ABHD11
entrez
83451
canonical
uniprot
Q8NFV4
canonical
ensembl
ENSG00000106077
resolver
ensp
ENSP00000222800
resolver
ensp
ENSP00000378579
resolver
ensp
ENSP00000397666
resolver
ensp
ENSP00000416970
resolver
ensp
ENSP00000671183
resolver
enst
ENST00000458339
resolver
genesymbol
ABHD11
resolver
genesymbol_syn
WBSCR21
resolver
hgnc
HGNC:16407
resolver
uniprot
C9J7Q4
resolver
uniprot
H7BYM8
resolver
uniprot
Q6PJU0
resolver
uniprot
Q8N722
resolver
uniprot
Q8N723
resolver
uniprot
Q8NFV2
resolver
uniprot
Q8NFV3
resolver
uniprot
Q9HBS8
resolver
uniprot_entry
ABHDB_HUMAN
resolver
uniprot_entry
C9J7Q4_HUMAN
resolver
uniprot_sec
H7BYM8
resolver
uniprot_sec
Q6PJU0
resolver
uniprot_sec
Q8N722
resolver
uniprot_sec
Q8N723
resolver
uniprot_sec
Q8NFV2
resolver
uniprot_sec
Q8NFV3
resolver
uniprot_sec
Q9HBS8
resolver
amino_acid_sequence
MLRWTRAWRLPREGLGPHGPSFARVPVAPSSSSGGRGGAEPRPLPLSYRLLDGEAALPAVVFLHGLFGSKTNFNSIAKILAQQTGRRVLTVDARNHGDSPHSPDMSYEIMSQDLQDLLPQLGLVPCVVVGHSMGGKTAMLLALQRPELVERLIAVDISPVESTGVSHFATYVAAMRAINIADELPRSRARKLADEQLSSVIQDMAVRQHLLTNLVEVDGRFVWRVNLDALTQHLDKILAFPQRQESYLGPTLFLLGGNSQFVHPSHHPEIMRLFPRAQMQTVPNAGHWIHADRPQDFIAAIRGFLV
uniprot
proteins
disease_involvement
DISEASE: Note=ABHD11 is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region.
uniprot
proteins
ec_number
3.1.1.116
uniprot
proteins
function
FUNCTION: Catalyzes the hydrolysis of diacylglycerol in vitro and may function as a key regulator in lipid metabolism, namely by regulating the intracellular levels of diacylglycerol (PubMed:32579589). 1,2-diacyl-sn-glycerols are the preferred substrate over 1,3-diacyl-sn-glycerols (By similarity). The enzyme hydrolyzes stearate in preference to palmitate from the sn-1 position of 1,2-diacyl-sn-glycerols (By similarity). Maintains the functional lipoylation of the 2-oxoglutarate dehydrogenase complex (OGDHc) through its interaction with the OGDHc by preventing the formation of lipoyl adducts (PubMed:32792488). In addition, is also required for the expansion and differentiation of embryonic stem cells (ESCs) (By similarity). {ECO:0000250|UniProtKB:Q3SZ73, ECO:0000250|UniProtKB:Q8K4F5, ECO:0000269|PubMed:32579589, ECO:0000269|PubMed:32792488}.
uniprot
proteins
mass_dalton
33747
uniprot
proteins
mutagenesis
MUTAGEN 132; /note="S->A: Loss of p-nitrophenyl ester hydrolysis. Does not affect mitochondrion location. Loss of DLST lipoylation."; /evidence="ECO:0000269|PubMed:32792488"; MUTAGEN 287; /note="H->A: Loss of DLST lipoylation."; /evidence="ECO:0000269|PubMed:32792488
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q3SZ73}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
pubmed
12073013
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15498874
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
32579589
uniprot
proteins
pubmed
32792488
uniprot
proteins
sequence_length
306
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:32579589}. Mitochondrion matrix {ECO:0000269|PubMed:32792488}.
uniprot
proteins