Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
GOA annotations for human MEFV
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The fetched GOA line for the contested GO:0061630 IBA annotation propagates ubiquitin protein ligase activity through PANTHER:PTN007774218 and a broad TRIM-family source set.
"UniProtKB O15553 MEFV enables GO:0061630 ubiquitin protein ligase activity molecular_function ECO:0000318 IBA GO_REF:0000033 MGI:MGI:2137355|MGI:MGI:2385051|MGI:MGI:2447992|MGI:MGI:2684862|MGI:MGI:2684869|MGI:MGI:3612190|PANTHER:PTN007774218|UniProtKB:P14373|UniProtKB:P19474|UniProtKB:Q12899|UniProtKB:Q86WT6|UniProtKB:Q8IWZ4|UniProtKB:Q8IYM9|UniProtKB:Q8WV44|UniProtKB:Q969Q1|UniProtKB:Q96A61|UniProtKB:Q9BVG3|UniProtKB:Q9BYV6|UniProtKB:Q9BZY9|UniProtKB:Q9C029|UniProtKB:Q9C030|UniProtKB:Q9H2S5 9606 Homo sapiens GO_Central Pyrin 20250903"
OpenScientist hypothesis investigation - MEFV ubiquitin protein ligase activity
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OpenScientist found that the GO:0061630 IBA assignment is a phylogenetic over-annotation and recommended removal.
"The annotation of MEFV/TRIM20/pyrin with GO:0061630 (ubiquitin protein ligase activity) is a phylogenetic over-annotation that should be removed."
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OpenScientist found no annotated RING domain in MEFV across the major domain resources checked.
"Critically, no RING finger domain is annotated by UniProt, InterPro (IPR050143), Pfam, SMART, or PROSITE."
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OpenScientist identified the supported MEFV functions as autophagy receptor activity and inflammasome sensing rather than E3 ubiquitin ligase activity.
"MEFV's primary documented functions are autophagy receptor activity and inflammasome sensing"
Hematopoietic-specific expression of MEFV, the gene mutated in familial Mediterranean fever, and subcellular localization of its corresponding protein, pyrin.
Alternative splicing at the MEFV locus involved in familial Mediterranean fever regulates translocation of the marenostrin/pyrin protein to the nucleus.
The familial Mediterranean fever protein, pyrin, associates with microtubules and colocalizes with actin filaments.
Interaction between pyrin and the apoptotic speck protein (ASC) modulates ASC-induced apoptosis.
Cryopyrin and pyrin activate caspase-1, but not NF-kappaB, via ASC oligomerization.
Clinical and subclinical inflammation in patients with familial Mediterranean fever and in heterozygous carriers of MEFV mutations.
The B30.2 domain of pyrin, the familial Mediterranean fever protein, interacts directly with caspase-1 to modulate IL-1beta production.
Pyrin activates the ASC pyroptosome in response to engagement by autoinflammatory PSTPIP1 mutants.
The familial Mediterranean fever protein, pyrin, is cleaved by caspase-1 and activates NF-kappaB through its N-terminal fragment.
Pyrin Modulates the Intracellular Distribution of PSTPIP1.
Missense mutations in the MEFV gene are associated with fibromyalgia syndrome and correlate with elevated IL-1beta plasma levels.
TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation.
Identification of multifaceted binding modes for pyrin and ASC pyrin domains gives insights into pyrin inflammasome assembly.
TRIM proteins regulate autophagy and can target autophagic substrates by direct recognition.
TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity.
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Pyrin/TRIM20 is a selective-autophagy receptor that targets inflammasome components NLRP3, NLRP1 and pro-caspase-1 for autophagic degradation by assembling ULK1, Beclin-1, ATG16L1 and ATG8/LC3; FMF mutations impair this autophagic function.
Familial autoinflammation with neutrophilic dermatosis reveals a regulatory mechanism of pyrin activation.
Familial Mediterranean fever mutations lift the obligatory requirement for microtubules in Pyrin inflammasome activation.
Inflammasome activation and assembly at a glance.
An N-terminal CDC42 T43I variant reveals the mechanism of pyrin inflammasome activation.
An autoinflammatory CDC42 variant M45L demonstrates the mechanism of pyrin inflammasome activation.
A genotype-first approach reveals the molecular basis of pyrin inflammasome activation.