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DLST (human)

Overview DLST The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). Forms a 24-polypeptide structural core with octahedral symmetry. Belongs to the 2-oxoacid dehydrogenase family. Note: This description may include information from UniProtKB. Protein type: Carbohydrate Metabolism - citrate (TCA) cycle; Mitochondrial; Amino Acid Metabolism - lysine degradation; EC 2.3.1.61; Transferase Cellular Component: intracellular membrane-bound organelle; mitochondrion; mitochondrial matrix; cytoplasm; plasma membrane; nucleus; oxoglutarate dehydrogenase complex Molecular Function: dihydrolipoyllysine-residue succinyltransferase activity; heat shock protein binding; chaperone binding Biological Process: generation of precursor metabolites and energy; NADH metabolic process; tricarboxylic acid cycle; L-lysine catabolic process to acetyl-CoA via saccharopine; lysine catabolic process; 2-oxoglutarate metabolic process Reference #:  P36957 (UniProtKB) Alt. Names/Synonyms: 2-oxoglutarate dehydrogenase complex component E2; dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex); Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial; DLST; DLTS; E2K; ODO2; OGDC-E2 Gene Symbols: DLST Molecular weight: 48,755 Da Basal Isoelectric point: 9.1  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below DLST

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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

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
0	4		S81-p	KTPAFAEsVTEGDVR
0	1		T138-p	GGKVEGGtPLFTLRK
0	1		K154	GAAPAKAKPAEAPAA
0	1		K203-u	GKPVSAVkPTVAPPL
0	1		K217-u	LAEPGAGkGLRSEHR
0	1		K226-a	LRSEHREkMNRMRQR
0	89		K267-a	QEMRARHkEAFLkkH
0	143		K272-a	RHkEAFLkkHNLkLG
0	5		K273-a	HkEAFLkkHNLkLGF
0	26		K277-a	FLkkHNLkLGFMSAF
0	1		S282	NLkLGFMSAFVKASA
0	1		K307-u	AVIDDTTkEVVYRDY
0	1		K307	AVIDDTTKEVVYRDY
0	1		K353-u	TITELGEkARKNELA

	mouse
S82-p	QTPAFAEsVTEGDVR
T139	GGKVEGGTPLFTLRK
K155-a	GAAPAKAkPAETPAP
K204	SKPVSAIKPTAAPPL
K218	LAEAGAAKGLRSEHR
K227-a	LRSEHREkMNRMRQR
K268-a	QEMRARHkDAFLkkH
K273-a	RHkDAFLkkHNLkLG
K274-a	HkDAFLkkHNLkLGF
K278-a	FLkkHNLkLGFMsAF
S283-p	NLkLGFMsAFVKASA
K308	AVIDDATKEVVYRDY
K308-a	AVIDDATkEVVYRDY
K354	TINELGEKARKNELA

	rat
S82	QTPAFAESVTEGDVR
T139	GGKVEGGTPLFTLRK
K155	GAAPAKAKPAEAPAT
K204	SKPVSAIKPTAAPPL
K218	LAEAGAAKGLRSEHR
K227	LRSEHREKMNRMRQR
K268-a	QEMRARHkDAFLkKH
K273-a	RHkDAFLkKHNLkLG
K274	HkDAFLkKHNLkLGF
K278-a	FLkKHNLkLGFMSAF
S283	NLkLGFMSAFVKASA
K308	AVIDDATKEVVYRDY
K308	AVIDDATKEVVYRDY
K354	TINELGEKARKNELA

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