ASRGL1
entrez
80150
canonical
uniprot
Q7L266
canonical
ensembl
ENSG00000162174
resolver
ensp
ENSP00000301776
resolver
ensp
ENSP00000400057
resolver
ensp
ENSP00000478649
resolver
ensp
ENSP00000675811
resolver
ensp
ENSP00000797480
resolver
genesymbol
ASRGL1
resolver
genesymbol_syn
ALP
resolver
genesymbol_syn
CRASH
resolver
hgnc
HGNC:16448
resolver
uniprot
A0A024R573
resolver
uniprot
B2R7Q0
resolver
uniprot
Q567Q4
resolver
uniprot
Q6P1P0
resolver
uniprot
Q8NI34
resolver
uniprot
Q9H6F7
resolver
uniprot_entry
A0A024R573_HUMAN
resolver
uniprot_entry
ASGL1_HUMAN
resolver
uniprot_sec
B2R7Q0
resolver
uniprot_sec
Q567Q4
resolver
uniprot_sec
Q6P1P0
resolver
uniprot_sec
Q8NI34
resolver
uniprot_sec
Q9H6F7
resolver
activity_regulation
ACTIVITY REGULATION: Glycine accelerates autocleavage into an alpha and beta chain. {ECO:0000269|PubMed:22861376}.
uniprot
proteins
amino_acid_sequence
MNPIVVVHGGGAGPISKDRKERVHQGMVRAATVGYGILREGGSAVDAVEGAVVALEDDPEFNAGCGSVLNTNGEVEMDASIMDGKDLSAGAVSAVQCIANPIKLARLVMEKTPHCFLTDQGAAQFAAAMGVPEIPGEKLVTERNKKRLEKEKHEKGAQKTDCQKNLGTVGAVALDCKGNVAYATSTGGIVNKMVGRVGDSPCLGAGGYADNDIGAVSTTGHGESILKVNLARLTLFHIEQGKTVEEAADLSLGYMKSRVKGLGGLIVVSKTGDWVAKWTSTSMPWAAAKDGKLHFGIDPDDTTITDLP
uniprot
proteins
ec_number
3.4.19.5
uniprot
proteins
ec_number
3.5.1.1
uniprot
proteins
function
FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity. May be involved in the production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions. Is highly active with L-Asp beta-methyl ester. Besides, has catalytic activity toward beta-aspartyl dipeptides and their methyl esters, including beta-L-Asp-L-Phe, beta-L-Asp-L-Phe methyl ester (aspartame), beta-L-Asp-L-Ala, beta-L-Asp-L-Leu and beta-L-Asp-L-Lys. Does not have aspartylglucosaminidase activity and is inactive toward GlcNAc-L-Asn. Likewise, has no activity toward glutamine. {ECO:0000269|PubMed:19839645, ECO:0000269|PubMed:27106100}.
uniprot
proteins
mass_dalton
32055
uniprot
proteins
mutagenesis
MUTAGEN 168; /note="T->A,C: Abolishes activation by autocleavage. Abolishes enzyme activity."; /evidence="ECO:0000269|PubMed:19839645, ECO:0000269|PubMed:22891768"; MUTAGEN 168; /note="T->S: Strongly reduced enzyme activity."; /evidence="ECO:0000269|PubMed:19839645, ECO:0000269|PubMed:22891768
uniprot
proteins
post_translational_modification
PTM: Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity. {ECO:0000269|PubMed:19839645, ECO:0000269|PubMed:22861376}.
uniprot
proteins
protein_family
Ntn-hydrolase family
uniprot
proteins
pubmed
11984834
uniprot
proteins
pubmed
14654938
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19839645
uniprot
proteins
pubmed
22861376
uniprot
proteins
pubmed
22891768
uniprot
proteins
pubmed
27106100
uniprot
proteins
sequence_length
308
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11984834, ECO:0000269|PubMed:27106100}. Note=Midpiece of sperm tail.
uniprot
proteins