In the nucleus acetylation of Histone H3 is linked to the function of the Elongator complex in transcription (Kim JH et al. 2002). Elongator complex protein 3 (ELP3), a catalytic acetyltransferase subunit of the Elongator complex, has been reported to regulate the transcription of HSP70 gene, and the histone acetyltransferase (HAT) domain of ELP3 is essential for this function (Han Q et al. 2007; Li F et al. 2001). ;", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P11142-1", "P07900-1" ], "evidence": [ { "id": "R-HSA-5082356", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5082356" } ] }, { "id": "R-HSA-5082409", "name": "Dissociation of HSF1:HSP90 complex in the nucleus", "equation": "", "summary": "The inactive HSF1 was reported to constitutively shuttle between the nucleus and the cytoplasm in mammalian cells (Vujanac M et al. 2005). There is no consensus on whether inactive HSF1 monomers localize in the nucleus or in the cytosol (Sarge KD et al. 1993; Zuo J et al. 1995; Mercier PA et al. 1999; Vujanac M et al. 2005). This event shows stress-induced activation of HSF1 in the nucleus.
In the absence of stress HSF1 is predominantly monomeric and is thought to be repressed in its inactive monomeric state by the following mechanisms:
In the absence of stress HSF1 is predominantly monomeric and is thought to be repressed in its inactive monomeric state by the following mechanisms:
FKBP52 (FKBP4) is a member of the immunophilin (IMM) protein family of intracellular proteins that are able to bind immunosuppressant drugs, from which the term immunophilin derives (Pratt and Toft 1997; Kang et al. 2008). These proteins are also known as peptidyl-prolyl cis/trans isomerases (PPIases) for their ability to convert proline bonds from cis to trans form, a rate-limiting step in protein folding (Harding et al. 1989; Standaert et al. 1990; Galat 2003; Davies and Sanchez 2005). In addition to the PPIase and TPR domains, there are two additional domains - the nucleotide-binding domain (also called FKBD2 in FKBP proteins) where ATP binds and the calmodulin-binding domain, a poorly characterized domain able to interact with calmodulin.", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P11142-1", "P07900-1", "Q02790-1" ], "evidence": [ { "id": "R-HSA-5618085", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5618085" } ] }, { "id": "R-HSA-5618093", "name": "ATP hydrolysis by HSP90", "equation": "", "summary": "The chaperoning function of HSP90 is coupled to its ATPase activity. Our current understanding of the ATPase mechanism of Hsp90 is based largely on structural and functional studied for the Saccharomyces cerevisiae Hsp90 complexes (Meyer P et al. 2003, 2004; Ali MM et al. 2006; Prodromou C et al. 2000; Prodromou C 2012). The ATPase cycle of human HSP90 is less well understood, however several studies suggest that the underlying enzymatic mechanisms and a set of conformational changes that accompany the ATPase cycle are highly similar in both species (Richter K et al. 2008; Vaughan CK et al. 2009). Once ATP is bound it helps to stabilize the closed ATP lid state, in which the gamma-phosphate of ATP provides a hydrogen bonding that promotes a stable association of the ATP lid with N-terminal domain (NTD) (Ali MM et al. 2006; Prodromou C et al. 2000; Chadli A et al. 2000). The association of ATP with NTD then stimulates structural changes in NTD and in the middle domain that are likely to involve movements of the ATP lid segment within each N-terminal domain that locates over the bound ATP. The movement of the lids exposes surface residues that are subsequently involved in transient dimerization of the N-terminal domains of HSP90 (Ali MM et al. 2006; Prodromou C et al. 2000; Chadli A et al. 2000). Furthermore, the intrachain associations of NTD with the middle domain leads to the active conformation of the catalytic loop of HSP90, which commits the ATP for hydrolysis (Meyer P et al. 2003). The subsequent conformational changes upon ATP binding are regulated by co-chaperone activities. For example, arrangement of the STIP1 domains in the complex seems to prevent the NTDs dimerization of HSP90 monomers and total closure of the HSP90 dimer that is required for an efficient HSP90-mediated ATP hydrolysis (Southworth DR & Agard DA 2011; Alvira S et al. 2014). In addition, client protein binding to HSP90 was found to increase ATPase activity of HSP90 up to 200-fold (McLaughlin SH et al. 2002).
After hydrolysis of ATP the ligand-bound steroid hormone receptor (SHR) is released from HSP90 complex. The Reactome module describes ATPase activity of HSP90 in the nucleus, however it is not entirely clear whether cytosolic hormone-bound SHR translocates through the nuclear pores before or after ATP-dependent dissociation from the HSP90 complex.", "cellular_location": "nucleoplasm", "input_participant_list": [], "output_participant_list": [ "R-HSA-5324621" ], "enzyme_list": [ "P07900-1", "Q02790-1", "Q15185-1" ], "evidence": [ { "id": "R-HSA-5618093", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5618093" } ] }, { "id": "R-HSA-5618098", "name": "p23 (PTGES3) binds HSP90:ATP:FKBP5:nascent protein", "equation": "", "summary": "Immunophilin p23 (also known as PTGES3) binds selectively to the ATP-bound state of HSP90. p23 stabilizes the closed state of HSP90, which weakens the binding of STIP1(HOP) and promotes its exit from the complex (McLaughlin H et al. 2006; Karag\u00f6z GE et al. 2011). When FKBP51 (FKBP5) is present, a stable intermediate FKBP51:GR:HSP90:p23 is formed by expulsion of HSP70 and STIP1(HOP) (Ebong I et al. 2016).", "cellular_location": "cytosol", "input_participant_list": [ "R-HSA-265269" ], "output_participant_list": [ "R-HSA-443857" ], "enzyme_list": [ "P11142-1", "P07900-1", "Q15185-1", "Q13451-1" ], "evidence": [ { "id": "R-HSA-5618098", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5618098" } ] }, { "id": "R-HSA-5618099", "name": "NR3C2 ligands bind NR3C2 (in the HSP90 chaperone complex)", "equation": "", "summary": "Steroid hormones receptors (SHRs) are intracellular transcription factors that can be activated by binding specific ligands (i.e., steroid hormones (SH)) to the ligand-binding domain (LBD) (Ray DW et AL. 1999; Pike AC et al. 1999; Bledsoe RK et al. 2002; Li Y et al. 2005; Kumar R and McEwan IJ 2012; Kumar R et al. 2011; Williams SP & Sigler PB 1998; Tanenbaum DM et al. 1998; Lusher SJ et al. 2012). LBD (E-region) resides in the C-terminal half of the receptor and in addition to ligand binding function contains a transcriptional activation function (AF2), sequences for dimerization, heat shock protein association, intermolecular silencing and intramolecular repression (Kumar R and McEwan IJ 2012). The binding of hormone acts as an allosteric switch to regulate SHR-DNA and SHR-protein interactions, including interdomain interactions and/or dimerization (Kumar R and McEwan IJ 2012).
SHs are synthesized from cholesterol in the adrenal cortex (glucocorticoids, mineralocorticoids, and adrenal androgens), the testes (testicular androgens, estrogen), and the ovary and placenta (estrogen and progestogen or progestins) (Payne AH & Hales DB 2004; Hu J et al. 2010;). SHs reach their target cells via the blood, where they are bound to specific carrier proteins (Grishkovskaya I et al. 2000; Hammond GL 2016). SHs detach from the carrier proteins and because of their lipophilic nature readily diffuse through the plasma membrane of cells (Oren I et al. 2004). Within the target cells SHs bind to steroid hormone receptors (SHRs) which are present in a heterocomplex with heat shock protein HSP90 and co-chaperones (e.g., immunophilins p23) (Echeverria PC & Picard D 2010). The ATP-bound form of HSP90 and chaperone-mediated conformational changes are required to keep SHRs in a ligand binding-competent state (McLaughlin SH et al. 2002; Pratt WB et al. 2008; Krukenberg KA et al. 2011).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q02790-1",
"Q15185-1"
],
"evidence": [
{
"id": "R-HSA-5618099",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5618099"
}
]
},
{
"id": "R-HSA-5618105",
"name": "FKBP5 binds HSP90:ATP:STIP1:HSP70:nascent protein",
"equation": "",
"summary": "FK506 binding protein 5 (FKBP51, also known as FKBP5) is a member of the immunophilin (IMM) protein family of intracellular proteins. The signature domain of the IMM family is the peptidyl-prolyl-cis/trans-isomerase (PPIase) domain, which is in turn the drug binding domain. IMMs are classified by their ability to bind immunosuppressant drugs \u2013 CyPs (cyclophilins) bind cyclosporine A (CsA), and FKBPs (FK506-binding pro-teins) bind FK506 (Pratt and Toft 1997; Kang et al. 2008). In addition to the PPIase domain, there are three additional domains \u2013 the nucleotide-binding domain, (also called FKBD2 in FKBP proteins) where ATP binds, the calmodulin-binding domain, a poorly characterized domain able to interact with calmodulin, and tetratricopeptide repeat (TPR) domains, sequences of 34 amino acids repeated in tandem through which FKBPs bind to the HSP90 C-terminal sequence MEEVD (Davies et al. 2005; Wu et al. 2004). Mass spectrometry analysis showed that FKBP51 (FKBP5) and FKBP52 (FKBP4) form analogous complexes with GR:HSP90:STIP1:HSP70:ATP (Ebong IO et al. 2016). Binding of FKBP51 (FKBP5) and other immunophilins may weaken the association of TPR domain containing protein STIP1 with HSP90 complex (Li et al. 2011).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"P07900-1",
"Q13451-1"
],
"evidence": [
{
"id": "R-HSA-5618105",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5618105"
}
]
},
{
"id": "R-HSA-5618107",
"name": "ATP binding to HSP90 triggers conformation change",
"equation": "",
"summary": "The molecular chaperone heat-shock protein 90 (HSP90) functions as a homodimer. Each HSP90 protomer contains three flexibly linked regions, the N-terminal ATP-binding domain (NTD), the middle domain, and the C-terminal dimerization domain (Prodromou C et al. 1997; Pearl LH and Prodromou C 2006). HSP90 dimer is rather a dynamic molecule and ATP binding and hydrolysis are associated with conformational changes (Obermann WM et al. 1998; Krukenberg KA et al. 2011; Li J & Buchner J 2013; Prodromou C 2012). The structures of the isolated yeast and human N-terminal domain (NTD) of HSP90 bound to ATP, ADP and adenylylimidodiphosphate (AMP-PNP, a non-hydrolysable analogue of ATP) suggest that nucleotides bind deep in the cleft of NTD in open apo state of HSP90 (Prodromou C et al.1997; Meyer P et al. 2003, 2004; Colombo G et al. 2008; Li J et al. 2012). The structural studies of NTD of human HSP90 with antitumor agent geldanamycin (that acts as an ADP/ATP mimetic) support the polar interactions in the binding pocket described for yeast Hsp90 and ADP or ATP (Stebbins CE et al. 1997; Prodromou C et al.1997; Grenert JP et al. 1997). Once ATP is bound it helps to stabilize the closed ATP lid state, in which the gamma-phosphate of ATP provides a hydrogen bonding that promotes a stable association of the ATP lid with NTD. The association of ATP or AMP-PNP with NTD then stimulates structural changes in NTD. NMR analysis of human full-length HSP90 protein with and without ATP confirmed that ATP binding led to conformational changes in NTD (Karag\u00f6z GE et al. 2010). No structural changes were observed in the middle and C-terminal domains (Karag\u00f6z GE et al. 2010). However, other studies suggest that ATP-dependent conformational changes occur both in NTD and in the middle domain of HSP90 (Ali MM et al. 2006; Prodromou C et al. 2000; Chadli A et al. 2000; Meyer P et al. 2003). The changes are likely to involve movements of the ATP lid segment within each N-terminal domain that locates over the bound ATP (Ali MM et al. 2006; Prodromou C et al. 2000; Chadli A et al. 2000). The movement of the lids exposes surface residues that are subsequently involved in transient dimerization of the N-terminal domains of HSP90 (Ali MM et al. 2006; Prodromou C et al. 2000; Chadli A et al. 2000). The subsequent conformational changes upon ATP binding are regulated by co-chaperone activities. For example, arrangement of the STIP1 domains in the complex seems to prevent the NTDs dimerization of HSP90 monomers and total closure of the HSP90 dimer that is required for an efficient HSP90-mediated ATP hydrolysis (Southworth DR & Agard DA 2011; Alvira S et al. 2014). Thus, ATP binding coupled to co-chaperone-mediated loading of client protein to HSP90 complex regulates ATPase activity of HSP90.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5618107",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5618107"
}
]
},
{
"id": "R-HSA-5618110",
"name": "p23 (PTGES3) binds HSP90:ATP:FKBP4:nascent protein",
"equation": "",
"summary": "Immunophilin p23 (also known as PTGES3) binds selectively to the ATP-bound state of HSP90. p23 stabilizes the closed state of HSP90, which weakens the binding of STIP1(HOP) and promotes its exit from the complex (McLaughlin H et al. 2006; Karag\u00f6z GE et al. 2011). When p23 is added to the client-transfer complex in the absence of the immunophilin or with FKBP51 (FKBP5), two copies of p23 are incorporated with concomitant loss of HSP70 and HOP (Ebong I et al. 2016). By contrast no stable complex with two p23 subunits is observed in the presence of FKBP52 (FKBP4); expulsion of HSP70, HOP and p23 occur with a low population of a complex incorporating only one p23 subunit (Ebong I et al. 2016).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"P07900-1",
"Q02790-1",
"Q15185-1"
],
"evidence": [
{
"id": "R-HSA-5618110",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5618110"
}
]
},
{
"id": "R-HSA-5626220",
"name": "C2CD3 binds the mother centriole",
"equation": "",
"summary": "C2 domain-containing protein 3 (C2CD3) is basal body-localized protein that is required for ciliogenesis and Hh signaling (Hoover et al, 2008; Balestra et al, 2013). C2CD3 is recruited to the centrosome in a pericentriolar material 1 protein (PCM1)- and microtubule-dependent manner and is required for the subsequent recruitment of the distal appendage proteins to the mother centriole (Tanos et al, 2013; Sillibourne et al, 2013; Ye et al, 2014; reviewed in Winey and O'Toole, 2014). The distal appendage proteins are thought to be a component of the transition fibres that anchor the basal body to the membrane at the base of the cilium and are themselves required for the recruitment of Tau-tubulin kinase 2 (TTBK2) and for docking ciliary vesicles to the mother centriole (Tanos et al, 2013; Wei et al, 2013; Joo et al, 2013; Schmidt et al, 2012; Sillibourne et al, 2013; Burke et al, 2014).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P48730-1",
"O00444-1",
"P17612-1",
"P49674-1",
"P07900-1",
"P51955-1",
"P06493-1",
"P53350-1",
"P68366-1",
"Q71U36-1"
],
"evidence": [
{
"id": "R-HSA-5626220",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5626220"
}
]
},
{
"id": "R-HSA-5626223",
"name": "C2CD3 and OFD1 recruit 5 distal appendage proteins to the centriole",
"equation": "",
"summary": "C2CD3 and the centrosome component OFD1 are required for the recruitment of distal appendage proteins CEP164, CEP83/CCDC41, CEP89, FBF1 and SCLT1 to the mother centriole (Ye et al, 2014; Tang et al, 2013; Singla et al, 2010). Distal appendage proteins are believed to form part of the transition fibres that anchor the basal bodies to the actin rich cortex at the base of the emerging cilium, and are also required for the recruitment and binding of ciliary vesicles and intraflagellar transport (IFT) complexes (Tanos et al, 2013; Wei et al, 2013; Joo et al, 2010; Schmidt et al, 2012; Sillibourne et al, 2013; Ye et al, 2014; reviewed in Winey and O'Toole, 2014).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P48730-1",
"O00444-1",
"P17612-1",
"P49674-1",
"P07900-1",
"P51955-1",
"P06493-1",
"P53350-1",
"P68366-1",
"Q71U36-1"
],
"evidence": [
{
"id": "R-HSA-5626223",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5626223"
}
]
},
{
"id": "R-HSA-5626227",
"name": "CP110 and CEP97 dissociate from the centriole",
"equation": "",
"summary": "CCP110 is a negative regulator of ciliogenesis that caps the mother centriole. CCP110 may inhibit ciliogenesis in part by preventing the CEP290-dependent recruitment of RAB8A to the centrosome and cilia (Spektor et al, 2007; Tsang et al, 2008; reviewed in Tsang and Dynlacht, 2013). CCP110 and CEP97 also form a complex with the KIF24, a kinesin with centriolar microtubule depolymerizing activity that is required for the initial recruitment and/or stability of CCP110 at the centriole (Kobayashi et al, 2011). Recruitment of TTBK2 promotes the displacement of CCP110 and its binding partner CEP97. This results in the formation of a basal body and promotes recruitment of IFT complex members and allows axonemal extension to occur (Goetz et al, 2012; Ye et al, 2014; reviewed in Tsang and Dynlacht, 2013). Although the kinase activity of TTBK2 is required for cilium formation and TTBK2 has been shown to phosphorylate CEP164, the relevant physiological target during ciliogenesis has not been unambiguously identified (Cajanek et al, 2014). Similarly, the kinase activity of MARK4 is also required for ciliogenesis, and the interaction between MARK4 and ODF2, a putative substrate, is needed to promote the dissociation of the CCP110 and CEP97 proteins from the centriole (Kuhns et al, 2013; reviewed in Kim and Dynlacht, 2013).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q6IQ55-1",
"P48730-1",
"Q96L34-1",
"O00444-1",
"P17612-1",
"P49674-1",
"P07900-1",
"P51955-1",
"P06493-1",
"P53350-1",
"P68366-1",
"Q71U36-1"
],
"evidence": [
{
"id": "R-HSA-5626227",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5626227"
}
]
},
{
"id": "R-HSA-5626228",
"name": "The distal appendage proteins recruit TTBK2",
"equation": "",
"summary": "C2CD3 and the distal appendage protein CEP164 are required for the recruitment of the kinase Tau tubulin kinase 2 (TTBK2) to the centriole (Ye et al, 2014; Cajanek et al, 2014). TTBK2 recruitment promotes the release of CCP110, a negative regulator of ciliogenesis that caps the mother centriole (Goetz et al, 2012; Ye et al, 2014; Tsang et al, 2008; Spektor et al, 2007). CCP110 is initially recruited and/or stabilized at the mother centriole in a KIF24-dependent manner; KIF24, a kinesin-like protein, also restricts ciliogenesis through its microtubule depolymerizing activity (Kobayashi et al, 2011). In addition to promoting the release of CCP110, TTBK2 also plays a role in the recruitment of intraflagellar transport (IFT) proteins and in this way contributes to extension of the ciliary axoneme (Goetz et al, 2012; Ye et al, 2014). Mutations in TTBK2 disrupt ciliogenesis and are associated with the development of spinocerebellar ataxia (Houlden et al, 2007; Bouskila et al, 2011; reviewed in Jackson, 2012).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q6IQ55-1",
"P48730-1",
"O00444-1",
"P17612-1",
"P49674-1",
"P07900-1",
"P51955-1",
"P06493-1",
"P53350-1",
"P68366-1",
"Q71U36-1"
],
"evidence": [
{
"id": "R-HSA-5626228",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5626228"
}
]
},
{
"id": "R-HSA-5626681",
"name": "Recruitment of transition zone proteins",
"equation": "",
"summary": "The transition zone is a protein-rich zone at the base of the cilium that forms after maturation of the mother centriole and prior to or concurrent with the initiation of intraflagellar transport (IFT) (reviewed in Benzing and Schermer, 2011; Reiter et al, 2012). The transition zone consists of a growing number of proteins and protein complexes, many of whose genes are associated with ciliopathies such as nephronophthisis, Meckel-Gruber syndrome and Joubert's syndrome (Reiter et al, 2006; Hu et al, 2010; Sang et al, 2011; Williams et al, 2011; Garcia-Gonzalo et al, 2011; Chih et al, 2012; reviewed in Reiter et al, 2012). In conjunction with SEPT2, which was recently shown to form a septin ring diffusion barrier at the base of the cilium, the transition zone and its resident proteins contribute to protein sorting and ciliary membrane composition and act as a ciliary gate (Hu et al, 2010; Williams et al, 2011; Garcia-Gonzalo et al, 2011; Chih et al, 2012; reviewed in Reiter et al, 2012).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q6IQ55-1",
"P48730-1",
"Q96L34-1",
"O00444-1",
"P17612-1",
"P49674-1",
"P07900-1",
"P51955-1",
"P06493-1",
"P53350-1",
"P68366-1",
"Q71U36-1"
],
"evidence": [
{
"id": "R-HSA-5626681",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5626681"
}
]
},
{
"id": "R-HSA-5626699",
"name": "MARK4 binds ODF2 in the centriole",
"equation": "",
"summary": "MARK4 (microtubule associated protein/microtubule affinity regulating kinase 4) was identified in a screen as a positive regulator of ciliogenesis (Kuhns et al, 2013). MARK4 interacts at the centriole with the subdistal appendage component ODF2 and this interaction is required to promote axonemal extension (Kuhns et al, 2013; reviewed in Kim and Dynlacht, 2013). Like Tau tubulin kinase 2 (TTBK2), MARK4 appears to have a role in promoting the dissociation of CCP110 and CEP97, uncapping the centriole and allowing axonemal extension to take place (Kuhns et al, 2013; Ye et al, 2014;; Goetz et al, 2012). Although this reaction shows that MARK4 is recruited to the centriole subsequent to TTBK2, the timing of the ODF2:MARK4 interaction is not known.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q6IQ55-1",
"P48730-1",
"Q96L34-1",
"O00444-1",
"P17612-1",
"P49674-1",
"P07900-1",
"P51955-1",
"P06493-1",
"P53350-1",
"P68366-1",
"Q71U36-1"
],
"evidence": [
{
"id": "R-HSA-5626699",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5626699"
}
]
},
{
"id": "R-HSA-5637764",
"name": "Binding of GRB2:GAB1 complex to p-EGFRvIII mutant",
"equation": "",
"summary": "Direct binding of the GRB2:GAB1 complex to phosphorylated homodimers of EGFRvIII cancer mutant has not been tested. This complex is recruted to EGFR via GRB2 binding to phosphorylated tyrosine residues Y1068 and Y1086 (corresponding to Y1092 and Y1110, respectively, when counting from the first amino acid of the EGFR precursor, prior to cleavage of the 24-amino acid signal peptide at the N-terminus). Phosphorylation of Y1068 (i.e. Y1092) has been directly demonstrated in EGFRvIII mutant (Huang et al. 2007).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637764",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637764"
}
]
},
{
"id": "R-HSA-5637765",
"name": "Binding of PI3K to complex of GRB2:GAB1 and p-EGFRvIII",
"equation": "",
"summary": "EGFRvIII cancer mutant is assumed to recruit the PI3K complex PIK3CA:PIK3R1 in a manner similar to wild-type EGFR (Rodrigues et al. 2000).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637765",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637765"
}
]
},
{
"id": "R-HSA-5637766",
"name": "Binding of SHC1 to p-5Y-EGFRvIII",
"equation": "",
"summary": "SHC1 (Src homology 2 domain-containing transforming protein) is known to bind two phosphorylated tyrosine docking sites of EGFR: Y1148 and Y1173 (corresponding to Y1172 and Y1197 when counting from the first amino acid of EGFR precursor, before the cleavage of the 24-amino acid signal peptide at the N-terminus takes place). Phosphorylation of Y1173 tyrosine residue was directly demonstrated in EGFRvIII mutant (Han et al. 2006, Grandal et al. 2007) as well as the phosphorylation of Y1148 (Huang et al. 2007).
Binding of SHC1 to EGFRvIII cancer mutant has not been tested but SHC1 is assumed to bind EGFRvIII in the same way it binds wild-type EGFR.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637766",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637766"
}
]
},
{
"id": "R-HSA-5637770",
"name": "Binding of GRB2:SOS1 complex to phosphorylated EGFRvIII",
"equation": "",
"summary": "Direct binding of GRB2:SOS1 complex to phosphorylated homodimers of EGFRvIII cancer mutant has not been tested. GRB2 binds to phosphorylated tyrosine residues Y1068 and Y1086 (corresponding to Y1092 and Y1110, respectively, when counting from the first amino acid of the EGFR precursor, prior to cleavage of the 24-amino acid signal peptide at the N-terminus). Phosphorylation of Y1068 (i.e. Y1092) has been directly demonstrated in EGFRvIII mutant (Huang et al. 2007).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637770",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637770"
}
]
},
{
"id": "R-HSA-5637792",
"name": "PLC-gamma 1 binds to p-EGFRvIII mutant",
"equation": "",
"summary": "Tyrosine residue Y992 (corresponding to Y1016 when counting from the first amino acid of the EGFR precursor, prior to cleavage of the 24-amino acid signal peptide at the N-terminus), a docking site for PLC-gamma 1 (PLCG1), is phosphorylated in EGFRvIII cancer mutant and expected to recruit PLC-gamma 1 in the same way as the wild-type EGFR receptor (Grandal et al. 2007).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P19174-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637792",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637792"
}
]
},
{
"id": "R-HSA-5637794",
"name": "EGFRvIII does not bind CBL",
"equation": "",
"summary": "In EGFRvIII mutant, Y1069 (i.e. Y1045 in the mature protein) is not phosphorylated (Han et al. 2006, Grandal et al. 2007). Han et al. detected no CBL binding to EGFRvIII mutant (Han et al. 2006), while Grandal et al. detected very little binding, which they explained by indirect recruitment of CBL to EGFRvIII through GRB2 (Grandal et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P22681-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637794",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637794"
}
]
},
{
"id": "R-HSA-5637795",
"name": "Phosphorylation of PLC-gamma 1 by p-EGFRvIII mutant",
"equation": "",
"summary": "Once recruited, PLC-gamma 1 is assumed to be phosphorylated by EGFRvIII cancer mutant in the same way it is phosphorylated by the wild-type EGFR (Meisenhelder et al. 1989, Wahl et al. 1990).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P19174-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637795",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637795"
}
]
},
{
"id": "R-HSA-5637796",
"name": "Phosphorylation of SHC1 by p-5Y-EGFRvIII",
"equation": "",
"summary": "EGFRvIII cancer mutant was not directly tested for its ability to phosphorylate SHC1, but is assumed to interact with SHC1 in the same way as the wild-type EGFR protein (Soler et al. 1994, VanderKuur et al. 1995).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637796",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637796"
}
]
},
{
"id": "R-HSA-5637798",
"name": "Phosphorylated SHC1 in complex with p-5Y-EGFRvIII recruits GRB2:SOS1 complex",
"equation": "",
"summary": "Recruitment of GRB2:SOS1 complex by SHC1 bound to phosphorylated dimers of EGFRvIII cancer mutant has not been directly tested, but is assumed to happen in the same way it happens with the SHC1 bound to the phosphorylated homodimer of wild-type EGFR (Chardin et al. 1993).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637798",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637798"
}
]
},
{
"id": "R-HSA-5637800",
"name": "Dissociation of phosphorylated PLC-gamma 1 from p-EGFRvIII mutant",
"equation": "",
"summary": "Once phosphorylated, PLC-gamma 1 is expected to dissociate from phosphorylated EGFRvIII cancer mutant and induce downstream signaling in the same way it does when activated by the wild-type EGFR. However, except for the phosphorylation of PLCG1 binding site in EGFRvIII (Grandal et al. 2007), other events involved in activation of PLCG1 signaling have not been studied in cells expressing EGFRvIII.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P19174-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637800",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637800"
}
]
},
{
"id": "R-HSA-5637801",
"name": "Conversion of PIP2 to PIP3 by PI3K bound to phosphorylated EGFRvIII",
"equation": "",
"summary": "The kinase activity of PI3K mediates the phosphorylation of PIP2 to form PIP3. It is assumed that EGFRvIII cancer mutant induces PI3K/AKT signaling in a manner similar to wild-type EGFR. Accordingly, activation of PI3K/AKT signaling cascade has been demonstrated in cells expressing EGFRvIII (Lammering et al. 2003, Li et al. 2004)",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5637801",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637801"
}
]
},
{
"id": "R-HSA-5637806",
"name": "SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with p-EGFRvIII)",
"equation": "",
"summary": "Based on the wild-type EGFR signaling, it is assumed that the guanine nucleotide exchange factor SOS1 interacts with phosphorylated EGFRvIII mutant through the adaptor protein, GRB2. Upon formation of this complex, SOS1 activates RAS by promoting GDP release and GTP binding. Although this reaction has not been directly confirmed for EGFRvIII cancer mutant, RAS-MAPK signaling cascade is activated in cells expressing EGFRvIII (Montgomery et al.1995).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P07900-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-5637806",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637806"
}
]
},
{
"id": "R-HSA-5637808",
"name": "SOS-mediated nucleotide exchange of RAS (mediated by GRB2:SOS1 in complex with phosphorylated SHC1 and p-EGFRvIII)",
"equation": "",
"summary": "SOS1 is the guanine nucleotide exchange factor (GEF) for RAS. SOS1, recruited by GRB2 bound to p-SHC1:p-EGFRvIII mutant, is assumed to activate RAS nucleotide exchange from the inactive form (bound to GDP) to an active form (bound to GTP). Although this reaction has not been shown to occur directly for EGFRvIII cancer mutant, activation of RAF/MAP kinase cascade has been demonstrated in cells expressing EGFRvIII (Montgomery et al. 1995).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P00533-1",
"P07900-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-5637808",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5637808"
}
]
},
{
"id": "R-HSA-5638009",
"name": "CEP164 recruits RAB3IP-carrying Golgi-derived vesicles to the basal body",
"equation": "",
"summary": "The distal appendage protein CEP164 interacts with RAB3IP, and in this way recruits Golgi-derived vesicles to the basal body to initiate ciliary membrane biogenesis (Schmidt et al, 2012; Westlake et al, 2011; Rohatgi and Snell, 2010). RAB3IP recruitment to the distal appendages of centrioles promotes the appropriate localization and activation of RAB8A (Nachury et al, 2007; Yoshimura et al, 2007; Westlake et al, 2011; Schmidt et al, 2012).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P62491-1",
"Q6IQ55-1",
"P48730-1",
"Q96L34-1",
"O00444-1",
"P17612-1",
"P49674-1",
"P07900-1",
"P51955-1",
"P06493-1",
"P53350-1",
"P68366-1",
"Q71U36-1"
],
"evidence": [
{
"id": "R-HSA-5638009",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5638009"
}
]
},
{
"id": "R-HSA-5638137",
"name": "EGFRvIII cancer variant does not bind EGF ligand",
"equation": "",
"summary": "EGFRvIII mutant lacks the ligand binding domain and is therefore unable to bind EGFR ligands (Fernandes et al. 2001).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-5638137",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5638137"
}
]
},
{
"id": "R-HSA-6790041",
"name": "Expression of STAT3-upregulated cytosolic proteins",
"equation": "",
"summary": "Signal transducer and activator of transcription 3 (STAT3) is a key regulator of gene expression in response to signaling of many cytokines including interleukin-6 (IL6), Oncostatin M, and leukemia inhibitory factor. Using microarray techniques, hundreds of genes have been reported as potential STAT3 target genes (Dauer et al. 2005, Hsieh et al. 2005). Some of these genes have been proven to be direct STAT3 targets using genome-wide chromatin immunoprecipitation screening (Snyder et al. 2008, Carpenter & Lo 2014). Genes for cytoplasmic proteins upregulated by STAT3 include Suppressor of cytokine signaling 3 (SOCS3) (He et al. 2003), Induced myeloid leukemia cell differentiation protein Mcl-1 (MCL1) (Becker et al. 2014), Heat shock protein HSP 90-alpha (HSP90AA1) (Chen et al. 2007), Fascin (FSCN1) (Snyder et al. 2011), Vimentin (VIM) (Wu et al. 2004), Rho-related GTP-binding protein RhoU (RHOU) (Schiavone et al. 2009), RAC-alpha serine/threonine-protein kinase (AKT1) (Xu et al. 2005), Cyclin-dependent kinase inhibitor 1 (CDKN1A) (Bellido et al. 1998), Phosphatidylinositol 3-kinase regulatory subunit alpha (PIK3R1) (Abell et al. 2005), Signal transducer and activator of transcription 1 (STAT1) (Han et al. 2013), Interferon regulatory factor 4 (IRF4) (Durant et al. 2010) and Nitric oxide synthase, inducible (NOS2) (Lo et al. 2005).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P31749-1",
"P07900-1",
"P35228-1"
],
"evidence": [
{
"id": "R-HSA-6790041",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6790041"
}
]
},
{
"id": "R-HSA-6798748",
"name": "Exocytosis of secretory granule lumen proteins",
"equation": "",
"summary": "Secretory vesicles provide a reservoir of secreted proteins and membrane-associated receptors that are required at the earliest stages of the neutrophil-mediated inflammatory response. They are mobilized in response to a wide variety of inflammatory stimuli (Sengelov et al. 1993a,b). Resultant cell surface changes allow the neutrophil to establish firm contact with activated vascular epithelium (Faurschou & Borregaard 2003).",
"cellular_location": "extracellular region, secretory granule lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P18669-1",
"Q13464-1",
"P32320-1",
"P09917-1",
"O00487-1",
"P13639-1",
"P12268-1",
"P62937-1",
"Q96G03-1",
"P68402-1",
"Q99436-1",
"P55072-1",
"P68104-1",
"P11142-1",
"Q9Y315-1",
"P13010-1",
"P04075-1",
"P09972-1",
"P07900-1",
"P09769-1",
"P09211-1",
"Q16539-1",
"P14618-1",
"P07741-1",
"Q01432-1",
"P12956-1",
"Q7Z6Z7-1",
"Q9UNP9-1",
"P14174-1",
"P04040-1",
"O00571-1",
"P06744-1",
"P52790-1",
"P11678-1",
"P00491-1",
"P06737-1",
"P00746-1",
"Q13162-1",
"P17858-1",
"P46976-1",
"P22392-1",
"P13716-1",
"O75874-1",
"P20839-1",
"O00764-1"
],
"evidence": [
{
"id": "R-HSA-6798748",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6798748"
}
]
},
{
"id": "R-HSA-6800434",
"name": "Exocytosis of ficolin-rich granule lumen proteins",
"equation": "",
"summary": "Ficoli-1 rich granules are a relatively new fourth neutrophil granule population that is enriched in the microbial lectin ficolin-1. Ficolin-1 is present in tertiary granules, but ficolin-1 rich granules can be differentiated by having low levels of gelatinases and an elevated exocytosis propensity (Rorvig et al. 2009, 2013). The importance of these granules may be to provide rapid release of pattern recognition molecules to activate the lectin complement pathway (Rorvig et al. 2009).",
"cellular_location": "extracellular region, ficolin-1-rich granule lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9UBR2-1",
"P18669-1",
"P32320-1",
"P09917-1",
"O00487-1",
"P13639-1",
"P12268-1",
"P62937-1",
"P15586-1",
"Q96G03-1",
"Q9P0J7-1",
"P68402-1",
"P36871-1",
"Q99436-1",
"P07339-1",
"P13798-1",
"P53396-1",
"P55072-1",
"P68104-1",
"P11142-1",
"Q9Y315-1",
"P04075-1",
"P09972-1",
"P07900-1",
"P09211-1",
"Q16539-1",
"P07858-1",
"P14618-1",
"P28482-1",
"Q01432-1",
"P12956-1",
"Q7Z6Z7-1",
"Q9UNP9-1",
"Q13510-1",
"P14174-1",
"P15848-1",
"P16278-1",
"Q8WVQ1-1",
"P04040-1",
"O00571-1",
"P14780-1",
"P06744-1",
"P52790-1",
"P00491-1",
"P06737-1",
"Q16769-1",
"P08236-1",
"P02794-1",
"P07384-1",
"Q14004-1",
"P00746-1",
"P98066-1",
"P25774-1",
"Q13162-1",
"P17858-1",
"P46976-1",
"P09960-1",
"P22392-1",
"P13716-1",
"O75874-1",
"P20839-1"
],
"evidence": [
{
"id": "R-HSA-6800434",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6800434"
}
]
},
{
"id": "R-HSA-8852362",
"name": "GTSE1 binds CDKN1A",
"equation": "",
"summary": "Stabilization of the newly synthesized protein product of the CDKN1A (p21) gene, a CDK inhibitor and a TP53 (p53) transcriptional target, requires binding of CDKN1A to FKBPL (WISp39). FKBPL simultaneously interacts with CDKN1A and a chaperone protein HSP90, forming a ternary complex (Jascur et al. 2005). GTSE1 was identified as another component of the complex of CDKN1A, FKBPL and HSP90. GTSE1 directly interacts with CDKN1A and FKBPL and contributes to CDKN1A stabilization (Bublik et al. 2010). Increased CDKN1A levels delay G2/M onset and rescue cells from G2 checkpoint-induced apoptosis, thus causing resistance to taxol induced cytotoxicity (Yu et al. 1998, Bublik et al. 2010).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-8852362",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8852362"
}
]
},
{
"id": "R-HSA-8853405",
"name": "TPX2 binds AURKA at centrosomes",
"equation": "",
"summary": "TPX2 binds to aurora kinase A (AURKA) at centrosomes. The first 43 amino acids at the N-terminus of TPX2 are needed for binding to AURKA (Bayliss et al. 2003). HMMR (RHAMM) binds to TPX2 (Groen et al. 2004, Maxwell et al. 2005) and is involved in the proper localization of TPX2 to centrosomes and TPX2-mediated AURKA activation (Chen et al. 2014, Scrofani et al. 2015).
TPX2 binding to Aurora A protects premature AURKA degradation by APC/C-mediated proteolysis during early mitosis. TPX2 differentially regulates AURKA stability, activity and localization. While amino acids 1-43 in TPX2 facilitate complex formation between AURKA and TPX2 and promote kinase activation, they are insufficient for AURKA targeting to the mitotic spindle (Giubettini et al. 2011).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P48730-1", "O00444-1", "P17612-1", "P49674-1", "P07900-1", "P51955-1", "O14965-1", "P06493-1", "P53350-1", "P68366-1", "Q71U36-1" ], "evidence": [ { "id": "R-HSA-8853405", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8853405" } ] }, { "id": "R-HSA-8853419", "name": "TPX2 promotes AURKA autophosphorylation", "equation": "", "summary": "TPX2 promotes aurora kinase A (AURKA) activation via autophosphorylation of AURKA on threonine residue T288. Continuous association of TPX2 with AURKA facilitates active state conformation of AURKA and may prevent inactivation of AURKA by protein phosphatases (Bayliss et al. 2003).
Molecular dynamic simulations suggest the existence of two TPX2-dependent switches for Aurora A activation. 1) TPX2 binding to Aurora A forces lysine residue K143 of AURKA into an \u201copen\u201d state, which pulls ADP out of the ATP binding site in AURKA to promote kinase activation. 2) Arginine residue R180 of AURKA undergoes a \u201cclosed\u201d movement upon TPX2 binding, thus capturing phosphorylated threonine T288 of AURKA into a buried position and locking AURKA in its active conformation. The existence of two TPX2-dependent switches in AURKA activation was further verified by the analysis of two AURKA mutants (K143A and R180A) (Xu et al. 2011).AURKA activation is enabled through phosphorylation and TPX2 binding; these two activating switches act synergistically and withough a predefined order (Dodson and Bayliss 2012).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P48730-1",
"O00444-1",
"P17612-1",
"P49674-1",
"P07900-1",
"P51955-1",
"O14965-1",
"P06493-1",
"P53350-1",
"P68366-1",
"Q71U36-1"
],
"evidence": [
{
"id": "R-HSA-8853419",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8853419"
}
]
},
{
"id": "R-HSA-8939203",
"name": "HSP90-dependent ATP hydrolysis promotes release of ESR:ESTG from chaperone complex",
"equation": "",
"summary": "Release of the estrogen receptor from the chaperone complex requires requires HSP90-dependent ATP hydrolysis, and occurs at the same rate in the presence and absence of ligand (Smith et al, 1992; Smith et al, 1993; Aumais et al, 1997; Grenert et al, 1997; Obermann et al, 1998; Panaretou et al, 1998; reviewed in Smith and Toft, 2008). In the absence of ligand, released ERs are recaptured by HSP40 through its interaction with the ligand binding domain (LBD), priming reassembly of the chaperone complex. Ligand binding may result in the loss of the HSP40-binding site, allowing the receptor to escape repetitive rounds of chaperone complex assembly, and freeing it for DNA-binding (reviewed in Smith and Toft, 2008).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q08752-1",
"P53041-1",
"P07900-1",
"Q02790-1",
"Q15185-1",
"Q13451-1"
],
"evidence": [
{
"id": "R-HSA-8939203",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8939203"
}
]
},
{
"id": "R-HSA-8939204",
"name": "ESTG binds ESR1:chaperone complex",
"equation": "",
"summary": "In the nucleus, estrogens bind to estrogen receptors, members of the nuclear receptor superfamily. Human cells have 2 estrogen receptors, ER alpha and ER beta, encoded by two genes. Expression of the two genes varies by tissue: both are expressed in the central nervous system, the cardiovascular system, the urogenital tract and in the breast and bone; ER alpha expression predominates in the uterus, mammary gland, and liver, and the gastrointestinal tract expresses only ER beta (Pearce and Jordan, 2004; Gustafsson et al, 1999; Pfaffl et al, 2001; reviewed in Bai and Gust, 2009). The receptors show 47% identity overall and share a common organization consisting of 6 domains: an N-terminal A/B domain with ligand-independent activation function, a C domain containing the 2 DNA-binding zinc fingers, a hinge region (D) with a nuclear localization signal, an E domain that contains the ligand binding and dimerization domains as well as a ligand-dependent transactivation function, and a C-terminal F domain of poorly characterized function. The DNA-binding domain is the most highly conserved (97% identity) while the ligand-bindind domain is more variable (47% identity) (reviewed in Ruff et al, 2000; Bai and Gust, 2009). ER alpha and beta can homo- and heterodimerize, and recognize a common estrogen-response element due to their shared DNA-binding domains (reviewed in Bai and Gust, 2009). Functional studies suggest that ER alpha and beta have overlapping but distinct roles in estrogen-responsive transcription (Harrington et al, 2003; Katzenellenbogen and Katzenellenbogen, 2000; Pearce and Jordan, 2004; Pfaffl et al, 2001)
In the unliganded state, estrogen receptors are part of a multi-subunit complex containing HSP90, p23 (also known as PTGES3) and other chaperone-associated proteins (Joab et al, 1984; Segnitz et al, 1995; Knoblauch et al, 1999; Bouhouche-Chatelier et al, 2001; Fliss et al, 2000; Oxelmart et al, 2006; reviewed in Smith and Toft, 2008; Bai and Gust, 2009). This complex is part of a chaperone binding and release cycle shared by many nuclear receptors (described in more detail in the pathway \\HSP90 chaperone cycle for steroid hormone receptors\\) that governs receptor folding and activity and may contribute to a high-affinity conformation of the ligand-binding domain (reviewed in Pratt and Toft, 1997; Smith and Toft, 2008). HSP90 release from the receptor complex requires ATP hydrolysis (Smith et al, 1993; Grenert et al, 1997; Panaretou et al, 1998; Obermann et al, 1998; Smith et al, 1992; reviewed in Smith and Toft, 2008).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q08752-1",
"P53041-1",
"P07900-1",
"Q02790-1",
"Q15185-1",
"Q13451-1"
],
"evidence": [
{
"id": "R-HSA-8939204",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8939204"
}
]
},
{
"id": "R-HSA-9018785",
"name": "RHOBTB2 binds GTP",
"equation": "",
"summary": "RHOBTB2 binds to GTP, but does not switch between GDP- and GTP-bound states (Manjarrez et al. 2014). ATP-dependent protein folding chaperone activity of the HSP90:CDC37 complex and binding of RHOBTB2 to the HSP90:CDC37 complex enables RHOBTB2 to bind GTP (Manjarrez et al. 2014). There are no known RHOBTB2 GAPs - DEBDC1B was reported to bind RHOBTB2 by Bagci et al. 2020, but its RHOBTB2-directed GAP activity has not been tested.",
"cellular_location": "cytosol, endosome membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9018785",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9018785"
}
]
},
{
"id": "R-HSA-9032751",
"name": "Estrogen-independent phosphorylation of ESR1 S118 by MAPK1 and MAPK3",
"equation": "",
"summary": "ESR1-mediated signaling can be initiated in an estrogen-independent manner downstream of stimuli such as EGF, NRG1, IGF, insulin, dopamine and cAMP (Ignar-Trowbridge et al, 1993, Pietras et al, 1995; Ma et al, 1994; Newton et al, 1994; Smith et al, 1993; Aronica and Katzenellenbogen, 1993). Stimulation with EGF or IFGF-1 promotes the MAPK-dependent phosphorylation of ESR1 at serine 118, which contributes to interaction with CBP/p300 and the p160 family of coactivators (Bunone et al, 1996; Chen et al, 2002; Cheng et al, 2007; reviewed in Anbalagan and Rowan, 2105). Serine 118 is also phosphorylated in response to estrogen stimulation (Chen et al, 2002; reviewed in Anbalagan and Rowan, 2015).
The relationship between MAPK-dependent S118 phosphorylation of ESR1 and the release from the cochaperone complex and ESR1 dimerization is not clear. In this reaction, all these events are shown happening simultaneously.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-5082403"
],
"enzyme_list": [
"Q08752-1",
"P27361-1",
"P53041-1",
"P07900-1",
"Q02790-1",
"Q15185-1",
"P28482-1",
"Q13451-1"
],
"evidence": [
{
"id": "R-HSA-9032751",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9032751"
}
]
},
{
"id": "R-HSA-9038161",
"name": "Progesterone stimulation promotes PGR:P4 binding to ESR1:ESTG",
"equation": "",
"summary": "In addition to being a target of estrogen-dependent transcription, the progesterone receptor (PGR) interacts directly with ER alpha after stimulation with progesterone and modulates ESR1:ESTG binding (Ballare et al, 2003; Mohammed et al, 2015). Progesterone stimulation under estrogen-rich conditions promotes the release of PGR from the chaperone complex to facilitate interaction with ESR1 (Mohammed et al, 2015; reviewed in ).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q02790-1",
"Q15185-1"
],
"evidence": [
{
"id": "R-HSA-9038161",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9038161"
}
]
},
{
"id": "R-HSA-9622831",
"name": "Substrate:LAMP2a binds HSP90",
"equation": "",
"summary": "Heat shock cognate 71 kDa protein (HSPA8) translocates substrates from cytosol to lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). HSPA8 is then released from this complex. Subsequently, Heat shock protein HSP 90 binds to the lysosomal luminal end of LAMP2a (Bandyopadhyay U et al. 2008). This facilitates the multimerization of LAMP2a and internalization of substrate into the lumen. Experiments confirming this binding were performed on rat models.",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9622831",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9622831"
}
]
},
{
"id": "R-HSA-9624158",
"name": "Substrate:LAMP2a:HSP90 polymerizes",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in the lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) acts as the constitutive chaperone that binds KFERQ-domain containing substrates in the cytosol. Consequently, the Hspa8:Substrate complex translocates from cytosol to lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, HSPA8 is released and Heat shock protein HSP 90 binds to the lysosomal luminal end of LAMP2a. Binding of HSP90 stabilizes LAMP2 to multimerize into a 700 kDa complex (Bandyopadhyay U et al. 2008). This facilitates the internalization of substrate into the lumen. Experiments confirming this binding were performed on rat models.",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9624158",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9624158"
}
]
},
{
"id": "R-HSA-9625188",
"name": "HSPA8 transports unfolded substrate to lysosomal lumen for degradation",
"equation": "",
"summary": "Heat shock cognate 71 kDa protein (HSPA8) translocates substrates from the cytosol to the lysosomal membrane. Subsequently, the substrate unfolds and binds to HSPA8 in the lysosomal lumen. HSPA8 facilitates the transport of the unfolded substrate to the lumen where it is then degraded (Agarraberes FA et al. 1997, Cuervo AM et al. 1997).",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9625188",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9625188"
}
]
},
{
"id": "R-HSA-9625196",
"name": "Unfolded substrate in LAMP2a multimeric complex binds HSPA8",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in the lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) acts as the constitutive chaperone that binds a KFERQ-domain containing substrate in the cytosol and translocates to lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, Hspa8 is released and Heat shock protein HSP90 binds to the lysosomal luminal end of LAMP2a. The LAMP2a complex then multimerizes and stabilizes. Now, the substrate unfolds and binds to HSPA8 in the lysosomal lumen (Agarraberes FA et al. 1997, Cuervo AM et al. 1997). Subsequently, the substrate is internalized and degraded in the lumen. Experiments confirming this interaction were performed in rats.",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9625196",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9625196"
}
]
},
{
"id": "R-HSA-9625197",
"name": "GFAP binds LAMP2a multimer",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in the lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) acts as the constitutive chaperone that binds KFERQ-domain containing substrates in the cytosol. Consequently, the HSPA8:Substrate complex translocates from cytosol to lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, HSPA8 is released and Heat shock protein HSP 90 binds to the lysosomal luminal end of LAMP2a. This LAMP2a complex then multimerizes into a 700 kDa entity and is stabilized by the binding of Glial fibrillary acidic protein (GFAP) (Bandyopadhyay U et al. 2010). Subsequently, the substrate is unfolded and internalized into the lumen. Experiments confirming this binding were performed on rat models.",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9625197",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9625197"
}
]
},
{
"id": "R-HSA-9626039",
"name": "pGFAP binds GFAP in LAMP2a multimer",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) transports substrates from the cytosol to the lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, LAMP2a forms a multimeric complex stabilized with the aid of HSP90 and glial fibrillary acidic protein (GFAP). This multimer allows the transfer of substrate into the lumen. The stability of this complex is regulated by the dynamics of GFAP and elongation factor 1\u03b1 (EEF1A1). During autophagy, a phosphorylated version of GFAP remains bound to EEF1A1. When GTP becomes available, EEF1A1 dissociates from GFAP and binds with GTP in the cytosol. Subsequently, EEF1A1 is translocated from lysosomal membrane to cytosol. This makes p-GFAP available to bind with GFAP in the LAMP2a multimer complex (Bandyopadhyay U et al. 2010). Experiments confirming this binding were performed in rats.",
"cellular_location": "lysosomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9626039",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9626039"
}
]
},
{
"id": "R-HSA-9626060",
"name": "HSPA8:Substrate dissociates from LAMP2a multimer",
"equation": "",
"summary": "Heat shock cognate 71 kDa protein (HSPA8) translocates substrates from the cytosol to the lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). The LAMP2a complex then multimerizes and stabilizes. Subsequently, the substrate unfolds and translocates to the lumen. The substrate bound HSPA8 then dissociates from LAMP2a multimer (Agarraberes FA et al. 1997, Cuervo AM et al. 1997). The function of LAMP2a multimer is now complete and starts to disassemble.",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P07998-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9626060",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9626060"
}
]
},
{
"id": "R-HSA-9626235",
"name": "HSPA8 dissociates from LAMP2a",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) transports substrates from the cytosol to the lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, LAMP2a forms a multimeric complex and transfers the substrate into the lumen. The stability of this complex is regulated by the dynamics of HSPA8. Cytosolic HSPA8 binds with LAMP2a multimers in the lysosomal membrane and triggers their disassembly into monomeric units (Bandyopadhyay U et al. 2008). HSPA8 dissociates from LAMP2a to make it available for further substrate autophagy. Experiments related to this event were performed in rats.",
"cellular_location": "cytosol, lysosomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9626235",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9626235"
}
]
},
{
"id": "R-HSA-9626242",
"name": "p-GFAP:GFAP dissociates from LAMP2a multimer",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) transports substrates from the cytosol to the lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, LAMP2a forms a multimeric complex and transfers the substrate into the lumen. The stability of this complex is regulated by the dynamics of glial fibrillary acidic protein (GFAP) and elongation factor 1\u03b1 (EEF1A1). During autophagy, a phosphorylated version of GFAP remains bound to EEF1A1. When GTP becomes available, EEF1A1 dissociates from GFAP and binds with GTP in the cytosol. This makes p-GFAP available to bind with GFAP in the LAMP2a multimer complex. Consequently, p-GFAP sequesters GFAP from LAMP2a multimer (Bandyopadhyay U et al. 2010). Experiments confirming this event were performed in rats.",
"cellular_location": "lysosomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9626242",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9626242"
}
]
},
{
"id": "R-HSA-9626253",
"name": "HSPA8 binds LAMP2a multimers",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) transports substrates from the cytosol to the lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, LAMP2a forms a multimeric complex and transfers the substrate into the lumen. The stability of this complex is regulated by the dynamics of HSPA8. Cytosolic HSPA8 binds with LAMP2a multimers in the lysosomal membrane and triggers their disassembly. Interestingly, substrate bound HSPA8 do not have this effect on LAMP2a (Bandyopadhyay U et al. 2008). Experiments confirming this event were performed in rats.",
"cellular_location": "cytosol, lysosomal membrane",
"input_participant_list": [
"R-HSA-9626026",
"R-HSA-264476"
],
"output_participant_list": [
"R-HSA-9626247"
],
"enzyme_list": [
"P11142-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9626253",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9626253"
}
]
},
{
"id": "R-HSA-9626256",
"name": "HSPA8:LAMP2a multimers depolymerizes to monomers",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) transports substrates from the cytosol to the lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, LAMP2a forms a multimeric complex and transfers the substrate into the lumen. The stability of this complex is regulated by the dynamics of HSPA8. Cytosolic HSPA8 binds with LAMP2a multimers in the lysosomal membrane. This triggers the disassembly of multimeric complexes into monomeric units (Bandyopadhyay U et al. 2008). Experiments confirming this event were performed in rats.",
"cellular_location": "cytosol, lysosomal membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P11142-1",
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9626256",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9626256"
}
]
},
{
"id": "R-HSA-9626276",
"name": "HSP90 dissociates from LAMP2a",
"equation": "",
"summary": "Intracellular proteins are targeted for proteolytic degradation in lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) transports substrates from the cytosol to the lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, LAMP2a forms a multimeric complex and transfers the substrate into the lumen. The stability of this complex is regulated by the dynamics of Heat shock protein HSP 90 (HSP90) and HSPA8 (Bandyopadhyay U et al. 2008). HSPA8 and HSP90 dissociate from LAMP2a to make it available for further substrate autophagy. Experiments related to this event were performed in rats.",
"cellular_location": "lysosomal membrane, lysosomal lumen",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9626276",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9626276"
}
]
},
{
"id": "R-HSA-9646347",
"name": "PolyUb-misfolded proteins bind VCP:HDAC6:HSP90:HSF1",
"equation": "",
"summary": "When the proteasome machinery is deregulated, misfolded proteins are eliminated by forming aggresomes. To this end, poly-ubiquitinated misfolded proteins bind to a complex comprising of Transitional endoplasmic reticulum ATPase (VCP), Histone deacetylase 6 (HDAC6), Heat shock protein HSP 90 (HSP90) and Heat shock factor protein 1 (HSF1). HDAC6 in the complex interacts with the ubiquitin molecules in the misfolded proteins. Following this binding event, this complex starts dissociating (Boyault C et al. 2007).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P55072-1",
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9646347",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646347"
}
]
},
{
"id": "R-HSA-9646354",
"name": "PolyUb-Misfolded Proteins:HDAC6 dissociate from complex",
"equation": "",
"summary": "Histone deacetylase 6 (HDAC6) appears to be a master regulator of the cell protective response to cytotoxic protein aggregate formation (Boyault et al. 2007).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P55072-1",
"P07900-1",
"Q99497-1",
"Q9UBN7-1",
"P13569-1"
],
"evidence": [
{
"id": "R-HSA-9646354",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9646354"
}
]
},
{
"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-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-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-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-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-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-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-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-HSA-9678925",
"name": "NR3C1 binds NR3C1 agonists",
"equation": "",
"summary": "Corticosteroids bind to the glucocorticoid receptor NR3C1 (Rupprecht et al. 1993, Lind et al. 2000), inhibiting pro-inflammatory NF-Kappa B and other inflammatory transcription factors, and promoting anti-inflammatory genes like interleukin-10. The short term effects of corticosteroids are decreased vasodilation and permeability of capillaries, as well as decreased leukocyte migration to sites of inflammation. From the Randomized Evaluation of COVID-19 Therapy (RECOVERY) trial in June 2020, dexamethasone was recommended for use in COVID-19 patients with severe respiratory symptoms. In the trial, dexamethasone reduced deaths by approximately one third in patients requiring ventilation and by one fifth in those requiring oxygen.;",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q02790-1",
"Q15185-1"
],
"evidence": [
{
"id": "R-HSA-9678925",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9678925"
}
]
},
{
"id": "R-HSA-9688459",
"name": "RIPK3 binds HSP90:CDC37",
"equation": "",
"summary": "Receptor-interacting serine/threonine protein kinase 3 (RIPK3 or RIP3) activation following the induction of necroptosis in human HT-29 colorectal adenocarcinoma cells requires the activity of a heat-shock protein 90 (HSP90) and cell division cycle 37 (CDC37) cochaperone complex (Li D et al. 2015). This complex physically associates with RIPK3. Chemical inhibitors of HSP90 efficiently block necroptosis by preventing RIP3 activation in HT-29. Cells with knocked down CDC37 were unable to respond to necroptosis stimuli (Li D et al. 2015). Further, geldanamycin, an inhibitor of HSP90, and siRNA/shRNA of HSP90\u03b1, protected cultured neurons from oxygen-glucose deprivation induced necroptosis by decreasing RIP3 expression (Wang Z et al. 2018). Geldanamycin was reported to nhibit programmed necrosis by suppressing RIPK3 protein expression (Cho YS et al. 2009).Moreover, the HSP90:CDC37 complex was found to interact and regulate the stability of mixed lineage kinase domain-like (MLKL), the downstream effector of the necroptotic signalling pathway (Bigenzahn JW et al. 2016; Jacobsen AV et al. 2016; Zhao XM et al. 2016).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q9Y572-1"
],
"evidence": [
{
"id": "R-HSA-9688459",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9688459"
}
]
},
{
"id": "R-HSA-9690534",
"name": "NR3C1 ligands bind NR3C1 (in the HSP90 chaperone complex)",
"equation": "",
"summary": "Steroid hormones receptors (SHRs) are intracellular transcription factors that can be activated by binding specific ligands (i.e., steroid hormones (SH)) to the ligand-binding domain (LBD) (Ray DW et AL. 1999; Pike AC et al. 1999; Bledsoe RK et al. 2002; Li Y et al. 2005; Kumar R and McEwan IJ 2012; Kumar R et al. 2011; Williams SP & Sigler PB 1998; Tanenbaum DM et al. 1998; Lusher SJ et al. 2012). LBD (E-region) resides in the C-terminal half of the receptor and in addition to ligand binding function contains a transcriptional activation function (AF2), sequences for dimerization, heat shock protein association, intermolecular silencing and intramolecular repression (Kumar R and McEwan IJ 2012). The binding of hormone acts as an allosteric switch to regulate SHR-DNA and SHR-protein interactions, including interdomain interactions and/or dimerization (Kumar R and McEwan IJ 2012).
SHs are synthesized from cholesterol in the adrenal cortex (glucocorticoids, mineralocorticoids, and adrenal androgens), the testes (testicular androgens, estrogen), and the ovary and placenta (estrogen and progestogen or progestins) (Payne AH & Hales DB 2004; Hu J et al. 2010;). SHs reach their target cells via the blood, where they are bound to specific carrier proteins (Grishkovskaya I et al. 2000; Hammond GL 2016). SHs detach from the carrier proteins and because of their lipophilic nature readily diffuse through the plasma membrane of cells (Oren I et al. 2004). Within the target cells SHs bind to steroid hormone receptors (SHRs) which are present in a heterocomplex with heat shock protein HSP90 and co-chaperones (e.g., immunophilins p23) (Echeverria PC & Picard D 2010). The ATP-bound form of HSP90 and chaperone-mediated conformational changes are required to keep SHRs in a ligand binding-competent state (McLaughlin SH et al. 2002; Pratt WB et al. 2008; Krukenberg KA et al. 2011).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P07900-1", "Q02790-1", "Q15185-1" ], "evidence": [ { "id": "R-HSA-9690534", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9690534" } ] }, { "id": "R-HSA-9698844", "name": "MLKL binds HSP90:CDC37", "equation": "", "summary": "The pseudokinase mixed lineage kinase domain-like (MLKL), is the terminal known obligatory effector in the necroptosis pathway, and is activated following phosphorylation by receptor interacting protein kinase-3 (RIPK3). Activated MLKL translocates to membranes, leading to membrane destabilisation and subsequent cell death. Heat\u2011shock protein 90 (HSP90) and cell division cycle 37 (CDC37) cochaperone complex contributes to activation of MLKL (Jacobsen AV et al. 2016; Zhao XM et al. 2016; Bigenzahn JW et al. 2016). Whether HSP90 exerts its effects on MLKL folding, oligomerization, or translocation to membranes has not been precisely determined, although it is plausible HSP90 impacts each of these activation steps (Murphy JM 2020).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P07900-1" ], "evidence": [ { "id": "R-HSA-9698844", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9698844" } ] }, { "id": "R-HSA-9705925", "name": "Androgens binds AR (in the HSP90 chaperone complex)", "equation": "", "summary": "Steroid hormones receptors (SHRs) are intracellular transcription factors that can be activated by binding specific ligands (steroid hormones (SH)) to the ligand-binding domain (LBD) (Ray DW et AL. 1999; Pike AC et al. 1999; Bledsoe RK et al. 2002; Li Y et al. 2005; Kumar R and McEwan IJ 2012; Kumar R et al. 2011; Williams SP & Sigler PB 1998; Tanenbaum DM et al. 1998; Lusher SJ et al. 2012). LBD (E-region) resides in the C-terminal half of the receptor and in addition to ligand binding function contains a transcriptional activation function (AF2), sequences for dimerization, heat shock protein association, intermolecular silencing and intramolecular repression (Kumar R and McEwan IJ 2012). The binding of hormone acts as an allosteric switch to regulate SHR-DNA and SHR-protein interactions, including interdomain interactions and/or dimerization (Kumar R and McEwan IJ 2012).
SHs are synthesized from cholesterol in the adrenal cortex (glucocorticoids, mineralocorticoids, and adrenal androgens), the testes (testicular androgens, estrogen), and the ovary and placenta (estrogen and progestogen or progestins) (Payne AH & Hales DB 2004; Hu J et al. 2010;). SHs reach their target cells via the blood, where they are bound to specific carrier proteins (Grishkovskaya I et al. 2000; Hammond GL 2016). SHs detach from the carrier proteins and because of their lipophilic nature readily diffuse through the plasma membrane of cells (Oren I et al. 2004). Within the target cells SHs bind to steroid hormone receptors (SHRs) which are present in a heterocomplex with heat shock protein HSP90 and co-chaperones (e.g., immunophilins p23) (Echeverria PC & Picard D 2010). The ATP-bound form of HSP90 and chaperone-mediated conformational changes are required to keep SHRs in a ligand binding-competent state (McLaughlin SH et al. 2002; Pratt WB et al. 2008; Krukenberg KA et al. 2011). Here, the androgens testosterone (TEST), dihydrotestosterone (DHTEST), androst-4-en-3,17-dione (ANDST) and 6-dehydrotestosterone bind the androgen receptor (AR), within the HSP90 chaperone complex.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q02790-1",
"Q15185-1"
],
"evidence": [
{
"id": "R-HSA-9705925",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705925"
}
]
},
{
"id": "R-HSA-9705926",
"name": "AR binds AR agonists",
"equation": "",
"summary": "Endogenous androgens such as testosterone and dihydrotestosterone are steroid hormones that regulate the development and maintenance of male characteristics in vertebrates through their binding to the androgen receptor (AR) (T\u00f3th & Zak\u00e1r 1982, Askew et al. 2007, Brinkmann 2011). They are synthesised from cholesterol in the testes, ovaries and the adrenal glands. Synthetic androgen agonists (AR agonists) are used in androgen replacement therapy to counter the effects of male hypogonadism (diminished functional activity of the gonads) (Rey & Grinspon 2020), to help with menopausal symptoms (Marina et al. 2020), in delayed puberty, the prophylactic treatment of hereditary angioedema (Bork 2018), the treatment of endometriosis (Simitsidellis et al. 2018, Gibson et al. 2020), muscle wasting (Woerdeman & de Ronde 2011, von Haehling 2017), erectile dysfunction (Morgunov et al. 2007, Aversa et al. 2019), osteoporosis (Chen et al. 2019) and to treat breast cancer in women (Kono et al. 2016, Kono et al. 2017, Chen et al. 2020, Basaria et al. 2001, Shahidi 2001).
Both natural and synthetic androgens can act as anabolic\u2013androgenic steroids (AAS, commonly called anabolic steroids). AASs can contribute to increases in body weight, often as lean mass increases can see gains in muscular strength and performance enhancement. For these reasons, their use in sport has been banned because of the potential to gain unfair advantage in physical competitions (Sj\u00f6qvist et al. 2008, Kicman 2008).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q02790-1",
"Q15185-1"
],
"evidence": [
{
"id": "R-HSA-9705926",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705926"
}
]
},
{
"id": "R-HSA-9706837",
"name": "AR binds AR antagonists",
"equation": "",
"summary": "The actions of androgens on the androgen receptors(AR) can potentiate the growth and survival of prostate cancer cells. AR antagonist drugs can competitively inhibit androgens from binding to AR, inhibit AR nuclear translocation, as well as AR-mediated transcription which can all result in a decrease in prostate cancer cell proliferation and tumour size (Furr & Tucker 1996, Hodgson et al. 2007, Tran et al. 2009, Fizazi et al. 2018, Fizazi et al. 2015, Clegg et al. 2012). Androgens can also contribute to the development of androgen-dependent conditions such as acne and alopecia. Clascoterone blocks the effects of androgens that bind AR to treat these conditions (Rosette et al. 2019 , Herbert et al. 2020).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q02790-1",
"Q15185-1"
],
"evidence": [
{
"id": "R-HSA-9706837",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9706837"
}
]
},
{
"id": "R-HSA-9709547",
"name": "ESTG binds ESR2:chaperone complex",
"equation": "",
"summary": "In the nucleus, estrogens bind to estrogen receptors, members of the nuclear receptor superfamily. Human cells have 2 estrogen receptors, ER alpha and ER beta, encoded by two genes (ESR1 and ESR2 respectively). Expression of the two genes varies by tissue: both are expressed in the central nervous system, the cardiovascular system, the urogenital tract and in the breast and bone; ER alpha expression predominates in the uterus, mammary gland, and liver, and the gastrointestinal tract expresses only ER beta (Pearce and Jordan, 2004; Gustafsson et al, 1999; Pfaffl et al, 2001; reviewed in Bai and Gust, 2009). The receptors show 47% identity overall and share a common organization consisting of 6 domains: an N-terminal A/B domain with ligand-independent activation function, a C domain containing the 2 DNA-binding zinc fingers, a hinge region (D) with a nuclear localization signal, an E domain that contains the ligand binding and dimerization domains as well as a ligand-dependent transactivation function, and a C-terminal F domain of poorly characterized function. The DNA-binding domain is the most highly conserved (97% identity) while the ligand-bindind domain is more variable (47% identity) (reviewed in Ruff et al, 2000; Bai and Gust, 2009). ER alpha and beta can homo- and heterodimerize, and recognize a common estrogen-response element due to their shared DNA-binding domains (reviewed in Bai and Gust, 2009). Functional studies suggest that ER alpha and beta have overlapping but distinct roles in estrogen-responsive transcription (Harrington et al, 2003; Katzenellenbogen and Katzenellenbogen, 2000; Pearce and Jordan, 2004; Pfaffl et al, 2001)
In the unliganded state, estrogen receptors are part of a multi-subunit complex containing HSP90, p23 (also known as PTGES3) and other chaperone-associated proteins (Joab et al, 1984; Segnitz et al, 1995; Knoblauch et al, 1999; Bouhouche-Chatelier et al, 2001; Fliss et al, 2000; Oxelmart et al, 2006; reviewed in Smith and Toft, 2008; Bai and Gust, 2009). This complex is part of a chaperone binding and release cycle shared by many nuclear receptors (described in more detail in the pathway \\HSP90 chaperone cycle for steroid hormone receptors\\) that governs receptor folding and activity and may contribute to a high-affinity conformation of the ligand-binding domain (reviewed in Pratt and Toft, 1997; Smith and Toft, 2008). HSP90 release from the receptor complex requires ATP hydrolysis (Smith et al, 1993; Grenert et al, 1997; Panaretou et al, 1998; Obermann et al, 1998; Smith et al, 1992; reviewed in Smith and Toft, 2008).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q08752-1",
"P53041-1",
"P07900-1",
"Q02790-1",
"Q15185-1",
"Q13451-1"
],
"evidence": [
{
"id": "R-HSA-9709547",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9709547"
}
]
},
{
"id": "R-HSA-9709831",
"name": "HSP90 binds TBK1 and IRF3",
"equation": "",
"summary": "During viral infection, cytosolic viral RNA triggers activation of mitochondrial antiviral-signaling protein (MAVS) and the formation of MAVS signalosome (Kawai T et al. 2005; Seth RB et al. 2005; Xu LG et al. 2005). Activated MAVS recruits TANK-binding kinase 1 (TBK1), interferon regulatory factor 3 (IRF3) and IRF7 to the mitochondria leading to the activation of IRF3/IRF7 and subsequent production of type I interferons (Kawai T et al. 2005; Seth RB et al. 2005; Xu LG et al. 2005).
Co-immunoprecipitation assay showed that both TBK1 and IRF3 associated with heat shock protein 90kDa (HSP90), which facilitated signal transduction from TBK1 to IRF3 in Sendai virus (SeV)-infected human embryonic kidney (HEK293) cells (Yang K et l. 2006). MAVS, TBK1 and IRF3 were found to associate with mitochondrial import receptor subunit TOM70 (TOMM70) in HEK293 cells (Liu XY et al. 2010). TOMM70 localizes on the outer membrane of the mitochondria to mediate the translocation of mitochondrial protein precursors from the cytosol into the mitochondria (reviewed in Fan AC & Young JC 2011; Sokol AM et al. 2014; Kreimendahl S & Rassow J 2020). The molecular chaperone complexes of HSP90 and HSP70 were shown to deliver precursor proteins to TOMM70 for subsequent import (Young JC et al. 2003; Zanphorlin LM et al. 2016). The C-terminal motif (EEVD) of HSP90 was found to bind the N-terminal TPR clamp-type domain of TOMM70 (Liu XY et al. 2010; Gava LM et al. 2011). Knockdown of HSP90 by small interfering RNA (siRNA) decreased the association of TOMM70 with TBK1 and IRF3 in HEK293T cells (Liu XY et al. 2010). Further, in SeV-stimulated HEK293 cells, cytosolic BAX translocated to the mitochondrial outer membrane and induced apoptosis in the IRF3-dependent manner via the formation of the TOMM70:HSP90:IRF3:BAX protein complex (Wei B et al. 2015). The data suggest that HSP90 forms a complex with TBK1 and IRF3 in the cytosol and deliver them to the MAVS signalosome on the mitochondria.
Interaction between HSP90 and US11, a viral protein derived from human herpesvirus 1 (HHV-1, also known as herpes simplex virus 1, HSV-1) disrupted the formation of the HSP90:TBK1:IRF3 complex and induced degradation of TBK1 through a proteasome-dependent pathway in mouse embryonic fibroblasts (MEFs) (Liu X et al. 2018). ;", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P07900-1", "Q9UHD2-1" ], "evidence": [ { "id": "R-HSA-9709831", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9709831" } ] }, { "id": "R-HSA-9709852", "name": "MAVS:TOMM70 recruits HSP90:TBK1:IRF3", "equation": "", "summary": "Mitochondrial import receptor subunit TOM70 (TOMM70) recognizes mitochondrial protein precursors in the cytosol and mediates their translocation to the mitochondrial compartments (reviewed in Fan ACY & Young JC et al. 2011; Sokol AM et al. 2014; Kreimendahl S & Rassow J 2020). The molecular chaperone complexes of heat shock protein 90 kDa (HSP90) and HSP70 were shown to deliver precursor proteins to TOMM70 for subsequent import (Young JC et al. 2003; Zanphorlin LM et al. 2016). Mitochondrial import receptor subunit TOM20 (TOMM20) competes with HSC70 (HSPA8) and HSP90 for TOMM70 binding (Fan ACY et al. 2011).
During viral infection, cytosolic viral RNA triggers activation of mitochondrial antiviral-signaling protein (MAVS) and the formation of MAVS signalosome (Kawai T et al. 2005; Seth RB et al. 2005; Xu LG et al. 2005). MAVS localizes on the outer membrane of mitochondria through its C-terminal transmembrane (TM) domain. Activated MAVS recruits TANK-binding kinase 1 (TBK1) and interferon regulatory factor 3 (IRF3) to mitochondria leading to the activation of IRF3 and subsequent production of type I interferons. MAVS activates TBK1 in the TNF receptor-associated factors (TRAF)-dependent manner (Liu S et al. 2013; Fang R et al. 2017). Further, NF-kappa-B essential modulator (NEMO) links TBK1 to MAVS via TANK (Zhao T et al. 2007; Fang R et al. 2017).
Immunoprecipitation assays coupled to mass spectrometry analysis revealed that TOMM70 interacted with exogenously expressed MAVS in Sendai virus (SeV)-stimulated human embryonic kidney (HEK293) cells (Liu XY et al. 2010). The TM domains of both MAVS and TOMM70 were required for their interaction. In addition, TOMM70 interacted strongly with the C-terminal motif (EEVD) of HSP90 (Liu XY et al. 2010; Gava LM et al. 2011). TOMM70 also co-immunoprecipitated with TBK1 and IRF3 in HEK293 cells (Liu XY et al. 2010). Further, both TBK1 and IRF3 associated with HSP90, which facilitated signal transduction from TBK1 to IRF3 in SeV-infected HEK293 cells (Yang K et l. 2006). Moreover, SeV infection enhanced the interaction between IRF3 and apoptosis regulator BAX (BAX) in HEK293T cells (Wei B et al. 2015). In SeV-stimulated HEK293 cells, cytosolic BAX translocated to the mitochondrial outer membrane and induced apoptosis in the IRF3-dependent manner via the formation of the TOMM70:HSP90:IRF3:BAX protein complex (Wei B et al. 2015). Knockdown of HSP90 by small interfering RNA (siRNA) decreased the association of TOMM70 with TBK1 and IRF3 (Liu XY et al. 2010). Overexpression of TOMM70 enhanced mRNA levels of IRF3-responsive genes (including IFNB, IFIT1 and RANTES) in HEK293 cells during SeV infection or poly(I:C) stimulation, whereas knockdown of TOMM70 by siRNA showed an inhibitory effect. Similar results were obtained in murine bone marrow-derived macrophages (BMDM) and bone marrow-derived dendritic cells (BMDC) (Liu XY et al. 2010). Thus, the association of MAVS with TOMM70 is thought to potentiate the HSP90-mediated recruitment of TBK1and IRF3 to mitochondria during viral infection thereby inducing IRF3-mediated host antiviral responses.
SARS-CoV-2 9b interaction with TOMM70 inhibits binding of HSP90 to TOMM70 (Jiang HW et al. 2020).",
"cellular_location": "cytosol, mitochondrial outer membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q9UHD2-1"
],
"evidence": [
{
"id": "R-HSA-9709852",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9709852"
}
]
},
{
"id": "R-HSA-9716913",
"name": "ESR1 binds ESR1 antagonists",
"equation": "",
"summary": "Estrogen receptor alpha (ER\u03b1, NR3A1, nuclear receptor subfamily 3 group A member 1), encoded by the ESR1 gene, is a nuclear hormone receptor that is activated by the sex hormone estrogen. ESR1 can mediate the physiological development and function of various organ systems, including the reproductive, central nervous, skeletal, and cardiovascular systems (Kassem 1997). Accordingly, ESR1 is widely expressed throughout the body.
Antiestrogens (aka estrogen antagonists or estrogen blockers) are a class of drugs which prevent endogenous estrogens like estradiol from mediating their biological effects in the body. They act by blocking the estrogen receptor (selective estrogen receptor modulators (SERMs)) or inhibiting/suppressing estrogen production (selective estrogen receptor downregulators (SERDs)) (Kuiper et al. 1997, Sasson 1991, Fan et al. 2007). SERMs include tamoxifen (Wang et al. 2004), clomifene (Kurosawa et al. 2010), bazedoxifene (Toniti et al. 2011) and raloxifene (Schafer et al. 1999), and a SERD drug is fulvestrant (Schmidt et al. 2003).
Bazedoxifene is used in the treatment of moderate to severe vasomotor symptoms associated with menopause and for postmenopausal osteoporosis (Genant 2011, Rossini et al. 2013). Fulvestrant used to treat hormone receptor (HR)-positive metastatic breast cancer in postmenopausal women (Lee et al. 2017, Lei et al. 2020).; Clomiphene, is a medication used to treat infertility in women who do not ovulate, including those with polycystic ovary syndrome (Hughes et al. 2010). Raloxifene medication used to prevent and treat osteoporosis in postmenopausal women and those on glucocorticoids. It is also used to reduce the risk of breast cancer in those at high risk (Scott et al. 1999). Tamoxifen is used for the treatment of both early and advanced estrogen receptor-positive (ER-positive or ER+) breast cancer in pre- and postmenopausal women (Jordan 2021). Tamoxifen is also used for ovulation induction to treat infertility in women with anovulatory disorders.;",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q08752-1",
"P53041-1",
"P07900-1",
"Q02790-1",
"Q15185-1",
"Q13451-1"
],
"evidence": [
{
"id": "R-HSA-9716913",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9716913"
}
]
},
{
"id": "R-HSA-9716947",
"name": "ESR1 binds ESR1 agonists",
"equation": "",
"summary": "Estrogen receptor alpha (ER\u03b1, NR3A1, nuclear receptor subfamily 3 group A member 1), encoded by the ESR1 gene, is a nuclear hormone receptor that is activated by the sex hormone estrogen. ESR1 can mediate the physiological development and function of various organ systems, including the reproductive, central nervous, skeletal, and cardiovascular systems. Accordingly, ESR1 is widely expressed throughout the body.
Synthetic nonsteroidal estrogen agonists are used to treat a variety of gynecological disorders (Stauffer et al. 2000, Sasson 1991, Kuiper et al. 1997). Diethylstilbestrol was previously used in the prevention of miscarriage or premature delivery but later only used in the treatment of prostate or breast cancer. Ethinylestradiol, when combined with progestins, is mainly used as a contraceptive and for certain menopausal conditions.
Tamoxifen has mixed estrogenic and antiestrogenic activity, dependent on tissue type. For instance, tamoxifen has predominantly antiestrogenic effects in breast tissue (Wang et al. 2004) but predominantly estrogenic effects in the uterus and liver. Tamoxifen was indicated to treat estrogen receptor positive metastatic breast cancer in adults but has since been superceded by aromatase inhibitors such as anastrozole (Howell et al. 2005). A beneficial side effect of tamoxifen is that it prevents osteoporosis by acting as an agonist in bone cells (Kassem 1997). Tibolone is an estrogen receptor agonist with a preference for ESR1 (Escande et al. 2009). It is indicated for the relief of post-menopausal symptoms and for the prevention of osteoporosis.",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q08752-1",
"P53041-1",
"P07900-1",
"Q02790-1",
"Q15185-1",
"Q13451-1"
],
"evidence": [
{
"id": "R-HSA-9716947",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9716947"
}
]
},
{
"id": "R-HSA-9725855",
"name": "NR3C2 binds NR3C2 antagonists",
"equation": "",
"summary": "The mineralocorticoid receptor (Nuclear receptor subfamily 3 group C member 2, NR3C2) is a receptor with equal affinity for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. NR3C2 is expressed in many tissues such as kidney, heart, the CNS and sweat glands. Its activation leads to the expression of proteins regulating ionic and water transport resulting in the reabsorption of sodium. Consequently, there is an increase in extracellular volume, an increase in blood pressure, and increased excretion of potassium to maintain normal salt concentrations.
Synthetic NR3C2 antagonists competitively inhibit NR3C2 (Kagawa et al. 1957, Pollow et al. 1992, Rupprecht et al. 1993) in the kidney distal convoluted tubule to promote sodium and water excretion and potassium retention. These diuretic drugs are typically indicated for congestive heart failure, hypertension and chronic kidney disease. Synthetic antagonists of NR3C2 include the steroidal compounds spironolactone, eplerenone, and drospirenone. Nimodipine, a calcium channel blocker, can also act as an NR3C2 antagonist (Dietz et al. 2008, Luther 2014).
The broad clinical use of steroidal mineralocorticoid receptor antagonists is limited by the potential risk of inducing hyperkalemia. Novel, non-steroidal NR3C2 antagonists demonstrate an improved therapeutic index for hyperkalemic risk compared to their steroidal counterparts in preclinical models (reviews Kolkhof et al. 2015, Kolkhof & B\u00e4rfacker 2017, Sueta et al. 2020). Compounds undergoing clinical trials include apararenone (no trial data), esaxerenone (Arai et al. 2015), and finerenone (B\u00e4rfacker et al. 2012, Amazit et al. 2015).",
"cellular_location": "cytosol, extracellular region",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q02790-1",
"Q15185-1"
],
"evidence": [
{
"id": "R-HSA-9725855",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9725855"
}
]
},
{
"id": "R-HSA-9725885",
"name": "P4 bind PGR (in the HSP90 chaperone complex)",
"equation": "",
"summary": "Steroid hormones receptors (SHRs) are intracellular transcription factors that can be activated by binding specific ligands (i.e., steroid hormones (SH)) to the ligand-binding domain (LBD) (Ray DW et AL. 1999; Pike AC et al. 1999; Bledsoe RK et al. 2002; Li Y et al. 2005; Kumar R and McEwan IJ 2012; Kumar R et al. 2011; Williams SP & Sigler PB 1998; Tanenbaum DM et al. 1998; Lusher SJ et al. 2012). LBD (E-region) resides in the C-terminal half of the receptor and in addition to ligand binding function contains a transcriptional activation function (AF2), sequences for dimerization, heat shock protein association, intermolecular silencing and intramolecular repression (Kumar R and McEwan IJ 2012). The binding of hormone acts as an allosteric switch to regulate SHR-DNA and SHR-protein interactions, including interdomain interactions and/or dimerization (Kumar R and McEwan IJ 2012).
SHs are synthesized from cholesterol in the adrenal cortex (glucocorticoids, mineralocorticoids, and adrenal androgens), the testes (testicular androgens, estrogen), and the ovary and placenta (estrogen and progestogen or progestins) (Payne AH & Hales DB 2004; Hu J et al. 2010;). SHs reach their target cells via the blood, where they are bound to specific carrier proteins (Grishkovskaya I et al. 2000; Hammond GL 2016). SHs detach from the carrier proteins and because of their lipophilic nature readily diffuse through the plasma membrane of cells (Oren I et al. 2004). Within the target cells SHs bind to steroid hormone receptors (SHRs) which are present in a heterocomplex with heat shock protein HSP90 and co-chaperones (e.g., immunophilins p23) (Echeverria PC & Picard D 2010). The ATP-bound form of HSP90 and chaperone-mediated conformational changes are required to keep SHRs in a ligand binding-competent state (McLaughlin SH et al. 2002; Pratt WB et al. 2008; Krukenberg KA et al. 2011).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q02790-1",
"Q15185-1"
],
"evidence": [
{
"id": "R-HSA-9725885",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9725885"
}
]
},
{
"id": "R-HSA-9726509",
"name": "NR3C2 binds fludrocortisone",
"equation": "",
"summary": "Fludrocortisone is a synthetic mineralocorticoid used in conjunction with hydrocortisone to replace missing endogenous corticosteroids in patients with adrenal insufficiency. It is functionally similar to aldosterone, the body's primary endogenous mineralocorticoid, and is structurally analogous to cortisol, differing only by a fluorine atom at the 9-position of the steroid structure and having similar affinity for the mineralocorticoid receptor (NR3C2) as aldosterone (Rupprecht et al. 1993, Oelkers et al. 1994).
Fludrocortisone is indicated as partial replacement therapy for primary or secondary adrenocortical insufficiency in Addison's disease and for the treatment of salt-losing androgenital syndrome (Charmandari et al. 2014, Hamitouche et al. 2017). Fludrocortisone has also shown to be effective in the treatment of cerebral salt-wasting syndrome (Taplin et al. 2006, Misra et al. 2018). Common side effects of fludrocortisone include high blood pressure, swelling, heart failure, and low blood potassium.",
"cellular_location": "cytosol, extracellular region",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q02790-1",
"Q15185-1"
],
"evidence": [
{
"id": "R-HSA-9726509",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9726509"
}
]
},
{
"id": "R-HSA-9726580",
"name": "PGR binds PGR agonists",
"equation": "",
"summary": "The actions of progesterone, a critical regulator of normal female reproductive function in the uterus, the ovary, the mammary gland and the brain, are mediated via the progesterone receptor (PGR). PGR agonists (Schindler et al. 2003, Kuhl 2005) are primarily used for birth control and as a part of menopausal hormone therapy and for the treatment of gynecological disorders. PGR agonists include the retroprogesterone dydrogestrone (Ri\u017ener et al. 2011), the 17alpha-hydroxyprogesterone derivative medroxyprogesterone (Zhi et al. 1998), and the 19-nortestosterone derivatives norethisterone (Edwards et al. 1998) and levonorgestrel (Bergink et al. 1983).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q02790-1",
"Q15185-1"
],
"evidence": [
{
"id": "R-HSA-9726580",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9726580"
}
]
},
{
"id": "R-HSA-9726621",
"name": "PGR binds PGR antagonists",
"equation": "",
"summary": "The actions of progesterone, a critical regulator of normal female reproductive function in the uterus, the ovary, the mammary gland and the brain, are mediated via the progesterone receptor (PGR). The PGR antagonists mifepristone and ulipristal acetate are indicated for the medical abortion of pregnancy and as an emergency contraceptive, respectively. They both work by preventing the effects of progesterone on PGR (Zhi et al. 2003, Lusher et al. 2012, Rewinkel et al. 2008).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1",
"Q02790-1",
"Q15185-1"
],
"evidence": [
{
"id": "R-HSA-9726621",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9726621"
}
]
},
{
"id": "R-HSA-9834736",
"name": "Synthesis of antigenomic RNA of human respiratory syncytial virus",
"equation": "",
"summary": "After the primary round of transcription, accumulation of the M2-2 protein leads to a rearrangement of the ribonucleocapsid of the human respiratory syncytial virus (RSV), likely through direct interaction of M2-2 with the ribonucleocapid (Blanchard et al. 2020). M2-2 promotes the switch from transcription of viral genes to replication of the viral genome for virion assembly (Bermingham et and Collins 1999) through M2-2-mediated structural rearrangement of the nucleocapsid (Blanchard et al. 2020). M2-2 does not interfere with the secondary round of transcription. The mechanism of M2-2 action has not been elucidated (Blanchard et al. 2020). The level of M2-2 expression has to be tightly regulated as overexpression of M2-2 inhibits replication (Cheng et al. 2005). RSV lacking M2-2 grows less efficiently, with reduced production of genomic RNA and increased production of viral proteins (Bermingham and Collins 1999).
The replication of the RSV negative sense single stranded RNA genome proceeds through synthesis of a positive sense RNA genome intermediate, also known as antigenomic RNA. Antigenomic RNA is produced at very low levels (Blanchard et al. 2020).
A cis element in the first 11 nucleotides of the 44 nucleotide-long leader region at the 3' terminus of the negative sense RSV genome is needed for the initiation of the replication. Nucleotides 16-34 of the leader region are needed for production of the full-length positive-sense RSV antigenome and encapsidation of the antigenome, which happens concurrently with replication (McGivern et al. 2005).
M2-1 acts as a transcription processivity factor and its function depends on the Cys3-His1 motif consisting of 3 conserved cysteine residues C7, C15, and C21, and one conserved histidine residue, H25 (Tang et al. 2001).
The RNA-dependent RNA polymerase (RdRP) complex of RSV starts the replication of viral RNA by incorporating the correct first nucleotide (ATP) independently of the template allowing highly accurate initiation of replication (Noton et al. 2010).
Replication of RSV is positively regulated by the heat shock protein, HSP90, which has been shown to bind directly to the viral L polymerase (Geller et al. 2013; Munday et al. 2015).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [
"R-RSY-9834740"
],
"enzyme_list": [
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9834736",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9834736"
}
]
},
{
"id": "R-HSA-9835171",
"name": "Budding of hRSV A virions from infected cell",
"equation": "",
"summary": "Based on mass spectroscopy of purified viral particles of human respiratory syncytial virus (RSV) A2, the ratio of fusion protein F to nucleocapsid protein N is ~3:4, while the ratio of mature glycoprotein G to F protein is ~1:30. This low G to F ratio could, however, be due to the hydrophobic nature of the G protein, which makes its recovery difficult, as well its heavy glycosylation, which interferes with peptide identification by mass spectroscopy (Radhakrishnan et al. 2010). In the same study, the SH protein was not detected, which may also have been a consequence of SH being highly hydrophobic.
In this reaction, we are showing SH protein in ~1:1 ratio with the G protein. Based on the curatorial estimation that viral genomic RNA is packaged around 209 oligomeric rings of N protein, of which 129 are N decamers (10 N subunits) and 80 are N hendecamers (11 N subunits), and taking into considerations the experimentally determined length of RSV genomic RNA (Bose et al. 2015), number of genomic RNA nucleotides bound by each N subunit (Tawar et al. 2009), and the ratio of N decamers to N hendecamers in RSV nucleocapsids (Tran et al. 2007), the total number of N proteins in a viral nucleocapsid is expected to be 2170. As the F protein forms trimers, and SH protein forms pentamers, we are showing that 542 F trimers, 54 G proteins, and 10 SH protein pentamers become embedded in the virion membrane.
Budding virions are observed as viral filaments at the plasma membrane of infected cells. Viral filaments are connected with cytoplasmic inclusion bodies where the virion assembly occurs. Viral nucleocapsids appear as strands along the length of viral filaments, with some viral filaments containing more than one viral nucleocapsid (Radhakrishnan et al. 2010; Liljeroos et al. 2013; Conley et al. 2022).
Based on cryogenic electron microscopy (cryoEM) and cryogenic electron tomography (cryoET), glycoproteins that stud the viral envelope are clustered in pairs and helically ordered; an organization that is coordinated by the M protein lattice (Conley et al. 2022; Liljeroos et al. 2013; Sibert et al. 2021).
The cortical actin network takes part in formation of viral filaments. In particular, the association of beta-actin (ACTB), filamin-1 (FLNA), and cofilin-1(CFL1) with viral filaments has been confirmed (Radhakrishnan et al. 2010, Huong et al. 2016). HSP90A is needed for formation of mature virions and both isoforms of HSP90A (HSP90AA1, and HSP90AB1) can be found as components of viral filaments (Radhakrishnan et al. 2010).;",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07900-1"
],
"evidence": [
{
"id": "R-HSA-9835171",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9835171"
}
]
}
],
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"id": "P00533",
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"url": "https://www.uniprot.org/uniprot/P00533"
}
]
},
{
"ec_number": "2.7.10.1",
"activity": "",
"evidence": [
{
"id": "P00533",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P00533"
}
]
}
]
},
{
"uniprot_ac": "P00746",
"gene_name": "CFD",
"activity": [
{
"ec_number": "3.4.21.46",
"activity": "Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor.",
"evidence": [
{
"id": "P00746",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P00746"
}
]
},
{
"ec_number": "3.4.21.46",
"activity": "",
"evidence": [
{
"id": "P00746",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P00746"
}
]
}
]
},
{
"uniprot_ac": "P01111",
"gene_name": "NRAS",
"activity": [
{
"ec_number": "3.6.5.2",
"activity": "GTP + H2O = GDP + H(+) + phosphate.",
"evidence": [
{
"id": "P01111",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P01111"
}
]
},
{
"ec_number": "3.6.5.2",
"activity": "",
"evidence": [
{
"id": "P01111",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P01111"
}
]
}
]
},
{
"uniprot_ac": "P01112",
"gene_name": "HRAS",
"activity": [
{
"ec_number": "3.6.5.2",
"activity": "GTP + H2O = GDP + H(+) + phosphate.",
"evidence": [
{
"id": "P01112",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P01112"
}
]
},
{
"ec_number": "3.6.5.2",
"activity": "",
"evidence": [
{
"id": "P01112",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P01112"
}
]
}
]
},
{
"uniprot_ac": "P02572",
"gene_name": "Act42A",
"activity": [
{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "P02572",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P02572"
}
]
}
]
},
{
"uniprot_ac": "P02574",
"gene_name": "Act79B",
"activity": [
{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "P02574",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P02574"
}
]
}
]
},
{
"uniprot_ac": "P02794",
"gene_name": "FTH1",
"activity": [
{
"ec_number": "1.16.3.1",
"activity": "4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O.",
"evidence": [
{
"id": "P02794",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P02794"
}
]
},
{
"ec_number": "1.16.3.1",
"activity": "",
"evidence": [
{
"id": "P02794",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P02794"
}
]
}
]
},
{
"uniprot_ac": "P04040",
"gene_name": "CAT",
"activity": [
{
"ec_number": "1.11.1.6",
"activity": "2 H2O2 = 2 H2O + O2.",
"evidence": [
{
"id": "P04040",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P04040"
}
]
},
{
"ec_number": "1.11.1.6",
"activity": "",
"evidence": [
{
"id": "P04040",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P04040"
}
]
}
]
},
{
"uniprot_ac": "P04075",
"gene_name": "ALDOA",
"activity": [
{
"ec_number": "4.1.2.13",
"activity": "beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate.",
"evidence": [
{
"id": "P04075",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P04075"
}
]
},
{
"ec_number": "4.1.2.13",
"activity": "",
"evidence": [
{
"id": "P04075",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P04075"
}
]
}
]
},
{
"uniprot_ac": "P04626",
"gene_name": "ERBB2",
"activity": [
{
"ec_number": "2.7.10.1",
"activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].",
"evidence": [
{
"id": "P04626",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P04626"
}
]
},
{
"ec_number": "2.7.10.1",
"activity": "",
"evidence": [
{
"id": "P04626",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P04626"
}
]
}
]
},
{
"uniprot_ac": "P05186",
"gene_name": "ALPL",
"activity": [
{
"ec_number": "3.1.3.1",
"activity": "a phosphate monoester + H2O = an alcohol + phosphate.",
"evidence": [
{
"id": "P05186",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P05186"
}
]
},
{
"ec_number": "3.9.1.1",
"activity": "H2O + N-phosphocreatine = creatine + phosphate.",
"evidence": [
{
"id": "P05186",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P05186"
}
]
},
{
"ec_number": "3.1.3.1",
"activity": "",
"evidence": [
{
"id": "P05186",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P05186"
}
]
},
{
"ec_number": "3.9.1.1",
"activity": "",
"evidence": [
{
"id": "P05186",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P05186"
}
]
}
]
},
{
"uniprot_ac": "P06493",
"gene_name": "CDK1",
"activity": [
{
"ec_number": "2.7.11.22",
"activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].",
"evidence": [
{
"id": "P06493",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06493"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase].",
"evidence": [
{
"id": "P06493",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06493"
}
]
},
{
"ec_number": "2.7.11.22",
"activity": "",
"evidence": [
{
"id": "P06493",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06493"
}
]
},
{
"ec_number": "2.7.11.23",
"activity": "",
"evidence": [
{
"id": "P06493",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06493"
}
]
}
]
},
{
"uniprot_ac": "P06634",
"gene_name": "DED1",
"activity": [
{
"ec_number": "3.6.4.13",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
"evidence": [
{
"id": "P06634",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06634"
}
]
},
{
"ec_number": "3.6.4.13",
"activity": "",
"evidence": [
{
"id": "P06634",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06634"
}
]
}
]
},
{
"uniprot_ac": "P06737",
"gene_name": "PYGL",
"activity": [
{
"ec_number": "2.4.1.1",
"activity": "[(1->4)-alpha-D-glucosyl](n) + phosphate = [(1->4)-alpha-D-glucosyl](n-1) + alpha-D-glucose 1-phosphate.",
"evidence": [
{
"id": "P06737",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06737"
}
]
},
{
"ec_number": "2.4.1.1",
"activity": "",
"evidence": [
{
"id": "P06737",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06737"
}
]
}
]
},
{
"uniprot_ac": "P06744",
"gene_name": "GPI",
"activity": [
{
"ec_number": "5.3.1.9",
"activity": "alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate.",
"evidence": [
{
"id": "P06744",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06744"
}
]
},
{
"ec_number": "5.3.1.9",
"activity": "",
"evidence": [
{
"id": "P06744",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06744"
}
]
}
]
},
{
"uniprot_ac": "P06761",
"gene_name": "Hspa5",
"activity": [
{
"ec_number": "3.6.4.10",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
"evidence": [
{
"id": "P06761",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06761"
}
]
},
{
"ec_number": "3.6.4.10",
"activity": "",
"evidence": [
{
"id": "P06761",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06761"
}
]
}
]
},
{
"uniprot_ac": "P06839",
"gene_name": "RAD3",
"activity": [
{
"ec_number": "3.6.4.12",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
"evidence": [
{
"id": "P06839",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06839"
}
]
},
{
"ec_number": "3.6.4.12",
"activity": "",
"evidence": [
{
"id": "P06839",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06839"
}
]
}
]
},
{
"uniprot_ac": "P07271",
"gene_name": "PIF1",
"activity": [
{
"ec_number": "3.6.4.12",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
"evidence": [
{
"id": "P07271",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07271"
}
]
},
{
"ec_number": "3.6.4.12",
"activity": "",
"evidence": [
{
"id": "P07271",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07271"
}
]
}
]
},
{
"uniprot_ac": "P07339",
"gene_name": "CTSD",
"activity": [
{
"ec_number": "3.4.23.5",
"activity": "Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.",
"evidence": [
{
"id": "P07339",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07339"
}
]
},
{
"ec_number": "3.4.23.5",
"activity": "",
"evidence": [
{
"id": "P07339",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07339"
}
]
}
]
},
{
"uniprot_ac": "P07384",
"gene_name": "CAPN1",
"activity": [
{
"ec_number": "3.4.22.52",
"activity": "Broad endopeptidase specificity.",
"evidence": [
{
"id": "P07384",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07384"
}
]
},
{
"ec_number": "3.4.22.52",
"activity": "",
"evidence": [
{
"id": "P07384",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07384"
}
]
}
]
},
{
"uniprot_ac": "P07741",
"gene_name": "APRT",
"activity": [
{
"ec_number": "2.4.2.7",
"activity": "AMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + adenine.",
"evidence": [
{
"id": "P07741",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07741"
}
]
},
{
"ec_number": "2.4.2.7",
"activity": "",
"evidence": [
{
"id": "P07741",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07741"
}
]
}
]
},
{
"uniprot_ac": "P07828",
"gene_name": "act18",
"activity": [
{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "P07828",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07828"
}
]
}
]
},
{
"uniprot_ac": "P07829",
"gene_name": "act3",
"activity": [
{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "P07829",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07829"
}
]
}
]
},
{
"uniprot_ac": "P07830",
"gene_name": "act19",
"activity": [
{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "P07830",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07830"
}
]
}
]
},
{
"uniprot_ac": "P07858",
"gene_name": "CTSB",
"activity": [
{
"ec_number": "3.4.22.1",
"activity": "Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.",
"evidence": [
{
"id": "P07858",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07858"
}
]
},
{
"ec_number": "3.4.22.1",
"activity": "",
"evidence": [
{
"id": "P07858",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07858"
}
]
}
]
},
{
"uniprot_ac": "P07900",
"gene_name": "HSP90AA1",
"activity": [
{
"ec_number": "3.6.4.10",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
"evidence": [
{
"id": "P07900",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07900"
}
]
},
{
"ec_number": "3.6.4.10",
"activity": "",
"evidence": [
{
"id": "P07900",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07900"
}
]
}
]
},
{
"uniprot_ac": "P07901",
"gene_name": "Hsp90aa1",
"activity": [
{
"ec_number": "3.6.4.10",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
"evidence": [
{
"id": "P07901",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07901"
}
]
},
{
"ec_number": "3.6.4.10",
"activity": "",
"evidence": [
{
"id": "P07901",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07901"
}
]
}
]
},
{
"uniprot_ac": "P07998",
"gene_name": "RNASE1",
"activity": [
{
"ec_number": "4.6.1.18",
"activity": "an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].",
"evidence": [
{
"id": "P07998",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07998"
}
]
},
{
"ec_number": "4.6.1.18",
"activity": "",
"evidence": [
{
"id": "P07998",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P07998"
}
]
}
]
},
{
"uniprot_ac": "P08236",
"gene_name": "GUSB",
"activity": [
{
"ec_number": "3.2.1.31",
"activity": "a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate.",
"evidence": [
{
"id": "P08236",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P08236"
}
]
},
{
"ec_number": "3.2.1.31",
"activity": "",
"evidence": [
{
"id": "P08236",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P08236"
}
]
}
]
},
{
"uniprot_ac": "P08289",
"gene_name": "Alpl",
"activity": [
{
"ec_number": "3.1.3.1",
"activity": "a phosphate monoester + H2O = an alcohol + phosphate.",
"evidence": [
{
"id": "P08289",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P08289"
}
]
},
{
"ec_number": "3.9.1.1",
"activity": "H2O + N-phosphocreatine = creatine + phosphate.",
"evidence": [
{
"id": "P08289",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P08289"
}
]
},
{
"ec_number": "3.1.3.1",
"activity": "",
"evidence": [
{
"id": "P08289",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P08289"
}
]
}
]
},
{
"uniprot_ac": "P09052",
"gene_name": "vas",
"activity": [
{
"ec_number": "3.6.4.13",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
"evidence": [
{
"id": "P09052",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09052"
}
]
},
{
"ec_number": "3.6.4.13",
"activity": "",
"evidence": [
{
"id": "P09052",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09052"
}
]
}
]
},
{
"uniprot_ac": "P09211",
"gene_name": "GSTP1",
"activity": [
{
"ec_number": "2.5.1.18",
"activity": "glutathione + RX = a halide anion + an S-substituted glutathione + H(+).",
"evidence": [
{
"id": "P09211",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09211"
}
]
},
{
"ec_number": "2.5.1.18",
"activity": "",
"evidence": [
{
"id": "P09211",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09211"
}
]
}
]
},
{
"uniprot_ac": "P09242",
"gene_name": "Alpl",
"activity": [
{
"ec_number": "3.1.3.1",
"activity": "a phosphate monoester + H2O = an alcohol + phosphate.",
"evidence": [
{
"id": "P09242",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09242"
}
]
},
{
"ec_number": "3.9.1.1",
"activity": "H2O + N-phosphocreatine = creatine + phosphate.",
"evidence": [
{
"id": "P09242",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09242"
}
]
},
{
"ec_number": "3.1.3.1",
"activity": "",
"evidence": [
{
"id": "P09242",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09242"
}
]
},
{
"ec_number": "3.9.1.1",
"activity": "",
"evidence": [
{
"id": "P09242",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09242"
}
]
}
]
},
{
"uniprot_ac": "P09769",
"gene_name": "FGR",
"activity": [
{
"ec_number": "2.7.10.2",
"activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].",
"evidence": [
{
"id": "P09769",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09769"
}
]
},
{
"ec_number": "2.7.10.2",
"activity": "",
"evidence": [
{
"id": "P09769",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P09769"
}
]
}
]
},
{
"uniprot_ac": "P09917",
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{
"ec_number": "1.13.11.-",
"activity": "",
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{
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}
]
},
{
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"activity": "(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = H2O + leukotriene A4.",
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{
"id": "P09917",
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}
]
}
]
},
{
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{
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}
]
},
{
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{
"id": "P09960",
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}
]
},
{
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{
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}
]
}
]
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{
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{
"ec_number": "4.1.2.13",
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{
"id": "P09972",
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}
]
},
{
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"activity": "",
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{
"id": "P09972",
"database": "UniProtKB",
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}
]
}
]
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{
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{
"ec_number": "3.6.4.10",
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"id": "P0CS90",
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}
]
},
{
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"activity": "",
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{
"id": "P0CS90",
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}
]
}
]
},
{
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{
"ec_number": "3.6.4.12",
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"database": "UniProtKB",
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}
]
},
{
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"activity": "",
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{
"id": "P0CX14",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
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}
]
},
{
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{
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"database": "UniProtKB",
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}
]
}
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},
{
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{
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"id": "P0CX20",
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}
]
},
{
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"activity": "",
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{
"id": "P0CX20",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "3.6.4.12",
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{
"id": "P0CX21",
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}
]
},
{
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"activity": "",
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{
"id": "P0CX21",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "3.6.4.12",
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{
"id": "P0CX22",
"database": "UniProtKB",
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}
]
},
{
"ec_number": "3.6.4.12",
"activity": "",
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{
"id": "P0CX22",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "3.6.5.-",
"activity": "",
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{
"id": "P0DPH7",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "3.6.5.-",
"activity": "",
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{
"id": "P0DPH8",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "3.6.4.13",
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{
"id": "P10081",
"database": "UniProtKB",
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}
]
},
{
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{
"id": "P10081",
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}
]
}
]
},
{
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{
"ec_number": "3.6.4.13",
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{
"id": "P10630",
"database": "UniProtKB",
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}
]
},
{
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{
"id": "P10630",
"database": "UniProtKB",
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]
}
]
},
{
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{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "P10981",
"database": "UniProtKB",
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}
]
}
]
},
{
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"gene_name": "Act5C",
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{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "P10987",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "3.6.4.10",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
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{
"id": "P11021",
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}
]
},
{
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{
"id": "P11021",
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}
]
}
]
},
{
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{
"ec_number": "3.6.4.10",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
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{
"id": "P11142",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P11142"
}
]
},
{
"ec_number": "3.6.4.10",
"activity": "",
"evidence": [
{
"id": "P11142",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "3.6.4.10",
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{
"id": "P11484",
"database": "UniProtKB",
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}
]
},
{
"ec_number": "3.6.4.10",
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{
"id": "P11484",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "1.11.1.7",
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{
"id": "P11678",
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}
]
},
{
"ec_number": "1.11.1.7",
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{
"id": "P11678",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "1.1.1.205",
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{
"id": "P12268",
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"url": "https://www.uniprot.org/uniprot/P12268"
}
]
},
{
"ec_number": "1.1.1.205",
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{
"id": "P12268",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P12268"
}
]
}
]
},
{
"uniprot_ac": "P12954",
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{
"ec_number": "5.6.2.4",
"activity": "Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.",
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{
"id": "P12954",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P12954"
}
]
},
{
"ec_number": "5.6.2.4",
"activity": "",
"evidence": [
{
"id": "P12954",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P12954"
}
]
}
]
},
{
"uniprot_ac": "P12956",
"gene_name": "XRCC6",
"activity": [
{
"ec_number": "4.2.99.-",
"activity": "",
"evidence": [
{
"id": "P12956",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P12956"
}
]
},
{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "P12956",
"database": "UniProtKB",
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}
]
}
]
},
{
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{
"ec_number": "3.6.4.-",
"activity": "",
"evidence": [
{
"id": "P13010",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P13010"
}
]
}
]
},
{
"uniprot_ac": "P13569",
"gene_name": "CFTR",
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{
"ec_number": "5.6.1.6",
"activity": "ATP + H2O + closed Cl(-) channel = ADP + phosphate + open Cl(-) channel.",
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{
"id": "P13569",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P13569"
}
]
},
{
"ec_number": "5.6.1.6",
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"evidence": [
{
"id": "P13569",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P13569"
}
]
}
]
},
{
"uniprot_ac": "P13639",
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{
"ec_number": "3.6.5.-",
"activity": "",
"evidence": [
{
"id": "P13639",
"database": "UniProtKB",
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}
]
}
]
},
{
"uniprot_ac": "P13716",
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{
"ec_number": "4.2.1.24",
"activity": "2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen.",
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{
"id": "P13716",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P13716"
}
]
},
{
"ec_number": "4.2.1.24",
"activity": "",
"evidence": [
{
"id": "P13716",
"database": "UniProtKB",
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}
]
}
]
},
{
"uniprot_ac": "P13798",
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{
"ec_number": "3.4.19.1",
"activity": "Internal cleavage of oxidized and glycated proteins.",
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{
"id": "P13798",
"database": "UniProtKB",
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}
]
},
{
"ec_number": "3.4.19.1",
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{
"id": "P13798",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P13798"
}
]
}
]
},
{
"uniprot_ac": "P14174",
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{
"ec_number": "5.3.2.1",
"activity": "3-phenylpyruvate = enol-phenylpyruvate.",
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{
"id": "P14174",
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}
]
},
{
"ec_number": "5.3.3.12",
"activity": "L-dopachrome = 5,6-dihydroxyindole-2-carboxylate.",
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{
"id": "P14174",
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}
]
},
{
"ec_number": "5.3.2.1",
"activity": "",
"evidence": [
{
"id": "P14174",
"database": "UniProtKB",
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]
}
]
},
{
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{
"ec_number": "2.7.1.40",
"activity": "CTP + pyruvate = CDP + H(+) + phosphoenolpyruvate.",
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{
"id": "P14618",
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"url": "https://www.uniprot.org/uniprot/P14618"
}
]
},
{
"ec_number": "2.7.1.40",
"activity": "",
"evidence": [
{
"id": "P14618",
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}
]
},
{
"ec_number": "2.7.10.2",
"activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].",
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{
"id": "P14618",
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"url": "https://www.uniprot.org/uniprot/P14618"
}
]
},
{
"ec_number": "2.7.11.1",
"activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].",
"evidence": [
{
"id": "P14618",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P14618"
}
]
}
]
},
{
"uniprot_ac": "P14780",
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{
"ec_number": "3.4.24.35",
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{
"id": "P14780",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P14780"
}
]
},
{
"ec_number": "3.4.24.35",
"activity": "",
"evidence": [
{
"id": "P14780",
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}
]
}
]
},
{
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{
"ec_number": "3.6.4.13",
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{
"id": "P15424",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P15424"
}
]
},
{
"ec_number": "3.6.4.13",
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"evidence": [
{
"id": "P15424",
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}
]
}
]
},
{
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{
"ec_number": "3.1.6.14",
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{
"id": "P15586",
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]
},
{
"ec_number": "3.1.6.14",
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{
"id": "P15586",
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]
}
]
},
{
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{
"ec_number": "3.1.6.12",
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{
"id": "P15848",
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]
},
{
"ec_number": "3.1.6.12",
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{
"id": "P15848",
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]
}
]
},
{
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{
"ec_number": "3.6.4.13",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
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{
"id": "P15938",
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}
]
},
{
"ec_number": "3.6.4.13",
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{
"id": "P15938",
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}
]
}
]
},
{
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{
"ec_number": "3.2.1.23",
"activity": "Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.",
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{
"id": "P16278",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P16278"
}
]
},
{
"ec_number": "3.2.1.23",
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{
"id": "P16278",
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}
]
}
]
},
{
"uniprot_ac": "P16381",
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{
"ec_number": "3.6.4.13",
"activity": "ATP + H2O = ADP + H(+) + phosphate.",
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{
"id": "P16381",
"database": "UniProtKB",
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}
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}
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}
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}
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}
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}
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}
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]
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]
}
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}
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}
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},
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{
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}
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},
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{
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{
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{
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{
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