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Protein Page:
ChAT (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
ChAT an enzyme that catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses. Four alternative splice variants have been described. Note: This description may include information from UniProtKB.
Protein type: Lipid Metabolism - glycerophospholipid; Acetyltransferase; EC 2.3.1.6
Cellular Component: cell soma; mitochondrion; axon; cytoplasm; cytosol; nucleus
Molecular Function: choline O-acetyltransferase activity
Biological Process: rhythmic excitation; muscle development; neurotransmitter secretion; glycerophospholipid biosynthetic process; adult walking behavior; synaptic transmission; rhythmic behavior; phospholipid metabolic process; phosphatidylcholine biosynthetic process; dendrite development; neuromuscular synaptic transmission; establishment of synaptic specificity at neuromuscular junction; neurotransmitter biosynthetic process
Reference #:  P28329 (UniProtKB)
Alt. Names/Synonyms: acetyl CoA:choline O-acetyltransferase; CHAT; CHOACTase; Choline acetylase; choline acetyltransferase; Choline O-acetyltransferase; CLAT; CMS1A; CMS1A2
Gene Symbols: CHAT
Molecular weight: 82,536 Da
Basal Isoelectric point: 8.9  Predict pI for various phosphorylation states
Select Structure to View Below

ChAT

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 K7-ac _MGLRTAkKRGLGGG
0 15 K16-ac RGLGGGGkWkREEGG
0 15 K18-ac LGGGGkWkREEGGGt
0 2 T25-p kREEGGGtRGRREVR
0 1 T123-p PRKMAAKtPsSEESG
0 2 S125-p KMAAKtPsSEESGLP
0 1 S237-p DQLRFAAsLISGVLs
0 1 S244-p sLISGVLsYKALLDS
1 0 T373 TVLVKDSTNRDsLDM
0 1 S377-p KDSTNRDsLDMIERC
0 1 T462-p EHLLKHVtQSSRKLI
1 0 S464 LLKHVtQSSRKLIRA
1 0 S465 LKHVtQSSRKLIRAD
0 1 R466 KHVtQSSRKLIRADs
0 4 S473-p RKLIRADsVsELPAP
0 2 S475-p LIRADsVsELPAPRR
0 1 T553-p LHRRLVPtyESASIR
0 1 Y554-p HRRLVPtyESASIRR
2 1 S558 VPtyESASIRRFQEG
1 1 T574 VDNIRSATPEALAFV
1 0 S594 HKAAVPASEKLLLLK
  ChAT iso3  
- gap
- gap
- gap
- gap
T5 ___MAAKTPSSEESG
S7 _MAAKTPSSEESGLP
S119 DQLRFAASLISGVLS
S126 SLISGVLSYKALLDS
T255-p TVLVKDStNRDSLDM
S259 KDStNRDSLDMIERC
T344 EHLLKHVTQssRKLI
S346-p LLKHVTQssRKLIRA
S347-p LKHVTQssRKLIRAD
R348 KHVTQssRKLIRADS
S355 RKLIRADSVSELPAP
S357 LIRADSVSELPAPRR
T435 LHRRLVPTYESAsIR
Y436 HRRLVPTYESAsIRR
S440-p VPTYESAsIRRFQEG
T456-p VDNIRSAtPEALAFV
S476-p HKAAVPAsEKLLLLK
  mouse

 
- gap
- gap
- gap
- gap
A15 PPKMPVQASSCEEVL
S17 KMPVQASSCEEVLDL
S130 DQLRFAASLISGVLS
S137 SLISGVLSYKALLDS
T266 TVLLKDSTNRDSLDM
S270 KDSTNRDSLDMIERC
M355 EHLLKHMMTGNkKLV
G357 LLKHMMTGNkKLVRV
N358 LKHMMTGNkKLVRVD
K359-ac KHMMTGNkKLVRVDs
S366-p kKLVRVDsVSELPAP
S368 LVRVDsVSELPAPRR
T446 LYQRLVPTYESASIR
Y447 YQRLVPTYESASIRR
S451 VPTYESASIRRFQEG
T467 VDNIRSATPEALAFV
S487 HKAAVLASEKLQLLQ
  rat

 
- gap
- gap
- gap
- gap
A15 PQKMPVKASsWEELD
S17-p KMPVKASsWEELDLP
C129 DQLRFAACLISGVLS
S136 CLISGVLSYKTLLDS
T265 TVLLKDSTNRDSLDM
S269 KDSTNRDSLDMIERC
M354 EHLLKHMMTSNKKLV
S356 LLKHMMTSNKKLVRA
N357 LKHMMTSNKKLVRAD
K358 KHMMTSNKKLVRADs
S365-p KKLVRADsVSELPAP
S367 LVRADsVSELPAPRR
T445 LYQRLVPTYESASIR
Y446 YQRLVPTYESASIRR
S450 VPTYESASIRRFQEG
T466 VDNIRSATPEALAFV
S486 HKAAMPASEKLQLLQ
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