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Protein Page:
OXCT1 (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
OXCT1 Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate. Defects in OXCT1 are a cause of succinyl-CoA-3-ketoacid- CoA transferase deficiency (SCOTD). A disorder of ketone body metabolism, characterized by episodic ketoacidosis. Patients are usually asymptomatic between episodes. Belongs to the 3-oxoacid CoA-transferase family. Note: This description may include information from UniProtKB.
Protein type: Lipid Metabolism - synthesis and degradation of ketone bodies; EC 2.8.3.5; Mitochondrial; Carbohydrate Metabolism - butanoate; Amino Acid Metabolism - valine, leucine and isoleucine degradation; Transferase
Chromosomal Location of Human Ortholog: 5p13.1
Cellular Component: mitochondrion; mitochondrial matrix
Molecular Function: protein homodimerization activity; 3-oxoacid CoA-transferase activity
Biological Process: response to starvation; response to drug; response to ethanol; heart development; ketone body catabolic process; response to hormone stimulus; ketone catabolic process; brain development; ketone body metabolic process; cellular lipid metabolic process; response to activity; response to nutrient
Disease: Succinyl-coa:3-oxoacid Coa Transferase Deficiency
Reference #:  P55809 (UniProtKB)
Alt. Names/Synonyms: 3-oxoacid CoA transferase 1; 3-oxoacid-CoA transferase 1; OXCT; OXCT1; SCOT; SCOT-s; SCOT1; somatic-type succinyl CoA:3-oxoacid CoA-transferase; Somatic-type succinyl-CoA:3-oxoacid-CoA-transferase; succinyl CoA:3-oxoacid CoA transferase; succinyl-CoA:3-ketoacid-CoA transferase; Succinyl-CoA:3-ketoacid-coenzyme A transferase 1, mitochondrial
Gene Symbols: OXCT1
Molecular weight: 56,158 Da
Basal Isoelectric point: 7.13  Predict pI for various phosphorylation states
Select Structure to View Below

OXCT1

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


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 2 K41 TSAHRHTKFYTDPVE
0 1 K83 ALLKTGVKGLTAVSN
0 2 S114-p QIKRMVSsyVGENAE
0 39 Y115-p IKRMVSsyVGENAEF
0 1 Y126-p NAEFERQyLSGELEV
0 1 T163-p YTPTGYGtLVQEGGs
0 9 S170-p tLVQEGGsPIKyNkD
0 1 Y174-p EGGsPIKyNkDGSVA
0 2 K176-ac GsPIKyNkDGSVAIA
0 1 K176-sc GsPIKyNkDGSVAIA
0 2 K185 GSVAIASKPREVREF
0 1 K214 FALVKAWKADRAGNV
0 1 K225-ac AGNVIFRkSARNFNL
0 1 K271 IYVHRLIKGEKYEKR
0 1 K274 HRLIKGEKYEKRIER
0 1 K293 KEGDGEAKsAKPGDD
0 1 S294-p EGDGEAKsAKPGDDV
0 2 K296 DGEAKsAKPGDDVRE
0 5 K406-ac LGAMQVSkYGDLANW
0 3 K418-ac ANWMIPGkMVkGMGG
0 7 K421-ac MIPGkMVkGMGGAMD
0 1 K421 MIPGkMVKGMGGAMD
0 1 K421-sc MIPGkMVkGMGGAMD
0 3 S431-p GGAMDLVssAKtKVV
0 3 S432-p GAMDLVssAKtKVVV
0 1 T435-p DLVssAKtKVVVTME
0 1 K436 LVssAKtKVVVTMEH
0 1 K446-sc VTMEHSAkGNAHKIM
0 1 K451 SAkGNAHKIMEkCTL
0 3 K455-ac NAHKIMEkCTLPLTG
0 1 K455-sc NAHKIMEkCTLPLTG
0 2 K473-ac VNRIITEkAVFDVDk
0 1 K473-sc VNRIITEkAVFDVDk
0 18 K480-ac kAVFDVDkkkGLTLI
0 52 K481-ac AVFDVDkkkGLTLIE
0 17 K482-ac VFDVDkkkGLTLIEL
0 1 S509-p TGCDFAVsPKLMPMQ
  mouse

 
K41-ac VSTRHHTkFYTDPVE
K83 ALLKTGVKDLTAVSN
S114 QIKRMISSYVGENAE
Y115 IKRMISSYVGENAEF
F126 NAEFERQFLSGELEV
T163 YTSTGYGTLVQEGGS
S170 TLVQEGGSPIKYNkD
Y174 EGGSPIKYNkDGSVA
K176-ac GSPIKYNkDGSVAIA
K176 GSPIKYNKDGSVAIA
K185-ac GSVAIASkPREVREF
K214 FALVKAWKADRAGNV
K225 AGNVIFRKSARNFNL
K271 IYVHRLIKGEKYEKR
K274 HRLIKGEKYEKRIER
K293-ac KEGDGKGkSGkPGGD
S294 EGDGKGkSGkPGGDV
K296-ac DGKGkSGkPGGDVRE
K406 LGAMQVSKYGDLANW
K418-ac ANWMIPGkMVkGMGG
K421-ac MIPGkMVkGMGGAMD
K421-ub MIPGkMVkGMGGAMD
K421 MIPGkMVKGMGGAMD
S431 GGAMDLVSSSKTKVV
S432 GAMDLVSSSKTKVVV
T435 DLVSSSKTKVVVTME
K436 LVSSSKTKVVVTMEH
K446 VTMEHSAKGNAHKIM
K451 SAKGNAHKIMEkCTL
K455-ac NAHKIMEkCTLPLTG
K455 NAHKIMEKCTLPLTG
K473 VNRIITEKGVFDVDk
K473 VNRIITEKGVFDVDk
K480-ac KGVFDVDkKNGLTLI
K481 GVFDVDkKNGLTLIE
N482 VFDVDkKNGLTLIEL
S509 TGCDFAVSPNLMPMQ
  rat

 
K41-ac VSTRHHTkFYTDPVE
K83-ac ALLKTGVkDLTAVSN
S114 QIKRMISSyVGENAE
Y115-p IKRMISSyVGENAEF
F126 NAEFERQFLSGELEV
T163 YTSTGYGTLVQEGGS
S170 TLVQEGGSPIKYNkD
Y174 EGGSPIKYNkDGSVA
K176-ac GSPIKYNkDGSVAIA
K176 GSPIKYNKDGSVAIA
K185-ac GSVAIASkPREVREF
K214-ac FALVKAWkADRAGNV
K225 AGNVIFRKSARNFNL
K271-ac IYVHRLIkGEkYEKR
K274-ac HRLIkGEkYEKRIER
K293 KEGEGKAKSGkPGED
S294 EGEGKAKSGkPGEDV
K296-ac EGKAKSGkPGEDVRE
K406 LGAMQVSKYGDLANW
K418-ac ANWMIPGkMVkGMGG
K421-ac MIPGkMVkGMGGAMD
K421 MIPGkMVKGMGGAMD
K421 MIPGkMVKGMGGAMD
S431 GGAMDLVSSSKTkVV
S432 GAMDLVSSSKTkVVV
T435 DLVSSSKTkVVVTME
K436-ub LVSSSKTkVVVTMEH
K446 VTMEHSAKGNAHkIM
K451-ac SAKGNAHkIMEkCTL
K455-ac NAHkIMEkCTLPLTG
K455 NAHkIMEKCTLPLTG
K473-ac VNRIITEkGVFDVDK
K473 VNRIITEKGVFDVDK
K480 kGVFDVDKKNGLTLI
K481 GVFDVDKKNGLTLIE
N482 VFDVDKKNGLTLIEL
S509 TGCDFAVSPNLMPMQ
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