id: Q15388
gene_symbol: TOMM20
product_type: PROTEIN
status: IN_PROGRESS
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  TOMM20 (Mitochondrial import receptor subunit TOM20 homolog) is a central receptor
  component of the translocase of the outer membrane of mitochondria (TOM complex).
  It is anchored in the mitochondrial outer membrane via a single-pass transmembrane
  domain and exposes its cytosolic TPR-containing domain to recognize N-terminal
  presequences (mitochondrial targeting sequences) of nuclear-encoded mitochondrial
  preproteins. Together with TOMM22, TOMM20 facilitates transfer of preproteins into
  the TOM40 translocation pore. TOMM20 is also a substrate of PRKN-mediated
  ubiquitination during mitophagy and plays a role in PINK1 stabilization at
  depolarized mitochondria (PMID:40080546, PMID:38848361). The protein recognizes
  the hydrophobic face of amphiphilic helical presequences via its binding groove
  (PMID:14557246, PMID:35733257).
existing_annotations:
- term:
    id: GO:0005742
    label: mitochondrial outer membrane translocase complex
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      TOMM20 is a well-established subunit of the TOM complex. Phylogenetic inference
      (IBA) for GO:0005742 is fully consistent with extensive experimental evidence
      showing TOMM20 as a core receptor component of the TOM complex in humans
      (PMID:18331822, PMID:35733257, PMID:40080546). The cryo-EM structure of the
      human TOM complex at 2.53 A resolution directly shows TOMM20 as a stoichiometric
      component (PMID:35733257). UniProt confirms membership in the TOM complex
      comprising TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, and TOMM40.
    action: ACCEPT
    reason: >-
      Core component of TOMM20 function. IBA annotation is well supported by multiple
      independent structural and biochemical studies in human cells.
    supported_by:
      - reference_id: PMID:35733257
        supporting_text: >-
          As a consequence, we resolved the human TOM complex containing Tom22
          and Tom20 cytosolic domains at 3.74 Å
      - reference_id: PMID:18331822
        supporting_text: >-
          We immuno-isolated the TOM complex from HeLa cells expressing hTom22-FLAG
          and identified the human counterparts of Tom5 and Tom6, together with the
          other components including Tom7.
- term:
    id: GO:0030943
    label: mitochondrion targeting sequence binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      TOMM20 is the primary receptor for N-terminal mitochondrial targeting
      sequences (presequences). This IBA annotation is strongly supported by
      direct experimental evidence including the structural determination of
      the Tom20 cytosolic domain binding groove that recognizes amphipathic
      helical presequences (PMID:35733257), pull-down assays showing Tom20
      binds Su9-DHFR-EGFP presequence fusion protein (PMID:35733257), and
      earlier work showing specific binding to mitochondrial preproteins but
      not proteins destined for other organelles (PMID:14557246). This is
      the core molecular function of TOMM20.
    action: ACCEPT
    reason: >-
      This is the primary molecular function of TOMM20 -- recognizing mitochondrial
      targeting sequences. Extensively validated by structural and biochemical evidence.
    supported_by:
      - reference_id: PMID:35733257
        supporting_text: >-
          both Tom20 and Tom22 were pulled down by the DHFR-EGFP protein fused
          with the presequence of subunit 9 of F0-ATPase (Su9) (42), but not by
          DHFR-EGFP protein without Su9, suggesting that Tom22 indeed forms a
          complex with the presequence as Tom20.
      - reference_id: PMID:14557246
        supporting_text: >-
          Preproteins with NH2-terminal presequences are initially recognized by
          the receptor Tom20, although preproteins with internal targeting signals
          such as carrier proteins are recognized preferentially by Tom70.
- term:
    id: GO:0008320
    label: protein transmembrane transporter activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation of TOMM20 to GO:0008320 "protein transmembrane transporter
      activity" is somewhat imprecise. TOMM20 itself is a receptor that recognizes
      presequences and hands substrates off to the TOMM40 pore. It does not form
      the translocation channel. TOMM40 is the actual pore-forming subunit. However,
      the TOM complex as a whole does function as a protein transmembrane transporter,
      and TOMM20 is an essential component of that activity. The IBA annotation
      likely reflects the holistic function of the complex. This is acceptable at
      the broader level since TOMM20 contributes to the overall transporter activity,
      though it is the receptor subunit rather than the channel.
    action: ACCEPT
    reason: >-
      While TOMM20 is specifically the receptor subunit rather than the pore,
      it is an integral and essential part of the protein translocation machinery.
      The IBA annotation reflects the conserved role of TOM20 family members
      in the protein import pathway. This broad annotation is phylogenetically
      well supported.
    supported_by:
      - reference_id: PMID:35733257
        supporting_text: >-
          Tom20, as the major import receptor, together with Tom70 and Tom22 target
          mitochondrial precursor proteins in the cytosol precisely
- term:
    id: GO:0016031
    label: tRNA import into mitochondrion
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      IBA annotation of TOMM20 to GO:0016031 "tRNA import into mitochondrion"
      is unexpected. While there is evidence in some organisms (yeast, plants) that
      the TOM complex may participate in tRNA import into mitochondria, this is
      not a well-established function of human TOMM20. The primary literature
      on human TOMM20 focuses exclusively on protein import. The IBA inference
      may reflect functions established in other organisms in the Tom20 family
      phylogeny. This is not a core function of TOMM20 in humans and should
      be flagged.
    action: KEEP_AS_NON_CORE
    reason: >-
      The IBA phylogenetic inference may be valid for some family members but
      this is not a well-documented function in human cells. TOMM20 is primarily
      characterized as a protein import receptor. Keeping as non-core since the
      IBA inference has phylogenetic basis but it does not represent the primary
      function of human TOMM20.
- term:
    id: GO:0030150
    label: protein import into mitochondrial matrix
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: >-
      TOMM20 recognizes presequence-bearing preproteins destined for the
      mitochondrial matrix and inner membrane. The TOM complex, of which TOMM20
      is the primary presequence receptor, is the essential entry gate for
      matrix-targeted proteins. This IBA annotation is well supported by the
      known biology: TOMM20 preferentially handles precursors destined for
      the matrix and inner membrane (deep research, Su et al. 2024). Knockdown
      of small Tom proteins compromises matrix import of preprotein
      (PMID:18331822).
    action: ACCEPT
    reason: >-
      Core biological process for TOMM20. As the presequence receptor of the
      TOM complex, TOMM20 is essential for protein import into the mitochondrial
      matrix.
    supported_by:
      - reference_id: PMID:18331822
        supporting_text: >-
          Matrix import of preprotein was affected by double knockdown of any
          combination of small Tom proteins.
      - reference_id: PMID:35733257
        supporting_text: >-
          the precursor proteins can be recognized and transferred from the cytosol
          to four different locations of mitochondria: the outer membrane (OM), the
          inner membrane (IM), the intermembrane space (IMS), and the matrix
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: >-
      IEA annotation from UniProt subcellular location mapping. TOMM20 is
      anchored in the mitochondrial outer membrane via an N-terminal
      transmembrane helix (residues 7-24, per UniProt). This is extensively
      confirmed by multiple IDA experiments and structural studies
      (PMID:25997101, PMID:40080546, PMID:35733257).
    action: ACCEPT
    reason: >-
      Correct localization. TOMM20 is an integral membrane protein of the
      mitochondrial outer membrane. The IEA mapping is fully consistent with
      experimental evidence.
- term:
    id: GO:0005742
    label: mitochondrial outer membrane translocase complex
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: >-
      IEA annotation from InterPro domain mapping. TOMM20 contains the MAS20
      domain (PF02064/IPR002056) which is diagnostic for the Tom20 family of
      mitochondrial import receptors. This correctly maps to TOM complex
      membership. Consistent with the IBA annotation and extensive experimental
      evidence.
    action: ACCEPT
    reason: >-
      Correct. The InterPro-based inference is fully supported by experimental
      data showing TOMM20 is a component of the TOM complex.
- term:
    id: GO:0006605
    label: protein targeting
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: >-
      IEA annotation from InterPro mapping. GO:0006605 "protein targeting" is a
      broad parent term. TOMM20 participates in protein targeting to the
      mitochondrion specifically. While correct, this is less informative than
      the more specific GO:0006626 "protein targeting to mitochondrion" which
      is also annotated to TOMM20 (IDA from PMID:14557246). The broader IEA
      annotation is acceptable as it does not conflict with the more specific
      terms.
    action: ACCEPT
    reason: >-
      Correct but broad. The IEA mapping captures the general protein targeting
      role of TOMM20. More specific terms (GO:0006626, GO:0030150) are also
      present in the annotation set.
- term:
    id: GO:0006886
    label: intracellular protein transport
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: >-
      IEA annotation from InterPro mapping. GO:0006886 "intracellular protein
      transport" is a broad parent term that is technically correct for TOMM20
      as it mediates transport of nuclear-encoded proteins into the mitochondrion.
      More specific process terms are present in the annotation set.
    action: ACCEPT
    reason: >-
      Correct but broad. The IEA mapping is consistent with TOMM20 function
      in mitochondrial protein import. Not misleading even though more specific
      terms exist.
- term:
    id: GO:0015031
    label: protein transport
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: >-
      IEA annotation from UniProt keyword mapping ("Protein transport"). This
      is a very broad term. TOMM20 is part of the protein import machinery
      of mitochondria, so this is technically correct but uninformative. More
      specific annotations already exist in the set.
    action: ACCEPT
    reason: >-
      Correct but very broad parent term. Acceptable as an IEA that is consistent
      with the more specific experimental annotations.
- term:
    id: GO:0030150
    label: protein import into mitochondrial matrix
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: >-
      IEA annotation from InterPro mapping. Duplicate of the IBA annotation
      to the same term. Both are correct -- TOMM20 is essential for protein
      import into the mitochondrial matrix as the primary presequence receptor
      of the TOM complex.
    action: ACCEPT
    reason: >-
      Correct. Consistent with the IBA annotation and extensive experimental
      evidence for TOMM20 role in matrix protein import.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:30021884
  review:
    summary: >-
      IPI annotation from a large-scale crosslinking mass spectrometry study
      of histone interactions in cell nuclei (PMID:30021884). TOMM20 appearing
      in this dataset is likely a contaminant or non-specific interaction, as
      TOMM20 is a mitochondrial outer membrane protein with no known nuclear
      function. The term "protein binding" is uninformative and does not
      reflect the actual molecular function of TOMM20.
    action: REMOVE
    reason: >-
      The annotation to "protein binding" from a nuclear crosslinking MS study
      is uninformative and likely reflects a non-specific or contaminating
      interaction. TOMM20 is a mitochondrial protein with no known nuclear
      role. "Protein binding" does not capture any meaningful functional
      information about TOMM20.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:35271311
  review:
    summary: >-
      IPI annotation from the OpenCell project (PMID:35271311), a large-scale
      endogenous tagging study. While TOMM20 certainly binds proteins (it
      is a receptor for preproteins and part of the TOM complex), the generic
      term "protein binding" does not convey any functional information. TOMM20
      has more specific molecular function annotations (GO:0030943 mitochondrion
      targeting sequence binding) that better capture its binding activity.
    action: REMOVE
    reason: >-
      "Protein binding" is uninformative for TOMM20. The specific binding
      function is already captured by GO:0030943 "mitochondrion targeting
      sequence binding." Per curation guidelines, generic protein binding
      annotations should be avoided in favor of more informative terms.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: >-
      IEA annotation from Ensembl Compara ortholog transfer. TOMM20 is a
      mitochondrial protein, confirmed by multiple IDA annotations and
      structural studies. The broader "mitochondrion" term is less specific
      than "mitochondrial outer membrane" but is not incorrect.
    action: ACCEPT
    reason: >-
      Correct. TOMM20 is a mitochondrial protein. More specific localization
      terms (mitochondrial outer membrane, TOM complex) are also present.
- term:
    id: GO:0005740
    label: mitochondrial envelope
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  review:
    summary: >-
      IEA annotation from combined automated methods. GO:0005740 "mitochondrial
      envelope" is correct but less specific than "mitochondrial outer membrane"
      (GO:0005741). TOMM20 is specifically in the outer membrane, not the inner
      membrane or intermembrane space. The annotation is not wrong, just broad.
    action: ACCEPT
    reason: >-
      Correct but broad. TOMM20 is in the mitochondrial outer membrane, which
      is part of the mitochondrial envelope. More specific annotations exist.
- term:
    id: GO:0071944
    label: cell periphery
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: >-
      IEA annotation from Ensembl Compara ortholog transfer. GO:0071944 "cell
      periphery" is unexpected for TOMM20, which is a mitochondrial outer
      membrane protein. There is no strong evidence that TOMM20 localizes to
      the cell periphery. This may result from erroneous ortholog transfer or
      a broad interpretation from a high-throughput study. TOMM20 is not
      primarily a cell periphery protein.
    action: REMOVE
    reason: >-
      TOMM20 is a mitochondrial outer membrane protein with no established
      localization to the cell periphery. This IEA annotation is likely
      erroneous or reflects non-specific detection in a high-throughput
      experiment. The primary localization is well established as the
      mitochondrial outer membrane.
- term:
    id: GO:0097225
    label: sperm midpiece
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: >-
      IEA annotation from Ensembl Compara ortholog transfer. The sperm midpiece
      is rich in mitochondria (the mitochondrial sheath), so detection of TOMM20
      there is expected for any mitochondrial outer membrane protein. This
      annotation is technically correct but reflects the general mitochondrial
      localization rather than a sperm-specific function.
    action: KEEP_AS_NON_CORE
    reason: >-
      Correct in the sense that mitochondria are abundant in the sperm midpiece
      and TOMM20 would be present there. However, this reflects general
      mitochondrial localization rather than a specific role in sperm biology.
      Not a core annotation for understanding TOMM20 function.
- term:
    id: GO:0140494
    label: migrasome
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  review:
    summary: >-
      IEA annotation from Ensembl Compara ortholog transfer. Migrasomes are
      cellular organelles released during cell migration. TOMM20 appearing in
      migrasomes could reflect mitochondrial content within migrasomes, which
      has been observed. However, this is not a primary localization of TOMM20
      and likely reflects incidental detection of mitochondrial proteins in
      migrasomes.
    action: KEEP_AS_NON_CORE
    reason: >-
      TOMM20 may be present in migrasomes due to mitochondrial content, but
      this does not represent a specific function or primary localization of
      TOMM20. Keeping as non-core since migrasomes can contain mitochondria.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IDA
  original_reference_id: GO_REF:0000052
  review:
    summary: >-
      IDA annotation based on immunofluorescence data curation. TOMM20 is
      routinely used as a mitochondrial marker in immunofluorescence studies,
      making this one of the most well-supported localization annotations
      possible. TOMM20 antibody staining is a standard method for visualizing
      mitochondria.
    action: ACCEPT
    reason: >-
      Well established. TOMM20 is one of the most commonly used mitochondrial
      markers in immunofluorescence.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: NAS
  original_reference_id: PMID:18331822
  review:
    summary: >-
      NAS annotation citing Kato & Mihara 2008, which identified Tom5 and Tom6
      in the human TOM complex. The paper immuno-isolated the TOM complex from
      HeLa cells and confirmed TOMM20 as a component, along with other subunits.
      As a TOM complex subunit, TOMM20 is in the mitochondrial outer membrane.
    action: ACCEPT
    reason: >-
      Correct. PMID:18331822 confirms TOMM20 as part of the TOM complex in
      human cells, which is in the mitochondrial outer membrane.
    supported_by:
      - reference_id: PMID:18331822
        supporting_text: >-
          We immuno-isolated the TOM complex from HeLa cells expressing
          hTom22-FLAG and identified the human counterparts of Tom5 and Tom6,
          together with the other components including Tom7.
- term:
    id: GO:0045040
    label: protein insertion into mitochondrial outer membrane
  evidence_type: NAS
  original_reference_id: PMID:18331822
  review:
    summary: >-
      NAS annotation to GO:0045040 "protein insertion into mitochondrial outer
      membrane" from PMID:18331822. This GO term describes the process of
      inserting proteins from outside the organelle into the mitochondrial outer
      membrane, mediated by large outer membrane translocase complexes. While
      the TOM complex does handle some outer membrane proteins, this process
      is more specifically associated with the SAM complex (GO:0001401) and
      MIM complex (GO:0140595). TOMM20 primarily recognizes presequence-bearing
      proteins destined for the matrix and inner membrane, not outer membrane
      insertion. The TOM complex mediates initial recognition and translocation
      across the outer membrane, but insertion into the outer membrane is
      primarily a SAM/MIM function.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      TOMM20 is the presequence receptor primarily handling matrix/inner membrane
      destined precursors. Protein insertion into the mitochondrial outer membrane
      is primarily mediated by the SAM complex, not the TOM complex receptor
      subunit TOMM20. While TOM participates in the initial recognition step
      for beta-barrel precursors, TOMM20 specifically recognizes N-terminal
      presequences, not the signals used by outer membrane beta-barrel proteins.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: HTP
  original_reference_id: PMID:34800366
  review:
    summary: >-
      HTP annotation from a quantitative high-confidence human mitochondrial
      proteome study (PMID:34800366). TOMM20 was identified as a mitochondrial
      protein with high confidence, consistent with its well-established
      localization.
    action: ACCEPT
    reason: >-
      Correct. High-throughput proteomics confirms TOMM20 in the mitochondrial
      proteome, consistent with all other evidence.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:38848361
  review:
    summary: >-
      IPI annotation from PMID:38848361 (Raimi et al. 2024), which demonstrated
      that TOMM20 interacts with PINK1 in a reconstituted system. The study
      showed that TOM20 and TOM70 receptor subunits are required for optimal
      PINK1 activation and mapped sites of interaction using AlphaFold modeling
      and mutagenesis. While the interaction with PINK1 is genuine and
      functionally significant, "protein binding" does not capture the specific
      nature of this interaction. A more informative term would describe the
      PINK1-TOMM20 interaction in the context of mitophagy signaling.
    action: REMOVE
    reason: >-
      The PINK1-TOMM20 interaction is real and important, but "protein binding"
      is uninformative per curation guidelines. The specific biological context
      is PINK1 activation at damaged mitochondria, which is better captured by
      process annotations. TOMM20 binding to PINK1 is part of its function as
      a TOM complex receptor, already captured by GO:0030943 and GO:0005742.
    supported_by:
      - reference_id: PMID:38848361
        supporting_text: >-
          We unambiguously demonstrate that the TOM20 and TOM70 receptor subunits
          are required for optimal PINK1 activation and map their sites of
          interaction with PINK1 using AlphaFold structural modeling and mutagenesis.
- term:
    id: GO:0030943
    label: mitochondrion targeting sequence binding
  evidence_type: IDA
  original_reference_id: PMID:35733257
  review:
    summary: >-
      IDA annotation from Su et al. 2022 (PMID:35733257), which determined the
      cryo-EM structure of the human TOM complex at 2.53 A and captured the
      TOM complex with Tom20 and Tom22 cytosolic domains at 3.74 A. Pull-down
      experiments directly demonstrated that Tom20 binds the presequence of
      Su9-DHFR-EGFP but not DHFR-EGFP without the presequence, confirming
      specific mitochondrial targeting sequence binding. This is the core
      molecular function of TOMM20.
    action: ACCEPT
    reason: >-
      Direct experimental evidence demonstrating TOMM20 binds mitochondrial
      targeting sequences specifically. This is the best-supported core
      molecular function annotation for TOMM20.
    supported_by:
      - reference_id: PMID:35733257
        supporting_text: >-
          both Tom20 and Tom22 were pulled down by the DHFR-EGFP protein fused
          with the presequence of subunit 9 of F0-ATPase (Su9) (42), but not
          by DHFR-EGFP protein without Su9, suggesting that Tom22 indeed forms
          a complex with the presequence as Tom20.As the cytosolic domain of
          Tom20 is the main site for presequence binding
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IDA
  original_reference_id: PMID:32848200
  review:
    summary: >-
      IDA annotation from PMID:32848200. The title of this paper is about
      Ttm50 facilitating calpain activation. TOMM20 was likely used as a
      mitochondrial marker in this study. The localization to mitochondrion
      is well established.
    action: ACCEPT
    reason: >-
      Correct localization. TOMM20 is a mitochondrial protein. Likely used
      as a marker in this study confirming mitochondrial localization.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5205649
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-5205649 "p62 links damaged
      mitochondria to LC3." TOMM20 is placed at the mitochondrial outer membrane
      in this mitophagy pathway, which is correct. TOMM20 is a ubiquitination
      substrate of PRKN during mitophagy.
    action: ACCEPT
    reason: >-
      Correct localization within the context of the PINK1-PRKN mitophagy
      pathway. TOMM20 is a substrate of PRKN ubiquitination on the mitochondrial
      outer membrane.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5205663
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-5205663 "LC3 binds the
      autophagosome membrane Atg5-Atg12 complex." TOMM20 localization to
      mitochondrial outer membrane in this autophagy context is correct.
    action: ACCEPT
    reason: >-
      Correct localization. Duplicate evidence for TOMM20 at the mitochondrial
      outer membrane from the mitophagy pathway context.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5205673
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-5205673 "p62 binds ubiquitinated
      mitochondrial substrates." TOMM20 is a known ubiquitination substrate on
      the mitochondrial outer membrane during mitophagy. Correct localization.
    action: ACCEPT
    reason: >-
      Correct. TOMM20 is ubiquitinated by PRKN at K35, K56, K61, and K68 on
      the mitochondrial outer membrane during mitophagy.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9824888
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-9824888 "OPTN, TBK1 bind
      ubiquitinated MOM proteins." TOMM20 is a ubiquitinated MOM substrate.
      Correct localization.
    action: ACCEPT
    reason: >-
      Correct localization in the mitophagy pathway context.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9824892
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-9824892 "MAP1LC3B binds
      p-S-OPTN bound to Ub-mitochondria." TOMM20 at mitochondrial outer
      membrane in mitophagy context. Correct localization.
    action: ACCEPT
    reason: >-
      Correct localization. Redundant with other mitochondrial outer membrane
      TAS annotations from Reactome mitophagy pathway.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9824894
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-9824894 "TBK1 is
      phosphorylated within TBK1:OPTN:Ub-mitochondrial proteins." TOMM20
      at mitochondrial outer membrane. Correct localization.
    action: ACCEPT
    reason: >-
      Correct localization in the mitophagy signaling context.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9824897
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-9824897 "p-S-TBK1
      phosphorylates OPTN." TOMM20 at mitochondrial outer membrane in
      the mitophagy signaling cascade. Correct localization.
    action: ACCEPT
    reason: >-
      Correct localization.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9834070
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-9834070 "PRKN ubiquitinates
      MOM substrates." TOMM20 is a direct ubiquitination substrate of PRKN
      on the mitochondrial outer membrane (PMID:24896179, PMID:25621951 per
      UniProt). Correct and specifically relevant.
    action: ACCEPT
    reason: >-
      Correct. TOMM20 is directly ubiquitinated by PRKN at K35, K56, K61,
      and K68 on the mitochondrial outer membrane.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9840807
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-9840807 "OPTN binds ATG9A."
      TOMM20 at mitochondrial outer membrane in the mitophagy context.
      Correct localization.
    action: ACCEPT
    reason: >-
      Correct localization.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9834945
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-9834945 "PINK1 phosphorylates
      Ub on MOM proteins." The Reactome entry explicitly lists TOMM20 as one
      of the MOM proteins whose ubiquitin moieties are phosphorylated by PINK1.
      Correct localization.
    action: ACCEPT
    reason: >-
      Correct. TOMM20 is specifically named as a PINK1 substrate in this
      Reactome pathway.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9835009
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-9835009 "PRKN binds
      p-S-Ub:MOM proteins." TOMM20 at mitochondrial outer membrane as a
      ubiquitinated substrate for PRKN binding. Correct localization.
    action: ACCEPT
    reason: >-
      Correct localization in the PINK1-PRKN mitophagy pathway.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9835011
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-9835011 "PINK1 phosphorylates
      PRKN at S65." TOMM20 at mitochondrial outer membrane in the context of
      PINK1 activation at the TOM complex. Correct localization.
    action: ACCEPT
    reason: >-
      Correct localization.
- term:
    id: GO:0097225
    label: sperm midpiece
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  review:
    summary: >-
      ISS annotation from manual transfer by curator judgment. The sperm midpiece
      contains the mitochondrial sheath, which is densely packed with mitochondria.
      TOMM20, as a ubiquitous mitochondrial outer membrane protein, would be
      present in sperm midpiece mitochondria. This is a valid localization
      but not specific to TOMM20 function.
    action: KEEP_AS_NON_CORE
    reason: >-
      Correct due to mitochondrial content of the sperm midpiece. Not a core
      annotation for understanding TOMM20 function; it simply reflects the
      general mitochondrial localization in a specialized cell type.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IDA
  original_reference_id: PMID:20628368
  review:
    summary: >-
      IDA annotation from PMID:20628368 (Liu et al. 2010), a study on Tom70
      mediating activation of IRF3 on mitochondria. TOMM20 was used as a
      mitochondrial marker or co-localization control in this study. UniProt
      cites this paper for subcellular location evidence. Correct localization.
    action: ACCEPT
    reason: >-
      Correct. TOMM20 mitochondrial localization confirmed in a study where
      it was used as a mitochondrial marker.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IDA
  original_reference_id: PMID:25327288
  review:
    summary: >-
      IDA annotation from PMID:25327288 (Dowdle et al. 2014), a study on
      VPS34 inhibitor and autophagy/ferritinophagy. TOMM20 was likely used
      as a mitochondrial marker in this study. Correct localization.
    action: ACCEPT
    reason: >-
      Correct localization. TOMM20 is widely used as a mitochondrial marker.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5696872
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-5696872 "USP30 deubiquitinates
      Ub-MOM proteins." TOMM20 is a substrate of both PRKN (ubiquitination) and
      USP30 (deubiquitination) at the mitochondrial outer membrane
      (PMID:24896179). Correct and functionally relevant localization.
    action: ACCEPT
    reason: >-
      Correct. TOMM20 is a known substrate of USP30 deubiquitination on the
      mitochondrial outer membrane, documented in PMID:24896179.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: IDA
  original_reference_id: PMID:25997101
  review:
    summary: >-
      IDA annotation from PMID:25997101 (Guarani et al. 2015), a study on
      QIL1/MICOS complex. TOMM20 was used as a mitochondrial outer membrane
      marker via immunofluorescence co-staining with MICOS subunits. The paper
      states alpha-TOMM20 was used for immunofluorescence analysis to verify
      mitochondrial localization. UniProt also cites this paper for subcellular
      location evidence. Correct localization.
    action: ACCEPT
    reason: >-
      Correct. TOMM20 used as a mitochondrial outer membrane marker in
      immunofluorescence studies, confirming its localization.
    supported_by:
      - reference_id: PMID:25997101
        supporting_text: >-
          Confocal microscopy after immunostaining with α-HA and α-TOMM20
          verified that each protein was targeted to mitochondria in HeLa cells
- term:
    id: GO:0044233
    label: mitochondria-associated endoplasmic reticulum membrane contact site
  evidence_type: IDA
  original_reference_id: PMID:23455425
  review:
    summary: >-
      IDA annotation from PMID:23455425 (Hamasaki et al. 2013),
      "Autophagosomes form at ER-mitochondria contact sites." TOMM20 was likely
      detected at MAM (mitochondria-associated ER membrane) contact sites. As
      an outer membrane protein of mitochondria, TOMM20 would be present at
      ER-mitochondria contact regions where the outer membrane faces the ER.
      This is consistent with its localization but may not represent a specific
      function at MAMs.
    action: KEEP_AS_NON_CORE
    reason: >-
      TOMM20 as a mitochondrial outer membrane protein could be present at
      MAM contact sites, but there is no evidence that TOMM20 has a specific
      functional role at these sites. This likely reflects detection of the
      mitochondrial outer membrane at ER contact points rather than a specific
      MAM-targeted function.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5205661
  review:
    summary: >-
      TAS annotation from Reactome pathway R-HSA-5205661 "Pink1 is recruited
      from the cytoplasm to the mitochondria." TOMM20 at the mitochondrial
      outer membrane in the context of PINK1 import. Recent evidence shows
      TOMM20 directly gates PINK1 activity and mediates tethering of TOM and
      TIM23 translocases upon mitochondrial stress (PMID:38416681 cited in
      UniProt). Correct and functionally relevant.
    action: ACCEPT
    reason: >-
      Correct. TOMM20 is at the mitochondrial outer membrane where it
      participates in PINK1 stabilization upon mitochondrial depolarization.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:20231292
  review:
    summary: >-
      IPI annotation from PMID:20231292 (Li et al. 2010), which identified
      the mitochondrial targeting sequence of APEX1 (apurinic/apyrimidinic
      endonuclease 1) and showed it interacts with TOMM20 for mitochondrial
      import. UniProt confirms this interaction. However, "protein binding" is
      uninformative. The actual function demonstrated is that TOMM20 recognizes
      the MTS of APEX1, which is already captured by GO:0030943 "mitochondrion
      targeting sequence binding."
    action: REMOVE
    reason: >-
      The interaction between TOMM20 and APEX1 is genuine and reflects TOMM20
      recognizing the mitochondrial targeting sequence of APEX1. However,
      "protein binding" is uninformative. This function is already captured by
      GO:0030943 "mitochondrion targeting sequence binding." Per curation
      guidelines, avoid generic protein binding annotations.
    supported_by:
      - reference_id: PMID:20231292
        supporting_text: >-
          Identification and characterization of mitochondrial targeting sequence
          of human apurinic/apyrimidinic endonuclease 1.
- term:
    id: GO:0005742
    label: mitochondrial outer membrane translocase complex
  evidence_type: TAS
  original_reference_id: PMID:15644312
  review:
    summary: >-
      TAS annotation from PMID:15644312 (Humphries et al. 2005), which
      dissected the import and assembly pathway for human Tom40. The study
      confirms TOMM20 as part of the TOM complex by showing that the Tom40
      precursor forms its first stable intermediate with the outer face of
      the TOM complex. Correct component annotation.
    action: ACCEPT
    reason: >-
      Correct. The study demonstrates the TOM complex in human cells and
      TOMM20 is a well-established component.
    supported_by:
      - reference_id: PMID:15644312
        supporting_text: >-
          The precursor then forms its first stable intermediate with the outer
          face of the TOM complex before its membrane integration and assembly.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:14557246
  review:
    summary: >-
      IPI annotation from PMID:14557246 (Yano et al. 2003), which showed
      that AIP binds to Tom20 and that both proteins bind mitochondrial
      preproteins. The binding between Tom20 and preproteins is specific to
      mitochondrial targeting sequences. "Protein binding" is uninformative
      and does not capture the specificity demonstrated in this paper.
    action: REMOVE
    reason: >-
      The interaction demonstrated is specific preprotein binding via
      mitochondrial targeting sequences, which is already captured by
      GO:0030943 "mitochondrion targeting sequence binding." The generic
      "protein binding" annotation does not add functional information.
    supported_by:
      - reference_id: PMID:14557246
        supporting_text: >-
          AIP as well as Tom20 binds specifically to mitochondrial preproteins
          [...] no or little binding of AIP and Tom20 to proteins destined for
          other organelles, including peroxisomes, ER, and nucleus, was observed.
- term:
    id: GO:0005742
    label: mitochondrial outer membrane translocase complex
  evidence_type: TAS
  original_reference_id: PMID:14557246
  review:
    summary: >-
      TAS annotation from PMID:14557246 (Yano et al. 2003). The paper
      describes Tom20 as part of the TOM complex, the preprotein translocase
      of the mitochondrial outer membrane. Correct component annotation.
    action: ACCEPT
    reason: >-
      Correct. The paper confirms TOMM20 as a component of the TOM complex.
    supported_by:
      - reference_id: PMID:14557246
        supporting_text: >-
          Preproteins with NH2-terminal presequences are initially recognized
          by the receptor Tom20, although preproteins with internal targeting
          signals such as carrier proteins are recognized preferentially by Tom70.
- term:
    id: GO:0015450
    label: protein-transporting ATPase activity
  evidence_type: IDA
  original_reference_id: PMID:14557246
  review:
    summary: >-
      IDA annotation of TOMM20 to GO:0015450 "protein-transporting ATPase
      activity" from PMID:14557246. This is problematic. GO:0015450 describes
      "primary active carrier-mediated transport of a protein across a membrane,
      driven by the hydrolysis of the diphosphate bond of inorganic pyrophosphate,
      ATP, or another nucleoside triphosphate." TOMM20 does not have ATPase
      activity. It is a receptor that recognizes presequences. The TOM complex
      as a whole translocates proteins, but the driving force is primarily the
      membrane potential and mitochondrial Hsp70 (mtHsp70) pulling from the
      matrix side, not ATP hydrolysis by TOMM20 itself. TOMM20 has no known
      ATPase catalytic activity. This annotation appears to be a misattribution
      of the overall translocation mechanism to the receptor subunit.
    action: REMOVE
    reason: >-
      TOMM20 does not possess ATPase activity. It is a receptor subunit that
      recognizes presequences via its TPR-like binding groove. The energy for
      protein translocation across the outer membrane comes from the membrane
      potential and mtHsp70 ATPase activity in the matrix, not from TOMM20.
      There is no evidence in PMID:14557246 or any other publication that
      TOMM20 itself has ATPase activity.
    supported_by:
      - reference_id: PMID:35733257
        supporting_text: >-
          Tom20, as the major import receptor, together with Tom70 and Tom22
          target mitochondrial precursor proteins in the cytosol precisely
- term:
    id: GO:0051082
    label: unfolded protein binding
  evidence_type: IDA
  original_reference_id: PMID:14557246
  review:
    summary: >-
      This annotation to GO:0051082 "unfolded protein binding" for TOMM20 is
      misleading and represents an over-annotation. The cited paper (Yano et al.
      2003, PMID:14557246) is primarily about AIP (arylhydrocarbon
      receptor-interacting protein), not Tom20. The paper demonstrates that AIP
      is the protein with chaperone-like activity that suppresses thermal
      aggregation of substrate proteins and binds unfolded proteins. Tom20 is
      shown to bind mitochondrial preproteins via their N-terminal presequences
      (targeting signals), not based on their folding state. The binding groove
      of Tom20 recognizes the hydrophobic face of amphiphilic helical
      presequences through hydrophobic interactions, which is a signal
      sequence recognition function, not an unfolded protein sensing function.
      The paper explicitly states that Tom20 binds preproteins and non-mitochondrial
      proteins were not bound, demonstrating specificity for mitochondrial targeting
      signals rather than unfolded protein states per se. Furthermore, TOMM20
      already has the correct and more specific annotation to GO:0030943
      "mitochondrion targeting sequence binding" (IDA from PMID:35733257 and
      IBA from GO_REF:0000033). The GO:0051082 term is being obsoleted
      (go-ontology issue 30962) precisely because it conflates signal recognition
      with chaperone activity. TOMM20 is a protein import receptor, not a
      chaperone.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      TOMM20 does not function as an unfolded protein binding chaperone. The
      evidence in PMID:14557246 shows Tom20 recognizes mitochondrial
      presequences via hydrophobic interactions with the amphiphilic helical
      targeting signal. The paper states: "The binding groove of Tom20 mainly
      consists of a TPR and a glutamine-rich segment, and hydrophobic residues
      in the groove interact with the hydrophobic face of the amphiphilic
      helical presequence" and "AIP as well as Tom20 binds specifically to
      mitochondrial preproteins" while "no or little binding of AIP and Tom20
      to proteins destined for other organelles" was observed. This
      demonstrates signal-specific recognition, not general unfolded protein
      binding. The chaperone-like aggregation suppression activity described in
      the paper belongs to AIP, not Tom20. TOMM20 already has the correct
      annotation GO:0030943 "mitochondrion targeting sequence binding" which
      accurately captures its molecular function. GO:0051082 is being
      obsoleted (go-ontology#30962) because it conflates distinct molecular
      mechanisms.
    proposed_replacement_terms:
      - id: GO:0030943
        label: mitochondrion targeting sequence binding
    additional_reference_ids:
      - PMID:35733257
    supported_by:
      - reference_id: PMID:14557246
        supporting_text: >-
          The binding groove of Tom20 mainly consists of a TPR and a
          glutamine-rich segment, and hydrophobic residues in the groove
          interact with the hydrophobic face of the amphiphilic helical
          presequence.
      - reference_id: PMID:14557246
        supporting_text: >-
          AIP as well as Tom20 binds specifically to mitochondrial
          preproteins [...] no or little binding of AIP and Tom20 to
          proteins destined for other organelles, including peroxisomes,
          ER, and nucleus, was observed.
      - reference_id: PMID:14557246
        supporting_text: >-
          AIP was found to function as a chaperone to suppress thermal
          aggregation of rhodanese and citrate synthase (Fig. 6). AIP may
          function as a chaperone to maintain mitochondria-targeted
          preproteins unfolded and to suppress their aggregation.
      - reference_id: PMID:14557246
        supporting_text: >-
          Preproteins with NH2-terminal presequences are initially
          recognized by the receptor Tom20, although preproteins with
          internal targeting signals such as carrier proteins are
          recognized preferentially by Tom70.
- term:
    id: GO:0070585
    label: protein localization to mitochondrion
  evidence_type: IDA
  original_reference_id: PMID:14557246
  review:
    summary: >-
      IDA annotation from PMID:14557246 (Yano et al. 2003). The paper
      demonstrates that Tom20 recognizes preproteins via their mitochondrial
      targeting sequences and is part of the TOM complex that facilitates
      protein import. GO:0070585 "protein localization to mitochondrion" is a
      broad process term that accurately describes the outcome of TOMM20
      activity. While more specific terms like GO:0006626 "protein targeting
      to mitochondrion" or GO:0030150 "protein import into mitochondrial
      matrix" are also appropriate, this broader term is not incorrect.
    action: ACCEPT
    reason: >-
      Correct. TOMM20 facilitates protein localization to the mitochondrion
      by recognizing mitochondrial targeting sequences. This is a core
      biological process for TOMM20.
    supported_by:
      - reference_id: PMID:14557246
        supporting_text: >-
          Preproteins with NH2-terminal presequences are initially recognized
          by the receptor Tom20
- term:
    id: GO:0005742
    label: mitochondrial outer membrane translocase complex
  evidence_type: NAS
  original_reference_id: PMID:7498524
  review:
    summary: >-
      NAS annotation from PMID:7498524 (Seki et al. 1995), one of the original
      papers identifying human TOMM20 (then called Mom19 homolog). The paper
      showed that the human Mom19 homolog is targeted to yeast mitochondria and
      specifically associates with the outer membrane receptor complex. This
      was the original identification of human TOMM20 as a TOM complex component.
    action: ACCEPT
    reason: >-
      Correct. This is the foundational paper identifying human TOMM20 as a
      component of the mitochondrial outer membrane translocase complex.
    supported_by:
      - reference_id: PMID:7498524
        supporting_text: >-
          the human Mom19 homolog is targeted to isolated yeast mitochondria
          and specifically associates with the outer membrane receptor complex,
          suggesting that indeed a mitochondrial import receptor was identified.
core_functions:
- description: >-
    TOMM20 is the primary presequence receptor of the TOM complex. Its cytosolic
    TPR-containing domain recognizes the hydrophobic face of amphiphilic helical
    N-terminal mitochondrial targeting sequences on nuclear-encoded preproteins,
    facilitating their transfer to TOMM22 and into the TOMM40 translocation pore
    for import into the mitochondrial matrix and inner membrane.
  molecular_function:
    id: GO:0030943
    label: mitochondrion targeting sequence binding
  directly_involved_in:
    - id: GO:0030150
      label: protein import into mitochondrial matrix
    - id: GO:0070585
      label: protein localization to mitochondrion
  locations:
    - id: GO:0005741
      label: mitochondrial outer membrane
  in_complex:
    id: GO:0005742
    label: mitochondrial outer membrane translocase complex
  supported_by:
    - reference_id: PMID:35733257
      supporting_text: >-
        both Tom20 and Tom22 were pulled down by the DHFR-EGFP protein fused
        with the presequence of subunit 9 of F0-ATPase (Su9) (42), but not by
        DHFR-EGFP protein without Su9, suggesting that Tom22 indeed forms a
        complex with the presequence as Tom20.
    - reference_id: PMID:14557246
      supporting_text: >-
        Preproteins with NH2-terminal presequences are initially recognized by
        the receptor Tom20, although preproteins with internal targeting signals
        such as carrier proteins are recognized preferentially by Tom70.
    - reference_id: PMID:7498524
      supporting_text: >-
        the human Mom19 homolog is targeted to isolated yeast mitochondria
        and specifically associates with the outer membrane receptor complex,
        suggesting that indeed a mitochondrial import receptor was identified.
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000024
  title: Manual transfer of experimentally-verified manual GO annotation data to orthologs
    by curator judgment of sequence similarity
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000043
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
    vocabulary mapping, accompanied by conservative changes to GO terms applied by
    UniProt
  findings: []
- id: GO_REF:0000052
  title: Gene Ontology annotation based on curation of immunofluorescence data
  findings: []
- id: GO_REF:0000107
  title: Automatic transfer of experimentally verified manual GO annotation data to
    orthologs using Ensembl Compara
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: PMID:14557246
  title: AIP is a mitochondrial import mediator that binds to both import receptor
    Tom20 and preproteins.
  findings: []
- id: PMID:15644312
  title: Dissection of the mitochondrial import and assembly pathway for human Tom40.
  findings: []
- id: PMID:18331822
  title: Identification of Tom5 and Tom6 in the preprotein translocase complex of
    human mitochondrial outer membrane.
  findings: []
- id: PMID:20231292
  title: Identification and characterization of mitochondrial targeting sequence of
    human apurinic/apyrimidinic endonuclease 1.
  findings: []
- id: PMID:20628368
  title: Tom70 mediates activation of interferon regulatory factor 3 on mitochondria.
  findings: []
- id: PMID:23455425
  title: Autophagosomes form at ER-mitochondria contact sites.
  findings: []
- id: PMID:25327288
  title: Selective VPS34 inhibitor blocks autophagy and uncovers a role for NCOA4
    in ferritin degradation and iron homeostasis in vivo.
  findings: []
- id: PMID:25997101
  title: QIL1 is a novel mitochondrial protein required for MICOS complex stability
    and cristae morphology.
  findings: []
- id: PMID:30021884
  title: Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry
    in Intact Cell Nuclei.
  findings: []
- id: PMID:32848200
  title: Ttm50 facilitates calpain activation by anchoring it to calcium stores and
    increasing its sensitivity to calcium.
  findings: []
- id: PMID:34800366
  title: Quantitative high-confidence human mitochondrial proteome and its dynamics
    in cellular context.
  findings: []
- id: PMID:35271311
  title: 'OpenCell: Endogenous tagging for the cartography of human cellular organization.'
  findings: []
- id: PMID:35733257
  title: Structural basis of Tom20 and Tom22 cytosolic domains as the human TOM complex
    receptors.
  findings: []
- id: PMID:38848361
  title: Mechanism of human PINK1 activation at the TOM complex in a reconstituted
    system.
  findings: []
- id: PMID:7498524
  title: A human homolog of the mitochondrial protein import receptor Mom19 can assemble
    with the yeast mitochondrial receptor complex.
  findings: []
- id: Reactome:R-HSA-5205649
  title: p62 links damaged mitochondria to LC3
  findings: []
- id: Reactome:R-HSA-5205661
  title: Pink1 is recruited from the cytoplasm to the mitochondria
  findings: []
- id: Reactome:R-HSA-5205663
  title: LC3 binds the autophagosome membrane Atg5-Atg12 complex
  findings: []
- id: Reactome:R-HSA-5205673
  title: p62 binds ubiquitinated mitochondrial substrates
  findings: []
- id: Reactome:R-HSA-5696872
  title: USP30 deubiquitinates Ub-MOM proteins
  findings: []
- id: Reactome:R-HSA-9824888
  title: OPTN, TBK1 bind ubiquitinated MOM proteins
  findings: []
- id: Reactome:R-HSA-9824892
  title: MAP1LC3B binds p-S-OPTN bound to Ub-mitochondria
  findings: []
- id: Reactome:R-HSA-9824894
  title: TBK1 is phosphorylated within TBK1:OPTN:Ub-mitochondrial proteins
  findings: []
- id: Reactome:R-HSA-9824897
  title: p-S-TBK1 phosphorylates OPTN
  findings: []
- id: Reactome:R-HSA-9834070
  title: PRKN ubiquitinates MOM substrates
  findings: []
- id: Reactome:R-HSA-9834945
  title: PINK1 phosphorylates Ub on MOM proteins
  findings: []
- id: Reactome:R-HSA-9835009
  title: PRKN binds p-S-Ub:MOM proteins
  findings: []
- id: Reactome:R-HSA-9835011
  title: PINK1 phosphorylates PRKN at S65
  findings: []
- id: Reactome:R-HSA-9840807
  title: OPTN binds ATG9A
  findings: []