PCMT1

From Wikipedia, the free encyclopedia

Protein-L-isoaspartate (D-aspartate) O-methyltransferase

PDB rendering based on 1i1n.

Available structures: 1i1n, 1kr5

Identifiers

Symbol(s)

PCMT1;

External IDs

OMIM: 176851 MGI: 97502 HomoloGene: 55895

Gene ontology
Molecular Function:	• protein-L-isoaspartate (D-aspartate) O-methyltransferase activity • methyltransferase activity • transferase activity
Cellular Component:	• endoplasmic reticulum
Biological Process:	• protein modification process • protein amino acid methylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005389 (mRNA)
NP_005380 (protein)

NM_008786 (mRNA)
NP_032812 (protein)

Location

Chr 6: 150.11 - 150.17 Mb

Chr 10: 7.32 - 7.35 Mb

Pubmed search

[1]

[2]

Protein-L-isoaspartate (D-aspartate) O-methyltransferase, also known as PCMT1, is a human gene.^[1]

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]^[1]

[edit] References

^ ^a ^b Entrez Gene: PCMT1 protein-L-isoaspartate (D-aspartate) O-methyltransferase.

[edit] 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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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. doi:10.1073/pnas.242603899. 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. 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. 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. 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: 89. doi:10.1038/msb4100134. PMID 17353931.