Version 5.4
Homo sapiens Protein: PCMTD2
Summary
InnateDB Protein IDBP-809361.1
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 Homo sapiens
Ensembl Protein ENSP00000476878
InnateDB Gene IDBG-87942 (PCMTD2)
Protein Structure
UniProt Annotation
Function
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 7 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 7 [view]
Protein-Protein 7 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004719 protein-L-isoaspartate (D-aspartate) O-methyltransferase activity
Biological Process
GO:0006464 cellular protein modification process
GO:0006479 protein methylation
Cellular Component
Protein Structure and Domains
PDB ID
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
PhosphoSite PhosphoSite-
TrEMBL V9GYL1
UniProt Splice Variant
Entrez Gene 55251
UniGene
RefSeq
HUGO HGNC:15882
OMIM
CCDS
HPRD
IMGT
EMBL AL121581 AL137028
GenPept

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