Reviewed, UniProtKB/Swiss-Prot P22303 (ACES_HUMAN)

Names and origin

Protein names

Recommended name:
    Acetylcholinesterase
      Short name=AChE
    EC=3.1.1.7

Gene names

Name:

ACHE

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	614 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	Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. Role in neuronal apoptosis. Ref.10 Ref.11 Ref.12 Ref.13
Catalytic activity	Acetylcholine + H2O = choline + acetate.
Subunit structure	Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers By similarity. Isoform H generates GPI-anchored dimers; disulfide linked. Isoform T generates multiple structures, ranging from monomers and dimers to collagen-tailed and hydrophobic-tailed forms, in which catalytic tetramers are associated with anchoring proteins that attach them to the basal lamina or to cell membranes. In the collagen-tailed forms, isoform T subunits are associated with a specific collagen, COLQ, which triggers the formation of isoform T tetramers, from monomers and dimers. Isoform R may be monomeric.
Subcellular location	Cell junction › synapse. Secreted By similarity. Cell membrane; Peripheral membrane protein By similarity. Isoform T: Nucleus. Note: Only observed in apoptotic nuclei. Ref.11 Ref.13 Isoform H: Cell membrane; Lipid-anchor › GPI-anchor; Extracellular side By similarity.
Tissue specificity	Isoform H is highly expressed in erythrocytes. Ref.10
Polymorphism	ACHE is responsible for the Yt blood group system. The molecular basis of the Yt(a)=Yt1/Yt(b)=Yt2 blood group antigens is a single variation in position 353; His-353 corresponds to Yt(a) and the rare variant with Asn-353 to Yt(b).
Involvement in disease	Behaves as an amyloid-promoting factor to promote the formation of amyloid plaques in Alzheimer disease. Ref.13
Sequence similarities	Belongs to the type-B carboxylesterase/lipase family.
Sequence caution	The sequence AAA68151.1 differs from that shown. Reason: Frameshift at position 604.

Ontologies

Keywords
Biological process	Neurotransmitter degradation
Cellular component	Cell junction Cell membrane Membrane Nucleus Secreted Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Molecular function	Blood group antigen Hydrolase Serine esterase
PTM	Disulfide bond GPI-anchor Glycoprotein Lipoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA replication Traceable author statement. Source: UniProtKB acetylcholine catabolic process in synaptic cleft Ref.12 Non-traceable author statement. Source: UniProtKB amyloid precursor protein metabolic process Traceable author statement. Source: UniProtKB cell adhesion Traceable author statement. Source: UniProtKB cell proliferation Traceable author statement. Source: UniProtKB muscle organ development Traceable author statement. Source: UniProtKB negative regulation of synaptic transmission, cholinergic Ref.12 Inferred by curator. Source: HGNC osteoblast development Inferred from expression pattern. Source: HGNC positive regulation of protein secretion Traceable author statement. Source: UniProtKB response to wounding Traceable author statement. Source: UniProtKB synaptogenesis Traceable author statement. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from direct assay. Source: HGNC anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW basal lamina Non-traceable author statement. Source: HGNC cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from direct assay. Source: HGNC synapse Inferred from direct assay. Source: HGNC
Molecular function	acetylcholine binding Ref.12 Non-traceable author statement. Source: UniProtKB acetylcholinesterase activity Ref.12 Inferred from mutant phenotype. Source: UniProtKB beta-amyloid binding Traceable author statement. Source: UniProtKB cholinesterase activity Ref.12 Inferred from direct assay. Source: HGNC collagen binding Inferred from direct assay. Source: HGNC laminin-1 binding Inferred from direct assay. Source: HGNC protein homodimerization activity Ref.12 Non-traceable author statement. Source: UniProtKB serine hydrolase activity Inferred from direct assay. Source: HGNC
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform T (identifier: P22303-1)

Also known as: ACHE-S; synaptic;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Only observed in apoptotic nuclei. Ref.11 Ref.13

Isoform H (identifier: P22303-2)

Also known as: ACHE-E; erythrocytic; E4-E5;

The sequence of this isoform differs from the canonical sequence as follows:
     575-614: DTLDEAERQW...YSKQDRCSDL → ASEAPSTCPG...LLFLSHLRRL

Note: The displayed full length sequence of this isoform is cleaved at position 589 to the mature form of the protein which is then linked to glycosylphosphatidyl inositol.

Isoform R (identifier: P22303-4)

Also known as: ACHE-R; readthrough;

The sequence of this isoform differs from the canonical sequence as follows:
     575-603: DTLDEAERQWKAEFHRWSSYMVHWKNQFD → GMQGPAGSAGRRGVGARQCNPSLLPLASE
     604-614: Missing.

Isoform 4 (identifier: P22303-3)

The sequence of this isoform differs from the canonical sequence as follows:
     357-444: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 31

31

Potential

Chain

32 – 614

583

Acetylcholinesterase

PRO_0000008587

Sites

Active site

234

1

Acyl-ester intermediate

Active site

365

1

Charge relay system

Active site

478

1

Charge relay system

Amino acid modifications

Glycosylation

296

1

N-linked (GlcNAc...) Potential

Glycosylation

381

1

N-linked (GlcNAc...) Ref.15

Glycosylation

495

1

N-linked (GlcNAc...) Ref.15

Disulfide bond

100 ↔ 127

Disulfide bond

288 ↔ 303

Disulfide bond

440 ↔ 560

Disulfide bond

611

Interchain

Natural variations

Alternative sequence

357 – 444

88

Missing in isoform 4.

VSP_035568

Alternative sequence

575 – 614

40

DTLDE…RCSDL → ASEAPSTCPGFTHGEAAPRP GLPLPLLLLHQLLLLFLSHL RRL in isoform H.

VSP_001457

Alternative sequence

575 – 603

29

DTLDE…KNQFD → GMQGPAGSAGRRGVGARQCN PSLLPLASE in isoform R.

VSP_035569

Alternative sequence

604 – 614

11

Missing in isoform R.

VSP_035570

Natural variant

34

1

R → Q: dbSNP rs17881553. Ref.5

VAR_021325

Natural variant

135

1

P → A: dbSNP rs17885778. Ref.5

VAR_021326

Natural variant

333

1

V → E: dbSNP rs8286.

VAR_011934

Natural variant

353

1

H → N in Yt(b) antigen. dbSNP rs1799805.

VAR_002359

Experimental info

Mutagenesis

206

1

D → N: Misfolding, absence of secretion. Ref.12

Mutagenesis

234

1

S → A: Loss of activity. Ref.12

Mutagenesis

365

1

E → A: Loss of activity. Ref.12

Mutagenesis

435

1

D → N: Misfolding, absence of secretion. Ref.12

Mutagenesis

478

1

H → A: Loss of activity. Ref.12

Mutagenesis

611

1

C → A: Impairment of interchain disulfide bridge formation. Ref.11

Sequence conflict

22

1

L → V in AAH94752. Ref.8

Sequence conflict

146

1

L → I in AAH94752. Ref.8

Secondary structure

1

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614

Helix Strand Turn

Details...

Beta strand

40 – 43

4

Beta strand

46 – 49

4

Beta strand

51 – 53

3

Beta strand

60 – 67

8

Helix

74 – 76

3

Beta strand

88 – 92

5

Beta strand

99 – 101

3

Helix

112 – 115

4

Beta strand

123 – 125

3

Beta strand

129 – 134

6

Beta strand

143 – 149

7

Turn

153 – 155

3

Helix

162 – 164

3

Helix

167 – 173

7

Beta strand

176 – 180

5

Helix

185 – 189

5

Beta strand

196 – 198

3

Helix

202 – 217

16

Helix

218 – 221

4

Beta strand

223 – 233

11

Helix

235 – 244

10

Helix

247 – 252

6

Beta strand

254 – 260

7

Turn

266 – 268

3

Helix

272 – 285

14

Helix

297 – 304

8

Helix

309 – 315

7

Turn

316 – 319

4

Beta strand

336 – 341

6

Helix

343 – 349

7

Beta strand

356 – 362

7

Beta strand

364 – 366

3

Helix

367 – 370

4

Turn

371 – 373

3

Beta strand

379 – 381

3

Helix

387 – 397

11

Helix

403 – 412

10

Helix

422 – 437

16

Helix

439 – 451

13

Beta strand

455 – 461

7

Helix

472 – 474

3

Helix

482 – 485

4

Helix

488 – 490

3

Helix

498 – 517

20

Turn

536 – 538

3

Beta strand

540 – 547

8

Beta strand

550 – 553

4

Helix

557 – 564

8

Helix

566 – 572

7

Helix

576 – 605

30

Sequences

	Sequence		Length	Mass (Da)
	Isoform T (ACHE-S) (synaptic) [UniParc]. Last modified August 1, 1991. Version 1. Checksum: B9AA84C77831C302	FASTA	614	67,796
	10 20 30 40 50 60 MRPPQCLLHT PSLASPLLLL LLWLLGGGVG AEGREDAELL VTVRGGRLRG IRLKTPGGPV 70 80 90 100 110 120 SAFLGIPFAE PPMGPRRFLP PEPKQPWSGV VDATTFQSVC YQYVDTLYPG FEGTEMWNPN 130 140 150 160 170 180 RELSEDCLYL NVWTPYPRPT SPTPVLVWIY GGGFYSGASS LDVYDGRFLV QAERTVLVSM 190 200 210 220 230 240 NYRVGAFGFL ALPGSREAPG NVGLLDQRLA LQWVQENVAA FGGDPTSVTL FGESAGAASV 250 260 270 280 290 300 GMHLLSPPSR GLFHRAVLQS GAPNGPWATV GMGEARRRAT QLAHLVGCPP GGTGGNDTEL 310 320 330 340 350 360 VACLRTRPAQ VLVNHEWHVL PQESVFRFSF VPVVDGDFLS DTPEALINAG DFHGLQVLVG 370 380 390 400 410 420 VVKDEGSYFL VYGAPGFSKD NESLISRAEF LAGVRVGVPQ VSDLAAEAVV LHYTDWLHPE 430 440 450 460 470 480 DPARLREALS DVVGDHNVVC PVAQLAGRLA AQGARVYAYV FEHRASTLSW PLWMGVPHGY 490 500 510 520 530 540 EIEFIFGIPL DPSRNYTAEE KIFAQRLMRY WANFARTGDP NEPRDPKAPQ WPPYTAGAQQ 550 560 570 580 590 600 YVSLDLRPLE VRRGLRAQAC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN 610 QFDHYSKQDR CSDL
	Isoform H (ACHE-E) (erythrocytic) (E4-E5). Checksum: 7AC0B2536131A89D	FASTA	617	67,376
	10 20 30 40 50 60 MRPPQCLLHT PSLASPLLLL LLWLLGGGVG AEGREDAELL VTVRGGRLRG IRLKTPGGPV 70 80 90 100 110 120 SAFLGIPFAE PPMGPRRFLP PEPKQPWSGV VDATTFQSVC YQYVDTLYPG FEGTEMWNPN 130 140 150 160 170 180 RELSEDCLYL NVWTPYPRPT SPTPVLVWIY GGGFYSGASS LDVYDGRFLV QAERTVLVSM 190 200 210 220 230 240 NYRVGAFGFL ALPGSREAPG NVGLLDQRLA LQWVQENVAA FGGDPTSVTL FGESAGAASV 250 260 270 280 290 300 GMHLLSPPSR GLFHRAVLQS GAPNGPWATV GMGEARRRAT QLAHLVGCPP GGTGGNDTEL 310 320 330 340 350 360 VACLRTRPAQ VLVNHEWHVL PQESVFRFSF VPVVDGDFLS DTPEALINAG DFHGLQVLVG 370 380 390 400 410 420 VVKDEGSYFL VYGAPGFSKD NESLISRAEF LAGVRVGVPQ VSDLAAEAVV LHYTDWLHPE 430 440 450 460 470 480 DPARLREALS DVVGDHNVVC PVAQLAGRLA AQGARVYAYV FEHRASTLSW PLWMGVPHGY 490 500 510 520 530 540 EIEFIFGIPL DPSRNYTAEE KIFAQRLMRY WANFARTGDP NEPRDPKAPQ WPPYTAGAQQ 550 560 570 580 590 600 YVSLDLRPLE VRRGLRAQAC AFWNRFLPKL LSATASEAPS TCPGFTHGEA APRPGLPLPL 610 LLLHQLLLLF LSHLRRL
	Isoform R (ACHE-R) (readthrough). Checksum: 3B65B9B3390C6AB1	FASTA	603	65,560
	10 20 30 40 50 60 MRPPQCLLHT PSLASPLLLL LLWLLGGGVG AEGREDAELL VTVRGGRLRG IRLKTPGGPV 70 80 90 100 110 120 SAFLGIPFAE PPMGPRRFLP PEPKQPWSGV VDATTFQSVC YQYVDTLYPG FEGTEMWNPN 130 140 150 160 170 180 RELSEDCLYL NVWTPYPRPT SPTPVLVWIY GGGFYSGASS LDVYDGRFLV QAERTVLVSM 190 200 210 220 230 240 NYRVGAFGFL ALPGSREAPG NVGLLDQRLA LQWVQENVAA FGGDPTSVTL FGESAGAASV 250 260 270 280 290 300 GMHLLSPPSR GLFHRAVLQS GAPNGPWATV GMGEARRRAT QLAHLVGCPP GGTGGNDTEL 310 320 330 340 350 360 VACLRTRPAQ VLVNHEWHVL PQESVFRFSF VPVVDGDFLS DTPEALINAG DFHGLQVLVG 370 380 390 400 410 420 VVKDEGSYFL VYGAPGFSKD NESLISRAEF LAGVRVGVPQ VSDLAAEAVV LHYTDWLHPE 430 440 450 460 470 480 DPARLREALS DVVGDHNVVC PVAQLAGRLA AQGARVYAYV FEHRASTLSW PLWMGVPHGY 490 500 510 520 530 540 EIEFIFGIPL DPSRNYTAEE KIFAQRLMRY WANFARTGDP NEPRDPKAPQ WPPYTAGAQQ 550 560 570 580 590 600 YVSLDLRPLE VRRGLRAQAC AFWNRFLPKL LSATGMQGPA GSAGRRGVGA RQCNPSLLPL ASE
	Isoform 4. Checksum: FB85F41EDFFF39DB	FASTA	526	58,352
	10 20 30 40 50 60 MRPPQCLLHT PSLASPLLLL LLWLLGGGVG AEGREDAELL VTVRGGRLRG IRLKTPGGPV 70 80 90 100 110 120 SAFLGIPFAE PPMGPRRFLP PEPKQPWSGV VDATTFQSVC YQYVDTLYPG FEGTEMWNPN 130 140 150 160 170 180 RELSEDCLYL NVWTPYPRPT SPTPVLVWIY GGGFYSGASS LDVYDGRFLV QAERTVLVSM 190 200 210 220 230 240 NYRVGAFGFL ALPGSREAPG NVGLLDQRLA LQWVQENVAA FGGDPTSVTL FGESAGAASV 250 260 270 280 290 300 GMHLLSPPSR GLFHRAVLQS GAPNGPWATV GMGEARRRAT QLAHLVGCPP GGTGGNDTEL 310 320 330 340 350 360 VACLRTRPAQ VLVNHEWHVL PQESVFRFSF VPVVDGDFLS DTPEALINAG DFHGLQLAGR 370 380 390 400 410 420 LAAQGARVYA YVFEHRASTL SWPLWMGVPH GYEIEFIFGI PLDPSRNYTA EEKIFAQRLM 430 440 450 460 470 480 RYWANFARTG DPNEPRDPKA PQWPPYTAGA QQYVSLDLRP LEVRRGLRAQ ACAFWNRFLP 490 500 510 520 KLLSATDTLD EAERQWKAEF HRWSSYMVHW KNQFDHYSKQ DRCSDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure." Soreq H., Ben-Aziz R., Prody C.A., Seidman S., Gnatt A., Neville L., Lieman-Hurwitz J., Lev-Lehman E., Ginzberg D., Lipidot-Lifson Y., Zakut H. Proc. Natl. Acad. Sci. U.S.A. 87:9688-9692(1990) [PubMed: 2263619] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM T).
[2]	"Expression of three alternative acetylcholinesterase messenger RNAs in human tumor cell lines of different tissue origins." Karpel R., Ben Aziz-Aloya R., Sternfeld M., Ehrlich G., Ginzberg D., Tarroni P., Clementi F., Zakut H., Soreq H. Exp. Cell Res. 210:268-277(1994) [PubMed: 8299725] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS H; R AND T).
[3]	Yang L., Zhang X.J. Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM T).
[5]	SeattleSNPs variation discovery resource Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-34; ALA-135 AND ASN-353.
[6]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS H AND T). Tissue: Brain.
[9]	"Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5." Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P., Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W., Koop B.F. Nucleic Acids Res. 29:1352-1365(2001) [PubMed: 11239002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 521-614.
[10]	"Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase." Chhajlani V., Derr D., Earles B., Schmell E., August T. FEBS Lett. 247:279-282(1989) [PubMed: 2714437] [Abstract] Cited for: PROTEIN SEQUENCE OF 256-273; 306-326; 396-422; 465-480 AND 528-551, FUNCTION, TISSUE SPECIFICITY. Tissue: Erythrocyte.
[11]	"The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580-->Ala mutant." Velan B., Grosfeld H., Kronman C., Leitner M., Gozes Y., Lazar A., Flashner Y., Marcus D., Cohen S., Shafferman A. J. Biol. Chem. 266:23977-23984(1991) [PubMed: 1748670] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-611.
[12]	"Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding." Shafferman A., Kronman C., Flashner Y., Leitner M., Grosfeld H., Ordentlich A., Gozes Y., Cohen S., Ariel N., Barak D. J. Biol. Chem. 267:17640-17648(1992) [PubMed: 1517212] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF ASP-206; SER-234; GLU-365; ASP-435 AND HIS-478.
[13]	"Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells." Yang L., He H.Y., Zhang X.J. Neurosci. Res. 42:261-268(2002) [PubMed: 11985878] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISEASE.
[14]	"External and internal electrostatic potentials of cholinesterase models." Felder C.E., Botti S.A., Lifson S., Silman I., Sussman J.L. J. Mol. Graph. Model. 15:318-327(1997) [PubMed: 9640563] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 35-574.
[15]	"Structures of recombinant native and E202Q mutant human acetylcholinesterase complexed with the snake-venom toxin fasciculin-II." Kryger G., Harel M., Giles K., Toker L., Velan B., Lazar A., Kronman C., Barak D., Ariel N., Shafferman A., Silman I., Sussman J.L. Acta Crystallogr. D 56:1385-1394(2000) [PubMed: 11053835] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 32-614 IN COMPLEX WITH FASCICULIN-2, GLYCOSYLATION AT ASN-381 AND ASN-495.
[16]	"The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix." Dvir H., Harel M., Bon S., Liu W.-Q., Vidal M., Garbay C., Sussman J.L., Massoulie J., Silman I. EMBO J. 23:4394-4405(2004) [PubMed: 15526038] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 575-614 IN COMPLEX WITH COLQ.
[17]	"Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene accounts for YT blood group polymorphism." Bartels C.F., Zelinski T., Lockridge O. Am. J. Hum. Genet. 52:928-936(1993) [PubMed: 8488842] [Abstract] Cited for: VARIANT BLOOD GROUP YT(B) ASN-353.
+	Additional computationally mapped references.

Web resources

dbRBC/BGMUT

Blood group antigen gene mutation database

Wikipedia

Acetylcholinesterase entry

SeattleSNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

M55040 mRNA. Translation: AAA68151.1.
S71129 Genomic DNA. Translation: AAC60618.1. Sequence problems.
AF334270 mRNA. Translation: AAO32948.1.
AK291321 mRNA. Translation: BAF84010.1.
AY750146 Genomic DNA. Translation: AAU43801.1.
AC011895 Genomic DNA. Translation: AAP22364.1.
AC011895 Genomic DNA. Translation: AAP22365.1.
CH236956 Genomic DNA. Translation: EAL23812.1.
CH236956 Genomic DNA. Translation: EAL23813.1.
CH471091 Genomic DNA. Translation: EAW76461.1.
CH471091 Genomic DNA. Translation: EAW76463.1.
BC036813 mRNA. Translation: AAH36813.1.
BC094752 mRNA. Translation: AAH94752.1. Frameshift.
BC105060 mRNA. Translation: AAI05061.1.
BC105062 mRNA. Translation: AAI05063.1.
AF312032 Genomic DNA. Translation: AAK21003.1.

IPI

IPI00026103.
IPI00220026.
IPI00844209.
IPI00913969.

PIR

A39256.

RefSeq

NP_000656.1.
NP_056646.1.

UniGene

Hs.154495

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B41	X-ray	2.76	A	36-574	[»]
1F8U	X-ray	2.90	A	32-614	[»]
1PUV	model	-	A	37-574	[»]
1PUW	model	-	A	37-574	[»]
1VZJ	X-ray	2.35	A/B/C/D/E/F/G/H	575-614	[»]
2CLJ	model	-	A	32-574	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1119N.

Protein family/group databases

MEROPS

S09.979.

2-D gel databases

SWISS-2DPAGE

P22303.

Proteomic databases

PRIDE

P22303.

Genome annotation databases

Ensembl

ENSG00000087085. Homo sapiens. [Contig view]

GeneID

43.

KEGG

hsa:43.

Organism-specific databases

GeneCards

GC07M100325.

H-InvDB

HIX0033555.

HGNC

HGNC:108. ACHE.

MIM

100740. gene+phenotype.
112100. phenotype.

PharmGKB

PA20.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P22303.

Enzyme and pathway databases

BRENDA

3.1.1.7. 247.

Gene expression databases

ArrayExpress

P22303.

Bgee

P22303.

GermOnline

ENSG00000087085. Homo sapiens.

Family and domain databases

InterPro

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

PANTHER

PTHR11559. CarbesteraseB. 1 hit.

Pfam

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

PRINTS

PR00878. CHOLNESTRASE.

PROSITE

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

ProtoNet

Search...

Other Resources

DrugBank

DB01122. Ambenonium.
DB00572. Atropine.
DB00122. Choline.
DB01245. Decamethonium.
DB00944. Demecarium bromide.
DB00843. Donepezil.
DB01010. Edrophonium.
DB01364. Ephedrine.
DB00674. Galantamine.
DB00483. Gallamine Triethiodide.
DB00677. Isoflurophate.
DB01400. Neostigmine.
DB00981. Physostigmine.
DB00545. Pyridostigmine.
DB00989. Rivastigmine.
DB00382. Tacrine.
DB01199. Tubocurarine.

NextBio

173.

SOURCE

Search...

Entry information

Entry name

ACES_HUMAN

Accession

Primary (citable) accession number: P22303
Secondary accession number(s): A4D2E2 , Q16169, Q29S23, Q2M324, Q504V3, Q86TM9, Q86YX9, Q9BXP7

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	June 16, 2009
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)