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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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  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  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 ]