Leucine carboxyl methyltransferase 1

LCMT1
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 3IEI, 3O7W, 3P71
Identifiers
Aliases	LCMT1, LCMT, PPMT1, CGI-68, leucine carboxyl methyltransferase 1
External IDs	MGI: 1353593 HomoloGene: 41123 GeneCards: LCMT1
Gene ontology Molecular function • methyltransferase activity • protein C-terminal leucine carboxyl O-methyltransferase activity • protein methyltransferase activity • S-adenosylmethionine-dependent methyltransferase activity • transferase activity • protein binding • protein C-terminal carboxyl O-methyltransferase activity Cellular component • cytosol Biological process • regulation of mitotic cell cycle spindle assembly checkpoint • methylation • C-terminal protein methylation • regulation of glucose metabolic process • regulation of apoptotic process • negative regulation of protein complex assembly • cellular protein modification process • protein methylation Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	51451	30949
Ensembl	ENSG00000205629	ENSMUSG00000030763
UniProt	Q9UIC8	n/a
RefSeq (mRNA)	NM_001032391 NM_016309	NM_025304
RefSeq (protein)	NP_001027563.1 NP_057393.2	n/a
Location (UCSC)	Chr 16: 25.11 – 25.18 Mb	Chr 7: 123.37 – 123.43 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Leucine carboxyl methyltransferase 1 is an enzyme that in humans is encoded by the LCMT1 gene.^[3][4]

Interactions

LCMT1 has been shown to interact with FXR2.^[5]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W (May 2000). "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics". Genome Research. 10 (5): 703–13. doi:10.1101/gr.10.5.703. PMC 310876. PMID 10810093.
4. "Entrez Gene: LCMT1 leucine carboxyl methyltransferase 1".
5. Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

Further reading

• Lee JA, Pallas DC (Oct 2007). "Leucine carboxyl methyltransferase-1 is necessary for normal progression through mitosis in mammalian cells". The Journal of Biological Chemistry. 282 (42): 30974–84. doi:10.1074/jbc.M704861200. PMC 3516869. PMID 17724024.
• De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J (Dec 1999). "Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue". Biochemistry. 38 (50): 16539–47. doi:10.1021/bi991646a. PMID 10600115.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 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.
• Maruyama K, Sugano S (Jan 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.