id: O94777
gene_symbol: DPM2
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  DPM2 is the small (84-residue), multi-pass endoplasmic reticulum (ER) membrane
  regulatory subunit of the dolichol-phosphate mannose (Dol-P-Man) synthase complex,
  which is composed of the catalytic subunit DPM1 together with DPM2 and DPM3.
  DPM2 is non-catalytic: it stabilizes the complex and enhances its activity rather
  than performing the mannosyltransfer itself. DPM2 forms a complex with DPM1 that is
  required for the correct ER localization and stable expression of DPM1, stabilizes
  DPM3, and enhances the enzyme's binding of the substrate dolichyl phosphate,
  increasing Dol-P-Man synthase activity roughly ten-fold. Dol-P-Man is the mannosyl
  donor used for glycosylphosphatidylinositol (GPI) anchor synthesis, the
  dolichol-linked oligosaccharide precursor of N-glycosylation, and protein O- and
  C-mannosylation. DPM2 additionally associates with, and enhances the activity of,
  the GPI-N-acetylglucosaminyltransferase (GPI-GnT) complex that initiates GPI-anchor
  biosynthesis, although it is not essential for that complex. In humans, loss-of-function
  variants cause DPM2-CDG (congenital disorder of glycosylation type Iu), a muscular
  dystrophy-dystroglycanopathy with severe epilepsy.
existing_annotations:
- term:
    id: GO:0005783
    label: endoplasmic reticulum
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: >-
      Phylogenetic (IBA) assignment that DPM2 is active in the endoplasmic reticulum.
      This is correct but less specific than the well-supported ER membrane
      localization; retained as an accurate, broader localization.
    action: ACCEPT
    reason: >-
      DPM2 is an ER membrane protein and the Dol-P-Man synthase complex acts in the
      ER. The more specific GO:0005789 (ER membrane) is separately annotated and
      preferred for the core localization.
    supported_by:
    - reference_id: PMID:9724629
      supporting_text: >-
        DPM2, an 84 amino acid
    - reference_id: file:human/DPM2/DPM2-uniprot.txt
      supporting_text: >-
        Endoplasmic reticulum membrane; Multi-pass
- term:
    id: GO:0006488
    label: dolichol-linked oligosaccharide biosynthetic process
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: >-
      Phylogenetic (IBA) assignment linking DPM2 to biosynthesis of the
      dolichol-linked oligosaccharide N-glycan precursor. Dol-P-Man produced by the
      DPM synthase complex is the mannosyl donor for elongation of the lipid-linked
      oligosaccharide, so DPM2's regulatory role is upstream of and required for this
      process.
    action: ACCEPT
    reason: >-
      Consistent with the established role of Dol-P-Man synthase in supplying mannose
      to the dolichol-linked oligosaccharide (LLO) pathway.
    supported_by:
    - reference_id: PMID:10835346
      supporting_text: >-
        Dolichol-phosphate-mannose (DPM) synthase generates mannosyl donors for
- term:
    id: GO:0033185
    label: dolichol-phosphate-mannose synthase complex
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: part_of
  review:
    summary: >-
      Phylogenetic (IBA) assignment of DPM2 as part of the dolichol-phosphate-mannose
      synthase complex. This is the core structural context of DPM2 and is strongly
      supported experimentally.
    action: ACCEPT
    reason: >-
      DPM2 is a bona fide subunit of the three-subunit human DPM synthase complex
      (DPM1/DPM2/DPM3).
    supported_by:
    - reference_id: PMID:10835346
      supporting_text: >-
        mammalian DPM synthase contains catalytic DPM1 and regulatory DPM2
- term:
    id: GO:0030234
    label: enzyme regulator activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: >-
      Phylogenetic (IBA) assignment of enzyme regulator activity, capturing DPM2's
      non-catalytic regulatory role in the DPM synthase complex. DPM2 enhances DPM
      synthase activity and substrate (dolichyl phosphate) binding without itself
      being catalytic.
    action: ACCEPT
    reason: >-
      Matches the experimentally supported function of DPM2 as a regulatory subunit.
      The more specific GO:0008047 (enzyme activator activity), separately annotated
      by IDA, better reflects the activating nature of this regulation.
    supported_by:
    - reference_id: PMID:10835346
      supporting_text: >-
        DPM synthase activity was 10 times
    - reference_id: PMID:9724629
      supporting_text: >-
        DPM2 enhances binding of dolichol phosphate, a substrate of DPM
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  review:
    summary: >-
      Electronic (IEA) assignment of ER membrane localization from InterPro/UniProt
      subcellular-location mapping. Correct and consistent with the experimentally
      determined multi-pass ER membrane topology of DPM2.
    action: ACCEPT
    reason: >-
      DPM2 is a multi-pass ER membrane protein; this is the core cellular location.
    supported_by:
    - reference_id: file:human/DPM2/DPM2-uniprot.txt
      supporting_text: >-
        Endoplasmic reticulum membrane; Multi-pass
- term:
    id: GO:0030234
    label: enzyme regulator activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: >-
      Electronic (IEA) InterPro2GO assignment of enzyme regulator activity based on
      the DPM2 domain (IPR009914). Consistent with the experimental IDA/IBA evidence
      for DPM2's regulatory role.
    action: ACCEPT
    reason: >-
      Correct molecular-function class for the DPM2 regulatory subunit; the more
      specific enzyme activator activity (GO:0008047) is also annotated.
    supported_by:
    - reference_id: PMID:10835346
      supporting_text: >-
        mammalian DPM synthase contains catalytic DPM1 and regulatory DPM2
- term:
    id: GO:0180047
    label: dolichol phosphate mannose biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: >-
      Electronic (IEA) InterPro2GO assignment to Dol-P-Man biosynthesis. This is the
      core biological process that the DPM synthase complex, and hence DPM2 as its
      regulatory subunit, carries out.
    action: ACCEPT
    reason: >-
      Directly matches DPM2's function as regulatory subunit of Dol-P-Man synthase;
      also supported by an experimental IDA annotation (PMID:10835346).
    supported_by:
    - reference_id: PMID:9724629
      supporting_text: >-
        DPM2 enhances binding of dolichol phosphate, a substrate of DPM
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:10835346
  qualifier: enables
  review:
    summary: >-
      IPI protein-binding annotation from co-purification/interaction of DPM2 with
      DPM3 (UniProtKB:Q9P2X0) in the DPM synthase complex. The interaction is real and
      biologically meaningful for complex assembly, but the bare "protein binding"
      term is uninformative about molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Per curation guidelines, bare protein binding (GO:0005515) is uninformative and
      is not retained as a core function. The underlying DPM2-DPM3 interaction is
      better captured by complex membership (GO:0033185) and by enzyme regulator/
      activator activity. Experimental IPI is kept, not removed.
    supported_by:
    - reference_id: PMID:10835346
      supporting_text: >-
        with DPM2 via its N-terminal portion
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:10944123
  qualifier: enables
  review:
    summary: >-
      IPI protein-binding annotations from interactions of DPM2 with GPI-GnT
      components (PIGA/P37287, PIGC/Q92535, PIGQ/Q9BRB3). These interactions underlie
      DPM2's association with, and enhancement of, the GPI-GnT complex, but the bare
      term itself is uninformative.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Bare protein binding is not retained as a core function per curation guidelines.
      The interactions are more informatively represented by GPI-GnT complex
      membership (GO:0000506) and enzyme regulator activity. Experimental IPI kept.
    supported_by:
    - reference_id: PMID:10944123
      supporting_text: >-
        associates with GPI-GnT through interactions with PIG-A, PIG-C and
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:16162815
  qualifier: enables
  review:
    summary: >-
      IPI protein-binding annotation from DPM2's identification as a component of the
      seven-subunit GPI-GnT complex (with PIGA/P37287). Real interaction but the bare
      term is uninformative.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      Bare protein binding is not retained as a core function per curation guidelines;
      complex membership (GO:0000506) captures the biology. Experimental IPI kept.
    supported_by:
    - reference_id: PMID:16162815
      supporting_text: >-
        complex GPI-N-acetylglucosaminyltransferase (GPI-GnT)
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: NAS
  original_reference_id: PMID:9724629
  qualifier: located_in
  review:
    summary: >-
      NAS assignment of ER membrane localization based on the original DPM2
      characterization. DPM2 was shown to be an ER-expressed membrane protein.
    action: ACCEPT
    reason: >-
      Consistent with experimental IDA/IEA support for ER membrane localization; this
      is the core cellular location of DPM2.
    supported_by:
    - reference_id: PMID:9724629
      supporting_text: >-
        DPM2, an 84 amino acid
- term:
    id: GO:0033185
    label: dolichol-phosphate-mannose synthase complex
  evidence_type: IPI
  original_reference_id: PMID:10835346
  qualifier: part_of
  review:
    summary: >-
      IPI (ComplexPortal) annotation of DPM2 as part of the DPM synthase complex,
      based on the physical characterization of the three-subunit human complex. This
      is a core annotation for DPM2.
    action: ACCEPT
    reason: >-
      Direct experimental support for DPM2 membership in the DPM1/DPM2/DPM3 complex.
    supported_by:
    - reference_id: PMID:10835346
      supporting_text: >-
        The third subunit, DPM3, comprises 92 amino acids associated with DPM1
- term:
    id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:10835346
  qualifier: involved_in
  review:
    summary: >-
      IDA annotation to "dolichyl monophosphate biosynthetic process". PMID:10835346
      concerns dolichol-phosphate-MANNOSE (Dol-P-Man) synthesis, i.e. the transfer of
      mannose onto dolichyl phosphate, rather than the biosynthesis of dolichyl
      monophosphate itself. The chosen term is therefore an imprecise/misleading match
      for the underlying experiment.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      DPM2 regulates addition of mannose to dolichyl phosphate to form Dol-P-Man; it
      is not shown to be involved in synthesis of the dolichyl monophosphate acceptor.
      Kept (experimental, not removed) but flagged; the accurate BP is GO:0180047
      (dolichol phosphate mannose biosynthetic process), which is separately annotated.
    supported_by:
    - reference_id: PMID:10835346
      supporting_text: >-
        Dolichol-phosphate-mannose (DPM) synthase generates mannosyl donors for
- term:
    id: GO:0180047
    label: dolichol phosphate mannose biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:10835346
  qualifier: involved_in
  review:
    summary: >-
      IDA annotation to Dol-P-Man biosynthesis, the core biological process of the
      DPM synthase complex. DPM2 was shown to be required for and to enhance this
      activity (~10-fold), and to be required for the ER localization/stability of the
      catalytic subunit DPM1.
    action: ACCEPT
    reason: >-
      Strong experimental support; this is the central biological process DPM2
      participates in as regulatory subunit of Dol-P-Man synthase.
    supported_by:
    - reference_id: PMID:10835346
      supporting_text: >-
        DPM synthase activity was 10 times
    - reference_id: PMID:9724629
      supporting_text: >-
        that is essential for the ER localization and stable expression of
- term:
    id: GO:0000506
    label: glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT)
      complex
  evidence_type: IPI
  original_reference_id: PMID:16162815
  qualifier: part_of
  review:
    summary: >-
      IPI (ComplexPortal) annotation of DPM2 as a component of the GPI-GnT complex.
      DPM2 co-purifies with the GPI-GnT machinery, but it is a secondary/moonlighting
      membership: DPM2 is not essential for GPI-GnT and its primary role is in the DPM
      synthase complex.
    action: KEEP_AS_NON_CORE
    reason: >-
      Real, experimentally supported association, but non-core relative to DPM2's
      primary role as regulatory subunit of Dol-P-Man synthase; DPM2 is dispensable
      for GPI-GnT activity (though it enhances it).
    supported_by:
    - reference_id: PMID:16162815
      supporting_text: >-
        complex GPI-N-acetylglucosaminyltransferase (GPI-GnT)
    - reference_id: PMID:10944123
      supporting_text: >-
        indicating that DPM2 is not essential for GPI-GnT; however, the enzyme activity
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: IDA
  original_reference_id: PMID:16162815
  qualifier: located_in
  review:
    summary: >-
      IDA (ComplexPortal) annotation of ER membrane localization, consistent with the
      ER-membrane topology of DPM2 and the ER location of the GPI-GnT and DPM synthase
      complexes.
    action: ACCEPT
    reason: >-
      Core cellular location, well supported across multiple lines of evidence.
    supported_by:
    - reference_id: file:human/DPM2/DPM2-uniprot.txt
      supporting_text: >-
        Endoplasmic reticulum membrane; Multi-pass
- term:
    id: GO:0000506
    label: glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT)
      complex
  evidence_type: IDA
  original_reference_id: PMID:16162815
  qualifier: part_of
  review:
    summary: >-
      IDA (UniProt) annotation of DPM2 as a component of the GPI-GnT complex, from the
      seven-component characterization of GPI-GnT (PIGA/PIGC/PIGH/PIGP/PIGQ/PIGY/DPM2).
      Secondary/moonlighting membership relative to DPM2's DPM-synthase role.
    action: KEEP_AS_NON_CORE
    reason: >-
      Experimentally supported but non-core; DPM2 is not essential for GPI-GnT.
    supported_by:
    - reference_id: PMID:16162815
      supporting_text: >-
        complex GPI-N-acetylglucosaminyltransferase (GPI-GnT)
- term:
    id: GO:0006506
    label: GPI anchor biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:16162815
  qualifier: involved_in
  review:
    summary: >-
      IDA annotation linking DPM2 to GPI anchor biosynthesis via its membership in
      GPI-GnT, the first enzyme of the GPI pathway. This is a genuine but secondary
      role; DPM2 also contributes to GPI biosynthesis indirectly by supplying Dol-P-Man
      as a mannosyl donor.
    action: KEEP_AS_NON_CORE
    reason: >-
      Real involvement but non-core; DPM2 enhances rather than is essential for
      GPI-GnT, and its core role is Dol-P-Man synthesis.
    supported_by:
    - reference_id: PMID:10944123
      supporting_text: >-
        DPM2, which regulates
    - reference_id: PMID:16162815
      supporting_text: >-
        Biosynthesis of glycosylphosphatidylinositol (GPI) is initiated by an unusually
- term:
    id: GO:0008047
    label: enzyme activator activity
  evidence_type: IDA
  original_reference_id: PMID:10835346
  qualifier: enables
  review:
    summary: >-
      IDA annotation of enzyme activator activity. DPM2 increases Dol-P-Man synthase
      activity ~10-fold and enhances dolichyl phosphate substrate binding, acting as a
      positive (activating) regulator of the catalytic DPM1 subunit. This is the most
      precise molecular-function term for DPM2.
    action: ACCEPT
    reason: >-
      Directly supported by the ~10x activation of DPM synthase in the presence of
      DPM2 and by enhanced substrate (dolichyl phosphate) binding; this is DPM2's core
      molecular function.
    supported_by:
    - reference_id: PMID:10835346
      supporting_text: >-
        DPM synthase activity was 10 times
    - reference_id: PMID:9724629
      supporting_text: >-
        DPM2 enhances binding of dolichol phosphate, a substrate of DPM
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-4719375
  qualifier: located_in
  review:
    summary: >-
      TAS (Reactome) ER membrane localization from the "Defective DPM2 does not
      transfer mannose to DOLP to form DOLPman" reaction. Correct localization.
    action: ACCEPT
    reason: >-
      Consistent with the well-established ER membrane localization of DPM2.
    supported_by:
    - reference_id: file:human/DPM2/DPM2-uniprot.txt
      supporting_text: >-
        Endoplasmic reticulum membrane; Multi-pass
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-162721
  qualifier: located_in
  review:
    summary: >-
      TAS (Reactome) ER membrane localization from the dolichyl phosphate +
      GDP-mannose -> Dol-P-Man reaction. Correct localization.
    action: ACCEPT
    reason: >-
      Consistent with the ER membrane localization of DPM2 and the DPM synthase
      complex.
    supported_by:
    - reference_id: file:human/DPM2/DPM2-uniprot.txt
      supporting_text: >-
        Endoplasmic reticulum membrane; Multi-pass
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-162730
  qualifier: located_in
  review:
    summary: >-
      TAS (Reactome) ER membrane localization from the GPI-GnT reaction
      (PI + UDP-GlcNAc -> GlcNAc-PI + UDP). Correct localization.
    action: ACCEPT
    reason: >-
      Consistent with the ER membrane localization of DPM2 and the GPI-GnT complex.
    supported_by:
    - reference_id: file:human/DPM2/DPM2-uniprot.txt
      supporting_text: >-
        Endoplasmic reticulum membrane; Multi-pass
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-4717406
  qualifier: located_in
  review:
    summary: >-
      TAS (Reactome) ER membrane localization from the "Defective DPM1 does not
      transfer mannose to DOLP to form DOLPman" reaction. Correct localization.
    action: ACCEPT
    reason: >-
      Consistent with the ER membrane localization of DPM2.
    supported_by:
    - reference_id: file:human/DPM2/DPM2-uniprot.txt
      supporting_text: >-
        Endoplasmic reticulum membrane; Multi-pass
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-4719354
  qualifier: located_in
  review:
    summary: >-
      TAS (Reactome) ER membrane localization from the "Defective DPM3 does not
      transfer mannose to DOLP to form DOLPman" reaction. Correct localization.
    action: ACCEPT
    reason: >-
      Consistent with the ER membrane localization of DPM2.
    supported_by:
    - reference_id: file:human/DPM2/DPM2-uniprot.txt
      supporting_text: >-
        Endoplasmic reticulum membrane; Multi-pass
- term:
    id: GO:0000506
    label: glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT)
      complex
  evidence_type: IDA
  original_reference_id: PMID:10944123
  qualifier: part_of
  review:
    summary: >-
      IDA (MGI) annotation of DPM2 as a component of the GPI-GnT complex, from the
      demonstration that DPM2 associates with GPI-GnT via PIG-A, PIG-C and GPI1.
      Secondary/moonlighting membership.
    action: KEEP_AS_NON_CORE
    reason: >-
      Experimentally supported but non-core relative to DPM2's DPM synthase role;
      DPM2 is not essential for GPI-GnT.
    supported_by:
    - reference_id: PMID:10944123
      supporting_text: >-
        associates with GPI-GnT through interactions with PIG-A, PIG-C and
- term:
    id: GO:0033185
    label: dolichol-phosphate-mannose synthase complex
  evidence_type: IDA
  original_reference_id: PMID:10835346
  qualifier: part_of
  review:
    summary: >-
      IDA (UniProt) annotation of DPM2 as part of the DPM synthase complex, from the
      physical characterization of the three-subunit human complex. Core annotation.
    action: ACCEPT
    reason: >-
      Directly supported experimental evidence for DPM2 membership in the DPM1/DPM2/
      DPM3 complex.
    supported_by:
    - reference_id: PMID:10835346
      supporting_text: >-
        mammalian DPM synthase contains catalytic DPM1 and regulatory DPM2
- term:
    id: GO:0000506
    label: glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT)
      complex
  evidence_type: TAS
  original_reference_id: PMID:16280320
  qualifier: part_of
  review:
    summary: >-
      TAS annotation of GPI-GnT complex membership. PMID:16280320 focuses on DPM3
      tethering/stabilizing DPM1 and notes DPM3 was co-purified with DPM1 and DPM2;
      the GPI-GnT membership of DPM2 is more directly established elsewhere
      (PMID:10944123, PMID:16162815). Secondary/moonlighting membership.
    action: KEEP_AS_NON_CORE
    reason: >-
      Real but non-core association; DPM2's primary complex is the DPM synthase
      complex.
    supported_by:
    - reference_id: PMID:16280320
      supporting_text: >-
        co-purified with DPM1 and DPM2
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: PMID:16280320
  qualifier: located_in
  review:
    summary: >-
      TAS ER membrane localization. Consistent with the ER-membrane setting of the DPM
      synthase and GPI-GnT complexes.
    action: ACCEPT
    reason: >-
      Consistent with the well-established ER membrane localization of DPM2.
    supported_by:
    - reference_id: PMID:16280320
      supporting_text: >-
        tethered
    - reference_id: file:human/DPM2/DPM2-uniprot.txt
      supporting_text: >-
        Endoplasmic reticulum membrane; Multi-pass
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: PMID:9724629
  qualifier: located_in
  review:
    summary: >-
      TAS ER membrane localization from the original DPM2 characterization, which
      described DPM2 as an ER-expressed membrane protein.
    action: ACCEPT
    reason: >-
      Core cellular location, supported by the primary DPM2 paper and consistent with
      multi-pass ER membrane topology.
    supported_by:
    - reference_id: PMID:9724629
      supporting_text: >-
        DPM2, an 84 amino acid
    - reference_id: file:human/DPM2/DPM2-uniprot.txt
      supporting_text: >-
        Endoplasmic reticulum membrane; Multi-pass
core_functions:
- description: >-
    Regulatory (non-catalytic) subunit of the dolichol-phosphate mannose (Dol-P-Man)
    synthase complex. As an activating regulator, DPM2 stabilizes the complex
    (required for ER localization/stability of catalytic DPM1 and for DPM3 stability),
    enhances binding of the dolichyl phosphate substrate, and increases Dol-P-Man
    synthase activity ~10-fold, thereby driving Dol-P-Man biosynthesis in the ER
    membrane. Dol-P-Man is the mannosyl donor for N-glycosylation, GPI-anchor
    synthesis, and protein O-/C-mannosylation.
  molecular_function:
    id: GO:0008047
    label: enzyme activator activity
  directly_involved_in:
  - id: GO:0180047
    label: dolichol phosphate mannose biosynthetic process
  - id: GO:0006488
    label: dolichol-linked oligosaccharide biosynthetic process
  locations:
  - id: GO:0005789
    label: endoplasmic reticulum membrane
  in_complex:
    id: GO:0033185
    label: dolichol-phosphate-mannose synthase complex
  supported_by:
  - reference_id: PMID:9724629
    supporting_text: >-
      that is essential for the ER localization and stable expression of
  - reference_id: PMID:9724629
    supporting_text: >-
      DPM2 enhances binding of dolichol phosphate, a substrate of DPM
  - reference_id: PMID:10835346
    supporting_text: >-
      DPM synthase activity was 10 times
  - reference_id: PMID:10835346
    supporting_text: >-
      mammalian DPM synthase contains catalytic DPM1 and regulatory DPM2
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: file:human/DPM2/DPM2-uniprot.txt
  title: UniProtKB entry O94777 (DPM2_HUMAN)
  findings: []
- id: PMID:10835346
  title: Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1,
    DPM2 and DPM3.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Primary paper establishing the three-subunit human DPM synthase (DPM1 catalytic,
      DPM2 and DPM3 regulatory/stabilizing) and DPM2's ~10x enhancement of activity.
      Abstract-only cache (full_text_available: false); claims anchored to the abstract.
- id: PMID:10944123
  title: Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P
    and is regulated by DPM2.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Establishes DPM2's association with, and ~3x enhancement of, GPI-GnT (via PIG-A,
      PIG-C, GPI1), while showing DPM2 is not essential for GPI-GnT.
- id: PMID:16162815
  title: The initial enzyme for glycosylphosphatidylinositol biosynthesis requires
    PIG-Y, a seventh component.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      Characterizes the seven-component GPI-GnT (including DPM2); primary focus is
      PIG-Y. Supports DPM2's GPI-GnT complex membership.
- id: PMID:16280320
  title: DPM1, the catalytic subunit of dolichol-phosphate mannose synthase, is tethered
    to and stabilized on the endoplasmic reticulum membrane by DPM3.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      Primarily about DPM3 tethering/stabilizing DPM1; confirms DPM3 co-purifies with
      DPM1 and DPM2 in the DPM synthase complex.
- id: PMID:9724629
  title: 'DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells:
    correct subcellular localization and stabilization of DPM1, and binding of dolichol
    phosphate.'
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Original DPM2 characterization: ER membrane protein that complexes with DPM1,
      required for DPM1 ER localization/stability, and enhances dolichyl phosphate
      binding. Abstract-only cache; claims anchored to abstract.
- id: Reactome:R-HSA-162721
  title: dolichyl phosphate + GDP-alpha-D-mannose -> dolichyl phosphate D-mannose
  findings: []
- id: Reactome:R-HSA-162730
  title: phosphatidylinositol + UDP-N-acetyl-D-glucosamine -> N-acetylglucosaminyl-PI
    + UDP
  findings: []
- id: Reactome:R-HSA-4717406
  title: Defective DPM1 does not transfer mannose to DOLP to form DOLPman
  findings: []
- id: Reactome:R-HSA-4719354
  title: Defective DPM3 does not transfer mannose to DOLP to form DOLPman
  findings: []
- id: Reactome:R-HSA-4719375
  title: Defective DPM2 does not transfer mannose to DOLP to form DOLPman
  findings: []