id: P36871
gene_symbol: PGM1
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  Phosphoglucomutase-1 (PGM1; EC 5.4.2.2) is the major human phosphoglucomutase,
  a cytosolic Mg2+-dependent enzyme that catalyzes the reversible interconversion of
  alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate. Catalysis proceeds via
  an alpha-D-glucose 1,6-bisphosphate intermediate and a catalytic phosphoserine (Ser117),
  with the bound Mg2+ ion coordinated by Ser117 and three active-site aspartates. PGM1
  sits at the junction of glycogen metabolism and glycolysis/gluconeogenesis. During
  glycogenolysis it converts the glucose-1-phosphate released by glycogen phosphorylase
  into glucose-6-phosphate for glycolysis (or, in liver after glucose-6-phosphatase,
  for blood glucose), and it runs in reverse to supply glucose-1-phosphate for glycogen
  synthesis. Its products also feed the nucleotide-sugar (UDP-glucose/UDP-galactose,
  Leloir), galactose, and pentose-phosphate pathways. The enzyme is a monomer of 562
  residues belonging to the alpha-D-phosphohexomutase superfamily. Loss-of-function
  variants cause PGM1 deficiency (PGM1-CDG; congenital disorder of glycosylation type
  It / glycogen storage disease type XIV), a mixed glycogenosis and glycosylation
  disorder featuring cleft palate, hepatopathy, hypoglycemia, dilated cardiomyopathy,
  exercise intolerance, and abnormal transferrin glycosylation, and it is notably
  responsive to galactose supplementation.
alternative_products:
- name: '1'
  id: P36871-1
- name: '2'
  id: P36871-2
  sequence_note: VSP_004686
- name: '3'
  id: P36871-3
  sequence_note: VSP_045204
existing_annotations:
- term:
    id: GO:0004614
    label: phosphoglucomutase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: Phylogenetic (IBA) assignment of the diagnostic phosphoglucomutase molecular
      function to PGM1. This is the well-established, experimentally confirmed core
      catalytic activity of the enzyme and is at the correct level of specificity.
    action: ACCEPT
    reason: The core molecular function is directly demonstrated experimentally (IDA/EXP,
      PMID:25288802, PMID:15378030) and the IBA call is consistent with the entire
      phosphohexomutase family. This is a core function of PGM1.
    supported_by:
    - reference_id: PMID:26972339
      supporting_text: It catalyzes the interconversion of glucose 1-phosphate and
        glucose 6-phosphate
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: Phylogenetic assignment of PGM1 activity to the cytosol, consistent with
      the cytoplasmic localization of the enzyme.
    action: ACCEPT
    reason: PGM1 is a soluble cytoplasmic enzyme; the cytosol is where its metabolic
      reaction takes place. Supported by direct immunofluorescence (IDA, HPA) and
      the UniProt subcellular location.
    supported_by:
    - reference_id: file:human/PGM1/PGM1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm'
- term:
    id: GO:0005975
    label: carbohydrate metabolic process
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: Phylogenetic assignment placing PGM1 in carbohydrate metabolism, the
      broad process encompassing its role in interconverting glucose phosphates.
    action: ACCEPT
    reason: Correct but general. It accurately captures PGM1's participation in
      carbohydrate metabolism; more specific processes (glucose metabolic process,
      glycogen metabolism, glycolysis/gluconeogenesis) are separately annotated.
      Retained as a broad, non-core parent term.
    supported_by:
    - reference_id: PMID:26972339
      supporting_text: It catalyzes the interconversion of glucose 1-phosphate and
        glucose 6-phosphate
- term:
    id: GO:0000287
    label: magnesium ion binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: InterPro-based electronic assignment of magnesium ion binding, the
      catalytic cofactor of PGM1.
    action: ACCEPT
    reason: PGM1 binds one Mg2+ per subunit as an essential catalytic cofactor; this
      is directly confirmed by crystallography (IDA, PMID:26972339) and the IEA mapping
      is correct.
    supported_by:
    - reference_id: PMID:26972339
      supporting_text: Mg2+ serves as an electron-withdrawing group to facilitate
        phosphoryl transfer from phosphoserine 117
- term:
    id: GO:0004614
    label: phosphoglucomutase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: Automated (multi-method IEA, incl. RHEA:23536/EC:5.4.2.2 mapping) assignment
      of phosphoglucomutase activity to PGM1.
    action: ACCEPT
    reason: Redundant with, and confirmed by, the experimental IDA/EXP annotations
      for the same term. The RHEA/EC mapping is correct for this enzyme.
    supported_by:
    - reference_id: file:human/PGM1/PGM1-uniprot.txt
      supporting_text: Catalyzes the reversible isomerization of alpha-D-glucose 1-
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Electronic assignment of cytoplasmic localization from the UniProt
      subcellular-location vocabulary.
    action: ACCEPT
    reason: Consistent with the well-supported cytosolic localization of PGM1; a
      broader parent of cytosol.
    supported_by:
    - reference_id: file:human/PGM1/PGM1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm'
- term:
    id: GO:0005975
    label: carbohydrate metabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: InterPro-based electronic assignment of carbohydrate metabolic process.
    action: ACCEPT
    reason: Redundant with the IBA annotation for the same term; correct but general
      parent process. Retained as non-core broad context.
    supported_by:
    - reference_id: PMID:26972339
      supporting_text: It catalyzes the interconversion of glucose 1-phosphate and
        glucose 6-phosphate
- term:
    id: GO:0016868
    label: intramolecular phosphotransferase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: InterPro-based electronic assignment of the parent molecular-function
      class (intramolecular phosphotransferase) that subsumes phosphoglucomutase
      activity.
    action: ACCEPT
    reason: This is the correct broad parent of GO:0004614 phosphoglucomutase activity
      (the reaction proceeds via intramolecular phosphoryl transfer through a
      glucose-1,6-bisphosphate intermediate). Accurate but redundant with the more
      specific phosphoglucomutase term; kept as a non-core general term.
    supported_by:
    - reference_id: PMID:26972339
      supporting_text: The reaction entails two consecutive phosphoryl transfers and
        proceeds via a bisphosphorylated intermediate
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21044950
  qualifier: enables
  review:
    summary: IntAct-curated protein-protein interaction (with TINF2, UniProtKB:Q9BSI4)
      captured by a genome-wide split-YFP fluorescence-complementation screen for
      telomere-signaling regulators.
    action: MARK_AS_OVER_ANNOTATED
    reason: Bare "protein binding" (GO:0005515) is uninformative about PGM1's molecular
      function. The interaction derives from a large-scale telomere-interactome screen
      that identified ~300 candidate binders and is not established as a functional
      partnership relevant to PGM1's enzymatic role; per curation policy this is marked
      as over-annotated rather than removed (it reflects a real IPI experiment).
    supported_by:
    - reference_id: PMID:21044950
      supporting_text: we identified over 300 proteins that associated with the six
        core telomeric proteins
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IDA
  original_reference_id: GO_REF:0000052
  qualifier: located_in
  review:
    summary: Direct immunofluorescence (Human Protein Atlas) localization of PGM1
      to the cytosol.
    action: ACCEPT
    reason: Direct experimental evidence for the primary subcellular location of this
      soluble metabolic enzyme; a core cellular-component annotation.
    supported_by:
    - reference_id: file:human/PGM1/PGM1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm'
- term:
    id: GO:0004614
    label: phosphoglucomutase activity
  evidence_type: EXP
  original_reference_id: PMID:15378030
  qualifier: enables
  review:
    summary: Experimental demonstration of PGM1 catalytic (phosphoglucomutase)
      activity, whose regulation by PAK1-mediated phosphorylation is characterized
      in this study.
    action: ACCEPT
    reason: Direct experimental support for the core catalytic function; PAK1
      phosphorylation of PGM1 was shown to enhance its enzymatic activity, confirming
      the activity being measured.
    supported_by:
    - reference_id: PMID:15378030
      supporting_text: selectively on threonine 466 significantly increased PGM enzymatic
- term:
    id: GO:0004614
    label: phosphoglucomutase activity
  evidence_type: IDA
  original_reference_id: PMID:30982613
  qualifier: enables
  review:
    summary: Direct assignment of phosphoglucomutase activity in the study mapping
      the metabolic pathomechanism and galactose treatment of PGM1-CDG.
    action: ACCEPT
    reason: Reinforces the core catalytic function; the paper explicitly describes
      PGM1 as the enzyme that interconverts glucose-6-P and glucose-1-P and studies
      the metabolic consequences of its deficiency.
    supported_by:
    - reference_id: PMID:30982613
      supporting_text: encodes the metabolic enzyme that interconverts
- term:
    id: GO:0033499
    label: beta-D-galactose catabolic process via UDP-galactose, Leloir pathway
  evidence_type: IMP
  original_reference_id: PMID:30982613
  qualifier: involved_in
  review:
    summary: Mutant-phenotype evidence linking PGM1 to the Leloir/UDP-galactose
      route, based on the galactose-responsive metabolic rewiring seen in PGM1-CDG
      fibroblasts.
    action: KEEP_AS_NON_CORE
    reason: PGM1's products (glucose-1-P/glucose-6-P) connect to the nucleotide-sugar
      and galactose (Leloir) pathways, and galactose treatment replenishes
      galactose-1-P, UDP-glucose, and UDP-galactose in PGM1-CDG. This is a real,
      pathway-adjacent role but peripheral to PGM1's core glucose-phosphate
      interconversion function, so it is retained as non-core.
    supported_by:
    - reference_id: PMID:30982613
      supporting_text: UDP-glucose and UDP-galactose, the nucleotide sugars
- term:
    id: GO:0005980
    label: glycogen catabolic process
  evidence_type: IMP
  original_reference_id: PMID:28882528
  qualifier: acts_upstream_of_or_within
  review:
    summary: Mutant-phenotype evidence that PGM1 deficiency blocks muscle
      glycogenolysis, placing PGM1 within glycogen catabolism.
    action: ACCEPT
    reason: Well supported and biologically central; in glycogenolysis PGM1 converts
      the glucose-1-phosphate released by glycogen phosphorylase into glucose-6-phosphate.
      Severe PGM1 loss causes blocked muscle glycogenolysis mimicking McArdle disease,
      directly demonstrating this role.
    supported_by:
    - reference_id: PMID:28882528
      supporting_text: 'severe loss of PGM1 activity causes blocked muscle'
- term:
    id: GO:0005576
    label: extracellular region
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6798745
  qualifier: located_in
  review:
    summary: Reactome-derived localization arising from PGM1's presence in neutrophil
      tertiary (secretory) granules that are exocytosed during degranulation.
    action: KEEP_AS_NON_CORE
    reason: A secondary/extracellular localization reflecting the release of granule
      contents during neutrophil degranulation; not the site of PGM1's cytosolic
      catalytic function. Retained as non-core rather than removed because it derives
      from curated Reactome pathway data.
- term:
    id: GO:0005576
    label: extracellular region
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6800434
  qualifier: located_in
  review:
    summary: Reactome-derived extracellular localization from exocytosis of
      ficolin-rich (granule) lumen proteins during neutrophil degranulation.
    action: KEEP_AS_NON_CORE
    reason: As above, a secondary localization tied to neutrophil granule exocytosis
      rather than PGM1's core cytosolic metabolic role; kept as non-core.
- term:
    id: GO:1904724
    label: tertiary granule lumen
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6798745
  qualifier: located_in
  review:
    summary: Reactome localization of PGM1 to the tertiary (secretory) granule lumen
      of neutrophils.
    action: KEEP_AS_NON_CORE
    reason: Reflects PGM1's presence in neutrophil secretory granules (degranulation
      pathway), a peripheral localization distinct from its principal cytosolic
      metabolic function; retained as non-core.
- term:
    id: GO:1904813
    label: ficolin-1-rich granule lumen
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6800434
  qualifier: located_in
  review:
    summary: Reactome localization of PGM1 to the ficolin-1-rich granule lumen of
      neutrophils.
    action: KEEP_AS_NON_CORE
    reason: Peripheral granule localization from the neutrophil-degranulation pathway,
      not PGM1's core cytosolic site of action; retained as non-core.
- term:
    id: GO:0000287
    label: magnesium ion binding
  evidence_type: IDA
  original_reference_id: PMID:26972339
  qualifier: enables
  review:
    summary: Direct (crystallographic) evidence that PGM1 binds one Mg2+ ion per
      subunit as an essential catalytic cofactor.
    action: ACCEPT
    reason: Crystal structures show the Mg2+ ion coordinated in octahedral geometry
      by Ser117 and three aspartates, functioning as an electron-withdrawing group
      to facilitate phosphoryl transfer. Core cofactor of the enzyme.
    supported_by:
    - reference_id: PMID:26972339
      supporting_text: Mg2+ serves as an electron-withdrawing group to facilitate
        phosphoryl transfer from phosphoserine 117
- term:
    id: GO:0004614
    label: phosphoglucomutase activity
  evidence_type: IDA
  original_reference_id: PMID:25288802
  qualifier: enables
  review:
    summary: Direct enzymatic characterization of recombinant wild-type PGM1 (and
      disease variants), confirming phosphoglucomutase catalytic activity and its
      kinetic parameters.
    action: ACCEPT
    reason: In vitro biochemical characterization provides direct experimental
      support for the core catalytic function, with variants showing reduced
      kcat/Km; a defining core function of PGM1.
    supported_by:
    - reference_id: PMID:25288802
      supporting_text: central role of the enzyme in glucose metabolism
- term:
    id: GO:0006006
    label: glucose metabolic process
  evidence_type: IDA
  original_reference_id: PMID:25288802
  qualifier: involved_in
  review:
    summary: Direct evidence placing PGM1 within glucose metabolism, reflecting its
      central role in interconverting glucose phosphates.
    action: ACCEPT
    reason: PGM1's reaction is a central node of glucose metabolism (breakdown and
      synthesis of glucose); this is a core biological-process annotation supported
      by the biochemical characterization of the enzyme and its deficiency phenotypes.
    supported_by:
    - reference_id: PMID:25288802
      supporting_text: central role of the enzyme in glucose metabolism
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5609939
  qualifier: located_in
  review:
    summary: Reactome (curated) cytosolic localization of PGM1, in the reaction where
      defective PGM1 fails to isomerise G6P to G1P.
    action: ACCEPT
    reason: Consistent with the well-established cytosolic localization; the reaction
      it participates in is cytosolic. A core cellular-component annotation.
    supported_by:
    - reference_id: file:human/PGM1/PGM1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm'
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:23533145
  qualifier: located_in
  review:
    summary: High-throughput mass-spectrometry detection of PGM1 in exosomes isolated
      from expressed prostatic secretions in urine.
    action: KEEP_AS_NON_CORE
    reason: A proteomic detection of the abundant cytosolic enzyme in secreted
      exosomes; represents a secondary localization rather than PGM1's functional
      site. Retained as non-core.
    supported_by:
    - reference_id: PMID:23533145
      supporting_text: exosome preparations were characterized by a shotgun proteomics
        procedure
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:19056867
  qualifier: located_in
  review:
    summary: High-throughput proteomic detection of PGM1 among proteins profiled in
      human urinary exosomes.
    action: KEEP_AS_NON_CORE
    reason: As above, a mass-spectrometry-based detection in exosomes; a common
      finding for abundant cytosolic enzymes and peripheral to PGM1's core function.
      Retained as non-core.
    supported_by:
    - reference_id: PMID:19056867
      supporting_text: profile the proteome of human urinary exosomes
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9638125
  qualifier: located_in
  review:
    summary: Reactome (curated) cytosolic localization of PGM1 in the reaction where
      PGM1:Mg2+ isomerises G1P to G6P.
    action: ACCEPT
    reason: Correct core localization; the phosphoglucomutase reaction (G1P to G6P) is
      cytosolic and requires the bound Mg2+ cofactor.
    supported_by:
    - reference_id: file:human/PGM1/PGM1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm'
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9638127
  qualifier: located_in
  review:
    summary: Reactome (curated) cytosolic localization of PGM1 in the reaction where
      PGM1:Mg2+ isomerises G6P to G1P (reverse direction).
    action: ACCEPT
    reason: Correct core localization; the reverse phosphoglucomutase reaction
      (G6P to G1P) is likewise cytosolic and Mg2+-dependent.
    supported_by:
    - reference_id: file:human/PGM1/PGM1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm'
- term:
    id: GO:0004614
    label: phosphoglucomutase activity
  evidence_type: IDA
  original_reference_id: PMID:1530890
  qualifier: enables
  review:
    summary: Direct assignment of phosphoglucomutase activity to the human PGM1 gene
      product characterized in the cDNA cloning study.
    action: ACCEPT
    reason: Establishes the identity of the cloned human PGM1 as the polymorphic
      phosphoglucomutase (EC 5.4.2.2); supports the core catalytic function.
    supported_by:
    - reference_id: PMID:1530890
      supporting_text: highly polymorphic human enzyme
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: NAS
  original_reference_id: PMID:1530890
  qualifier: located_in
  review:
    summary: Non-traceable author statement assigning cytoplasmic localization to
      PGM1 in the cloning/mapping study.
    action: ACCEPT
    reason: Consistent with the well-established cytoplasmic/cytosolic localization
      of PGM1 (corroborated by IDA immunofluorescence and UniProt); accepted as a
      broad, correct localization.
    supported_by:
    - reference_id: file:human/PGM1/PGM1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm'
- term:
    id: GO:0006006
    label: glucose metabolic process
  evidence_type: NAS
  original_reference_id: PMID:1530890
  qualifier: involved_in
  review:
    summary: Non-traceable author statement placing PGM1 in glucose metabolism.
    action: ACCEPT
    reason: Redundant with the IDA glucose-metabolic-process annotation and consistent
      with PGM1's central metabolic role; a correct core biological process.
    supported_by:
    - reference_id: PMID:25288802
      supporting_text: central role of the enzyme in glucose metabolism
- term:
    id: GO:0004614
    label: phosphoglucomutase activity
  evidence_type: TAS
  original_reference_id: PMID:8257433
  qualifier: enables
  review:
    summary: Traceable author statement (gene-structure study) affirming PGM1 as the
      phosphoglucomutase enzyme.
    action: ACCEPT
    reason: The study explicitly notes PGM1's central role in glycolysis and
      gluconeogenesis; supports the core catalytic function.
    supported_by:
    - reference_id: PMID:8257433
      supporting_text: central role in glycolysis and gluconeogenesis
- term:
    id: GO:0006094
    label: gluconeogenesis
  evidence_type: TAS
  original_reference_id: PMID:8257433
  qualifier: involved_in
  review:
    summary: Traceable author statement placing PGM1 in gluconeogenesis.
    action: ACCEPT
    reason: In gluconeogenesis/glycogen synthesis PGM1 runs in the G6P to G1P direction;
      the enzyme participates in glucose synthesis. A genuine biological role
      supported by the literature, retained as a core metabolic process.
    supported_by:
    - reference_id: PMID:8257433
      supporting_text: central role in glycolysis and gluconeogenesis
- term:
    id: GO:0006096
    label: glycolytic process
  evidence_type: TAS
  original_reference_id: PMID:8257433
  qualifier: involved_in
  review:
    summary: Traceable author statement placing PGM1 in glycolysis.
    action: KEEP_AS_NON_CORE
    reason: PGM1 feeds glycolysis by producing glucose-6-phosphate from the
      glucose-1-phosphate liberated during glycogenolysis, but it is not a core
      enzyme of the canonical glycolytic pathway itself (glucose to pyruvate).
      It is best regarded as an upstream/adjacent contributor, so it is kept as
      non-core.
    supported_by:
    - reference_id: PMID:8257433
      supporting_text: central role in glycolysis and gluconeogenesis
core_functions:
- description: Cytosolic Mg2+-dependent phosphoglucomutase that reversibly interconverts
    alpha-D-glucose 1-phosphate and alpha-D-glucose 6-phosphate, linking glycogen
    metabolism to glycolysis/gluconeogenesis.
  molecular_function:
    id: GO:0004614
    label: phosphoglucomutase activity
  supported_by:
  - reference_id: PMID:26972339
    supporting_text: It catalyzes the interconversion of glucose 1-phosphate and glucose
      6-phosphate
  directly_involved_in:
  - id: GO:0006006
    label: glucose metabolic process
  locations:
  - id: GO:0005829
    label: cytosol
- description: In glycogenolysis, converts the glucose-1-phosphate released by glycogen
    phosphorylase into glucose-6-phosphate, enabling glycogen breakdown.
  molecular_function:
    id: GO:0004614
    label: phosphoglucomutase activity
  supported_by:
  - reference_id: PMID:28882528
    supporting_text: 'severe loss of PGM1 activity causes blocked muscle'
  directly_involved_in:
  - id: GO:0005980
    label: glycogen catabolic process
  locations:
  - id: GO:0005829
    label: cytosol
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: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: PMID:1530890
  title: 'Phosphoglucomutase 1: complete human and rabbit mRNA sequences and direct
    mapping of this highly polymorphic marker on human chromosome 1.'
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: Cloning/mapping of human PGM1 cDNA; identifies it as the highly
      polymorphic phosphoglucomutase (EC 5.4.2.2). Supports enzyme identity and
      chromosomal localization; abstract-only in cache.
- id: PMID:15378030
  title: Regulation of phosphoglucomutase 1 phosphorylation and activity by a signaling
    kinase.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Demonstrates PGM1 catalytic activity and its enhancement by PAK1
      phosphorylation (at Thr-466/Thr-467). Directly supports the phosphoglucomutase
      molecular function.
- id: PMID:19056867
  title: Large-scale proteomics and phosphoproteomics of urinary exosomes.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Proteomic detection of PGM1 in urinary exosomes; supports a
      peripheral extracellular-exosome localization, not core function.
- id: PMID:21044950
  title: Genome-wide YFP fluorescence complementation screen identifies new regulators
    for telomere signaling in human cells.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Large-scale split-YFP telomere-interactome screen underlying the
      IntAct PGM1-TINF2 interaction. Well-formed citation, but supports only a bare
      protein-binding annotation of unclear functional relevance to PGM1.
- id: PMID:23533145
  title: In-depth proteomic analyses of exosomes isolated from expressed prostatic
    secretions in urine.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Shotgun proteomics of prostatic-secretion exosomes; PGM1 among
      ~900 detected proteins. Supports peripheral exosome localization only.
- id: PMID:25288802
  title: Compromised catalysis and potential folding defects in in vitro studies of
    missense mutants associated with hereditary phosphoglucomutase 1 deficiency.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: In vitro biochemical characterization of WT and disease-variant
      PGM1, confirming catalytic activity/kinetics and its central role in glucose
      metabolism.
- id: PMID:26972339
  title: Induced Structural Disorder as a Molecular Mechanism for Enzyme Dysfunction
    in Phosphoglucomutase 1 Deficiency.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: First WT and variant human PGM1 crystal structures; documents Mg2+
      coordination, phosphoserine (Ser117) catalytic mechanism, monomeric state, and
      reversible G1P/G6P interconversion. Full text available and verified.
- id: PMID:28882528
  title: Impaired glycogen breakdown and synthesis in phosphoglucomutase 1 deficiency.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Shows PGM1 deficiency blocks muscle glycogenolysis (McArdle-like
      second wind) and may limit glycogen synthesis; supports the glycogen
      catabolic-process role.
- id: PMID:30982613
  title: The Metabolic Map into the Pathomechanism and Treatment of PGM1-CDG.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Defines PGM1 as the enzyme interconverting glucose-6-P and
      glucose-1-P; establishes galactose-responsive rewiring of nucleotide-sugar
      (UDP-glucose/UDP-galactose, Leloir) metabolism in PGM1-CDG.
- id: PMID:8257433
  title: 'Phosphoglucomutase 1: a gene with two promoters and a duplicated first exon.'
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: PGM1 gene-structure study; notes its central role in glycolysis and
      gluconeogenesis. Supports enzyme identity and metabolic context.
- id: Reactome:R-HSA-5609939
  title: Defective PGM1 does not isomerise G6P to G1P
  findings: []
- id: Reactome:R-HSA-6798745
  title: Exocytosis of tertiary granule lumen proteins
  findings: []
- id: Reactome:R-HSA-6800434
  title: Exocytosis of ficolin-rich granule lumen proteins
  findings: []
- id: Reactome:R-HSA-9638125
  title: PGM1:Mg2+ isomerises G1P to G6P
  findings: []
- id: Reactome:R-HSA-9638127
  title: PGM1:Mg2+ isomerises G6P to G1P
  findings: []