Ntan1
entrez
18203
canonical
uniprot
Q64311
canonical
ensembl
ENSMUSG00000022681
resolver
ensp
ENSMUSP00000023362
resolver
ensp
ENSMUSP00000111472
resolver
ensp
ENSMUSP00000173844
resolver
ensp
ENSMUSP00000173846
resolver
enst
ENSMUST00000023362
resolver
enst
ENSMUST00000115805
resolver
genesymbol
Ntan1
resolver
uniprot
D3YZ99
resolver
uniprot
Q8BRX4
resolver
uniprot_entry
D3YZ99_MOUSE
resolver
uniprot_entry
NTAN1_MOUSE
resolver
uniprot_entry
Q8BRX4_MOUSE
resolver
amino_acid_sequence
MPLLVDGQRVRLPRSAVELVRAHPPLEERARLLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGSDTKAEVPLIMSSIKSFSEHAECGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDKQDDDIHLVTLCVTELNDREENENHFPIIYGIAVNIKTAEIYRASFQDRGPEEQLRAARALAGGPMISIYDAKTEQLRIGPCSWTPFPQVDFWLQQDDKQILESLSTSPLAEPPHFVEHIRSTLMFLKKFPSPENILFPGNKALLYKKNKDGLWEKISSPGS
uniprot
proteins
ec_number
3.5.1.121
uniprot
proteins
function
FUNCTION: N-terminal asparagine deamidase that mediates 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 NTAN1/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. {ECO:0000269|PubMed:8910481}.
uniprot
proteins
mass_dalton
34595
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8910481
uniprot
proteins
sequence_length
310
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q28955}.
uniprot
proteins