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{{Infobox_gene}}
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'''Protein-S-isoprenylcysteine O-methyltransferase''' is an [[enzyme]] that in humans is encoded by the ''ICMT'' [[gene]].<ref name="pmid9614111">{{cite journal |vauthors=Dai Q, Choy E, Chiu V, Romano J, Slivka SR, Steitz SA, Michaelis S, Philips MR | title = Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum | journal = J Biol Chem | volume = 273 | issue = 24 | pages = 15030–4 |date=Jul 1998 | pmid = 9614111 | pmc =  | doi =10.1074/jbc.273.24.15030 }}</ref><ref name="pmid10441503">{{cite journal |vauthors=Desrosiers RR, Nguyen QT, Beliveau R | title = The carboxyl methyltransferase modifying G proteins is a metalloenzyme | journal = Biochem Biophys Res Commun | volume = 261 | issue = 3 | pages = 790–7 |date=Sep 1999 | pmid = 10441503 | pmc =  | doi = 10.1006/bbrc.1999.0936 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ICMT isoprenylcysteine carboxyl methyltransferase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23463| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Isoprenylcysteine carboxyl methyltransferase
| HGNCid = 5350
| Symbol = ICMT
| AltSymbols =; HSTE14; MGC39955; MST098; MSTP098; PCCMT; PCMT; PPMT
| OMIM = 605851
| ECnumber =
| Homologene = 5735
| MGIid = 1888594
  | GeneAtlas_image1 = PBB_GE_ICMT_201611_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ICMT_201609_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_ICMT_201610_at_tn.png
  | Function = {{GNF_GO|id=GO:0004671 |text = protein-S-isoprenylcysteine O-methyltransferase activity}} {{GNF_GO|id=GO:0008168 |text = methyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
  | Process = {{GNF_GO|id=GO:0006464 |text = protein modification process}} {{GNF_GO|id=GO:0006481 |text = C-terminal protein amino acid methylation}} {{GNF_GO|id=GO:0006612 |text = protein targeting to membrane}} {{GNF_GO|id=GO:0008104 |text = protein localization}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 23463
    | Hs_Ensembl = ENSG00000116237
    | Hs_RefseqProtein = NP_036537
    | Hs_RefseqmRNA = NM_012405
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 6203840
    | Hs_GenLoc_end = 6218619
    | Hs_Uniprot = O60725
    | Mm_EntrezGene = 57295
    | Mm_Ensembl = ENSMUSG00000039662
    | Mm_RefseqmRNA = NM_133788
    | Mm_RefseqProtein = NP_598549
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 151141104
    | Mm_GenLoc_end = 151150919
    | Mm_Uniprot = Q3U4N2
  }}
}}
'''Isoprenylcysteine carboxyl methyltransferase''', also known as '''ICMT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ICMT isoprenylcysteine carboxyl methyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23463| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: ICMT isoprenylcysteine carboxyl methyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23463| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Dai Q, Choy E, Chiu V, ''et al.'' |title=Mammalian prenylcysteine carboxyl methyltransferase is in the endoplasmic reticulum. |journal=J. Biol. Chem. |volume=273 |issue= 24 |pages= 15030-4 |year= 1998 |pmid= 9614111 |doi=  }}
*{{cite journal  | author=Choy E |title=Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi |journal=Cell |volume=98 |issue= 1 |pages= 69–80 |year= 1999 |pmid= 10412982 |doi= 10.1016/S0092-8674(00)80607-8  |name-list-format=vanc| author2=Chiu VK  | author3=Silletti J  | display-authors=3  | last4=Feoktistov  | first4=| last5=Morimoto  | first5=| last6=Michaelson  | first6=| last7=Ivanov  | first7=| last8=Philips  | first8=M }}
*{{cite journal  | author=Choy E, Chiu VK, Silletti J, ''et al.'' |title=Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi. |journal=Cell |volume=98 |issue= 1 |pages= 69-80 |year= 1999 |pmid= 10412982 |doi= 10.1016/S0092-8674(00)80607-8 }}
*{{cite journal  | author=Lin X |title=Polyglutamine expansion down-regulates specific neuronal genes before pathologic changes in SCA1 |journal=Nat. Neurosci. |volume=3 |issue= 2 |pages= 157–63 |year= 2000 |pmid= 10649571 |doi= 10.1038/72101 |name-list-format=vanc| author2=Antalffy B  | author3=Kang D  | display-authors=3  | last4=Kang  | first4=Dongcheul  | last5=Orr  | first5=Harry T. }}
*{{cite journal | author=Desrosiers RR, Nguyen QT, Béliveau R |title=The carboxyl methyltransferase modifying G proteins is a metalloenzyme. |journal=Biochem. Biophys. Res. Commun. |volume=261 |issue= 3 |pages= 790-7 |year= 1999 |pmid= 10441503 |doi= 10.1006/bbrc.1999.0936 }}
*{{cite journal  |vauthors=Van Dessel GA, De Busser HM, Lagrou AR |title=Prenylcysteine carboxymethyltransferase type III activity is decreased in retinoic acid-treated SH-SY5Y neuroblastoma cells |journal=Int. J. Biochem. Cell Biol. |volume=34 |issue= 5 |pages= 477–86 |year= 2002 |pmid= 11906819 |doi=10.1016/S1357-2725(01)00151-0 }}
*{{cite journal  | author=Lin X, Antalffy B, Kang D, ''et al.'' |title=Polyglutamine expansion down-regulates specific neuronal genes before pathologic changes in SCA1. |journal=Nat. Neurosci. |volume=3 |issue= 2 |pages= 157-63 |year= 2000 |pmid= 10649571 |doi= 10.1038/72101 }}
*{{cite journal  | author=Ahmad M |title=Role of isoprenylcysteine carboxyl methyltransferase in tumor necrosis factor-alpha stimulation of expression of vascular cell adhesion molecule-1 in endothelial cells |journal=Arterioscler. Thromb. Vasc. Biol. |volume=22 |issue= 5 |pages= 759–64 |year= 2002 |pmid= 12006387 |doi=10.1161/01.ATV.0000015884.61894.DC  |name-list-format=vanc| author2=Zhang Y  | author3=Zhang Y  | display-authors=3  | last4=Papharalambus  | first4=C  | last5=Alexander  | first5=RW }}
*{{cite journal  | author=Van Dessel GA, De Busser HM, Lagrou AR |title=Prenylcysteine carboxymethyltransferase type III activity is decreased in retinoic acid-treated SH-SY5Y neuroblastoma cells. |journal=Int. J. Biochem. Cell Biol. |volume=34 |issue= 5 |pages= 477-86 |year= 2002 |pmid= 11906819 |doi=  }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Ahmad M, Zhang Y, Zhang Y, ''et al.'' |title=Role of isoprenylcysteine carboxyl methyltransferase in tumor necrosis factor-alpha stimulation of expression of vascular cell adhesion molecule-1 in endothelial cells. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=22 |issue= 5 |pages= 759-64 |year= 2002 |pmid= 12006387 |doi=  }}
*{{cite journal  | author=Kramer K |title=Isoprenylcysteine carboxyl methyltransferase activity modulates endothelial cell apoptosis |journal=Mol. Biol. Cell |volume=14 |issue= 3 |pages= 848–57 |year= 2004 |pmid= 12631708 |doi= 10.1091/mbc.E02-07-0390 | pmc=151564  |name-list-format=vanc| author2=Harrington EO  | author3=Lu Q  | display-authors=3  | last4=Bellas  | first4=R  | last5=Newton  | first5=J  | last6=Sheahan  | first6=KL  | last7=Rounds  | first7=S }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Winter-Vann AM |title=Targeting Ras signaling through inhibition of carboxyl methylation: an unexpected property of methotrexate |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 11 |pages= 6529–34 |year= 2003 |pmid= 12750467 |doi= 10.1073/pnas.1135239100 | pmc=164480  |name-list-format=vanc| author2=Kamen BA  | author3=Bergo MO  | display-authors=3  | last4=Young  | first4=SG  | last5=Melnyk  | first5=S  | last6=James  | first6=SJ  | last7=Casey  | first7=PJ }}
*{{cite journal  | author=Kramer K, Harrington EO, Lu Q, ''et al.'' |title=Isoprenylcysteine carboxyl methyltransferase activity modulates endothelial cell apoptosis. |journal=Mol. Biol. Cell |volume=14 |issue= 3 |pages= 848-57 |year= 2004 |pmid= 12631708 |doi= 10.1091/mbc.E02-07-0390 }}
*{{cite journal  | author=Ota T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |name-list-format=vanc| author2=Suzuki Y  | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
*{{cite journal  | author=Winter-Vann AM, Kamen BA, Bergo MO, ''et al.'' |title=Targeting Ras signaling through inhibition of carboxyl methylation: an unexpected property of methotrexate. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 11 |pages= 6529-34 |year= 2003 |pmid= 12750467 |doi= 10.1073/pnas.1135239100 }}
*{{cite journal  | author=Bergo MO |title=Inactivation of Icmt inhibits transformation by oncogenic K-Ras and B-Raf |journal=J. Clin. Invest. |volume=113 |issue= 4 |pages= 539–50 |year= 2004 |pmid= 14966563 |doi= 10.1172/JCI18829  | pmc=338259  |name-list-format=vanc| author2=Gavino BJ  | author3=Hong C  | display-authors=3  | last4=Beigneux  | first4=AP  | last5=McMahon  | first5=M  | last6=Casey  | first6=PJ  | last7=Young  | first7=SG }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Brandenberger R |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707–16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 |name-list-format=vanc| author2=Wei H  | author3=Zhang S  | display-authors=3  | last4=Lei  | first4=Shirley  | last5=Murage  | first5=Jaji  | last6=Fisk  | first6=Gregory J  | last7=Li  | first7=Yan  | last8=Xu  | first8=Chunhui  | last9=Fang  | first9=Rixun }}
*{{cite journal  | author=Bergo MO, Gavino BJ, Hong C, ''et al.'' |title=Inactivation of Icmt inhibits transformation by oncogenic K-Ras and B-Raf. |journal=J. Clin. Invest. |volume=113 |issue= 4 |pages= 539-50 |year= 2004 |pmid= 14966563 |doi= 10.1172/JCI200418829 }}
*{{cite journal  | author=Gerhard DS |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal  | author=Brandenberger R, Wei H, Zhang S, ''et al.'' |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707-16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 }}
*{{cite journal  | author=Lu Q |title=Inhibition of ICMT induces endothelial cell apoptosis through GRP94 |journal=Am. J. Respir. Cell Mol. Biol. |volume=37 |issue= 1 |pages= 20–30 |year= 2007 |pmid= 17347446 |doi= 10.1165/rcmb.2006-0301SM | pmc=1899353  |name-list-format=vanc| author2=Harrington EO  | author3=Newton J  | display-authors=3  | last4=Jankowich  | first4=M.  | last5=Rounds  | first5=S. }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Lu Q, Harrington EO, Newton J, ''et al.'' |title=Inhibition of ICMT induces endothelial cell apoptosis through GRP94. |journal=Am. J. Respir. Cell Mol. Biol. |volume=37 |issue= 1 |pages= 20-30 |year= 2007 |pmid= 17347446 |doi= 10.1165/rcmb.2006-0301SM }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
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{{gene-1-stub}}

Latest revision as of 23:31, 31 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. 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.
  2. 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.
  3. 3.0 3.1 "Entrez Gene: ICMT isoprenylcysteine carboxyl methyltransferase".

Further reading