Component
Human F-box and leucine-rich repeat protein 5 / FBXL5
Human F-box and leucine-rich repeat protein 5 / FBXL5. Species, exposure and limitations are retained in each linked claim.
2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What acts on it
Iron or oxygen depletion triggered FBXL5 degradation through a process requiring its N-terminal hemerythrin-like iron-binding domain.
Experimental context and source evidence
- availability_state
- nutrient_deficiency Imported condition classification; unverified.
- evidence_span
- {"source_cache": "artifacts/iron-research/19762596.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9308ac435b303ee150d6c92a21c3d68731fed61f0894312026a8a19e57d5aac6", "start_char": 0, "end_char": 824, "text_sha256": "9308ac435b303ee150d6c92a21c3d68731fed61f0894312026a8a19e57d5aac6"}
- experimental_model
- Protein association, ubiquitination and degradation experiments
- exposure
- Iron and oxygen availability; FBXL5 stability
- limitations
- Cellular sensing mechanism, not a serum-iron diagnostic rule.
- nutrient_topic
- Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
- organism
- Mammalian cellular systems
- plain_language
- The control system responds to both iron and oxygen availability.
- primary_references
- [iron-p19762596] Control of iron homeostasis by an iron-regulated ubiquitin ligase. (2009). https://pubmed.ncbi.nlm.nih.gov/19762596/ DOI: 10.1126/science.1176333
- tissue_or_cell_type
- Cytosolic iron regulation
- trigger_kind
- nutrient_deficiency Imported condition classification; unverified.
Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 693–704
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein association, ubiquitination and degradation experiments · source_derived_draft · unverified_draft
### iron-fbxl5-iron-sensing Iron or oxygen depletion triggered FBXL5 degradation through a process requiring its N-terminal hemerythrin-like iron-binding domain. Condition category: nutrient_deficiency nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The control system responds to both iron and oxygen availability. organism: Mammalian cellular systems tissue_or_cell_type: Cytosolic iron regulation experimental_model: Protein association, ubiquitination and degradation experiments limitations: Cellular sensing mechanism, not a serum-iron diagnostic rule. exposure: Iron and oxygen availability; FBXL5 stability evidence_span: {"source_cache": "artifacts/iron-research/19762596.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9308ac435b303ee150d6c92a21c3d68731fed61f0894312026a8a19e57d5aac6", "start_char": 0, "end_char": 824, "text_sha256": "9308ac435b303ee150d6c92a21c3d68731fed61f0894312026a8a19e57d5aac6"} [iron-p19762596] Control of iron homeostasis by an iron-regulated ubiquitin ligase. (2009). https://pubmed.ncbi.nlm.nih.gov/19762596/ DOI: 10.1126/science.1176333
Complete structured claim and evidence
Where it participates (unsigned role)
A SKP1-CUL1-FBXL5 ligase complex associated with IRP2 and promoted its iron-dependent ubiquitination and degradation.
Experimental context and source evidence
- evidence_span
- {"source_cache": "artifacts/iron-research/19762596.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9308ac435b303ee150d6c92a21c3d68731fed61f0894312026a8a19e57d5aac6", "start_char": 0, "end_char": 824, "text_sha256": "9308ac435b303ee150d6c92a21c3d68731fed61f0894312026a8a19e57d5aac6"}
- experimental_model
- Protein association, ubiquitination and degradation experiments
- exposure
- Iron and oxygen availability; FBXL5 stability
- limitations
- Cellular sensing mechanism, not a serum-iron diagnostic rule.
- nutrient_topic
- Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
- organism
- Mammalian cellular systems
- plain_language
- When iron is available, an enzyme complex can remove a regulator that otherwise favors iron acquisition.
- primary_references
- [iron-p19762596] Control of iron homeostasis by an iron-regulated ubiquitin ligase. (2009). https://pubmed.ncbi.nlm.nih.gov/19762596/ DOI: 10.1126/science.1176333
- tissue_or_cell_type
- Cytosolic iron regulation
Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 680–691
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Protein association, ubiquitination and degradation experiments · source_derived_draft · unverified_draft
### iron-fbxl5-irp2 A SKP1-CUL1-FBXL5 ligase complex associated with IRP2 and promoted its iron-dependent ubiquitination and degradation. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: When iron is available, an enzyme complex can remove a regulator that otherwise favors iron acquisition. organism: Mammalian cellular systems tissue_or_cell_type: Cytosolic iron regulation experimental_model: Protein association, ubiquitination and degradation experiments limitations: Cellular sensing mechanism, not a serum-iron diagnostic rule. exposure: Iron and oxygen availability; FBXL5 stability evidence_span: {"source_cache": "artifacts/iron-research/19762596.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "9308ac435b303ee150d6c92a21c3d68731fed61f0894312026a8a19e57d5aac6", "start_char": 0, "end_char": 824, "text_sha256": "9308ac435b303ee150d6c92a21c3d68731fed61f0894312026a8a19e57d5aac6"} [iron-p19762596] Control of iron homeostasis by an iron-regulated ubiquitin ligase. (2009). https://pubmed.ncbi.nlm.nih.gov/19762596/ DOI: 10.1126/science.1176333
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.