UniProtKB - P21836 (ACES_MOUSE)

BLAST

>sp|P21836|ACES_MOUSE Acetylcholinesterase OS=Mus musculus OX=10090 GN=Ache PE=1 SV=1
MRPPWYPLHTPSLAFPLLFLLLSLLGGGARAEGREDPQLLVRVRGGQLRGIRLKAPGGPV
SAFLGIPFAEPPVGSRRFMPPEPKRPWSGVLDATTFQNVCYQYVDTLYPGFEGTEMWNPN
RELSEDCLYLNVWTPYPRPASPTPVLIWIYGGGFYSGAASLDVYDGRFLAQVEGAVLVSM
NYRVGTFGFLALPGSREAPGNVGLLDQRLALQWVQENIAAFGGDPMSVTLFGESAGAASV
GMHILSLPSRSLFHRAVLQSGTPNGPWATVSAGEARRRATLLARLVGCPPGGAGGNDTEL
IACLRTRPAQDLVDHEWHVLPQESIFRFSFVPVVDGDFLSDTPEALINTGDFQDLQVLVG
VVKDEGSYFLVYGVPGFSKDNESLISRAQFLAGVRIGVPQASDLAAEAVVLHYTDWLHPE
DPTHLRDAMSAVVGDHNVVCPVAQLAGRLAAQGARVYAYIFEHRASTLTWPLWMGVPHGY
EIEFIFGLPLDPSLNYTTEERIFAQRLMKYWTNFARTGDPNDPRDSKSPQWPPYTTAAQQ
YVSLNLKPLEVRRGLRAQTCAFWNRFLPKLLSATDTLDEAERQWKAEFHRWSSYMVHWKN
QFDHYSKQERCSDL

Align
Format
Add to basket Added to basket
History
Entry version 172 (07 Nov 2018)
Sequence version 1 (01 May 1991)
Previous versions | rss
Other tutorials and videos
Help video
Feedback

Protein

Acetylcholinesterase

Gene

Ache

Organism

Mus musculus (Mouse)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft.

Miscellaneous

Synapses usually contain asymmetric molecules of cholinesterase, with a collagen-like part disulfide-bonded to the catalytic part. A different, globular type of cholinesterase occurs on the outer surfaces of cell membranes, including those of erythrocytes.

This is the catalytic subunit of an asymmetric or soluble form of ACHE.

Catalytic activityⁱ

Acetylcholine + H₂O = choline + acetate.

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	234	Acyl-ester intermediate	1
Active siteⁱ	365	Charge relay system	1
Active siteⁱ	478	Charge relay system	1

GO - Molecular functionⁱ

acetylcholine binding Source: MGI
acetylcholinesterase activity
Source: MGI
Inferred from direct assayⁱ
- 16434405
- 7512968
choline binding Source: MGI
cholinesterase activity Source: MGI
collagen binding Source: MGI
hydrolase activity Source: MGI
laminin binding
Source: MGI
Inferred from physical interactionⁱ
- 15474030
protein homodimerization activity Source: MGI
protein self-association
Source: MGI
Inferred from physical interactionⁱ
- 8626792
serine hydrolase activity Source: MGI

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

acetylcholine catabolic process
Source: MGI
Inferred from direct assayⁱ
- 16434405
- 7512968
acetylcholine metabolic process Source: MGI
cell adhesion Source: MGI
choline metabolic process Source: MGI
neuron death Source: MGI
neurotransmitter receptor biosynthetic process
Source: MGI
Inferred from mutant phenotypeⁱ
- 14645660
osteoblast development Source: Ensembl
positive regulation of axonogenesis Source: MGI
positive regulation of cold-induced thermogenesis
Source: YuBioLab
Inferred from mutant phenotypeⁱ
- 17038428
positive regulation of dendrite morphogenesis Source: MGI
protein tetramerization
Source: MGI
Inferred from direct assayⁱ
- 8626792
receptor internalization
Source: MGI
Inferred from mutant phenotypeⁱ
- 14645660
regulation of receptor recycling
Source: MGI
Inferred from mutant phenotypeⁱ
- 14645660
retina development in camera-type eye
Source: MGI
Inferred from mutant phenotypeⁱ
- 15579149
synapse assembly Source: MGI

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Serine esterase
Biological process	Neurotransmitter degradation

Enzyme and pathway databases

BRENDAⁱ	3.1.1.7 3474
Reactomeⁱ	R-MMU-112311 Neurotransmitter clearance R-MMU-1483191 Synthesis of PC R-MMU-422085 Synthesis, secretion, and deacylation of Ghrelin
SABIO-RKⁱ	P21836

Protein family/group databases

ESTHERⁱ	mouse-ACHE AChE
MEROPS protease database More...MEROPSⁱ	S09.979

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Acetylcholinesterase (EC:3.1.1.7) Short name: AChE
Gene namesⁱ	Name:Ache
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 5

Organism-specific databases

MGIⁱ	MGI:87876 Ache

Keywords - Cellular componentⁱ

Cell junction, Cell membrane, Membrane, Secreted, Synapse

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL3198

ChEMBLⁱ

CHEMBL3198

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 31	Add BLAST		31
ChainⁱPRO_0000008588	32 – 614	AcetylcholinesteraseAdd BLAST		583

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Disulfide bondⁱ	100 ↔ 127
Disulfide bondⁱ	288 ↔ 303
Glycosylationⁱ	296	N-linked (GlcNAc...) asparagineSequence analysis	1
Glycosylationⁱ	381	N-linked (GlcNAc...) asparagine	1
Disulfide bondⁱ	440 ↔ 560
Glycosylationⁱ	495	N-linked (GlcNAc...) asparagine	1
Disulfide bondⁱ	611	InterchainBy similarity

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbⁱ	P21836
PRIDEⁱ	P21836

PTM databases

iPTMnetⁱ	P21836
PhosphoSitePlusⁱ	P21836

Expressionⁱ

Tissue specificityⁱ

Predominates in most expressing tissues except erythrocytes where a glycophospholipid-attached form of ACHE predominates.

Gene expression databases

Bgeeⁱ	ENSMUSG00000023328 Expressed in 88 organ(s), highest expression level in medulla oblongata
CleanExⁱ	MM_ACHE
ExpressionAtlasⁱ	P21836 baseline and differential
Genevisibleⁱ	P21836 MM

Interactionⁱ

Subunit structureⁱ

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 (By similarity). Interacts with PRIMA1. The interaction with PRIMA1 is required to anchor it to the basal lamina of cells and organize into tetramers.By similarity2 Publications

GO - Molecular functionⁱ

laminin binding
Source: MGI
Inferred from physical interactionⁱ
- 15474030
protein homodimerization activity Source: MGI
protein self-association
Source: MGI
Inferred from physical interactionⁱ
- 8626792

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	197921, 1 interactor
IntActⁱ	P21836, 2 interactors
Molecular INTeraction database More...MINTⁱ	P21836
STRINGⁱ	10090.ENSMUSP00000024099

Chemistry databases

BindingDBⁱ

P21836

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	32 – 34	Combined sources	3
Helixⁱ	37 – 39	Combined sources	3
Beta strandⁱ	40 – 43	Combined sources	4
Beta strandⁱ	46 – 49	Combined sources	4
Beta strandⁱ	51 – 55	Combined sources	5
Beta strandⁱ	58 – 67	Combined sources	10
Helixⁱ	74 – 76	Combined sources	3
Beta strandⁱ	88 – 92	Combined sources	5
Beta strandⁱ	99 – 101	Combined sources	3
Helixⁱ	112 – 115	Combined sources	4
Beta strandⁱ	123 – 125	Combined sources	3
Beta strandⁱ	129 – 137	Combined sources	9
Beta strandⁱ	143 – 149	Combined sources	7
Turnⁱ	153 – 155	Combined sources	3
Helixⁱ	162 – 164	Combined sources	3
Helixⁱ	167 – 173	Combined sources	7
Beta strandⁱ	176 – 180	Combined sources	5
Helixⁱ	185 – 189	Combined sources	5
Beta strandⁱ	196 – 198	Combined sources	3
Helixⁱ	202 – 217	Combined sources	16
Helixⁱ	218 – 221	Combined sources	4
Beta strandⁱ	223 – 233	Combined sources	11
Helixⁱ	235 – 244	Combined sources	10
Helixⁱ	247 – 250	Combined sources	4
Beta strandⁱ	254 – 260	Combined sources	7
Beta strandⁱ	263 – 268	Combined sources	6
Helixⁱ	272 – 285	Combined sources	14
Turnⁱ	286 – 290	Combined sources	5
Beta strandⁱ	291 – 293	Combined sources	3
Helixⁱ	297 – 306	Combined sources	10
Helixⁱ	309 – 315	Combined sources	7
Helixⁱ	316 – 318	Combined sources	3
Beta strandⁱ	321 – 323	Combined sources	3
Beta strandⁱ	336 – 341	Combined sources	6
Helixⁱ	343 – 349	Combined sources	7
Beta strandⁱ	356 – 362	Combined sources	7
Turnⁱ	363 – 366	Combined sources	4
Helixⁱ	367 – 370	Combined sources	4
Turnⁱ	371 – 373	Combined sources	3
Beta strandⁱ	379 – 381	Combined sources	3
Helixⁱ	387 – 397	Combined sources	11
Helixⁱ	403 – 413	Combined sources	11
Beta strandⁱ	416 – 418	Combined sources	3
Helixⁱ	422 – 437	Combined sources	16
Helixⁱ	439 – 451	Combined sources	13
Beta strandⁱ	455 – 461	Combined sources	7
Helixⁱ	472 – 474	Combined sources	3
Turnⁱ	478 – 481	Combined sources	4
Helixⁱ	482 – 485	Combined sources	4
Helixⁱ	488 – 490	Combined sources	3
Helixⁱ	492 – 494	Combined sources	3
Helixⁱ	498 – 517	Combined sources	20
Turnⁱ	523 – 525	Combined sources	3
Beta strandⁱ	526 – 528	Combined sources	3
Turnⁱ	536 – 538	Combined sources	3
Beta strandⁱ	540 – 547	Combined sources	8
Beta strandⁱ	550 – 553	Combined sources	4
Helixⁱ	557 – 564	Combined sources	8
Helixⁱ	567 – 570	Combined sources	4

Show more details

3D structure databases

ProteinModelPortalⁱ	P21836
SMRⁱ	P21836
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P21836

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the type-B carboxylesterase/lipase family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	KOG4389 Eukaryota COG2272 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00760000118946
HOGENOMⁱ	HOG000091866
HOVERGENⁱ	HBG008839
InParanoidⁱ	P21836
KEGG Orthology (KO) More...KOⁱ	K01049
OMAⁱ	HYSKQDR
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0I4G
PhylomeDBⁱ	P21836
TreeFamⁱ	TF315470

Family and domain databases

Gene3Dⁱ	3.40.50.1820, 1 hit
InterProⁱ	View protein in InterPro IPR029058 AB_hydrolase IPR014788 AChE_tetra IPR002018 CarbesteraseB IPR019826 Carboxylesterase_B_AS IPR019819 Carboxylesterase_B_CS IPR000997 Cholinesterase
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08674 AChE_tetra, 1 hit PF00135 COesterase, 1 hit
PRINTSⁱ	PR00878 CHOLNESTRASE
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD415333 AChE_tetra, 1 hit
SUPFAMⁱ	SSF53474 SSF53474, 1 hit
PROSITEⁱ	View protein in PROSITE PS00122 CARBOXYLESTERASE_B_1, 1 hit PS00941 CARBOXYLESTERASE_B_2, 1 hit

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show all Align All

Isoform T (identifier: P21836-1) [UniParc]FASTA Add to basket

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.

« Hide

        10         20         30         40         50
MRPPWYPLHT PSLAFPLLFL LLSLLGGGAR AEGREDPQLL VRVRGGQLRG 
        60         70         80         90        100
IRLKAPGGPV SAFLGIPFAE PPVGSRRFMP PEPKRPWSGV LDATTFQNVC 
       110        120        130        140        150
YQYVDTLYPG FEGTEMWNPN RELSEDCLYL NVWTPYPRPA SPTPVLIWIY 
       160        170        180        190        200
GGGFYSGAAS LDVYDGRFLA QVEGAVLVSM NYRVGTFGFL ALPGSREAPG 
       210        220        230        240        250
NVGLLDQRLA LQWVQENIAA FGGDPMSVTL FGESAGAASV GMHILSLPSR 
       260        270        280        290        300
SLFHRAVLQS GTPNGPWATV SAGEARRRAT LLARLVGCPP GGAGGNDTEL 
       310        320        330        340        350
IACLRTRPAQ DLVDHEWHVL PQESIFRFSF VPVVDGDFLS DTPEALINTG 
       360        370        380        390        400
DFQDLQVLVG VVKDEGSYFL VYGVPGFSKD NESLISRAQF LAGVRIGVPQ 
       410        420        430        440        450
ASDLAAEAVV LHYTDWLHPE DPTHLRDAMS AVVGDHNVVC PVAQLAGRLA 
       460        470        480        490        500
AQGARVYAYI FEHRASTLTW PLWMGVPHGY EIEFIFGLPL DPSLNYTTEE 
       510        520        530        540        550
RIFAQRLMKY WTNFARTGDP NDPRDSKSPQ WPPYTTAAQQ YVSLNLKPLE 
       560        570        580        590        600
VRRGLRAQTC AFWNRFLPKL LSATDTLDEA ERQWKAEFHR WSSYMVHWKN 
       610 
QFDHYSKQER CSDL

Length:614

Mass (Da):68,169

Last modified:May 1, 1991 - v1

Checksum:ⁱ66E2512463C21172

Isoform H (identifier: P21836-2)

Sequence is not available

Note: No experimental confirmation available.

Length:–

Mass (Da):–

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A0G2JDM6	A0A0G2JDM6_MOUSE	Carboxylic ester hydrolase Carboxylic ester hydrolase, EC 3.1.1.-	Ache	526	Annotation score:
D3Z064	D3Z064_MOUSE	Acetylcholinesterase Acetylcholinesterase	Ache	40	Annotation score:

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X56518 mRNA Translation: CAA39867.1 AF312033 Genomic DNA Translation: AAK28816.1 BC046327 mRNA Translation: AAH46327.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS19763.1 [P21836-1]
PIRⁱ	JH0314
NCBI Reference Sequences More...RefSeqⁱ	NP_001276939.1, NM_001290010.1 [P21836-1] NP_033729.1, NM_009599.4 [P21836-1]
UniGeneⁱ	Mm.255464 Mm.489229

Genome annotation databases

Ensemblⁱ	ENSMUST00000024099; ENSMUSP00000024099; ENSMUSG00000023328 [P21836-1] ENSMUST00000085934; ENSMUSP00000083097; ENSMUSG00000023328 [P21836-1]
GeneIDⁱ	11423
KEGGⁱ	mmu:11423
UCSC genome browser More...UCSCⁱ	uc009abt.1 mouse [P21836-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P21836	Carboxylic ester hydrolase		MOUSE		614	UniRef100_P21836
UPI000023C5F8		MOUSE		580
UPI00002323D8		MOUSE		549

Protein	Similar proteins		Species	Score	Length	Source
P21836	Acetylcholinesterase		RAT		614	UniRef90_P21836
Acetylcholinesterase		BOVIN		613
Carboxylic ester hydrolase		MOUSE		614
Carboxylic ester hydrolase		CEREH		681
Carboxylic ester hydrolase		AILME		637
+83

Protein	Similar proteins		Species	Score	Length	Source
P21836	Acetylcholinesterase	)	HUMAN		614	UniRef50_P22303
Acetylcholinesterase (Fragment)		RABIT		584
Acetylcholinesterase		RAT		614
Acetylcholinesterase		BOVIN		613
Acetylcholinesterase		FELCA		611
+258

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X56518 mRNA Translation: CAA39867.1 AF312033 Genomic DNA Translation: AAK28816.1 BC046327 mRNA Translation: AAH46327.1
CCDSⁱ	CCDS19763.1 [P21836-1]
PIRⁱ	JH0314
RefSeqⁱ	NP_001276939.1, NM_001290010.1 [P21836-1] NP_033729.1, NM_009599.4 [P21836-1]
UniGeneⁱ	Mm.255464 Mm.489229

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1C2B	X-ray	4.50	A	35-574	[»]
	1C2O	X-ray	4.20	A/B/C/D	36-574	[»]
	1J06	X-ray	2.35	A/B	32-574	[»]
	1J07	X-ray	2.35	A/B	32-574	[»]
	1KU6	X-ray	2.50	A	32-580	[»]
	1MAA	X-ray	2.90	A/B/C/D	32-578	[»]
	1MAH	X-ray	3.20	A	32-574	[»]
	1N5M	X-ray	2.20	A/B	32-572	[»]
	1N5R	X-ray	2.25	A/B	32-574	[»]
	1Q83	X-ray	2.65	A/B	1-580	[»]
	1Q84	X-ray	2.45	A/B	1-580	[»]
	2C0P	X-ray	2.50	A/B	32-574	[»]
	2C0Q	X-ray	2.50	A/B	32-574	[»]
	2GYU	X-ray	2.20	A/B	32-574	[»]
	2GYV	X-ray	2.50	A/B	32-574	[»]
	2GYW	X-ray	2.40	A/B	32-574	[»]
	2H9Y	X-ray	2.40	A/B	32-574	[»]
	2HA0	X-ray	2.20	A/B	32-574	[»]
	2HA2	X-ray	2.05	A/B	32-574	[»]
	2HA3	X-ray	2.25	A/B	32-574	[»]
	2HA4	X-ray	2.56	A/B	32-574	[»]
	2HA5	X-ray	2.15	A/B	32-574	[»]
	2HA6	X-ray	2.25	A/B	32-574	[»]
	2HA7	X-ray	2.66	A/B	32-574	[»]
	2JEY	X-ray	2.70	A/B	32-574	[»]
	2JEZ	X-ray	2.60	A/B	32-574	[»]
	2JF0	X-ray	2.50	A/B	32-574	[»]
	2JGE	X-ray	2.60	A/B	32-574	[»]
	2JGF	X-ray	2.50	A/B	32-574	[»]
	2JGI	X-ray	2.90	A/B	32-574	[»]
	2JGJ	X-ray	2.50	A/B	32-574	[»]
	2JGK	X-ray	2.90	A/B	32-574	[»]
	2JGL	X-ray	2.60	A/B	32-574	[»]
	2JGM	X-ray	2.90	A/B	32-574	[»]
	2WHP	X-ray	2.20	A/B	32-573	[»]
	2WHQ	X-ray	2.15	A/B	32-574	[»]
	2WHR	X-ray	2.54	A/B	32-574	[»]
	2WLS	X-ray	2.60	A/B	32-574	[»]
	2WU3	X-ray	2.70	A/B	32-574	[»]
	2WU4	X-ray	2.40	A/B	32-574	[»]
	2XUD	X-ray	2.65	A/B	32-574	[»]
	2XUF	X-ray	2.55	A/B	32-575	[»]
	2XUG	X-ray	2.60	A/B	32-575	[»]
	2XUH	X-ray	2.65	A/B	32-574	[»]
	2XUI	X-ray	2.60	A/B	32-574	[»]
	2XUJ	X-ray	2.65	A/B	32-574	[»]
	2XUK	X-ray	2.75	A/B	32-574	[»]
	2XUO	X-ray	2.80	A/B	32-574	[»]
	2XUP	X-ray	2.70	A/B	32-574	[»]
	2XUQ	X-ray	2.70	A/B	32-574	[»]
	2Y2U	X-ray	2.60	A/B	32-574	[»]
	2Y2V	X-ray	2.45	A/B	32-574	[»]
	3DL4	X-ray	2.50	A/B	32-574	[»]
	3DL7	X-ray	2.50	A/B	32-574	[»]
	3ZLT	X-ray	2.60	A/B	32-574	[»]
	3ZLU	X-ray	2.60	A/B	32-574	[»]
	3ZLV	X-ray	2.50	A/B	32-574	[»]
	4A16	X-ray	2.65	A/B/C/D	35-574	[»]
	4A23	X-ray	2.40	A/B	32-574	[»]
	4ARA	X-ray	2.50	A/B	32-574	[»]
	4ARB	X-ray	2.25	A/B	32-574	[»]
	4B7Z	X-ray	2.30	A/B	32-574	[»]
	4B80	X-ray	2.50	A/B	32-574	[»]
4B81	X-ray	2.80	A/B	32-574	[»]
4B82	X-ray	2.10	A/B	32-574	[»]
4B83	X-ray	2.40	A/B	32-574	[»]
4B84	X-ray	2.60	A/B	32-574	[»]
4B85	X-ray	2.10	A/B	32-574	[»]
4BC0	X-ray	3.35	A/B/C/D	32-574	[»]
4BC1	X-ray	2.95	A/B/C/D	32-574	[»]
4BTL	X-ray	2.50	A/B	32-574	[»]
5DTI	X-ray	2.00	A/B	32-573	[»]
5DTJ	X-ray	2.71	A/B	32-573	[»]
5EHN	X-ray	2.60	A/B	32-574	[»]
5EHQ	X-ray	2.50	A/B	32-574	[»]
5EHZ	X-ray	2.50	A/B	32-574	[»]
5EIA	X-ray	2.70	A/B	32-574	[»]
5EIE	X-ray	2.10	A/B	32-574	[»]
5EIH	X-ray	2.70	A/B	32-574	[»]
5FKJ	X-ray	3.13	A/B/C/D	32-574	[»]
5FPP	X-ray	2.40	A/B	32-574	[»]
5FUM	X-ray	2.50	A/B	32-574	[»]
5HCU	X-ray	2.42	A/B	32-571	[»]
5OV9	X-ray	2.40	A/B	32-574	[»]
ProteinModelPortalⁱ	P21836
SMRⁱ	P21836
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	197921, 1 interactor
IntActⁱ	P21836, 2 interactors
MINTⁱ	P21836
STRINGⁱ	10090.ENSMUSP00000024099

Chemistry databases

BindingDBⁱ	P21836
ChEMBLⁱ	CHEMBL3198

Protein family/group databases

ESTHERⁱ	mouse-ACHE AChE
MEROPSⁱ	S09.979

PTM databases

iPTMnetⁱ	P21836
PhosphoSitePlusⁱ	P21836

Proteomic databases

PaxDbⁱ	P21836
PRIDEⁱ	P21836

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000024099; ENSMUSP00000024099; ENSMUSG00000023328 [P21836-1] ENSMUST00000085934; ENSMUSP00000083097; ENSMUSG00000023328 [P21836-1]
GeneIDⁱ	11423
KEGGⁱ	mmu:11423
UCSCⁱ	uc009abt.1 mouse [P21836-1]

Organism-specific databases

CTDⁱ	43
MGIⁱ	MGI:87876 Ache

Phylogenomic databases

eggNOGⁱ	KOG4389 Eukaryota COG2272 LUCA
GeneTreeⁱ	ENSGT00760000118946
HOGENOMⁱ	HOG000091866
HOVERGENⁱ	HBG008839
InParanoidⁱ	P21836
KOⁱ	K01049
OMAⁱ	HYSKQDR
OrthoDBⁱ	EOG091G0I4G
PhylomeDBⁱ	P21836
TreeFamⁱ	TF315470

Enzyme and pathway databases

BRENDAⁱ	3.1.1.7 3474
Reactomeⁱ	R-MMU-112311 Neurotransmitter clearance R-MMU-1483191 Synthesis of PC R-MMU-422085 Synthesis, secretion, and deacylation of Ghrelin
SABIO-RKⁱ	P21836

Miscellaneous databases

EvolutionaryTraceⁱ	P21836
Protein Ontology More...PROⁱ	PR:P21836
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000023328 Expressed in 88 organ(s), highest expression level in medulla oblongata
CleanExⁱ	MM_ACHE
ExpressionAtlasⁱ	P21836 baseline and differential
Genevisibleⁱ	P21836 MM

Family and domain databases

Gene3Dⁱ	3.40.50.1820, 1 hit
InterProⁱ	View protein in InterPro IPR029058 AB_hydrolase IPR014788 AChE_tetra IPR002018 CarbesteraseB IPR019826 Carboxylesterase_B_AS IPR019819 Carboxylesterase_B_CS IPR000997 Cholinesterase
Pfamⁱ	View protein in Pfam PF08674 AChE_tetra, 1 hit PF00135 COesterase, 1 hit
PRINTSⁱ	PR00878 CHOLNESTRASE
ProDomⁱ	View protein in ProDom or Entries sharing at least one domain PD415333 AChE_tetra, 1 hit
SUPFAMⁱ	SSF53474 SSF53474, 1 hit
PROSITEⁱ	View protein in PROSITE PS00122 CARBOXYLESTERASE_B_1, 1 hit PS00941 CARBOXYLESTERASE_B_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ACES_MOUSE
Accessionⁱ	P21836Primary (citable) accession number: P21836
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
	Last sequence update:	May 1, 1991
	Last modified:	November 7, 2018
	This is version 172 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P21836 (ACES_MOUSE)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Acetylcholinesterase

Ache

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Plasma membrane

Extracellular region or secreted

Other locations

Plasma membrane

Endoplasmic reticulum

Extracellular region or secreted

Golgi apparatus

Nucleus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ