PCMT1

Protein-L-isoaspartate (D-aspartate) O-methyltransferase
File:PBB Protein PCMT1 image.jpg PDB rendering based on 1i1n.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1i1n​, 1kr5​
Identifiers
Symbols	PCMT1 ;
External IDs	Template:OMIM5 Template:MGI HomoloGene: 55895
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE PCMT1 210156 s at tn.png
File:PBB GE PCMT1 205202 at tn.png
File:PBB GE PCMT1 208857 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Protein-L-isoaspartate (D-aspartate) O-methyltransferase, also known as PCMT1, is a human 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. PMID 1339271.CS1 maint: Multiple names: authors list (link)
• MacLaren DC, O'Connor CM, Xia YR; et al. (1993). "The L-isoaspartyl/D-aspartyl protein methyltransferase gene (PCMT1) maps to human chromosome 6q22.3-6q24 and the syntenic region of mouse chromosome 10". Genomics. 14 (4): 852–6. PMID 1478665.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 1998518.CS1 maint: Multiple names: authors list (link)
• 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. PMID 2684970.CS1 maint: Multiple names: authors list (link)
• 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. PMID 3167043.CS1 maint: Multiple names: authors list (link)
• 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. PMID 3355545.CS1 maint: Multiple names: authors list (link)
• 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. PMID 7592526.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. doi:10.1006/abbi.1996.0513. PMID 8914929.CS1 maint: Multiple names: authors list (link)
• DeVry CG, Clarke S (1999). "Assignment of the protein L-isoaspartate (D-aspartate) O-methyltransferase gene (PCMT1) to human chromosome bands 6q24-->q25 with radiation hybrid mapping". Cytogenet. Cell Genet. 84 (1–2): 130–1. PMID 10343128.
• 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. 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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-A resolution and modeling of an isoaspartyl-containing peptide at the active site". Protein Sci. 11 (3): 625–35. PMID 11847284.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 12943661.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 16256389.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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: 89. doi:10.1038/msb4100134. PMID 17353931.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)