Version 5.4
Mus musculus Protein: Asphd2
Summary
InnateDB Protein IDBP-191282.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Asphd2
Protein Name aspartate beta-hydroxylase domain containing 2
Synonyms 2900006N09Rik; 9230106G13Rik;
Species Mus musculus
Ensembl Protein ENSMUSP00000031291
InnateDB Gene IDBG-191280 (Asphd2)
Protein Structure
UniProt Annotation
Function May function as 2-oxoglutarate-dependent dioxygenase. {ECO:0000250}.
Subcellular Localization Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
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.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0008150 biological_process
GO:0018193 peptidyl-amino acid modification
GO:0055114 oxidation-reduction process
Cellular Component
GO:0005575 cellular_component
GO:0016020 membrane
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1920148
InterPro IPR007803 Arginine/Asparagine/Proline hydroxylase
PFAM PF05118
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q80VP9
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 72898
UniGene Mm.151745
RefSeq NP_082662
MGI ID
MGI Symbol Asphd2
OMIM
CCDS CCDS19542
HPRD
IMGT
EMBL AK013495 BC046606
GenPept AAH46606 BAB28881

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