence-specific transcription factor or give SYK DNA-binding activity. The preserved original source is PMID:21044950. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21516116 Next-generation sequencing to generate interactome datasets. | MODIFY | Summary: The preserved partner P40763 is STAT3, a DNA-binding transcription factor. Reason: The preserved partner P40763 is STAT3, a DNA-binding transcription factor. PMID:20133729 directly reports human SYKβSTAT3 association and phosphorylation during oxidative stress, independently corroborating the interactome entries. Refine bare binding to DNA-binding transcription factor binding without implying that every screen used the same stress condition or that SYK binds DNA. The preserved original source is PMID:21516116. Proposed replacements: DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:21516116 Next-generation sequencing to generate interactome datasets. | REMOVE | Summary: The preserved Q9UHP3 partner is USP25. Reason: The preserved Q9UHP3 partner is USP25. Curated human UniProt independently records the interaction and SYK-dependent regulation of USP25 levels; the screen evidence is not rejected. Remove the uninformative bare protein-binding label under current policy while preserving this deubiquitinase-associated mechanism, without assigning USP25βs catalytic activity to SYK or inventing a phosphatase-binding replacement. The preserved original source is PMID:21516116. Supporting Evidence: file:human/SYK/SYK-uniprot.txt with USP25 (via C-terminus); phosphorylates USP25 |
| GO:0005515 protein binding | IPI PMID:22019427 The protein-tyrosine kinase Syk interacts with the C-termina... | MODIFY | Summary: PMID:22019427 directly identifies SYK interaction with the C-terminal SH2/PTB-containing region of tensin2 and colocalization in cytoplasmic puncta. Reason: PMID:22019427 directly identifies SYK interaction with the C-terminal SH2/PTB-containing region of tensin2 and colocalization in cytoplasmic puncta. Refine to scaffold protein binding. The available evidence does not isolate which domain supplies binding, so it does not justify replacing the row specifically with SH2-domain binding. The preserved original source is PMID:22019427. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22624718 Tetraspanin CD37 directly mediates transduction of survival ... | UNDECIDED | Summary: PMID:22624718 describes CD37-dependent survival and apoptotic signaling and opposing cytoplasmic tyrosine motifs. Reason: PMID:22624718 describes CD37-dependent survival and apoptotic signaling and opposing cytoplasmic tyrosine motifs. Its accessible abstract does not resolve the exact SYKβCD37 interaction or whether the assay is phosphorylation-dependent. Retain this pair-specific uncertainty rather than convert receptor pathway participation into an unverified direct binding interface. The preserved original source is PMID:22624718. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23001182 Interactions among HCLS1, HAX1 and LEF-1 proteins are essent... | REMOVE | Summary: Full PMID:23001182 explicitly reports constitutive SYKβHCLS1 association increasing after G-CSF stimulation in human CD34-positive cells (Supplementary Fig2b). Reason: Full PMID:23001182 explicitly reports constitutive SYKβHCLS1 association increasing after G-CSF stimulation in human CD34-positive cells (Supplementary Fig2b). Preserve that substrate/adaptor association in the rationale but remove the uninformative bare protein-binding term; SYK does not acquire HCLS1βs actin-binding or nuclear transport activities. The preserved original source is PMID:23001182. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23299888 Germinal centre protein HGAL promotes lymphoid hyperplasia a... | REMOVE | Summary: Full PMID:23299888 demonstrates human HGAL/GCSAM binding to SYK and enhancement of BCR-triggered kinase signaling. Reason: Full PMID:23299888 demonstrates human HGAL/GCSAM binding to SYK and enhancement of BCR-triggered kinase signaling. Remove the bare binding annotation as uninformative while retaining the activating partner mechanism; human-HGAL transgenic mice do not establish a native mouse ortholog assay. The preserved original source is PMID:23299888. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24525236 SYK is a critical regulator of FLT3 in acute myeloid leukemi... | MODIFY | Summary: Full PMID:24525236 directly demonstrates SYKβFLT3 binding and FLT3 transactivation in AML, including wild-type and oncogenic contexts. Reason: Full PMID:24525236 directly demonstrates SYKβFLT3 binding and FLT3 transactivation in AML, including wild-type and oncogenic contexts. Refine to protein tyrosine kinase binding; this does not make SYK a receptor kinase or universalize the oncogenic dependency. The preserved original source is PMID:24525236. Proposed replacements: protein tyrosine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: The full PMID:24728074 main text describes a quantitative SH2 phosphopeptide interaction matrix, but the precise preserved SYKβMET/GAB1 pair and phosphosite entry are not resolved in the inspected text. Reason: The full PMID:24728074 main text describes a quantitative SH2 phosphopeptide interaction matrix, but the precise preserved SYKβMET/GAB1 pair and phosphosite entry are not resolved in the inspected text. Retain uncertainty about the pair-specific assay rather than infer a binding geometry or claim that MET/GAB1 was not screened. The preserved original source is PMID:24728074. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24728074 Enhanced prediction of Src homology 2 (SH2) domain binding p... | UNDECIDED | Summary: The full PMID:24728074 main text describes a quantitative SH2 phosphopeptide interaction matrix, but the precise preserved SYKβMET/GAB1 pair and phosphosite entry are not resolved in the inspected text. Reason: The full PMID:24728074 main text describes a quantitative SH2 phosphopeptide interaction matrix, but the precise preserved SYKβMET/GAB1 pair and phosphosite entry are not resolved in the inspected text. Retain uncertainty about the pair-specific assay rather than infer a binding geometry or claim that MET/GAB1 was not screened. The preserved original source is PMID:24728074. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: The preserved partner P40763 is STAT3, a DNA-binding transcription factor. Reason: The preserved partner P40763 is STAT3, a DNA-binding transcription factor. PMID:20133729 directly reports human SYKβSTAT3 association and phosphorylation during oxidative stress, independently corroborating the interactome entries. Refine bare binding to DNA-binding transcription factor binding without implying that every screen used the same stress condition or that SYK binds DNA. The preserved original source is PMID:25416956. Proposed replacements: DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | UNDECIDED | Summary: The preserved Q9NP31 interaction comes from the large-scale PMID:25416956 binary interactome. Reason: The preserved Q9NP31 interaction comes from the large-scale PMID:25416956 binary interactome. The inspected main text does not expose the exact SYK pair or assay validation. Preserve this provenance and unresolved pair-specific evidence rather than assert a physiological complex or remove it on the ground that the title lacks SYK. The preserved original source is PMID:25416956. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The preserved Q9UHP3 partner is USP25. Reason: The preserved Q9UHP3 partner is USP25. Curated human UniProt independently records the interaction and SYK-dependent regulation of USP25 levels; the screen evidence is not rejected. Remove the uninformative bare protein-binding label under current policy while preserving this deubiquitinase-associated mechanism, without assigning USP25βs catalytic activity to SYK or inventing a phosphatase-binding replacement. The preserved original source is PMID:25416956. Supporting Evidence: file:human/SYK/SYK-uniprot.txt with USP25 (via C-terminus); phosphorylates USP25 |
| GO:0005515 protein binding | IPI PMID:25605870 Syk is involved in NLRP3 inflammasome-mediated caspase-1 act... | MODIFY | Summary: PMID:25605870 directly reports SYK association with the ASC inflammasome scaffold through its kinase domain and ASC phosphorylation/oligomerization. Reason: PMID:25605870 directly reports SYK association with the ASC inflammasome scaffold through its kinase domain and ASC phosphorylation/oligomerization. Refine to scaffold protein binding; the HEK293T reconstituted inflammasome is distinguished from every native myeloid context, and SYK does not acquire ASCβs caspase-recruitment activity. The preserved original source is PMID:25605870. Proposed replacements: scaffold protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25814554 Phospho-tyrosine dependent protein-protein interaction netwo... | UNDECIDED | Summary: The preserved Q96IP4 pair comes from PMID:25814554, a phosphotyrosine-dependent yeast two-hybrid screen containing SYK as one of the coexpressed kinases. Reason: The preserved Q96IP4 pair comes from PMID:25814554, a phosphotyrosine-dependent yeast two-hybrid screen containing SYK as one of the coexpressed kinases. The exact pairβs role as bait, prey or kinase and its phosphorylation dependence were not resolved from the inspected main text. Do not infer binding specificity merely because SYK was used to phosphorylate screen proteins. The preserved original source is PMID:25814554. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:28086240 ABL2 suppresses FLT3-ITD-induced cell proliferation through ... | MODIFY | Summary: Full PMID:28086240 explicitly includes SYK among SH2 domains with affinity for FLT3 phosphopeptides, despite the paperβs detailed follow-up focusing on ABL2. Reason: Full PMID:28086240 explicitly includes SYK among SH2 domains with affinity for FLT3 phosphopeptides, despite the paperβs detailed follow-up focusing on ABL2. Independent PMID:24525236 establishes direct SYKβFLT3 association. Refine the measured phosphopeptide recognition to phosphotyrosine residue binding; do not dismiss this row based on the ABL2 title. The preserved original source is PMID:28086240. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | MODIFY | Summary: The preserved partner P40763 is STAT3, a DNA-binding transcription factor. Reason: The preserved partner P40763 is STAT3, a DNA-binding transcription factor. PMID:20133729 directly reports human SYKβSTAT3 association and phosphorylation during oxidative stress, independently corroborating the interactome entries. Refine bare binding to DNA-binding transcription factor binding without implying that every screen used the same stress condition or that SYK binds DNA. The preserved original source is PMID:31515488. Proposed replacements: DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:31875558 LACC1 Required for NOD2-Induced, ER Stress-Mediated Innate I... | REMOVE | Summary: Full PMID:31875558 explicitly states that LACC1 did not associate with SYK after NOD2 or Dectin-1 stimulation in the tested human macrophage assays (FigS4E); Dectin1βSYK was the positive-control pair. Reason: Full PMID:31875558 explicitly states that LACC1 did not associate with SYK after NOD2 or Dectin-1 stimulation in the tested human macrophage assays (FigS4E); Dectin1βSYK was the positive-control pair. This directly contradicts the positive LACC1βSYK claim as sourced, rather than being inferred from abstract emphasis. The original machine assertion is preserved, and the judgment does not exclude an interaction in every untested condition. The preserved original source is PMID:31875558. Supporting Evidence: PMID:31875558 LACC1 did not associate with either Dectin-1 or Syk |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The preserved partner P40763 is STAT3, a DNA-binding transcription factor. Reason: The preserved partner P40763 is STAT3, a DNA-binding transcription factor. PMID:20133729 directly reports human SYKβSTAT3 association and phosphorylation during oxidative stress, independently corroborating the interactome entries. Refine bare binding to DNA-binding transcription factor binding without implying that every screen used the same stress condition or that SYK binds DNA. The preserved original source is PMID:32296183. Proposed replacements: DNA-binding transcription factor binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: The preserved Q9UHP3 partner is USP25. Reason: The preserved Q9UHP3 partner is USP25. Curated human UniProt independently records the interaction and SYK-dependent regulation of USP25 levels; the screen evidence is not rejected. Remove the uninformative bare protein-binding label under current policy while preserving this deubiquitinase-associated mechanism, without assigning USP25βs catalytic activity to SYK or inventing a phosphatase-binding replacement. The preserved original source is PMID:32296183. Supporting Evidence: file:human/SYK/SYK-uniprot.txt with USP25 (via C-terminus); phosphorylates USP25 |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | REMOVE | Summary: The preserved Q9UHP3 partner is USP25. Reason: The preserved Q9UHP3 partner is USP25. Curated human UniProt independently records the interaction and SYK-dependent regulation of USP25 levels; the screen evidence is not rejected. Remove the uninformative bare protein-binding label under current policy while preserving this deubiquitinase-associated mechanism, without assigning USP25βs catalytic activity to SYK or inventing a phosphatase-binding replacement. The preserved original source is PMID:32707033. Supporting Evidence: file:human/SYK/SYK-uniprot.txt with USP25 (via C-terminus); phosphorylates USP25 |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | UNDECIDED | Summary: PMID:32814053 is a neurodegeneration-focused interaction map; the exact SYKβAPP pair and assay/construct details are not available in the abstract-only cache. Reason: PMID:32814053 is a neurodegeneration-focused interaction map; the exact SYKβAPP pair and assay/construct details are not available in the abstract-only cache. Preserve the specific interaction as unresolved rather than infer APP processing or a direct amyloid-binding function of SYK. The preserved original source is PMID:32814053. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35512704 Systematic discovery of mutation-directed neo-protein-protei... | UNDECIDED | Summary: The full PMID:35512704 main text describes a mutation-directed interaction screen, but does not expose the exact SYKβEGFR pair, variant or wild-type comparison in the inspected source. Reason: The full PMID:35512704 main text describes a mutation-directed interaction screen, but does not expose the exact SYKβEGFR pair, variant or wild-type comparison in the inspected source. A mutation-specific gain of interaction cannot automatically be asserted for unmutated protein, so preserve source-specific uncertainty pending the pair table. The preserved original source is PMID:35512704. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:7761456 Analysis of the interaction of ZAP-70 and syk protein-tyrosi... | MODIFY | Summary: Direct phosphopeptide binding and structural experiments establish SYK recognition of phosphorylated receptor signaling chains, including CD3E, CD22 and Fc-receptor gamma. Reason: Direct phosphopeptide binding and structural experiments establish SYK recognition of phosphorylated receptor signaling chains, including CD3E, CD22 and Fc-receptor gamma. Refine bare binding to phosphotyrosine residue binding, already represented here. Original pair-specific assay provenance is retained, and the interaction is mediated by SYKβs SH2 domains rather than being binding to an SH2 domain on these receptor chains. The preserved original source is PMID:7761456. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:8627166 CD22 associates with protein tyrosine phosphatase 1C, Syk, a... | MODIFY | Summary: Direct phosphopeptide binding and structural experiments establish SYK recognition of phosphorylated receptor signaling chains, including CD3E, CD22 and Fc-receptor gamma. Reason: Direct phosphopeptide binding and structural experiments establish SYK recognition of phosphorylated receptor signaling chains, including CD3E, CD22 and Fc-receptor gamma. Refine bare binding to phosphotyrosine residue binding, already represented here. Original pair-specific assay provenance is retained, and the interaction is mediated by SYKβs SH2 domains rather than being binding to an SH2 domain on these receptor chains. The preserved original source is PMID:8627166. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:8647200 Involvement of p72syk kinase, p53/56lyn kinase and phosphati... | MODIFY | Summary: Direct phosphopeptide binding and structural experiments establish SYK recognition of phosphorylated receptor signaling chains, including CD3E, CD22 and Fc-receptor gamma. Reason: Direct phosphopeptide binding and structural experiments establish SYK recognition of phosphorylated receptor signaling chains, including CD3E, CD22 and Fc-receptor gamma. Refine bare binding to phosphotyrosine residue binding, already represented here. Original pair-specific assay provenance is retained, and the interaction is mediated by SYKβs SH2 domains rather than being binding to an SH2 domain on these receptor chains. The preserved original source is PMID:8647200. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:8657103 Phospholipase C-gamma1 interacts with conserved phosphotyros... | MODIFY | Summary: PMID:8657103 directly shows PLCgamma1 C-terminal SH2 binding to phosphorylated SYK linker residues and substrate phosphorylation. Reason: PMID:8657103 directly shows PLCgamma1 C-terminal SH2 binding to phosphorylated SYK linker residues and substrate phosphorylation. Refine bare binding to both phospholipase binding and SH2 domain binding, preserving the direction of recognition: PLCgamma1 supplies the SH2 domain. The preserved original source is PMID:8657103. Proposed replacements: phospholipase binding SH2 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:8798676 Identification of the site in the Syk protein tyrosine kinas... | MODIFY | Summary: The preserved partner P06239 is LCK. Reason: The preserved partner P06239 is LCK. PMID:8798676 directly identifies the LCK SH2 interaction with phosphorylated SYK; refine to protein tyrosine kinase binding and SH2 domain binding. PMID:15536084 foregrounds p85 binding and does not expose the exact LCK experiment in its abstract, so the independent LCK paper grounds the refinement without a wrong-gene allegation. The preserved original source is PMID:8798676. Proposed replacements: protein tyrosine kinase binding SH2 domain binding |
| GO:0005515 protein binding | IPI PMID:8810294 Interaction of phosphorylated FcepsilonRIgamma immunoglobuli... | MODIFY | Summary: Direct phosphopeptide binding and structural experiments establish SYK recognition of phosphorylated receptor signaling chains, including CD3E, CD22 and Fc-receptor gamma. Reason: Direct phosphopeptide binding and structural experiments establish SYK recognition of phosphorylated receptor signaling chains, including CD3E, CD22 and Fc-receptor gamma. Refine bare binding to phosphotyrosine residue binding, already represented here. Original pair-specific assay provenance is retained, and the interaction is mediated by SYKβs SH2 domains rather than being binding to an SH2 domain on these receptor chains. The preserved original source is PMID:8810294. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:9280292 Glycoprotein VI is the collagen receptor in platelets which ... | MODIFY | Summary: Direct phosphopeptide binding and structural experiments establish SYK recognition of phosphorylated receptor signaling chains, including CD3E, CD22 and Fc-receptor gamma. Reason: Direct phosphopeptide binding and structural experiments establish SYK recognition of phosphorylated receptor signaling chains, including CD3E, CD22 and Fc-receptor gamma. Refine bare binding to phosphotyrosine residue binding, already represented here. Original pair-specific assay provenance is retained, and the interaction is mediated by SYKβs SH2 domains rather than being binding to an SH2 domain on these receptor chains. The preserved original source is PMID:9280292. Proposed replacements: phosphotyrosine residue binding |
| GO:0005515 protein binding | IPI PMID:9698567 Structural basis for Syk tyrosine kinase ubiquity in signal ... | MODIFY | Summary: Direct phosphopeptide binding and structural experiments establish SYK recognition of phosphorylated receptor signaling chains, including CD3E, CD22 and Fc-receptor gamma. Reason: Direct phosphopeptide binding and structural experiments establish SYK recognition of phosphorylated receptor signaling chains, including CD3E, CD22 and Fc-receptor gamma. Refine bare binding to phosphotyrosine residue binding, already represented here. Original pair-specific assay provenance is retained, and the interaction is mediated by SYKβs SH2 domains rather than being binding to an SH2 domain on these receptor chains. The preserved original source is PMID:9698567. Proposed replacements: phosphotyrosine residue binding |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: ATP is the phosphate donor in the directly measured human SYK kinase reaction; purified full-length enzyme has measured ATP dependence. Reason: ATP is the phosphate donor in the directly measured human SYK kinase reaction; purified full-length enzyme has measured ATP dependence. This is not an independent ATPase function. Supporting Evidence: |
| GO:0005634 nucleus | IDA PMID:23071339 Serine phosphorylation by SYK is critical for nuclear locali... | KEEP AS NON CORE | Summary: PMID:23071339 examines SYKβIkaros in human cells and supports a nuclear as well as cytoplasmic pool. Reason: PMID:23071339 examines SYKβIkaros in human cells and supports a nuclear as well as cytoplasmic pool. Retain contextual nuclear localization rather than exclude it because receptor signaling is mainly cytoplasmic. Nuclear localization of Ikaros is a separate substrate response. The preserved original source is PMID:23071339. |
| GO:0005737 cytoplasm | IDA PMID:23071339 Serine phosphorylation by SYK is critical for nuclear locali... | ACCEPT | Summary: SYK has cytoplasmic soluble and receptor-associated pools, supported by native human B-cell studies and the human-cell SYKβIkaros analysis. Reason: SYK has cytoplasmic soluble and receptor-associated pools, supported by native human B-cell studies and the human-cell SYKβIkaros analysis. The broad cytoplasm claim remains valid across these pools and is retained alongside the more specific cytosol annotations. The preserved original source is PMID:23071339. |
| GO:0005737 cytoplasm | IEA GO_REF:0000002 | ACCEPT | Summary: SYK has cytoplasmic soluble and receptor-associated pools, supported by native human B-cell studies and the human-cell SYKβIkaros analysis. Reason: SYK has cytoplasmic soluble and receptor-associated pools, supported by native human B-cell studies and the human-cell SYKβIkaros analysis. The broad cytoplasm claim remains valid across these pools and is retained alongside the more specific cytosol annotations. |
| GO:0005737 cytoplasm | ISS GO_REF:0000024 | ACCEPT | Summary: SYK has cytoplasmic soluble and receptor-associated pools, supported by native human B-cell studies and the human-cell SYKβIkaros analysis. Reason: SYK has cytoplasmic soluble and receptor-associated pools, supported by native human B-cell studies and the human-cell SYKβIkaros analysis. The broad cytoplasm claim remains valid across these pools and is retained alongside the more specific cytosol annotations. |
| GO:0005829 cytosol | IC PMID:8163536 Molecular cloning of human Syk. A B cell protein-tyrosine ki... | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. The preserved original source is PMID:8163536. |
| GO:0005829 cytosol | IEA GO_REF:0000120 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-1112666 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-139842 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029268 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029270 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029271 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029272 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029273 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029451 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029452 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029453 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029458 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2029467 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-210289 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2197697 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2395412 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2395801 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2396594 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424480 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424482 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424484 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424486 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2424487 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2454240 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730833 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730843 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730851 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730884 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-2730886 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-429415 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-429441 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-429449 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-434836 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-437118 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-453183 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-453200 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-508282 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-508292 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5621347 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5621363 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5621366 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5621370 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5684801 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9606151 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664261 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664270 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664271 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664273 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9664278 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9666425 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9666426 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9666428 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9666430 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9666435 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9674816 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9691421 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9705738 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9706336 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9707977 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983700 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983703 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-983707 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005829 cytosol | TAS Reactome:R-NUL-5607748 | ACCEPT | Summary: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Reason: SYK is a cytoplasmic non-receptor kinase that exchanges between a soluble pool and membrane-recruited signaling complexes. Native human B-cell isolation and human-cell imaging independently support cytosolic residence; each preserved Reactome record supplies a pathway-specific occurrence of the same location rather than a new localization experiment. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Tandem SH2 recognition recruits SYK to phosphorylated receptor signaling chains at the plasma membrane. Reason: Tandem SH2 recognition recruits SYK to phosphorylated receptor signaling chains at the plasma membrane. The structure and quantitative ITAM-binding studies support this peripheral membrane pool independently of the broad PTN002521457 ancestral localization assertion. Retain plasma membrane without implying an integral membrane helix or exclusive residence. |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Tandem SH2 recognition recruits SYK to phosphorylated receptor signaling chains at the plasma membrane. Reason: Tandem SH2 recognition recruits SYK to phosphorylated receptor signaling chains at the plasma membrane. The structure and quantitative ITAM-binding studies support this peripheral membrane pool independently of the broad PTN002521457 ancestral localization assertion. Retain plasma membrane without implying an integral membrane helix or exclusive residence. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-429441 | ACCEPT | Summary: Tandem SH2 recognition recruits SYK to phosphorylated receptor signaling chains at the plasma membrane. Reason: Tandem SH2 recognition recruits SYK to phosphorylated receptor signaling chains at the plasma membrane. The structure and quantitative ITAM-binding studies support this peripheral membrane pool independently of the broad PTN002521457 ancestral localization assertion. Retain plasma membrane without implying an integral membrane helix or exclusive residence. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-508282 | ACCEPT | Summary: Tandem SH2 recognition recruits SYK to phosphorylated receptor signaling chains at the plasma membrane. Reason: Tandem SH2 recognition recruits SYK to phosphorylated receptor signaling chains at the plasma membrane. The structure and quantitative ITAM-binding studies support this peripheral membrane pool independently of the broad PTN002521457 ancestral localization assertion. Retain plasma membrane without implying an integral membrane helix or exclusive residence. |
| GO:0006357 regulation of transcription by RNA polymerase II | IMP PMID:23071339 Serine phosphorylation by SYK is critical for nuclear locali... | KEEP AS NON CORE | Summary: Human-cell SYK depletion reduces native Ikaros nuclear localization, DNA binding and target-gene expression in PMID:23071339. Reason: Human-cell SYK depletion reduces native Ikaros nuclear localization, DNA binding and target-gene expression in PMID:23071339. Retain downstream transcriptional regulation in this substrate-specific context; SYK supplies phosphorylation, not sequence-specific DNA recognition or RNA polymerase catalysis. The preserved original source is PMID:23071339. |
| GO:0006468 protein phosphorylation | IDA PMID:17681949 SLP-65 signal transduction requires Src homology 2 domain-me... | ACCEPT | Summary: SYK directly phosphorylates proteins, while the cited SLP65 reconstitution study additionally resolves a kinase-independent adaptor role. Reason: SYK directly phosphorylates proteins, while the cited SLP65 reconstitution study additionally resolves a kinase-independent adaptor role. Keep the broad phosphorylation process because both tyrosine and contextual serine substrate chemistry are experimentally supported; do not reduce all SYK function to its adaptor effect or to one phosphorylation class. The preserved original source is PMID:17681949. |
| GO:0006606 protein import into nucleus | IMP PMID:23071339 Serine phosphorylation by SYK is critical for nuclear locali... | MODIFY | Summary: SYK phosphorylates Ikaros and thereby promotes its nuclear accumulation; it is not demonstrated to carry Ikaros through the pore as an import receptor. Reason: SYK phosphorylates Ikaros and thereby promotes its nuclear accumulation; it is not demonstrated to carry Ikaros through the pore as an import receptor. Refine the role to positive regulation of protein import into nucleus, supported by SYK knockdown and Ikaros phosphosite/phosphomimetic mutants. This is a lateral role correction, not a claim that the regulatory term is a descendant of nuclear import. The preserved original source is PMID:23071339. Proposed replacements: positive regulation of protein import into nucleus |
| GO:0007159 leukocyte cell-cell adhesion | IDA PMID:12885943 A role for Syk-kinase in the control of the binding cycle of... | KEEP AS NON CORE | Summary: Human neutrophil experiments in PMID:12885943 connect SYK to the CD18 adhesionβdetachment cycle: piceatannol increases adhesion/spreading but reduces chemotactic migration. Reason: Human neutrophil experiments in PMID:12885943 connect SYK to the CD18 adhesionβdetachment cycle: piceatannol increases adhesion/spreading but reduces chemotactic migration. Retain participation in adhesion and migration without converting this context into a universal positive-adhesion sign. The preserved original source is PMID:12885943. Supporting Evidence: |
| GO:0007159 leukocyte cell-cell adhesion | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Human neutrophil experiments in PMID:12885943 connect SYK to the CD18 adhesionβdetachment cycle: piceatannol increases adhesion/spreading but reduces chemotactic migration. Reason: Human neutrophil experiments in PMID:12885943 connect SYK to the CD18 adhesionβdetachment cycle: piceatannol increases adhesion/spreading but reduces chemotactic migration. Retain participation in adhesion and migration without converting this context into a universal positive-adhesion sign. Supporting Evidence: |
| GO:0007229 integrin-mediated signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: SYK executes integrin-triggered signaling through ITAM-bearing adaptors and substrate phosphorylation. Reason: SYK executes integrin-triggered signaling through ITAM-bearing adaptors and substrate phosphorylation. Native mouse myeloid deletion/reconstitution and human neutrophil/platelet association support the conserved pathway, with receptor- and cell-specific assembly rather than a universal direct integrin-tail mechanism. |
| GO:0007229 integrin-mediated signaling pathway | ISS GO_REF:0000024 | ACCEPT | Summary: SYK executes integrin-triggered signaling through ITAM-bearing adaptors and substrate phosphorylation. Reason: SYK executes integrin-triggered signaling through ITAM-bearing adaptors and substrate phosphorylation. Native mouse myeloid deletion/reconstitution and human neutrophil/platelet association support the conserved pathway, with receptor- and cell-specific assembly rather than a universal direct integrin-tail mechanism. |
| GO:0007229 integrin-mediated signaling pathway | NAS PMID:12885943 A role for Syk-kinase in the control of the binding cycle of... | ACCEPT | Summary: SYK executes integrin-triggered signaling through ITAM-bearing adaptors and substrate phosphorylation. Reason: SYK executes integrin-triggered signaling through ITAM-bearing adaptors and substrate phosphorylation. Native mouse myeloid deletion/reconstitution and human neutrophil/platelet association support the conserved pathway, with receptor- and cell-specific assembly rather than a universal direct integrin-tail mechanism. The preserved original source is PMID:12885943. |
| GO:0009887 animal organ morphogenesis | TAS PMID:7477352 Perinatal lethality and blocked B-cell development in mice l... | UNDECIDED | Summary: The original mouse knockout paper PMID:7477352 exposes perinatal bleeding and lymphocyte-development defects in the accessible abstract, but not the exact organ-morphogenesis experiment behind this human TAS. Reason: The original mouse knockout paper PMID:7477352 exposes perinatal bleeding and lymphocyte-development defects in the accessible abstract, but not the exact organ-morphogenesis experiment behind this human TAS. Independent vascular-network evidence supports a narrower developmental context, not every organ. Preserve uncertainty about this broad citation-specific claim rather than infer a wrong-gene error or invent an organ assay. The preserved original source is PMID:7477352. |
| GO:0010543 regulation of platelet activation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Reason: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Human platelet SYK association/activation and GPVI studies independently support conserved platelet signaling. Retain the specified output as a contextual inference, without asserting that SYK synthesizes serotonin/arachidonate or controls every platelet agonist. |
| GO:0010543 regulation of platelet activation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Reason: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Human platelet SYK association/activation and GPVI studies independently support conserved platelet signaling. Retain the specified output as a contextual inference, without asserting that SYK synthesizes serotonin/arachidonate or controls every platelet agonist. |
| GO:0010803 regulation of tumor necrosis factor-mediated signaling pathway | IMP PMID:19151749 The protein-tyrosine kinase Syk interacts with TRAF-interact... | KEEP AS NON CORE | Summary: Full PMID:19151749 studies human mammary epithelial cells: SYK binds TRIP, enhances TNF-dependent NF-kappaB activation, and opposes TRIP-associated sensitization to apoptosis. Reason: Full PMID:19151749 studies human mammary epithelial cells: SYK binds TRIP, enhances TNF-dependent NF-kappaB activation, and opposes TRIP-associated sensitization to apoptosis. Retain contextual TNF-pathway regulation without making its sign universal across immune and epithelial cells. The preserved original source is PMID:19151749. Supporting Evidence: |
| GO:0016170 interleukin-15 receptor binding | IPI PMID:15123770 Interleukin-15 enhances human neutrophil phagocytosis by a S... | KEEP AS NON CORE | Summary: The original human-neutrophil study explicitly reports physical association of SYK with IL15RA and a SYK-dependent increase in phagocytosis. Reason: The original human-neutrophil study explicitly reports physical association of SYK with IL15RA and a SYK-dependent increase in phagocytosis. Retain this receptor-binding context; it does not assign IL15 ligand activity to SYK. The preserved original source is PMID:15123770. Supporting Evidence: |
| GO:0016301 kinase activity | IDA PMID:9490415 Immunoreceptor DAP12 bearing a tyrosine-based activation mot... | MODIFY | Summary: SYK is principally a non-receptor tyrosine kinase, established by purified full-length human enzyme and native B-cell autophosphorylation. Reason: SYK is principally a non-receptor tyrosine kinase, established by purified full-length human enzyme and native B-cell autophosphorylation. Direct Ikaros serine phosphorylation in PMID:23071339 also supports a contextual serine/threonine kinase activity; refine the broad kinase claim to both supported classes rather than erase that chemistry. These activities are already represented in this review. The preserved original source is PMID:9490415. Proposed replacements: non-membrane spanning protein tyrosine kinase activity protein serine/threonine kinase activity |
| GO:0018108 peptidyl-tyrosine phosphorylation | ISS GO_REF:0000024 | ACCEPT | Summary: SYK catalyzes protein tyrosine phosphorylation, established directly for the human protein and independently supported by native chicken SYK-dependent BLNK phosphorylation. Reason: SYK catalyzes protein tyrosine phosphorylation, established directly for the human protein and independently supported by native chicken SYK-dependent BLNK phosphorylation. This is catalytic participation rather than a phenotype-only inference. |
| GO:0019815 B cell receptor complex | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: SYK associates transiently with the activated BCR through phosphorylated signaling chains. Reason: SYK associates transiently with the activated BCR through phosphorylated signaling chains. Native human B-cell isolation in PMID:8163536 corroborates the mouse reconstitution evidence. Retain the signaling-complex context without describing SYK as a constitutive antigen-binding receptor subunit. |
| GO:0019901 protein kinase binding | IEA GO_REF:0000107 | MODIFY | Summary: The transferred mouse FgrβSYK association is a protein tyrosine kinase interaction. Reason: The transferred mouse FgrβSYK association is a protein tyrosine kinase interaction. PMID:11672534 identifies Fgr SH2 binding to Syk Tyr342, while direct LckβSYK binding independently supports the human claim. Refine generic protein kinase binding to protein tyrosine kinase binding; do not reverse the direction of SH2 recognition. Proposed replacements: protein tyrosine kinase binding |
| GO:0019902 phosphatase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse TLR4βCEACAM1βSYK complexes recruit SHP1 in PMID:22496641, and human platelet SYK association with TULA2 is directly supported in PMID:20585042. Reason: Mouse TLR4βCEACAM1βSYK complexes recruit SHP1 in PMID:22496641, and human platelet SYK association with TULA2 is directly supported in PMID:20585042. Retain the phosphatase-binding class while distinguishing complex coassociation from a purified binary SHP1 interface. |
| GO:0030168 platelet activation | TAS Reactome:R-HSA-76002 | KEEP AS NON CORE | Summary: SYK executes a receptor-proximal kinase step in collagen/GPVI platelet activation. Reason: SYK executes a receptor-proximal kinase step in collagen/GPVI platelet activation. Human platelet studies and mouse genetics support this Reactome pathway context; the reaction is not universally required for thrombin-triggered activation. |
| GO:0030593 neutrophil chemotaxis | IDA PMID:12885943 A role for Syk-kinase in the control of the binding cycle of... | KEEP AS NON CORE | Summary: Human neutrophil experiments in PMID:12885943 connect SYK to the CD18 adhesionβdetachment cycle: piceatannol increases adhesion/spreading but reduces chemotactic migration. Reason: Human neutrophil experiments in PMID:12885943 connect SYK to the CD18 adhesionβdetachment cycle: piceatannol increases adhesion/spreading but reduces chemotactic migration. Retain participation in adhesion and migration without converting this context into a universal positive-adhesion sign. The preserved original source is PMID:12885943. Supporting Evidence: |
| GO:0031334 positive regulation of protein-containing complex assembly | IMP PMID:22267217 Dectin-1 is an extracellular pathogen sensor for the inducti... | KEEP AS NON CORE | Summary: PMID:22267217 explicitly links Dectin-1/SYK signaling to assembly of the CARD9βBCL10βMALT1βcaspase8βASC machinery for IL1B transcription and processing. Reason: PMID:22267217 explicitly links Dectin-1/SYK signaling to assembly of the CARD9βBCL10βMALT1βcaspase8βASC machinery for IL1B transcription and processing. Retain positive complex-assembly regulation; caspase8 recruitment here does not by itself establish apoptosis. The preserved original source is PMID:22267217. Supporting Evidence: |
| GO:0031623 receptor internalization | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse studies identify SYKβPLCgamma2 signaling in CD14-dependent TLR4 endocytosis (PMID:22078883) and SYK-dependent CD36 internalization (PMID:23395392). Reason: Native mouse studies identify SYKβPLCgamma2 signaling in CD14-dependent TLR4 endocytosis (PMID:22078883) and SYK-dependent CD36 internalization (PMID:23395392). These support conserved receptor-trafficking and associated interferon responses in human as orthology inferences, not direct human experiments for every receptor. IFN effects depend on cell type and stimulus, as the dendritic-cell results in PMID:26708990 show. |
| GO:0031623 receptor internalization | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Native mouse studies identify SYKβPLCgamma2 signaling in CD14-dependent TLR4 endocytosis (PMID:22078883) and SYK-dependent CD36 internalization (PMID:23395392). Reason: Native mouse studies identify SYKβPLCgamma2 signaling in CD14-dependent TLR4 endocytosis (PMID:22078883) and SYK-dependent CD36 internalization (PMID:23395392). These support conserved receptor-trafficking and associated interferon responses in human as orthology inferences, not direct human experiments for every receptor. IFN effects depend on cell type and stimulus, as the dendritic-cell results in PMID:26708990 show. |
| GO:0032009 early phagosome | IEA GO_REF:0000107 | ACCEPT | Summary: The mouse Dectin-1 study PMID:15845454 identifies early phagosome-associated SYK signaling; conserved receptor recruitment supports the human transfer. Reason: The mouse Dectin-1 study PMID:15845454 identifies early phagosome-associated SYK signaling; conserved receptor recruitment supports the human transfer. This is a peripheral signaling pool at the developing phagosome, not constitutive luminal residency. Supporting Evidence: |
| GO:0032009 early phagosome | ISS GO_REF:0000024 | ACCEPT | Summary: The mouse Dectin-1 study PMID:15845454 identifies early phagosome-associated SYK signaling; conserved receptor recruitment supports the human transfer. Reason: The mouse Dectin-1 study PMID:15845454 identifies early phagosome-associated SYK signaling; conserved receptor recruitment supports the human transfer. This is a peripheral signaling pool at the developing phagosome, not constitutive luminal residency. Supporting Evidence: |
| GO:0032481 positive regulation of type I interferon production | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse studies identify SYKβPLCgamma2 signaling in CD14-dependent TLR4 endocytosis (PMID:22078883) and SYK-dependent CD36 internalization (PMID:23395392). Reason: Native mouse studies identify SYKβPLCgamma2 signaling in CD14-dependent TLR4 endocytosis (PMID:22078883) and SYK-dependent CD36 internalization (PMID:23395392). These support conserved receptor-trafficking and associated interferon responses in human as orthology inferences, not direct human experiments for every receptor. IFN effects depend on cell type and stimulus, as the dendritic-cell results in PMID:26708990 show. |
| GO:0032733 positive regulation of interleukin-10 production | IMP PMID:19358895 Dectin-1 is required for human dendritic cells to initiate i... | KEEP AS NON CORE | Summary: Positive IL10 regulation is directly demonstrated for the Dectin-1/SYK pathway in native mouse dendritic cells in PMID:15845454. Reason: Positive IL10 regulation is directly demonstrated for the Dectin-1/SYK pathway in native mouse dendritic cells in PMID:15845454. Human PMID:19358895 supports the same receptor/kinase response but its abstract does not expose the IL10-specific measurement. Retain the conserved cytokine-specific context with that limit; the opposite LPS/DC effect in PMID:26708990 shows why this is not a universal sign. The preserved original source is PMID:19358895. |
| GO:0032735 positive regulation of interleukin-12 production | IMP PMID:19358895 Dectin-1 is required for human dendritic cells to initiate i... | KEEP AS NON CORE | Summary: The original human dendritic-cell study PMID:19358895 explicitly reports that SYK inhibition suppresses Candida-induced IL12, IL6, TNF-alpha and superoxide output. Reason: The original human dendritic-cell study PMID:19358895 explicitly reports that SYK inhibition suppresses Candida-induced IL12, IL6, TNF-alpha and superoxide output. Retain the respective measured output in the Dectin-1 context, without conflating these immune consequences with SYKβs molecular kinase activity. The preserved original source is PMID:19358895. Supporting Evidence: |
| GO:0032753 positive regulation of interleukin-4 production | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The native mouse source PMID:19098920 shows IL3-receptor/FcRgamma recruitment of SYK and an ITAM-dependent IL4-production branch in basophils. Reason: The native mouse source PMID:19098920 shows IL3-receptor/FcRgamma recruitment of SYK and an ITAM-dependent IL4-production branch in basophils. Retain the conserved human inference as a conditional cytokine-receptor signaling role; it does not establish that all IL3 responses require SYK or that human basophils were the knockout host. Supporting Evidence: |
| GO:0032753 positive regulation of interleukin-4 production | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The native mouse source PMID:19098920 shows IL3-receptor/FcRgamma recruitment of SYK and an ITAM-dependent IL4-production branch in basophils. Reason: The native mouse source PMID:19098920 shows IL3-receptor/FcRgamma recruitment of SYK and an ITAM-dependent IL4-production branch in basophils. Retain the conserved human inference as a conditional cytokine-receptor signaling role; it does not establish that all IL3 responses require SYK or that human basophils were the knockout host. Supporting Evidence: |
| GO:0032755 positive regulation of interleukin-6 production | IMP PMID:19358895 Dectin-1 is required for human dendritic cells to initiate i... | KEEP AS NON CORE | Summary: The original human dendritic-cell study PMID:19358895 explicitly reports that SYK inhibition suppresses Candida-induced IL12, IL6, TNF-alpha and superoxide output. Reason: The original human dendritic-cell study PMID:19358895 explicitly reports that SYK inhibition suppresses Candida-induced IL12, IL6, TNF-alpha and superoxide output. Retain the respective measured output in the Dectin-1 context, without conflating these immune consequences with SYKβs molecular kinase activity. The preserved original source is PMID:19358895. Supporting Evidence: |
| GO:0032757 positive regulation of interleukin-8 production | IMP PMID:25251945 Human intestinal epithelial cells respond to Ξ²-glucans via D... | KEEP AS NON CORE | Summary: PMID:25251945 directly studies human intestinal epithelial cells and reports Dectin-1/SYK-dependent beta-glucan-induced IL8 and CCL2 secretion. Reason: PMID:25251945 directly studies human intestinal epithelial cells and reports Dectin-1/SYK-dependent beta-glucan-induced IL8 and CCL2 secretion. Retain the specified chemokine output as contextual native human biology, not a newly inferred B-cell core function. The preserved original source is PMID:25251945. Supporting Evidence: |
| GO:0032760 positive regulation of tumor necrosis factor production | IMP PMID:19358895 Dectin-1 is required for human dendritic cells to initiate i... | KEEP AS NON CORE | Summary: The original human dendritic-cell study PMID:19358895 explicitly reports that SYK inhibition suppresses Candida-induced IL12, IL6, TNF-alpha and superoxide output. Reason: The original human dendritic-cell study PMID:19358895 explicitly reports that SYK inhibition suppresses Candida-induced IL12, IL6, TNF-alpha and superoxide output. Retain the respective measured output in the Dectin-1 context, without conflating these immune consequences with SYKβs molecular kinase activity. The preserved original source is PMID:19358895. Supporting Evidence: |
| GO:0032928 regulation of superoxide anion generation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Reason: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Retain the corresponding conserved human response as non-core orthology-supported biology. Normal inflammatory-cell recruitment in that study prevents conflating all those outputs with a generalized migration defect. Supporting Evidence: |
| GO:0032928 regulation of superoxide anion generation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Reason: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Retain the corresponding conserved human response as non-core orthology-supported biology. Normal inflammatory-cell recruitment in that study prevents conflating all those outputs with a generalized migration defect. Supporting Evidence: |
| GO:0032930 positive regulation of superoxide anion generation | IMP PMID:19358895 Dectin-1 is required for human dendritic cells to initiate i... | KEEP AS NON CORE | Summary: The original human dendritic-cell study PMID:19358895 explicitly reports that SYK inhibition suppresses Candida-induced IL12, IL6, TNF-alpha and superoxide output. Reason: The original human dendritic-cell study PMID:19358895 explicitly reports that SYK inhibition suppresses Candida-induced IL12, IL6, TNF-alpha and superoxide output. Retain the respective measured output in the Dectin-1 context, without conflating these immune consequences with SYKβs molecular kinase activity. The preserved original source is PMID:19358895. Supporting Evidence: |
| GO:0032991 protein-containing complex | IDA PMID:23071339 Serine phosphorylation by SYK is critical for nuclear locali... | ACCEPT | Summary: SYK participates in multiple experimentally identified signaling complexes, including Ikaros-associated complexes in human cells and DAP12/Siglec15 complexes in mouse osteoclasts. Reason: SYK participates in multiple experimentally identified signaling complexes, including Ikaros-associated complexes in human cells and DAP12/Siglec15 complexes in mouse osteoclasts. The general complex term remains as precise as their different architectures permit; it is not reduced arbitrarily to one complex or made a constitutive receptor-subunit claim. The preserved original source is PMID:23071339. |
| GO:0032991 protein-containing complex | IEA GO_REF:0000107 | ACCEPT | Summary: SYK participates in multiple experimentally identified signaling complexes, including Ikaros-associated complexes in human cells and DAP12/Siglec15 complexes in mouse osteoclasts. Reason: SYK participates in multiple experimentally identified signaling complexes, including Ikaros-associated complexes in human cells and DAP12/Siglec15 complexes in mouse osteoclasts. The general complex term remains as precise as their different architectures permit; it is not reduced arbitrarily to one complex or made a constitutive receptor-subunit claim. |
| GO:0033630 positive regulation of cell adhesion mediated by integrin | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Native mouse platelet spreading and myeloid ITAMβintegrin signaling support the PTN002815343 positive-adhesion assertion. Reason: Native mouse platelet spreading and myeloid ITAMβintegrin signaling support the PTN002815343 positive-adhesion assertion. Human platelet complex experiments corroborate this context. The increased static human neutrophil adhesion after SYK inhibition in PMID:12885943 reflects a different attachmentβdetachment assay and does not invalidate all positive integrin-adhesion roles. |
| GO:0033630 positive regulation of cell adhesion mediated by integrin | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse platelet spreading and myeloid ITAMβintegrin signaling support the PTN002815343 positive-adhesion assertion. Reason: Native mouse platelet spreading and myeloid ITAMβintegrin signaling support the PTN002815343 positive-adhesion assertion. Human platelet complex experiments corroborate this context. The increased static human neutrophil adhesion after SYK inhibition in PMID:12885943 reflects a different attachmentβdetachment assay and does not invalidate all positive integrin-adhesion roles. |
| GO:0033630 positive regulation of cell adhesion mediated by integrin | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Native mouse platelet spreading and myeloid ITAMβintegrin signaling support the PTN002815343 positive-adhesion assertion. Reason: Native mouse platelet spreading and myeloid ITAMβintegrin signaling support the PTN002815343 positive-adhesion assertion. Human platelet complex experiments corroborate this context. The increased static human neutrophil adhesion after SYK inhibition in PMID:12885943 reflects a different attachmentβdetachment assay and does not invalidate all positive integrin-adhesion roles. |
| GO:0034165 positive regulation of toll-like receptor 9 signaling pathway | IDA PMID:40980882 TLR9 signaling requires ligand-induced phosphorylation of tw... | KEEP AS NON CORE | Summary: Full PMID:40980882 resolves sequential TLR9 phosphorylation: SYK targets Tyr870 before EGFR-dependent Tyr980 phosphorylation and adaptor recruitment. Reason: Full PMID:40980882 resolves sequential TLR9 phosphorylation: SYK targets Tyr870 before EGFR-dependent Tyr980 phosphorylation and adaptor recruitment. Retain this direct, context-specific innate-signaling role. The source abstractβs wording grouping SYK with Src kinases is not adopted: SYK belongs to the SYK/ZAP70 family. The preserved original source is PMID:40980882. Supporting Evidence: |
| GO:0035325 Toll-like receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse TLR4 complex association in PMID:22496641 supports the transfer, and human-cell TLR9 interaction in PMID:40980882 independently supports this receptor-binding class. Reason: Mouse TLR4 complex association in PMID:22496641 supports the transfer, and human-cell TLR9 interaction in PMID:40980882 independently supports this receptor-binding class. These do not imply equivalent affinity or mechanism for every Toll-like receptor. |
| GO:0035556 intracellular signal transduction | IDA PMID:11606584 Tyrosine residues in phospholipase Cgamma 2 essential for th... | ACCEPT | Summary: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Reason: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Purified BLNK/PLCgamma assays, human BCR knockdown, and native receptor studies establish catalytic signaling participation. The microglial source additionally exposes SYK phosphorylation after phosphatidylserine-liposome challenge in its accessible extended-data legend; no binary PLCG2-binding conclusion is inferred from that response. The preserved original source is PMID:11606584. Supporting Evidence: url:https://www.nature.com/articles/s41593-020-0650-6 |
| GO:0035556 intracellular signal transduction | IDA PMID:15509800 Mechanism of B-cell receptor-induced phosphorylation and act... | ACCEPT | Summary: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Reason: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Purified BLNK/PLCgamma assays, human BCR knockdown, and native receptor studies establish catalytic signaling participation. The microglial source additionally exposes SYK phosphorylation after phosphatidylserine-liposome challenge in its accessible extended-data legend; no binary PLCG2-binding conclusion is inferred from that response. The preserved original source is PMID:15509800. Supporting Evidence: url:https://www.nature.com/articles/s41593-020-0650-6 |
| GO:0035556 intracellular signal transduction | IEA GO_REF:0000002 | ACCEPT | Summary: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Reason: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Purified BLNK/PLCgamma assays, human BCR knockdown, and native receptor studies establish catalytic signaling participation. The microglial source additionally exposes SYK phosphorylation after phosphatidylserine-liposome challenge in its accessible extended-data legend; no binary PLCG2-binding conclusion is inferred from that response. Supporting Evidence: url:https://www.nature.com/articles/s41593-020-0650-6 |
| GO:0035556 intracellular signal transduction | IGI PMID:14656219 Glycoproteins VI and Ib-IX-V stimulate tyrosine phosphorylat... | ACCEPT | Summary: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Reason: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Purified BLNK/PLCgamma assays, human BCR knockdown, and native receptor studies establish catalytic signaling participation. The microglial source additionally exposes SYK phosphorylation after phosphatidylserine-liposome challenge in its accessible extended-data legend; no binary PLCG2-binding conclusion is inferred from that response. The preserved original source is PMID:14656219. Supporting Evidence: url:https://www.nature.com/articles/s41593-020-0650-6 |
| GO:0035556 intracellular signal transduction | IMP PMID:11606584 Tyrosine residues in phospholipase Cgamma 2 essential for th... | ACCEPT | Summary: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Reason: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Purified BLNK/PLCgamma assays, human BCR knockdown, and native receptor studies establish catalytic signaling participation. The microglial source additionally exposes SYK phosphorylation after phosphatidylserine-liposome challenge in its accessible extended-data legend; no binary PLCG2-binding conclusion is inferred from that response. The preserved original source is PMID:11606584. Supporting Evidence: url:https://www.nature.com/articles/s41593-020-0650-6 |
| GO:0035556 intracellular signal transduction | IMP PMID:32514138 Alzheimer's-associated PLCΞ³2 is a signaling node required fo... | ACCEPT | Summary: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Reason: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Purified BLNK/PLCgamma assays, human BCR knockdown, and native receptor studies establish catalytic signaling participation. The microglial source additionally exposes SYK phosphorylation after phosphatidylserine-liposome challenge in its accessible extended-data legend; no binary PLCG2-binding conclusion is inferred from that response. The preserved original source is PMID:32514138. Supporting Evidence: url:https://www.nature.com/articles/s41593-020-0650-6 |
| GO:0035556 intracellular signal transduction | ISS GO_REF:0000024 | ACCEPT | Summary: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Reason: Intracellular signal transduction remains an appropriate broad process for a kinase acting in BCR, integrin, Fc-receptor and innate-receptor pathways. Purified BLNK/PLCgamma assays, human BCR knockdown, and native receptor studies establish catalytic signaling participation. The microglial source additionally exposes SYK phosphorylation after phosphatidylserine-liposome challenge in its accessible extended-data legend; no binary PLCG2-binding conclusion is inferred from that response. Supporting Evidence: url:https://www.nature.com/articles/s41593-020-0650-6 |
| GO:0038095 Fc-epsilon receptor signaling pathway | TAS Reactome:R-HSA-2454202 | ACCEPT | Summary: SYK executes proximal Fc-receptor kinase signaling after phosphorylated ITAM recognition. Reason: SYK executes proximal Fc-receptor kinase signaling after phosphorylated ITAM recognition. Native mast-cell loss and myeloid ITAM-dependent uptake studies support Fc-epsilon and Fc-gamma contexts, respectively; individual receptor outcomes are not asserted to be identical. |
| GO:0038096 Fc-gamma receptor signaling pathway involved in phagocytosis | TAS Reactome:R-HSA-2029480 | ACCEPT | Summary: SYK executes proximal Fc-receptor kinase signaling after phosphorylated ITAM recognition. Reason: SYK executes proximal Fc-receptor kinase signaling after phosphorylated ITAM recognition. Native mast-cell loss and myeloid ITAM-dependent uptake studies support Fc-epsilon and Fc-gamma contexts, respectively; individual receptor outcomes are not asserted to be identical. |
| GO:0038096 Fc-gamma receptor signaling pathway involved in phagocytosis | TAS Reactome:R-HSA-9664422 | ACCEPT | Summary: SYK executes proximal Fc-receptor kinase signaling after phosphorylated ITAM recognition. Reason: SYK executes proximal Fc-receptor kinase signaling after phosphorylated ITAM recognition. Native mast-cell loss and myeloid ITAM-dependent uptake studies support Fc-epsilon and Fc-gamma contexts, respectively; individual receptor outcomes are not asserted to be identical. |
| GO:0038156 interleukin-3-mediated signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The native mouse source PMID:19098920 shows IL3-receptor/FcRgamma recruitment of SYK and an ITAM-dependent IL4-production branch in basophils. Reason: The native mouse source PMID:19098920 shows IL3-receptor/FcRgamma recruitment of SYK and an ITAM-dependent IL4-production branch in basophils. Retain the conserved human inference as a conditional cytokine-receptor signaling role; it does not establish that all IL3 responses require SYK or that human basophils were the knockout host. Supporting Evidence: |
| GO:0038156 interleukin-3-mediated signaling pathway | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The native mouse source PMID:19098920 shows IL3-receptor/FcRgamma recruitment of SYK and an ITAM-dependent IL4-production branch in basophils. Reason: The native mouse source PMID:19098920 shows IL3-receptor/FcRgamma recruitment of SYK and an ITAM-dependent IL4-production branch in basophils. Retain the conserved human inference as a conditional cytokine-receptor signaling role; it does not establish that all IL3 responses require SYK or that human basophils were the knockout host. Supporting Evidence: |
| GO:0042101 T cell receptor complex | IDA PMID:8176201 Differential expression of ZAP-70 and Syk protein tyrosine k... | KEEP AS NON CORE | Summary: PMID:8176201 explicitly reports stimulation-dependent SYK association with TCR complexes, including heterologous phosphorylated zeta-chain reconstitution. Reason: PMID:8176201 explicitly reports stimulation-dependent SYK association with TCR complexes, including heterologous phosphorylated zeta-chain reconstitution. Retain this conditional receptor-associated pool; SYK is not a constitutive structural component of the antigen-binding TCR and is not interchangeable with ZAP70 in every developmental stage. The preserved original source is PMID:8176201. |
| GO:0042101 T cell receptor complex | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: PMID:8176201 explicitly reports stimulation-dependent SYK association with TCR complexes, including heterologous phosphorylated zeta-chain reconstitution. Reason: PMID:8176201 explicitly reports stimulation-dependent SYK association with TCR complexes, including heterologous phosphorylated zeta-chain reconstitution. Retain this conditional receptor-associated pool; SYK is not a constitutive structural component of the antigen-binding TCR and is not interchangeable with ZAP70 in every developmental stage. |
| GO:0042169 SH2 domain binding | IEA GO_REF:0000107 | ACCEPT | Summary: SYKβs phosphorylated linker binds partner SH2 domains, directly shown for PLCgamma in PMID:8657103 and mouse/human platelet domain pull-downs in PMID:27609517. Reason: SYKβs phosphorylated linker binds partner SH2 domains, directly shown for PLCgamma in PMID:8657103 and mouse/human platelet domain pull-downs in PMID:27609517. This is distinct from the phosphotyrosine-binding activity of SYKβs own SH2 domains; retaining both does not reverse the interaction. |
| GO:0042742 defense response to bacterium | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Reason: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Retain the corresponding conserved human response as non-core orthology-supported biology. Normal inflammatory-cell recruitment in that study prevents conflating all those outputs with a generalized migration defect. Supporting Evidence: |
| GO:0042742 defense response to bacterium | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Reason: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Retain the corresponding conserved human response as non-core orthology-supported biology. Normal inflammatory-cell recruitment in that study prevents conflating all those outputs with a generalized migration defect. Supporting Evidence: |
| GO:0043274 phospholipase binding | IPI PMID:14656219 Glycoproteins VI and Ib-IX-V stimulate tyrosine phosphorylat... | ACCEPT | Summary: SYK associates with PLCgamma proteins through phosphorylation-dependent interfaces, directly supported by PLCgamma domain pull-downs and phosphorylation assays. Reason: SYK associates with PLCgamma proteins through phosphorylation-dependent interfaces, directly supported by PLCgamma domain pull-downs and phosphorylation assays. The original microglial paperβs accessible portions do not resolve an isolated SYKβPLCG2 binding assay, but independent platelet experiments support the general phospholipase-binding claim. PLCgamma2 binding is weaker than PLCgamma1 in the tested platelet lysates and is not equated with equal catalytic efficiency. The preserved original source is PMID:14656219. |
| GO:0043274 phospholipase binding | IPI PMID:32514138 Alzheimer's-associated PLCΞ³2 is a signaling node required fo... | ACCEPT | Summary: SYK associates with PLCgamma proteins through phosphorylation-dependent interfaces, directly supported by PLCgamma domain pull-downs and phosphorylation assays. Reason: SYK associates with PLCgamma proteins through phosphorylation-dependent interfaces, directly supported by PLCgamma domain pull-downs and phosphorylation assays. The original microglial paperβs accessible portions do not resolve an isolated SYKβPLCG2 binding assay, but independent platelet experiments support the general phospholipase-binding claim. PLCgamma2 binding is weaker than PLCgamma1 in the tested platelet lysates and is not equated with equal catalytic efficiency. The preserved original source is PMID:32514138. |
| GO:0043313 regulation of neutrophil degranulation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Reason: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Retain the corresponding conserved human response as non-core orthology-supported biology. Normal inflammatory-cell recruitment in that study prevents conflating all those outputs with a generalized migration defect. Supporting Evidence: |
| GO:0043313 regulation of neutrophil degranulation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Reason: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Retain the corresponding conserved human response as non-core orthology-supported biology. Normal inflammatory-cell recruitment in that study prevents conflating all those outputs with a generalized migration defect. Supporting Evidence: |
| GO:0045087 innate immune response | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: SYK participates catalytically in innate leukocyte receptor responses, including Dectin-1-dependent cytokine signaling and integrin-dependent antimicrobial functions. Reason: SYK participates catalytically in innate leukocyte receptor responses, including Dectin-1-dependent cytokine signaling and integrin-dependent antimicrobial functions. Native mouse genetics and human dendritic-cell perturbation support these broad immune-context claims; they are not evidence that every immune output has the same direction. |
| GO:0045087 innate immune response | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: SYK participates catalytically in innate leukocyte receptor responses, including Dectin-1-dependent cytokine signaling and integrin-dependent antimicrobial functions. Reason: SYK participates catalytically in innate leukocyte receptor responses, including Dectin-1-dependent cytokine signaling and integrin-dependent antimicrobial functions. Native mouse genetics and human dendritic-cell perturbation support these broad immune-context claims; they are not evidence that every immune output has the same direction. |
| GO:0045579 positive regulation of B cell differentiation | IMP PMID:18369315 The kinase Syk as an adaptor controlling sustained calcium s... | KEEP AS NON CORE | Summary: The SYKβSLP65 feedback study shows that failure to form the complex impairs sustained calcium signaling and B-cell developmental progression. Reason: The SYKβSLP65 feedback study shows that failure to form the complex impairs sustained calcium signaling and B-cell developmental progression. Retain the downstream differentiation consequence, distinguishing human constructs and mouse developmental experiments; SYKβs defining contribution is signal transmission. The preserved original source is PMID:18369315. Supporting Evidence: |
| GO:0045621 positive regulation of lymphocyte differentiation | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The SYKβSLP65 feedback study shows that failure to form the complex impairs sustained calcium signaling and B-cell developmental progression. Reason: The SYKβSLP65 feedback study shows that failure to form the complex impairs sustained calcium signaling and B-cell developmental progression. Retain the downstream differentiation consequence, distinguishing human constructs and mouse developmental experiments; SYKβs defining contribution is signal transmission. Supporting Evidence: |
| GO:0045780 positive regulation of bone resorption | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse osteoclast Syk deletion in PMID:17353363 impairs mature-cell cytoskeletal organization and bone resorption, not primarily differentiation. Reason: Native mouse osteoclast Syk deletion in PMID:17353363 impairs mature-cell cytoskeletal organization and bone resorption, not primarily differentiation. Retain the human orthology-based resorption role with that distinction and without claiming direct mineral dissolution by SYK. Supporting Evidence: |
| GO:0045780 positive regulation of bone resorption | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Native mouse osteoclast Syk deletion in PMID:17353363 impairs mature-cell cytoskeletal organization and bone resorption, not primarily differentiation. Reason: Native mouse osteoclast Syk deletion in PMID:17353363 impairs mature-cell cytoskeletal organization and bone resorption, not primarily differentiation. Retain the human orthology-based resorption role with that distinction and without claiming direct mineral dissolution by SYK. Supporting Evidence: |
| GO:0048514 blood vessel morphogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The source mouse knockout study PMID:12522250 demonstrates defective bloodβlymphatic separation and hematopoietic dependence, not a requirement for SYK expression in every endothelial cell. Reason: The source mouse knockout study PMID:12522250 demonstrates defective bloodβlymphatic separation and hematopoietic dependence, not a requirement for SYK expression in every endothelial cell. Retain the human orthology-based vascular-development role with that source-specific cellular boundary; a conserved immune kinase does not by itself prove native human endothelial action. Supporting Evidence: |
| GO:0048514 blood vessel morphogenesis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The source mouse knockout study PMID:12522250 demonstrates defective bloodβlymphatic separation and hematopoietic dependence, not a requirement for SYK expression in every endothelial cell. Reason: The source mouse knockout study PMID:12522250 demonstrates defective bloodβlymphatic separation and hematopoietic dependence, not a requirement for SYK expression in every endothelial cell. Retain the human orthology-based vascular-development role with that source-specific cellular boundary; a conserved immune kinase does not by itself prove native human endothelial action. Supporting Evidence: |
| GO:0050729 positive regulation of inflammatory response | IDA PMID:26708990 Syk negatively regulates TLR4-mediated IFNΞ² and IL-10 produc... | KEEP AS NON CORE | Summary: The full source PMID:26708990 demonstrates SYK-dependent TNF/IL6 and NF-kappaB responses primarily in murine dendritic cells, while IFNbeta/IL10 increase after Syk loss. Reason: The full source PMID:26708990 demonstrates SYK-dependent TNF/IL6 and NF-kappaB responses primarily in murine dendritic cells, while IFNbeta/IL10 increase after Syk loss. Retain the conserved positive inflammatory-response claim with this organism and stimulus boundary, rather than describing the source as a direct assay of every human cytokine or rejecting it because the abstract names mouse cells. The preserved original source is PMID:26708990. Supporting Evidence: |
| GO:0050764 regulation of phagocytosis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Reason: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Retain the corresponding conserved human response as non-core orthology-supported biology. Normal inflammatory-cell recruitment in that study prevents conflating all those outputs with a generalized migration defect. Supporting Evidence: |
| GO:0050764 regulation of phagocytosis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Reason: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Retain the corresponding conserved human response as non-core orthology-supported biology. Normal inflammatory-cell recruitment in that study prevents conflating all those outputs with a generalized migration defect. Supporting Evidence: |
| GO:0050776 regulation of immune response | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: SYK participates catalytically in innate leukocyte receptor responses, including Dectin-1-dependent cytokine signaling and integrin-dependent antimicrobial functions. Reason: SYK participates catalytically in innate leukocyte receptor responses, including Dectin-1-dependent cytokine signaling and integrin-dependent antimicrobial functions. Native mouse genetics and human dendritic-cell perturbation support these broad immune-context claims; they are not evidence that every immune output has the same direction. |
| GO:0050853 B cell receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: SYK directly phosphorylates receptor-associated substrates and BLNK to transmit BCR signals. Reason: SYK directly phosphorylates receptor-associated substrates and BLNK to transmit BCR signals. Human Ramos/native B-cell biochemistry, purified complex assays and chicken DT40 deletion/reconstitution corroborate the PTN002815343 ancestral assertion. The human target appearing among descendant evidence is legitimate phylogenetic grounding, not circularity. |
| GO:0050853 B cell receptor signaling pathway | IMP PMID:15509800 Mechanism of B-cell receptor-induced phosphorylation and act... | ACCEPT | Summary: SYK directly phosphorylates receptor-associated substrates and BLNK to transmit BCR signals. Reason: SYK directly phosphorylates receptor-associated substrates and BLNK to transmit BCR signals. Human Ramos/native B-cell biochemistry, purified complex assays and chicken DT40 deletion/reconstitution corroborate the PTN002815343 ancestral assertion. The human target appearing among descendant evidence is legitimate phylogenetic grounding, not circularity. The preserved original source is PMID:15509800. |
| GO:0050853 B cell receptor signaling pathway | ISS GO_REF:0000024 | ACCEPT | Summary: SYK directly phosphorylates receptor-associated substrates and BLNK to transmit BCR signals. Reason: SYK directly phosphorylates receptor-associated substrates and BLNK to transmit BCR signals. Human Ramos/native B-cell biochemistry, purified complex assays and chicken DT40 deletion/reconstitution corroborate the PTN002815343 ancestral assertion. The human target appearing among descendant evidence is legitimate phylogenetic grounding, not circularity. |
| GO:0050900 leukocyte migration | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Human neutrophil experiments in PMID:12885943 connect SYK to the CD18 adhesionβdetachment cycle: piceatannol increases adhesion/spreading but reduces chemotactic migration. Reason: Human neutrophil experiments in PMID:12885943 connect SYK to the CD18 adhesionβdetachment cycle: piceatannol increases adhesion/spreading but reduces chemotactic migration. Retain participation in adhesion and migration without converting this context into a universal positive-adhesion sign. Supporting Evidence: |
| GO:0070372 regulation of ERK1 and ERK2 cascade | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Reason: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Retain the corresponding conserved human response as non-core orthology-supported biology. Normal inflammatory-cell recruitment in that study prevents conflating all those outputs with a generalized migration defect. Supporting Evidence: |
| GO:0070372 regulation of ERK1 and ERK2 cascade | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Reason: The mouse donor PMID:19797524 uses myeloid/neutrophil-specific Syk deletion and directly measures defective oxidase activation, granule exocytosis, bacterial uptake/clearance and ERK signaling. Retain the corresponding conserved human response as non-core orthology-supported biology. Normal inflammatory-cell recruitment in that study prevents conflating all those outputs with a generalized migration defect. Supporting Evidence: |
| GO:0071226 cellular response to molecule of fungal origin | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse Dectin-1 experiments and human Candida/beta-glucan perturbation establish SYK-dependent cellular responses to fungal material and lectin-receptor engagement. Reason: Native mouse Dectin-1 experiments and human Candida/beta-glucan perturbation establish SYK-dependent cellular responses to fungal material and lectin-receptor engagement. Retain these stimulus-specific outcomes outside the molecular core, without making SYK the extracellular fungal-ligand-binding receptor. |
| GO:0071226 cellular response to molecule of fungal origin | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Native mouse Dectin-1 experiments and human Candida/beta-glucan perturbation establish SYK-dependent cellular responses to fungal material and lectin-receptor engagement. Reason: Native mouse Dectin-1 experiments and human Candida/beta-glucan perturbation establish SYK-dependent cellular responses to fungal material and lectin-receptor engagement. Retain these stimulus-specific outcomes outside the molecular core, without making SYK the extracellular fungal-ligand-binding receptor. |
| GO:0071396 cellular response to lipid | IMP PMID:32514138 Alzheimer's-associated PLCΞ³2 is a signaling node required fo... | KEEP AS NON CORE | Summary: The normally cached publisher page for PMID:32514138 exposes Extended Data Fig4a: endogenous SYK Y525/526 phosphorylation in human iPSC-derived microglia challenged with PC/PS liposomes, with inhibitor controls. Reason: The normally cached publisher page for PMID:32514138 exposes Extended Data Fig4a: endogenous SYK Y525/526 phosphorylation in human iPSC-derived microglia challenged with PC/PS liposomes, with inhibitor controls. This directly supports a lipid-stimulus response despite the PMID cache being abstract-only. It is not proof of direct lipid binding by SYK. The preserved original source is PMID:32514138. Supporting Evidence: url:https://www.nature.com/articles/s41593-020-0650-6 Levels of SYK phosphorylated at Y525/526 in WT iMG stimulated with 70% PC/30% PS liposomes |
| GO:0071404 cellular response to low-density lipoprotein particle stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The source mouse CD36 study uses oxidized-LDL/receptor-internalization signaling and identifies SYK downstream of a CD36βintegrinβFcRgamma assembly. Reason: The source mouse CD36 study uses oxidized-LDL/receptor-internalization signaling and identifies SYK downstream of a CD36βintegrinβFcRgamma assembly. Retain the conserved human response to LDL particles, not a claim that SYK binds or transports LDL directly. Supporting Evidence: |
| GO:0071404 cellular response to low-density lipoprotein particle stimulus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The source mouse CD36 study uses oxidized-LDL/receptor-internalization signaling and identifies SYK downstream of a CD36βintegrinβFcRgamma assembly. Reason: The source mouse CD36 study uses oxidized-LDL/receptor-internalization signaling and identifies SYK downstream of a CD36βintegrinβFcRgamma assembly. Retain the conserved human response to LDL particles, not a claim that SYK binds or transports LDL directly. Supporting Evidence: |
| GO:0071639 positive regulation of monocyte chemotactic protein-1 production | IMP PMID:25251945 Human intestinal epithelial cells respond to Ξ²-glucans via D... | KEEP AS NON CORE | Summary: PMID:25251945 directly studies human intestinal epithelial cells and reports Dectin-1/SYK-dependent beta-glucan-induced IL8 and CCL2 secretion. Reason: PMID:25251945 directly studies human intestinal epithelial cells and reports Dectin-1/SYK-dependent beta-glucan-induced IL8 and CCL2 secretion. Retain the specified chemokine output as contextual native human biology, not a newly inferred B-cell core function. The preserved original source is PMID:25251945. Supporting Evidence: |
| GO:0090237 regulation of arachidonate secretion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Reason: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Human platelet SYK association/activation and GPVI studies independently support conserved platelet signaling. Retain the specified output as a contextual inference, without asserting that SYK synthesizes serotonin/arachidonate or controls every platelet agonist. |
| GO:0090237 regulation of arachidonate secretion | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Reason: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Human platelet SYK association/activation and GPVI studies independently support conserved platelet signaling. Retain the specified output as a contextual inference, without asserting that SYK synthesizes serotonin/arachidonate or controls every platelet agonist. |
| GO:0090330 regulation of platelet aggregation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Reason: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Human platelet SYK association/activation and GPVI studies independently support conserved platelet signaling. Retain the specified output as a contextual inference, without asserting that SYK synthesizes serotonin/arachidonate or controls every platelet agonist. |
| GO:0090330 regulation of platelet aggregation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Reason: The mouse donor PMID:9171347 shows loss of collagen-induced secretion and aggregation in Syk-deficient platelets, while thrombin responses persist. Human platelet SYK association/activation and GPVI studies independently support conserved platelet signaling. Retain the specified output as a contextual inference, without asserting that SYK synthesizes serotonin/arachidonate or controls every platelet agonist. |
| GO:0097110 scaffold protein binding | IPI PMID:11606584 Tyrosine residues in phospholipase Cgamma 2 essential for th... | ACCEPT | Summary: SYK directly engages the BLNK scaffold and phosphorylates it in purified complex assays; sustained SYKβSLP65 association also has an adaptor component. Reason: SYK directly engages the BLNK scaffold and phosphorylates it in purified complex assays; sustained SYKβSLP65 association also has an adaptor component. Retain scaffold protein binding without assigning BLNKβs enzymeless scaffold mechanism to SYK as its sole function. The preserved original source is PMID:11606584. |
| GO:0097190 apoptotic signaling pathway | IMP PMID:22267217 Dectin-1 is an extracellular pathogen sensor for the inducti... | UNDECIDED | Summary: The accessible PMID:22267217 abstract and publisher figure headings establish a noncanonical caspase8 inflammasome for IL1beta processing, not an apoptosis assay. Reason: The accessible PMID:22267217 abstract and publisher figure headings establish a noncanonical caspase8 inflammasome for IL1beta processing, not an apoptosis assay. Caspase8 activation alone is not sufficient to infer apoptotic signaling. The complete article remains unavailable after normal PMID and publisher recovery, so retain source-specific uncertainty instead of declaring the experimental annotation false. The preserved original source is PMID:22267217. |
| GO:0097242 amyloid-beta clearance | IDA PMID:27477018 TREM2 Binds to Apolipoproteins, Including APOE and CLU/APOJ,... | UNDECIDED | Summary: PMID:27477018 directly describes TREM2-dependent uptake of amyloidβlipoprotein complexes, but the accessible abstract does not expose the specific SYK perturbation or construct assay underlying this IDA. Reason: PMID:27477018 directly describes TREM2-dependent uptake of amyloidβlipoprotein complexes, but the accessible abstract does not expose the specific SYK perturbation or construct assay underlying this IDA. Normal recovery and the publisher PDF attempt did not recover full text. Preserve the curatorβs claim as unresolved rather than treating a TREM2-focused abstract as proof that SYK was not tested. The preserved original source is PMID:27477018. Supporting Evidence: |
| GO:0120162 positive regulation of cold-induced thermogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Full PMID:29235464 uses mouse adipocyte-specific deletion and beta-agonist/inhibitor experiments to establish SYK-dependent brown-fat formation and thermogenic responses. Reason: Full PMID:29235464 uses mouse adipocyte-specific deletion and beta-agonist/inhibitor experiments to establish SYK-dependent brown-fat formation and thermogenic responses. Retain the explicitly comparative human attribution as non-core, not a direct human cold-challenge experiment or universal immune-cell function. Supporting Evidence: |
| GO:0120162 positive regulation of cold-induced thermogenesis | ISS PMID:29235464 SYK kinase mediates brown fat differentiation and activation... | KEEP AS NON CORE | Summary: Full PMID:29235464 uses mouse adipocyte-specific deletion and beta-agonist/inhibitor experiments to establish SYK-dependent brown-fat formation and thermogenic responses. Reason: Full PMID:29235464 uses mouse adipocyte-specific deletion and beta-agonist/inhibitor experiments to establish SYK-dependent brown-fat formation and thermogenic responses. Retain the explicitly comparative human attribution as non-core, not a direct human cold-challenge experiment or universal immune-cell function. The preserved original source is PMID:29235464. Supporting Evidence: |
| GO:0140374 antiviral innate immune response | IDA PMID:39694035 MYO1F positions cGAS on the plasma membrane to ensure full a... | KEEP AS NON CORE | Summary: PMID:39694035 explicitly links SYK phosphorylation of MYO1F to KAT2A recruitment, cGAS acetylation and antiviral signaling in human and mouse macrophages. Reason: PMID:39694035 explicitly links SYK phosphorylation of MYO1F to KAT2A recruitment, cGAS acetylation and antiviral signaling in human and mouse macrophages. Retain this defined cGAS/STING branch and antiviral context, rather than extrapolating from an unrelated DNA sensor or assigning cGAS catalytic activity to SYK. The preserved original source is PMID:39694035. Supporting Evidence: |
| GO:0141111 positive regulation of cGAS/STING signaling pathway | IDA PMID:39694035 MYO1F positions cGAS on the plasma membrane to ensure full a... | KEEP AS NON CORE | Summary: PMID:39694035 explicitly links SYK phosphorylation of MYO1F to KAT2A recruitment, cGAS acetylation and antiviral signaling in human and mouse macrophages. Reason: PMID:39694035 explicitly links SYK phosphorylation of MYO1F to KAT2A recruitment, cGAS acetylation and antiviral signaling in human and mouse macrophages. Retain this defined cGAS/STING branch and antiviral context, rather than extrapolating from an unrelated DNA sensor or assigning cGAS catalytic activity to SYK. The preserved original source is PMID:39694035. Supporting Evidence: |
| GO:1904263 positive regulation of TORC1 signaling | IDA PMID:34634301 Tyrosine phosphorylation of DEPTOR functions as a molecular ... | KEEP AS NON CORE | Summary: Full PMID:34634301 identifies SYK-dependent DEPTOR Tyr289 phosphorylation, reducing DEPTOR association with mTOR and increasing mTORC1/2 signaling in the tested ephrin/cell context. Reason: Full PMID:34634301 identifies SYK-dependent DEPTOR Tyr289 phosphorylation, reducing DEPTOR association with mTOR and increasing mTORC1/2 signaling in the tested ephrin/cell context. Retain the positive TORC1 regulatory process, without assuming the same sign during every starvation or immune stimulus. The preserved original source is PMID:34634301. Supporting Evidence: |
| GO:1904646 cellular response to amyloid-beta | IDA PMID:29518356 TREM2 Is a Receptor for Ξ²-Amyloid that Mediates Microglial F... | KEEP AS NON CORE | Summary: PMID:29518356 explicitly reports amyloid-enhanced TREM2βDAP12 interaction and downstream SYK phosphorylation. Reason: PMID:29518356 explicitly reports amyloid-enhanced TREM2βDAP12 interaction and downstream SYK phosphorylation. Retain the cellular amyloid-response attribution, distinguishing mouse microglial physiology and receptor/construct assays from a direct human brain experiment. This does not itself establish SYK-mediated amyloid clearance. The preserved original source is PMID:29518356. Supporting Evidence: |
| GO:1990858 cellular response to lectin | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Native mouse Dectin-1 experiments and human Candida/beta-glucan perturbation establish SYK-dependent cellular responses to fungal material and lectin-receptor engagement. Reason: Native mouse Dectin-1 experiments and human Candida/beta-glucan perturbation establish SYK-dependent cellular responses to fungal material and lectin-receptor engagement. Retain these stimulus-specific outcomes outside the molecular core, without making SYK the extracellular fungal-ligand-binding receptor. |
| GO:1990858 cellular response to lectin | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Native mouse Dectin-1 experiments and human Candida/beta-glucan perturbation establish SYK-dependent cellular responses to fungal material and lectin-receptor engagement. Reason: Native mouse Dectin-1 experiments and human Candida/beta-glucan perturbation establish SYK-dependent cellular responses to fungal material and lectin-receptor engagement. Retain these stimulus-specific outcomes outside the molecular core, without making SYK the extracellular fungal-ligand-binding receptor. |
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