Version 5.4
Mus musculus Protein: Hddc3
Summary
InnateDB Protein IDBP-195105.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Hddc3
Protein Name HD domain containing 3
Synonyms 1110033O09Rik; C86475; MESH1;
Species Mus musculus
Ensembl Protein ENSMUSP00000032747
InnateDB Gene IDBG-195103 (Hddc3)
Protein Structure
UniProt Annotation
Function ppGpp hydrolyzing enzyme involved in starvation response. {ECO:0000250}.
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 3 interaction(s) predicted by orthology.
Predicted by orthology
Total 3 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0003824 catalytic activity
GO:0008081 phosphoric diester hydrolase activity
GO:0008893 guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity
GO:0046872 metal ion binding
Biological Process
GO:0008150 biological_process
GO:0008152 metabolic process
Cellular Component
GO:0005575 cellular_component
Protein Structure and Domains
PDB ID MGI:1915945
InterPro IPR003607 HD/PDEase domain
IPR006674 HD domain
PFAM PF01966
PF13023
PRINTS
PIRSF
SMART SM00471
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q9D114
PhosphoSite PhosphoSite-Q9D114
TrEMBL
UniProt Splice Variant
Entrez Gene 68695
UniGene
RefSeq NP_081088
MGI ID
MGI Symbol Hddc3
OMIM
CCDS CCDS21396
HPRD
IMGT
EMBL AK004078 BC038310
GenPept AAH38310 BAB23158

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