id: Q9UPQ8
gene_symbol: DOLK
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  DOLK is dolichol kinase, a polytopic endoplasmic reticulum membrane enzyme that
  catalyzes the CTP-dependent phosphorylation of dolichol to dolichyl monophosphate
  (Dol-P), the terminal step in de novo Dol-P biosynthesis (EC 2.7.1.108). Dol-P is
  the essential lipid carrier that primes assembly of the dolichol-linked
  oligosaccharide for protein N-linked glycosylation and is also required for
  O-mannosylation, C-mannosylation and GPI-anchor biosynthesis, so DOLK supplies the
  activated lipid carrier used throughout the glycosylation system. The enzyme has a
  cytoplasmically oriented CTP-binding site and belongs to the polyprenol kinase
  family. Loss-of-function mutations cause DOLK-CDG (congenital disorder of
  glycosylation type Im), whose features include dilated cardiomyopathy (linked to
  deficient alpha-dystroglycan O-mannosylation), ichthyosis and neurological disease.
existing_annotations:
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: >-
      Phylogenetically inferred ER membrane localization, consistent with the
      experimentally demonstrated ER membrane localization of human dolichol kinase
      and its yeast ortholog SEC59.
    action: ACCEPT
    reason: >-
      DOLK is an experimentally validated polytopic ER membrane protein (PMID:16923818),
      so the IBA localization is correct and represents a core aspect of where the
      enzyme acts.
    supported_by:
    - reference_id: PMID:16923818
      supporting_text: >-
        shown to be a polytopic membrane protein localized in the endoplasmic
        reticulum with an N terminus extended into the lumen and a cytoplasmically
        oriented C terminus.
- term:
    id: GO:0004168
    label: dolichol kinase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: >-
      Phylogenetically inferred dolichol kinase activity, the defining and
      experimentally established molecular function of DOLK.
    action: ACCEPT
    reason: >-
      This is the core molecular function of the gene, directly demonstrated
      biochemically (PMID:12213788, PMID:16923818) and by disease-variant enzyme
      assays (PMID:17273964, PMID:22242004). GOA carries this exact current term
      (GO:0004168, EC 2.7.1.108).
    supported_by:
    - reference_id: PMID:12213788
      supporting_text: >-
        Dolichol kinase (DK) catalyzes the CTP-mediated phosphorylation of dolichol
        in eukaryotic cells, the terminal step in dolichyl monophosphate (Dol-P)
        biosynthesis de novo.
- term:
    id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: >-
      Phylogenetically inferred involvement in dolichyl monophosphate (Dol-P)
      biosynthesis, the pathway output of the dolichol kinase reaction.
    action: ACCEPT
    reason: >-
      Dol-P biosynthesis is the direct biological process to which the DOLK reaction
      contributes; this is well supported experimentally and the IBA is at an
      appropriate level of specificity.
    supported_by:
    - reference_id: PMID:12213788
      supporting_text: >-
        the terminal step in dolichyl monophosphate (Dol-P) biosynthesis de novo.
- term:
    id: GO:0004168
    label: dolichol kinase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: >-
      Automated annotation of dolichol kinase activity from the RHEA/EC mapping
      (RHEA:13133, EC 2.7.1.108).
    action: ACCEPT
    reason: >-
      The EC/RHEA mapping is exactly correct for DOLK and matches the experimentally
      established catalytic activity. The reaction is documented in UniProt.
    supported_by:
    - reference_id: file:human/DOLK/DOLK-uniprot.txt
      supporting_text: >-
        Reaction=a di-trans,poly-cis-dolichol + CTP = a di-trans,poly-cis-
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: >-
      Automated ER membrane localization from the UniProt subcellular-location
      keyword mapping, consistent with experimental data.
    action: ACCEPT
    reason: >-
      DOLK is an experimentally confirmed integral ER membrane protein; the SubCell
      mapping is accurate.
    supported_by:
    - reference_id: file:human/DOLK/DOLK-uniprot.txt
      supporting_text: >-
        SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25416956
  qualifier: enables
  review:
    summary: >-
      Interactor identified in a proteome-scale binary interactome map. The generic
      "protein binding" term is uninformative about DOLK's actual molecular function.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      This annotation comes from a large-scale high-throughput interactome screen and
      only asserts the uninformative term GO:0005515 protein binding. Per curation
      guidelines this term should not be treated as core function; the physiologically
      meaningful function is dolichol kinase activity. Retained as an experimental IPI
      rather than removed.
    supported_by:
    - reference_id: PMID:25416956
      supporting_text: A proteome-scale map of the human interactome network.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:26871637
  qualifier: enables
  review:
    summary: >-
      Interactor reported in a large-scale alternative-splicing interactome study;
      the term is uninformative for DOLK function.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      High-throughput protein-protein interaction annotation using the generic
      GO:0005515 term. It does not inform the molecular function of DOLK and is not a
      core annotation. Retained as an experimental IPI.
    supported_by:
    - reference_id: PMID:26871637
      supporting_text: >-
        Widespread Expansion of Protein Interaction Capabilities by Alternative
        Splicing.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:28514442
  qualifier: enables
  review:
    summary: >-
      Interactors reported in a large-scale interactome map (e.g. KCNA6, LRRC4C);
      the generic term is uninformative for DOLK function.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      High-throughput interactome annotation using the uninformative GO:0005515 term.
      DOLK's interactors here are largely co-resident ER membrane proteins and the
      binding data do not establish a specific molecular function. Retained as an
      experimental IPI.
    supported_by:
    - reference_id: PMID:28514442
      supporting_text: >-
        Architecture of the human interactome defines protein communities and disease
        networks.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32296183
  qualifier: enables
  review:
    summary: >-
      Multiple interactors reported in the HuRI binary interactome map; the generic
      term is uninformative for DOLK function.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      High-throughput binary interactome annotation using the uninformative GO:0005515
      term. The many interactors (largely ER/membrane proteins) do not define a
      specific molecular function for DOLK. Retained as an experimental IPI.
    supported_by:
    - reference_id: PMID:32296183
      supporting_text: A reference map of the human binary protein interactome.
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:33961781
  qualifier: enables
  review:
    summary: >-
      Interactors reported in a proteome-scale AP-MS network study; the generic term
      is uninformative for DOLK function.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      High-throughput proteome-scale interaction annotation using the uninformative
      GO:0005515 term. Does not inform DOLK molecular function and is not core.
      Retained as an experimental IPI.
    supported_by:
    - reference_id: PMID:33961781
      supporting_text: >-
        Dual proteome-scale networks reveal cell-specific remodeling of the human
        interactome.
- term:
    id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-446199
  qualifier: involved_in
  review:
    summary: >-
      Reactome-asserted involvement in dolichyl phosphate synthesis, matching the
      enzyme's pathway role.
    action: ACCEPT
    reason: >-
      DOLK catalyzes the terminal step producing Dol-P; the Reactome pathway
      "Synthesis of dolichyl-phosphate" correctly captures this biological process.
    supported_by:
    - reference_id: PMID:12213788
      supporting_text: >-
        the terminal step in dolichyl monophosphate (Dol-P) biosynthesis de novo.
- term:
    id: GO:0004168
    label: dolichol kinase activity
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-446195
  qualifier: enables
  review:
    summary: >-
      Reactome-asserted dolichol kinase activity (DOLK phosphorylates dolichol to
      Dol-P), matching the core molecular function.
    action: ACCEPT
    reason: >-
      Correct assignment of the enzyme's defining catalytic activity, corroborated by
      biochemical assays.
    supported_by:
    - reference_id: PMID:16923818
      supporting_text: >-
        Human dolichol kinase, a polytopic endoplasmic reticulum membrane protein with
        a cytoplasmically oriented CTP-binding site.
- term:
    id: GO:0004168
    label: dolichol kinase activity
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-4755600
  qualifier: enables
  review:
    summary: >-
      Reactome-asserted dolichol kinase activity (disease-annotated reaction),
      matching the core molecular function.
    action: ACCEPT
    reason: >-
      Correct assignment of the defining catalytic activity of DOLK.
    supported_by:
    - reference_id: PMID:16923818
      supporting_text: >-
        Human dolichol kinase, a polytopic endoplasmic reticulum membrane protein with
        a cytoplasmically oriented CTP-binding site.
- term:
    id: GO:0005730
    label: nucleolus
  evidence_type: IDA
  original_reference_id: GO_REF:0000052
  qualifier: located_in
  review:
    summary: >-
      Single high-throughput immunofluorescence (HPA) annotation to the nucleolus,
      inconsistent with the well-established integral ER membrane localization of this
      polytopic membrane kinase.
    action: MARK_AS_OVER_ANNOTATED
    reason: >-
      DOLK is a ~15-pass integral ER membrane protein (PMID:16923818); a nucleolar
      localization is biologically implausible for its function and is contradicted by
      IDA, IBA, IEA and Reactome ER membrane annotations. This is most likely
      background/off-target signal in the HPA immunofluorescence screen. Not removed
      (single experimental IF datum) but flagged as over-annotation.
    supported_by:
    - reference_id: PMID:16923818
      supporting_text: >-
        shown to be a polytopic membrane protein localized in the endoplasmic
        reticulum with an N terminus extended into the lumen and a cytoplasmically
        oriented C terminus.
- term:
    id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  evidence_type: IGI
  original_reference_id: PMID:12213788
  qualifier: involved_in
  review:
    summary: >-
      Genetic interaction evidence: human DOLK (hDK1) complements the yeast sec59-1
      (SEC59/dolichol kinase) mutant, restoring dolichol kinase activity, Dol-P levels
      and N-glycosylation, establishing its role in Dol-P biosynthesis.
    action: ACCEPT
    reason: >-
      Cross-species complementation (with yeast SEC59, UniProtKB:P20048) demonstrates
      DOLK functions in de novo Dol-P biosynthesis. This is a well-supported core
      biological process annotation.
    supported_by:
    - reference_id: PMID:12213788
      supporting_text: >-
        hDK1 is capable of complementing the growth defect, elevating DK activity, and
        consequently increasing Dol-P levels in vivo and restoring normal
        N-glycosylation of carboxypeptidase Y at the restrictive temperature in the
        temperature-sensitive mutant sec59-1.
- term:
    id: GO:0004168
    label: dolichol kinase activity
  evidence_type: EXP
  original_reference_id: PMID:17273964
  qualifier: enables
  review:
    summary: >-
      Experimental demonstration of dolichol kinase activity via disease-variant
      characterization: CDG1M variants Cys99Ser and Tyr441Ser have only 2-4% residual
      DK activity.
    action: ACCEPT
    reason: >-
      Direct experimental measurement of the enzyme's catalytic activity in patient
      cells and by yeast complementation; core molecular function.
    supported_by:
    - reference_id: PMID:17273964
      supporting_text: >-
        The residual activity of mutant DK1 was 2%-4% when compared with control cells.
- term:
    id: GO:0004168
    label: dolichol kinase activity
  evidence_type: IMP
  original_reference_id: PMID:22242004
  qualifier: enables
  review:
    summary: >-
      Mutant-phenotype evidence: pathogenic DOLK mutations cause a dolichol kinase
      deficiency confirmed by enzyme analysis in patient fibroblasts.
    action: ACCEPT
    reason: >-
      Loss of catalytic activity upon mutation directly supports the dolichol kinase
      molecular function of DOLK; core.
    supported_by:
    - reference_id: PMID:22242004
      supporting_text: >-
        Enzyme analysis in patients' fibroblasts confirmed a dolichol kinase
        deficiency in all families.
- term:
    id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  evidence_type: IMP
  original_reference_id: PMID:22242004
  qualifier: involved_in
  review:
    summary: >-
      Mutant-phenotype evidence that DOLK is required for dolichol-phosphate formation;
      DOLK mutations abolish dolichol kinase activity and downstream glycosylation.
    action: ACCEPT
    reason: >-
      DOLK mutations cause deficient formation of dolichol-phosphate and impaired
      N-glycosylation / O-mannosylation, supporting its role in Dol-P biosynthesis.
      Core biological process.
    supported_by:
    - reference_id: PMID:22242004
      supporting_text: >-
        pathogenic mutations were identified in DOLK, encoding the dolichol kinase
        responsible for formation of dolichol-phosphate.
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-4755600
  qualifier: located_in
  review:
    summary: >-
      Reactome-asserted ER membrane localization, consistent with experimental data.
    action: ACCEPT
    reason: >-
      Correct; matches the experimentally established ER membrane localization of DOLK.
    supported_by:
    - reference_id: PMID:16923818
      supporting_text: >-
        localized in the endoplasmic reticulum
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-446195
  qualifier: located_in
  review:
    summary: >-
      Reactome-asserted ER membrane localization, consistent with experimental data.
    action: ACCEPT
    reason: >-
      Correct; matches the experimentally established ER membrane localization of DOLK.
    supported_by:
    - reference_id: PMID:16923818
      supporting_text: >-
        localized in the endoplasmic reticulum
- term:
    id: GO:0004168
    label: dolichol kinase activity
  evidence_type: IDA
  original_reference_id: PMID:12213788
  qualifier: enables
  review:
    summary: >-
      Direct assay evidence: overexpression of human DOLK (hDK1) increased dolichol
      kinase activity ~15-fold in microsomes and complemented the yeast DK-deficient
      mutant.
    action: ACCEPT
    reason: >-
      Biochemical demonstration of the enzyme's catalytic activity; the defining and
      core molecular function.
    supported_by:
    - reference_id: PMID:12213788
      supporting_text: >-
        overexpression of hDK1p in Sf-9 cells resulted in a 15-fold increase in DK
        activity but not DAG kinase activity in crude microsomal fractions.
- term:
    id: GO:0004168
    label: dolichol kinase activity
  evidence_type: IDA
  original_reference_id: PMID:16923818
  qualifier: enables
  review:
    summary: >-
      Direct assay evidence with mapping of the CTP-binding site and kinetics
      (KM 22.8 uM dolichol; 3.5 uM CTP); G443D abolishes activity.
    action: ACCEPT
    reason: >-
      Detailed biochemical characterization of DOLK's dolichol kinase activity; core
      molecular function.
    supported_by:
    - reference_id: file:human/DOLK/DOLK-uniprot.txt
      supporting_text: >-
        KM=22.8 uM for dolichol {ECO:0000269|PubMed:16923818};
- term:
    id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:12213788
  qualifier: involved_in
  review:
    summary: >-
      Direct evidence that DOLK produces Dol-P: expression elevates DK activity and
      increases in vivo Dol-P levels, restoring N-glycosylation.
    action: ACCEPT
    reason: >-
      DOLK catalyzes the terminal step of Dol-P biosynthesis; increased Dol-P upon
      expression directly supports this process. Core.
    supported_by:
    - reference_id: PMID:12213788
      supporting_text: >-
        elevating DK activity, and consequently increasing Dol-P levels in vivo
- term:
    id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:16923818
  qualifier: involved_in
  review:
    summary: >-
      Direct evidence linking DOLK catalytic activity to dolichyl monophosphate
      biosynthesis, with functional mapping of catalytic residues.
    action: ACCEPT
    reason: >-
      DOLK catalyzes CTP-dependent dolichol phosphorylation, the terminal step of
      Dol-P biosynthesis; mutations abolishing activity confirm the requirement. Core.
    supported_by:
    - reference_id: PMID:16923818
      supporting_text: >-
        Dolichol kinase (DK) catalyzes the CTP-dependent phosphorylation of dolichol
        in the biosynthesis de novo and possibly the recycling of dolichyl
        monophosphate
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: IDA
  original_reference_id: PMID:16923818
  qualifier: located_in
  review:
    summary: >-
      Direct assay evidence that human DOLK is a polytopic ER membrane protein, from
      overexpression and topology mapping in CHO cells.
    action: ACCEPT
    reason: >-
      Experimentally demonstrated ER membrane localization by the primary
      characterization paper; this is the core location where DOLK acts.
    supported_by:
    - reference_id: PMID:16923818
      supporting_text: >-
        shown to be a polytopic membrane protein localized in the endoplasmic
        reticulum with an N terminus extended into the lumen and a cytoplasmically
        oriented C terminus.
- term:
    id: GO:0006488
    label: dolichol-linked oligosaccharide biosynthetic process
  evidence_type: IGI
  original_reference_id: PMID:12213788
  qualifier: involved_in
  review:
    summary: >-
      Proposed annotation capturing DOLK's role in supplying Dol-P for assembly of
      the dolichol-linked oligosaccharide (LLO) used in N-glycosylation. DOLK
      complementation of the yeast dolichol kinase mutant restores N-glycosylation,
      demonstrating this downstream involvement.
    action: NEW
    reason: >-
      The existing GOA BP annotations stop at dolichyl monophosphate biosynthesis
      (GO:0043048). DOLK is upstream of, and required for, LLO assembly for protein
      N-linked glycosylation; adding GO:0006488 records this downstream biological
      role explicitly, supported by rescue of N-glycosylation in the yeast
      complementation assay.
    supported_by:
    - reference_id: PMID:12213788
      supporting_text: >-
        restoring normal N-glycosylation of carboxypeptidase Y at the restrictive
        temperature in the temperature-sensitive mutant sec59-1.
core_functions:
- description: >-
    CTP-dependent dolichol kinase activity: phosphorylates dolichol to dolichyl
    monophosphate (Dol-P) at the ER membrane, the terminal step of de novo Dol-P
    biosynthesis (EC 2.7.1.108).
  molecular_function:
    id: GO:0004168
    label: dolichol kinase activity
  directly_involved_in:
  - id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  locations:
  - id: GO:0005789
    label: endoplasmic reticulum membrane
  supported_by:
  - reference_id: PMID:16923818
    supporting_text: >-
      Dolichol kinase (DK) catalyzes the CTP-dependent phosphorylation of dolichol
      in the biosynthesis de novo and possibly the recycling of dolichyl
      monophosphate
- description: >-
    Supplies dolichyl monophosphate, the activated lipid carrier that primes assembly
    of the dolichol-linked oligosaccharide for protein N-linked glycosylation (and is
    also required for O-/C-mannosylation and GPI-anchor biosynthesis).
  molecular_function:
    id: GO:0004168
    label: dolichol kinase activity
  directly_involved_in:
  - id: GO:0006488
    label: dolichol-linked oligosaccharide biosynthetic process
  locations:
  - id: GO:0005789
    label: endoplasmic reticulum membrane
  supported_by:
  - reference_id: PMID:12213788
    supporting_text: >-
      restoring normal N-glycosylation of carboxypeptidase Y at the restrictive
      temperature in the temperature-sensitive mutant sec59-1.
proposed_new_terms: []
suggested_questions:
- question: >-
    Does DOLK activity contribute to Dol-P recycling in addition to de novo synthesis,
    and how is this partitioned in vivo?
- question: >-
    Why do some DOLK-CDG patients present predominantly with dilated cardiomyopathy
    (via alpha-dystroglycan O-mannosylation) while others show multisystem or purely
    neurological disease?
suggested_experiments:
- description: >-
    Tissue-specific conditional Dolk knockout in mouse heart to test whether dilated
    cardiomyopathy arises specifically from reduced alpha-dystroglycan O-mannosylation.
- description: >-
    Structure determination (cryo-EM) of human DOLK to define the dolichol- and
    CTP-binding pockets and rationalize CDG1M variant effects.
references:
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  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:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: file:human/DOLK/DOLK-uniprot.txt
  title: UniProtKB entry DOLK_HUMAN (Q9UPQ8)
  findings: []
- id: PMID:12213788
  title: 'Expression and characterization of a human cDNA that complements the temperature-sensitive
    defect in dolichol kinase activity in the yeast sec59-1 mutant: the enzymatic
    phosphorylation of dolichol and diacylglycerol are catalyzed by separate CTP-mediated
    kinase activities in Saccharomyces cerevisiae.'
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Primary paper establishing human DOLK/hDK1 as dolichol kinase via yeast sec59-1
      complementation; supports MF and Dol-P biosynthesis annotations. Abstract-only in
      cache but title/abstract fully support the cited claims.
- id: PMID:16923818
  title: Human dolichol kinase, a polytopic endoplasmic reticulum membrane protein
    with a cytoplasmically oriented CTP-binding site.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Biochemical characterization of human DOLK: ER membrane topology, CTP-binding
      site, kinetics, inactivating mutations. Supports MF and ER membrane annotations.
- id: PMID:17273964
  title: A defect in dolichol phosphate biosynthesis causes a new inherited disorder
    with death in early infancy.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Identifies DOLK/DK1 deficiency (DOLK-CDG); characterizes variants with 2-4%
      residual activity. Full text available; supports EXP MF annotation and disease role.
- id: PMID:22242004
  title: Autosomal recessive dilated cardiomyopathy due to DOLK mutations results
    from abnormal dystroglycan O-mannosylation.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      DOLK mutations cause dilated cardiomyopathy via deficient alpha-dystroglycan
      O-mannosylation; enzyme deficiency confirmed in fibroblasts. Supports IMP MF/BP.
- id: PMID:25416956
  title: A proteome-scale map of the human interactome network.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      Large-scale binary interactome map; source of a generic protein-binding IPI that
      does not inform DOLK molecular function.
- id: PMID:26871637
  title: Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      High-throughput interactome study; source of an uninformative protein-binding IPI.
- id: PMID:28514442
  title: Architecture of the human interactome defines protein communities and disease
    networks.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      High-throughput interactome study; source of uninformative protein-binding IPIs.
- id: PMID:32296183
  title: A reference map of the human binary protein interactome.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      HuRI binary interactome map; source of multiple uninformative protein-binding IPIs.
- id: PMID:33961781
  title: Dual proteome-scale networks reveal cell-specific remodeling of the human
    interactome.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: >-
      Proteome-scale AP-MS network study; source of uninformative protein-binding IPIs.
- id: Reactome:R-HSA-446195
  title: DOLK phosphorylates DCHOL to DOLP
  findings: []
- id: Reactome:R-HSA-446199
  title: Synthesis of dolichyl-phosphate
  findings: []
- id: Reactome:R-HSA-4755600
  title: Defective DOLK does not phosphorylate DCHOL
  findings: []