P06276 (CHLE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cholinesterase
EC=3.1.1.8

Alternative name(s):
Acylcholine acylhydrolase
Butyrylcholine esterase
Choline esterase II
Pseudocholinesterase

Gene names

Name:	BCHE
Synonyms:	CHE1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	602 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters. Ref.10 Ref.12
Catalytic activity	An acylcholine + H2O = choline + a carboxylate. Ref.12 Ref.19
Enzyme regulation	Inhibited by mercury. Inhibited by Tabun. Tabun forms a covalent adduct with Ser-226 that becomes irreversible upon aging. Ref.17 Ref.18 Ref.19
Subunit structure	Homotetramer; disulfide-linked. Dimer of dimers. Ref.7 Ref.10 Ref.14 Ref.15 Ref.16 Ref.17
Subcellular location	Secreted Ref.10 Ref.19.
Tissue specificity	Detected in blood plasma (at protein level). Present in most cells except erythrocytes. Ref.10 Ref.19
Involvement in disease	Butyrylcholinesterase deficiency (BChE deficiency) [MIM:177400]: Metabolic disorder characterized by prolonged apnoea after the use of certain anesthetic drugs, including the muscle relaxants succinylcholine or mivacurium and other ester local anesthetics. The duration of the prolonged apnoea varies significantly depending on the extent of the enzyme deficiency. BChE deficiency is a multifactorial disorder. The hereditary condition is transmitted as an autosomal recessive trait. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal
Molecular function	Hydrolase Serine esterase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	choline metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome cocaine metabolic process Traceable author statement PubMed 8622553. Source: UniProtKB synaptic transmission, cholinergic Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	endoplasmic reticulum lumen Inferred from Biological aspect of Ancestor. Source: RefGenome extracellular space Inferred from Biological aspect of Ancestor. Source: RefGenome membrane Inferred from electronic annotation. Source: InterPro nuclear envelope lumen Inferred from electronic annotation. Source: Compara
Molecular_function	acetylcholinesterase activity Inferred from sequence or structural similarity. Source: UniProtKB beta-amyloid binding Non-traceable author statement PubMed 11569538. Source: UniProtKB carboxylesterase activity Inferred from Biological aspect of Ancestor. Source: RefGenome enzyme binding Non-traceable author statement PubMed 11569538. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 28

28

Ref.6

Chain

29 – 602

574

Cholinesterase

PRO_0000008613

Regions

Region

144 – 145

2

Substrate binding

Sites

Active site

226

1

Acyl-ester intermediate Ref.6 Ref.14

Active site

353

1

Charge relay system Ref.14

Active site

466

1

Charge relay system Ref.14

Amino acid modifications

Modified residue

226

1

Phosphoserine Ref.13

Glycosylation

45

1

N-linked (GlcNAc...) Ref.6 Ref.9

Glycosylation

85

1

N-linked (GlcNAc...) Ref.6 Ref.9 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Glycosylation

134

1

N-linked (GlcNAc...) Ref.6 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Glycosylation

269

1

N-linked (GlcNAc...) Ref.6 Ref.14 Ref.15 Ref.17 Ref.19

Glycosylation

284

1

N-linked (GlcNAc...) Ref.6 Ref.11 Ref.18 Ref.19

Glycosylation

369

1

N-linked (GlcNAc...) Ref.6 Ref.9 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Glycosylation

483

1

N-linked (GlcNAc...) Ref.6 Ref.9

Glycosylation

509

1

N-linked (GlcNAc...) Ref.6 Ref.8 Ref.9

Glycosylation

513

1

N-linked (GlcNAc...) Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Glycosylation

514

1

N-linked (GlcNAc...) Ref.6 Ref.8 Ref.9

Disulfide bond

93 ↔ 120

Ref.7 Ref.14 Ref.15 Ref.16 Ref.17

Disulfide bond

280 ↔ 291

Ref.7 Ref.14 Ref.15 Ref.16 Ref.17

Disulfide bond

428 ↔ 547

Ref.7 Ref.14 Ref.15 Ref.16 Ref.17

Disulfide bond

599

Interchain Ref.7 Ref.14 Ref.15 Ref.16 Ref.17

Natural variations

Natural variant

32

1

Missing in BChE deficiency. Ref.30

VAR_040011

Natural variant

52

1

T → M in BChE deficiency. Ref.30
Corresponds to variant rs56309853 [ dbSNP | Ensembl ].

VAR_040012

Natural variant

56

1

F → I in BChE deficiency. Ref.35

VAR_040013

Natural variant

61

1

Y → C in BChE deficiency; enzymatically inactive in the plasma. Ref.27

VAR_040014

Natural variant

65

1

P → S in BChE deficiency; seems to cause reduced expression of the protein. Ref.27

VAR_040015

Natural variant

98

1

D → G in BChE deficiency; BChE atypical form; dibucaine-resistant. Ref.20 Ref.24 Ref.31 Ref.34
Corresponds to variant rs1799807 [ dbSNP | Ensembl ].

VAR_002360

Natural variant

98

1

D → H in BChE deficiency. Ref.34

VAR_040016

Natural variant

124

1

N → Y in BChE deficiency. Ref.35

VAR_040017

Natural variant

128

1

P → S in BChE deficiency. Ref.30
Corresponds to variant rs3732880 [ dbSNP | Ensembl ].

VAR_040018

Natural variant

143

1

G → D in BChE deficiency. Ref.31

VAR_040019

Natural variant

153

1

L → F in BChE deficiency; seems to cause reduced expression of the protein. Ref.27

VAR_040020

Natural variant

156

1

Y → C in BChE deficiency. Ref.28

VAR_040021

Natural variant

170

1

V → M in BChE deficiency; allele H variant. Ref.24

VAR_040022

Natural variant

198

1

D → E in BChE deficiency; seems to cause reduced expression of the protein. Ref.27

VAR_040023

Natural variant

226

1

S → G in BChE deficiency; enzymatically inactive in the plasma. Ref.27

VAR_040024

Natural variant

227

1

A → V in BChE deficiency. Ref.32

VAR_040025

Natural variant

229

1

A → T in BChE deficiency; enzymatically inactive in the plasma. Ref.27

VAR_040026

Natural variant

271

1

T → M in BChE deficiency; allele fluoride-1. Ref.22 Ref.34
Corresponds to variant rs28933389 [ dbSNP | Ensembl ].

VAR_040027

Natural variant

278

1

T → P in BChE deficiency. Ref.25 Ref.30

VAR_040028

Natural variant

283

1

E → D.
Corresponds to variant rs16849700 [ dbSNP | Ensembl ].

VAR_040029

Natural variant

295

1

K → R in BChE deficiency. Ref.30

VAR_040030

Natural variant

335

1

L → P in BChE deficiency; expressed at very low level. Ref.37

VAR_040031

Natural variant

356

1

A → D in BChE deficiency. Ref.38

VAR_040032

Natural variant

358

1

L → I in BChE deficiency; BChE variant form; fluoride-resistant; Japanese type. Ref.26 Ref.29 Ref.30 Ref.33

VAR_002362

Natural variant

393

1

G → R in BChE deficiency. Ref.23 Ref.25 Ref.30 Ref.33

VAR_040033

Natural variant

414

1

R → C in BChE deficiency. Ref.35 Ref.36

VAR_040034

Natural variant

418

1

G → V in BChE deficiency; allele fluoride-2. Ref.22
Corresponds to variant rs28933390 [ dbSNP | Ensembl ].

VAR_040035

Natural variant

446

1

F → S in BChE deficiency. Ref.25 Ref.30

VAR_040036

Natural variant

488

1

E → K in BChE deficiency. Ref.35

VAR_040037

Natural variant

499

1

W → R in BChE deficiency; seems to cause reduced expression of the protein. Ref.27

VAR_040038

Natural variant

502

1

F → L in BChE deficiency. Ref.36

VAR_040039

Natural variant

525

1

E → V in BChE deficiency; allele J variant. Ref.21

VAR_040040

Natural variant

543

1

R → C in BChE deficiency. Ref.25 Ref.30 Ref.33

VAR_040041

Natural variant

546

1

Q → L in BChE deficiency; seems to cause reduced expression of the protein. Ref.27

VAR_040042

Natural variant

567

1

A → T in BChE deficiency; allele K variant; with reduced enzyme activity. Ref.4 Ref.25 Ref.30 Ref.34
Corresponds to variant rs1803274 [ dbSNP | Ensembl ].

VAR_002364

Secondary structure

1

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602

Helix Strand Turn

Details...

Beta strand

33 – 36

4

Beta strand

39 – 42

4

Beta strand

44 – 48

5

Beta strand

51 – 60

10

Helix

67 – 69

3

Beta strand

82 – 85

4

Helix

105 – 108

4

Beta strand

116 – 118

3

Beta strand

122 – 130

9

Beta strand

133 – 141

9

Turn

145 – 147

3

Helix

154 – 156

3

Helix

159 – 165

7

Beta strand

168 – 172

5

Helix

177 – 181

5

Beta strand

190 – 192

3

Helix

194 – 209

16

Helix

210 – 213

4

Beta strand

215 – 225

11

Helix

227 – 237

11

Helix

239 – 244

6

Beta strand

246 – 252

7

Turn

258 – 260

3

Helix

264 – 277

14

Helix

285 – 292

8

Helix

297 – 304

8

Helix

305 – 307

3

Beta strand

308 – 310

3

Beta strand

324 – 326

3

Helix

331 – 336

6

Beta strand

345 – 350

6

Beta strand

352 – 354

3

Helix

355 – 358

4

Turn

359 – 361

3

Beta strand

367 – 369

3

Helix

375 – 385

11

Beta strand

387 – 389

3

Helix

391 – 401

11

Turn

405 – 408

4

Helix

412 – 425

14

Helix

427 – 438

12

Turn

439 – 441

3

Beta strand

444 – 449

6

Helix

460 – 462

3

Turn

466 – 469

4

Helix

470 – 473

4

Helix

476 – 478

3

Helix

480 – 482

3

Helix

486 – 505

20

Turn

511 – 514

4

Turn

523 – 525

3

Beta strand

527 – 531

5

Beta strand

538 – 541

4

Helix

544 – 551

8

Turn

552 – 555

4

Sequences

	Sequence		Length	Mass (Da)
	P06276 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: C9836409D9057F27	FASTA	602	68,418
	10 20 30 40 50 60 MHSKVTIICI RFLFWFLLLC MLIGKSHTED DIIIATKNGK VRGMNLTVFG GTVTAFLGIP 70 80 90 100 110 120 YAQPPLGRLR FKKPQSLTKW SDIWNATKYA NSCCQNIDQS FPGFHGSEMW NPNTDLSEDC 130 140 150 160 170 180 LYLNVWIPAP KPKNATVLIW IYGGGFQTGT SSLHVYDGKF LARVERVIVV SMNYRVGALG 190 200 210 220 230 240 FLALPGNPEA PGNMGLFDQQ LALQWVQKNI AAFGGNPKSV TLFGESAGAA SVSLHLLSPG 250 260 270 280 290 300 SHSLFTRAIL QSGSFNAPWA VTSLYEARNR TLNLAKLTGC SRENETEIIK CLRNKDPQEI 310 320 330 340 350 360 LLNEAFVVPY GTPLSVNFGP TVDGDFLTDM PDILLELGQF KKTQILVGVN KDEGTAFLVY 370 380 390 400 410 420 GAPGFSKDNN SIITRKEFQE GLKIFFPGVS EFGKESILFH YTDWVDDQRP ENYREALGDV 430 440 450 460 470 480 VGDYNFICPA LEFTKKFSEW GNNAFFYYFE HRSSKLPWPE WMGVMHGYEI EFVFGLPLER 490 500 510 520 530 540 RDNYTKAEEI LSRSIVKRWA NFAKYGNPNE TQNNSTSWPV FKSTEQKYLT LNTESTRIMT 550 560 570 580 590 600 KLRAQQCRFW TSFFPKVLEM TGNIDEAEWE WKAGFHRWNN YMMDWKNQFN DYTSKKESCV GL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the gene for human butyrylcholinesterase. Evidence for a single copy." Arpagaus M., Kott M., Vatsis K.P., Bartels C.F., la Du B.N., Lockridge O. Biochemistry 29:124-131(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues." Prody C.A., Zevin-Sonkin D., Gnatt A., Goldberg O., Soreq H. Proc. Natl. Acad. Sci. U.S.A. 84:3555-3559(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetus.
[3]	"Brain cDNA clone for human cholinesterase." McTiernan C., Adkins S., Chatonnet A., Vaughan T.A., Bartels C.F., Kott M., Rosenberry T.L., la Du B.N., Lockridge O. Proc. Natl. Acad. Sci. U.S.A. 84:6682-6686(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-567. Tissue: Stomach.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[6]	"Complete amino acid sequence of human serum cholinesterase." Lockridge O., Bartels C.F., Vaughan T.A., Wong C.K., Norton S.E., Johnson L.L. J. Biol. Chem. 262:549-557(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 29-602. Tissue: Plasma.
[7]	"Location of disulfide bonds within the sequence of human serum cholinesterase." Lockridge O., Adkins S., la Du B.N. J. Biol. Chem. 262:12945-12952(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
[8]	"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry." Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-509 AND ASN-514, MASS SPECTROMETRY. Tissue: Plasma.
[9]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45; ASN-85; ASN-369; ASN-483; ASN-509 AND ASN-514, MASS SPECTROMETRY. Tissue: Plasma.
[10]	"Adenovirus-transduced human butyrylcholinesterase in mouse blood functions as a bioscavenger of chemical warfare nerve agents." Chilukuri N., Duysen E.G., Parikh K., diTargiani R., Doctor B.P., Lockridge O., Saxena A. Mol. Pharmacol. 76:612-617(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT.
[11]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-134 AND ASN-284, MASS SPECTROMETRY. Tissue: Liver.
[12]	"The structure of G117H mutant of butyrylcholinesterase: nerve agents scavenger." Amitay M., Shurki A. Proteins 77:370-377(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[13]	"Identification of phosphorylated butyrylcholinesterase in human plasma using immunoaffinity purification and mass spectrometry." Aryal U.K., Lin C.T., Kim J.S., Heibeck T.H., Wang J., Qian W.J., Lin Y. Anal. Chim. Acta 723:68-75(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-226.
[14]	"Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products." Nicolet Y., Lockridge O., Masson P., Fontecilla-Camps J.C., Nachon F. J. Biol. Chem. 278:41141-41147(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITH SUBSTRATE, SUBUNIT, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513, DISULFIDE BONDS, ACTIVE SITE.
[15]	"Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging." Nachon F., Asojo O.A., Borgstahl G.E.O., Masson P., Lockridge O. Biochemistry 44:1154-1162(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH ECHOTHIOPHATE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513.
[16]	"Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase." Ngamelue M.N., Homma K., Lockridge O., Asojo O.A. Acta Crystallogr. F 63:723-727(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), DISULFIDE BONDS, GLYCOSYLATION AT ASN-85; ASN-134; ASN-369 AND ASN-513, SUBUNIT.
[17]	"Mechanisms of cholinesterase inhibition by inorganic mercury." Frasco M.F., Colletier J.-P., Weik M., Carvalho F., Guilhermino L., Stojan J., Fournier D. FEBS J. 274:1849-1861(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 29-557 IN COMPLEX WITH MERCURY IONS AND BUTANOIC ACID, DISULFIDE BONDS, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-369 AND ASN-513, ENZYME REGULATION.
[18]	"Aging of cholinesterases phosphylated by tabun proceeds through O-dealkylation." Carletti E., Li H., Li B., Ekstroem F., Nicolet Y., Loiodice M., Gillon E., Froment M.T., Lockridge O., Schopfer L.M., Masson P., Nachon F. J. Am. Chem. Soc. 130:16011-16020(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 29-557 IN COMPLEX WITH TABUN, ENZYME REGULATION, MASS SPECTROMETRY, GLYCOSYLATION AT ASN-85; ASN-134; ASN-284; ASN-369 AND ASN-513.
[19]	"Structure-activity analysis of aging and reactivation of human butyrylcholinesterase inhibited by analogues of tabun." Carletti E., Aurbek N., Gillon E., Loiodice M., Nicolet Y., Fontecilla-Camps J.C., Masson P., Thiermann H., Nachon F., Worek F. Biochem. J. 421:97-106(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 29-557 IN COMPLEX WITH TABUN ANALOGS, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-85; ASN-134; ASN-269; ASN-284; ASN-369 AND ASN-513, ENZYME REGULATION.
[20]	"Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase." McGuire M.C., Nogueira C.P., Bartels C.F., Lightstone H., Hajra A., van der Spek A.F.L., Lockridge O., la Du B.N. Proc. Natl. Acad. Sci. U.S.A. 86:953-957(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BCHE DEFICIENCY GLY-98.
[21]	"DNA mutations associated with the human butyrylcholinesterase J-variant." Bartels C.F., James K., La Du B.N. Am. J. Hum. Genet. 50:1104-1114(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BCHE DEFICIENCY VAL-525.
[22]	"Identification of two different point mutations associated with the fluoride-resistant phenotype for human butyrylcholinesterase." Nogueira C.P., Bartels C.F., McGuire M.C., Adkins S., Lubrano T., Rubinstein H.M., Lightstone H., Van Der Spek A.F.L., Lockridge O., La Du B.N. Am. J. Hum. Genet. 51:821-828(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BCHE DEFICIENCY MET-271 AND VAL-418.
[23]	"A variant serum cholinesterase and a confirmed point mutation at Gly-365 to Arg found in a patient with liver cirrhosis." Hada T., Muratani K., Ohue T., Imanishi H., Moriwaki Y., Itoh M., Amuro Y., Higashino K. Intern. Med. 31:357-362(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BCHE DEFICIENCY ARG-393.
[24]	"Structural basis of the butyrylcholinesterase H-variant segregating in two Danish families." Jensen F.S., Bartels C.F., La Du B.N. Pharmacogenetics 2:234-240(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BCHE DEFICIENCY GLY-98 AND MET-170.
[25]	"Genetic basis of the silent phenotype of serum butyrylcholinesterase in three compound heterozygotes." Maekawa M., Sudo K., Kanno T., Kotani K., Dey D.C., Ishikawa J., Izumi M., Etoh K. Clin. Chim. Acta 235:41-57(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BCHE DEFICIENCY PRO-278; ARG-393; SER-446; CYS-543 AND THR-567.
[26]	"Mutations of human butyrylcholinesterase gene in a family with hypocholinesterasemia." Iida S., Kinoshita M., Fujii H., Moriyama Y., Nakamura Y., Yura N., Moriwaki K. Hum. Mutat. 6:349-351(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BCHE DEFICIENCY ILE-358.
[27]	"Characterization of 12 silent alleles of the human butyrylcholinesterase (BCHE) gene." Primo-Parmo S.L., Bartels C.F., Wiersema B., van der Spek A.F.L., Innis J.W., La Du B.N. Am. J. Hum. Genet. 58:52-64(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BCHE DEFICIENCY CYS-61; SER-65; PHE-153; GLU-198; GLY-226; THR-229; ARG-499 AND LEU-546, CHARACTERIZATION OF VARIANTS BCHE DEFICIENCY SER-65; PHE-153; GLU-198; ARG-499 AND LEU-546.
[28]	"Genetic analysis of a Japanese patient with butyrylcholinesterase deficiency." Hidaka K., Iuchi I., Tomita M., Watanabe Y., Minatogawa Y., Iwasaki K., Gotoh K., Shimizu C. Ann. Hum. Genet. 61:491-496(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BCHE DEFICIENCY CYS-156.
[29]	"Human butyrylcholinesterase L330I mutation belongs to a fluoride-resistant gene, by expression in human fetal kidney cells." Sudo K., Maekawa M., Akizuki S., Magara T., Ogasawara H., Tanaka T. Biochem. Biophys. Res. Commun. 240:372-375(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BUTYRYLCHOLINESTERASE DEFICIENCY ILE-358.
[30]	"Genetic mutations of butyrylcholine esterase identified from phenotypic abnormalities in Japan." Maekawa M., Sudo K., Dey D.C., Ishikawa J., Izumi M., Kotani K., Kanno T. Clin. Chem. 43:924-929(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BCHE DEFICIENCY ILE-32 DEL; MET-52; SER-128; PRO-278; ARG-295; ILE-358; ARG-393; SER-446; CYS-543 AND THR-567.
[31]	"Characterization of an unstable variant (BChE115D) of human butyrylcholinesterase." Primo-Parmo S.L., Lightstone H., La Du B.N. Pharmacogenetics 7:27-34(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BCHE DEFICIENCY GLY-98 AND ASP-143.
[32]	"Identification of a point mutation associated with a silent phenotype of human serum butyrylcholinesterase - a case of familial cholinesterasemia." Sakamoto N., Hidaka K., Fujisawa T., Maeda M., Iuchi I. Clin. Chim. Acta 274:159-166(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BCHE DEFICIENCY VAL-227.
[33]	"Three point mutations of human butyrylcholinesterase in a Japanese family and the alterations of three-dimensional structure." Asanuma K., Yagihashi A., Uehara N., Kida T., Watanabe N. Clin. Chim. Acta 283:33-42(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BCHE DEFICIENCY ILE-358; ARG-393 AND CYS-543.
[34]	"Naturally occurring mutation, Asp70His, in human butyrylcholinesterase." Boeck A.T., Fry D.L., Sastre A., Lockridge O. Ann. Clin. Biochem. 39:154-156(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BCHE DEFICIENCY GLY-98; HIS-98; MET-271 AND THR-567.
[35]	"Butyrylcholinesterase (BCHE) genotyping for post-succinylcholine apnea in an Australian population." Yen T., Nightingale B.N., Burns J.C., Sullivan D.R., Stewart P.M. Clin. Chem. 49:1297-1308(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BCHE DEFICIENCY ILE-56; TYR-124; CYS-414 AND LYS-488.
[36]	"Novel mutations in the BCHE gene in patients with no butyrylcholinesterase activity." On-Kei Chan A., Lam C.-W., Tong S.-F., Man Tung C., Yung K., Chan Y.-W., Au K.-M., Yuen Y.-P., Hung C.-T., Ng K.-P., Shek C.-C. Clin. Chim. Acta 351:155-159(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BCHE DEFICIENCY CYS-414 AND LEU-502.
[37]	"Naturally occurring mutation Leu307Pro of human butyrylcholinesterase in the Vysya community of India." Manoharan I., Wieseler S., Layer P.G., Lockridge O., Boopathy R. Pharmacogenet. Genomics 16:461-468(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BCHE DEFICIENCY PRO-335, CHARACTERIZATION OF VARIANT BCHE DEFICIENCY PRO-335.
[38]	"Two novel mutations in the BCHE gene in patients with prolonged duration of action of mivacurium or succinylcholine during anaesthesia." Gaetke M.R., Bundgaard J.R., Viby-Mogensen J. Pharmacogenet. Genomics 17:995-999(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BCHE DEFICIENCY ASP-356.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M32391, M32389, M32390 Genomic DNA. Translation: AAA99296.1.
M16541 mRNA. Translation: AAA98113.1.
M16474 mRNA. Translation: AAA52015.1.
AK292063 mRNA. Translation: BAF84752.1.
BC018141 mRNA. Translation: AAH18141.1.

IPI

IPI00025864.

PIR

ACHU. A33769.

RefSeq

NP_000046.1. NM_000055.2.

UniGene

Hs.420483.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EHO	model	-	A	30-560	[»]
1EHQ	model	-	A	30-560	[»]
1KCJ	model	-	A	30-560	[»]
1P0I	X-ray	2.00	A	29-557	[»]
1P0M	X-ray	2.38	A	29-557	[»]
1P0P	X-ray	2.30	A	29-557	[»]
1P0Q	X-ray	2.43	A	29-557	[»]
1XLU	X-ray	2.20	A	29-557	[»]
1XLV	X-ray	2.25	A	29-557	[»]
1XLW	X-ray	2.10	A	29-557	[»]
2J4C	X-ray	2.75	A	29-557	[»]
2PM8	X-ray	2.80	A/B	29-602	[»]
2WID	X-ray	2.30	A	29-557	[»]
2WIF	X-ray	2.25	A	29-557	[»]
2WIG	X-ray	2.15	A	29-557	[»]
2WIJ	X-ray	2.10	A	29-557	[»]
2WIK	X-ray	2.10	A	29-557	[»]
2WIL	X-ray	3.10	A/B	29-557	[»]
2WSL	X-ray	2.00	A	29-557	[»]
2XMB	X-ray	2.10	A	29-557	[»]
2XMC	X-ray	2.40	A	29-557	[»]
2XMD	X-ray	2.30	A	29-557	[»]
2XMG	X-ray	2.70	A	29-557	[»]
2XQF	X-ray	2.10	A	31-557	[»]
2XQG	X-ray	2.30	A	31-557	[»]
2XQI	X-ray	2.60	A	31-557	[»]
2XQJ	X-ray	2.40	A	31-557	[»]
2XQK	X-ray	2.40	A	31-557	[»]
2Y1K	X-ray	2.50	A	29-557	[»]
3DJY	X-ray	2.10	A	29-557	[»]
3DKK	X-ray	2.31	A	29-557	[»]
3O9M	X-ray	2.98	A/B	29-602	[»]
4AQD	X-ray	2.50	A/B	29-557	[»]
4AXB	X-ray	2.40	A	31-557	[»]
4B0O	X-ray	2.35	A	29-557	[»]
4B0P	X-ray	2.50	A	29-557	[»]
4BBZ	X-ray	2.70	A	29-557	[»]

ProteinModelPortal

P06276.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-46476N.

STRING

9606.ENSP00000264381.

Protein family/group databases

MEROPS

S09.980.

PTM databases

PhosphoSite

P06276.

Polymorphism databases

DMDM

116353.

Proteomic databases

PaxDb

P06276.

PRIDE

P06276.

Protocols and materials databases

DNASU

590.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264381; ENSP00000264381; ENSG00000114200.

GeneID

590.

KEGG

hsa:590.

UCSC

uc003fem.4. human.

Organism-specific databases

CTD

590.

GeneCards

GC03M165490.

HGNC

HGNC:983. BCHE.

HPA

HPA001560.

MIM

177400. gene+phenotype.

neXtProt

NX_P06276.

Orphanet

132. Butyrylcholinesterase deficiency.
240861. Cisatracurium toxicity.
240891. Mivacurium toxicity.
240895. Pancuronium toxicity.
240907. Rocuronium toxicity.
240911. Satracurium toxicity.
241023. Susceptibility to prolonged paralysis due to cisatracurium treatment.
241025. Susceptibility to prolonged paralysis due to mivacurium treatment.
241027. Susceptibility to prolonged paralysis due to pancuronium treatment.
241029. Susceptibility to prolonged paralysis due to rocuronium treatment.
241031. Susceptibility to prolonged paralysis due to satracurium treatment.
241033. Susceptibility to prolonged paralysis due to vecuronium treatment.
240917. Vecuronium toxicity.

PharmGKB

PA25294.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2272.

HOVERGEN

HBG008839.

InParanoid

P06276.

KO

K01050.

OMA

GNDAFFY.

OrthoDB

EOG46WZ86.

PhylomeDB

P06276.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

SABIO-RK

P06276.

Gene expression databases

ArrayExpress

P06276.

Bgee

P06276.

CleanEx

HS_BCHE.

Genevestigator

P06276.

GermOnline

ENSG00000114200. Homo sapiens.

Family and domain databases

InterPro

IPR014788. AChE_tetra.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
IPR000997. Cholinesterase.
[Graphical view]

Pfam

PF08674. AChE_tetra. 1 hit.
PF00135. COesterase. 1 hit.
[Graphical view]

PRINTS

PR00878. CHOLNESTRASE.

ProDom

PD415333. AChE_tetra. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P06276.

ChEMBL

CHEMBL1914.

ChiTaRS

BCHE. human.

DrugBank

DB01122. Ambenonium.
DB00572. Atropine.
DB01408. Bambuterol.
DB00477. Chlorpromazine.
DB00122. Choline.
DB00568. Cinnarizine.
DB00944. Demecarium bromide.
DB00527. Dibucaine.
DB00843. Donepezil.
DB01057. Echothiophate Iodide.
DB01010. Edrophonium.
DB00392. Ethopropazine.
DB00292. Etomidate.
DB00674. Galantamine.
DB00941. Hexafluronium bromide.
DB00677. Isoflurophate.
DB00358. Mefloquine.
DB01226. Mivacurium.
DB01400. Neostigmine.
DB01337. Pancuronium.
DB00733. Pralidoxime.
DB01035. Procainamide.
DB00545. Pyridostigmine.
DB00989. Rivastigmine.
DB00202. Succinylcholine.
DB00871. Terbutaline.
DB01116. Trimethaphan.

EvolutionaryTrace

P06276.

GenomeRNAi

590.

NextBio

2405.

SOURCE

Search...

Entry information

Entry name

CHLE_HUMAN

Accession

Primary (citable) accession number: P06276
Secondary accession number(s): A8K7P8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	August 1, 1988
Last modified:	May 1, 2013
This is version 145 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.