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    PCMT1 protein-L-isoaspartate (D-aspartate) O-methyltransferase [ Bos taurus (domestic cattle) ]

    Gene ID: 613854, updated on 30-Jan-2025

    Summary

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    Official Symbol
    PCMT1provided by VGNC
    Official Full Name
    protein-L-isoaspartate (D-aspartate) O-methyltransferaseprovided by VGNC
    Primary source
    VGNC:VGNC:53799
    See related
    BGD:BT13797; EnsemblRapid:ENSBTAG00070012462
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Bos taurus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos
    Orthologs
    human mouse all
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    Genomic context

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    See PCMT1 in Genome Data Viewer
    Location:
    chromosome: 9
    Exon count:
    9
    Annotation release Status Assembly Chr Location
    RS_2024_12 current ARS-UCD2.0 (GCF_002263795.3) 9 NC_037336.1 (86919461..86962345)

    Chromosome 9 - NC_037336.1Genomic Context describing neighboring genes Neighboring gene large tumor suppressor kinase 1 Neighboring gene nucleolin-like Neighboring gene nucleoporin 43 Neighboring gene uncharacterized LOC104969619 Neighboring gene LDL receptor related protein 11 Neighboring gene nucleolar and spindle-associated protein 1 pseudogene Neighboring gene homeobox protein NANOG-like

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_037336.1 Chromosome 9 Reference ARS-UCD2.0 Primary Assembly

    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: Dominette sequence data
    • BioProject: PRJNA294306
    • Analysis date: Tue Dec 17 08:57:05 2024

    Bibliography

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    Related articles in PubMed

    1. The primary structure of a protein carboxyl methyltransferase from bovine brain that selectively methylates L-isoaspartyl sites. Henzel WJ, et al. J Biol Chem, 1989 Sep 25. PMID 2777770
    2. The type II isoform of bovine brain protein L-isoaspartyl methyltransferase has an endoplasmic reticulum retention signal (...RDEL) at its C-terminus. Potter SM, et al. Biochemistry, 1992 Jul 14. PMID 1627573
    3. Purification of homologous protein carboxyl methyltransferase isozymes from human and bovine erythrocytes. Gilbert JM, et al. Biochemistry, 1988 Jul 12. PMID 3167043
    4. A whole-genome assembly of the domestic cow, Bos taurus. Zimin AV, et al. Genome Biol, 2009. PMID 19393038, Free PMC Article
    5. Manual GO annotation of predictive protein signatures: the InterPro approach to GO curation. Burge S, et al. Database (Oxford), 2012. PMID 22301074, Free PMC Article

    See all (6) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Pathways from PubChem

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    General gene information

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    Markers

    Homology

    Gene Ontology Provided by RefSeq

    Function Evidence Code Pubs
    enables protein-L-isoaspartate (D-aspartate) O-methyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in protein modification process IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    protein-L-isoaspartate(D-aspartate) O-methyltransferase
    Names
    L-isoaspartyl protein carboxyl methyltransferase
    PIMT
    protein L-isoaspartyl/D-aspartyl methyltransferase
    protein-beta-aspartate methyltransferase
    NP_001073085.1
    XP_005211096.1
    XP_005211097.1
    XP_010806976.1

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001079617.2 → NP_001073085.1  protein-L-isoaspartate(D-aspartate) O-methyltransferase

      See identical proteins and their annotated locations for NP_001073085.1

      Status: PROVISIONAL

      Source sequence(s)
      BC109663
      UniProtKB/Swiss-Prot
      P15246
      Related
      ENSBTAP00070017339.1, ENSBTAT00070028393.1
      Conserved Domains (2) summary
      pfam01135
      Location:8 → 216
      PCMT; Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT)
      cl17173
      Location:13 → 220
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    RefSeqs of Annotated Genomes: GCF_002263795.3-RS_2024_12

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference ARS-UCD2.0 Primary Assembly

    Genomic

    1. NC_037336.1 Reference ARS-UCD2.0 Primary Assembly

      Range
      86919461..86962345
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_005211039.3 → XP_005211096.1  protein-L-isoaspartate(D-aspartate) O-methyltransferase isoform X1

      UniProtKB/TrEMBL
      A0AAA9T615, A0AAA9TDC9
      Related
      ENSBTAP00070017324.1, ENSBTAT00070028368.1
      Conserved Domains (2) summary
      pfam01135
      Location:66 → 274
      PCMT; Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT)
      cl17173
      Location:71 → 278
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    2. XM_005211040.3 → XP_005211097.1  protein-L-isoaspartate(D-aspartate) O-methyltransferase isoform X2

      UniProtKB/TrEMBL
      A0AAA9TMG5, G3MZZ6
      Related
      ENSBTAP00070017372.1, ENSBTAT00070028447.1
      Conserved Domains (2) summary
      pfam01135
      Location:66 → 274
      PCMT; Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT)
      cl17173
      Location:71 → 278
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...

    3. XM_010808674.3 → XP_010806976.1  protein-L-isoaspartate(D-aspartate) O-methyltransferase isoform X3

      See identical proteins and their annotated locations for XP_010806976.1

      UniProtKB/TrEMBL
      A0AAA9TMG5
      Related
      ENSBTAP00070017362.1, ENSBTAT00070028430.1
      Conserved Domains (2) summary
      pfam01135
      Location:66 → 274
      PCMT; Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT)
      cl17173
      Location:71 → 278
      AdoMet_MTases; S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). ...
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P15246.2 GenPept UniProtKB/Swiss-Prot:P15246

    Gene LinkOut

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