The interaction of RPTP-alpha and the SH2 domain of Fyn induces an interaction of Fyn Tyr531 with the D1 domain of RPTP-alpha. This induces dephosphorylation of Tyr531 and activates Fyn.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [ "R-HSA-388755" ], "output_participant_list": [], "enzyme_list": [ "P06241-1", "P18433-5" ], "evidence": [ { "id": "R-HSA-391868", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-391868" } ] }, { "id": "R-HSA-391871", "name": "Autophosphorylation of NCAM1 bound Fyn", "equation": "", "summary": "The Tyr420 residue located in the activation loop of Fyn is responsible for its enzymatic activity. Once the Tyr531 in its negative regulatory site is dephosphorylated by RPTPalpha, Fyn undergoes autophosphorylation on Tyr420 for its maximum activity.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P06241-1", "P18433-5" ], "evidence": [ { "id": "R-HSA-391871", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-391871" } ] }, { "id": "R-HSA-392051", "name": "Recruitment of Grb2 to pFAK:NCAM1", "equation": "", "summary": "Phosphorylated tyrosine 925 in the FAT domain of PTK2/FAK creates a docking site for the SH2 domain of GRB2 and recruits the GRB2/SOS complex. PTK2 may use this mechanism to activate Ras and the MAP kinase pathway.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P06241-1", "P18433-5", "Q05397-1" ], "evidence": [ { "id": "R-HSA-392051", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-392051" } ] }, { "id": "R-HSA-392053", "name": "SOS binds Grb2 bound to pFAK:NCAM1", "equation": "", "summary": "Guanine nucleotide releasing factor Sos associates with FAK bound Grb2 to activate Ras and initiate Ras-MAPK signaling. This interaction occurs between the carboxy terminal domain of SOS and the Src homology 3 (SH3) domains of GRB2.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P06241-1", "P18433-5", "Q05397-1" ], "evidence": [ { "id": "R-HSA-392053", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-392053" } ] }, { "id": "R-HSA-392054", "name": "NCAM1:pFAK:Grb2:Sos-mediated nucleotide exchange of Ras", "equation": "", "summary": "The guanine nucleotide exchange factor SOS interacts with GRB2 bound to phosphorylated FAK bound to NCAM. Upon formation of this complex, SOS activates Ras by promoting GDP release and GTP binding.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P01111-1", "P06241-1", "P01112-1", "P18433-5", "Q05397-1" ], "evidence": [ { "id": "R-HSA-392054", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-392054" } ] }, { "id": "R-HSA-3928580", "name": "SFKs phosphorylate EFNBs", "equation": "", "summary": "The Src-family kinases (SFKs) SRC and FYN, colocalised with ephrinBs (EFNBs) at the membrane, are required for EFNB phosphorylation. The cytoplasmic domains of all three EFNBs consist of five conserved tyrosine residues of which three undergo phosphorylation. Electrospray tandem mass spectrometry and site-directed mutagenesis identified tyrosines 312, 317, and 331 (human 324, 329 and 343) of EFNB1 as phosphorylation sites (Kalo et al. 2001, Palmer et al. 2002).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P06241-1", "P29323-1", "P54760-1", "P54753-1", "P54762-1" ], "evidence": [ { "id": "R-HSA-3928580", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928580" } ] }, { "id": "R-HSA-3928583", "name": "FYN phosphorylates NMDAR2B", "equation": "", "summary": "Protein phosphorylation is an important mechanism modulating the function of NMDA receptors (NMDARs). SRC-family kinases that associate with EPHB are important for the phosphorylation of ionotropic glutamate receptor, NR2B (NMDAR2B, GRIN2B) Tyrosines 1252, 1336, and 1474 (1252, 1336, and 1472 in mouse) on NR2B are phosphorylated by FYN/SRC bound to EPHB2, thereby enhancing NMDA-dependent calcium influx upon glutamate stimulation (Takasu et al. 2002, Dalva et al. 2000). Tyrosine phosphorylation of NMDAR2B also regulates the surface expression of NMDARs. EPHB mediated phosphorylation of NMDARs can also increase the surface retention of NMDAR2B-containing NMDARs by preventing clathrin-dependent endocytosis. Phosphorylation at tyrosine 1474 (mouse Y1472) of NMDAR2B blocks binding of the mu2 subunit of clathrin adaptor protein 2 (AP2) complex thus preventing clathrin-dependent endocytosis (Chen & Roche 2007).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P06241-1", "P07947-1", "P07948-1", "P29323-1", "P54760-1", "P54753-1", "P54762-1" ], "evidence": [ { "id": "R-HSA-3928583", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928583" } ] }, { "id": "R-HSA-3928584", "name": "p-EPHs bind SRC,FYN,YES,LYN", "equation": "", "summary": "Src family kinases (SFKs) are one of the important components of EPH receptor-mediated axon guidance. Inhibition of SFK-mediated phosphorylation in retinal axons, abolishes EPHA-mediated repulsion in stripe and growth cone collapse assays (Knoll & Drescher 2004). Several members of the Src family, including SRC, FYN, LYN and YES, are expressed widely in the same places as EPH receptors. Autophosphorylated tyrosines in the juxtamembrane region of the EPH receptors have been shown to be critical for the association of the SRC and FYN SH2 domain (Ellis et al. 1996, Zisch et al. 1998). These SFKs are involved in the phosphorylation of RhoGEF ephexin1 and cortactin (Knoll & Drescher 2004). This event is deduced on the basis of experimental evidence from chicken assay studies (Knoll & Drescher 2004).
Specifically, activated EPHA4 was shown to form a complex with FYN and LYN kinases (Prevost et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P29320-1",
"P29323-1",
"Q5JZY3-1",
"P54764-1",
"P54760-1",
"P29317-1",
"P29322-1",
"P54753-1",
"P54756-1",
"P54762-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928584",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928584"
}
]
},
{
"id": "R-HSA-3928594",
"name": "SFKs phosphorylate GIT1",
"equation": "",
"summary": "G-protein-coupled receptor kinase-interacting protein 1 (GIT1) has been shown to be critical for spine morphogenesis and synapse formation through assembling and targeting multiprotein signaling complexes, which contain important actin regulators including PIX, Rac GEF, and PAK, between the sub-cellular compartments (Zhang et al. 2003). Activation of ephrinBs (EFNBs) by EPHB receptors may lead to the phosphorylation of GIT1 on Tyr392 (in humans Tyr385, based on sequence similarity). The Src-family kinases (SFKs) recruited to EFNB expression domains are involved in this phosphorylation. Tyr392 in the N-terminal of the SLD domain is required for GIT1s binding to the SH2 domain of GRB4 (Segura et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [
"R-HSA-430326"
],
"output_participant_list": [
"R-HSA-3928463"
],
"enzyme_list": [
"P06241-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928594",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928594"
}
]
},
{
"id": "R-HSA-3928602",
"name": "NGEF binds EPHA",
"equation": "",
"summary": "Ephexin1/NGEF (Neuronal guanine nucleotide exchange factor) is a member of the Dbl family of guanine nucleotide exchange factors (GEFs) for Rho GTPases, which interacts with cytoplasmic domain of EPHAs. NGEF is highly expressed in the CNS during development and is enriched in neuronal growth cones. NGEF binds to the kinase domain of EPHA through its Dbl homology (DH)-pleckstrin-homology (PH) domains and this binding does not require activation of the receptor. EPHA activation by ephrinA ligands increases the catalytic activity of ephexin1 resulting in enhanced RHOA activation in cortical neurons (Noren & Pasquale 2004, Shamah et al. 2001). Ephrin-A1 also induces the dispersal of acetylcholine receptors clusters at the neuromuscular junction through the activation of NGEF and RhoA (Shi et al., 2010). NGEF is involved in both axonal growth,growth cone collapse, dendritic spine elimination and stabilization of the neuromuscular junction. In the absence of ephrin stimulation, NGEF promotes actin polymerization and axonal growth by stimulating RHOA, RAC1 and CDC42. Whereas in the presence of ephrin stimulation, NGEF induces growth cone collapse by activating RHOA, but not RAC1 and CDC42 (Shamah et al. 2001, Sahin et al. 2005).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P29320-1",
"Q5JZY3-1",
"P54764-1",
"P29317-1",
"P29322-1",
"P54756-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928602",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928602"
}
]
},
{
"id": "R-HSA-3928604",
"name": "SFKs phosphorylate VAV2,3",
"equation": "",
"summary": "Upon ephrin (EFN)-mediated stimulation, proto-oncogene vav (VAV) is transiently tyrosine phosphorylated and activated in neurons, possibly by Src family kinases (SFKs). VAV2 and VAV3 are phosphorylated on Y172 and Y173 respectively in the acidic domain and this phosphorylation disrupts the inhibitory interaction of the acidic domain with the DH domain (Cowan et al. 2005, Marignani & Carpenter 2001).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P29320-1",
"P29323-1",
"Q5JZY3-1",
"P54764-1",
"P54760-1",
"P29317-1",
"P29322-1",
"P54753-1",
"P54756-1",
"P54762-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928604",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928604"
}
]
},
{
"id": "R-HSA-3928607",
"name": "p-EPHs bind VAV2,3",
"equation": "",
"summary": "The alternate method required for the initial EPH receptor:ephrin (EPH:EFN) adhesion into repulsion is by RAC-dependent endocytosis, an atypical endocytic mechanism by which the EPH:EFN complex and surrounding plasma membrane are internalized into one cell. Proto-oncogene vavs (VAVs) provide a molecular link between activated EPHs and RAC-dependent endocytosis. Upon the activation of EPH receptor, VAV proteins are recruited to the intracellular domain of EPHs and become transiently activated. Cowan et al. showed that VAV2 interacts with either EPHA4 or EPHB2, indicating that VAV can bind to either EPHA or EPHB subclass receptors. Autophosphorylated juxta-membrane tyrosines (Y596 and Y602 of human EPHA4) provide docking sites for VAV proteins (Cowan et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P29320-1",
"P29323-1",
"Q5JZY3-1",
"P54764-1",
"P54760-1",
"P29317-1",
"P29322-1",
"P54753-1",
"P54756-1",
"P54762-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928607",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928607"
}
]
},
{
"id": "R-HSA-3928614",
"name": "EFNB:GRB4 binds GIT1",
"equation": "",
"summary": "G-protein-coupled receptor kinase-interacting protein 1 (GIT1) is enriched in both presynaptic and postsynaptic terminals and after phosphorylation is targeted to the synapse by binding to cytoplasmic protein GRB4 (NCK2 aka GRB4). GRB4 binds by its SH2 domain to Tyr392 (Human Tyr383) in the synaptic localization domain (SLD) of GIT1. GIT1 acts as an adapter protein by providing docking site for beta-PIX (PAK interacting exchange factor) and serves to localize Rac activity (Segura et al. 2007, Zhang et al. 2003).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928614",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928614"
}
]
},
{
"id": "R-HSA-3928615",
"name": "EFNBs bind SFKs",
"equation": "",
"summary": "Src-family kinases (SFKs) are required for ephrinB (EFNB)-mediated axon guidance and angiogenic responses in endothelial cells. Following interaction with their cognate EPHB receptors and formation of circular tetramers and higher order clusters, EFNBs recruit SFKs and become tyrosine phosphorylated on the cytoplasmic tail. SFK recruitment and activation represents one of the first events in EFNB reverse signaling (Palmer et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928615",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928615"
}
]
},
{
"id": "R-HSA-3928623",
"name": "EPHBs bind NMDARs",
"equation": "",
"summary": "EPHBs are involved in spine synapse formation and also for the recruitment and clustering of glutamate receptors to synapses. At the time of synaptogenesis, EPHBs are localized to the postsynaptic region of excitatory synapses. These postsynaptic EPHBs, upon activation by presynaptic ephrinBs (EFNBs), directly interact with ionotropic glutamate receptor, NR1 and NR2B (NMDAR1and 2B aka GRIN1and 2B). The interaction between EPHB and NMDARs is mediated by the extracellular domains of these two proteins. This interaction promotes clustering of NMDARs at synaptic locations and leads to the formation of functional presynaptic release sites. Activated EPHBs function as tyrosine kinases and may also indirectly potentiate NMDAR-mediated calcium influx (Dalva et al. 2000, Takasu et al. 2002).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07947-1",
"P07948-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928623",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928623"
}
]
},
{
"id": "R-HSA-3928625",
"name": "PAKs autophosphorylate",
"equation": "",
"summary": "PAK is also locally activated in the synapse. PAK1 needs autophosphorylation for complete activation. PAK1 is autophosphorylated at several sites, but serine 144 (S144) in the GTPase-binding domain and threonine 423 (T423) in the activation loop are the two conserved sites that regulate the catalytic activity (Bokoch 2003).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P63000-1",
"Q13153-1",
"Q13177-1",
"P29323-1",
"P54760-1",
"O75914-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928625",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928625"
}
]
},
{
"id": "R-HSA-3928627",
"name": "EPHB phosphorylates TIAM1",
"equation": "",
"summary": "Once recruited to the EPHB:NMDAR complex, T-lymphoma invasion and metastasis-inducing protein 1 (TIAM1) is phosphorylated on tyrosine 829 by either EPHB or a kinase that associates with activated EPHB. TIAM1 may then activate Rac1, leading to actin cytoskeletal remodelling required for spine development and morphogenesis (Tolias et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07947-1",
"P07948-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928627",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928627"
}
]
},
{
"id": "R-HSA-3928628",
"name": "VAV exchanges GTP for GDP on RAC1, activating it",
"equation": "",
"summary": "Activated proto-oncogene vav (VAV) act as guanine nucleotide exchange factors (GEFs) for RAC1, catalysing the exchange of bound GDP for GTP. Endocytosis of large EPH:EFN complexes is dependent on RAC1-regulated actin polymerization. RAC1 signaling is positively linked to EPH:EFN internalization but the exact link to clathrin endocytosis machinery remains unclear. Inhibiting RAC1 signalling and Arp2/3-driven actin polymerization in EPH receptor-expressing cells completely blocks both endocytosis of EPH:EFN complexes and cell retraction (Marston et al. 2003). In response to repulsive guidance molecules, the function of RAC1 changes from promoting actin polymerization associated with axon growth to driving endocytosis of the plasma membrane, resulting in growth cone collapse (Jurney et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P63000-1",
"P07947-1",
"P07948-1",
"P29320-1",
"P29323-1",
"Q5JZY3-1",
"P54764-1",
"P54760-1",
"P29317-1",
"P29322-1",
"P54753-1",
"P54756-1",
"P54762-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928628",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928628"
}
]
},
{
"id": "R-HSA-3928631",
"name": "GIT1 binds bPIX",
"equation": "",
"summary": "p-21-activated kinase (PAK) interacting exchange factor (beta-PIX, bPIX aka ARHGEF7) is a Rac guanine nucleotide exchange factor that acts downstream of GIT1 to affect spine morphology and synapse formation. Endogenous bPIX is present in hippocampal neurons and is targeted to the synapses by binding to GIT1. bPIX serves as an exchange factor for Rac and a binding protein for a Rac effector, PAK (Zhang et al. 2003).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928631",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928631"
}
]
},
{
"id": "R-HSA-3928633",
"name": "bPIX exchanges GTP for GDP on RAC, activating it",
"equation": "",
"summary": "p-21-activated kinase (PAK) interacting exchange factor (beta-PIX, bPIX aka ARHGEF7) a Rac GEF localised at the dendritic spines, activates Rac by exchanging GDP for GTP.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P63000-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928633",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928633"
}
]
},
{
"id": "R-HSA-3928639",
"name": "p-EFNB binds GRB4",
"equation": "",
"summary": "Unlike EPH receptors, ephrinBs (EFNBs) do not possess intrinsic catalytic activity and thus rely on the recruitment of signaling molecules to signal. Phosphorylated ephrinB (p-EFNB) provides docking site for the SH2/SH3 domain-containing adapter protein cytoplasmic protein NCK2 (NCK2 aka GRB4) (Cowan & Henkemeyer 2001). GRB4 is able to bind to phosphotyrosines in EFNBs through their SH2 domains and 'PxxP' motifs through their SH3 domains. It has been postulated that GRB4 acts as a bridge between EFNBs and G protein-coupled receptor kinase interacting protein (GIT) 1 and Rac at synapses (Segura et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928639",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928639"
}
]
},
{
"id": "R-HSA-3928640",
"name": "PAKs phosphorylate MLC",
"equation": "",
"summary": "Myosin II regulatory light chain (MLC) acts downstream of serine/threonine-protein kinase PAK (PAK) to mediate its effect on spine morphogenesis and excitatory synapse formation. PAK directly phosphorylates MLC on serine 19. MLC phosphorylation could promote dendritic spine morphogenesis by stabilizing the actin network at this site (Zhang et al. 2005).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [
"R-HSA-390735"
],
"output_participant_list": [
"R-HSA-390749"
],
"enzyme_list": [
"P06241-1",
"P63000-1",
"Q13153-1",
"Q13177-1",
"P29323-1",
"P54760-1",
"O75914-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928640",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928640"
}
]
},
{
"id": "R-HSA-3928641",
"name": "PAK binds RAC and bPIX",
"equation": "",
"summary": "Serine/threonine-protein kinases PAK1, 2 and 3 (PAK1,2,3) serve as downstream effectors of RACs in regulating spine and synapse formation. Once activated, Ras-related C3 botulinum toxin substrate 1 (RAC1) binds to a variety of downstream effector proteins. Among the most well characterized effectors are PAKs. In addition to binding active RAC, PAKs also directly bind p-21-activated kinase (PAK) interacting exchange factor (beta-PIX, bPIX aka ARHGEF7) (Zhang et al. 2005).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P63000-1",
"Q13153-1",
"Q13177-1",
"P29323-1",
"P54760-1",
"O75914-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928641",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928641"
}
]
},
{
"id": "R-HSA-3928642",
"name": "TIAM1 exchanges GTP for GDP on RAC1, activating it",
"equation": "",
"summary": "Activation of EPH receptors triggers the local activation of T-lymphoma invasion and metastasis-inducing protein 1 (TIAM1) and this in turn activates RAC1 (Yoo et al. 2010). RAC1 signaling is positively linked to EPH:ephrin (EFN) internalization but the exact link to clathrin endocytosis machinery remains unclear. TIAM1 co-localizes with the ARP2/3 complex at sites of actin polymerization. RAC1 activated by TIAM1 then subsequently activates the ARP2/3 complex proteins leading to actin polymerization (Ten Klooster et al. 2006).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P63000-1",
"P07947-1",
"P07948-1",
"P29320-1",
"Q5JZY3-1",
"P54764-1",
"P29317-1",
"P29322-1",
"P54756-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928642",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928642"
}
]
},
{
"id": "R-HSA-3928645",
"name": "EPHB:NMDAR binds TIAM1",
"equation": "",
"summary": "T-lymphoma invasion and metastasis-inducing protein 1 (TIAM1) is a Rac1-specific GEF, highly expressed in the nervous system, which is necessary for proper spinal and synapse development. It is one of the critical mediators of NMDA receptor (NMDAR)-dependent spine development (Tolias et al. 2005). TIAM1 might also play a role in regulating EPHB-dependent spine morphogenesis. TIAM1 appears to be required for ephrinB (EFNB)-induced increase in spine density. TIAM1 is recruited to EPHB complexes containing NMDAR after EPHB receptor activation in neurons. The PH-CC-Ex (consisting of a pleckstrin homology (PH) domain followed by a coiled-coiled (CC) domain and an adjacent region (Ex) domain) of TIAM1 is required for binding to EPHB2 (Tolias et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07947-1",
"P07948-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-3928645",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928645"
}
]
},
{
"id": "R-HSA-3928648",
"name": "SFKs phosphorylate NGEF",
"equation": "",
"summary": "Activation of EPHAs leads to phosphorylation of ephexin1 (NGEF) on conserved tyrosine (Y) 179 (Y87 in isoform3) by Src family kinases (SFKs). This phosphorylation preferentially activates NGEF\u2019s GDP/GTP exchange activity specifically towards RHOA but not RAC1 and CDC42, thus switching the substrate preference of NGEF and leading to actin cytoskeletal changes that result in growth cone collapse (Sahin et al. 2005, Knoll and Drescher 2004).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P29320-1",
"Q5JZY3-1",
"P54764-1",
"P29317-1",
"P29322-1",
"P54756-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928648",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928648"
}
]
},
{
"id": "R-HSA-3928651",
"name": "NGEF exchanges GTP for GDP on RHOA",
"equation": "",
"summary": "The tyrosine phosphorylation of ephexin1 (NGEF)/Ephexin-1 enhances its exchange activity and specifically activates inactive RHOA:GDP to active RHOA:GTP. Activated RHOA regulates myosin II activity in neurons through Rho-associated kinase (ROCK), and leads to rapid growth cone collapse, neurite retraction, or neurite growth inhibition in axons. Through this repulsive mechanism EPH receptors and ephrins (EFNs) guide retinal axons to their targets in the visual centres in the brain (Sahin et al. 2005).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P61586-1",
"P29320-1",
"Q5JZY3-1",
"P54764-1",
"P29317-1",
"P29322-1",
"P54756-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-3928651",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3928651"
}
]
},
{
"id": "R-HSA-399928",
"name": "Recruitment of Rnd1 to Plexin A",
"equation": "",
"summary": "Binding of Sema3A to the Neuropilin-1-Plexin-A receptor complex results in the recruitment of Rnd1 to the cytoplasmic linker region of Plexin-A. Rnd1 activates the cytoplasmic GTPase signaling domain of Plexin-A.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P63000-1",
"P07332-1"
],
"evidence": [
{
"id": "R-HSA-399928",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399928"
}
]
},
{
"id": "R-HSA-399930",
"name": "Activation of PAK by Rac1",
"equation": "",
"summary": "Plexin-bound Rac1 binds to and stimulates the kinase activity of PAK. PAK dimers are arranged in head-to-tail fashion, in which the catalytic domain binds the kinase inhibitory (KI) domain and is supported by associated PAK-interacting exchange factor (PIX) dimers. Upon Rac1 binding the kinase undergoes conformational change that allows autophosphorylation. Phosphorylation of serine residues disables the KI-domain-kinase interaction and thereby reduces the affinity of PIX.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P63000-1",
"P07332-1",
"Q13153-1",
"Q13177-1",
"O75914-1"
],
"evidence": [
{
"id": "R-HSA-399930",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399930"
}
]
},
{
"id": "R-HSA-399931",
"name": "Activation of Fyn",
"equation": "",
"summary": "PlexinA1 and A2 are constitutively bound to the src family tyrosine kinase, Fyn. Stimulation with Sema3A causes Fyn activation and leads to the recruitment of Cdk5 into the complex.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1"
],
"evidence": [
{
"id": "R-HSA-399931",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399931"
}
]
},
{
"id": "R-HSA-399933",
"name": "Sema3A binds Nrp-1 bound to PlexinA",
"equation": "",
"summary": "Although neuropilin-1 is required for Sema-3A action, it is incapable of transmitting a Sema-3A signal to the growth cone interior. The function of Sema-3A is mediated by Plexins. Sema-3A binds with high affinity to Plexin when the latter is complexed with Neuropilin-1.
Plexin-A1 is known to act as an R-Ras GAP (GTPase activating protein) when bound by Sema-3A. Plexin's GAP activity is regulated by FARP2 mediated Rac1 activation. Sema-3A binding to neuropilin-1/Plexin-A1 seems to induce a conformational change of plexin-A1 necessary for releasing FARP2. This suggests that neuropilin1 is required not only for ligand binding, but also for signaling, by modulating the interaction of FARP2 with plexin-A1.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1"
],
"evidence": [
{
"id": "R-HSA-399933",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399933"
}
]
},
{
"id": "R-HSA-399934",
"name": "Phosphorylation of Plexin-A",
"equation": "",
"summary": "Sema3A binding to Neuropilin-1:Plexin-A complex results in conformational change of plexin-A and this conformational change permits Fes nonreceptor tyrosine kinase to bind and phosphorylate Plexin-A. The specific tyrosine residues phosphorylated in the cytoplasmic domain of plexins in response to semaphorin stimulation have not yet been identified.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [
"R-HSA-396937"
],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07332-1"
],
"evidence": [
{
"id": "R-HSA-399934",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399934"
}
]
},
{
"id": "R-HSA-399935",
"name": "Inactivation of R-Ras by Sema3A-Plexin-A GAP activity",
"equation": "",
"summary": "Plexin-A's are GAPs for the Ras family GTPase R-Ras. On stimulation with Rnd-1, plexin-A directly and specifically down regulates R-Ras activity. R-Ras activity is critical for PI3K activation and ECM-mediated beta1 integrin activation and cell migration. Inactivation of R-Ras by Sema3A/Plexin-A1 reduces integrin-mediated adhesions. It has been suggested that the final step in the Sema3A repulsive signaling pathway is inhibition of integrin activity. Reduced integrin activity allows detachment from the substratum and subsequent cell retraction.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P63000-1",
"P07332-1",
"P10301-1"
],
"evidence": [
{
"id": "R-HSA-399935",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399935"
}
]
},
{
"id": "R-HSA-399939",
"name": "Autophosphorylation of PAK",
"equation": "",
"summary": "PAK is autophosphorylated at several sites but S-144 flanking the kinase inhibitor region and T-423 (S-141/T-402 in PAK-gamma) within the catalytic domain are the two conserved sites that regulate the catalytic activity.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P63000-1",
"P07332-1",
"Q13153-1",
"Q13177-1",
"O75914-1"
],
"evidence": [
{
"id": "R-HSA-399939",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399939"
}
]
},
{
"id": "R-HSA-399941",
"name": "Rac1 binds PlexinA",
"equation": "",
"summary": "Active Rac1 associates directly with Plexin-A1 in the linker region separating Plexin-A1's cytoplasmic GAP domains. Rac1 association relieves an inhibitory intramolecular interaction between the two Plexin-A1 GAP domains C1 and C2.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P63000-1",
"P07332-1"
],
"evidence": [
{
"id": "R-HSA-399941",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399941"
}
]
},
{
"id": "R-HSA-399942",
"name": "Plexin-A1-4 binds NRP1",
"equation": "",
"summary": "The best characterized receptors for mediating semaphorin signaling are members of the neuropilin and plexin families of transmembrane proteins. Neuropilins form complexes with Plexin-A which in turn can act as a signaling moiety. Also, when complexed with neuropilin-1, plexin-A1 can associate directly with the FERM domain containing guanine nucleotide exchange factor (GEF) FARP2. FARP2 exerts GEF activity for Rac but not Cdc42 and Rho.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1"
],
"evidence": [
{
"id": "R-HSA-399942",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399942"
}
]
},
{
"id": "R-HSA-399944",
"name": "Phosphorylation of CRMPs by Cdk5",
"equation": "",
"summary": "Cdk5:p35 complex is associated with Plexin-A through the actived form of Fyn. CRMPs are the downstream substrates for Cdk5. Cdk5 phosphorylates serine 522 of CRMPs. Phosphorylation of CRMPs mediates the Sema3A induced growth cone collapse.
Collapsin response mediator proteins (CRMPs) are five homologous cytosolic phosphoproteins (CRMP1\u20135) involved in neuronal differentiation and axonal guidance. These members oligomerize and exist as tetramers.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"Q00535-1"
],
"evidence": [
{
"id": "R-HSA-399944",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399944"
}
]
},
{
"id": "R-HSA-399946",
"name": "Recruitment and activation of Cdk5",
"equation": "",
"summary": "Cyclin-dependent kinase 5 (CDK5), a member of the serine/threonine kinase Cdk family, is complexed with p35 a neuron specific activator of Cdk5. The complex CDK5:p35 is required for neurite outgrowth and cortical lamination. CDK5:p35 complex is recruited to the growth cone by associating with active Fyn. FYN promotes the kinase activity of CDK5 by phosphorylating CDK5 on tyrosine residue 15. Activation of CDK5 by FYN via Tyr15 phosphorylation might facilitate suppression of RAC-PAK signaling downstream of PlexinA.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"Q00535-1"
],
"evidence": [
{
"id": "R-HSA-399946",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399946"
}
]
},
{
"id": "R-HSA-399947",
"name": "Tyrosine phosphorylation of CRMPs by Fes",
"equation": "",
"summary": "Fes bound to Plexin-A is able to phosphorylate all five forms of CRMP, though neither specific sites nor the consequence of tyrosine phosphorylation in CRMP's have yet been investigated directly.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07332-1"
],
"evidence": [
{
"id": "R-HSA-399947",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399947"
}
]
},
{
"id": "R-HSA-399951",
"name": "Phosphorylation of CRMPs by GSK3beta",
"equation": "",
"summary": "The phosphorylation of CRMPs at Ser522 allows the subsequent phosphorylation of CRMP1, CRMP2 and CRMP4 at Ser518, Thr509, and Thr514 mediated by serine/threonine kinase GSK3beta. Phosphorylation of CRMP by GSK3beta results in decreased CRMP affinity for beta-tubulin and changes in microtubule dynamics.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P49841-1",
"Q00535-1"
],
"evidence": [
{
"id": "R-HSA-399951",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399951"
}
]
},
{
"id": "R-HSA-399952",
"name": "Phosphorylation of LIMK-1 by PAK",
"equation": "",
"summary": "LIM kinases are serine protein kinases with a unique combination of two N-terminal LIM motifs, a central PDZ domain, and a C-terminal protein kinase domain. LIMK1 is one of the downstream targets of PAK1 and is activated through phosphorylation by PAK1 on T508 within its activation loop (Edwards et al. 1999, Aizawa et al. 2001). LIM-kinase is responsible for the tight regulation of the activity of cofilin (a protein that depolymerizes actin filaments) and thus maintains the balance between actin assembly and disassembly. Phosphorylated cofilin is inactive, resulting in stabilization of the actin cytoskeleton.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P53667-1",
"P06241-1",
"P63000-1",
"P07332-1",
"Q13153-1",
"Q13177-1",
"O75914-1"
],
"evidence": [
{
"id": "R-HSA-399952",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-399952"
}
]
},
{
"id": "R-HSA-4093327",
"name": "EPHA binds TIAM1",
"equation": "",
"summary": "T-lymphoma invasion and metastasis-inducing protein 1 (TIAM1) is a GEF exhibiting highest specificity for RAC1 and is critically involved in EPH/ephrin (EFN)-mediated neurite outgrowth and dendritic spine development (Tanaka et al. 2004, Tolias et al. 2007). TIAM1 has a role in regulating the endocytosis of EPHA receptors, by regulating the RAC1 signaling downstream of the EPHA8 receptor. Yoo and his colleagues found that TIAM1, a RAC-specific guanine nucleotide exchange factor, co-immunoprecipitates with EPHA8 in response to EFNA5 stimulation. TIAM1 associates with EPHA8 in the juxtamembrane (JM) region. Deletion of the JM region or down-regulation of TIAM1 expression compromises EPHA8:EFNA5 endocytosis (Yoo et al. 2010).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P21709-1",
"P06241-1",
"P07947-1",
"P07948-1",
"P29320-1",
"Q5JZY3-1",
"P54764-1",
"P29317-1",
"P29322-1",
"P54756-1",
"Q15375-1",
"Q9UF33-1"
],
"evidence": [
{
"id": "R-HSA-4093327",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4093327"
}
]
},
{
"id": "R-HSA-4093336",
"name": "p-TIAM1 exchanges GTP for GDP on RAC1, activating it",
"equation": "",
"summary": "Phosphorylated T-lymphoma invasion and metastasis-inducing protein 1 (p-TIAM1) bound to EPHB complexes containing NMDARs, promotes spine morphogenesis by activating RAC1, which triggers actin cytoskeletal remodelling that is essential for spine development (Tolias et al. 2007, Tolias et al. 2005).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P63000-1",
"P07947-1",
"P07948-1",
"P29323-1",
"P54760-1",
"P54753-1",
"P54762-1"
],
"evidence": [
{
"id": "R-HSA-4093336",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-4093336"
}
]
},
{
"id": "R-HSA-432295",
"name": "GPVI binds Fyn and Lyn",
"equation": "",
"summary": "Fyn and Lyn constitutively associate with GPVI-Fc epsilon R1 gamma in platelets. The proline-rich region of GPVI is required for this interaction.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-432295",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-432295"
}
]
},
{
"id": "R-HSA-437118",
"name": "GPVI stimulates PI3K beta, gamma",
"equation": "",
"summary": "GPVI downstream signaling involves PI3K. Mouse knockouts of PI3Kbeta/PI3Kgamma suggest that though both isoforms are required for a full platelet response, only beta is absolutely required for Akt phosphorylation, Rap1 activation, and platelet aggregation downstream. The pathway connecting GPVI to PI3K is unclear. Two possible routes are suggested by interactions of the PI3K p85 regulatory subunit with LAT and with peptides representing the ITAM motif of Fc Epsilon R1 gamma.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P48736-1",
"P06241-1",
"P07948-1",
"P43405-1",
"P42338-1"
],
"evidence": [
{
"id": "R-HSA-437118",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-437118"
}
]
},
{
"id": "R-HSA-451758",
"name": "p85 associates with both p-Nephrin and CD2AP",
"equation": "",
"summary": "The regulatory p85 subunit of PI3K recognizes and binds to both phosphorylated nephrin and its binding partner, CD2AP. By mutation analysis, nephrin Y1158 was shown to be necessary for the interaction. This interaction allows the catalytic subunit p110 to act on phospholipids of the inner leaflet of the cell membrane. This leads to downstream phosphorylation and inactivation of the apoptotic factor Bad via the serine-threonine kinase AKT.",
"cellular_location": "plasma membrane",
"input_participant_list": [
"R-HSA-74693"
],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P42338-1"
],
"evidence": [
{
"id": "R-HSA-451758",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-451758"
}
]
},
{
"id": "R-HSA-453183",
"name": "p-Y348-SYK dissociates",
"equation": "",
"summary": "Structural and biophysical studies indicate that the adaptability of the Syk tandem SH2 domains is made possible by relatively weak interactions between the two SH2 domains and the flexibility of interdomain A (Zhang et al. 2008).; A large proportion of phosphorylated Syk is released into the cytosol. One factor that has been proposed for modulating the interactions of Syk with the receptor ITAM is the phosphorylation of Syk on Y130 (Keshvara et al. 1997).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07948-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-453183",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-453183"
}
]
},
{
"id": "R-HSA-453200",
"name": "SYK autophosphorylates",
"equation": "",
"summary": "Binding of Syk causes conformational changes that lead to Syk activation by autophosphorylation. Syk can be activated by a number of phosphorylation events, and it has been proposed that Syk may function as a switch whereby any of several possible stimuli trigger the acquisition of similar activated conformations. (Tsang et al. 2008). These phosphorylations both modulate Syk's catalytic activity (Keshvara et al. 1997) and generate docking sites for SH2 domain-containing proteins, such as c-Cbl, PLC, and Vav1. ; ; Syk tyrosine phosphorylation is reduced in the presence of the ITIM-containing immunoglobulin superfamily transmembrane protein G6B (Mori et al. 2008).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07948-1",
"Q06124-2",
"P43405-1",
"P29350-1"
],
"evidence": [
{
"id": "R-HSA-453200",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-453200"
}
]
},
{
"id": "R-HSA-5218804",
"name": "p38 MAPK activation by VEGFR",
"equation": "",
"summary": "In primary cultured human umbilical vein endothelial cells (HUVECs) VEGF-induced activation of SAPK2/p38MAPK, and pharmacological inhibition of p38MAPK attenuated VEGF-induced cell migration (Rouseseau et al. 1997, 2000). The p38MAPK pathway conveys the VEGF signal to microfilaments inducing rearrangements of the actin cytoskeleton. These actin structures are thought to generate the contractile force within cells that is required for endothelial cell migration. Activation of p38 requires the activity of FYN and PAK2 (Lamalice et al. 2004). However, little is known of the exact molecular events that follow activation of PAK2 and lead to p38 activation. Like all MAP kinases, p38 MAP kinases are activated by dual kinases termed the MAP kinase kinases (MKKs). There are two main MAPKKs that are known to activate p38, MKK3 and MKK6 (Zarubin & Han 2005). Along with FYN and PAK these MKKs might contribute to the activation of p38. Activation of p38 resulted in activation of MAP kinase activated protein kinase 2/3 (MAPK 2/3) and phosphorylation of the F-actin polymerization modulator, heat shock protein 27 (HSP27) (Rousseau et al. 1997).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P35968-1",
"O15264-1",
"P06241-1",
"P60953-2",
"Q16539-1",
"Q13177-1",
"P53778-1",
"Q15759-1"
],
"evidence": [
{
"id": "R-HSA-5218804",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5218804"
}
]
},
{
"id": "R-HSA-5218806",
"name": "FYN autophosphorylates",
"equation": "",
"summary": "FYN recruited to VEGFR2 is activated; this is required for VEGF-induced actin remodelling and endothelial migration. Once Y531 in the negative regulatory site is dephosphorylated by a phosphatase, FYN undergoes autophosphorylation on Y420 (Yeo et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P35968-1",
"P06241-1"
],
"evidence": [
{
"id": "R-HSA-5218806",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5218806"
}
]
},
{
"id": "R-HSA-5218812",
"name": "FYN phosphorylates PAK2",
"equation": "",
"summary": "PAK2 activity via GTPases can be strongly potentiated by concurrent stimulation of cellular tyrosine kinase activity. FYN may be involved in this potentiation by phosphorylating Y130 in the N-terminal regulatory domain leading to a robust enhancement of the catalytic activity of PAK2 (Renkema et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P35968-1",
"P06241-1",
"P60953-2",
"Q13177-1"
],
"evidence": [
{
"id": "R-HSA-5218812",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5218812"
}
]
},
{
"id": "R-HSA-5218814",
"name": "PAK2 autophorylates",
"equation": "",
"summary": "PAK2 undergoes autophosphorylation on serine and threonine residues, which maintains PAK2 in a catalytically active state. PAK is autophosphorylated at several sites but S141 flanking the kinase inhibitor region and T402 within the catalytic domain are the two conserved sites that regulate the catalytic activity (Chong et al. 2001, Gatti et al. 1999).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P35968-1",
"P06241-1",
"P60953-2",
"Q13177-1"
],
"evidence": [
{
"id": "R-HSA-5218814",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5218814"
}
]
},
{
"id": "R-HSA-5218824",
"name": "p-6Y-VEGFR2 binds FYN",
"equation": "",
"summary": "Tyrosine-1214 phosphorylation allows recruitment of cytoplasmic tyrosine kinase FYN along with NCK to VEGFR2. FYN and NCK associate with each other. This complex mediates phosphorylation of p21-activated protein kinase 2 (PAK2) and subsequent activation of p38MAPK mediating actin reorganization and cell migration (Lamalice et al. 2006).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P35968-1",
"P06241-1"
],
"evidence": [
{
"id": "R-HSA-5218824",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5218824"
}
]
},
{
"id": "R-HSA-5218832",
"name": "CDC42:GTP binds PAK2",
"equation": "",
"summary": "The PAK family of serine/threonine kinases are known to be activated by binding to the GTP-bound form of CDC42 or RAC1, small GTPases of the Rho family that are involved in regulating the organization of the actin cytoskeleton. PAK exists as homodimer in a trans-inhibited conformation. The kinase inhibitory (KI) domain of one PAK molecule binds to the C-terminal catalytic domain of the other and inhibits catalytic activity. Association of GTP-bound forms of CDC42 or RAC1 with the PAK PBD/CRIB domain induces conformational changes in the N-terminal domain that no longer support its autoinhibitory function. CDC42-mediated activation primes PAK2 for superactivation by tyrosine phosphorylation (Renkema et al. 2002).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P35968-1",
"P06241-1",
"P60953-2",
"Q13177-1"
],
"evidence": [
{
"id": "R-HSA-5218832",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5218832"
}
]
},
{
"id": "R-HSA-5218847",
"name": "PAK2 binds NCK",
"equation": "",
"summary": "P21-activated kinase 2 (PAK2) is an effector of GTP-bound CDC42. It associates with NCK and possibly links activated CDC42 to the SAPK2/p38 module (Lamalice et al. 2006, Zhao et al. 2000).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P35968-1",
"P06241-1",
"Q13177-1"
],
"evidence": [
{
"id": "R-HSA-5218847",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5218847"
}
]
},
{
"id": "R-HSA-5218854",
"name": "p-Y420-FYN is phosphorylated on S21",
"equation": "",
"summary": "FYN has multiple phosphorylation sites which can affect its kinase activity. Among these phosphorylation sites, serine 21 (S21) has been identified as a target site for protein kinase A (PKA). The phosphorylation of FYN S21 is critical for both FYN's tyrosine kinase activity and its focal adhesion targeting (Yeo et al. 2007).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22612-1",
"P35968-1",
"P06241-1",
"P17612-1",
"P22694-1"
],
"evidence": [
{
"id": "R-HSA-5218854",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5218854"
}
]
},
{
"id": "R-HSA-532603",
"name": "Nephrin mediated activation of N-WASP",
"equation": "",
"summary": "The NCK adaptor protein binds to a proline rich region on WASP and N-WASP through its SH3 domains and has been implicated in the recruitment of WASP/N-WASP to sites of tyrosine phosphorylation. NCK stimulates actin nucleation by N WASP:Arp2/3 complexes. Recruitment of NCK to phosphorylated YDxV sites on nephrin could therefore directly control the cytoskeletal actin architecture of podocytes.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1"
],
"evidence": [
{
"id": "R-HSA-532603",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-532603"
}
]
},
{
"id": "R-HSA-5621355",
"name": "LYN and FYN phosphorylate FCER1G in CLEC6A:FCERG and CLEC4E:FCERG",
"equation": "",
"summary": "Ligation of CLEC6A (C-type lectin domain family 6 member A/Dectin-2) and CLEC4E (Mincle) with their appropriate ligands trigger the tyrosine phosphorylation of the immune receptor tyrosine-based activation motif (ITAM) in the cytoplasmic tail of FCER1G chain. Tyrosine Y65 and Y76 in the ITAM are phosphorylated and this phosphorylation is mediated by Src kinases Lyn and Fyn (Sato et al. 2006, Yamasaki et al. 2008, Quek et al. 1998).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-5621355",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5621355"
}
]
},
{
"id": "R-HSA-5624486",
"name": "SFKs phosphorylates RAF1 on Y340,Y341",
"equation": "",
"summary": "Phosphorylation of tyrosine 340, 341 (Y340,341) on RAF1 in response to CD209 (DC-SIGN) signalling depends on yet unidentified members of the Src family of tyrosine kinases (SFKs). In imunoprecipitation studies, CD209 from lipid rafts of dendritic cells was found to co-precipitate with LYN, a member of the SFK, as well as with SYK tyrosine kinase, indicating their possible involvement in DC-SIGN signalling (Caparros et al. 2006, Svajger et al. 2010).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P06241-1",
"P04049-1",
"P07948-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-5624486",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5624486"
}
]
},
{
"id": "R-HSA-5672965",
"name": "RAS GEFs promote RAS nucleotide exchange",
"equation": "",
"summary": "The human genome is predicted to encode 27 RAS guanine nucleotide exchange factors (GEFs) that promote the exchange of GDP for GTP on membrane-associated RAS in response to RAS-MAPK pathway activation by growth factors, hormones, cytokines and other stimuli (reviewed in Cherfils and Zeghouf, 2013; Cargnello and Roux, 2011). Nucleotide exchange stimulates a conformational change in RAS to facilitate its interaction with RAF, ultimately promoting the phosphorylation of downstream effectors MAPK3 and MAPK1 (also known as ERK1 and ERK2) (reviewed in Cseh et al, 2014; Vigil et al, 2010).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P07949-1",
"P22455-1",
"P52333-1",
"P16234-1",
"O60674-1",
"Q9UQM7-1",
"P00533-1",
"P04626-1",
"P06241-1",
"P10721-1",
"Q13554-1",
"Q02763-1",
"P01112-1",
"P36888-1",
"P09619-1",
"P18433-5",
"Q05397-1",
"Q13557-1",
"P08581-1",
"P23458-1",
"Q13555-1"
],
"evidence": [
{
"id": "R-HSA-5672965",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5672965"
}
]
},
{
"id": "R-HSA-879917",
"name": "CBL, GRB2, FYN and PI3K p85 subunit are constitutively associated",
"equation": "",
"summary": "Cbl is constitutively associated with Grb2 in resting hematopoietic cells (Anderson et al. 1997, Odai et al. 1995, Park et al. 1998, Panchamoorthy et al. 1996). Both the SH2 and SH3 domains of Grb2 are involved. Cbl has 2 distinct C-terminal domains, proximal and distal. The proximal domain binds Grb2 in resting and stimulated cells, and in stimulated cells also binds Shc. The distal domain can bind the adaptor protein CRKL.
; Tyrosine phosphorylation of Cbl in response to IL-3 releases the SH3 domain of Grb2 which then is free to bind other molecules (Park et al. 1998).
Cbl also associates with Fyn (Anderson et al. 1997) and the related kinases Hck and Lyn (Hunter et al. 1999). Binding studies indicate that this binding is independent of the phosphorylation state of Cbl; The association of Fyn with Cbl has been described as constitutive (Hunter et al. 1999).
; Cbl further associates with the p85 subunit of PI3K (Hartley et al. 1995, Anderson et al. 1997, Hunter et al. 1997), this is also described as constitutive and is mediated by the SH3 domain of p85 (Hunter et al. 1997).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P22681-1",
"P07947-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-879917",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-879917"
}
]
},
{
"id": "R-HSA-8855237",
"name": "FYN phosphorylates DAB1 in RELN:VLDLR:DAB1:SH3KBP1",
"equation": "",
"summary": "One of the three domains in disabled homolog 1 (DAB1) is a tyrosine-rich region consists of five highly conserved tyrosine residues; Y185, Y198, Y200, Y220 and Y232. These residues correspond to two consensus Src family kinase recognition sites (YQxI, Y185 and Y198) and two consensus Abl/Crk recognition sites (YxVP, Y220 and Y232). At least three of the tyrosine residues (Y198, Y220 and Y232) can be phosphorylated by the Src kinase family member, tyrosine protein kinase fyn (FYN) in response to Reelin (RELN) stimulation (Katyal et al. 2007). Tyrosine-phosphorylated DAB1 acts as a hub to recruit different Src homology 2 (SH2) domain-containing proteins, including the p85 regulatory subunit of phosphatidylinositide-3-kinase (PI3K), cellular adaptors CrkL, Crk, Nck-beta and SOCS (suppressor of cytokine signaling) (Gao & Godbout 2013). Tyrosine phosphorylation of DAB1 also appears to strengthen the association of DAB1 with SH3KBP1 (aka CIN85), an adaptor protein involved in endocytic down-regulation of receptor-tyrosine kinases (Fuchigami et al. 2013).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P78509-1"
],
"evidence": [
{
"id": "R-HSA-8855237",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8855237"
}
]
},
{
"id": "R-HSA-8981534",
"name": "Nephrin dimer:KIRREL binds FYN",
"equation": "",
"summary": "Nephrin (NPHS1) is tyrosine phosphorylated by the Src family tyrosine kinase FYN in developing and injured podocytes. Phosphorylation of three tyrosines (1176, 1193 and 1217) results in the formation of a preferred binding motif (YDXV) for the SH2 domain of the adaptor protein NCK, which links Nephrin to the cytoskeleton. Phosphorylation of NPHS1 tyrosine 1158 results in a binding motif for the p85 regulatory subunit of PI3K.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1"
],
"evidence": [
{
"id": "R-HSA-8981534",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8981534"
}
]
},
{
"id": "R-HSA-912627",
"name": "CBL ubiquitinates PI3K",
"equation": "",
"summary": "Cbl is an E3 ubiquitin-protein ligase that negatively regulates signaling pathways by targeting proteins for ubiquitination and proteasomal degradation (Rao et al. 2002). Cbl-B targets PI3K for ubiquitination and degradation in T cells (Fang et al. 2000). Similarly, Cbl activation by tyrosine phosphorylation increases PI3K ubiquitination and proteasomal degradation (Dufour et al. 2008).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P22681-1",
"P07947-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-912627",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912627"
}
]
},
{
"id": "R-HSA-912629",
"name": "CBL is tyrosine phosphorylated",
"equation": "",
"summary": "Cbl is tyrosine phosphorylated following stimulation with IL-3 (Anderson et al. 1997) and GM-CSF (Odai et al. 1995). Cbl may be phosphorylated prior to this IL-3 stimulated tyrosyl phosphorylation (Park et al. 1998). The kinase responsible for Cbl phosphorylation may be dependent on cell type; Fyn is demonstrated to have the ability to phosphorylate Cbl (Hunter et al. 1999), other candidates include Hck, Lyn (Hunter et al. 1999) and Syk (Park et al. 1998).
; Tyrosines 700, 731 and 774 are the major sites of Cbl phosphorylation by non-receptor protein tyrosine kinases, with none showing any particular specificity for sites (Tsygankov et al. 2001). Fyn was observed to be constitutively associated with Cbl in lysates of several different cell types including the interleukin-3-dependent murine myeloid cell line 32Dcl3, and the prolactin-dependent rat thymoma cell line Nb2. Cbl phosphorylation at Y731 is postulated to provide an additional interaction between Cbl and the SH2 domain of p85-PI3K (Hunter et al. 1999). Cbl-p85 association increases in activated cells (Panchamoorthy et al. 1996). Expression of a Cbl Y731F mutant which abolishes binding of Cbl to p85 markedly increased levels of p85-PI3K (Dufour et al. 2008). Cbl-p85 binding negatively regulates PI3K activity (Fang et al. 2001); Cbl phosphorylation increased PI3K ubiquitination and proteasome degradation (Dufour et al. 2008). Cbl association with members of the Crk family is mediated by phosphorylation of Y700 and Y774 (Andoniou et al. 1996), binding with Vav is mediated by Y770 (Marengere et al 1997).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P22681-1",
"P07947-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-912629",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912629"
}
]
},
{
"id": "R-HSA-9605259",
"name": "Active FLT3 binds FYN",
"equation": "",
"summary": "Feline McDonough Sarcoma-like tyrosine kinase (FLT3) is a member of the class III tyrosine kinase receptor family. Ligand binding induces conformational changes in the FLT3 receptor, which facilitates its dimerization and autophosphorylation. Subsequently, tyrosine-protein kinase Fyn (FYN) associates with the phosphorylated residues of fully active FLT3 (Y591, Y599 and pY955) through its SH2 domain (Dosil et al. 1993, Chougule et al. 2016). Experiments confirming this event were performed in mouse cells.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P36888-1"
],
"evidence": [
{
"id": "R-HSA-9605259",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9605259"
}
]
},
{
"id": "R-HSA-9664261",
"name": "Src phosphorylate SYK in IgG:Leishmania surface:p-FCGR3A:SYK",
"equation": "",
"summary": "Multiple sites of phosphorylation are known to exist in SYK, which both regulate its activity and also serve as docking sites for other proteins. Some of these sites include Y131 of interdomain A, Y323, Y348, and Y352 of interdomain B, and Y525 and Y526 within the activation loop of the kinase domain and Y630 in the C-terminus (Zhang et al. 2002, Lupher et al. 1998, Furlong et al. 1997). Phosphorylation of these tyrosine residues disrupts autoinhibitory interactions and results in kinase activation even in the absence of phosphorylated ITAM tyrosines (Tsang et al. 2008). SYK is primarily phosphorylated by Src family kinases and this acts as an initiating trigger by generating few molecules of activated SYK which are then involved in major SYK autophosphorylation (Hillal et al. 1997).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07947-1",
"P07948-1",
"P09769-1",
"P08631-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-9664261",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664261"
}
]
},
{
"id": "R-HSA-9664275",
"name": "Src phosphorylates CD3 dimers in IgG:Lma antigens:FCGR3A:CD3 dimers",
"equation": "",
"summary": "After cross linking, Fc gamma receptors are sequestered to lipid rafts where they are complexed with some of the tyrosine kinases of Src family and undergo phosphorylation on the tyrosine residues contained in conserved ITAM sequences. At least six out of nine members of the Src family kinases (SRC, FYN, FGR, HCK, YES and LYN ) have been identified in the phagocytic cells and are implicated in the initiation of Fc gamma mediated signaling. (Suzuki et al. 2000, Majeed et al. 2001, Kwiatkowska et al. 2003). Some of these kinases have been found associated with specific receptors. In monocytes HCK and LYN have been found associated with FCGRI (Durden et al. 1995), whereas only HCK with FCGRIIA (Ghazizadeh et al. 1994) while FGR in neutrophils (Hamada et al. 1993) and LCK in NK cells with FCGRIIIA (Pignata et al. 1993)
The implication of Src kinases in phosphorylation was first supported by pharmacological findings that herbimycin A, a tyrosine kinase inhibitor relatively specific for Src-family kinases, potently suppressed Fc receptor mediated functions (Greenberg et al. 1993, Suzuki et al. 2000). However, their particular involvement in phagocytosis remains unclear, as targeted disruption of single or multiple Src family genes did not result in significant alterations in phagocytosis (Hunter et al. 1993, Fitzer Attas et al. 2000, Suzuki et al. 2000). HCK, FGR and LYN triple-deficient (-/-) macrophages have shown significant delays in FCGR mediated phagocytosis, but these deficiencies do not completly disrupt the process (Fitzer Attas et al. 2000).
Tyrosine residues Y288 and Y304 (Y282 and Y298 according to the literature reference, it is 6 residues shorter compared to uniprot entry due to an alternate initiation codon usage), within ITAM sequence in the cytoplasmic domain of FCGRIIA are the key target sites that are phosphorylated by Src family kinases (Mitchell et al, 1994). In case of FCGRIA and FCGRIIIA the specific tyrosine residues within ITAMs of the associated gamma/zeta chains are phosphorylated by activated Src family kinases (SFKs) (Park et al. 1993).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07947-1",
"P07948-1",
"P09769-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9664275",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664275"
}
]
},
{
"id": "R-HSA-9670412",
"name": "Phosphorylation of STATs downstream of KIT mutants",
"equation": "",
"summary": "Extracellular- , juxtamembrane- and kinase-domain mutants of KIT have been shown to activate the STAT pathway, as assessed by STAT phosphorylation. The biological relevance of each STAT isoform varies between tumor types (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hara et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004; reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670412",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670412"
}
]
},
{
"id": "R-HSA-9670413",
"name": "JAK2 binds to p-KIT mutants",
"equation": "",
"summary": "Activation of STAT signaling has been observed downstream of a number of oncogenic KIT mutants, both juxtamembrane and kinase domain mutants, although the biological relevance or each STAT isoform varies between tumor types (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hana et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004). Although the pathway details haven't been examined in all cases, this likely occurs through the recruitment of JAK2 and SRC family kinases, as is the case for the wild type receptor (reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670413",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670413"
}
]
},
{
"id": "R-HSA-9670414",
"name": "KIT mutants bind SFKs",
"equation": "",
"summary": "Signaling downstream of KIT mutants occurs in part through SRC family kinases, as is the case for the wild-type receptor (Paronetto et al, 2004; Krystal et al, 1998; Schittenhelm et al, 2006; Tatton et al, 2003; Timokhina et al, 1998; reviewed in Lanneartsson and Roonstrand, 2012). The dependence of different KIT mutants on SRC family signaling varies, however, with mutants such as the common D816V showing less requirement for SFK-mediated signaling (Sun et al, 2009).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670414",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670414"
}
]
},
{
"id": "R-HSA-9670416",
"name": "Recruitment of STATs by KIT mutants",
"equation": "",
"summary": "Extracellular- , juxtamembrane- and kinase-domain mutants of KIT have been shown to signal through the STAT pathway, although the biological relevance or each STAT isoform varies between tumor types (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hara et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004). Although the pathway details haven't been examined in all cases, STAT pathway activation likely occurs through the recruitment of JAK2 and SRC family kinases, as is the case for the wild type receptor (reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670416",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670416"
}
]
},
{
"id": "R-HSA-9670417",
"name": "Dimerization of STATs downstream of KIT mutants",
"equation": "",
"summary": "Activation of STAT signaling suggests that STATs dimerize downstream of activating KIT mutations as is the case with the wild-type receptor, although this hasn't been directly demonstrated in all cases (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hara et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004; reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670417",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670417"
}
]
},
{
"id": "R-HSA-9670418",
"name": "Phosphorylation of JAK2 downstream of KIT mutants",
"equation": "",
"summary": "Although the details haven't been examined in detail in all cases, phosphorylation of JAK2 likely occurs downstream of oncogenic mutations of KIT, as is the case for the wild-type receptor (Brizzi et al, 1999; Ning et al, 2001; Hirota et al, 1998; reviewed in Lennartsson and Roonstrand, 2012).; ;",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670418",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670418"
}
]
},
{
"id": "R-HSA-9670426",
"name": "Disassociation and translocation of STATs to the nucleus downstream of KIT mutants",
"equation": "",
"summary": "STATs are assumed to dissociate from the receptor and translocate to the nucleus downstream of activated KIT receptors to propagate STAT-dependent signaling (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hara et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004; reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, nucleoplasm, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670426",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670426"
}
]
},
{
"id": "R-HSA-9680348",
"name": "PIK3R1:PIK3CA,B,G (PI3K), PLCG2 (PLCgamma2), SHC1 (SHC), PTPN11 (SHP2), GRB2:GAB2, GRB2:GAB3, GRAP2 (MONA), CBL:GRB2, INPP5D (SHIP1), INPPL1 (SHIP2) bind PolyUb,p-8Y-CSF1R and are activated",
"equation": "",
"summary": "The PIK3R1 (p85alpha) subunit of phosphatidylinositol 3-kinase (PI3K) is phosphorylated and binds CBL and CSF1R (inferred from mouse homologs). CBL also directly binds phosphorylated CSF1R (inferred from mouse homologs). GRB2:SOS1 transiently interacts with CSF1R (inferred from mouse homologs) and PI3K (Saleem et al. 1995) in response to CSF1. SHC1 (SHC) interacts with CBL and CSF1R (inferred from mouse homologs). CBL is constitutively bound to GRB2, CBL is phosphorylated, and phosphorylated CBL binds phosphorylated SHC (inferred from mouse homologs). PLCG2 (PLC-gamma2), expressed in the myeloid lineage, binds phosphorylated tyrosine-723 of CSF1R and PLCG2 is phosphorylated in a process that requires the activity of PI3K (inferred from mouse homologs). GRAP2 (MONA) binds phosphorylated tyrosine-699 of CSF1R. GRB2 also interacts with CSF1R (Kharbanda et al. 1995) via phosphotyrosine-699 ( inferred from mouse homologs). GRAP2 binds GAB3, which is then phosphorylated (inferred from mouse homologs). In response to CSF1, the scaffolding protein GAB2 associates with INPP5D (SHIP1) and other proteins involved in CSF1 signaling and GAB2 is phosphorylated directly or indirectly by CSF1R (inferred from mouse homologs). INPPD5D also interacts with the kinase LYN (Baran et al. 2003). INPPL1 (SHIP2), a homolog of INPPD5, binds CSF1R in response to CSF1 (inferred from mouse homologs). GAB3, a homolog of GAB2, associates with CSF1R, is phosphorylated, and interacts with PI3K and PTPN11 (SHP2) (inferred from mouse homologs). The SRC family kinases SRC, FYN, and YES1 (YES) bind phosphorylated CSF1R (Courtneidge et al. 1993, Li et al. 1997, also inferred from mouse homologs). STAT proteins STAT1 and STAT3 bind CSF1R and are phosphorylated (inferred from mouse homologs). STAT5 also appears to be phosphorylated in response to CSF1 (Knowlton et al. 2010). THOC5 (FMIP) binds CSF1R and is phosphorylated (inferred from mouse homologs). The order of binding and phosphorylation of the interactors of CSF1R is unknown. Different subpopulations of CSF1R may be bound to different sets of interactors (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [
"R-HSA-197940",
"R-HSA-202367",
"R-HSA-354251",
"R-HSA-200917",
"R-HSA-9628701",
"R-HSA-373640",
"R-HSA-913354",
"R-HSA-9682751"
],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P42336-1",
"P48736-1",
"P06241-1",
"P12931-1",
"P22681-1",
"O15357-1",
"P07947-1",
"P07948-1",
"P16885-1",
"Q06124-2",
"P08631-1",
"P42338-1",
"Q92835-1"
],
"evidence": [
{
"id": "R-HSA-9680348",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9680348"
}
]
},
{
"id": "R-HSA-9680385",
"name": "CSF1R-associated SOS1 mediates exchange of GTP for GDP bound to RAS",
"equation": "",
"summary": "SOS1 (SOS) is stably bound to GRB2, which transiently associates with phosphorylated CSF1R. In response to the activation of CSF1R by CSF1, SOS1 promotes RAS to exchange of GDP for GTP (inferred from mouse homologs) and thereby activates the RAS-RAF-MEK-ERK1,2 signaling pathway. Myeloid cells contain the KRAS isoform of RAS. KRAS:GTP enhances proliferation of macrophages (inferred from mouse homologs).
GRB2 has been shown to bind phosphotyrosine-699 of CSF1R (phosphotyrosine-697 of mouse Csf1r), however phosphorylation of tyrosines 544, 559, and 807 of mouse Csf1r are together sufficient for the full proliferative response mediated via the RS-RAF-MEK-ERK1,2 pathway (Yu et al. 2012) and mouse Csf1r lacking phosophotyrosine-697 can still activate ERK (Lee and States 2000), Csf1r phosphotyrosine-697 (human CSF1R phosphotyrosine-699) is likely not the only GRB2:SOS binding site",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P07947-1",
"P08631-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-9680385",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9680385"
}
]
},
{
"id": "R-HSA-9680388",
"name": "CSF1R-associated PLCG2 hydrolyzes phosphatidylcholine",
"equation": "",
"summary": "In response to CSF1, PLCG2 (phospholipase C gamma2) associates with CSF1R, is activated by phosphorylation, and hydrolyzes phosphatidylcholine to yield choline phosphate (ChoP, phosphocholine) and 1,2-diacylglycerol (Imamura et al. 1990, Nakamura et al. 1992, Obba et al. 2015, also inferred from mouse homologs). PLCG2 activates pathways that enhance differentiation of macrophages (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P42336-1",
"P48736-1",
"P06241-1",
"P12931-1",
"P22681-1",
"O15357-1",
"P07947-1",
"P07948-1",
"P16885-1",
"Q06124-2",
"P08631-1",
"P42338-1",
"Q92835-1"
],
"evidence": [
{
"id": "R-HSA-9680388",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9680388"
}
]
},
{
"id": "R-HSA-9680389",
"name": "CSF1R-associated phosphatidylinositol 3-kinase (PI3K) phosphorylates PI(4,5)P2",
"equation": "",
"summary": "Phosphatidylinositol 3-kinase (PI3K) associated with the activated receptor for CSF1, CSF1R (M-CSFR), phosphorylates phosphatidylinositol 4,5-bisphosphate (PIP2) to yield phosphatidylinositol 3,4,5-trisphosphate (PIP3) (Saleem et al. 1995, also inferred from mouse homologs). The regulatory subunit of PI3K, PIK3R1 (p85alpha), binds phosphotyrosine-723 (721 in the mouse homologs) of CSF1R (inferred from mouse homologs). PI3K is important for proliferation, migration, and anti-inflammatory activity of macrophages (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P42336-1",
"P48736-1",
"P06241-1",
"P12931-1",
"P22681-1",
"O15357-1",
"P07947-1",
"P07948-1",
"P16885-1",
"Q06124-2",
"P08631-1",
"P42338-1",
"Q92835-1"
],
"evidence": [
{
"id": "R-HSA-9680389",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9680389"
}
]
},
{
"id": "R-HSA-9733316",
"name": "p-Y-CBL autoubiquitinates and multiubiquitinates p-Y561-CSF1R in CSF1 dimer:p-Y561-CSF1R dimer:p-Y-CBL",
"equation": "",
"summary": "After CBL is phosphorylated and binds CSF1R, CBL autopolyubiquitinates and polyubiquitinates CSF1R (inferred from mouse homologs). The ubiquitination of CSF1R results in a subsequent wave of phosphorylation by CSF1R and the internalization and proteolysis of CSF1R (inferred from mouse homologs). Thus multiubiquitination of CSF1R is required for full activity of CSF1R and for termination of signaling by CSF1R.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P22681-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9733316",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9733316"
}
]
},
{
"id": "R-HSA-9733323",
"name": "Src family kinases phosphorylate CBL in CSF1 dimer:p-Y561-CSF1R dimer:CBL",
"equation": "",
"summary": "CBL binds the phosphorylated CSF1R and is phosphorylated (inferred from mouse homologs). CBL is observed to bind phosphotyrosine-969 but mutation of tyrosine-561 has a greater effect on phosphoryation of CBL and multiubiquitination of CSF1R by CBL (inferred from mouse homologs). Based on response to inhibitors, the phosphorylation of CBL is catalyzed by SRC family kinases (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P22681-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9733323",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9733323"
}
]
},
{
"id": "R-HSA-9733330",
"name": "CSF1 dimer,IL34 dimer:p-Y561-CSF1R dimer:SFK binds GRB2:SOS1",
"equation": "",
"summary": "After an initial wave of phosphorylation of CSF1R, the stable GRB2:SOS1 complex transiently binds phospho-CSF1R (inferred from mouse homologs). GRB2 has been shown to bind phosphotyrosine-699, though another phosphotyrosine residue may be involved in transient binding of GRB2 (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9733330",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9733330"
}
]
},
{
"id": "R-HSA-9733331",
"name": "CSF1 dimer,IL34 dimer:p-Y561-CSF1R:GRB2:SOS1 dissociates yielding CSF1 dimer,IL34 dimer:p-Y561-CSF1R:SFK and GRB2:SOS1",
"equation": "",
"summary": "GRB2:SOS1 transiently associates with phosphorylated CSF1R after CSF1R undergoes an initial wave of autophosphorylation (Wang et al. 1999). GRB2:SOS1 then dissociates from CSF1R.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9733331",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9733331"
}
]
},
{
"id": "R-HSA-9817983",
"name": "CSF1 dimer,IL34 dimer:p-Y561-CSF1R dimer:SFK binds CBL",
"equation": "",
"summary": "The ubiquitin E3 ligase CBL associates with the phosphorylated CSF1R.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P22681-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9817983",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9817983"
}
]
},
{
"id": "R-HSA-9818010",
"name": "CSF1 dimer,IL34 dimer:p-Y561-CSF1R dimer binds SRC family kinases FYN,HCK,SRC,YES1",
"equation": "",
"summary": "After phosphorylation of CSF-1R tyrosine-Y561, SFKs bind the phosphotyrosine-561 site (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9818010",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9818010"
}
]
},
{
"id": "R-HSA-983709",
"name": "LYN, FYN, BLK phosphorylate ITAMs of Ig-alpha (CD79A) and Ig-beta (CD79B)",
"equation": "",
"summary": "The B cell receptor (BCR) comprises an immunoglobulin complexed with a heterodimer of Ig-alpha (CD79A, MB-1) and Ig-beta (CD79B, B29). After immunoglobulin IgM or IgD binds antigen the associated Ig-alpha and Ig-beta are each observed to be phosphorylated at two tyrosine residues in the cytoplasmic immunoreceptor tyrosine-activated motif (ITAM) (Sanchez et al. 1993, Hata et al. 1994, Saouaf et al. 1994, Saouaf et al. 1995). Saouaf et al. (1995) showed that the kinase Blk could phosphorylate both tyrosines of each ITAM and that the kinase SYK specifically bound phosphorylated but not unphosphorylated ITAMs. In mouse the kinase Lyn and other kinases phosphorylate one tyrosine and Syk is believed to phosphorylate the other (Yamanashi et al. 1991, Flaswinkel and Reth 1994, Rolli et al. 2002).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P07948-1",
"P51451-1",
"P29350-1"
],
"evidence": [
{
"id": "R-HSA-983709",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-983709"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-HSA-195066",
"participant_name": "VAV1 [cytosol]",
"crossref": [
{
"id": "P15498",
"database": "UniProt",
"url": ""
},
{
"id": "6NF1",
"database": "PDB",
"url": ""
},
{
"id": "P15498",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "6NFA",
"database": "PDB",
"url": ""
},
{
"id": "ENSG00000141968",
"database": "OpenTargets",
"url": ""
},
{
"id": "P15498",
"database": "PRO",
"url": ""
},
{
"id": "P15498",
"database": "ZINC target",
"url": ""
},
{
"id": "HMDBP10969",
"database": "HMDB Protein",
"url": ""
},
{
"id": "VAV_HUMAN",
"database": "ZINC - Substances",
"url": ""
},
{
"id": "3BJI",
"database": "PDB",
"url": ""
},
{
"id": "NP_001245136.1",
"database": "RefSeq",
"url": ""
},
{
"id": "NP_005419.2",
"database": "RefSeq",
"url": ""
},
{
"id": "3KY9",
"database": "PDB",
"url": ""
},
{
"id": "6NEW",
"database": "PDB",
"url": ""
},
{
"id": "2CRH",
"database": "PDB",
"url": ""
},
{
"id": "2LCT",
"database": "PDB",
"url": ""
},
{
"id": "2MC1",
"database": "PDB",
"url": ""
},
{
"id": "2ROR",
"database": "PDB",
"url": ""
},
{
"id": "P15498",
"database": "GeneCards",
"url": ""
},
{
"id": "VAV_HUMAN",
"database": "ZINC - Predictions - Purchasable",
"url": ""
},
{
"id": "ENSP00000469450",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000141968",
"database": "Ensembl",
"url": ""
},
{
"id": "ENST00000596764",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSP00000472929",
"database": "Ensembl",
"url": ""
},
{
"id": "ENST00000602142",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000141968-VAV1",
"database": "HPA",
"url": ""
}
]
},
{
"participant_id": "R-HSA-197940",
"participant_name": "INPP5D [cytosol]",
"crossref": [
{
"id": "Q92835",
"database": "UniProt",
"url": ""
},
{
"id": "6IBD",
"database": "PDB",
"url": ""
},
{
"id": "NP_005532.2",
"database": "RefSeq",
"url": ""
},
{
"id": "NP_001017915.1",
"database": "RefSeq",
"url": ""
},
{
"id": "5RXI",
"database": "PDB",
"url": ""
},
{
"id": "5RWF",
"database": "PDB",
"url": ""
},
{
"id": "5RYL",
"database": "PDB",
"url": ""
},
{
"id": "5RYK",
"database": "PDB",
"url": ""
},
{
"id": "5RXJ",
"database": "PDB",
"url": ""
},
{
"id": "5RXH",
"database": "PDB",
"url": ""
},
{
"id": "5RWE",
"database": "PDB",
"url": ""
},
{
"id": "5RXM",
"database": "PDB",
"url": ""
},
{
"id": "5RXO",
"database": "PDB",
"url": ""
},
{
"id": "8PDG",
"database": "PDB",
"url": ""
},
{
"id": "Q92835",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "6XY7",
"database": "PDB",
"url": ""
},
{
"id": "5RWG",
"database": "PDB",
"url": ""
},
{
"id": "5RXK",
"database": "PDB",
"url": ""
},
{
"id": "5RWH",
"database": "PDB",
"url": ""
},
{
"id": "5RXL",
"database": "PDB",
"url": ""
},
{
"id": "5RXQ",
"database": "PDB",
"url": ""
},
{
"id": "5RWK",
"database": "PDB",
"url": ""
},
{
"id": "5RXP",
"database": "PDB",
"url": ""
},
{
"id": "8PDH",
"database": "PDB",
"url": ""
},
{
"id": "8PDJ",
"database": "PDB",
"url": ""
},
{
"id": "ENSG00000168918-INPP5D",
"database": "HPA",
"url": ""
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