Version 5.4
Mus musculus Protein: Dph3
Summary
InnateDB Protein IDBP-147260.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Dph3
Protein Name DPH3 homolog (KTI11, S. cerevisiae)
Synonyms DELGIP1; DelgipP1; Desr1; KTI11; Zcsl2;
Species Mus musculus
Ensembl Protein ENSMUSP00000068491
InnateDB Gene IDBG-147256 (Dph3)
Protein Structure
UniProt Annotation
Function Essential for the first step in the synthesis of diphthamide, a post-translational modification of histidine which occurs in elongation factor 2.Down-regulation increases extracellular release of proteoglycans, indicating a possible role in the secretion process. Stimulates binding of GNEFR to SEC5 (By similarity). {ECO:0000250}.
Subcellular Localization Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Disease Associations
Tissue Specificity Widely expressed with highest levels in heart, liver, kidney and testis. {ECO:0000269PubMed:14527407}.
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:0005515 protein binding
GO:0046872 metal ion binding
Biological Process
GO:0017183 peptidyl-diphthamide biosynthetic process from peptidyl-histidine
GO:0050709 negative regulation of protein secretion
GO:0051099 positive regulation of binding
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID MGI:1922658
InterPro IPR007872 Zinc finger, DPH-type
PFAM PF05207
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8K0W9
PhosphoSite PhosphoSite-Q8K0W9
TrEMBL
UniProt Splice Variant
Entrez Gene 105638
UniGene Mm.2519
RefSeq NP_758458
MGI ID 1WGE
MGI Symbol Dph3
OMIM
CCDS CCDS36861
HPRD
IMGT
EMBL AK011448 AK048097 BC029910 BC039954
GenPept AAH29910 AAH39954 BAC25335 BAC33240

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