IMPDH2

IMPDH2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1B3O, 1NF7, 1NFB
Identifiers
Aliases	IMPDH2 , IMPD2, IMPDH-II, IMP (inosine 5'-monophosphate) dehydrogenase 2, inosine monophosphate dehydrogenase 2
External IDs	OMIM: 146691; MGI: 109367; HomoloGene: 48919; GeneCards: IMPDH2; OMA:IMPDH2 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) [1] Band 3p21.31 Start 49,024,325 bp [1] End 49,029,447 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9|9 F2 Start 108,437,485 bp [2] End 108,442,783 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left ovary body of pancreas cartilage tissue right ovary right uterine tube gingival epithelium ventricular zone canal of the cervix skin of leg vulva Top expressed in morula epiblast uterus ventricular zone embryo embryo blastocyst spermatid yolk sac ovary More reference expression data BioGPS n/a
Gene ontology Molecular function DNA binding metal ion binding catalytic activity protein binding RNA binding oxidoreductase activity nucleotide binding IMP dehydrogenase activity Cellular component cytoplasm membrane peroxisomal membrane extracellular exosome nucleus extracellular region cytosol secretory granule lumen ficolin-1-rich granule lumen Biological process cellular response to interleukin-4 purine nucleotide biosynthetic process retina development in camera-type eye purine ribonucleoside monophosphate biosynthetic process lymphocyte proliferation GMP biosynthetic process protein homotetramerization GTP biosynthetic process neutrophil degranulation circadian rhythm Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3615 23918 Ensembl ENSG00000178035 ENSMUSG00000062867 UniProt P12268 P24547 RefSeq (mRNA) NM_000884 NM_011830 NM_001378921 RefSeq (protein) NP_000875 NP_035960 NP_001365850 Location (UCSC) Chr 3: 49.02 – 49.03 Mb Chr 9: 108.44 – 108.44 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Inosine-5'-monophosphate dehydrogenase 2, also known as IMP dehydrogenase 2, is an enzyme that in humans is encoded by the IMPDH2 gene. ^{[5] [6] [7]}

Function

IMP dehydrogenase 2 is the rate-limiting enzyme in the de novo guanine nucleotide biosynthesis. It is thus involved in maintaining cellular guanine deoxy- and ribonucleotide pools needed for DNA and RNA synthesis. IMPDH2 catalyzes the NAD-dependent oxidation of inosine-5'-monophosphate into xanthine-5'-monophosphate, which is then converted into guanosine-5'-monophosphate. ^[5] IMPDH2 has been identified as an intracellular target of the natural product sanglifehrin A. ^[8]

Clinical significance

This gene is up-regulated in some neoplasms, suggesting it may play a role in malignant transformation. ^[5]

See also

• IMP dehydrogenase

References

1. GRCh38: Ensembl release 89: ENSG00000178035 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000062867 – 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. "Entrez Gene: IMP (inosine monophosphate) dehydrogenase 2". Archived from the original on 2024-04-22. Retrieved 2017-10-29.
6. Natsumeda Y, Ohno S, Kawasaki H, Konno Y, Weber G, Suzuki K (March 1990). "Two distinct cDNAs for human IMP dehydrogenase". J. Biol. Chem. 265 (9): 5292–5. doi: 10.1016/S0021-9258(19)34120-1 . PMID   1969416.
7. Kost-Alimova MV, Glesne DA, Huberman E, Zelenin AV (1998). "Assignment1 of inosine '-monophosphate dehydrogenase type 2 (IMPDH2) to human chromosome band 3p21.2 by in situ hybridization". Cytogenet. Cell Genet. 82 (3–4): 145–6. doi:10.1159/000015088. PMID   9858805. S2CID   46764436. Archived from the original on 2024-04-22. Retrieved 2019-07-05.
8. Pua KH, Stiles DT, Sowa ME, Verdine GL (10 January 2017). "IMPDH2 Is an Intracellular Target of the Cyclophilin A and Sanglifehrin A Complex". Cell Rep. 18 (2): 432–442. doi: 10.1016/j.celrep.2016.12.030 . PMID   28076787.

Further reading

• Garat A, Cauffiez C, Hamdan-Khalil R, et al. (2009). "IMPDH2 genetic polymorphism: a promoter single-nucleotide polymorphism disrupts a cyclic adenosine monophosphate responsive element". Genet Test Mol Biomarkers. 13 (6): 841–7. doi:10.1089/gtmb.2009.0096. PMID   19810816.
• Wang J, Zeevi A, Webber S, et al. (2007). "A novel variant L263F in human inosine 5'-monophosphate dehydrogenase 2 is associated with diminished enzyme activity". Pharmacogenet. Genomics. 17 (4): 283–90. doi:10.1097/FPC.0b013e328012b8cf. PMID   17496727. S2CID   21301713.
• So HC, Fong PY, Chen RY, et al. (2010). "Identification of neuroglycan C and interacting partners as potential susceptibility genes for schizophrenia in a Southern Chinese population". Am. J. Med. Genet. B Neuropsychiatr. Genet. 153B (1): 103–13. doi:10.1002/ajmg.b.30961. PMID   19367581. S2CID   20522961. Archived from the original on 2019-09-28. Retrieved 2019-09-28.
• Grinyó J, Vanrenterghem Y, Nashan B, et al. (2008). "Association of four DNA polymorphisms with acute rejection after kidney transplantation". Transpl. Int. 21 (9): 879–91. doi:10.1111/j.1432-2277.2008.00679.x. PMID   18444945. S2CID   42432512.
• Ohmann EL, Burckart GJ, Brooks MM, et al. (2010). "Genetic polymorphisms influence mycophenolate mofetil-related adverse events in pediatric heart transplant patients". The Journal of Heart and Lung Transplantation. 29 (5): 509–516. doi:10.1016/j.healun.2009.11.602. PMID   20061166.
• Sombogaard F, van Schaik RH, Mathot RA, et al. (2009). "Interpatient variability in IMPDH activity in MMF-treated renal transplant patients is correlated with IMPDH type II 3757T > C polymorphism". Pharmacogenet. Genomics. 19 (8): 626–34. doi:10.1097/FPC.0b013e32832f5f1b. PMID   19617864. S2CID   41882586.
• Fellenberg J, Bernd L, Delling G, et al. (2007). "Prognostic significance of drug-regulated genes in high-grade osteosarcoma". Mod. Pathol. 20 (10): 1085–94. doi: 10.1038/modpathol.3800937 . PMID   17660802.
• Lim J, Hao T, Shaw C, et al. (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): 801–14. doi: 10.1016/j.cell.2006.03.032 . PMID   16713569. S2CID   13709685.
• He Y, Mou Z, Li W, et al. (2009). "Identification of IMPDH2 as a tumor-associated antigen in colorectal cancer using immunoproteomics analysis". Int J Colorectal Dis. 24 (11): 1271–9. doi:10.1007/s00384-009-0759-2. PMID   19597826. S2CID   24143679.
• Peñuelas S, Noé V, Ciudad CJ (2005). "Modulation of IMPDH2, survivin, topoisomerase I and vimentin increases sensitivity to methotrexate in HT29 human colon cancer cells". FEBS J. 272 (3): 696–710. doi: 10.1111/j.1742-4658.2004.04504.x . PMID   15670151. S2CID   43226077.
• Winnicki W, Weigel G, Sunder-Plassmann G, et al. (2010). "An inosine 5'-monophosphate dehydrogenase 2 single-nucleotide polymorphism impairs the effect of mycophenolic acid". Pharmacogenomics J. 10 (1): 70–6. doi: 10.1038/tpj.2009.43 . PMID   19770842.
• Patel CG, Richman K, Yang D, et al. (2007). "Effect of diabetes mellitus on mycophenolate sodium pharmacokinetics and inosine monophosphate dehydrogenase activity in stable kidney transplant recipients". Ther Drug Monit. 29 (6): 735–42. doi:10.1097/FTD.0b013e31815d8ace. PMC   4082794 . PMID   18043470.
• Sanquer S, Maison P, Tomkiewicz C, et al. (2008). "Expression of inosine monophosphate dehydrogenase type I and type II after mycophenolate mofetil treatment: a 2-year follow-up in kidney transplantation". Clin. Pharmacol. Ther. 83 (2): 328–35. doi:10.1038/sj.clpt.6100300. PMID   17713475. S2CID   44919245.
• Mohamed MF, Frye RF, Langaee TY (2008). "Interpopulation variation frequency of human inosine 5'-monophosphate dehydrogenase type II (IMPDH2) genetic polymorphisms". Genet. Test. 12 (4): 513–6. doi:10.1089/gte.2008.0049. PMID   18976158.
• Mannava S, Grachtchouk V, Wheeler LJ, et al. (2008). "Direct role of nucleotide metabolism in C-MYC-dependent proliferation of melanoma cells". Cell Cycle. 7 (15): 2392–400. doi:10.4161/cc.6390. PMC   3744895 . PMID   18677108.
• Chen L, Petrelli R, Olesiak M, et al. (2008). "Bis(sulfonamide) isosters of mycophenolic adenine dinucleotide analogues: inhibition of inosine monophosphate dehydrogenase". Bioorg. Med. Chem. 16 (15): 7462–9. doi:10.1016/j.bmc.2008.06.003. PMID   18583139.
• 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. Bibcode:2005BBRC..337.1308G. doi:10.1016/j.bbrc.2005.09.191. PMID   16236267.
• Kudo M, Saito Y, Sasaki T, et al. (2009). "Genetic variations in the HGPRT, ITPA, IMPDH1, IMPDH2, and GMPS genes in Japanese individuals". Drug Metab. Pharmacokinet. 24 (6): 557–64. doi:10.2133/dmpk.24.557. PMID   20045992.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC   1847948 . PMID   17353931.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.