Version 5.4
Mus musculus Protein: Dph5
Summary
InnateDB Protein IDBP-189758.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Dph5
Protein Name DPH5 homolog (S. cerevisiae)
Synonyms 2410012M04Rik; AU045680; C80186;
Species Mus musculus
Ensembl Protein ENSMUSP00000043730
InnateDB Gene IDBG-189756 (Dph5)
Protein Structure
UniProt Annotation
Function S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EFE2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. {ECO:0000269PubMed:15485916}.
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 2 interaction(s) predicted by orthology.
Predicted by orthology
Total 2 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0004164 diphthine synthase activity
GO:0008168 methyltransferase activity
Biological Process
GO:0008150 biological_process
GO:0008152 metabolic process
GO:0017183 peptidyl-diphthamide biosynthetic process from peptidyl-histidine
GO:0032259 methylation
Cellular Component
GO:0005575 cellular_component
Protein Structure and Domains
PDB ID MGI:1916990
InterPro IPR000878 Tetrapyrrole methylase
IPR004551 Diphthine synthase
PFAM PF00590
PRINTS
PIRSF PIRSF036432
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9CWQ0
PhosphoSite PhosphoSite-
TrEMBL V9GXP1
UniProt Splice Variant
Entrez Gene 69740
UniGene Mm.5915
RefSeq NP_081469
MGI ID
MGI Symbol Dph5
OMIM
CCDS CCDS17782
HPRD
IMGT
EMBL AC131113 AK010475 BC060372 CH466532
GenPept AAH60372 BAB26968 EDL12394 EDL12395

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