NameProtein-L-isoaspartate(D-aspartate) O-methyltransferase
Synonyms
  • 2.1.1.77
  • L-isoaspartyl protein carboxyl methyltransferase
  • PIMT
  • Protein L-isoaspartyl/D-aspartyl methyltransferase
  • Protein-beta-aspartate methyltransferase
Gene NamePCMT1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0037130|Protein-L-isoaspartate(D-aspartate) O-methyltransferase
MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKCNPYMDSPQSIGFQATIS
APHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGCTGKVIGIDHIKELVDDSV
NNVRKDDPTLLSSGRVQLVVGDGRMGYAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLI
LPVGPAGGNQMLEQYDKLQDGSIKMKPLMGVIYVPLTDKEKQWSRWK
Number of residues227
Molecular Weight24636.21
Theoretical pI7.25
GO Classification
Functions
  • protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
Processes
  • protein repair
  • protein methylation
Components
  • extracellular exosome
  • extracellular vesicle
  • cytoplasm
  • endoplasmic reticulum
General FunctionProtein-l-isoaspartate (d-aspartate) o-methyltransferase activity
Specific FunctionCatalyzes 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 EIF4EBP2, 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.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID180637
UniProtKB IDP22061
UniProtKB Entry NamePIMT_HUMAN
Cellular LocationCytoplasm
Gene sequence
>lcl|BSEQ0019071|Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT1)
ATGCCGGGAGCGCGCAGTGGCGGCAGCGGCGGCGACGGCAGTAACAGCGGCAGCTACAGC
GGGGACGCGAGCGGGGCGGTGACGGTGTGGGAGGTGGTCTCACTCTTGGGAAAACTGCTG
GGCACCGTCGTCGCGCTGAAGGTGGTTCTGTACCTGCTCCGAGTGTGCTTAGCGATGGCC
TGGAAATCCGGCGGCGCCAGCCACTCGGAGCTAATCCACAATCTCCGCAAAAATGGAATC
ATCAAGACAGATAAAGTATTTGAAGTGATGCTGGCTACAGACCGCTCCCACTATGCAAAA
TGTAACCCATACATGGATTCTCCACAATCAATAGGTTTCCAAGCAACAATCAGTGCTCCA
CACATGCATGCATATGCGCTAGAACTTCTATTTGATCAGTTGCATGAAGGAGCTAAAGCT
CTTGATGTAGGATCTGGAAGTGGAATCCTTACTGCATGTTTTGCACGTATGGTTGGATGT
ACTGGAAAAGTCATAGGAATTGATCACATTAAAGAGCTAGTAGATGACTCAGTAAATAAT
GTCAGGAAGGACGATCCAACACTTCTGTCTTCAGGGAGAGTACAGCTTGTTGTGGGGGAT
GGAAGAATGGGATATGCTGAAGAAGCCCCTTATGATGCCATTCATGTGGGAGCTGCAGCC
CCTGTTGTACCCCAGGCGCTAATAGATCAGTTAAAGCCCGGAGGAAGATTGATATTGCCT
GTTGGTCCTGCAGGCGGAAACCAAATGTTGGAGCAGTATGACAAGCTACAAGATGGCAGC
ATCAAAATGAAGCCTCTGATGGGGGTGATATACGTGCCTTTAACAGATAAAGAAAAGCAG
TGGTCCAGGGATGAATTGTAA
GenBank Gene IDM93008
GeneCard IDNot Available
GenAtlas IDPCMT1
HGNC IDHGNC:8728
Chromosome Location6
Locus6q24-q25
References
  1. 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. 2684970
  2. 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. 1339271
  3. 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. 7592526
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