ICMT

Isoprenylcysteine carboxyl methyltransferase

Identifiers

ICMT; HSTE14; MGC39955; MST098; MSTP098; PCCMT; PCMT; PPMT

External IDs

OMIM: 605851 MGI: 1888594 HomoloGene: 5735 GeneCards: ICMT Gene

2.1.1.100

Gene Ontology
Molecular function	• protein C-terminal carboxyl O-methyltransferase activity • protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity • cAMP response element binding protein binding • methyltransferase activity • transferase activity
Cellular component	• membrane fraction • endoplasmic reticulum • endoplasmic reticulum membrane • membrane • integral to membrane
Biological process	• in utero embryonic development • liver development • protein modification process • C-terminal protein methylation • protein targeting to membrane • protein localization • positive regulation of cell proliferation • multicellular organism growth • S-adenosylhomocysteine metabolic process • S-adenosylmethioninamine metabolic process • regulation of Ras protein signal transduction
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 4:
151.67 – 151.68 Mb

PubMed search

[1]

[2]

Protein-S-isoprenylcysteine O-methyltransferase is an enzyme that in humans is encoded by the ICMT gene.^[1]^[2]^[3]

This gene encodes the third of three enzymes that posttranslationally modify isoprenylated C-terminal cysteine residues in certain proteins and target those proteins to the cell membrane. This enzyme localizes to the endoplasmic reticulum. Alternative splicing may result in other transcript variants, but the biological validity of those transcripts has not been determined.^[3]

References

^ Dai Q, Choy E, Chiu V, Romano J, Slivka SR, Steitz SA, Michaelis S, Philips MR (Jul 1998). "Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum". J Biol Chem 273 (24): 15030–4. doi:10.1074/jbc.273.24.15030. PMID 9614111.
^ Desrosiers RR, Nguyen QT, Beliveau R (Sep 1999). "The carboxyl methyltransferase modifying G proteins is a metalloenzyme". Biochem Biophys Res Commun 261 (3): 790–7. doi:10.1006/bbrc.1999.0936. PMID 10441503.
^ ^a ^b "Entrez Gene: ICMT isoprenylcysteine carboxyl methyltransferase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23463.

Choy E, Chiu VK, Silletti J et al. (1999). "Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi". Cell 98 (1): 69–80. doi:10.1016/S0092-8674(00)80607-8. PMID 10412982.
Lin X, Antalffy B, Kang D et al. (2000). "Polyglutamine expansion down-regulates specific neuronal genes before pathologic changes in SCA1". Nat. Neurosci. 3 (2): 157–63. doi:10.1038/72101. PMID 10649571.
Van Dessel GA, De Busser HM, Lagrou AR (2002). "Prenylcysteine carboxymethyltransferase type III activity is decreased in retinoic acid-treated SH-SY5Y neuroblastoma cells". Int. J. Biochem. Cell Biol. 34 (5): 477–86. doi:10.1016/S1357-2725(01)00151-0. PMID 11906819.
Ahmad M, Zhang Y, Zhang Y et al. (2002). "Role of isoprenylcysteine carboxyl methyltransferase in tumor necrosis factor-alpha stimulation of expression of vascular cell adhesion molecule-1 in endothelial cells". Arterioscler. Thromb. Vasc. Biol. 22 (5): 759–64. doi:10.1161/01.ATV.0000015884.61894.DC. PMID 12006387.
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.
Kramer K, Harrington EO, Lu Q et al. (2004). "Isoprenylcysteine carboxyl methyltransferase activity modulates endothelial cell apoptosis". Mol. Biol. Cell 14 (3): 848–57. doi:10.1091/mbc.E02-07-0390. PMC 151564. PMID 12631708. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=151564.
Winter-Vann AM, Kamen BA, Bergo MO et al. (2003). "Targeting Ras signaling through inhibition of carboxyl methylation: an unexpected property of methotrexate". Proc. Natl. Acad. Sci. U.S.A. 100 (11): 6529–34. doi:10.1073/pnas.1135239100. PMC 164480. PMID 12750467. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=164480.
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.
Bergo MO, Gavino BJ, Hong C et al. (2004). "Inactivation of Icmt inhibits transformation by oncogenic K-Ras and B-Raf". J. Clin. Invest. 113 (4): 539–50. doi:10.1172/JCI200418829. PMC 338259. PMID 14966563. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=338259.
Brandenberger R, Wei H, Zhang S et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197.
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.
Lu Q, Harrington EO, Newton J et al. (2007). "Inhibition of ICMT induces endothelial cell apoptosis through GRP94". Am. J. Respir. Cell Mol. Biol. 37 (1): 20–30. doi:10.1165/rcmb.2006-0301SM. PMC 1899353. PMID 17347446. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1899353.

ICMT

References

Further reading