PGM2/YMR105C Summary Help

Standard Name PGM2 1
Systematic Name YMR105C
Alias GAL5 2
Feature Type ORF, Verified
Description Phosphoglucomutase; catalyzes the conversion from glucose-1-phosphate to glucose-6-phosphate, which is a key step in hexose metabolism; functions as the acceptor for a Glc-phosphotransferase; protein abundance increases in response to DNA replication stress; PGM2 has a paralog, PGM1, that arose from the whole genome duplication (1, 3, 4, 5 and see Summary Paragraph)
Name Description PhosphoGlucoMutase 6
Chromosomal Location
ChrXIII:477606 to 475897 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All PGM2 GO evidence and references
  View Computational GO annotations for PGM2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 13 genes
Classical genetics
Large-scale survey
100 total interaction(s) for 85 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 20
  • Affinity Capture-RNA: 2
  • PCA: 13

Genetic Interactions
  • Dosage Lethality: 1
  • Dosage Rescue: 3
  • Negative Genetic: 47
  • Phenotypic Enhancement: 2
  • Phenotypic Suppression: 1
  • Positive Genetic: 8
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 1
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 569
Molecular Weight (Da) 63,088
Isoelectric Point (pI) 6.6
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXIII:477606 to 475897 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1710 477606..475897 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004711

Phosphoglucomutase (EC: catalyzes the interconversion of glucose-6-phosphate and glucose-1-phosphate and is important for carbohydrate metabolism in a variety of organisms, ranging from bacteria to humans (7, 8, 1, 9). The direction of the interconversion is determined by the availability of substrate carbon sources (8). Saccharomyces cerevisiae contains a major phosphoglucomutase isoform, Pgm2p, and a minor phosphoglucomutase isoform, Pgm1p. Pgm2p and Pgm1p functions are involved in glycolysis, the pentose phosphate shunt, and the metabolism of glycogen, trehalose, and galactose. Phosphoglucomutase is also required for the synthesis of N-linked glycoproteins, extracellular glycans, and UDP-glucose (7, 8, 9, 10). Phosphoglucomutase also indirectly effects calcium uptake and homeostasis because glucose-1-phosphate and glucose-6-phosphate effect cation uptake (11, 12, 8).

Pgm2p accounts for approximately 80%-90% of all phosphoglucomutase activity in S. cerevisiae. Basal expression of Pgm2p is constitutive, and expression increases in response to: heat shock during conditions of glucose repression, glucose depletion, ethanol stress, salt stress, lithium stress and during adaptation to cold (13, 7, 14, 15, 16, 17). Pgm2p expression is also induced during growth on galactose (8, 2) and at the diauxic shift (18). Induction at the diauxic transition is dependent on Msn2p/Msn4p functions (18), and induction in response to heat shock or salt stress is dependent on Msn2p/Msn4p and glycogen synthase kinase 3 (Mck1p, Mrk1p, Rim11p and Ygk3p) (15). Although Pgm2p has been shown to be post-translationally glycosylated to different degrees under different conditions (7, 3), there is no evidence that the modifications alter the enzymatic activity of Pgm2p (13). Phosphoglucomutase activity is inhibited by lithium in both yeast and humans, making it an important in vivo lithium target, as lithium is frequently used as a treatment for manic depressive disorders in humans (14). In yeast, this inhibition leads to glucose-1-phosphate accumulation during growth on galactose (19).

pgm2 null mutants are viable, but accumulate more glucose-1-phosphate and intracellular calcium during growth on galactose as compared to wild type (11). pgm2 null mutants also display increased sensitivity to toxic cations such as lithium, calcium, aminoglycosides, and polyamines (12). pgm1 pgm2 double null mutants are viable, but cannot use galactose as a sole carbon source, and accumulate lower levels of glycogen and trehalose than wild type (1). The growth phenotypes of pgm2 null mutants can be complemented by expression of E. coli phosphoglucomutase (9).

Last updated: 2005-09-08 Contact SGD

References cited on this page View Complete Literature Guide for PGM2
1) Boles E, et al.  (1994) A family of hexosephosphate mutases in Saccharomyces cerevisiae. Eur J Biochem 220(1):83-96
2) Oh D and Hopper JE  (1990) Transcription of a yeast phosphoglucomutase isozyme gene is galactose inducible and glucose repressible. Mol Cell Biol 10(4):1415-22
3) Marchase RB, et al.  (1993) Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic glycoprotein and the acceptor for a Glc-phosphotransferase. J Biol Chem 268(11):8341-9
4) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
5) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
6) Bevan P and Douglas HC  (1969) Genetic control of phosphoglucomutase variants in Saccharomyces cerevisiae. J Bacteriol 98(2):532-5
7) Dey NB, et al.  (1994) The glycosylation of phosphoglucomutase is modulated by carbon source and heat shock in Saccharomyces cerevisiae. J Biol Chem 269(43):27143-8
8) Fu L, et al.  (2000) Loss of the major isoform of phosphoglucomutase results in altered calcium homeostasis in Saccharomyces cerevisiae. J Biol Chem 275(8):5431-40
9) Aiello DP, et al.  (2002) Intracellular glucose 1-phosphate and glucose 6-phosphate levels modulate Ca2+ homeostasis in Saccharomyces cerevisiae. J Biol Chem 277(48):45751-8
10) Daran JM, et al.  (1997) Physiological and morphological effects of genetic alterations leading to a reduced synthesis of UDP-glucose in Saccharomyces cerevisiae. FEMS Microbiol Lett 153(1):89-96
11) Aiello DP, et al.  (2004) The Ca2+ homeostasis defects in a pgm2Delta strain of Saccharomyces cerevisiae are caused by excessive vacuolar Ca2+ uptake mediated by the Ca2+-ATPase Pmc1p. J Biol Chem 279(37):38495-502
12) Mulet JM, et al.  (2004) The trehalose pathway and intracellular glucose phosphates as modulators of potassium transport and general cation homeostasis in yeast. Yeast 21(7):569-82
13) Fu L, et al.  (1995) The posttranslational modification of phosphoglucomutase is regulated by galactose induction and glucose repression in Saccharomyces cerevisiae. J Bacteriol 177(11):3087-94
14) Masuda CA, et al.  (2001) Phosphoglucomutase is an in vivo lithium target in yeast. J Biol Chem 276(41):37794-801
15) Hirata Y, et al.  (2003) Yeast glycogen synthase kinase-3 activates Msn2p-dependent transcription of stress responsive genes. Mol Biol Cell 14(1):302-12
16) Alexandre H, et al.  (2001) Global gene expression during short-term ethanol stress in Saccharomyces cerevisiae. FEBS Lett 498(1):98-103
17) Schade B, et al.  (2004) Cold adaptation in budding yeast. Mol Biol Cell 15(12):5492-502
18) Boy-Marcotte E, et al.  (1998) Msn2p and Msn4p control a large number of genes induced at the diauxic transition which are repressed by cyclic AMP in Saccharomyces cerevisiae. J Bacteriol 180(5):1044-52
19) Csutora P, et al.  (2005) Inhibition of phosphoglucomutase activity by lithium alters cellular calcium homeostasis and signaling in Saccharomyces cerevisiae. Am J Physiol Cell Physiol 289(1):C58-67