Phosphoglycerate dehydrogenase

PDB rendering based on 2g76.

Available structures
PDB	2g76

Identifiers

Symbols

PHGDH; 3-PGDH; 3PGDH; MGC3017; PDG; PGAD; PGD; PGDH; SERA

External IDs

OMIM: 606879 MGI: 1355330 HomoloGene: 39318 GeneCards: PHGDH Gene

EC number

1.1.1.95

Gene Ontology
Molecular function	• phosphoglycerate dehydrogenase activity • electron carrier activity • oxidoreductase activity • cofactor binding • NAD binding
Cellular component	• extracellular region
Biological process	• glutamine metabolic process • glycine metabolic process • L-serine biosynthetic process • threonine metabolic process • brain development • cellular amino acid biosynthetic process • gamma-aminobutyric acid metabolic process • regulation of gene expression • taurine metabolic process • spinal cord development • glial cell development • neural tube development • neurogenesis • cell cycle process • neuron projection development
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
120.2 – 120.29 Mb

Chr 3:
98.12 – 98.14 Mb

PubMed search

[1]

[2]

D-3-phosphoglycerate dehydrogenase is an enzyme that in humans is encoded by the PHGDH gene.^[1]

3-Phosphoglycerate dehydrogenase (PHGDH; EC 1.1.1.95) catalyzes the transition of 3-phosphoglycerate into 3-phosphohydroxypyruvate, which is the first and rate-limiting step in the phosphorylated pathway of serine biosynthesis, using NAD+/NADH as a cofactor.^[1] Certain breast cancers are dependent on the overexpression of PHGDH.^[2]

References

^ ^a ^b "Entrez Gene: PHGDH phosphoglycerate dehydrogenase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26227.
^ Possemato, Richard; Marks, Kevin M., Shaul, Yoav D., Pacold, Michael E., Kim, Dohoon, Birsoy, Kıvanç, Sethumadhavan, Shalini, Woo, Hin-Koon, Jang, Hyun G., Jha, Abhishek K., Chen, Walter W., Barrett, Francesca G., Stransky, Nicolas, Tsun, Zhi-Yang, Cowley, Glenn S., Barretina, Jordi, Kalaany, Nada Y., Hsu, Peggy P., Ottina, Kathleen, Chan, Albert M., Yuan, Bingbing, Garraway, Levi A., Root, David E., Mino-Kenudson, Mari, Brachtel, Elena F., Driggers, Edward M., Sabatini, David M. (17 August 2011). "Functional genomics reveal that the serine synthesis pathway is essential in breast cancer". Nature 476 (7360): 346–350. doi:10.1038/nature10350.

Tsang HT, Connell JW, Brown SE, et al. (2006). "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex.". Genomics 88 (3): 333–46. doi:10.1016/j.ygeno.2006.04.003. PMID 16730941.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1.". Nature 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.
Guo D, Han J, Adam BL, et al. (2005). "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress.". Biochem. Biophys. Res. Commun. 337 (4): 1308–18. doi:10.1016/j.bbrc.2005.09.191. PMID 16236267.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Pind S, Slominski E, Mauthe J, et al. (2002). "V490M, a common mutation in 3-phosphoglycerate dehydrogenase deficiency, causes enzyme deficiency by decreasing the yield of mature enzyme.". J. Biol. Chem. 277 (9): 7136–43. doi:10.1074/jbc.M111419200. PMID 11751922.
Klomp LW, de Koning TJ, Malingré HE, et al. (2001). "Molecular characterization of 3-phosphoglycerate dehydrogenase deficiency--a neurometabolic disorder associated with reduced L-serine biosynthesis.". Am. J. Hum. Genet. 67 (6): 1389–99. doi:10.1086/316886. PMC 1287916. PMID 11055895. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1287916.
Pineda M, Vilaseca MA, Artuch R, et al. (2000). "3-phosphoglycerate dehydrogenase deficiency in a patient with West syndrome.". Developmental medicine and child neurology 42 (9): 629–33. doi:10.1017/S0012162200001171. PMID 11034457.
Baek JY, Jun DY, Taub D, Kim YH (2000). "Assignment of human 3-phosphoglycerate dehydrogenase (PHGDH) to human chromosome band 1p12 by fluorescence in situ hybridization.". Cytogenet. Cell Genet. 89 (1-2): 6–7. doi:10.1159/000015577. PMID 10894924.
Cho HM, Jun DY, Bae MA, et al. (2000). "Nucleotide sequence and differential expression of the human 3-phosphoglycerate dehydrogenase gene.". Gene 245 (1): 193–201. doi:10.1016/S0378-1119(00)00009-3. PMID 10713460.
Jaeken J, Detheux M, Van Maldergem L, et al. (1996). "3-Phosphoglycerate dehydrogenase deficiency: an inborn error of serine biosynthesis.". Arch. Dis. Child. 74 (6): 542–5. doi:10.1136/adc.74.6.542. PMC 1511571. PMID 8758134. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1511571.

PDB gallery

2g76: Crystal structure of human 3-phosphoglycerate dehydrogenase

Phosphoglycerate dehydrogenase

References

Further reading