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ChAT (human)

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: EC 2.3.1.6; Lipid Metabolism - glycerophospholipid; Acetyltransferase Cellular Component: mitochondrion; cell soma; axon; cytoplasm; nucleus; cytosol Molecular Function: choline binding; choline O-acetyltransferase activity Biological Process: response to drug; rhythmic excitation; antral ovarian follicle growth; neurotransmitter secretion; glycerophospholipid biosynthetic process; adult walking behavior; memory; synaptic transmission; rhythmic behavior; response to ethanol; acetylcholine biosynthetic process; phospholipid metabolic process; response to hypoxia; phosphatidylcholine biosynthetic process; dendrite development; neuromuscular synaptic transmission; establishment of synaptic specificity at neuromuscular junction; response to nutrient 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 2FY2 - A=120-733 (human) 2FY3 - A=120-733 (human) 2FY4 - A=120-733 (human) 2FY5 - A=120-733 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 2FY2 2FY3 2FY4 2FY5  |  ENZYME  |  Phospho3D  |  DISEASE 118490 254210  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	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

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-a	_MGLRTAkKRGLGGG
0	15		K16-a	RGLGGGGkWkREEGG
0	15		K18-a	LGGGGkWkREEGGGt
0	2		T25-p	kREEGGGtRGRREVR
0	1		T123-p	PRKMAAKtPsSEESG
0	2		S125-p	KMAAKtPsSEESGLP
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
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
T266	TVLLKDSTNRDSLDM
S270	KDSTNRDSLDMIERC
M355	EHLLKHMMTGNkKLV
G357	LLKHMMTGNkKLVRV
N358	LKHMMTGNkKLVRVD
K359-a	KHMMTGNkKLVRVDs
S366-p	kKLVRVDsVSELPAP
S368	LVRVDsVSELPAPRR
T446	LYQRLVPTYESASIR
Y447	YQRLVPTYESASIRR
S451	VPTYESASIRRFQEG
T467	VDNIRSATPEALAFV
S487	HKAAVLASEKLQLLQ

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