PCMT1

PCMT1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1I1N, 1KR5
Identifiers
Aliases	PCMT1, PIMT, protein-L-isoaspartate (D-aspartate) O-methyltransferase
External IDs	OMIM: 176851; MGI: 97502; HomoloGene: 55895; GeneCards: PCMT1; OMA:PCMT1 - orthologs
Gene location (Human) Chr. Chromosome 6 (human) Band 6q25.1 Start 149,749,443 bp End 149,811,420 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10 A1|10 2.26 cM Start 7,629,373 bp End 7,681,136 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in endothelial cell Brodmann area 23 middle temporal gyrus pons frontal pole spinal ganglia prefrontal cortex orbitofrontal cortex trigeminal ganglion superior vestibular nucleus Top expressed in spermatocyte hypothalamus testicle lens quadriceps femoris muscle primary visual cortex superior frontal gyrus neural tube hippocampus proper cerebellar cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function methyltransferase activity transferase activity protein binding protein-L-isoaspartate (D-aspartate) O-methyltransferase activity cadherin binding Cellular component extracellular vesicle extracellular exosome cytoplasm cytosol Biological process methylation protein repair protein methylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5110 18537 Ensembl ENSG00000120265 ENSMUSG00000019795 UniProt P22061 P23506 RefSeq (mRNA) NM_001252049 NM_001252050 NM_001252051 NM_001252052 NM_001252053 NM_005389 NM_001360452 NM_001360456 NM_008786 NM_001347228 NM_001358647 NM_001358649 NM_001358651 NM_001358652 NM_001358653 NM_001358654 NM_001358657 RefSeq (protein) NP_001238978 NP_001238979 NP_001238980 NP_001238981 NP_001238982 NP_005380 NP_001347381 NP_001347385 n/a Location (UCSC) Chr 6: 149.75 – 149.81 Mb Chr 10: 7.63 – 7.68 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

Three classes of protein carboxyl methyltransferases, distinguished by their methyl-acceptor substrate specificity, have been found in prokaryotic and eukaryotic cells. The type II enzyme catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the free carboxyl groups of D-aspartyl and L-isoaspartyl residues. These methyl-accepting residues result from the spontaneous deamidation, isomerization, and racemization of normal L-aspartyl and L-asparaginyl residues and represent sites of covalent damage to aging proteins PCMT1 (EC 2.1.1.77) is a protein repair enzyme that initiates the conversion of abnormal D-aspartyl and L-isoaspartyl residues to the normal L-aspartyl form.[supplied by OMIM]

Further reading

• MacLaren DC, Kagan RM, Clarke S (1992). "Alternative splicing of the human isoaspartyl protein carboxyl methyltransferase RNA leads to the generation of a C-terminal -RDEL sequence in isozyme II". Biochem. Biophys. Res. Commun. 185 (1): 277–83. doi:10.1016/S0006-291X(05)80987-8. PMID 1339271.
• Ingrosso D, Kagan RM, Clarke S (1991). "Distinct C-terminal sequences of isozymes I and II of the human erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase". Biochem. Biophys. Res. Commun. 175 (1): 351–8. doi:10.1016/S0006-291X(05)81242-2. PMID 1998518.
• Ingrosso D, Fowler AV, Bleibaum J, Clarke S (1989). "Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA, and small molecule S-adenosylmethionine-dependent methyltransferases". J. Biol. Chem. 264 (33): 20131–9. doi:10.1016/S0021-9258(19)47228-1. PMID 2684970.
• Gilbert JM, Fowler A, Bleibaum J, Clarke S (1988). "Purification of homologous protein carboxyl methyltransferase isozymes from human and bovine erythrocytes". Biochemistry. 27 (14): 5227–33. doi:10.1021/bi00414a042. PMID 3167043.
• Ota IM, Gilbert JM, Clarke S (1988). "Two major isozymes of the protein D-aspartyl/L-isoaspartyl methyltransferase from human erythrocytes". Biochem. Biophys. Res. Commun. 151 (3): 1136–43. doi:10.1016/S0006-291X(88)80484-4. PMID 3355545.
• Takeda R, Mizobuchi M, Murao K, et al. (1995). "Characterization of three cDNAs encoding two isozymes of an isoaspartyl protein carboxyl methyltransferase from human erythroid leukemia cells". J. Biochem. 117 (4): 683–5. doi:10.1093/jb/117.2.267. PMID 7592526.
• Tsai W, Clarke S (1994). "Amino acid polymorphisms of the human L-isoaspartyl/D-aspartyl methyltransferase involved in protein repair". Biochem. Biophys. Res. Commun. 203 (1): 491–7. doi:10.1006/bbrc.1994.2209. PMID 8074695.
• DeVry CG, Tsai W, Clarke S (1997). "Structure of the human gene encoding the protein repair L-isoaspartyl (D-aspartyl) O-methyltransferase". Arch. Biochem. Biophys. 335 (2): 321–32. CiteSeerX 10.1.1.630.8527. doi:10.1006/abbi.1996.0513. PMID 8914929.
• DeVry CG, Clarke S (1999). "Polymorphic forms of the protein L-isoaspartate (D-aspartate) O-methyltransferase involved in the repair of age-damaged proteins". J. Hum. Genet. 44 (5): 275–88. doi:10.1007/s100380050161. PMID 10496068.
• Ryttersgaard C, Griffith SC, Sawaya MR, et al. (2002). "Crystal structure of human L-isoaspartyl methyltransferase". J. Biol. Chem. 277 (12): 10642–6. doi:10.1074/jbc.M200229200. PMID 11792715.
• Smith CD, Carson M, Friedman AM, et al. (2002). "Crystal structure of human L-isoaspartyl-O-methyl-transferase with S-adenosyl homocysteine at 1.6-Å resolution and modeling of an isoaspartyl-containing peptide at the active site". Protein Sci. 11 (3): 625–35. doi:10.1110/ps.37802. PMC 2373461. PMID 11847284.
• Misra P, Qi C, Yu S, et al. (2002). "Interaction of PIMT with transcriptional coactivators CBP, p300, and PBP differential role in transcriptional regulation". J. Biol. Chem. 277 (22): 20011–9. doi:10.1074/jbc.M201739200. PMID 11912212.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Enünlü I, Pápai G, Cserpán I, et al. (2003). "Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus". Biochem. Biophys. Res. Commun. 309 (1): 44–51. doi:10.1016/S0006-291X(03)01514-6. PMID 12943661.
• 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.
• Zhu H, Yang W, Lu W, et al. (2006). "A known functional polymorphism (Ile120Val) of the human PCMT1 gene and risk of spina bifida". Mol. Genet. Metab. 87 (1): 66–70. doi:10.1016/j.ymgme.2005.09.008. PMC 2947858. PMID 16256389.
• Lanthier J, Desrosiers RR (2007). "Regulation of protein L-isoaspartyl methyltransferase by cell-matrix interactions: involvement of integrin alphavbeta3, PI 3-kinase, and the proteasome". Biochem. Cell Biol. 84 (5): 684–94. doi:10.1139/o06-055. PMID 17167531.
• 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.