PCMT1

PCMT1
Available structures
PDB	Human UniProt 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 HomoloGene: 55895 GeneCards: PCMT1
Gene location (Human)
Chr.	Chromosome 6 (human)
End	149,811,420 bp
RNA expression pattern
	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;
	n/a
	More reference expression data
	; ; ; ;
	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
	5110
	n/a
	ENSG00000120265
	n/a
	P22061
	n/a
NM_001252049 ; NM_001252050 ; NM_001252051 ; NM_001252052 ; NM_001252053 ;
	NM_005389 ; NM_001360452 ; NM_001360456
	n/a
NP_001238978 ; NP_001238979 ; NP_001238980 ; NP_001238981 ; NP_001238982 ;
	NP_005380 ; NP_001347381 ; NP_001347385
	n/a
	Wikidata
View/Edit Human

Last updated March 28, 2024

Protein-L-isoaspartate(D-aspartate) O-methyltransferase is an enzyme that in humans is encoded by the PCMT1 gene.^[3]^[4]^[5]

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]^[5]

Related Research Articles

Isoaspartic acid is an aspartic acid residue isomeric to the typical α peptide linkage. It is a β-amino acid, with the side chain carboxyl moved to the backbone. Such a change is caused by a chemical reaction in which the nitrogen atom on the N+1 following peptide bond nucleophilically attacks the γ-carbon of the side chain of an asparagine or aspartic acid residue, forming a succinimide intermediate. Hydrolysis of the intermediate results in two products, either aspartic acid or isoaspartic acid, which is a β-amino acid. The reaction also results in the deamidation of the asparagine residue. Racemization may occur leading to the formation of D-aminoacids.

Aldolase B also known as fructose-bisphosphate aldolase B or liver-type aldolase is one of three isoenzymes of the class I fructose 1,6-bisphosphate aldolase enzyme, and plays a key role in both glycolysis and gluconeogenesis. The generic fructose 1,6-bisphosphate aldolase enzyme catalyzes the reversible cleavage of fructose 1,6-bisphosphate (FBP) into glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP) as well as the reversible cleavage of fructose 1-phosphate (F1P) into glyceraldehyde and dihydroxyacetone phosphate. In mammals, aldolase B is preferentially expressed in the liver, while aldolase A is expressed in muscle and erythrocytes and aldolase C is expressed in the brain. Slight differences in isozyme structure result in different activities for the two substrate molecules: FBP and fructose 1-phosphate. Aldolase B exhibits no preference and thus catalyzes both reactions, while aldolases A and C prefer FBP.

Cathepsin A is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the CTSA gene.

Prosaposin, also known as PSAP, is a protein which in humans is encoded by the PSAP gene.

Insulin-like growth factor-binding protein 5(IBF-5) is a protein that in humans is encoded by the IGFBP5 gene. An IGFBP5 gene was recently identified as being important for adaptation to varying water salinity in fish.

Cytochrome b5, form A, is a human microsomal cytochrome b5.

Calpastatin is a protein that in humans is encoded by the CAST gene.

Beta-1,4-galactosyltransferase 1 is an enzyme that in humans is encoded by the B4GALT1 gene.

Ran-binding protein 9 is a protein that in humans is encoded by the RANBP9 gene.

Disintegrin and metalloproteinase domain-containing protein 9 is an enzyme that in humans is encoded by the ADAM9 gene.

Alcohol dehydrogenase class-3 is an enzyme that in humans is encoded by the ADH5 gene.

Sterile alpha motif and leucine zipper containing kinase AZK, also known as ZAK, is a human gene.

Phosphofructokinase, platelet, also known as PFKP is an enzyme which in humans is encoded by the PFKP gene.

Tropomodulin-1 is a protein that in humans is encoded by the TMOD1 gene.

Aspartyl-tRNA synthetase, cytoplasmic is an enzyme that in humans is encoded by the DARS gene.

Triadin, also known as TRDN, is a human gene associated with the release of calcium ions from the sarcoplasmic reticulum triggering muscular contraction through calcium-induced calcium release. Triadin is a multiprotein family, arising from different processing of the TRDN gene on chromosome 6. It is a transmembrane protein on the sarcoplasmic reticulum due to a well defined hydrophobic section and it forms a quaternary complex with the cardiac ryanodine receptor (RYR2), calsequestrin (CASQ2) and junctin proteins. The luminal (inner compartment of the sarcoplasmic reticulum) section of Triadin has areas of highly charged amino acid residues that act as luminal Ca²⁺ receptors. Triadin is also able to sense luminal Ca²⁺ concentrations by mediating interactions between RYR2 and CASQ2. Triadin has several different forms; Trisk 95 and Trisk 51, which are expressed in skeletal muscle, and Trisk 32 (CT1), which is mainly expressed in cardiac muscle.

Aspartate aminotransferase, cytoplasmic is an enzyme that in humans is encoded by the GOT1 gene.

Protein-S-isoprenylcysteine O-methyltransferase is an enzyme that in humans is encoded by the ICMT gene.

NEDD9-interacting protein with calponin homology and LIM domains is a protein that in humans is encoded by the MICAL1 gene.

Solute carrier family 2, facilitated glucose transporter member 12 is a protein that in humans is encoded by the SLC2A12 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000120265 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ MacLaren DC, O'Connor CM, Xia YR, Mehrabian M, Klisak I, Sparkes RS, Clarke S, Lusis AJ (Feb 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. doi:10.1016/S0888-7543(05)80104-1. PMID 1478665.
↑ DeVry CG, Clarke S (Jun 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. doi:10.1159/000015239. PMID 10343128. S2CID 38976877.
1 2 "Entrez Gene: PCMT1 protein-L-isoaspartate (D-aspartate) O-methyltransferase".

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.

This article on a gene on human chromosome 6 is a stub. You can help Wikipedia by expanding it.

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000120265 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1478665-3] MacLaren DC, O'Connor CM, Xia YR, Mehrabian M, Klisak I, Sparkes RS, Clarke S, Lusis AJ (Feb 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. doi:10.1016/S0888-7543(05)80104-1. PMID 1478665.

[pmid10343128-4] DeVry CG, Clarke S (Jun 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. doi:10.1159/000015239. PMID 10343128. S2CID 38976877.

[entrez-5] 1 2 "Entrez Gene: PCMT1 protein-L-isoaspartate (D-aspartate) O-methyltransferase".

[1]

[2]

[3]

[4]

[5]

PCMT1

Related Research Articles

References

Further reading