Publication
Landscape of activating cancer mutations in FGFR kinases and their differential responses to inhibitors in clinical use.
Authors not recorded
- Source
- PubMed
- Retrieved
- Sep 8, 2026
- Layer
- normalized (units and labels harmonized; values unchanged)
- Run
- ING-CIVIC-20260908-000001
Abstract
Abstract (excerpt)
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Linked entities
Linked entities (7)
How each link was made (MeSH, dictionary, registry reference, curation…) and whether it has been validated. Candidate links are not counted in entity statistics.
Validated 7
- cancerMalignant Neoplasmcivic_curation1.00
- geneFGFR3civic_curation1.00
- variantFGFR3 A500Tcivic_curation1.00
- variantFGFR3 G697Ccivic_curation1.00
- variantFGFR3 N540Kcivic_curation1.00
- variantFGFR3 V555Mcivic_curation1.00
- variantFGFR3 Y647Ccivic_curation1.00
Curated evidence
Evidence citing this paper (15)
- Source
- CIViC — Clinical Interpretation of Variants in Cancer
- Dataset
- CIViC evidence items
- Version
- civic-2026-09-08
- Retrieved
- Sep 8, 2026
- Layer
- normalized (units and labels harmonized; values unchanged)
- Evidence
- expert curation
- License
- CC0 1.0
- PMID
- 26992226
- Run
- ING-CIVIC-20260908-000001
| Therapy | Cancer | Type | Level | Direction · significance | Rating (1–5) | Status | Evidence | Source |
|---|---|---|---|---|---|---|---|---|
| FGFR3 G697C1 | ||||||||
| (oncogenic) | Malignant NeoplasmALIAS | Oncogenic | D | Does Not Support Oncogenicity | 3 | accepted | EID10839Purified proteins of 26 FGFR3 kinase domain variants were used to directly compare the impact of different mutations on FGFR3 auto-phosphorylation. While known hotspot mutations K650E and N540K result… (full text at CIViC) PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| FGFR3 N540K2 | ||||||||
| (oncogenic) | Malignant NeoplasmALIAS | Oncogenic | D | Supports Oncogenicity | 3 | accepted | EID12702In NIH3T3 colony formation assays, cells expressing N540K displayed a transformed phenotype and showed approximately 20 fold increased colony formation over wildtype cells. In comparison, activating v… (full text at CIViC) PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| (functional) | —UNRESOLVED | Functional | D | Supports Gain Of Function | 3 | accepted | EID1008425 FGFR3 mutant proteins were isolated and their auto-phosphorylation and kinase activity was measured and compared to wild-type. 6 mutations (N540K, N540S, K650E, K650N, R669G, R669Q) demonstrated in… (full text at CIViC) PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| FGFR3 A500T1 | ||||||||
| (functional) | —UNRESOLVED | Functional | D | Does Not Support Gain Of Function | 2 | accepted | EID13090FGFR3 variant A500T was assessed among a panel of 26 FGFR3 kinase domain variants using purified protein in vitro auto-phosphorylation assays (Figure 2A). Compared to wild type, A500T showed only a sm… (full text at CIViC) PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| FGFR3 D617G1 | ||||||||
| (functional) | —UNRESOLVED | Functional | D | Supports Loss Of Function | 3 | submitted | EID1009025 FGFR3 mutant proteins were isolated and their auto-phosphorylation and kinase activity was measured and compared to wild-type. 2 mutations (D617G, G637W) eliminated kinase activity. PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| FGFR3 E466K1 | ||||||||
| (functional) | —UNRESOLVED | Functional | D | Does Not Support Gain Of Function | 3 | rejected | EID1008325 FGFR3 mutant proteins were isolated and their auto-phosphorylation and kinase activity was measured and compared to wild-type. 12 mutations (E466K, A500T, I538F, P572A, C582F, E627D, V630M, H643D, … (full text at CIViC) PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| FGFR3 G637W1 | ||||||||
| (functional) | —UNRESOLVED | Functional | D | Supports Loss Of Function | 3 | submitted | EID1009125 FGFR3 mutant proteins were isolated and their auto-phosphorylation and kinase activity was measured and compared to wild-type. 2 mutations (D617G, G637W) eliminated kinase activity. PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| FGFR3 K650E1 | ||||||||
| (functional) | —UNRESOLVED | Functional | D | Supports Gain Of Function | 3 | submitted | EID1008625 FGFR3 mutant proteins were isolated and their auto-phosphorylation and kinase activity was measured and compared to wild-type. 6 mutations (N540K, N540S, K650E, K650N, R669G, R669Q) demonstrated in… (full text at CIViC) PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| FGFR3 K650N1 | ||||||||
| (functional) | —UNRESOLVED | Functional | D | Supports Gain Of Function | 3 | submitted | EID1008725 FGFR3 mutant proteins were isolated and their auto-phosphorylation and kinase activity was measured and compared to wild-type. 6 mutations (N540K, N540S, K650E, K650N, R669G, R669Q) demonstrated in… (full text at CIViC) PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| FGFR3 N540S1 | ||||||||
| (functional) | —UNRESOLVED | Functional | D | Supports Gain Of Function | 3 | submitted | EID1008525 FGFR3 mutant proteins were isolated and their auto-phosphorylation and kinase activity was measured and compared to wild-type. 6 mutations (N540K, N540S, K650E, K650N, R669G, R669Q) demonstrated in… (full text at CIViC) PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| FGFR3 R669G1 | ||||||||
| (functional) | —UNRESOLVED | Functional | D | Supports Gain Of Function | 3 | submitted | EID1008825 FGFR3 mutant proteins were isolated and their auto-phosphorylation and kinase activity was measured and compared to wild-type. 6 mutations (N540K, N540S, K650E, K650N, R669G, R669Q) demonstrated in… (full text at CIViC) PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| FGFR3 R669Q1 | ||||||||
| (functional) | —UNRESOLVED | Functional | D | Supports Gain Of Function | 3 | submitted | EID1008925 FGFR3 mutant proteins were isolated and their auto-phosphorylation and kinase activity was measured and compared to wild-type. 6 mutations (N540K, N540S, K650E, K650N, R669G, R669Q) demonstrated in… (full text at CIViC) PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| FGFR3 V555M1 | ||||||||
| (functional) | —UNRESOLVED | Functional | D | Supports Gain Of Function | 4 | accepted | EID12988Purified recombinant FGFR3 kinase domain protein harboring the V555M substitution exhibited increased in vitro kinase activity compared with wild-type FGFR3. Both autophosphorylation and peptide subst… (full text at CIViC) PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| FGFR3 Y647C2 | ||||||||
| (functional) | —UNRESOLVED | Functional | D | Does Not Support Gain Of Function | 2 | rejected | EID9705Variant reported within a comprehensive study of FGFRs intracellular variants (highlight in the KD) and insight in FGFR-selective tyrosine kinase inhibitors. Y647C was related to lung cancer, observed… (full text at CIViC) PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |
| 〃 | —UNRESOLVED | Functional | D | Supports Gain Of Function | 3 | accepted | EID13187Purified FGFR3 protein with the Y647C substitution had higher kinase activity in vitro than wild-type FGFR3 protein, as measured by autophosphorylation. PMID 26992226 · Patani et al., 2016 · Open in CIViC | civic |