Variant · Snv
FGFR3 E466K
CI-VAR-00000756Explore in graph →NP_000133.1:p.Glu466LysNM_000142.5:c.1396G>ACIViC 3692
Curated evidence
Evidence by cancer (2 items)
Grouped by cancer context first, then therapy. The same variant can be sensitizing in one cancer and irrelevant in another — contexts are never merged. 50 items per page; a cancer group may continue on the next page.
- 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
| Molecular profile | Therapy | Type | Level | Direction · significance | Rating (1–5) | Status | Evidence | Source |
|---|---|---|---|---|---|---|---|---|
| Unmapped disease2unmapped disease | ||||||||
| FGFR3 E466K | (functional) | 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 E466K | (functional) | Functional | D | Supports Gain Of Function | 3 | submitted | EID10390Protein co-chaperone Cdc37 is required in FGFR3 remodeling for recognition by chaperone protein Hsp90. Cdc37 must partially deactivate the kinase and present it in a particular orientation to Hsp90. S… (full text at CIViC) PMID 29478821 · Bunney et al., 2018 · Open in CIViC | civic |
ClinVar
Clinical significance (0)
ClinVar interpretations are shown as structured records — significance, review status, star rating, conditions — never flattened into one word.
Data not yet available