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Identification
HMDB Protein ID HMDBP00412
Secondary Accession Numbers
  • 5649
Name Protein-L-isoaspartate(D-aspartate) O-methyltransferase
Synonyms
  1. L-isoaspartyl protein carboxyl methyltransferase
  2. PIMT
  3. Protein L-isoaspartyl/D-aspartyl methyltransferase
  4. Protein-beta-aspartate methyltransferase
Gene Name PCMT1
Protein Type Unknown
Biological Properties
General Function Involved in protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
Specific Function Catalyzes the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. Acts on microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin carboxyl-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein (By similarity).
Pathways Not Available
Reactions
S-Adenosylmethionine + protein L-isoaspartate → S-Adenosylhomocysteine + protein L-isoaspartate alpha-methyl ester details
GO Classification
Biological Process
protein repair
S-adenosylhomocysteine metabolic process
S-adenosylmethionine metabolic process
Cellular Component
endoplasmic reticulum
Function
catalytic activity
transferase activity
s-adenosylmethionine-dependent methyltransferase activity
protein-l-isoaspartate (d-aspartate) o-methyltransferase activity
transferase activity, transferring one-carbon groups
methyltransferase activity
Molecular Function
protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
Process
metabolic process
macromolecule metabolic process
macromolecule modification
protein modification process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 6
Locus 6q24-q25
SNPs PCMT1
Gene Sequence
>684 bp
ATGGCCTGGAAATCCGGCGGCGCCAGCCACTCGGAGCTAATCCACAATCTCCGCAAAAAT
GGAATCATCAAGACAGATAAAGTATTTGAAGTGATGCTGGCTACAGACCGCTCCCACTAT
GCAAAATGTAACCCATACATGGATTCTCCACAATCAATAGGTTTCCAAGCAACAATCAGT
GCTCCACACATGCATGCATATGCGCTAGAACTTCTATTTGATCAGTTGCATGAAGGAGCT
AAAGCTCTTGATGTAGGATCTGGAAGTGGAATCCTTACTGCATGTTTTGCACGTATGGTT
GGATGTACTGGAAAAGTCATAGGAATTGATCACATTAAAGAGCTAGTAGATGACTCAGTA
AATAATGTCAGGAAGGACGATCCAACACTTCTGTCTTCAGGGAGAGTACAGCTTGTTGTG
GGGGATGGAAGAATGGGATATGCTGAAGAAGCCCCTTATGATGCCATTCATGTGGGAGCT
GCAGCCCCTGTTGTACCCCAGGCGCTAATAGATCAGTTAAAGCCCGGAGGAAGATTGATA
TTGCCTGTTGGTCCTGCAGGCGGAAACCAAATGTTGGAGCAGTATGACAAGCTACAAGAT
GGCAGCATCAAAATGAAGCCTCTGATGGGGGTGATATACGTGCCTTTAACAGATAAAGAA
AAGCAGTGGTCCAGGTGGAAGTGA
Protein Properties
Number of Residues 227
Molecular Weight 30357.695
Theoretical pI 6.725
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Protein-L-isoaspartate(D-aspartate) O-methyltransferase
MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATIS
APHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSI
NNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLI
LPVGPAGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLTDKEKQWSRWK
GenBank ID Protein 158260471
UniProtKB/Swiss-Prot ID P22061
UniProtKB/Swiss-Prot Entry Name PIMT_HUMAN
PDB IDs
GenBank Gene ID AK289724
GeneCard ID PCMT1
GenAtlas ID PCMT1
HGNC ID HGNC:8728
References
General References
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  4. Ingrosso D, Fowler AV, Bleibaum J, Clarke S: 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. 1989 Nov 25;264(33):20131-9. [PubMed:2684970 ]
  5. MacLaren DC, Kagan RM, Clarke S: 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. 1992 May 29;185(1):277-83. [PubMed:1339271 ]
  6. Takeda R, Mizobuchi M, Murao K, Sato M, Takahara J: Characterization of three cDNAs encoding two isozymes of an isoaspartyl protein carboxyl methyltransferase from human erythroid leukemia cells. J Biochem. 1995 Apr;117(4):683-5. [PubMed:7592526 ]
  7. DeVry CG, Tsai W, Clarke S: Structure of the human gene encoding the protein repair L-isoaspartyl (D-aspartyl) O-methyltransferase. Arch Biochem Biophys. 1996 Nov 15;335(2):321-32. [PubMed:8914929 ]
  8. Gilbert JM, Fowler A, Bleibaum J, Clarke S: Purification of homologous protein carboxyl methyltransferase isozymes from human and bovine erythrocytes. Biochemistry. 1988 Jul 12;27(14):5227-33. [PubMed:3167043 ]
  9. Tsai W, Clarke S: Amino acid polymorphisms of the human L-isoaspartyl/D-aspartyl methyltransferase involved in protein repair. Biochem Biophys Res Commun. 1994 Aug 30;203(1):491-7. [PubMed:8074695 ]
  10. Ingrosso D, Kagan RM, Clarke S: Distinct C-terminal sequences of isozymes I and II of the human erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase. Biochem Biophys Res Commun. 1991 Feb 28;175(1):351-8. [PubMed:1998518 ]
  11. DeVry CG, Clarke S: Polymorphic forms of the protein L-isoaspartate (D-aspartate) O-methyltransferase involved in the repair of age-damaged proteins. J Hum Genet. 1999;44(5):275-88. [PubMed:10496068 ]
  12. Ryttersgaard C, Griffith SC, Sawaya MR, MacLaren DC, Clarke S, Yeates TO: Crystal structure of human L-isoaspartyl methyltransferase. J Biol Chem. 2002 Mar 22;277(12):10642-6. Epub 2002 Jan 15. [PubMed:11792715 ]
  13. Smith CD, Carson M, Friedman AM, Skinner MM, Delucas L, Chantalat L, Weise L, Shirasawa T, Chattopadhyay D: 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. 2002 Mar;11(3):625-35. [PubMed:11847284 ]