GO_REF:0000002

GO reference used by source annotation pipeline

Source annotation pipeline provenance for Pgam2 annotations including catalytic activity; intramolecular phosphotransferase activity.

"GO_REF entry used only to trace the source annotation method; biological support was assessed against UniProt and cached literature where available."

GO_REF:0000024

GO reference used by source annotation pipeline

Source annotation pipeline provenance for Pgam2 annotations including bisphosphoglycerate mutase activity; phosphoglycerate mutase activity.

"GO_REF entry used only to trace the source annotation method; biological support was assessed against UniProt and cached literature where available."

GO_REF:0000033

GO reference used by source annotation pipeline

Source annotation pipeline provenance for Pgam2 annotations including canonical glycolysis; cytosol; phosphoglycerate mutase activity.

"GO_REF entry used only to trace the source annotation method; biological support was assessed against UniProt and cached literature where available."

GO_REF:0000107

GO reference used by source annotation pipeline

Source annotation pipeline provenance for Pgam2 annotations including canonical glycolysis; cytosol; identical protein binding; nucleoplasm; striated muscle contraction.

"GO_REF entry used only to trace the source annotation method; biological support was assessed against UniProt and cached literature where available."

GO_REF:0000120

GO reference used by source annotation pipeline

Source annotation pipeline provenance for Pgam2 annotations including bisphosphoglycerate mutase activity; glycolytic process; phosphoglycerate mutase activity.

"GO_REF entry used only to trace the source annotation method; biological support was assessed against UniProt and cached literature where available."

GO_REF:0000121

GO reference used by source annotation pipeline

Source annotation pipeline provenance for Pgam2 annotations including Notch signaling pathway; canonical glycolysis; cytosol; glycolytic process; identical protein binding; and 3 other terms.

"GO_REF entry used only to trace the source annotation method; biological support was assessed against UniProt and cached literature where available."

PMID:15720133

Monochloroacetic acid inhibits liver gluconeogenesis by inactivating glyceraldehyde-3-phosphate dehydrogenase

This paper concludes that MCA-induced inhibition of liver gluconeogenesis is caused by inactivation of GAPDH, not PGAM. Phosphoglycerate mutase was measured as a negative control and shown NOT to be inactivated by MCA. It therefore demonstrates assayable phosphoglycerate mutase activity but does not support a direct PGAM role in gluconeogenesis.

"GAPDH was inactivated by MCA in vitro, but enolase, phosphoglycerate mutase, and phosphoglycerate kinase were not inactivated at the same or higher concentrations of MCA."

PMID:2158448

Location of phosphoglycerate mutase in rat skeletal muscle. An immunocytochemical and biochemical study

For Pgam2, this immunocytochemical/biochemical study localizes PGAM to both cytosol and nucleus of rat skeletal muscle (nuclear localization confirmed biochemically, ~25% of total specific activity in nuclei). It is the supporting evidence for nucleus/nucleoplasm (kept as non-core) and argues against the ooplasm annotation (the study is skeletal muscle, not oocyte).

"With the aid of highly affinity-purified anti-phosphoglycerate mutase antibodies, the enzyme was found in both cytosol and nucleus of rat skeletal muscle."

PMID:2850701

Inactivation of type MM phosphoglycerate mutase by sulfhydryl group reagents during facial embryogenesis

For Pgam2, this publication provides evidence/provenance for direct annotations to phosphoglycerate mutase activity and contextual annotations to response to mercury ion.

"Type MM phosphoglycerate mutase from free dissected mandibular processes from embryonic rats was reversibly inactivated by tetrathionate, p-chloromercuribenzoate, and Hg2+."

PMID:7867621

The muscle-specific phosphoglycerate mutase gene is specifically expressed in testis during spermatogenesis

For Pgam2, this publication shows the muscle-specific PGAM-M gene is developmentally expressed in testis during spermatogenesis, framing PGAM as an essential glycolytic enzyme for the spermatozoa energy supply (IEP expression evidence; reviewed as context for spermatogenesis, which is treated as over-annotation).

"we have investigated the expression during spermatogenesis of the genes that encode phosphoglycerate mutase, an essential glycolytic enzyme for the spermatozoa energy supply"

file:rat/Pgam2/Pgam2-deep-research-falcon.md

Falcon (Edison Scientific) deep research report for rat Pgam2 (UniProt P16290)

PGAM2 is the muscle-specific phosphoglycerate mutase isoform (PGAM-M), distinct from the brain-predominant PGAM1, consistent with the UniProt identity for P16290 and the muscle/heart bias of Pgam2 expression.

"Mammals express at least two major PGAM isoforms: **PGAM1 (Pgam1; often described as brain-predominant)** and **PGAM2 (Pgam2; muscle-specific)**"
PGAM2 catalyzes the reversible interconversion of 3-phosphoglycerate and 2-phosphoglycerate in lower glycolysis, supporting the phosphoglycerate mutase activity and glycolysis annotations.

"PGAM2 is a **glycolytic enzyme** that catalyzes the **reversible isomerization of 3-phosphoglycerate (3-PG) to 2-phosphoglycerate (2-PG)** in the “lower” portion of glycolysis"
The PGAM-family catalytic mechanism is a 2,3-bisphosphoglycerate-dependent phospho-histidine cycle, consistent with the BPG-dependent PGAM subfamily assignment and bisphosphoglycerate mutase activity.

"The canonical PGAM-family mechanism proceeds via a **phospho-histidine catalytic cycle**, commonly summarized as involving an **active-site histidine (often referred to as His11)** and a **2,3-bisphosphoglycerate (2,3-BPG/2,3-DPG)**-dependent priming/turnover mechanism"
PGAM2 is a cytosolic enzyme; no evidence supports stable non-cytosolic localization, with the dominant functional context being intracellular carbohydrate metabolism.

"Within the provided evidence set, PGAM2 is described as a **cytosolic** enzyme in an isoform table summary"
No support for stable extracellular or organellar localization of mammalian PGAM2; the dominant context is intracellular carbohydrate metabolism (argues against the ooplasm over-annotation).

"No evidence in the retrieved texts supports stable extracellular localization for mammalian PGAM2, and the dominant functional context is **intracellular carbohydrate metabolism**"
PGAM2 is expressed mainly in skeletal muscle and heart, the basis for its muscle-context annotations (e.g. striated muscle contraction kept as non-core/over-annotation rather than core MF).

"PGAM2 is described as expressed mainly in **skeletal muscle and heart**"
PGAM2 activity is regulated by SUMOylation at K49 and K176, which is functionally tied to myogenic differentiation (regulatory context, not a core catalytic annotation).

"PGAM2 is reported to undergo **SUMOylation**, with two primary SUMO acceptor lysines **K49 and K176**; mutating either lysine prevents SUMOylation"
PGAM2 catalytic activity is gated by reversible acetylation at K100, with SIRT2-mediated deacetylation activating the enzyme under oxidative stress (regulatory context).

"PGAM2 activity is strongly regulated by lysine acetylation at **K100**: acetylation at K100 inhibits PGAM2 activity, whereas deacetylation activates it"
Inherited human PGAM2 (PGAM-M) deficiency causes glycogen storage disease type X with exercise intolerance and cramps, underscoring its essential role in high-flux muscle glycolysis.

"Heart-focused work cites that **human PGAM deficiency** causes **glycogen storage disease type X**, characterized by **exercise intolerance and cramps**, consistent with an essential role for PGAM2 in high-flux muscle glycolysis"