ASPA
entrez
443
canonical
uniprot
P45381
canonical
ensembl
ENSG00000108381
resolver
ensp
ENSP00000263080
resolver
ensp
ENSP00000409976
resolver
ensp
ENSP00000528495
resolver
enst
ENST00000263080
resolver
enst
ENST00000456349
resolver
enst
ENST00000858436
resolver
genesymbol
ASPA
resolver
genesymbol_syn
ACY2
resolver
genesymbol_syn
ASP
resolver
hgnc
HGNC:756
resolver
uniprot
Q6FH48
resolver
uniprot_entry
ACY2_HUMAN
resolver
uniprot_entry
Q6FH48_HUMAN
resolver
amino_acid_sequence
MTSCHIAEEHIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAVKKCTRYIDCDLNRIFDLENLGKKMSEDLPYEVRRAQEINHLFGPKDSEDSYDIIFDLHNTTSNMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIEHPSLKYATTRSIAKYPVGIEVGPQPQGVLRADILDQMRKMIKHALDFIHHFNEGKEFPPCAIEVYKIIEKVDYPRDENGEIAAIIHPNLQDQDWKPLHPGDPMFLTLDGKTIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTKLTLNAKSIRCCLH
uniprot
proteins
disease_involvement
DISEASE: Canavan disease (CAND) [MIM:271900]: A rare neurodegenerative condition of infancy or childhood characterized by white matter vacuolization and demyelination that gives rise to a spongy appearance. The clinical features are onset in early infancy, atonia of neck muscles, hypotonia, hyperextension of legs and flexion of arms, blindness, severe mental defect, megalocephaly, and death by 18 months on the average. {ECO:0000269|PubMed:10407784, ECO:0000269|PubMed:10564886, ECO:0000269|PubMed:10909858, ECO:0000269|PubMed:12205125, ECO:0000269|PubMed:12638939, ECO:0000269|PubMed:12706335, ECO:0000269|PubMed:24036223, ECO:0000269|PubMed:28101991, ECO:0000269|PubMed:7599639, ECO:0000269|PubMed:7668285, ECO:0000269|PubMed:8023850, ECO:0000269|PubMed:8252036, ECO:0000269|PubMed:8659549, ECO:0000269|PubMed:9452117}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.5.1.15
uniprot
proteins
function
FUNCTION: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it acts as a scavenger of NAA from body fluids. {ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:24036223, ECO:0000269|PubMed:8252036}.
uniprot
proteins
mass_dalton
35735
uniprot
proteins
mutagenesis
MUTAGEN 71; /note="R->K: Reduces activity by 99%."; /evidence="ECO:0000269|PubMed:18293939"; MUTAGEN 164; /note="Y->F: Reduces activity by 99%."; /evidence="ECO:0000269|PubMed:18293939"; MUTAGEN 168; /note="R->K: Reduces activity by 99%."; /evidence="ECO:0000269|PubMed:18293939"; MUTAGEN 178; /note="E->A: Reduces activity by 99%."; /evidence="ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:18293939"; MUTAGEN 178; /note="E->D: Abolishes enzymatic activity."; /evidence="ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:18293939"; MUTAGEN 178; /note="E->Q: Abolishes enzymatic activity."; /evidence="ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:18293939"; MUTAGEN 285; /note="E->D: 5-fold decrease in activity."; /evidence="ECO:0000269|PubMed:12706335"; MUTAGEN 288; /note="Y->F: Reduces activity by 99%."; /evidence="ECO:0000269|PubMed:18293939
uniprot
proteins
protein_family
AspA/AstE family
uniprot
proteins
protein_family
Aspartoacylase subfamily
uniprot
proteins
pubmed
10407784
uniprot
proteins
pubmed
10564886
uniprot
proteins
pubmed
10909858
uniprot
proteins
pubmed
12205125
uniprot
proteins
pubmed
12638939
uniprot
proteins
pubmed
12706335
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17027983
uniprot
proteins
pubmed
17194761
uniprot
proteins
pubmed
18293939
uniprot
proteins
pubmed
24036223
uniprot
proteins
pubmed
28101991
uniprot
proteins
pubmed
7599639
uniprot
proteins
pubmed
7668285
uniprot
proteins
pubmed
8023850
uniprot
proteins
pubmed
8252036
uniprot
proteins
pubmed
8659549
uniprot
proteins
pubmed
9452117
uniprot
proteins
sequence_length
313
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9R1T5}. Nucleus {ECO:0000250|UniProtKB:Q9R1T5}.
uniprot
proteins