Version 5.4
Homo sapiens Protein: PET112
Summary
InnateDB Protein IDBP-41196.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol PET112
Protein Name PET112 homolog (yeast)
Synonyms PET112; PET112L;
Species Homo sapiens
Ensembl Protein ENSP00000263985
InnateDB Gene IDBG-41194 (PET112)
Protein Structure
UniProt Annotation
Function Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). {ECO:0000255HAMAP-Rule:MF_03147, ECO:0000269PubMed:19805282}.
Subcellular Localization Mitochondrion {ECO:0000255HAMAP- Rule:MF_03147, ECO:0000269PubMed:9878253}.
Disease Associations
Tissue Specificity Predominantly expressed in tissues characterized by high rates of oxidative phosphorylation (OxPhos), including muscle and heart. {ECO:0000269PubMed:9878253}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 5 experimentally validated interaction(s) in this database.
Experimentally validated
Total 5 [view]
Protein-Protein 2 [view]
Protein-DNA 3 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0005524 ATP binding
GO:0008135 translation factor activity, nucleic acid binding
GO:0016874 ligase activity
GO:0016884 carbon-nitrogen ligase activity, with glutamine as amido-N-donor
GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Biological Process
GO:0006412 translation
GO:0032543 mitochondrial translation
GO:0070681 glutaminyl-tRNAGln biosynthesis via transamidation
Cellular Component
GO:0005739 mitochondrion
GO:0030956 glutamyl-tRNA(Gln) amidotransferase complex
Protein Structure and Domains
PDB ID
InterPro IPR003789 Aspartyl/glutamyl-tRNA amidotransferase subunit B-related
IPR004413 Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase, B subunit
IPR006075 Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic
IPR018027 Asn/Gln amidotransferase
PFAM PF02934
PF02637
PRINTS
PIRSF
SMART SM00845
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt O75879
PhosphoSite PhosphoSite-O75879
TrEMBL
UniProt Splice Variant
Entrez Gene 5188
UniGene Hs.636045
RefSeq NP_004555
HUGO HGNC:8849
OMIM 603645
CCDS CCDS3776
HPRD 04706
IMGT
EMBL AB019410 AC092611 AF026851 AF151033 AK222887 AK312957 BC130348 BC136547 CH471056
GenPept AAD08640 AAF36119 AAI30349 AAI36548 AAY40897 BAD96607 BAG35796 EAX04981

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