Version 5.4
Mus musculus Protein: Trmt12
Summary
InnateDB Protein IDBP-143584.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Trmt12
Protein Name tRNA methyltranferase 12 homolog (S. cerevisiae)
Synonyms 4632406N01Rik; AI449275; Tyw2;
Species Mus musculus
Ensembl Protein ENSMUSP00000047831
InnateDB Gene IDBG-143582 (Trmt12)
Protein Structure
UniProt Annotation
Function S-adenosyl-L-methionine-dependent transferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the transfer of the alpha-amino-alpha- carboxypropyl (acp) group from S-adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14) to produce wybutosine-86 (By similarity). {ECO:0000250}.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 3 interaction(s) predicted by orthology.
Predicted by orthology
Total 3 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0008168 methyltransferase activity
GO:0016740 transferase activity
Biological Process
GO:0008033 tRNA processing
GO:0008150 biological_process
GO:0032259 methylation
Cellular Component
GO:0005575 cellular_component
Protein Structure and Domains
PDB ID MGI:1915510
InterPro IPR003402 tRNA transferase Trm5/Tyw2
IPR029063 S-adenosyl-L-methionine-dependent methyltransferase-like
PFAM PF02475
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8BG71
PhosphoSite PhosphoSite-Q8BG71
TrEMBL
UniProt Splice Variant
Entrez Gene 68260
UniGene Mm.278805
RefSeq NP_080918
MGI ID
MGI Symbol Trmt12
OMIM
CCDS CCDS37081
HPRD
IMGT
EMBL AK019481 AK031429 AK076857 AK079291 BC052533 BC055850
GenPept AAH52533 AAH55850 BAB31750 BAC27399 BAC36508 BAC37597

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