InterPro2GO mapping of the Tom20 domain signature, the source of the TOM complex, protein targeting, intracellular protein transport and protein import into mitochondrial matrix annotations for TOMM20. Domain-based mapping supports complex membership and pathway involvement but does not by itself distinguish receptor from channel roles.

Curator-judged ISS transfer from a characterised orthologue; for TOMM20 this is the basis of the sperm midpiece localization, which reflects mitochondrial enrichment in the sperm midpiece rather than a distinct TOMM20 function.

Source of the PANTHER phylogenetically-inferred (IBA) annotations for TOMM20, correctly propagating TOM complex membership, mitochondrion targeting sequence binding, protein transmembrane transporter activity and protein import into the mitochondrial matrix across the deeply conserved Tom20/Mom19 family.

The same IBA propagation also produced a tRNA import into mitochondrion annotation. TOM-complex involvement in tRNA import is documented in yeast and plants, but the human TOMM20 literature is exclusively about protein import, so this term reflects family-level inference rather than a demonstrated human function.

UniProtKB keyword-to-GO mapping, the source of the generic protein transport annotation; it is correct but far less informative than the presequence-receptor function established experimentally.

Mapping of the UniProtKB subcellular location statement onto GO, supporting the mitochondrial outer membrane location of TOMM20 as a single-pass outer-membrane protein with a cytosol-facing receptor domain.

Immunofluorescence-based curation supporting a mitochondrial staining pattern for TOMM20; because TOMM20 antibodies are widely used as generic mitochondrial markers, this evidence establishes the organelle but not the outer-membrane sub-compartment.

Ensembl Compara orthology projection, the source of the coarse mitochondrion annotation and of the cell periphery, sperm midpiece and migrasome locations. The latter three describe structures that contain mitochondria rather than distinct TOMM20 localizations.

Combined multi-method IEA pipeline supporting the mitochondrial envelope location; correct but subsumed by the more specific outer-membrane assignment.

Establishes the canonical division of labour at the TOM complex - Tom20 is the receptor for N-terminal presequences while Tom70 handles internal targeting signals such as those of carrier proteins.

The cytosolic co-chaperone AIP was identified as a Tom20 interactor in a two-hybrid screen, binding through the extreme C-terminal acidic segment of Tom20.

A ternary Tom20-AIP-preprotein complex was observed, showing that the Tom20 receptor engages preproteins together with cytosolic delivery factors.

Dissection of the human Tom40 import pathway; the Tom40 precursor forms its first stable intermediate on the outer face of the TOM complex, of which TOMM20 is a component, so this supports complex membership rather than a TOMM20-specific activity.

Background framing of the paper, stating the subunit composition of the fungal TOM complex, in which Tom20 is one of the three import receptors alongside Tom70 and Tom22; the paper notes these components are conserved in mammals.

The TOM complex was immuno-isolated from human (HeLa) cells via hTom22-FLAG and found to contain the human counterparts of Tom5 and Tom6 together with the other TOM components, providing direct human evidence for the composition of the translocase complex of which TOMM20 is a subunit.

Peptide-array screening against the three purified TOM receptors was used to map the unconventional mitochondrial targeting sequence of APE1, an assay that reports TOMM20 targeting-sequence recognition.

Study of Tom70 as an adaptor linking MAVS to TBK1/IRF3 in antiviral signalling; the innate-immune role demonstrated here is specific to TOMM70, so it does not transfer to TOMM20.

Demonstrates that autophagosomes form at ER-mitochondria contact sites; TOMM20 serves in this work as a mitochondrial outer-membrane marker for the contact site rather than as a functional participant in autophagosome biogenesis.

Ubiquitin-affinity proteomics of VPS34-inhibited cells identifying NCOA4 as a ferritin receptor; TOMM20 appears in this dataset as a ubiquitinated mitochondrial outer-membrane protein, consistent with its role as a mitophagy substrate rather than a mediator.

Systematic proteomic analysis of the human MICOS complex that identified QIL1; TOMM20 appears in the associated interaction data as an outer-membrane protein, which supports its localization but not MICOS membership.

Crosslinking mass spectrometry of intact human nuclei; a TOMM20 crosslink in this nuclear dataset is most parsimoniously explained as carry-over of an abundant outer-membrane protein and does not support a nuclear function or location.

Drosophila study of Ttm50 (a Tim23-complex subunit) anchoring calpain at Golgi/ER calcium stores; the protein studied is a TIM, not a TOM, subunit, so the calpain regulation described here is not a TOMM20 function.

TOMM20 is a member of the stringently defined human mitochondrial high-confidence proteome (MitoCoP), corroborating mitochondrial localization.

OpenCell endogenous-tagging resource combining live-cell imaging and interaction proteomics; TOMM20 entries derived from it are systematic localization and interaction data points rather than evidence for a specific molecular function.

The paper's framing of prior work (cited to earlier literature, not a result of this study) that Tom20 is the major import receptor which, with Tom70 and Tom22, targets mitochondrial precursor proteins in the cytosol; this study's own presequence pull-down result concerns Tom22 as well as Tom20 (see finding below).

Tom20 and Tom22 both adopt three-helix bundle cytosolic domains, and pull-down assays show both engage a presequence-bearing precursor.

Abstract-level background statement that deficiency of the TOM receptor components (Tom20, Tom22, Tom70 collectively) has been linked to neurodegenerative disease and cardiac pathology; the body of the paper attributes the specific disease links to Tom40 and Tom22 (neurodegeneration) and Tom70 (cardiac pathology), so no Tom20-specific disease association is established here.

A reconstituted yeast system co-expressing human PINK1 with all seven TOM subunits showed that TOM20 and TOM70 are required for optimal PINK1 activation, a receptor role distinct from bulk presequence import.

Stabilisation of PINK1 at the TOM complex of damaged mitochondria is the critical step in PINK1 activation, placing TOMM20 upstream of PINK1/Parkin mitophagy signalling.

FEM1B, the substrate receptor of the CRL2 E3 ubiquitin ligase, associates directly with TOM20, and this association recruits the ligase to the outer membrane to drive PLD6 turnover.

Disrupting the FEM1B-TOM20 interaction impairs PLD6 degradation and causes mitochondrial morphology defects, establishing a TOM20 function in mitochondrial dynamics that is separate from presequence import.

The human TOMM20 cDNA was identified as a homologue of the fungal import receptor Mom19, with the three diagnostic features of an N-terminal hydrophobic anchor, a central TPR motif and an acidic C-terminus.

The human protein assembles with the yeast outer membrane receptor complex, functionally identifying it as a mitochondrial import receptor.

Mitophagy step in which p62 links a damaged mitochondrion to LC3. TOMM20 features in this pathway as an ubiquitinated outer-membrane cargo rather than as an actor in the reaction.

Reactome step describing constitutive PINK1 import into mitochondria and its voltage-sensitive cleavage in healthy mitochondria. The cached Reactome summary does not itself name the TOM complex; the mechanistic link to TOMM20 (PINK1 entering via, and being stabilised on, the TOM complex) comes from the primary literature (PMID:38848361), not from this Reactome record.

Autophagosome-membrane step of mitophagy; TOMM20 is present only as a component of the engulfed mitochondrion and is a degradation substrate here.

Step in which p62 binds Parkin-ubiquitinated mitochondrial substrates; TOMM20 is one of the ubiquitinated outer-membrane substrates recognised, i.e. a target rather than an effector.

USP30 deubiquitinates outer-membrane proteins, opposing Parkin-driven mitophagy; TOMM20 is among the ubiquitinated outer-membrane proteins subject to this editing.

OPTN and TBK1 bind ubiquitin chains conjugated to mitochondrial outer-membrane proteins; TOMM20 contributes as one of the ubiquitinated MOM proteins that flag the damaged organelle.

MAP1LC3B binds phosphorylated OPTN on ubiquitinated mitochondria; TOMM20 participates only as part of the ubiquitin-decorated outer membrane being recognised.

TBK1 autophosphorylation within the TBK1:OPTN:ubiquitinated-mitochondrial-protein assembly; TOMM20's involvement is as a constituent of the ubiquitinated outer membrane.

Activated TBK1 phosphorylates OPTN on ubiquitin-flagged mitochondria; again TOMM20 appears as ubiquitinated cargo rather than as a signalling component.

Reactome states explicitly that Parkin ubiquitinates a broad range of outer-membrane substrates including TOMM20; this is the pathway basis for treating TOMM20 as a mitophagy substrate.

PINK1 phosphorylates Ser65 of ubiquitin conjugated to outer-membrane proteins, amplifying Parkin recruitment; TOMM20-linked ubiquitin is among the substrates.

Parkin binds phospho-Ser65-ubiquitin on outer-membrane proteins; TOMM20 contributes as a ubiquitinated MOM protein in the feed-forward mitophagy loop.

Reactome step in which PINK1 phosphorylates PRKN at Ser65 on the mitochondrial outer membrane of damaged mitochondria. The cached Reactome summary describes PINK1/PRKN and outer-membrane ubiquitin but does not name the TOM complex; TOMM20's relevance as a TOM subunit contributing to PINK1 stabilisation and activation is established by the primary literature (PMID:38848361) rather than by this record.

OPTN recruits ATG9A vesicles to damaged mitochondria during PINK1/Parkin mitophagy; TOMM20 is not a participant in this step and is present only as outer-membrane cargo.