Version 5.4
Mus musculus Protein: Pcmtd2
Summary
InnateDB Protein IDBP-214248.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Pcmtd2
Protein Name protein-L-isoaspartate (D-aspartate) O-methyltransferase domain containing 2
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000029116
InnateDB Gene IDBG-214246 (Pcmtd2)
Protein Structure
UniProt Annotation
Function
Subcellular Localization Cytoplasm {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
They are also associated with 6 interaction(s) predicted by orthology.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 6 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0004719 protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
Biological Process
GO:0006464 cellular protein modification process
GO:0006479 protein methylation
GO:0008150 biological_process
Cellular Component
GO:0005575 cellular_component
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID MGI:1923927
InterPro IPR000682 Protein-L-isoaspartate(D-aspartate) O-methyltransferase
IPR029063 S-adenosyl-L-methionine-dependent methyltransferase-like
PFAM PF01135
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8BHD8
PhosphoSite PhosphoSite-Q8BHD8
TrEMBL B0R0D0
UniProt Splice Variant
Entrez Gene 245867
UniGene Mm.404123
RefSeq NP_705822
MGI ID
MGI Symbol Pcmtd2
OMIM
CCDS CCDS17224
HPRD
IMGT
EMBL AK031335 AK077319 AK079927 AK088800 AK146080 AL845173 BC024791 BC031360 BC040385
GenPept AAH24791 AAH31360 AAH40385 BAC27352 BAC36747 BAC37785 BAC40579 BAE26884

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca