FANCL (FANCL) — AIGR vs Affinage

FANCL (FANCL) — AIGR vs Affinage

Affinage record: 2026-06-09 · 22 discoveries · self-eval pairwise win (faith 100%) · gates passed.

Agreement (brief)

Both sources converge on FANCL's core biology: FANCL (PHF9) is the catalytic RING-type E3
ubiquitin ligase subunit of the Fanconi anemia core complex that, with its dedicated E2
UBE2T, site-specifically monoubiquitinates FANCD2 (Lys561) and FANCI (Lys523) to activate
replication-coupled interstrand-crosslink (ICL) repair. Both resolve the modular
architecture (N-terminal ELF/E2-like fold, central DRWD/RWD-like substrate-binding domain,
C-terminal RING that recruits UBE2T), the essential RING Cys307 and Trp341, FA core-complex
membership, chromatin/nuclear localization, and the requirement of FANCL RING activity for
all major FA phenotypes. Affinage's 22-citation narrative is factually consistent with the
AIGR review and overlaps on the foundational mechanistic PMIDs (12973351, 16916645, 17938197,
19111657, 19589784, 24389026, 22343915). No factual contradictions on core function.

Disagreements

Topic Affinage says AIGR review says Verdict (who is right + why)
Molecular activity GO layer mechanism_profile: GO:0016874 ligase activity, GO:0140096 catalytic activity acting on a protein, GO:0031386 protein tag activity GO:0061630 ubiquitin protein ligase activity (+ parent GO:0004842) and GO:0031624 ubiquitin conjugating enzyme binding for the E2-recruitment MF AIGR right; Affinage coarse. Affinage collapses to high parents; GO:0016874 and GO:0140096 are non-specific ancestors and GO:0031386 "protein tag activity" is the wrong sense (that term is for ubiquitin/UBL as the tag, not the ligase). AIGR's specific RING-E3 term and the E2-binding MF are the correct branches.
E2 interaction MF Lists UBE2T/UBE2W as partners; narrative treats the RING–E2 interface as central Corrected E3→E2 term: MODIFY GO:0031625 (ubiquitin protein ligase binding, = binding an E3) → GO:0031624 (ubiquitin conjugating enzyme binding, = binding an E2) because UBE2T/UBE2W are E2s AIGR right (key fix). GOA's IPI carried the E3-binding term for an E2 partner; AIGR fixes the branch. Affinage's coarse layer neither surfaces nor corrects this.
Localization mechanism_profile: nucleus, GO:0000228 nuclear chromosome, GO:0005739 mitochondrion Nucleus + nucleoplasm + GO:0000785 chromatin (IDA); cytoplasm/cytosol KEEP_AS_NON_CORE; mitochondrion not annotated AIGR more precise + appropriately conservative. Mitochondrial localization rests on a single ligase-independent-mitophagy study (PMID:35644338); AIGR keeps it out of GO core localization. Chromatin (the active-holoenzyme site) is captured experimentally.
ELF-domain ubiquitin binding Narrative flags ELF domain binds free ubiquitin (Ile44 patch), required for efficient in-vivo FANCD2 monoubiquitination (PMID:26149689) Was absent from the review Affinage surfaced a genuine gap. Now incorporated as NEW GO:0043130 ubiquitin binding (regulatory/non-core). Legitimate distinct MF of the ELF domain.
Wnt / β-catenin K11 chains K11-linked non-proteolytic ubiquitination of β-catenin enhancing Wnt targets in HSPCs (PMID:22653977) Not annotated AIGR correctly conservative. Single 2012 study, distinct substrate/chain type; a moonlighting claim not established as a core human FANCL function. Documentable in notes, not promoted to GO.
Ligase-independent mitophagy Supports Parkin-mediated mitophagy via a ubiquitin-ligase-independent mitochondrial role; rescued by catalytic-dead C307A (PMID:35644338) Not annotated AIGR correctly conservative. Single study, mechanism-independent of FANCL's defining activity; over-reach to import as human GO core function.
Germline / reproduction PGC proliferation, oocyte survival, sex-reversal phenotypes (mouse Pog PMID:12417526; zebrafish fancl PMID:20661450; GGN interaction PMID:12574169) Not annotated AIGR correctly conservative. Non-human organism/tissue-level consequences of FA-pathway loss, not FANCL's direct molecular function.

Papers incorporated into the review

PMID Supports How used
PMID:26149689 FANCL ELF (E2-like fold) domain binds free ubiquitin non-covalently via the Ile44 patch; dispensable in vitro but required for efficient DNA-damage-induced FANCD2 monoubiquitination in vivo Added to references (reference_review MEDIUM/VERIFIED, PMC4543658 full text verified); added NEW annotation GO:0043130 ubiquitin binding (IDA, action NEW, non-core) with two verbatim supported_by quotes. GO:0043130 confirmed molecular_function (QuickGO, not obsolete).

Net assessment

The AIGR review is materially more precise and better-grounded than the Affinage record on
FANCL's molecular function: it uses the specific RING-E3 term (GO:0061630) and, crucially,
corrects a GOA branch error by remapping the UBE2T/UBE2W interaction from E3-binding
(GO:0031625) to the correct E2-binding term (GO:0031624), whereas Affinage's coarse
mechanism_profile sits at non-specific parents (GO:0016874/GO:0140096) and even mis-tags a
"protein tag activity." Affinage's dense narrative was nonetheless valuable as a sourcing
layer: it surfaced one genuine molecular function the review had missed — non-covalent
ubiquitin binding by the ELF domain (PMID:26149689) — now incorporated as a non-core
GO:0043130 annotation with verbatim support. Affinage's remaining extensions (β-catenin/Wnt,
ligase-independent mitophagy, and germ-cell/reproduction phenotypes) are single-study and/or
non-human organism/tissue phenotypes that AIGR correctly declines to promote to human GO core
functions. 1 paper incorporated, 1 new annotation (GO:0043130 ubiquitin binding),
validation ✓ Valid (1 benign deep-research warning).