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Reviewed, UniProtKB/Swiss-Prot P23506 (PIMT_MOUSE)

Last modified June 16, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Protein-L-isoaspartate(D-aspartate) O-methyltransferase
      Short name=PIMT
    EC=2.1.1.77
Alternative name(s):
    Protein-beta-aspartate methyltransferase
    Protein L-isoaspartyl/D-aspartyl methyltransferase
    L-isoaspartyl protein carboxyl methyltransferase
Gene names
Name: Pcmt1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

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.

Catalytic activity

S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the L-isoaspartyl/D-aspartyl protein methyltransferase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processprotein amino acid methylation

Inferred from direct assay. Source: MGI

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein-L-isoaspartate (D-aspartate) O-methyltransferase activity

Inferred from direct assay. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P23506-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P23506-2)

The sequence of this isoform differs from the canonical sequence as follows:
     226-227: WK → DEL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 227226Protein-L-isoaspartate(D-aspartate) O-methyltransferase
PRO_0000111876

Sites

Active site601 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Natural variations

Alternative sequence226 – 2272WK → DEL in isoform 2.
VSP_004717

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 954E2491A9DA9249

FASTA22724,634
        10         20         30         40         50         60 
MAWKSGGASH SELIHNLRKN GIIKTDKVFE VMLATDRSHY AKSNPYMDSP QSIGFQATIS 

        70         80         90        100        110        120 
APHMHAYALE LLFDQLHEGA KALDVGSGSG ILTACFARMV GNSGKVIGID HIKELVDDSI 

       130        140        150        160        170        180 
TNVKKDDPML LSSGRVRLVV GDGRMGYAEE APYDAIHVGA AAPVVPQALI DQLKPGGRLI 

       190        200        210        220 
LPVGPAGGNQ MLEQYDKLQD GSVKMKPLMG VIYVPLTDKE KQWSRWK 

« Hide

Isoform 2.

Checksum: 07ED77F491A9DA92
Show »

FASTA22824,677

References

« Hide 'large scale' references
[1]"Genomic organization and tissue expression of the murine gene encoding the protein beta-aspartate methyltransferase."
Romanik E.A., Ladino C.A., Killoy L.C., D'Ardenne S.C., O'Connor C.M.
Gene 118:217-222(1992) [PubMed: 1511895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6.
Tissue: Brain and Testis.
[3]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 82-98, MASS SPECTROMETRY.
Tissue: Hippocampus.
[4]"Structural analysis of transcripts for the protein L-isoaspartyl methyltransferase reveals multiple transcription initiation sites and a distinct pattern of expression in mouse testis: identification of a 5'-flanking sequence with promoter activity."
Galus A., Lagos A., Romanik E.A., O'Connor C.M.
Arch. Biochem. Biophys. 312:524-533(1994) [PubMed: 8037467] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 186-227 (ISOFORM 2).
[5]"Proteomic identification of novel substrates of a protein isoaspartyl methyltransferase repair enzyme."
Vigneswara V., Lowenson J.D., Powell C.D., Thakur M., Bailey K., Clarke S., Ray D.E., Carter W.G.
J. Biol. Chem. 281:32619-32629(2006) [PubMed: 16923807] [Abstract]
Cited for: SUBSTRATES.
+Additional computationally mapped references.

Cross-references

Sequence databases

M60320 mRNA. Translation: AAA92742.1. Sequence problems.
M84684 Genomic DNA. Translation: AAA74565.1.
BC049613 mRNA. Translation: AAH49613.1. Different initiation.
BC058966 mRNA. Translation: AAH58966.1.
S72473 mRNA. Translation: AAB31369.1.
IPIIPI00329913.
IPI00757109.
PIRJC1248.
UniGeneMm.258431

3D structure databases

HSSPHSSP built from PDB template 1I1N based on UniProtKB P22061.
SMRP23506. Positions 3-226.
ModBaseSearch...

2-D gel databases

REPRODUCTION-2DPAGEP23506.

Proteomic databases

PRIDEP23506.

Genome annotation databases

EnsemblENSMUSG00000019795. Mus musculus. [Contig view]
KEGGmmu:18537.

Organism-specific databases

MGIMGI:97502. Pcmt1.

Phylogenomic databases

HOGENOMP23506.
HOVERGENP23506.
OMAP23506. EKQWSRW.

Enzyme and pathway databases

BRENDA2.1.1.77. 244.

Gene expression databases

ArrayExpressP23506.
BgeeP23506.
GermOnlineENSMUSG00000019795. Mus musculus.

Family and domain databases

InterProIPR000682. PCMT.
[Graphical view]
PANTHERPTHR11579. PCMT. 1 hit.
PfamPF01135. PCMT. 1 hit.
[Graphical view]
TIGRFAMsTIGR00080. pimt. 1 hit.
PROSITEPS01279. PCMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio294308.
SOURCESearch...

Entry information

Entry namePIMT_MOUSE
AccessionPrimary (citable) accession number: P23506
Secondary accession number(s): Q810R4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents