BCHE
entrez
590
canonical
uniprot
P06276
canonical
ensembl
ENSG00000114200
resolver
ensp
ENSP00000264381
resolver
ensp
ENSP00000525395
resolver
ensp
ENSP00000525398
resolver
enst
ENST00000264381
resolver
enst
ENST00000855336
resolver
enst
ENST00000855339
resolver
genesymbol
BCHE
resolver
genesymbol_syn
CHE1
resolver
hgnc
HGNC:983
resolver
uniprot
A8K7P8
resolver
uniprot_entry
CHLE_HUMAN
resolver
uniprot_sec
A8K7P8
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by mercury. Inhibited by Tabun. Tabun forms a covalent adduct with Ser-226 that becomes irreversible upon aging. {ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19368529}.
uniprot
proteins
amino_acid_sequence
MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCVGL
uniprot
proteins
disease_involvement
DISEASE: Butyrylcholinesterase deficiency (BCHED) [MIM:617936]: An autosomal recessive metabolic condition characterized by increased sensitivity to certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium. BCHED results in slower hydrolysis of these drugs and, consequently, a prolonged neuromuscular block, leading to apnea. The duration of the prolonged apnea varies significantly depending on the extent of the enzyme deficiency. {ECO:0000269|PubMed:10404729, ECO:0000269|PubMed:11928765, ECO:0000269|PubMed:12881446, ECO:0000269|PubMed:1306123, ECO:0000269|PubMed:1349196, ECO:0000269|PubMed:1415224, ECO:0000269|PubMed:15563885, ECO:0000269|PubMed:15781196, ECO:0000269|PubMed:1611188, ECO:0000269|PubMed:16788378, ECO:0000269|PubMed:17700357, ECO:0000269|PubMed:18075469, ECO:0000269|PubMed:18300943, ECO:0000269|PubMed:25054547, ECO:0000269|PubMed:25264279, ECO:0000269|PubMed:2915989, ECO:0000269|PubMed:7634491, ECO:0000269|PubMed:8554068, ECO:0000269|PubMed:8680411, ECO:0000269|PubMed:9110359, ECO:0000269|PubMed:9191541, ECO:0000269|PubMed:9388484, ECO:0000269|PubMed:9543549, ECO:0000269|PubMed:9694584}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.1.8
uniprot
proteins
function
FUNCTION: Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. {ECO:0000269|PubMed:19452557, ECO:0000269|PubMed:19542320}.
uniprot
proteins
mass_dalton
68418
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. No other PTM detected (PubMed:20946535). The major N-glycan structures are of the complex diantennary type with 1 and 2 N-acetylneuraminic acid molecules (Neu5Ac) making up approximately 33% and 47% of the total N-glycans, respectively. Only low amounts of fucosylated diantennary N-glycans are detected (approximately 2%). Triantennary N-glycans with or without fucose amount to approximately 13%, whereas 5% of the total N-glycans are of the oligomannosidic or hybrid type. {ECO:0000269|PubMed:12869558, ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15667209, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17355286, ECO:0000269|PubMed:17768338, ECO:0000269|PubMed:18203274, ECO:0000269|PubMed:18975951, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:20946535}.
uniprot
proteins
protein_family
Type-B carboxylesterase/lipase family
uniprot
proteins
pubmed
10404729
uniprot
proteins
pubmed
11928765
uniprot
proteins
pubmed
12869558
uniprot
proteins
pubmed
12881446
uniprot
proteins
pubmed
1306123
uniprot
proteins
pubmed
1349196
uniprot
proteins
pubmed
1415224
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14760718
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15563885
uniprot
proteins
pubmed
15667209
uniprot
proteins
pubmed
15781196
uniprot
proteins
pubmed
1611188
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16788378
uniprot
proteins
pubmed
17355286
uniprot
proteins
pubmed
17700357
uniprot
proteins
pubmed
17768338
uniprot
proteins
pubmed
18075469
uniprot
proteins
pubmed
18203274
uniprot
proteins
pubmed
18300943
uniprot
proteins
pubmed
18975951
uniprot
proteins
pubmed
19139490
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19368529
uniprot
proteins
pubmed
19452557
uniprot
proteins
pubmed
19542320
uniprot
proteins
pubmed
20946535
uniprot
proteins
pubmed
22444575
uniprot
proteins
pubmed
2322535
uniprot
proteins
pubmed
23679855
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25054547
uniprot
proteins
pubmed
25264279
uniprot
proteins
pubmed
2915989
uniprot
proteins
pubmed
3035536
uniprot
proteins
pubmed
3115973
uniprot
proteins
pubmed
3477799
uniprot
proteins
pubmed
3542989
uniprot
proteins
pubmed
7634491
uniprot
proteins
pubmed
8554068
uniprot
proteins
pubmed
8680411
uniprot
proteins
pubmed
9110359
uniprot
proteins
pubmed
9191541
uniprot
proteins
pubmed
9388484
uniprot
proteins
pubmed
9543549
uniprot
proteins
pubmed
9694584
uniprot
proteins
sequence_length
602
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19368529, ECO:0000269|PubMed:19542320}.
uniprot
proteins