Seroatlas · Human Serome Atlas

PGAM2

Phosphoglycerate mutase 2

Also known as: PGAM-M, PGAM2_HUMAN

Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene

Protein identityUniProt · HPA

UniProt accession: P15259
Gene: PGAM2
Ensembl: ENSG00000164708
Chromosome: 7
Canonical length: 253 aa
Protein class: Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins
Subcellular location: Nucleoplasm,Nucleoli,Cytosol
Quaternary structure: Homodimer

OverviewNCBI Gene

Phosphoglycerate mutase (PGAM) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. The PGAM is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). This gene encodes muscle-specific PGAM subunit. Mutations in this gene cause muscle phosphoglycerate mutase eficiency, also known as glycogen storage disease X. [provided by RefSeq, Sep 2009]

Canonical amino-acid sequenceUniProt

253 residues, UniProt reviewed canonical sequence.

>P15259|PGAM2
     1  MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL
    61  KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD
   121  IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR
   181  VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR
   241  KAMEAVAAQG KAK

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against PGAM2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability: Intracellular
Secreted: No
Transmembrane segments: 0
Mean surface accessibility (rSASA): 0.25
Highest tissue expression: 4,078 nTPM

Expression across tissuesHPA

Tissue

skeletal muscle: 4,078 nTPM
tongue: 1,637 nTPM
heart muscle: 1,112 nTPM
testis: 176 nTPM
cerebellum: 65 nTPM
esophagus: 56 nTPM

Single-cell type

late spermatids: 3,000 nCPM
late primary spermatocytes: 645 nCPM
early spermatids: 504 nCPM
thymic myoid cells: 110 nCPM
myonuclei: 65 nCPM
vascular smooth muscle cells: 45 nCPM

Immune cell

T-reg: 0.3 nTPM
eosinophil: 0.2 nTPM
plasmacytoid DC: 0.2 nTPM
neutrophil: 0.1 nTPM
basophil: 0 nTPM
classical monocyte: 0 nTPM

Brain region

thalamus: 50 nTPM
pons: 48 nTPM
hypothalamus: 48 nTPM
cerebellum: 38 nTPM
midbrain: 38 nTPM
white matter: 34 nTPM

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about PGAM2.

Disease | AllUniProt

Conditions PGAM2 is implicated in, by any mechanism.

Glycogen storage disease 10 (GSD10) MIM:261670

Disease | GeneticClinVar

12 pathogenic / likely-pathogenic of 201 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

Glycogen storage disease type X
PGAM2-related disorder
Rhabdomyolysis

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance): 1.77
gnomAD pLI: 0
gnomAD missense Z: -0.67
DepMap mean gene effect: -0.01
DepMap dependency class: selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

Molecular functions

Cellular components

Protein domainsUniProt · Pfam · InterPro

KeywordsUniProt

InteractionsUniProt · HPA

Protein binding partners of PGAM2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

Antibody and autoantibody relevanceSeroatlas analysis

Seroatlas reads PGAM2 as an antibody target. Whether an autoantibody or antibody against PGAM2 could matter depends on whether native PGAM2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.

PGAM2 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.

Annotation status

The present source text does not explicitly label PGAM2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.

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