UniProt ID | ODO2_HUMAN | |
---|---|---|
UniProt AC | P36957 | |
Protein Name | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial | |
Gene Name | DLST | |
Organism | Homo sapiens (Human). | |
Sequence Length | 453 | |
Subcellular Localization | Mitochondrion matrix . Nucleus . Mainly localizes in the mitochondrion. A small fraction localizes to the nucleus, where the 2-oxoglutarate dehydrogenase complex is required for histone succinylation. | |
Protein Description | Dihydrolipoamide succinyltransferase (E2) component of the 2-oxoglutarate dehydrogenase complex (By similarity). The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2) (By similarity). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. [PubMed: 29211711 A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A] | |
Protein Sequence | MLSRSRCVSRAFSRSLSAFQKGNCPLGRRSLPGVSLCQGPGYPNSRKVVINNSVFSVRFFRTTAVCKDDLVTVKTPAFAESVTEGDVRWEKAVGDTVAEDEVVCEIETDKTSVQVPSPANGVIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAEAPAAAAPKAEPTAAAVPPPAAPIPTQMPPVPSPSQPPSGKPVSAVKPTVAPPLAEPGAGKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEIDMSNIQEMRARHKEAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDTTKEVVYRDYIDISVAVATPRGLVVPVIRNVEAMNFADIERTITELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHGIFDRPVAIGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 | O-linked_Glycosylation | -----MLSRSRCVSR -----CCCHHHHHHH | 27.23 | 30379171 | |
5 | O-linked_Glycosylation | ---MLSRSRCVSRAF ---CCCHHHHHHHHH | 27.01 | 30379171 | |
53 | Phosphorylation | RKVVINNSVFSVRFF CEEEEECCEEEEEEE | 21.76 | 29083192 | |
56 | Phosphorylation | VINNSVFSVRFFRTT EEECCEEEEEEEEEE | 15.38 | 29083192 | |
74 | Succinylation | KDDLVTVKTPAFAES CCCEEEECCHHHHCC | 39.15 | 23954790 | |
74 | Ubiquitination | KDDLVTVKTPAFAES CCCEEEECCHHHHCC | 39.15 | - | |
75 | Phosphorylation | DDLVTVKTPAFAESV CCEEEECCHHHHCCC | 18.60 | 27251275 | |
81 | Phosphorylation | KTPAFAESVTEGDVR CCHHHHCCCCCCCCC | 30.80 | 25693802 | |
83 | Phosphorylation | PAFAESVTEGDVRWE HHHHCCCCCCCCCHH | 43.46 | 30108239 | |
108 | Phosphorylation | EVVCEIETDKTSVQV EEEEEEECCCCEEEC | 48.75 | 28060719 | |
110 | Lipoylation | VCEIETDKTSVQVPS EEEEECCCCEEECCC | 50.55 | - | |
110 | N6-lipoyllysine | VCEIETDKTSVQVPS EEEEECCCCEEECCC | 50.55 | - | |
111 | Phosphorylation | CEIETDKTSVQVPSP EEEECCCCEEECCCC | 36.62 | 28060719 | |
112 | Phosphorylation | EIETDKTSVQVPSPA EEECCCCEEECCCCC | 19.12 | 28060719 | |
117 | Phosphorylation | KTSVQVPSPANGVIE CCEEECCCCCCCEEE | 37.48 | 28060719 | |
138 | Phosphorylation | GGKVEGGTPLFTLRK CCEECCCCCCEEEEE | 27.89 | 21406692 | |
142 | Phosphorylation | EGGTPLFTLRKTGAA CCCCCCEEEEECCCC | 33.08 | 24719451 | |
154 | Malonylation | GAAPAKAKPAEAPAA CCCCCCCCCCCCCCC | 44.01 | 26320211 | |
154 | Acetylation | GAAPAKAKPAEAPAA CCCCCCCCCCCCCCC | 44.01 | - | |
203 | Malonylation | GKPVSAVKPTVAPPL CCCCCCCCCCCCCCC | 34.39 | 26320211 | |
203 | Ubiquitination | GKPVSAVKPTVAPPL CCCCCCCCCCCCCCC | 34.39 | - | |
205 | Phosphorylation | PVSAVKPTVAPPLAE CCCCCCCCCCCCCCC | 24.47 | 20068231 | |
217 | Ubiquitination | LAEPGAGKGLRSEHR CCCCCCCCCCCHHHH | 54.99 | 21890473 | |
221 | Acetylation | GAGKGLRSEHREKMN CCCCCCCHHHHHHHH | 42.68 | - | |
221 | Ubiquitination | GAGKGLRSEHREKMN CCCCCCCHHHHHHHH | 42.68 | - | |
221 | Phosphorylation | GAGKGLRSEHREKMN CCCCCCCHHHHHHHH | 42.68 | 20068231 | |
267 | Succinylation | QEMRARHKEAFLKKH HHHHHHHHHHHHHHH | 45.22 | 27452117 | |
267 | Ubiquitination | QEMRARHKEAFLKKH HHHHHHHHHHHHHHH | 45.22 | - | |
267 | 2-Hydroxyisobutyrylation | QEMRARHKEAFLKKH HHHHHHHHHHHHHHH | 45.22 | - | |
267 | Malonylation | QEMRARHKEAFLKKH HHHHHHHHHHHHHHH | 45.22 | 26320211 | |
267 | Ubiquitination | QEMRARHKEAFLKKH HHHHHHHHHHHHHHH | 45.22 | 19608861 | |
267 | Acetylation | QEMRARHKEAFLKKH HHHHHHHHHHHHHHH | 45.22 | 19608861 | |
272 | Acetylation | RHKEAFLKKHNLKLG HHHHHHHHHHCCCHH | 45.60 | 19608861 | |
273 | Acetylation | HKEAFLKKHNLKLGF HHHHHHHHHCCCHHH | 39.61 | 2402213 | |
277 | Ubiquitination | FLKKHNLKLGFMSAF HHHHHCCCHHHHHHH | 52.46 | - | |
277 | Acetylation | FLKKHNLKLGFMSAF HHHHHCCCHHHHHHH | 52.46 | 23954790 | |
277 | Malonylation | FLKKHNLKLGFMSAF HHHHHCCCHHHHHHH | 52.46 | 26320211 | |
282 | Phosphorylation | NLKLGFMSAFVKASA CCCHHHHHHHHHHHH | 19.12 | - | |
307 | Ubiquitination | AVIDDTTKEVVYRDY EEECCCCCEEEEECC | 51.08 | 21906983 | |
307 | Acetylation | AVIDDTTKEVVYRDY EEECCCCCEEEEECC | 51.08 | 23236377 | |
323 | Phosphorylation | DISVAVATPRGLVVP CEEEEEECCCCEEEE | 13.61 | - | |
338 | Sulfoxidation | VIRNVEAMNFADIER EECCHHHCCHHHHHH | 2.41 | 21406390 | |
353 | Ubiquitination | TITELGEKARKNELA HHHHHHHHHHHCCCE | 52.25 | 21906983 | |
437 | Methylation | REAVTFLRKIKAAVE HHHHHHHHHHHHHHC | 34.17 | - | |
440 | 2-Hydroxyisobutyrylation | VTFLRKIKAAVEDPR HHHHHHHHHHHCCCC | 33.07 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of ODO2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ODO2_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of ODO2_HUMAN !! |
Kegg Disease | ||||||
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OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, AND MASS SPECTROMETRY. |