{"subject": "NCBIGene:6714", "predicate": "biolink:related_to", "object": "NCBIGene:55971", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:21840312"], "description": ["Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility."], "original_subject": "UniProtKB:P12931", "original_object": "UniProtKB:Q9UHR4"}
{"subject": "NCBIGene:6714", "predicate": "biolink:regulates", "object": "NCBIGene:55971", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:21840312"], "description": ["Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility."], "object_direction_qualifier": "upregulates", "object_aspect_qualifier": "activity", "original_subject": "UniProtKB:P12931", "original_object": "UniProtKB:Q9UHR4"}
{"subject": "NCBIGene:7942", "predicate": "biolink:affects", "object": "NCBIGene:2629", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:28552616"], "description": ["Nucleus-Translocated ACSS2 Promotes Gene Transcription for Lysosomal Biogenesis and Autophagy|A chromatin immunoprecipitation (ChIP) assay with antibodies against TFEB or ACSS2 demonstrated that glucose deprivation results in the binding of TFEB (Figure 3D) and ACSS2 (Figure 3E) to the promoter regions of CTSA, GBA, GUSB, and LAMP1|These results indicated that TFEB and ACSS2 are mutually required for their binding to the promoter regions of lysosomal genes. In line with these findings, glucose deprivation induced mRNA (Figure 3F) and protein (Figure 3G) expression for these lysosomal genes, which was largely abrogated by knockin of ACSS2 mutants"], "qualified_predicate": "RO:0003303", "object_direction_qualifier": "increased", "object_aspect_qualifier": "expression", "original_subject": "UniProtKB:P19484", "original_object": "UniProtKB:P04062"}
{"subject": "CHEBI:135946", "predicate": "biolink:related_to", "object": "NCBIGene:886", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:31160049"], "description": ["Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0."], "species_context_qualifier": "NCBITaxon:9606", "anatomical_context_qualifier": "BTO:0002524", "original_subject": "PUBCHEM.COMPOUND:9833444", "original_object": "UniProtKB:P32238"}
{"subject": "CHEBI:135946", "predicate": "biolink:regulates", "object": "NCBIGene:886", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:31160049"], "description": ["Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0."], "species_context_qualifier": "NCBITaxon:9606", "anatomical_context_qualifier": "BTO:0002524", "object_direction_qualifier": "upregulates", "object_aspect_qualifier": "activity", "original_subject": "PUBCHEM.COMPOUND:9833444", "original_object": "UniProtKB:P32238"}
{"subject": "NCBIGene:5885", "predicate": "biolink:regulates", "object": "GO:0006281", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:20711430"], "description": ["Rad21-cohesin haploinsufficiency impedes DNA repair and enhances gastrointestinal radiosensitivity in mice"], "species_context_qualifier": "NCBITaxon:10090", "object_direction_qualifier": "upregulates", "object_aspect_qualifier": "activity", "original_subject": "UniProtKB:O60216", "original_object": "GO:0006281"}
{"subject": "CHEBI:31347", "predicate": "biolink:related_to", "object": "NCBIGene:7113", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:32142651"], "description": ["Ndeed, the clinically proven serine protease inhibitor camostat mesylate, which is active against TMPRSS2 (Kawase et al., 2012), partially blocked SARS-2-S-driven entry into Caco-2 (Figure S3 B) and Vero-TMPRSS2 cells, efficiently blocked 2019-nCoV-S-driven entry into Caco-2 (TMPRSS2+) but not 293T (TMPRSS2- 110 ) cells while the CatB/L inhibitor E64d had the opposite effect"], "species_context_qualifier": "NCBITaxon:9606", "original_subject": "PUBCHEM.COMPOUND:5284360", "original_object": "UniProtKB:O15393"}
{"subject": "CHEBI:31347", "predicate": "biolink:regulates", "object": "NCBIGene:7113", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:32142651"], "description": ["Ndeed, the clinically proven serine protease inhibitor camostat mesylate, which is active against TMPRSS2 (Kawase et al., 2012), partially blocked SARS-2-S-driven entry into Caco-2 (Figure S3 B) and Vero-TMPRSS2 cells, efficiently blocked 2019-nCoV-S-driven entry into Caco-2 (TMPRSS2+) but not 293T (TMPRSS2- 110 ) cells while the CatB/L inhibitor E64d had the opposite effect"], "species_context_qualifier": "NCBITaxon:9606", "object_direction_qualifier": "downregulates", "object_aspect_qualifier": "activity", "original_subject": "PUBCHEM.COMPOUND:5284360", "original_object": "UniProtKB:O15393"}
{"subject": "NCBIGene:4843", "predicate": "biolink:regulates", "object": "CHEBI:16349", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:7537672"], "description": ["Activation with lipopolysaccharide induces macrophages to produce the enzymes arginase and nitric oxide (NO) synthase. Both enzymes use as a substrate the ammino acid L-arginine, which can be either hydrolyzed by arginase to urea and ornithine or oxidized by NO synthase to NO and citrulline"], "species_context_qualifier": "NCBITaxon:9606", "object_direction_qualifier": "upregulates", "original_subject": "UniProtKB:P35228", "original_object": "PUBCHEM.COMPOUND:9750"}
{"subject": "NCBIGene:10908", "predicate": "biolink:related_to", "object": "CHEBI:138424", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:25033069"], "description": ["PNPLA6 encodes NTE, a lysophospholipase that converts lysophosphatidylcholine (LPC) to glycerophosphocholine. PNPLA6 is expressed in neurons throughout the brain, particularly in the cortex, Purkinje cells of the cerebellum, and hippocampus"], "species_context_qualifier": "NCBITaxon:9606", "original_subject": "UniProtKB:Q8IY17", "original_object": "PUBCHEM.COMPOUND:5311264"}
{"subject": "NCBIGene:8557", "predicate": "biolink:related_to", "object": "GO:0045214", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:9804419"], "description": ["The giant muscle protein titin (connectin) is essential in the temporal and spatial control of the assembly of the highly ordered sarcomeres (contractile units) of striated muscle. "], "species_context_qualifier": "NCBITaxon:9606", "anatomical_context_qualifier": "BTO:0001103", "original_subject": "UniProtKB:O15273", "original_object": "GO:0045214"}
{"subject": "GO:0006909", "predicate": "biolink:regulates", "object": "NCBIGene:7040", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:22933625"], "description": ["Furthermore, phagocytosis of apoptotic neutrophils by M1 macrophages increased production of the Th2 cytokine TGFβ by the macrophages, while reducing expression of the Th1 cytokines IL-1β and TNF-α, reflecting a shift toward an M2 phenotype"], "anatomical_context_qualifier": "BTO:0000801", "object_direction_qualifier": "upregulates", "object_aspect_qualifier": "abundance", "original_subject": "GO:0006909", "original_object": "UniProtKB:P01137"}
{"subject": "NCBIGene:7343", "predicate": "biolink:affects", "object": "GO:0009303", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:7877691"], "description": ["Rb specifically inhibits the activity of the RNA polymerase I transcription factor UBF (upstream binding factor) in vitro. |These results indicate that there is an additional mechanism by which Rb suppresses cell growth, namely that Rb directly represses transcription of the rRNA genes."], "species_context_qualifier": "NCBITaxon:9606", "anatomical_context_qualifier": "BTO:0001412", "qualified_predicate": "RO:0003303", "object_direction_qualifier": "increased", "object_aspect_qualifier": "expression", "original_subject": "UniProtKB:P17480", "original_object": "GO:0009303"}
{"subject": "NCBIGene:51533", "predicate": "biolink:in_complex_with", "object": "NCBIGene:6604", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:33941892"], "description": ["Mechanistically, PHF7 localizes to cardiac super enhancers in fibroblasts, and through cooperation with the SWI/SNF complex, it increases chromatin accessibility and transcription factor binding at these sites. Furthermore, PHF7 recruits cardiac transcription factors to activate a positive transcriptional autoregulatory circuit in reprogramming. PHF7 interacts with SMARCD3 to promote reprogramming."], "species_context_qualifier": "NCBITaxon:9606", "original_subject": "UniProtKB:Q9BWX1", "original_object": "UniProtKB:Q6STE5"}
{"subject": "NCBIGene:51533", "predicate": "biolink:directly_physically_interacts_with", "object": "NCBIGene:6604", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:33941892"], "description": ["Mechanistically, PHF7 localizes to cardiac super enhancers in fibroblasts, and through cooperation with the SWI/SNF complex, it increases chromatin accessibility and transcription factor binding at these sites. Furthermore, PHF7 recruits cardiac transcription factors to activate a positive transcriptional autoregulatory circuit in reprogramming. PHF7 interacts with SMARCD3 to promote reprogramming."], "species_context_qualifier": "NCBITaxon:9606", "original_subject": "UniProtKB:Q9BWX1", "original_object": "UniProtKB:Q6STE5"}
{"subject": "NCBIGene:1633", "predicate": "biolink:related_to", "object": "GO:0044818", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:27879648"], "description": ["Deoxycytidine kinase (dCK) is a key enzyme in deoxyribonucleoside salvage and the anti-tumor activity for many nucleoside analogs. dCK is activated in response to ionizing radiation (IR)-induced DNA damage and it is phosphorylated on Serine 74 by the Ataxia-Telangiectasia Mutated (ATM) kinase in order to activate the cell cycle G2/M checkpoint."], "original_subject": "UniProtKB:P27707", "original_object": "GO:0044818"}
{"subject": "NCBIGene:1633", "predicate": "biolink:regulates", "object": "GO:0044818", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:27879648"], "description": ["Deoxycytidine kinase (dCK) is a key enzyme in deoxyribonucleoside salvage and the anti-tumor activity for many nucleoside analogs. dCK is activated in response to ionizing radiation (IR)-induced DNA damage and it is phosphorylated on Serine 74 by the Ataxia-Telangiectasia Mutated (ATM) kinase in order to activate the cell cycle G2/M checkpoint."], "object_direction_qualifier": "upregulates", "original_subject": "UniProtKB:P27707", "original_object": "GO:0044818"}
{"subject": "GO:0042119", "predicate": "biolink:regulates", "object": "GO:0043312", "primary_knowledge_source": "infores:signor", "knowledge_level": "knowledge_assertion", "agent_type": "manual_agent", "publications": ["PMID:2161532"], "description": ["ANCA cause normal human neutrophils to undergo an oxidative burst and degranulate. Both ANCA phenotypes (i.e., cytoplasmic-pattern ANCA and myeloperoxidase-specific ANCA) induce neutrophil activation."], "species_context_qualifier": "NCBITaxon:9606", "anatomical_context_qualifier": "BTO:0000133", "object_direction_qualifier": "upregulates", "original_subject": "GO:0042119", "original_object": "GO:0043312"}