Version 5.4
Homo sapiens Protein: NTAN1
Summary
InnateDB Protein IDBP-15844.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol NTAN1
Protein Name N-terminal asparagine amidase
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000287706
InnateDB Gene IDBG-15842 (NTAN1)
Protein Structure
UniProt Annotation
Function Side-chain deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N- terminal asparagine to aspartate by PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N- terminal peptidyl Asn. {ECO:0000269PubMed:21375249}.
Subcellular Localization Cytoplasm {ECO:0000250}.
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:0008418 protein-N-terminal asparagine amidohydrolase activity
Biological Process
GO:0007613 memory
GO:0008152 metabolic process
GO:0008344 adult locomotory behavior
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID
InterPro
PFAM
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q96AB6
PhosphoSite PhosphoSite-Q96AB6
TrEMBL Q658S0
UniProt Splice Variant
Entrez Gene 123803
UniGene Hs.592045
RefSeq NP_775745
HUGO HGNC:29909
OMIM 615367
CCDS CCDS10558
HPRD 17649
IMGT
EMBL AC138932 AC139256 AF092440 AL833023 BC017336
GenPept AAH17336 AAP97215 CAH56267

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