ICMT

Last updated
ICMT
Identifiers
Aliases ICMT , HSTE14, MST098, MSTP098, PCCMT, PCMT, PPMT, isoprenylcysteine carboxyl methyltransferase, ICMT protein, human
External IDs OMIM: 605851 MGI: 1888594 HomoloGene: 5735 GeneCards: ICMT
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_012405
NM_170705

NM_133788

RefSeq (protein)

NP_036537

NP_598549

Location (UCSC) Chr 1: 6.22 – 6.24 Mb Chr 4: 152.3 – 152.31 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Protein-S-isoprenylcysteine O-methyltransferase is an enzyme that in humans is encoded by the ICMT gene. [5] [6] [7]

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. [7]

Related Research Articles

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<span class="mw-page-title-main">DMAP1</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">PCMT1</span>

Protein-L-isoaspartate(D-aspartate) O-methyltransferase is an enzyme that in humans is encoded by the PCMT1 gene.

<span class="mw-page-title-main">DNAJB11</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">USP16</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">PIGS (gene)</span>

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<span class="mw-page-title-main">LCMT2</span>

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<span class="mw-page-title-main">FTSJ3</span> Enzyme

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<span class="mw-page-title-main">RASGRF2</span>

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<span class="mw-page-title-main">RCE1</span>

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<span class="mw-page-title-main">METTL3</span> Gene encodes the 70 kDa subunit of MT-A which is part of N6-adenosine-methyltransferase

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Protein methylation is a type of post-translational modification featuring the addition of methyl groups to proteins. It can occur on the nitrogen-containing side-chains of arginine and lysine, but also at the amino- and carboxy-termini of a number of different proteins. In biology, methyltransferases catalyze the methylation process, activated primarily by S-adenosylmethionine. Protein methylation has been most studied in histones, where the transfer of methyl groups from S-adenosyl methionine is catalyzed by histone methyltransferases. Histones that are methylated on certain residues can act epigenetically to repress or activate gene expression.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000116237 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000039662 - 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. 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.
  6. 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.
  7. 1 2 "Entrez Gene: ICMT isoprenylcysteine carboxyl methyltransferase".

Further reading