Phosphoglucomutase 3

PGM3
Identifiers
Aliases	PGM3 , AGM1, IMD23, PAGM, PGM 3, Phosphoglucomutase 3
External IDs	OMIM: 172100; MGI: 97566; HomoloGene: 9205; GeneCards: PGM3; OMA:PGM3 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) [1] Band 6q14.1 Start 83,161,150 bp [1] End 83,193,936 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9 E3.1|9 46.58 cM Start 86,436,430 bp [2] End 86,453,895 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas islet of Langerhans stromal cell of endometrium anterior pituitary Achilles tendon cartilage tissue gonad left ovary sperm minor salivary glands Top expressed in epithelium of small intestine seminal vesicula umbilical cord yolk sac otolith organ utricle islet of Langerhans proximal tubule hand Paneth cell More reference expression data BioGPS More reference expression data
Gene ontology Molecular function intramolecular transferase activity, phosphotransferases phosphoglucomutase activity isomerase activity magnesium ion binding metal ion binding phosphoacetylglucosamine mutase activity Cellular component cytosol cellular component Biological process UDP-N-acetylglucosamine biosynthetic process protein O-linked glycosylation glucosamine metabolic process protein N-linked glycosylation glucose 1-phosphate metabolic process organic substance metabolic process spermatogenesis carbohydrate metabolic process hemopoiesis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5238 109785 Ensembl ENSG00000013375 ENSMUSG00000056131 UniProt O95394 Q9CYR6 RefSeq (mRNA) NM_001199917 NM_001199918 NM_001199919 NM_015599 NM_001367286 NM_001367287 NM_001163746 NM_028352 RefSeq (protein) NP_001186846 NP_001186847 NP_001186848 NP_056414 NP_001354215 NP_001354216 NP_001157218 NP_082628 Location (UCSC) Chr 6: 83.16 – 83.19 Mb Chr 9: 86.44 – 86.45 Mb PubMed search [3] [4]
Wikidata
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Phosphoacetylglucosamine mutase is an enzyme that in humans is encoded by the PGM3 gene. ^{[5] [6] [7]}

Clinical significance

Mutations in PGM3 are associated to congenital disorder of glycosylation. ^[8]

References

1. GRCh38: Ensembl release 89: ENSG00000013375 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000056131 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Pang H, Koda Y, Soejima M, Kimura H (March 2002). "Identification of human phosphoglucomutase 3 (PGM3) as N-acetylglucosamine-phosphate mutase (AGM1)". Annals of Human Genetics. 66 (Pt 2): 139–44. doi:10.1046/j.1469-1809.2002.00103.x. PMID   12174217. S2CID   90947429.
6. Li C, Rodriguez M, Banerjee D (January 2000). "Cloning and characterization of complementary DNA encoding human N-acetylglucosamine-phosphate mutase protein". Gene. 242 (1–2): 97–103. doi:10.1016/S0378-1119(99)00543-0. PMID   10721701.
7. "Entrez Gene: PGM3 phosphoglucomutase 3".
8. Stray-Pedersen A, Backe PH, Sorte HS, Mørkrid L, Chokshi NY, Erichsen HC, et al. (July 2014). "PGM3 mutations cause a congenital disorder of glycosylation with severe immunodeficiency and skeletal dysplasia". American Journal of Human Genetics. 95 (1): 96–107. doi:10.1016/j.ajhg.2014.05.007. PMC   4085583 . PMID   24931394.

Further reading

• Chen SH, Anderson JE, Giblett ER, Stamatoyannopoulos G (1978). "Isozyme patterns in erythrocytes from human fetuses". American Journal of Hematology. 3: 23–8. doi:10.1002/ajh.2830030103. PMID   203189. S2CID   19875224.
• Yoshida H, Abe T, Nakamura F (1979). "Studies on the frequencies of PGM1, PGM3 and Es-D types from hair roots in Japanese subjects and the determination of these types from old hair roots". Forensic Science International. 14 (1): 1–7. doi:10.1016/0379-0738(79)90150-6. PMID   468082.
• Marshall MJ, Neal FE, Goldberg DM (September 1979). "Isoenzymes of hexokinase, 6-phosphogluconate dehydrogenase, phosphoglucomutase and lactate dehydrogenase in uterine cancer". British Journal of Cancer. 40 (3): 380–90. doi:10.1038/bjc.1979.192. PMC   2010033 . PMID   508567.
• Cantu JM, Ibarra B (May 1982). "Phosphoglucomutase: evidence for a new locus expressed in human milk". Science. 216 (4546): 639–40. Bibcode:1982Sci...216..639C. doi:10.1126/science.6461922. PMID   6461922.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Mio T, Yamada-Okabe T, Arisawa M, Yamada-Okabe H (July 2000). "Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for the catalysis". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1492 (2–3): 369–76. doi:10.1016/S0167-4781(00)00120-2. PMID   11004509.

External links

• Overview of all the structural information available in the PDB for UniProt : Q9CYR6 (Mouse Phosphoacetylglucosamine mutase) at the PDBe-KB .