SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0CHLE_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameBCHE
DescriptionCholinesterase precursor (ec 3.1.1.8) (acylcholine acylhydrolase) (choline esterase ii) (butyrylcholine esterase) (pseudocholinesterase).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005576 extracellular region (NAS)
0001540 beta-amyloid binding (NAS)
0003824 catalytic activity (NAS)
0004104 cholinesterase activity (NAS)
0019899 enzyme binding (NAS)
0050783 cocaine metabolism (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/767437308.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
Group B carboxylesterases constitute a family of enzymes that includes proteins that catalyse the conversion of an acylcholine to a choline and a weak acid:Acylcholine + H2O -> Choline + COO-and those that catalyse the hydrolysis of acetylcholine to choline and acetate (acetylcholinesterases):Acetylcholine + H2O -> Choline + Acetate Acetylcholinesterase also acts on a variety of acetic esters and catalyses transacetylations. It is found in.r attached to.ellular or basement membranes of presynaptic cholinergic neurons and postsynaptic cholinoceptive cells. To prevent continuous firing of nerve impulses.cetylcholinesterase has a high K(cat) (~14000/s).o ensure that acetylcholine is broken down quickly. Cholinesterases themselves constitute a family of enzymes that fall into two main types.epending on their substrate preference; enzymes that preferentially hydrolyse acetyl esters are termed acetylcholinesterase (AChE) (); and those that prefer other types of ester.uch as butyrylcholine are termed butyrylcholinesterase (BChE) (). The 3D structure of acetylcholinesterase from Torpedo californica (Pacific Electric Ray) has been determined . The fold belongs to the alpha/beta class.ith a 3-layer alpha-beta-alpha sandwich architecture.Some of the proteins in this group are responsible for the molecular basis of the blood group antigens.urface markers on the outside of the red blood cell membrane. Most of these markers are proteins.ut some are carbohydrates attached to lipids or proteins [Reid M.E..omas-Francis C. The Blood Group Antigen FactsBook Academic Press.ondon / San Diego.1997)]. Acetylcholinesterase () belongs to the Yt blood group system and is associated with Yt(a/b) antigen.
  IPR000997:Cholinesterase
InterPro domains unassigned to SynO:
Higher eukaryotes have many distinct esterases. Among the different types arethose which act on carboxylic esters (). Carboxyl-esterases havebeen classified into three categories (A. and C) on the basis ofdifferential patterns of inhibition by organophosphates. The sequence of anumber of type-B carboxylesterases indicates that the majority are evolutionary related. As is the case for lipases and serine proteases.he catalytic apparatus ofesterases involves three residues (catalytic triad): a serine. glutamate oraspartate and a histidine.
  IPR002018:Carboxylesterase, type B
IPR002018:COesterase 
Evalue:-260.221862792969 
Location:9-550
SequencesProtein: CHLE_HUMAN (602 aa)
mRNA: NM_000055
Local Annotation
Synapse Ontology
the plasma membrane of the postsynaptic neuron. It apposes with presynaptic actiove zone.
sdb:0108 postsynaptic plasma membrane  (Evidence:domains)
transmitter inactivated by its enzyme etc.
sdb:0141 extracellular metabolism  (Evidence:domains)
KO assignmentK01050
  Level 3 annotation:
    cholinesterase
  Level 2 annotation:
    Other enzymes
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 201 residues, 166973386-166973988Exon2: 57 residues, 166986626-166986793Exon3: 510 residues, 167029998-167031523Exon4: 51 residues, 167037795-167037944Exon5: 2 residues, -Jump to CHLE_HUMAN  
Tune and view alternative isoforms