Version 5.4
Mus musculus Protein: Trmt6
Summary
InnateDB Protein IDBP-207488.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Trmt6
Protein Name tRNA methyltransferase 6 homolog (S. cerevisiae)
Synonyms 3300001M20Rik; AU016412; AW492787; CGI-09; mKIAA1153;
Species Mus musculus
Ensembl Protein ENSMUSP00000044687
InnateDB Gene IDBG-207486 (Trmt6)
Protein Structure
UniProt Annotation
Function Substrate-binding subunit of tRNA (adenine-N(1)-)- methyltransferase, which catalyzes the formation of N(1)- methyladenine at position 58 (m1A58) in initiator methionyl-tRNA. {ECO:0000250}.
Subcellular Localization Nucleus {ECO:0000250}.
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 9 interaction(s) predicted by orthology.
Predicted by orthology
Total 9 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003743 translation initiation factor activity
GO:0044822 poly(A) RNA binding
Biological Process
GO:0006413 translational initiation
GO:0006446 regulation of translational initiation
GO:0008033 tRNA processing
Cellular Component
GO:0005575 cellular_component
GO:0005634 nucleus
Protein Structure and Domains
PDB ID MGI:1914176
InterPro IPR007316 Eukaryotic initiation factor 3, gamma subunit
IPR017423 tRNA (adenine-N(1)-)-methyltransferase, non-catalytic TRM6 subunit
PFAM PF04189
PRINTS
PIRSF PIRSF038170
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8CE96
PhosphoSite PhosphoSite-Q8CE96
TrEMBL
UniProt Splice Variant
Entrez Gene 66926
UniGene Mm.468313
RefSeq NP_780322
MGI ID
MGI Symbol Trmt6
OMIM
CCDS CCDS50728
HPRD
IMGT
EMBL AK014359 AK028755 AK129300 AK165976 AK167222 BC049083 BC052648
GenPept AAH49083 AAH52648 BAC25432 BAC26100 BAC98110 BAE38495 BAE39347

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