Binding of SHC1 to activated ERBB2 and the consequent RAS signaling activation is inhibited by the action of the PTPN12 protein tyrosine phosphatase. PTPN12 dephosphorylates tyrosine residue Y1248 of activated ERBB2 which serves as one of the docking sites for SHC1 in the ERBB2 C-terminus (Sun et al. 2011).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"Q05209-1"
],
"evidence": [
{
"id": "R-HSA-1963578",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1963578"
}
]
},
{
"id": "R-HSA-1963581",
"name": "Trans-autophosphorylation of p-Y877-ERBB2 heterodimers",
"equation": "",
"summary": "Phosphorylation of ERBB2 on tyrosine residue Y877 by SRC family kinases significantly increases trans-autophosphorylation rate of ERBB2 heterodimers, presumably by enabling the kinase domain of ERBB2 to achieve a conformation that positively affects ERBB2 kinase activity. The downstream signaling of phosphorylated ERBB2 heterodimers that are phosphorylated on Y877 of ERBB2, in addition to the known trans-autophosphorylation sites, has not been studied extensively; it is assumed that the behavior of Y877-phosphorylated ERBB2 heterodimers is qualitatively similar to the behavior of trans-autophosphorylated ERBB2 heterodimers which do not harbor this modification.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-1963581",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1963581"
}
]
},
{
"id": "R-HSA-1963582",
"name": "Trans-autophosphorylation of ERBB2 heterodimers",
"equation": "",
"summary": "Dimers of ERBB2 and EGF-bound EGFR trans-autophosphorylate on six EGFR tyrosine residues and six ERBB2 tyrosine residues to form phosphorylated heterodimers that activate downstream signaling cascades (Ricci et al. 1995, Pinkas-Kramarski et al. 1996, Walton et al. 1990, Margolis et al. 1989, Hazan et al. 1990, Helin et al. 1991).
In heterodimers of ERBB2 and neuregulin-stimulated ERBB3, ERBB2 phosphorylates ERBB3 on tyrosine residues that serve as docking sites for the p85 subunit of PI3K (Y1054, Y1197, Y1222, Y1224, Y1260, Y1276 and Y1289), as well as SHC1 (Y1328) and GRB7 (Y1199 and Y1262). Since ERBB3 lacks catalytic activity, it cannot phosphorylate ERBB2. Hovewer, since ERBB2:ERBB3 heterodimers usually oligomerize on the cell surface, ERBB2 can become trans-autophosphorylated by an adjacent ERBB2 protein. It is not known if ERBB2 in the ERBB2:ERBB3 hetero-oligomer is phosphorylated on all conserved tyrosine residues and if the phosphorylation status of ERBB2 in the ERBB2:ERBB3 hetero-oligomer significantly affects signaling (Li et al. 2007, Pinkas-Kramarski et al. 1996, Prigent et al. 1994, Vijapurkar et al. 2003, Wallasch et al. 1995).
Heterodimers of ERBB2 and ERBB4 trans-autophosphorylate on tyrosine residues that serve as docking sites for PLC-gamma, GRB2 and SHC1, as well as p85 subunit of PI3K (PIK3R1) in the case of ERBB2 heterodimers with ERBB4 CYT1 isoforms (ERBB4cyt1) - ERBB4 JM-A CYT1 and ERBB4 JM-B-CYT1 (Li et al. 2007, Kaushansky et al. 2008, Hazan et al. 1990, Cohen et al. 1996).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-1963582",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1963582"
}
]
},
{
"id": "R-HSA-1963586",
"name": "SRC family kinases phosphorylate ERBB2",
"equation": "",
"summary": "Dissociation of HSP90 from ERBB2 upon formation of ERBB2 heterodimers (with either EGFR, ERBB3 or ERBB4) enables phosphorylation of ERBB2 on the tyrosine residue Y877, mediated by one of SRC family kinases - SRC, FYN or YES1. Although not a mandatory prerequisite of ERBB2 catalytic activity, the phosphorylation at Y877 significantly increases the kinase activity of ERBB2.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P06241-1",
"P12931-1",
"P07947-1"
],
"evidence": [
{
"id": "R-HSA-1963586",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1963586"
}
]
},
{
"id": "R-HSA-1963589",
"name": "ERBB2 forms heterodimers with ligand-activated ERBB receptors: EGFR, ERBB3 and ERBB4",
"equation": "",
"summary": "ERBB2, which does not bind any known ligand, is activated through formation of a heterodimer with another ligand-activated ERBB family member. ERBB2 heterodimerization partners are EGF-stimulated EGFR (Wada et al. 1990, Karunagaran et al. 1996), ERBB3 stimulated by neuregulins NRG1 or NRG2 (Pinkas-Kramarski et al. 1996), and ERBB4 stimulated by neuregulins or EGF-like ligands (Li et al. 2007). In the process of dimerization, ERBB2 dissociates from chaperone proteins HSP90 and CDC37 (Xu et al 2001, Citri et al. 2004). Activated ERBB2 also dissociates from ERBB2IP, the protein responsible for proper localization of ERBB2 to basolateral membranes of epithelial cells (Borg et al. 2000).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-1963589",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1963589"
}
]
},
{
"id": "R-HSA-2316434",
"name": "PI3K phosphorylates PIP2 to PIP3",
"equation": "",
"summary": "A number of different extracellular signals converge on PI3K activation. PI3K can be activated downstream of receptor tyrosine kinases (RTKs) such as FGFR (Ong et al. 2001, Eswarakumar et al. 2005), KIT (Chian et al. 2001, Ronnstrand 2004, Reber et al. 2006), PDGF (Coughlin et al. 1989, Fantl et al. 1992, Heldin et al. 1998), insulin receptor IGF1R (Hadari et al. 1992, Kooijman et al. 1995), and EGFR and its family members (Rodrigues et al. 2000, Jackson et al. 2004, Kainulainen et al. 2000, Junttila et al. 2009). Other proteins, such as CD28 (Pages et al. 1996, Koyasu 2003, Kane and Weiss, 2003) and TRAT1 (Bruyns et al. 1998, Koyasu 2003, Kolsch et al. 2006), can also trigger PI3K activity.
In unstimulated cells, PI3K class IA exists as an inactive heterodimer of a p85 regulatory subunit (encoded by PIK3R1, PIK3R2 or PIK3R3) and a p110 catalytic subunit (encoded by PIK3CA, PIK3CB or PIK3CD). Binding of the iSH2 domain of the p85 regulatory subunit to the ABD and C2 domains of the p110 catalytic subunit both stabilizes p110 and inhibits its catalytic activity. This inhibition is relieved when the SH2 domains of p85 bind phosphorylated tyrosines on activated RTKs or their adaptor proteins. Binding to membrane-associated receptors brings activated PI3K in proximity to its membrane-localized substrate, PIP2 (Mandelker et al. 2009, Burke et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22455-1",
"P16234-1",
"P42336-1",
"Q9NWZ3-1",
"P00533-1",
"P04626-1",
"P06241-1",
"P10721-1",
"P12931-1",
"P63000-1",
"P06239-1",
"Q06124-2",
"Q9Y4K3-1",
"P36888-1",
"P09619-1",
"P42338-1",
"O00329-1",
"P08581-1",
"Q01638-1",
"P51617-1"
],
"evidence": [
{
"id": "R-HSA-2316434",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2316434"
}
]
},
{
"id": "R-HSA-2400009",
"name": "PI3K inhibitors block PI3K catalytic activity",
"equation": "",
"summary": "A variety of inhibitors capable of blocking the phosphoinositide kinase activity of PI3K have been developed. These inhibitors display differential selectivity and inhibit kinase activity of their substrates by distinct mechanisms. For example, the first-generation PI3K inhibitor wortmannin (Wymann et al. 1996) covalently and irreversibly binds all classes of PI3K enzymes, as well as other kinases including mTOR, at a residue critical for catalytic activity. Although wortmannin is precluded from in vivo and clinical use due to its toxicity, it has proven to be a useful tool for in vitro laboratory studies. Newer inhibitors, such as BEZ235, are currently being investigated in Phase I clinical trials. BEZ235 is a dual pan-class I PI3K/mTOR inhibitor that blocks kinase activity by binding competitively to the ATP-binding pocket of these enzymes (Serra et al. 2008, Maira et al. 2008). BGT226 (Chang et al. 2011) and XL765 (Prasad et al. 2011) also inhibits both PI3K class I enzymes and mTOR. Other inhibitors in clinical trials, such as BKM120 (Maira et al. 2012), GDC0941 (Folkes et al. 2008, Junttila et al. 2009) and XL147 (Chakrabarty et al. 2012), are specific for class I PI3Ks and exhibit no activity against mTOR. Current research aims to identify isoform-specific PI3K inhibitors. Small molecule inhibitors that selectively inhibit PIK3CA (p110alpha), e.g. PIK-75 and A66, were used to study the role of p110alpha in signaling and growth of tumor cells (Knight et al. 2006, Sun et al. 2010, Jamieson et al. 2011, Utermark et al. 2012). The PIK3CB (p110beta) specific inhibitor TGX221 has been used in in vitro models of vascular injury (Jackson et al. 2005), and the TGX221 derivative KIN-193 has been shown to block AKT activity and tumor growth in mice with p110beta activation or PTEN loss (Ni et al. 2012). CAL-101 is a PIK3CD (p110delta) specific inhibitor that is being clinically investigated as a therapeutic for lymphoid malignancies (Herman et al. 2010). It is hoped that, in the future, more specific inhibitors, such as those targeting selective PI3K isoforms, will provide optimum treatment while minimizing unwanted side effects. For a recent review, please refer to Liu et al. 2009.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22455-1",
"P16234-1",
"P42336-1",
"P00533-1",
"P04626-1",
"P06241-1",
"P10721-1",
"P12931-1",
"P63000-1",
"P06239-1",
"Q06124-2",
"P36888-1",
"P09619-1",
"P42338-1",
"O00329-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-2400009",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2400009"
}
]
},
{
"id": "R-HSA-373750",
"name": "SEMA4D interacts with Plexin-B1:ErbB2",
"equation": "",
"summary": "Sema4D binds Plexin-B1 to induce repulsive or attractive effects in neuronal and nonneuronal cells. Plexins constitute a large family of transmembrane proteins that function as receptors for semaphorins and their interaction governs cell adhesion and migration in a variety of tissues. All B-class plexins can interact with the receptor tyrosine kinases Met and ErbB2. Upon binding of Sema4D to plexin-B1, the kinase activity of ErbB2 is increased resulting in tyrosine phosphorylation of both Plexin-B1 and ErbB2. ErbB2 has been shown to mediate Sema4D-induced growth cone collapse in hippocampal neurons by the activation of RhoA via plexinB1 and PDZRhoGEF/LARG.
Sequence alignment reveals the presence of 13 conserved tyrosine residues (highly conserved sites 1918, 1953, 2038) but 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": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-373750",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-373750"
}
]
},
{
"id": "R-HSA-416588",
"name": "Activation of Rho by LARG and PDZ-RhoGEF",
"equation": "",
"summary": "The RhoGEFs LARG and PDZ-RhoGEF complexed with Plexin-B1 stimulate the exchange of GDP for GTP on RhoA through their DH and PH domains.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P61586-1"
],
"evidence": [
{
"id": "R-HSA-416588",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-416588"
}
]
},
{
"id": "R-HSA-416594",
"name": "LARG and PDZ-RhoGEF binds to Plexin-B1",
"equation": "",
"summary": "Plexin-B1 activates RhoA and induces growth cone collapse and and cytoskeletal reorganization through Rho-specific guanine nucleotide exchange factors PDZ-RhoGEF (ARHGEF11) and leukemia-associated RhoGEF (LARG, ARHGEF12). Plexin-B1 directly interacts with PDZ-RhoGEF through its c-terminal PDZ domain binding motif. It has been suggested that Rnd1, which binds to the cytoplasmic part of plexin-B1, can promote the interaction between plexin-B1 and PDZ-RhoGEF. The PDZ domain of LARG is directly involved in the interaction with the c-terminal sequence of Plexin-B1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-416594",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-416594"
}
]
},
{
"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-6785636",
"name": "Phosphorylated ERBB2 heterodimers bind MEMO1",
"equation": "",
"summary": "ERBB2 phosphorylated on tyrosine residue Y1222 binds MEMO1 (mediator of ERBB2-driven cell motility) (Marone et al. 2004, Qiu et al. 2008, Zaoui et al. 2010, Feracci et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-6785636",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6785636"
}
]
},
{
"id": "R-HSA-6785648",
"name": "MEMO1 binds RHOA:GTP:DIAPH1",
"equation": "",
"summary": "MEMO1, in complex with phosphorylated ERBB2 heterodimers, associates with the complex of activated RHOA and formin family member DIAPH1. MEMO1 maintains the plasma membrane association of the RHOA:GTP:DIAPH1 complex (Zaoui et al. 2008) and modulates RHOA:GTP:DIAPH1-regulated actin and microtubule dynamics and the consequent cell motility/migration downstream of ERBB2 (Marone et al. 2004, Zaoui et al. 2010).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P61586-1"
],
"evidence": [
{
"id": "R-HSA-6785648",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6785648"
}
]
},
{
"id": "R-HSA-8847995",
"name": "Activated ERBB2 binds PTK6 (BRK)",
"equation": "",
"summary": "PTK6 (BRK) is a nonreceptor tyrosine kinase that can bind activated ERBB2 receptor (Xiang et al. 2008).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13882-1",
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-8847995",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8847995"
}
]
},
{
"id": "R-HSA-8848005",
"name": "ERBB2 promotes PTK6 autophosphorylation",
"equation": "",
"summary": "Binding of PTK6 (BRK) to activated ERBB2 receptor stimulates autophosphorylation of PTK6 on tyrosine residue Y342 (Xiang et al. 2008, Peng et al. 2015). Autophosphorylation at Y342 significantly increases catalytic activity of PTK6 (Qiu and Miller 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-8848007"
],
"enzyme_list": [
"Q13882-1",
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-8848005",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8848005"
}
]
},
{
"id": "R-HSA-8863804",
"name": "PTPN12 dephosphorylates ERBB2 on tyrosine Y1248",
"equation": "",
"summary": "PTPN12 protein tyrosine phosphatase dephosphorylates activated ERBB2 at tyrosine residue Y1248 and activated EGFR at tyrosine residue Y1148 (Y1148 corresponds to Y1172 of the nascent EGFR, with 24 amino acid signal peptide at the N-terminus). PTPN12-mediated dephosphorylation of ERBB2 attenuates downstream RAS activation, as Y1248 is involved in SHC1 recruitment. Similar to Y1148 of EGFR, Y1248 of ERBB2 is part of the NPXY motif that is, when phosphorylated on the tyrosine residue, recognized by the N-terminal phosphotyrosine interaction domain (PID) of SHC1 (Batzer et al. 1995, Songyang et al. 1995). SHC1 itself could be a target for PTPN12. PTPN12 function is frequently lost in triple negative breast cancer (Sun et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"Q05209-1"
],
"evidence": [
{
"id": "R-HSA-8863804",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8863804"
}
]
},
{
"id": "R-HSA-8864105",
"name": "PTPN18 binds ERBB2:EGFR heterodimers",
"equation": "",
"summary": "PTPN18 protein tyrosine phosphatase (BDP1) binds ERBB2, activated in response to EGF stimulation, via PEST and catalytic domains of PTPN18 (Wang et al. 2014).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"Q99952-1"
],
"evidence": [
{
"id": "R-HSA-8864105",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8864105"
}
]
},
{
"id": "R-HSA-8864125",
"name": "PTPN18 dephosphorylates ERBB2 at Y1196, Y1112 and Y1248",
"equation": "",
"summary": "Protein tyrosine kinase PTPN18 dephosphorylates ERBB2, activated in response to EGF stimulation (Gensler et al. 2004), at tyrosine residues Y1196, Y1112 and Y1248 (Wang et al. 2014). PTPN18 does not dephosphorylate activated EGFR. Dephosphorylation of ERBB2 tyrosines Y1196 and Y1248 attenuates downstream activation of PI3K/AKT and RAS signaling. Dephosphorylation of Y1112 interferes with the recruitment of CBL E3 ubiquitin ligase to activated ERBB2 and CBL-mediated lysosomal route of ERBB2 down-regulation. When phosphorylated by an unknown serine/threonine kinase in an AKT-dependent manner on serine residues S419 and S423, PTPN18 recruits beta-TRCP ubiquitin ligase complex to ERBB2, thus promoting proteasome-dependent ERBB2 degradation (Wang et al. 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"Q99952-1"
],
"evidence": [
{
"id": "R-HSA-8864125",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8864125"
}
]
},
{
"id": "R-HSA-8864466",
"name": "TFAP2A,(TFAP2B,TFAP2C) homo- and heterodimers and YY1 stimulate ERBB2 gene expression",
"equation": "",
"summary": "Binding of AP-2 transcription factors TFAP2A (AP-2 alpha), TFAP2B (AP-2 beta) and TFAP2C (AP-2 gamma) to AP-2 response elements in the ERBB2 gene promoter stimulates ERBB2 transcription, with TFAP2B having the weakest effect (Bosher et al. 1996). Association of YY1 transcription factor with TFAP2A (and, possibly, TFAP2B and TFAP2C) significantly increases the ERBB2 gene transcription rate (Begon et al. 2005).",
"cellular_location": "nucleoplasm, plasma membrane",
"input_participant_list": [
"R-HSA-8864449"
],
"output_participant_list": [
"R-HSA-372889"
],
"enzyme_list": [
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-8864466",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8864466"
}
]
},
{
"id": "R-HSA-9634390",
"name": "ERBB2 homodimer phosphorylates SHC1",
"equation": "",
"summary": "While phosphorylation of SHC1 upon binding to homodimers of overexpressed ERBB2 has not been tested, it is assumed, based on SHC1 binding and downstream activation of RAS signaling (Pickl and Ries 2009), that ERBB2 homodimers, similar to ERBB2 heterodimers, phosphorylate SHC1, enabling it to recruit GRB2:SOS1 complex and activate downstream RAS/RAF/MAPK signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9634390",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9634390"
}
]
},
{
"id": "R-HSA-9634391",
"name": "SHC1 binds phosphorylated ERBB2 homodimer",
"equation": "",
"summary": "SHC1 binds to autophosphorylated ERBB2 homodimers (Pickl and Ries 2009). As PTPN12 dephosphorylates tyrosine Y1248 of ERBB2, inhibiting SHC1 binding to ERBB2 (Sun et al. 2011), and as Y1248 is autophosphorylated in ERBB2 homodimers (Pickl and Ries 2009, Maadi et al. 2018), it is assumed that PTPN12 negatively regulates SHC1 binding to ERBB2 homodimers.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"Q05209-1"
],
"evidence": [
{
"id": "R-HSA-9634391",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9634391"
}
]
},
{
"id": "R-HSA-9634402",
"name": "Recruitment of GRB2:SOS1 to p-SHC1 in complex with phosphorylated ERBB2 homodimer",
"equation": "",
"summary": "Both GRB2 and SHC1 are recruited to autophosphorylated ERBB2 homodimers (Pickl and Ries 2009). It is assumed, by analogy to the behavior of normal ERBB2 heterodimers, that GRB2 is recruited to ERBB2 homodimers through SHC1, and that GRB2 is in complex with SOS1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9634402",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9634402"
}
]
},
{
"id": "R-HSA-9634418",
"name": "RAS guanyl-nucleotide exchange mediated by SOS1 in complex with GRB2 and ERBB2 homodimer:p-SHC1",
"equation": "",
"summary": "Based on activation of RAS signaling by autophosphorylated ERBB2 homodimers, as well as binding of GRB2 and SHC1 to ERBB2 homodimers (Pickl and Ries 2009), it is assumed that SOS1, recruited to ERBB2 homodimers through GRB2, mediates GDP to GTP exchange on RAS protein family, resulting in formation of the active RAS:GTP complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9634418",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9634418"
}
]
},
{
"id": "R-HSA-9649393",
"name": "ERBB2 KD mutants bind trastuzumab",
"equation": "",
"summary": "The following ERBB2 KD mutants are at least partially sensitive to the therapeutic antibody trastuzumab (herceptin):
ERBB2 L755M (Nagano et al. 2018);
ERBB2 D769H (Nagano et al. 2018);
ERBB2 V777M (Nagano et al. 2018);
ERBB2 H878Y (Nagano et al. 2018);",
"cellular_location": "cytosol, extracellular region",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9649393",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9649393"
}
]
},
{
"id": "R-HSA-9652264",
"name": "ERBB2 binds TKIs",
"equation": "",
"summary": "ERBB2 can bind to and be inhibited by the following tyrosine kinase inhibitors (TKIs):
lapatinib (Xia et al. 2002, Wood et al. 2004)
neratinib (Rabindran et al. 2004)
afatinib (Li et al. 2008)
AZ5104 (Hanker et al. 2017)
tesevatinib (Gendreau et al. 2007)
canertinib (Nelson and Fry 2001)
sapitinib (Hickinson et al. 2010)
CP-724714 (Jani et al. 2007)
AEE788 (Traxler et al. 2014). Tyrosine kinase inhibitors do not prevent ERBB2 heterodimerization, but intefere with its kinase activity.
The following tyrosine kinase inhibitors were shown to be especially effective against overexpressed ERBB2 and to inhibit kinase activity of ERBB2 homodimers:
afatinib (Rabindran et al. 2004)
neratinib (Rabindran et al. 2004)
lapatinib (Rabindran et al. 2004).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9652264",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9652264"
}
]
},
{
"id": "R-HSA-9652277",
"name": "ERBB2 binds trastuzumab",
"equation": "",
"summary": "ERBB2 signaling is inhibited by binding of ERBB2 to ERBB2-directed therapeutic recombinant antibody trastuzumab (herceptin), used an anti-cancer therapeutic in tumors that overexpress ERBB2 (Hudziak et al. 1989, Carter et al. 1992). Trastuzumab does not prevent homodimerization of overexpressed ERBB2 and remains bound to ERBB2 (HER2) homodimers (Maadi et al. 2018). Autophosphorylation of ERBB2 homodimers and downstream signaling is inhibited by trastuzumab (Pickl and Ries 2009). It is unclear whether trastuzumab mainly acts through endocytosis-mediated downregulation of ERBB2 receptor on the cell surface or through interference with the kinase activity. The mechanism of trastuzumab action may also rely on antibody-dependent cellular cytotoxicity (ADCC) (Maadi et al. 2008).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9652277",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9652277"
}
]
},
{
"id": "R-HSA-9664567",
"name": "ERBB2 KD mutants heterodimerize",
"equation": "",
"summary": "The following ERBB2 KD mutants were directly or indirectly shown to form heterodimers with EGFR:
ERBB2 L755P (Kancha et al. 2011 \u2013 indirect, higher catalytic activity in the presence of EGF stimulated EGFR);
ERBB2 L755S (Kancha et al. 2011, Bose et al. 2013 \u2013 indirect, higher kinase activity in the presence of EGFR);
ERBB2 I767M (Bose et al. 2013 \u2013 indirect, EGFR is phosphorylated in the presence of ERBB2 I767M);
ERBB2 D769H (Bose et al. 2013 \u2013 indirect, trans autophosphorylation in the presence of EGFR);
ERBB2 D769Y (Bose et al. 2013 \u2013 indirect, trans autophosphorylation in the presence of EGFR);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013 \u2013 indirect, increased catalytic activity in the presence of EGF activated EGFR);
ERBB2 G778_P780dup (Bose et al. 2013, Suzawa et al. 2016, Ogoshi et al. 2019 \u2013 indirect, trans-autophosphorylates in the presence of EGFR);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013 \u2013 indirect, trans-autophosphorylation in the presence of EGF-stimulated EGFR);
ERBB2 V842I (Bose et al. 2013 \u2013 indirect, trans-autophosphorylation in the presence of EGFR);
ERBB2 T862A (Kancha et al. 2011 \u2013indirect, increased catalytic activity in the presence of EGF activated EGFR);
ERBB2 H878Y (Kancha et al. 2011 \u2013 indirect, activated in the presence of EGF-stimulated EGFR);
ERBB2 R896C (Bose et al. 2013 \u2013 indirect, trans autophosphorylation in the presence of EGFR);
ERBB2 L755_T759del (Bose et al. 2013 \u2013 indirect, EGFR phosphorylated in the presence of the mutant);
ERBB2 Y772_A775dup (Wang et al. 2006 - direct)
The following ERBB2 KD mutants were directly or indirectly shown to form heterodimers with ERBB3:
ERBB2 L755P (Kancha et al. 2011 \u2013 indirect, higher catalytic activity in the presence of neuregulin stimulated ERBB3);
ERBB2 L755S (Croessmann et al. 2019 \u2013 direct, mutant forms heterodimers with ERBB3 at a higher rate than the wild type ERBB2; Kancha et al. 2011, Bose et al. 2013 \u2013 indirect, higher kinase activity in the presence of ERBB3);
ERBB2 I767M (Ng et al. 2015 \u2013 indirect, catalytic activity induced by neuregulin-1 (NRG1));
ERBB2 D769H (Collier al. 2013 \u2013 direct, 3-fold increase in catalytic activity upon heterodimerization);
ERBB2 D769Y (Collier al. 2013 \u2013 direct, 3-fold increase in catalytic activity upon heterodimerization);
ERBB2 G776S (Fan et al. 2008 \u2013 indirect, trans-autophosphorylation increased in the presence of the mutant);
ERBB2 V777L (Croessmann et al. 2019 \u2013 direct, mutant forms heterodimers with ERBB3 at a higher rate than the wild type ERBB2; Kancha et al. 2011, Bose et al. 2013 \u2013 indirect, increased catalytic activity in the presence of neuregulin-activated ERBB3);
ERBB2 T798M (Rexer et al. 2013 \u2013 direct, co-immunoprecipitates with ERBB3; Kancha et al. 2011, Rexer et al. 2013 \u2013 indirect, trans-autophosphorylation in the presence of neuregulin-stimulated ERBB3);
ERBB2 V842I (Bose et al. 2013 \u2013 indirect, trans-autophosphorylation in the presence of ERBB3);
ERBB2 T862A (Kancha et al. 2011 - indirect, increased catalytic activity in the presence of neuregulin-activated ERBB3);
ERBB2 L869R (Hanker et al. 2017 \u2013 direct, heterodimerization may be increased in the presence of ERBB3 E928G mutant);
ERBB2 H878Y (Kancha et al. 2011 \u2013 indirect, activated in the presence of neuregulin-stimulated ERBB3);
ERBB2 L755_T759del (Bose et al. 2013 \u2013 indirect, ERBB3 phosphorylated in the presence of the mutant);
ERBB2 Y772_A775dup (Wang et al. 2006 - direct)
Heterodimerizaton of ERBB2 KD mutants with ERBB4 has not been tested and ERBB4 is shown as a heterodimerization candidate.
Heterodimerization properties of the following ERBB2 KD mutants have not been tested and they are annotated as candidates based on their substituted residue being identical to the substituted residue of functionally studied mutants and based on computational prediction of the pathogenicity of the mutation in COSMIC database:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769N
ERBB2 V777E
ERBB2 V777M
ERBB2 T733I
ERBB2 T798I
ERBB2 V842E
ERBB2 L869Q
ERBB2 H878R
ERBB2 R896H
ERBB2 G776C
ERBB2 G776L
ERBB2 G776V",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9664567",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664567"
}
]
},
{
"id": "R-HSA-9664588",
"name": "ERBB2 KD mutants trans-autophosphorylate",
"equation": "",
"summary": "The following ERBB2 KD mutants were shown to undergo trans-autophosphorylation in the presence of EGFR:
ERBB2 L755P (Bose et al. 2013);
ERBB2 L755S (Kancha et al. 2011, Bose et al. 2013);
ERBB2 I767M (Bose et al. 2013);
ERBB2 D769H (Bose et al. 2013);
ERBB2 D769Y (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Bose et al. 2013, Suzawa et al. 2016, Ogoshi et al. 2019);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013)
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);ERBB2 Y772_A775dup (Wang et al. 2006)
The following ERBB2 KD mutants were shown to undergo trans-autophosphorylation in the presence of ERBB3:
ERBB2 L755P (Bose et al. 2013);
ERBB2 L755S (Kancha et al. 2011, Bose et al. 2013);
ERBB2 I767M (Ng et al. 2015 \u2013 indirect, in response to neuregulin-1 (NRG1) treatment);
ERBB2 D769H (Bose et al. 2013, Collier et al. 2013);
ERBB2 D769Y (Bose et al. 2013, Collier et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 G776S (Fan et al. 2008);
ERBB2 Y772_A775dup (Wang et al. 2006)
In the majority of studies, trans-autophosphorylation of specific tyrosine residues of ERBB2 KD mutants and its heterodimerization partners, EGFR and ERBB3 (and ERBB4), has not been examined, and they are assumed to be identical to tyrosine residues that undergo trans-autophosphorylation in the wild type ERBB2 heterodimers. ERBB2 H878Y is also phosphorylated on the substitution tyrosine Y878 (Hu, Wan et al. 2015). EGFR and ERBB3 undergo trans-autophosphorylation in the presence of ERBB2 L755_T759del mutant, while ERBB2 L755_T759del remains unphosphorylated (Bose et al. 2013).
Phosphorylation at tyrosine Y1221 was demonstrated for the following ERBB2 KD mutants:
ERBB2 L755S (Trowe et al. 2008);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 L869R (Hanker et al. 2017);
Phosphorylation at tyrosine Y1222 was demonstrated for the following ERBB2 KD mutants:
ERBB2 L755S (Trowe et al. 2008);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 L869R (Hanker et al. 2017);
Phosphorylation at tyrosine Y1248 was demonstrated for the following ERBB2 KD mutants:
ERBB2 L755S (Croessmann et al. 2019);
ERBB2 V777L (Croessmann et al. 2019);
ERBB2 T798M (Rexer et al. 2013);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 Y772_A775dup (Wang et al. 2006);
Phosphorylation of EGFR at tyrosine Y1068 was demonstrated in the presence of the following ERBB2 KD mutants:
ERBB2 T798M (Rexer et al. 2013);
ERBB2 Y772_A775dup (Wang et al. 2006)
Phosphorylation of ERBB3 at tyrosine Y1197 was demonstrated in the presence of the following ERBB2 KD mutants:
ERBB2 L755S (Croessmann et al. 2019);
ERBB2 V777L (Croessmann et al. 2019);
ERBB2 T798M (Rexer et al. 2013);
ERBB2 L869R (Hanker et al. 2017);
Phosphorylation of ERBB3 at tyrosine Y1289 was demonstrated in the presence of the following ERBB2 KD mutants:
ERBB2 Y772_A775dup (Wang et al. 2006, Minami et al. 2007);
Trans-autophosphorylation of the following ERBB2 KD mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 L869Q
ERBB2 H878R
ERBB2 R896H
ERBB2 G776C
ERBB2 G776L
ERBB2 G776V",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9664588",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664588"
}
]
},
{
"id": "R-HSA-9664646",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants and ERBB3 bind PI3K",
"equation": "",
"summary": "Many ERBB3-binding ERBB2 KD mutants were shown to activate PI3K/AKT signaling, as evidenced by activating phosphorylation of AKT in the presence of these ERBB2 KD mutants. Phosphorylated heterodimers of the following ERBB2 KD mutants with ERBB3 are assumed to, like the wild type ERBB2:ERBB3 heterodimer, bind to the PI3K complex:
ERBB2 L755S (Kancha et al. 2011, Cocco et al. 2018, Croessmann et al. 2019);
ERBB2 L755P (Kancha et al. 2011);
ERBB2 I767M (Ng et al. 2015);
ERBB2 V777L (Kancha et al. 2011);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of PI3K/AKT signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 L869Q
ERBB2 H878R",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664646",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664646"
}
]
},
{
"id": "R-HSA-9664664",
"name": "PI3K bound to phosphorylated heterodimers of ERBB2 KD mutants and ERBB3 converts PIP2 to PIP3",
"equation": "",
"summary": "For the ERBB3-binding ERBB2 KD mutants that were shown to activate PI3K/AKT signaling (evidenced by activating phosphorylation of AKT), it is assumed that, like the wild type ERBB2:ERBB3 heterodimer, the heterodimers of these ERBB2 KD mutants with ERBB3 bind to the PI3K complex, leading to conversion of PIP2 to PIP3.
Phosphorylated heterodimers of the following ERBB2 KD mutants with ERBB3 are assumed to, like the wild type ERBB2:ERBB3 heterodimer, recruit and activate the PI3K complex, resulting in conversion of PIP2 to PIP3:
ERBB2 L755S (Kancha et al. 2011, Cocco et al. 2018, Croessmann et al. 2019);
ERBB2 L755P (Kancha et al. 2011);
ERBB2 I767M (Ng et al. 2015);
ERBB2 V777L (Kancha et al. 2011);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 Y772_A775dup (Wang et al. 2006)
Activation of PI3K/AKT signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 L869Q
ERBB2 H878R",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664664",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664664"
}
]
},
{
"id": "R-HSA-9664918",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind GRB2:GAB1",
"equation": "",
"summary": "Many EGFR-binding ERBB2 KD mutants were shown to activate PI3K/AKT signaling, as evidenced by activating phosphorylation of AKT in the presence of these ERBB2 KD mutants. Phosphorylated heterodimers of the following ERBB2 KD mutants with EGFR are assumed to, like the wild type ERBB2:EGFR heterodimer, bind to the GRB2:GAB1 complex:
ERBB2 L755S (Kancha et al. 2011, Cocco et al. 2018, Croessmann et al. 2019);
ERBB2 L755P (Kancha et al. 2011);
ERBB2 I767M (Ng et al. 2015; heterodimerization with EGFR indirectly shown by Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of PI3K/AKT signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 H878R",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664918",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664918"
}
]
},
{
"id": "R-HSA-9664933",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants and EGFR, in complex with GRB2:GAB1, bind PI3K",
"equation": "",
"summary": "For the following EGFR-binding ERBB2 KD mutants that activate PI3K/AKT signaling, it is assumed that, like the wild type ERBB2:EGFR heterodimer, binding to the GRB2:GAB1 adaptor complex leads to recruitment of the PI3K complex:
ERBB2 L755S (Kancha et al. 2011, Cocco et al. 2018, Croessmann et al. 2019);
ERBB2 L755P (Kancha et al. 2011);
ERBB2 I767M (Ng et al. 2015; heterodimerization with EGFR indirectly shown by Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of PI3K/AKT signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 H878R",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664933",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664933"
}
]
},
{
"id": "R-HSA-9664940",
"name": "PI3K bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR converts PIP2 to PIP3",
"equation": "",
"summary": "For the following EGFR-binding ERBB2 KD mutants that were shown to activate PI3K/AKT signaling, it is assumed that heterodimers of these mutants with EGFR, like the wild type ERBB2:EGFR heterodimer, bind to the PI3K complex through GRB2:GAB1, leading to conversion of PIP2 to PIP3:
ERBB2 L755S (Kancha et al. 2011, Cocco et al. 2018, Croessmann et al. 2019);
ERBB2 L755P (Kancha et al. 2011);
ERBB2 I767M (Ng et al. 2015; heterodimerization with EGFR indirectly shown by Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of PI3K/AKT signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 H878R",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664940",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664940"
}
]
},
{
"id": "R-HSA-9664950",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants bind SHC1",
"equation": "",
"summary": "Many ERBB2 KD mutants were shown to activate RAS/RAF/MAPK signaling, evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). Based on downstream activation of RAS/RAF/MAPK cascade, it is assumed that phosphorylated heterodimers of the following ERBB2 KD mutants, like phosphorylated heterodimers of the wild type ERBB2, bind to SHC1:
ERBB2 L755P (Kancha et al. 2011);
ERBB2 L755S (Trowe et al. 2008, Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018);
ERBB2 I767M (Ng et al. 2015);
ERBB2 D769H (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 G776S (Fan et al. 2008);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of RAS/RAF/MAPK signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769Y
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 L869Q
ERBB2 H878R
ERBB2 R896H
ERBB2 G776C
ERBB2 G776L
ERBB2 G776V",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664950",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664950"
}
]
},
{
"id": "R-HSA-9664976",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants phosphorylate SHC1",
"equation": "",
"summary": "For the following ERBB2 KD mutants that were shown to activate RAS/RAF/MAPK signaling, it is assumed that they, like phosphorylated heterodimers of the wild type ERBB2, bind to SHC1 and phosphorylate it:
ERBB2 L755P (Kancha et al. 2011);
ERBB2 L755S (Trowe et al. 2008, Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018);
ERBB2 I767M (Ng et al. 2015);
ERBB2 D769H (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 G776S (Fan et al. 2008);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of RAS/RAF/MAPK signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769Y
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 L869Q
ERBB2 H878R
ERBB2 R896H
ERBB2 G776C
ERBB2 G776L
ERBB2 G776V",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664976",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664976"
}
]
},
{
"id": "R-HSA-9664983",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants recruit GRB2:SOS1 through SHC1",
"equation": "",
"summary": "For the following ERBB2 KD mutants that were shown to activate RAS/RAF/MAPK signaling, it is assumed that they, like phosphorylated heterodimers of the wild type ERBB2, bind to and phosphorylate SHC1, leading to recruitment of the GRB2:SOS1 complex:
ERBB2 L755P (Kancha et al. 2011);
ERBB2 L755S (Trowe et al. 2008, Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018);
ERBB2 I767M (Ng et al. 2015);
ERBB2 D769H (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 G776S (Fan et al. 2008);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of RAS/RAF/MAPK signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769Y
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 L869Q
ERBB2 H878R
ERBB2 R896H
ERBB2 G776C
ERBB2 G776L
ERBB2 G776V",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9664983",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664983"
}
]
},
{
"id": "R-HSA-9664991",
"name": "RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants",
"equation": "",
"summary": "For the following ERBB2 KD mutants that were shown to activate RAS/RAF/MAPK signaling, it is assumed that they, like phosphorylated heterodimers of the wild type ERBB2, bind to and phosphorylate SHC1, leading to recruitment of the GRB2:SOS1 complex and activating guanyl-nucleotide exchange on RAS:
ERBB2 L755P (Kancha et al. 2011);
ERBB2 L755S (Trowe et al. 2008, Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018);
ERBB2 I767M (Ng et al. 2015);
ERBB2 D769H (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 G776S (Fan et al. 2008);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of RAS/RAF/MAPK signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769Y
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 L869Q
ERBB2 H878R
ERBB2 R896H
ERBB2 G776C
ERBB2 G776L
ERBB2 G776V",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9664991",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9664991"
}
]
},
{
"id": "R-HSA-9665000",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind GRB2:SOS1",
"equation": "",
"summary": "The following EGFR-binding ERBB2 KD mutants that were shown to activate RAS/RAF/MAPK signaling, evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3), are assumed to, like the wild type ERBB2:EGFR heterodimer, directly bind to the GRB2:SOS1 complex:
ERBB2 L755S (Trowe et al. 2008, Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018);
ERBB2 L755P (Kancha et al. 2011);
ERBB2 I767M (Ng et al. 2015; binding to EGFR indirectly demonstrated by Bose et al. 2013);
ERBB2 D769H (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of RAS/RAF/MAPK signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769Y
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 H878R
ERBB2 R896H",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665000",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665000"
}
]
},
{
"id": "R-HSA-9665009",
"name": "RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 KD mutants and EGFR",
"equation": "",
"summary": "The following EGFR-binding ERBB2 KD mutants that were shown to activate RAS/RAF/MAPK signaling, evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3), are assumed to, like the wild type ERBB2:EGFR heterodimer, directly bind to the GRB2:SOS1 complex, leading to activating guanyl nucleotide exchange on RAS:
ERBB2 L755S (Trowe et al. 2008, Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018);
ERBB2 L755P (Kancha et al. 2011);
ERBB2 I767M (Ng et al. 2015; binding to EGFR indirectly demonstrated by Bose et al. 2013);
ERBB2 D769H (Bose et al. 2013);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013);
ERBB2 G778_P780dup (Suzawa et al. 2016);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013);
ERBB2 T798I (Hanker et al. 2017);
ERBB2 V842I (Bose et al. 2013);
ERBB2 T862A (Kancha et al. 2011);
ERBB2 H878Y (Kancha et al. 2011, Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 Y772_A775dup (Wang et al. 2006);
Activation of RAS/RAF/MAPK signaling downstream of the following ERBB2 KD cancer mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769Y
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 T733I
ERBB2 V842E
ERBB2 H878R
ERBB2 R896H",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9665009",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665009"
}
]
},
{
"id": "R-HSA-9665032",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants and EGFR phosphorylate PLCG1",
"equation": "",
"summary": "It is assumed that the following EGFR-binding ERBB2 mutants that were shown to activate PLCG1 (PLCgamma-1) signaling, evidenced by activating phosphorylation of PLCG1, recruit and phosphorylate PLCG1:
ERBB2 L755S (Bose et al. 2013);
ERBB2 I767M (Bose et al. 2013);
ERBB2 D769H (Bose et al. 2013);
ERBB2 D769Y (Bose et al. 2013);
ERBB2 V777L (Bose et al. 2013);
ERBB2 G778_P780dup (Bose et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 H878Y (Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
It is assumed that, like the wild type ERBB2:EGFR heterodimer, phosphorylated heterodimers of these ERBB2 KD mutants and EGFR recruit PLCG1.
ERBB2 L755_T759del does not activate PLCG1 signaling (Bose et al. 2013).
Activation of PLCG1 downstream of the following PLCG1 mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 V842E
ERBB2 H878R
ERBB2 R896H",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-9665032",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665032"
}
]
},
{
"id": "R-HSA-9665034",
"name": "Phosphorylated heterodimers of ERBB2 KD mutants and EGFR bind PLCG1",
"equation": "",
"summary": "Activating phosphorylation of PLCG1 (PLCgamma-1) is increased in the presence of the following EGFR-binding ERBB2 KD mutants:
ERBB2 L755S (Bose et al. 2013);
ERBB2 I767M (Bose et al. 2013);
ERBB2 D769H (Bose et al. 2013);
ERBB2 D769Y (Bose et al. 2013);
ERBB2 V777L (Bose et al. 2013);
ERBB2 G778_P780dup (Bose et al. 2013);
ERBB2 V842I (Bose et al. 2013);
ERBB2 H878Y (Hu, Hu et al. 2015, Hu, Wan et al. 2015);
ERBB2 R896C (Bose et al. 2013);
It is assumed that, like the wild type ERBB2:EGFR heterodimer, phosphorylated heterodimers of these ERBB2 KD mutants and EGFR recruit PLCG1.
ERBB2 L755_T759del does not activate PLCG1 signaling (Bose et al. 2013).
Activation of PLCG1 downstream of the following PLCG1 mutants has not been studied and they are annotated as candidates:
ERBB2 L755M
ERBB2 L755W
ERBB2 D769N
ERBB2 V777M
ERBB2 V777E
ERBB2 V842E
ERBB2 H878R
ERBB2 R896H",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-9665034",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665034"
}
]
},
{
"id": "R-HSA-9665121",
"name": "ERBB2 KD mutants bind TKIs",
"equation": "",
"summary": "Sensitivity to different tyrosine kinase inhibitors varies among ERBB2 mutants.
The following ERBB2 KD mutants are at least partially sensitive to lapatinib:
ERBB2 L755M (Nagano et al. 2018 - partial sensitivity);
ERBB2 D769H (Bose et al. 2013, Nagano et al. 2018);
ERBB2 V777L (Kancha et al. 2011, Bose et al. 2013, Nagano et al. 2018);
ERBB2 V777M (Nagano et al. 2018);
ERBB2 T862A (Kancha et al. 2011 - partial sensitivity, Nagano et al. 2018 - partial sensitivity);
ERBB2 H878Y (Kancha et al. 2011, Nagano et al. 2018);
The following ERBB2 KD mutants are at least partially sensitive to neratinib (HKI-272):
ERBB2 L755M (Nagano et al. 2018);
ERBB2 L755P (Nagano et al. 2018 - partial sensitivity);
ERBB2 L755S (Cocco et al. 2018; Nagano et al. 2018 - partial sensitivity);
ERBB2 I767M (Bose et al. 2013, Nagano et al. 2018);
ERBB2 D769H (Bose et al. 2013, Nagano et al. 2018);
ERBB2 D769Y (Bose et al. 2013, Nagano et al. 2018);
ERBB2 V777L (Bose et al. 2013, Nagano et al. 2018);
ERBB2 V777M (Nagano et al. 2018);
ERBB2 G778_P780dup (Bose et al. 2013, Nagano et al. 2018, Ogoshi et al. 2018);
ERBB2 V842I (Bose et al. 2013, Nagano et al. 2018);
ERBB2 T862A (Nagano et al. 2018);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Hu, Hu et al. 2015, Hu, Wan et al. 2015, Nagano et al. 2018);
ERBB2 R896C (Bose et al. 2013, Nagano et al. 2018);
ERBB2 L755_T759del (Bose et al. 2013);
ERBB2 Y772_A775dup (Minami et al. 2007)
The following ERBB2 KD mutants are at least partially sensitive to osimertinib:
ERBB2 L755M (Nagano et al. 2018);
ERBB2 L755P (Nagano et al. 2018);
ERBB2 L755S (Nagano et al. 2018);
ERBB2 I767M (Nagano et al. 2018);
ERBB2 D769H (Nagano et al. 2018);
ERBB2 D769Y (Nagano et al. 2018);
ERBB2 V777L (Nagano et al. 2018);
ERBB2 V777M (Nagano et al. 2018);
ERBB2 G778_P780dup (Nagano et al. 2018 - partial response);
ERBB2 V842I (Nagano et al. 2018);
ERBB2 T862A (Nagano et al. 2018);
ERBB2 H878Y (Nagano et al. 2018);
ERBB2 R896C (Nagano et al. 2018);
The following ERBB2 KD mutants are at least partially sensitive to afatinib (BIBW2992):
ERBB2 L755M (Nagano et al. 2018);
ERBB2 L755P (Nagano et al. 2018 - partial sensitivity);
ERBB2 L755S (Nagano et al. 2018 - partial sensitivity);
ERBB2 D769H (Nagano et al. 2018);
ERBB2 D769Y (Nagano et al. 2018);
ERBB2 V777L (Nagano et al. 2018);
ERBB2 V777M (Nagano et al. 2018);
ERBB2 G778_P780dup (Suzawa et al. 2016, Nagano et al. 2018)
ERBB2 T798I (Hanker et al. 2017);
ERBB2 V842I (Nagano et al. 2018);
ERBB2 T862A (Nagano et al. 2018);
ERBB2 L869R (Hanker et al. 2017);
ERBB2 H878Y (Hu, Wan et al. 2015, Nagano et al. 2018);
ERBB2 R896C (Nagano et al. 2018);
The following ERBB2 KD mutants are at least partially sensitive to AZ5104:
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Hanker et al. 2017 \u2013 partial sensitivity);
ERBB2 L869R (Hanker et al. 2017);
The following ERBB2 KD mutants are at least partially sensitive to tesevatinib (EXEL-7647):
ERBB2 L755S (Trowe et al. 2008);
ERBB2 T798I (Trowe et al. 2008);
The following ERBB2 KD mutants are at least partially sensitive to canertinib (CI-1033):
ERBB2 H878Y (Hu, Wan et al. 2015);
The following ERBB2 KD mutants are at least partially sensitive to sapitinib:
ERBB2 L755M (Nagano et al. 2018 - partial sensitivity);
ERBB2 L755P (Nagano et al. 2018 - partial sensitivity);
ERBB2 L755S (Nagano et al. 2018 - partial sensitivity);
ERBB2 I767M (Nagano et al. 2018 - partial response);
ERBB2 D769H (Nagano et al. 2018);
ERBB2 D769Y (Nagano et al. 2018);
ERBB2 V777L (Nagano et al. 2018);
ERBB2 V777M (Nagano et al. 2018 - partial response);
ERBB2 G778_P780dup (Nagano et al. 2018);
ERBB2 V842I (Nagano et al. 2018 - partial response);
ERBB2 H878Y (Nagano et al. 2018 - partial sensitivity)
ERBB2 R896C (Nagano et al. 2018 partial sensitivity);
The following ERBB2 KD mutants are at least partially sensitive to CP-724714:
ERBB2 H878Y (Hu, Wan et al. 2015);
The following ERBB2 KD mutants are at least partially sensitive to AEE788:
ERBB2 H878Y (Kancha et al. 2011; Hu, Wan et al. 2015);
The following ERBB2 KD mutants are at least partially sensitive to gefitinib
ERBB2 L755_T759del (Bose et al. 2013);",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665121",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665121"
}
]
},
{
"id": "R-HSA-9665232",
"name": "Resistant ERBB2 KD mutants do not bind trastuzumab",
"equation": "",
"summary": "The following ERBB2 KD mutants are resistant to the therapeutic antibody trastuzumab (herceptin):
ERBB2 L755P (Nagano et al. 2018);
ERBB2 L755S (Nagano et al. 2018);
ERBB2 I767M (Bose et al. 2013);
ERBB2 D769Y (Nagano et al. 2018);
ERBB2 V777L (Nagano et al. 2018);
ERBB2 G778_P780dup (Bose et al. 2013, Nagano et al. 2018);
ERBB2 T798M (Rexer et al. 2013);
ERBB2 V842I (Nagano et al. 2018);
ERBB2 T862A (Nagano et al. 2018);
ERBB2 L869R (Hanker et al. 2017);
For ERBB2 R896C, both resistance (Bose et al. 2013) and sensitivity (Nagano et al. 2018) to trastuzumab have been reported.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665232",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665232"
}
]
},
{
"id": "R-HSA-9665278",
"name": "Resistant ERBB2 KD mutants do not bind AEE788",
"equation": "",
"summary": "The following ERBB2 KD mutants are resistant to AEE788:
ERBB2 L755P (Kancha et al. 2011);
ERBB2 L755S (Kancha et al. 2011);
ERBB2 V777L (Kancha et al. 2011);
ERBB2 T798M (Kancha et al. 2011);
ERBB2 T862A (Kancha et al. 2011);",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665278",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665278"
}
]
},
{
"id": "R-HSA-9665280",
"name": "ERBB2 KD mutants do not bind osimertinib",
"equation": "",
"summary": "The following ERBB2 KD mutants are resistant to osmertinib:
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Hanker et al. 2017);
ERBB2 L869R (Hanker et al. 2017);",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665280",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665280"
}
]
},
{
"id": "R-HSA-9665284",
"name": "Resistant ERBB2 KD mutants do not bind lapatinib",
"equation": "",
"summary": "The following ERBB2 KD mutants are resistant to lapatinib:
ERBB2 L755P (Kancha et al. 2011; Yang et al. 2015 - the L755P substitution results in a structural change that makes binding to lapatinib energetically unfavorable; Nagano et al. 2018);
ERBB2 L755S (Kancha et al. 2011, Bose et al. 2013, Cocco et al. 2018, Nagano et al. 2018);
ERBB2 D769Y (Bose et al. 2013; partial sensitivity reported by Nagano et al. 2018);
ERBB2 T798I (Trowe et al. 2008);
ERBB2 T798M (Kancha et al. 2011, Rexer et al. 2013, Hanker et al. 2017);
ERBB2 T733I (Trowe et al. 2008);
ERBB2 V842I (Bose et al. 2013, Nagano et al. 2018);
ERBB2 L869R (Hanker et al. 2017);
One study reported sensitivity of ERBB2 I767M, ERBB2 G778_P780dup and ERBB2 R896C to lapatinib (Nagano et al. 2018), while another study reported resistance (Bose et al. 2013).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665284",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665284"
}
]
},
{
"id": "R-HSA-9665286",
"name": "Resistant ERBB2 KD mutants do not bind neratinib",
"equation": "",
"summary": "The following ERBB2 KD mutants are resistant to neratinib (HKI-272):
ERBB2 T798I (Hanker et al. 2017);
ERBB2 T798M (Hanker et al. 2017);",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665286",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665286"
}
]
},
{
"id": "R-HSA-9665304",
"name": "ERBB2 T862A does not bind sapitinib",
"equation": "",
"summary": "The following ERBB2 KD mutants are resistant to sapitinib:
ERBB2 T862A (Nagano et al. 2018);",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665304",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665304"
}
]
},
{
"id": "R-HSA-9665311",
"name": "ERBB2 T798M does not bind afatinib",
"equation": "",
"summary": "The following ERBB2 KD mutants are resistant to afatinib (BIBW2992):
ERBB2 T798M (Rexer et al. 2013, Hanker et al. 2017);",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665311",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665311"
}
]
},
{
"id": "R-HSA-9665315",
"name": "ERBB2 T733I does not bind tesevatinib",
"equation": "",
"summary": "The following ERBB2 KD mutants are resistant to tesevatinib (EXEL-7647):
ERBB2 T733I (Trowe et al. 2008);",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665315",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665315"
}
]
},
{
"id": "R-HSA-9665388",
"name": "ERBB2 ECD mutants heterodimerize with EGFR",
"equation": "",
"summary": "ERBB2 extracellular domain (ECD) mutants harbor missense mutations that lead to substitutions of amino acid residues in the heterodimerization arm contact surface, involved in formation of ERBB2 heterodimers. The functionally studied ERBB2 ECD mutants, ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012) seem to preferntially heterodimerize with EGFR. Heterodimerization of ERBB2 G309E involves formation of disulfide bonds (Greulich et al. 2012).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665388",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665388"
}
]
},
{
"id": "R-HSA-9665389",
"name": "Heterodimers of ERBB2 ECD mutants and EGFR trans-autophosphorylate",
"equation": "",
"summary": "ERBB2 S310F shows stronger activation of downstream signaling than ERBB2 G309A and ERBB2 G309E, and is hyperphosphorylated on tyrosine residues in the C-tail (Greulich et al. 2012), while the C-tail phosphorylation of ERBB2 G309A (Bose et al. 2013) and ERBB2 G309E (Greulich et al. 2012) is comparable to the wild type ERBB2. Phosphorylation of EGFR was demonstrated in the presence of ERBB2 G309A (Bose et al. 2013). Except for ERBB2 C-tail tyrosine residues Y1221 and Y1222, which were shown to undergo trans-autophosphorylation in ERBB2 G309E, ERBB2 S310F and ERBB2 S310Y (Greulich et al. 2012), phosphorylation of specific tyrosine residues in ERBB2 and EGFR has not been examined and they are assumed to be the same as in the wild type ERBB2 heterodimers with EGFR.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665389",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665389"
}
]
},
{
"id": "R-HSA-9665404",
"name": "RAS guanyl nucleotide exchange mediated by the p-6Y- ERBB2 ECD mutants:EGF:p-6Y-EGFR:p-SHC1:GRB2:SOS1",
"equation": "",
"summary": "RAS signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like phosphorylated heterodimers of the wild type ERBB2, can recruit the GRB2:SOS1 complex through phosphorylated SHC1, leading to guanyl nucleotide exchange on RAS and activation of RAS signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9665404",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665404"
}
]
},
{
"id": "R-HSA-9665405",
"name": "ERBB2 ECD mutants bind trastuzumab",
"equation": "",
"summary": "Comapred with the wild type ERBB2, ERBB2 G309E, ERBB2 S310F and ERBB2 S310Y are more sensitive to the ERBB2-directed therapeutic antibody trastuzumab (herceptin) (Greulich et al. 2012). ERBB2 G309A was also responsive to trastuzumab (Bose et al. 2013).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665405",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665405"
}
]
},
{
"id": "R-HSA-9665406",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR phosphorylate SHC1",
"equation": "",
"summary": "RAS signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like phosphorylated heterodimers of the wild type ERBB2, can bind to and phosphorylate SHC1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665406",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665406"
}
]
},
{
"id": "R-HSA-9665407",
"name": "PI3K bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR converts PIP2 to PIP3",
"equation": "",
"summary": "ERBB2 G309E and ERBB2 S310F activate PI3K/AKT signaling, demonstrated by activating phosphorylation of AKT1 (Greulich et al. 2012). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like the wild type heterodimers of ERBB2 and EGFR, can bind to the GRB2:GAB1 complex, leading to recruitment of the PI3K complex, which results in conversion of PIP2 to PIP3 and activation of the AKT signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665407",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665407"
}
]
},
{
"id": "R-HSA-9665408",
"name": "RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR through GRB2",
"equation": "",
"summary": "RAS signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like phosphorylated heterodimers of the wild type ERBB2, can directly recruit the GRB2:SOS1 complex, leading to guanyl nucleotide exchange on RAS and activation of RAS signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9665408",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665408"
}
]
},
{
"id": "R-HSA-9665409",
"name": "GRB2:SOS1 binds to phosphorylated heterodimers of ERBB2 ECD mutants and EGFR",
"equation": "",
"summary": "RAS signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like phosphorylated heterodimers of the wild type ERBB2, can directly recruit the GRB2:SOS1 complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665409",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665409"
}
]
},
{
"id": "R-HSA-9665410",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind PLCG1",
"equation": "",
"summary": "PLCgamma1 signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of PLCG1. It is assumed that heterodimers of ERBB2 ECD mutants and EGFR, like the wild type heterodimers of ERBB2 and EGFR, bind to PLCG1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-9665410",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665410"
}
]
},
{
"id": "R-HSA-9665411",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR phosphorylate PLCG1",
"equation": "",
"summary": "PLCgamma1 signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of PLCG1. It is assumed that heterodimers of ERBB2 ECD mutants and EGFR, like the wild type heterodimers of ERBB2 and EGFR, bind to and phosphorylated PLCG1, leading to activation of PLCG1 signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-9665411",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665411"
}
]
},
{
"id": "R-HSA-9665412",
"name": "ERBB2 ECD mutants bind TKIs",
"equation": "",
"summary": "Comapred with the wild type ERBB2, ERBB2 G309E, ERBB2 S310F and ERBB2 S310Y are more sensitive to tyrosine kinase inhibitors lapatinib, neratinib and afatinib (Greulich et al. 2012). ERBB2 G309A was also responsive to lapatinib and neratinib (Bose et al. 2013).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665412",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665412"
}
]
},
{
"id": "R-HSA-9665413",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR recruit GRB2:SOS1 through SHC1",
"equation": "",
"summary": "RAS signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like phosphorylated heterodimers of the wild type ERBB2, can recruit the GRB2:SOS1 complex through phosphorylated SHC1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665413",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665413"
}
]
},
{
"id": "R-HSA-9665415",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, in complex with GRB2:GAB1, bind PI3K",
"equation": "",
"summary": "ERBB2 G309E and ERBB2 S310F activate PI3K/AKT signaling, demonstrated by activating phosphorylation of AKT1 (Greulich et al. 2012). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like the wild type heterodimers of ERBB2 and EGFR, can bind to the GRB2:GAB1 complex, leading to the recruitment of the PI3K complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665415",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665415"
}
]
},
{
"id": "R-HSA-9665416",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind SHC1",
"equation": "",
"summary": "RAS signaling is activated dowsntream of ERBB2 ECD mutants ERBB2 G309A (Bose et al. 2013), ERBB2 G309E (Greulich et al. 2012) and ERBB2 S310F (Greulich et al. 2012), as evidenced by activating phosphorylation of ERKs (MAPK1 and MAPK3). It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like phosphorylated heterodimers of the wild type ERBB2, bind to SHC1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665416",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665416"
}
]
},
{
"id": "R-HSA-9665417",
"name": "Phosphorylated heterodimers of ERBB2 ECD mutants and EGFR bind GRB2:GAB1",
"equation": "",
"summary": "ERBB2 G309E and ERBB2 S310F activate PI3K/AKT signaling, demonstrated by activating phosphorylation of AKT1 (Greulich et al. 2012). Activation of PI3K/AKT signaling downstream of ERBB2 G309A has not been tested. It is assumed that phosphorylated heterodimers of ERBB2 ECD mutants and EGFR, like the wild type heterodimers of ERBB2 and EGFR, can bind to the GRB2:GAB1 complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665417",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665417"
}
]
},
{
"id": "R-HSA-9665696",
"name": "ERBB2 TMD/JMD mutants bind trastuzumab",
"equation": "",
"summary": "The following ERBB2 TMD/JMD mutants are sensitive to the therapeutic antibody trastuzumab (herceptin):
ERBB2 V659E (Pahuja et al. 2018);
ERBB2 G660D (Pahuja et al. 2018);
ERBB2 G660R (Pahuja et al. 2018);
ERBB2 R678Q (Bose et al. 2013, Pahuja et al. 2018);
ERBB2 Q709L (Pahuja et al. 2018);",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665696",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665696"
}
]
},
{
"id": "R-HSA-9665697",
"name": "ERBB2 TMD/JMD mutants hetrodimerize",
"equation": "",
"summary": "TMD/JMD mutants that are activating in the presence of wild type ERBB2, such as ERBB2 R678Q, may form homodimers with the wild type ERBB2 (Pahuja et al. 2018).
Based on trans-autophosphorylation of ERBB2 and its dimerization partners EGFR and ERBB3, the following ERBB2 TMD/JMD mutants are assumed to form heterodimers with EGFR and ERBB3:
ERBB2 S653C (de Martino et al. 2014)
ERBB2 R678Q (Bose et al. 2013, Pahuja et al. 2018).
TMD/JMD mutants that are activating in the presence of wild type ERBB2, such as ERBB2 R678Q, may form homodimers with the wild type ERBB2 (Pahuja et al. 2018).
Signaling by ERBB2 V659E, ERBB2 V659K, ERBB2 G660D, ERBB2 G660R, ERBB2 R677L, ERBB2 E693K and ERBB2 Q709L has not been sufficiently studied and they are annotated as candidates.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665697",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665697"
}
]
},
{
"id": "R-HSA-9665698",
"name": "Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR bind GRB2:SOS1",
"equation": "",
"summary": "Activation of downstream RAS signaling was shown for ERBB2 S653C (de Martino et al. 2014) and ERBB2 R678Q (Bose et al. 2013, de Martino et al. 2014) through activating tyrosine phosphorylation on ERKs (MAPK1 and MAPK3). It is assumed that heterodimers of ERBB2 TMD/JMD mutants and EGFR, like the wild type ERBB2:EGFR heterodimers, directly bind to GRB:SOS1 complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665698",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665698"
}
]
},
{
"id": "R-HSA-9665699",
"name": "Phosphorylated heterodimers of ERBB2 TMD/JMD mutants recruit GRB2:SOS1 through SHC1",
"equation": "",
"summary": "Activation of downstream RAS signaling was shown for ERBB2 S653C (de Martino et al. 2014) and ERBB2 R678Q (Bose et al. 2013, de Martino et al. 2014) through activating tyrosine phosphorylation on ERKs (MAPK1 and MAPK3) and SHC1. It is assumed that heterodimers of ERBB2 TMD/JMD mutants, like the wild type ERBB2 heterodimers, bind to and phosphorylate SHC1, leading to the recruitment of the GRB2:SOS1 complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665699",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665699"
}
]
},
{
"id": "R-HSA-9665700",
"name": "RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants",
"equation": "",
"summary": "Activation of downstream RAS signaling was shown for ERBB2 S653C (de Martino et al. 2014) and ERBB2 R678Q (Bose et al. 2013, de Martino et al. 2014) through activating tyrosine phosphorylation on ERKs (MAPK1 and MAPK3) and SHC1. It is assumed that heterodimers of ERBB2 TMD/JMD mutants, like the wild type ERBB2 heterodimers, bind to and phosphorylate SHC1, leading to the recruitment of the GRB2:SOS1 complex and activation of RAS through guanyl nucleotide exchange.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9665700",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665700"
}
]
},
{
"id": "R-HSA-9665701",
"name": "Phosphorylated ERBB2 TMD/JMD heterodimers bind SHC1",
"equation": "",
"summary": "Activation of downstream RAS signaling was shown for ERBB2 S653C (de Martino et al. 2014) and ERBB2 R678Q (Bose et al. 2013, de Martino et al. 2014) through activating tyrosine phosphorylation on ERKs (MAPK1 and MAPK3) and SHC1. It is assumed that heterodimers of ERBB2 TMD/JMD mutants, like the wild type ERBB2 heterodimers, bind SHC1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665701",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665701"
}
]
},
{
"id": "R-HSA-9665702",
"name": "ERBB2 TMD/JMD mutants bind TKIs",
"equation": "",
"summary": "The following ERBB2 TMD/JMD mutants are sensitive to lapatinib:
ERBB2 S653C (de Martino et al. 2014);
ERBB2 R678Q (Bose et al. 2013);
The following ERBB2 TMD/JMD mutants are sensitive to neratinib:
ERBB2 V659E (Pahuja et al. 2018);
ERBB2 G660D (Pahuja et al. 2018);
ERBB2 G660R (Pahuja et al. 2018);
ERBB2 R678Q (Bose et al. 2013, Pahuja et al. 2018);
ERBB2 Q709L (Pahuja et al. 2018);
The following ERBB2 TMD/JMD mutants are sensitive to afatinib:
ERBB2 G660D (Pahuja et al. 2018);
ERBB2 G660R (Pahuja et al. 2018);
ERBB2 S653C (de Martino et al. 2014);
ERBB2 R678Q (Pahuja et al. 2018);
ERBB2 Q709L (Pahuja et al. 2018).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665702",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665702"
}
]
},
{
"id": "R-HSA-9665703",
"name": "ERBB2 TMD/JMD mutants bind pertuzumab",
"equation": "",
"summary": "ERBB2 R678Q is sensitive to pertuzumab (Pahuja et al. 2018).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665703",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665703"
}
]
},
{
"id": "R-HSA-9665704",
"name": "Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR phosphorylate PLCG1",
"equation": "",
"summary": "Activation of downstream PLCG1 signaling was demonstrated for ERBB2 R678Q, through activating tyrosine phosphorylation on PLCG1 (Bose et al. 2013). It is assumed that the heterodimer of ERBB2 R678Q and EGFR, like the wild type ERBB2:EGFR heterodimer, binds to and phosphorylates PLCG1, leading to activation of PLCgamma1 signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-9665704",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665704"
}
]
},
{
"id": "R-HSA-9665705",
"name": "Phosphorylated heterodimers of ERBB2 TMD/JMD mutants phosphorylate SHC1",
"equation": "",
"summary": "Activation of downstream RAS signaling was shown for ERBB2 S653C (de Martino et al. 2014) and ERBB2 R678Q (Bose et al. 2013, de Martino et al. 2014) through activating tyrosine phosphorylation on ERKs (MAPK1 and MAPK3) and SHC1. It is assumed that heterodimers of ERBB2 TMD/JMD mutants, like the wild type ERBB2 heterodimers, bind to and phosphorylate SHC1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665705",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665705"
}
]
},
{
"id": "R-HSA-9665706",
"name": "Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR bind PLCG1",
"equation": "",
"summary": "Activation of downstream PLCG1 signaling was demonstrated for ERBB2 R678Q, through activating tyrosine phosphorylation on PLCG1 (Bose et al. 2013). It is assumed that the heterodimer of ERBB2 R678Q and EGFR, like the wild type ERBB2:EGFR heterodimer, binds PLCG1.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P19174-1"
],
"evidence": [
{
"id": "R-HSA-9665706",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665706"
}
]
},
{
"id": "R-HSA-9665707",
"name": "RAS activation by SOS1 bound to phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR",
"equation": "",
"summary": "Activation of downstream RAS signaling was shown for ERBB2 S653C (de Martino et al. 2014) and ERBB2 R678Q (Bose et al. 2013, de Martino et al. 2014) through activating tyrosine phosphorylation on ERKs (MAPK1 and MAPK3). It is assumed that heterodimers of ERBB2 TMD/JMD mutants and EGFR, like the wild type ERBB2:EGFR heterodimers, directly bind to GRB:SOS1 complex, resulting in activation of RAS signaling to guanyl nucleotide exchange on RAS.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P04626-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9665707",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665707"
}
]
},
{
"id": "R-HSA-9665708",
"name": "ERBB2 TMD/JMD mutants do not bind pertuzumab",
"equation": "",
"summary": "ERBB2 V659E, ERBB2 G660D, ERBB2 G660R and probably ERBB2 Q709L are resistant to therapeutic antibody pertuzumab (Pahuja et al. 2018).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665708",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665708"
}
]
},
{
"id": "R-HSA-9665709",
"name": "ERBB2 TMD/JMD heterodimers trans-autophosphorylate",
"equation": "",
"summary": "Phosphorylation of tyrosine residues in the C-tail of ERBB2 was shown for the following ERBB2 TMD/JMD mutants:
ERBB2 V659E (Pahuja et al. 2018);
ERBB2 V659K (Pahuja et al. 2018);
ERBB2 G660D (Pahuja et al. 2018);
ERBB2 G660R (Pahuja et al. 2018);
ERBB2 S653C (de Martino et al. 2014 - phosphorylation at Y1248 demonstrated);
ERBB2 R677L (Pahuja et al. 2018);
ERBB2 R678Q (Bose et al. 2013; de Martino et al. 2014 - phosphorylation at Y1248 demonstrated; Pahuja et al. 2018); ERBB2 Q709L (Pahuja et al. 2018)
Phosphorylation of tyrosine residues in the C-tail of EGFR was demonstrated for ERBB2 S653C (de Martino et al. 2014 - phosphorylation at Y1068) and ERBB2 R678Q (Bose et al. 2013; de Martino et al. 2014 - phosphorylation at Y1068).
Phosphorylation of tyrosine residues in the C-tail of ERBB3 was demonstrated for ERBB2 S653C (de Martino et al. 2014 - phosphorylation at Y1197) and ERBB2 R678Q (Bose et al. 2013; de Martino et al. 2014 - phosphorylation at Y1197).
Signaling by ERBB2 V659K, ERBB2 G660D, ERBB2 G660R, ERBB2 R677L, ERBB2 E693K and ERBB2 Q709L has not been sufficiently studied and they are annotated as candidates.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-HSA-9665709",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665709"
}
]
},
{
"id": "R-HSA-9665726",
"name": "ERBB2 binds pertuzumab",
"equation": "",
"summary": "Pertuzumab is an ERBB2-directed therapeutic antibody that binds to ERBB2 and sterically blocks receptor dimerization and signaling (Franklin et al. 2004).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9665726",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9665726"
}
]
},
{
"id": "R-NUL-1248744",
"name": "Shc1 binds phosphorylated ERBB2:EGFR heterodimers",
"equation": "",
"summary": "Shc1 binds phosphorylated ERBB2:EGFR heterodimers in engineered mouse 32D cells (Pinkas-Kramarski et al. 1996).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-NUL-1248744",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-NUL-1248744"
}
]
},
{
"id": "R-NUL-1248753",
"name": "Shc1 binds phosphorylated ERBB2:ERBB3 heterodimers",
"equation": "",
"summary": "Shc1 binds phosphorylated ERBB2:ERBB3 heterodimer in engineered mouse 32D cells (Pinkas-Kramarski et al. 1996).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P04626-1"
],
"evidence": [
{
"id": "R-NUL-1248753",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-NUL-1248753"
}
]
},
{
"id": "R-NUL-1251923",
"name": "Plcg1 binds P-ERBB2:P-EGFR",
"equation": "",
"summary": "Mouse phospholipase C gamma 1 is phosphorylated by human recombinant ERBB2 exogenously expressed in mouse fibroblasts.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-NUL-1251923",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-NUL-1251923"
}
]
},
{
"id": "R-NUL-1251929",
"name": "Plcg1 phosphorylation by P-ERBB2:P-EGFR",
"equation": "",
"summary": "Mouse phospholipase C gamma 1 is phosphorylated by human recombinant ERBB2 exogenously expressed in mouse fibroblasts.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1"
],
"evidence": [
{
"id": "R-NUL-1251929",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-NUL-1251929"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-HSA-167679",
"participant_name": "p-4Y-PLCG1 [plasma membrane]",
"crossref": [
{
"id": "P19174",
"database": "PRO",
"url": ""
},
{
"id": "PLCG1_HUMAN",
"database": "ZINC - Predictions - Purchasable",
"url": ""
},
{
"id": "NP_002651.2",
"database": "RefSeq",
"url": ""
},
{
"id": "2HSP",
"database": "PDB",
"url": ""
},
{
"id": "ENSP00000508698",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000124181",
"database": "OpenTargets",
"url": ""
},
{
"id": "1HSQ",
"database": "PDB",
"url": ""
},
{
"id": "PLCG1_HUMAN",
"database": "ZINC - Substances",
"url": ""
},
{
"id": "ENST00000373271",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000124181-PLCG1",
"database": "HPA",
"url": ""
},
{
"id": "ENST00000244007",
"database": "Ensembl",
"url": ""
},
{
"id": "P19174",
"database": "ZINC target",
"url": ""
},
{
"id": "P19174",
"database": "UniProt",
"url": ""
},
{
"id": "4FBN",
"database": "PDB",
"url": ""
},
{
"id": "ENSG00000124181",
"database": "Ensembl",
"url": ""
},
{
"id": "P19174",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "ENSP00000362368",
"database": "Ensembl",
"url": ""
},
{
"id": "4EY0",
"database": "PDB",
"url": ""
},
{
"id": "7NXE",
"database": "PDB",
"url": ""
},
{
"id": "P19174",
"database": "GeneCards",
"url": ""
},
{
"id": "1407",
"database": "Guide to Pharmacology - Targets",
"url": ""
},
{
"id": "ENSP00000244007",
"database": "Ensembl",
"url": ""
},
{
"id": "NP_877963.1",
"database": "RefSeq",
"url": ""
},
{
"id": "HMDBP00244",
"database": "HMDB Protein",
"url": ""
},
{
"id": "ENST00000685551",
"database": "Ensembl",
"url": ""
}
]
},
{
"participant_id": "R-HSA-372889",
"participant_name": "ERBB2 [plasma membrane]",
"crossref": [
{
"id": "NP_001276865.1",
"database": "RefSeq",
"url": ""
},
{
"id": "3BE1",
"database": "PDB",
"url": ""
},
{
"id": "1S78",
"database": "PDB",
"url": ""
},
{
"id": "3PP0",
"database": "PDB",
"url": ""
},
{
"id": "4GFU",
"database": "PDB",
"url": ""
},
{
"id": "1MFG",
"database": "PDB",
"url": ""
},
{
"id": "6BGT",
"database": "PDB",
"url": ""
},
{
"id": "NP_001276867.1",
"database": "RefSeq",
"url": ""
},
{
"id": "NP_004439.2",
"database": "RefSeq",
"url": ""
},
{
"id": "8HGO",
"database": "PDB",
"url": ""
},
{
"id": "5OB4",
"database": "PDB",
"url": ""
},
{
"id": "7MN8",
"database": "PDB",
"url": ""
},
{
"id": "6J71",
"database": "PDB",
"url": ""
},
{
"id": "3RCD",
"database": "PDB",
"url": ""
},
{
"id": "3H3B",
"database": "PDB",
"url": ""
},
{
"id": "4HRM",
"database": "PDB",
"url": ""
},
{
"id": "8HGP",
"database": "PDB",
"url": ""
},
{
"id": "ERBB2_HUMAN",
"database": "ZINC - Metabolites",
"url": ""
},
{
"id": "ENST00000406381",
"database": "Ensembl",
"url": ""
},
{
"id": "ERBB2_HUMAN",
"database": "ZINC - Investigational",
"url": ""
},
{
"id": "ERBB2_HUMAN",
"database": "ZINC - FDA approved",
"url": ""
},
{
"id": "5O4G",
"database": "PDB",
"url": ""
},
{
"id": "5K33",
"database": "PDB",
"url": ""
},
{
"id": "5KWG",
"database": "PDB",
"url": ""
},
{
"id": "ENSP00000269571",
"database": "Ensembl",
"url": ""
},
{
"id": "ERBB2_HUMAN",
"database": "ZINC - World Drugs",
"url": ""
},
{
"id": "ENST00000269571",
"database": "Ensembl",
"url": ""
},
{
"id": "2KS1",
"database": "PDB",
"url": ""
},
{
"id": "2A91",
"database": "PDB",
"url": ""
},
{
"id": "2N2A",
"database": "PDB",
"url": ""
},
{
"id": "7MN5",
"database": "PDB",
"url": ""
},
{
"id": "6LBX",
"database": "PDB",
"url": ""
},
{
"id": "4HRL",
"database": "PDB",
"url": ""
},
{
"id": "3WLW",
"database": "PDB",
"url": ""
},
{
"id": "P04626",
"database": "PRO",
"url": ""
},
{
"id": "NP_001005862.1",
"database": "RefSeq",
"url": ""
},
{
"id": "7JXH",
"database": "PDB",
"url": ""
},
{
"id": "3WSQ",
"database": "PDB",
"url": ""
},
{
"id": "1MW4",
"database": "PDB",
"url": ""
},
{
"id": "3MZW",
"database": "PDB",
"url": ""
},
{
"id": "ENSG00000141736",
"database": "OpenTargets",
"url": ""
},
{
"id": "ERBB2_HUMAN",
"database": "ZINC - Biogenic",
"url": ""
},
{
"id": "2019",
"database": "Guide to Pharmacology - Targets",
"url": ""
},
{
"id": "ENSG00000141736-ERBB2",
"database": "HPA",
"url": ""
},
{
"id": "ENST00000584601",
"database": "Ensembl",
"url": ""
},
{
"id": "5MY6",
"database": "PDB",
"url": ""
},
{
"id": "4NND",
"database": "PDB",
"url": ""
},
{
"id": "5TQS",
"database": "PDB",
"url": ""
},
{
"id": "7MN6",
"database": "PDB",
"url": ""
},
{
"id": "3N85",
"database": "PDB",
"url": ""
},
{
"id": "6OGE",
"database": "PDB",
"url": ""
},
{
"id": "ENST00000541774",
"database": "Ensembl",
"url": ""
},
{
"id": "6ATT",
"database": "PDB",
"url": ""
},
{
"id": "1QR1",
"database": "PDB",
"url": ""
},
{
"id": "P04626",
"database": "UniProt",
"url": ""
},
{
"id": "8FFJ",
"database": "PDB",
"url": ""
},
{
"id": "ERBB2_HUMAN",
"database": "ZINC - Predictions - Purchasable",
"url": ""
},
{
"id": "4HRN",
"database": "PDB",
"url": ""
},
{
"id": "ENSP00000385185",
"database": "Ensembl",
"url": ""
},
{
"id": "1N8Z",
"database": "PDB",
"url": ""
},
{
"id": "ERBB2_HUMAN",
"database": "ZINC - Substances",
"url": ""
},
{
"id": "7PCD",
"database": "PDB",
"url": ""
},
{
"id": "2L4K",
"database": "PDB",
"url": ""
},
{
"id": "P04626",
"database": "GeneCards",
"url": ""
},
{
"id": "ENSP00000446466",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSG00000141736",
"database": "Ensembl",
"url": ""
},
{
"id": "ENSP00000462438",
"database": "Ensembl",
"url": ""
},
{
"id": "7QVK",
"database": "PDB",
"url": ""
},
{
"id": "P04626",
"database": "ZINC target",
"url": ""
},
{
"id": "2JWA",
"database": "PDB",
"url": ""
},
{
"id": "HMDBP01473",
"database": "HMDB Protein",
"url": ""
},
{
"id": "P04626",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "1MFL",
"database": "PDB",
"url": ""
}
]
},
{
"participant_id": "R-HSA-8848007",
"participant_name": "p-Y342-PTK6 [cytosol]",
"crossref": [
{
"id": "NP_005966.1",
"database": "RefSeq",
"url": ""
},
{
"id": "HMDBP01216",
"database": "HMDB Protein",
"url": ""
},
{
"id": "PTK6_HUMAN",
"database": "ZINC - Substances",
"url": ""
},
{
"id": "6CZ4",
"database": "PDB",
"url": ""
},
{
"id": "PTK6_HUMAN",
"database": "ZINC - FDA approved",
"url": ""
},
{
"id": "ENSG00000101213",
"database": "Ensembl",
"url": ""
},
{
"id": "2182",
"database": "Guide to Pharmacology - Targets",
"url": ""
},
{
"id": "ENST00000217185",
"database": "Ensembl",
"url": ""
},
{
"id": "5D7V",
"database": "PDB",
"url": ""
},
{
"id": "6CZ3",
"database": "PDB",
"url": ""
},
{
"id": "ENSG00000101213-PTK6",
"database": "HPA",
"url": ""
},
{
"id": "PTK6_HUMAN",
"database": "ZINC - World Drugs",
"url": ""
},
{
"id": "Q13882",
"database": "GeneCards",
"url": ""
},
{
"id": "ENSP00000442460",
"database": "Ensembl",
"url": ""
},
{
"id": "Q13882",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "Q13882",
"database": "UniProt",
"url": ""
},
{
"id": "Q13882",
"database": "PRO",
"url": ""
},
{
"id": "1RJA",
"database": "PDB",
"url": ""
},
{
"id": "ENSP00000217185",
"database": "Ensembl",
"url": ""
},
{
"id": "2KGT",
"database": "PDB",
"url": ""
},
{
"id": "5H2U",
"database": "PDB",
"url": ""
},
{
"id": "5DA3",
"database": "PDB",
"url": ""
},
{
"id": "PTK6_HUMAN",
"database": "ZINC - Predictions - Purchasable",
"url": ""
},
{
"id": "ENST00000542869",
"database": "Ensembl",
"url": ""
},
{
"id": "6CZ2",
"database": "PDB",
"url": ""
},
{
"id": "NP_001243287.1",
"database": "RefSeq",
"url": ""
},
{
"id": "Q13882",
"database": "ZINC target",
"url": ""
},
{
"id": "PTK6_HUMAN",
"database": "ZINC - Biogenic",
"url": ""
},
{
"id": "PTK6_HUMAN",
"database": "ZINC - Investigational",
"url": ""
},
{
"id": "ENSG00000101213",
"database": "OpenTargets",
"url": ""
}
]
},
{
"participant_id": "R-HSA-8864449",
"participant_name": "ERBB2 Gene [nucleoplasm]",
"crossref": [
{
"id": "ENSG00000141736",
"database": "ENSEMBL",
"url": ""
}
]
}
],
"reaction_enzymes": [
{
"uniprot_ac": "A0A0G2JW59",
"gene_name": "Flt3",
"activity": [
{
"ec_number": "2.7.10.1",
"activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].",
"evidence": [
{
"id": "A0A0G2JW59",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/A0A0G2JW59"
}
]
},
{
"ec_number": "2.7.10.1",
"activity": "",
"evidence": [
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"title",
"journal",
"date",
"authors"
]
}
]
}