ASL
entrez
435
canonical
uniprot
P04424
canonical
ensembl
ENSG00000126522
resolver
ensp
ENSP00000307188
resolver
ensp
ENSP00000370219
resolver
ensp
ENSP00000378740
resolver
ensp
ENSP00000378741
resolver
genesymbol
ASL
resolver
hgnc
HGNC:746
resolver
uniprot
A0A024RDL8
resolver
uniprot
A0A0S2Z316
resolver
uniprot
E7EMI0
resolver
uniprot
E9PE48
resolver
uniprot
Q6LDS5
resolver
uniprot
Q96HS2
resolver
uniprot_entry
A0A024RDL8_HUMAN
resolver
uniprot_entry
A0A0S2Z316_HUMAN
resolver
uniprot_entry
ARLY_HUMAN
resolver
uniprot_sec
E7EMI0
resolver
uniprot_sec
E9PE48
resolver
uniprot_sec
Q6LDS5
resolver
uniprot_sec
Q96HS2
resolver
activity_regulation
ACTIVITY REGULATION: Enzyme activity is regulated by acetylation. {ECO:0000269|PubMed:20167786}.
uniprot
proteins
amino_acid_sequence
MASESGKLWGGRFVGAVDPIMEKFNASIAYDRHLWEVDVQGSKAYSRGLEKAGLLTKAEMDQILHGLDKVAEEWAQGTFKLNSNDEDIHTANERRLKELIGATAGKLHTGRSRNDQVVTDLRLWMRQTCSTLSGLLWELIRTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEVRKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYCTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMSAVLQVATGVISTLQIHQENMGQALSPDMLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVALNQLSLQELQTISPLFSGDVICVWDYGHSVEQYGALGGTARSSVDWQIRQVRALLQAQQA
uniprot
proteins
disease_involvement
DISEASE: Argininosuccinic aciduria (ARGINSA) [MIM:207900]: An autosomal recessive disorder of the urea cycle. The disease is characterized by mental and physical retardation, liver enlargement, skin lesions, dry and brittle hair showing trichorrhexis nodosa microscopically and fluorescing red, convulsions, and episodic unconsciousness. {ECO:0000269|PubMed:11747432, ECO:0000269|PubMed:11747433, ECO:0000269|PubMed:12408190, ECO:0000269|PubMed:1705937, ECO:0000269|PubMed:17326097, ECO:0000269|PubMed:19703900, ECO:0000269|PubMed:22081021, ECO:0000269|PubMed:2263616, ECO:0000269|PubMed:24166829, ECO:0000269|PubMed:9045711}. Note=The disease is caused by variants affecting the gene represented in this entry. The phenotype heterogeneity among patients is associated with interallelic complementation resulting in either complete loss of activity or partial regeneration of functional active sites in the heterotetrameric mutant protein. {ECO:0000269|PubMed:11747433}.
uniprot
proteins
ec_number
4.3.2.1
uniprot
proteins
function
FUNCTION: Catalyzes the reversible cleavage of L-argininosuccinate to fumarate and L-arginine, an intermediate step reaction in the urea cycle mostly providing for hepatic nitrogen detoxification into excretable urea as well as de novo L-arginine synthesis in nonhepatic tissues (PubMed:11747432, PubMed:11747433, PubMed:22081021, PubMed:2263616, PubMed:9045711). Essential regulator of intracellular and extracellular L-arginine pools. As part of citrulline-nitric oxide cycle, forms tissue-specific multiprotein complexes with argininosuccinate synthase ASS1, transport protein SLC7A1 and nitric oxide synthase NOS1, NOS2 or NOS3, allowing for cell-autonomous L-arginine synthesis while channeling extracellular L-arginine to nitric oxide synthesis pathway (PubMed:22081021). {ECO:0000269|PubMed:11747432, ECO:0000269|PubMed:11747433, ECO:0000269|PubMed:22081021, ECO:0000269|PubMed:9045711}.
uniprot
proteins
mass_dalton
51658
uniprot
proteins
mutagenesis
MUTAGEN 51; /note="K->N: 2-fold reduction in activity."; /evidence="ECO:0000269|PubMed:1705937"; MUTAGEN 89; /note="H->Q: 10-fold reduction in activity."; /evidence="ECO:0000269|PubMed:1705937"; MUTAGEN 288; /note="K->R: Refractory to inhibition by TSA and NAM and by addition of extra amino acids. No effect on protein structure."; /evidence="ECO:0000269|PubMed:20167786
uniprot
proteins
pathway_participation
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3. {ECO:0000305|PubMed:11747433}.; PATHWAY: Nitrogen metabolism; urea cycle; L-arginine and fumarate from (N(omega)-L-arginino)succinate: step 1/1. {ECO:0000305|PubMed:11747433}.
uniprot
proteins
post_translational_modification
PTM: Acetylation modifies enzyme activity in response to alterations of extracellular nutrient availability. Acetylation increased with trichostin A (TSA) or with nicotinamide (NAM). Glucose increases acetylation by about a factor of 3 with decreasing enzyme activity. Acetylation on Lys-288 is decreased on the addition of extra amino acids resulting in activation of enzyme activity. {ECO:0000269|PubMed:20167786}.
uniprot
proteins
protein_family
Argininosuccinate lyase subfamily
uniprot
proteins
protein_family
Lyase 1 family
uniprot
proteins
pubmed
11747432
uniprot
proteins
pubmed
11747433
uniprot
proteins
pubmed
12408190
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
1705937
uniprot
proteins
pubmed
17326097
uniprot
proteins
pubmed
19703900
uniprot
proteins
pubmed
20167786
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22081021
uniprot
proteins
pubmed
2263616
uniprot
proteins
pubmed
24166829
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2644168
uniprot
proteins
pubmed
3368457
uniprot
proteins
pubmed
3391281
uniprot
proteins
pubmed
3463959
uniprot
proteins
pubmed
9045711
uniprot
proteins
pubmed
9256435
uniprot
proteins
sequence_length
464
uniprot
proteins