Version 5.4
Homo sapiens Protein: TRMT112
Summary
InnateDB Protein IDBP-598998.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol TRMT112
Protein Name tRNA methyltransferase 11-2 homolog (S. cerevisiae)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000438349
InnateDB Gene IDBG-53606 (TRMT112)
Protein Structure
UniProt Annotation
Function Participates both in methylation of protein and tRNA species. The heterodimer with HEMK2/N6AMT1 catalyzes N5- methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as methyl donor. The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species. {ECO:0000269PubMed:18539146}.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 30 experimentally validated interaction(s) in this database.
Experimentally validated
Total 30 [view]
Protein-Protein 29 [view]
Protein-DNA 1 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0008276 protein methyltransferase activity
Biological Process
GO:0018364 peptidyl-glutamine methylation
Cellular Component
GO:0043234 protein complex
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID
InterPro IPR005651 Uncharacterised protein family UPF0434/Trm112
PFAM PF03966
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9UI30
PhosphoSite PhosphoSite-Q9UI30
TrEMBL F5GYQ2
UniProt Splice Variant
Entrez Gene 51504
UniGene Hs.591577
RefSeq NP_057488
HUGO HGNC:26940
OMIM
CCDS CCDS8068
HPRD 13705
IMGT
EMBL AF110774 AF161501 AF229068 AK312050 AP001453 BC017172 BC029482 BC105294 CH471076
GenPept AAF14857 AAF29116 AAF82266 AAH17172 AAH29482 AAI05295 BAG34986 EAW74251 EAW74252

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