ASNS
entrez
440
canonical
uniprot
P08243
canonical
ensembl
ENSG00000070669
resolver
ensp
ENSP00000175506
resolver
ensp
ENSP00000377845
resolver
ensp
ENSP00000377846
resolver
ensp
ENSP00000406994
resolver
ensp
ENSP00000408472
resolver
ensp
ENSP00000414379
resolver
genesymbol
ASNS
resolver
genesymbol_syn
TS11
resolver
hgnc
HGNC:753
resolver
uniprot
A4D1I8
resolver
uniprot
B4DXZ1
resolver
uniprot
B7ZAA9
resolver
uniprot
D6W5R3
resolver
uniprot
E9PCI3
resolver
uniprot
E9PCX6
resolver
uniprot
P08184
resolver
uniprot
Q15666
resolver
uniprot
Q549T9
resolver
uniprot
Q96HD0
resolver
uniprot_entry
ASNS_HUMAN
resolver
uniprot_sec
A4D1I8
resolver
uniprot_sec
B4DXZ1
resolver
uniprot_sec
B7ZAA9
resolver
uniprot_sec
D6W5R3
resolver
uniprot_sec
E9PCI3
resolver
uniprot_sec
E9PCX6
resolver
uniprot_sec
P08184
resolver
uniprot_sec
Q15666
resolver
uniprot_sec
Q549T9
resolver
uniprot_sec
Q96HD0
resolver
amino_acid_sequence
MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPFLPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPKWINATDPSARTLTHYKSAVKA
uniprot
proteins
disease_involvement
DISEASE: Asparagine synthetase deficiency (ASNSD) [MIM:615574]: An inborn error of asparagine biosynthesis that results in a severe neurologic disorder characterized by microcephaly, severely delayed psychomotor development, progressive encephalopathy, cortical atrophy, and seizure or hyperekplexic activity. {ECO:0000269|PubMed:24139043, ECO:0000269|PubMed:26318253, ECO:0000269|PubMed:27469131, ECO:0000269|PubMed:27522229, ECO:0000269|PubMed:27743885, ECO:0000269|PubMed:28776279, ECO:0000269|PubMed:29279279, ECO:0000269|PubMed:29375865, ECO:0000269|PubMed:29405484, ECO:0000269|PubMed:30057589, ECO:0000269|PubMed:31123592, ECO:0000269|PubMed:32255274, ECO:0000269|PubMed:32741967, ECO:0000269|PubMed:34080208, ECO:0000269|PubMed:35985424, ECO:0000269|PubMed:36613999, ECO:0000269|PubMed:37167844, ECO:0000269|PubMed:37900678, ECO:0000269|PubMed:38043418, ECO:0000269|PubMed:40421135}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.5.1.2
uniprot
proteins
ec_number
6.3.5.4
uniprot
proteins
function
FUNCTION: Catalyzes the ATP-dependent synthesis of L-asparagine from L-aspartate, using L-glutamine as a source of nitrogen (PubMed:2564390, PubMed:2573597). Can also use ammonia as the nitrogen source in vitro (PubMed:2564390, PubMed:2573597). {ECO:0000269|PubMed:2564390, ECO:0000269|PubMed:2573597}.
uniprot
proteins
mass_dalton
64370
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="C->A: Loss of the glutamine-dependent asparagine synthetase activity. No effect on ammonia-dependent activity."; /evidence="ECO:0000269|PubMed:2573597"; MUTAGEN 143; /note="R->A: Decreased glutamine-dependent asparagine synthetase activity. No effect on ammonia-dependent asparagine synthetase activity. Does not affect the affinity for aspartate. 45-fold increased affinity for glutamine. 2-fold decreased affinity for ammonia."; /evidence="ECO:0000269|PubMed:39627226"; MUTAGEN 143; /note="R->I: Decreased glutamine-dependent asparagine synthetase activity. No effect on ammonia-dependent activity. 3-fold increased affinity for aspartate. 90-fold increased affinity for glutamine. 2-fold increased affinity for ammonia."; /evidence="ECO:0000269|PubMed:39627226"; MUTAGEN 365; /note="E->A: Loss of ammonia-dependent asparagine synthetase activity in vitro."; /evidence="ECO:0000269|PubMed:31552298"; MUTAGEN 365; /note="E->Q: Loss of ammonia-dependent asparagine synthetase activity in vitro."; /evidence="ECO:0000269|PubMed:31552298"; MUTAGEN 368; /note="D->A: Loss of ammonia-dependent asparagine synthetase activity in vitro."; /evidence="ECO:0000269|PubMed:31552298"; MUTAGEN 368; /note="D->N: Decreased ammonia-dependent asparagine synthetase activity in vitro."; /evidence="ECO:0000269|PubMed:31552298
uniprot
proteins
pathway_participation
PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (L-Gln route): step 1/1.
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24139043
uniprot
proteins
pubmed
2564390
uniprot
proteins
pubmed
2565875
uniprot
proteins
pubmed
2569668
uniprot
proteins
pubmed
2573597
uniprot
proteins
pubmed
26318253
uniprot
proteins
pubmed
27469131
uniprot
proteins
pubmed
27522229
uniprot
proteins
pubmed
27743885
uniprot
proteins
pubmed
28776279
uniprot
proteins
pubmed
2886907
uniprot
proteins
pubmed
28875262
uniprot
proteins
pubmed
29279279
uniprot
proteins
pubmed
29375865
uniprot
proteins
pubmed
29405484
uniprot
proteins
pubmed
30057589
uniprot
proteins
pubmed
31123592
uniprot
proteins
pubmed
31552298
uniprot
proteins
pubmed
32255274
uniprot
proteins
pubmed
32741967
uniprot
proteins
pubmed
34080208
uniprot
proteins
pubmed
3470743
uniprot
proteins
pubmed
35985424
uniprot
proteins
pubmed
36613999
uniprot
proteins
pubmed
37167844
uniprot
proteins
pubmed
37900678
uniprot
proteins
pubmed
37965492
uniprot
proteins
pubmed
38043418
uniprot
proteins
pubmed
39627226
uniprot
proteins
pubmed
40421135
uniprot
proteins
sequence_length
561
uniprot
proteins