ODO1_HUMAN - dbPTM
ODO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ODO1_HUMAN
UniProt AC Q02218
Protein Name 2-oxoglutarate dehydrogenase, mitochondrial
Gene Name OGDH
Organism Homo sapiens (Human).
Sequence Length 1023
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 2-oxoglutarate dehydrogenase (E1) component of the 2-oxoglutarate dehydrogenase complex, which mediates the decarboxylation of alpha-ketoglutarate. [PubMed: 24495017 The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2)]
Protein Sequence MFHLRTCAAKLRPLTASQTVKTFSQNRPAAARTFQQIRCYSAPVAAEPFLSGTSSNYVEEMYCAWLENPKSVHKSWDIFFRNTNAGAPPGTAYQSPLPLSRGSLAAVAHAQSLVEAQPNVDKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGILDADLDSSVPADIISSTDKLGFYGLDESDLDKVFHLPTTTFIGGQESALPLREIIRRLEMAYCQHIGVEFMFINDLEQCQWIRQKFETPGIMQFTNEEKRTLLARLVRSTRFEEFLQRKWSSEKRFGLEGCEVLIPALKTIIDKSSENGVDYVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINRVTDRNITLSLVANPSHLEAADPVVMGKTKAEQFYCGDTEGKKVMSILLHGDAAFAGQGIVYETFHLSDLPSYTTHGTVHVVVNNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNSDDPEAVMYVCKVAAEWRSTFHKDVVVDLVCYRRNGHNEMDEPMFTQPLMYKQIRKQKPVLQKYAELLVSQGVVNQPEYEEEISKYDKICEEAFARSKDEKILHIKHWLDSPWPGFFTLDGQPRSMSCPSTGLTEDILTHIGNVASSVPVENFTIHGGLSRILKTRGEMVKNRTVDWALAEYMAFGSLLKEGIHIRLSGQDVERGTFSHRHHVLHDQNVDKRTCIPMNHLWPNQAPYTVCNSSLSEYGVLGFELGFAMASPNALVLWEAQFGDFHNTAQCIIDQFICPGQAKWVRQNGIVLLLPHGMEGMGPEHSSARPERFLQMCNDDPDVLPDLKEANFDINQLYDCNWVVVNCSTPGNFFHVLRRQILLPFRKPLIIFTPKSLLRHPEARSSFDEMLPGTHFQRVIPEDGPAAQNPENVKRLLFCTGKVYYDLTRERKARDMVGQVAITRIEQLSPFPFDLLLKEVQKYPNAELAWCQEEHKNQGYYDYVKPRLRTTISRAKPVWYAGRDPAAAPATGNKKTHLTELQRLLDTAFDLDVFKNFS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
15PhosphorylationAAKLRPLTASQTVKT
HHHHCCCCHHHHHHH		27.2628851738
17PhosphorylationKLRPLTASQTVKTFS
HHCCCCHHHHHHHHH		22.5828851738
19PhosphorylationRPLTASQTVKTFSQN
CCCCHHHHHHHHHCC		22.8328851738
24PhosphorylationSQTVKTFSQNRPAAA
HHHHHHHHCCCHHHH		31.6028851738
74UbiquitinationENPKSVHKSWDIFFR
HCCCCCCCCCEEEEC		51.6021890473
74SuccinylationENPKSVHKSWDIFFR
HCCCCCCCCCEEEEC		51.60-
74SuccinylationENPKSVHKSWDIFFR
HCCCCCCCCCEEEEC		51.6021890473
74UbiquitinationENPKSVHKSWDIFFR
HCCCCCCCCCEEEEC		51.60-
74UbiquitinationENPKSVHKSWDIFFR
HCCCCCCCCCEEEEC		51.6021890473
75PhosphorylationNPKSVHKSWDIFFRN
CCCCCCCCCEEEECC		18.3327251275
95PhosphorylationPPGTAYQSPLPLSRG
CCCCCCCCCCCCCHH		18.74-
100PhosphorylationYQSPLPLSRGSLAAV
CCCCCCCCHHHHHHH		32.43-
103PhosphorylationPLPLSRGSLAAVAHA
CCCCCHHHHHHHHHH		17.4522673903
122AcetylationEAQPNVDKLVEDHLA
HHCCCHHHHHHHHHH		50.5825038526
132PhosphorylationEDHLAVQSLIRAYQI
HHHHHHHHHHHHHHH		21.1124719451
171UbiquitinationDIISSTDKLGFYGLD
HHHCCCCCCCCCCCC		51.07-
175NitrationSTDKLGFYGLDESDL
CCCCCCCCCCCHHHH		18.25-
180PhosphorylationGFYGLDESDLDKVFH
CCCCCCHHHHCHHEE		43.04-
240PhosphorylationWIRQKFETPGIMQFT
HHHHHCCCCCHHHCC		29.92-
2512-HydroxyisobutyrylationMQFTNEEKRTLLARL
HHCCCHHHHHHHHHH		44.50-
261PhosphorylationLLARLVRSTRFEEFL
HHHHHHHHHCHHHHH		19.2220068231
262PhosphorylationLARLVRSTRFEEFLQ
HHHHHHHHCHHHHHH		28.9020068231
271AcetylationFEEFLQRKWSSEKRF
HHHHHHHHCCCCCCC		38.1730585163
276AcetylationQRKWSSEKRFGLEGC
HHHCCCCCCCCCCCH		55.7825953088
276SuccinylationQRKWSSEKRFGLEGC
HHHCCCCCCCCCCCH		55.7823954790
304PhosphorylationSSENGVDYVIMGMPH
CCCCCCCEEEECCCC		6.89-
335PhosphorylationQIFCQFDSKLEAADE
HHHHHHHHHHHCCCC		40.1930377224
336UbiquitinationIFCQFDSKLEAADEG
HHHHHHHHHHCCCCC		52.79-
344PhosphorylationLEAADEGSGDVKYHL
HHCCCCCCCCHHHHH		29.7630377224
3482-HydroxyisobutyrylationDEGSGDVKYHLGMYH
CCCCCCHHHHHHEEC		31.52-
367PhosphorylationRVTDRNITLSLVANP
CCCCCCCEEEEEECH		17.53-
369PhosphorylationTDRNITLSLVANPSH
CCCCCEEEEEECHHH		16.49-
375PhosphorylationLSLVANPSHLEAADP
EEEEECHHHHHHCCC		40.28-
389UbiquitinationPVVMGKTKAEQFYCG
CEEECCCCCEEEECC		54.11-
3892-HydroxyisobutyrylationPVVMGKTKAEQFYCG
CEEECCCCCEEEECC		54.11-
401AcetylationYCGDTEGKKVMSILL
ECCCCCCCEEEEEEE		35.6426051181
402AcetylationCGDTEGKKVMSILLH
CCCCCCCEEEEEEEE		54.772401481
457PhosphorylationTDPRMARSSPYPTDV
CCHHHHCCCCCCCHH		26.5721406692
458PhosphorylationDPRMARSSPYPTDVA
CHHHHCCCCCCCHHH		23.9321406692
460PhosphorylationRMARSSPYPTDVARV
HHHCCCCCCCHHHHH		22.2521406692
462PhosphorylationARSSPYPTDVARVVN
HCCCCCCCHHHHHHC		36.9421406692
495PhosphorylationKVAAEWRSTFHKDVV
HHHHHHHHHCCCCEE		36.1828348404
496PhosphorylationVAAEWRSTFHKDVVV
HHHHHHHHCCCCEEE		22.6128348404
499AcetylationEWRSTFHKDVVVDLV
HHHHHCCCCEEEEEE		48.297823115
527PhosphorylationMFTQPLMYKQIRKQK
CCCHHHHHHHHHHCC		13.8721214269
532UbiquitinationLMYKQIRKQKPVLQK
HHHHHHHHCCHHHHH		65.39-
534UbiquitinationYKQIRKQKPVLQKYA
HHHHHHCCHHHHHHH		39.8817370265
546PhosphorylationKYAELLVSQGVVNQP
HHHHHHHHCCCCCCH		22.61-
555PhosphorylationGVVNQPEYEEEISKY
CCCCCHHHHHHHHHH		35.01-
555NitrationGVVNQPEYEEEISKY
CCCCCHHHHHHHHHH		35.01-
561UbiquitinationEYEEEISKYDKICEE
HHHHHHHHHHHHHHH		64.23-
561AcetylationEYEEEISKYDKICEE
HHHHHHHHHHHHHHH		64.2325038526
561SuccinylationEYEEEISKYDKICEE
HHHHHHHHHHHHHHH		64.2323954790
564SuccinylationEEISKYDKICEEAFA
HHHHHHHHHHHHHHH		46.28-
564UbiquitinationEEISKYDKICEEAFA
HHHHHHHHHHHHHHH		46.28-
564SuccinylationEEISKYDKICEEAFA
HHHHHHHHHHHHHHH		46.28-
5642-HydroxyisobutyrylationEEISKYDKICEEAFA
HHHHHHHHHHHHHHH		46.28-
564AcetylationEEISKYDKICEEAFA
HHHHHHHHHHHHHHH		46.2825038526
577UbiquitinationFARSKDEKILHIKHW
HHCCCCCCEEEEEEE		61.78-
663PhosphorylationAEYMAFGSLLKEGIH
HHHHHHHHHHHCCEE		24.8724719451
682PhosphorylationGQDVERGTFSHRHHV
CCCCCCCCCCCCCCC		28.34-
684PhosphorylationDVERGTFSHRHHVLH
CCCCCCCCCCCCCCC		21.32-
6972-HydroxyisobutyrylationLHDQNVDKRTCIPMN
CCCCCCCCCCEEEHH		45.37-
697AcetylationLHDQNVDKRTCIPMN
CCCCCCCCCCEEEHH		45.372413423
801SulfoxidationRPERFLQMCNDDPDV
CHHHHHHHHCCCCCC		2.2221406390
858PhosphorylationRKPLIIFTPKSLLRH
CCCEEEECCHHHHCC		21.28-
860AcetylationPLIIFTPKSLLRHPE
CEEEECCHHHHCCHH		51.1626051181
861PhosphorylationLIIFTPKSLLRHPEA
EEEECCHHHHCCHHH		33.5624719451
870PhosphorylationLRHPEARSSFDEMLP
HCCHHHHCCHHHCCC		42.2628348404
871PhosphorylationRHPEARSSFDEMLPG
CCHHHHCCHHHCCCC		31.0328348404
899UbiquitinationAQNPENVKRLLFCTG
CCCHHHHHHHHHCCC		49.24-
8992-HydroxyisobutyrylationAQNPENVKRLLFCTG
CCCHHHHHHHHHCCC		49.24-
899AcetylationAQNPENVKRLLFCTG
CCCHHHHHHHHHCCC		49.2426051181
909PhosphorylationLFCTGKVYYDLTRER
HHCCCCCHHHCCCHH		8.51-
921SulfoxidationRERKARDMVGQVAIT
CHHHHHHHHHHHHHH		2.8021406390
928PhosphorylationMVGQVAITRIEQLSP
HHHHHHHHCHHHHCC		18.8221406692
934PhosphorylationITRIEQLSPFPFDLL
HHCHHHHCCCCHHHH		24.96-
943AcetylationFPFDLLLKEVQKYPN
CCHHHHHHHHHHCCC		56.6725038526
947AcetylationLLLKEVQKYPNAELA
HHHHHHHHCCCCCCC		68.7825038526
947UbiquitinationLLLKEVQKYPNAELA
HHHHHHHHCCCCCCC		68.78-
966PhosphorylationEHKNQGYYDYVKPRL
HHCCCCCHHHCCHHH		13.97-
968PhosphorylationKNQGYYDYVKPRLRT
CCCCCHHHCCHHHCC		8.34-
970UbiquitinationQGYYDYVKPRLRTTI
CCCHHHCCHHHCCCH		20.4219608861
970AcetylationQGYYDYVKPRLRTTI
CCCHHHCCHHHCCCH		20.4219608861
970SuccinylationQGYYDYVKPRLRTTI
CCCHHHCCHHHCCCH		20.4223954790
999AcetylationAAPATGNKKTHLTEL
CCCCCCCCCHHHHHH		61.462413425
999SuccinylationAAPATGNKKTHLTEL
CCCCCCCCCHHHHHH		61.4627452117
9992-HydroxyisobutyrylationAAPATGNKKTHLTEL
CCCCCCCCCHHHHHH		61.46-
999UbiquitinationAAPATGNKKTHLTEL
CCCCCCCCCHHHHHH		61.46-
1000UbiquitinationAPATGNKKTHLTELQ
CCCCCCCCHHHHHHH		45.22-
1012PhosphorylationELQRLLDTAFDLDVF
HHHHHHHHHHCHHHH		29.24-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 ODO1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ODO1_HUMAN !!
Disease-associated PTM Sites based on SAP

* 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 ODO1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLS1_HUMANPLSCR1physical
16189514
DLDH_HUMANDLDphysical
9727038
ODO2_HUMANDLSTphysical
9727038
ODO2_HUMANDLSTphysical
22939629
TSR1_HUMANTSR1physical
22939629
ODPA_HUMANPDHA1physical
22939629
ODPX_HUMANPDHXphysical
22939629
ODP2_HUMANDLATphysical
22939629
ODPB_HUMANPDHBphysical
22939629
SSBP_HUMANSSBP1physical
22939629
RM13_HUMANMRPL13physical
22939629
RM15_HUMANMRPL15physical
22939629
PYRD_HUMANDHODHphysical
22939629
RT02_HUMANMRPS2physical
22939629
RM41_HUMANMRPL41physical
22939629
SCFD1_HUMANSCFD1physical
22939629
RM38_HUMANMRPL38physical
22939629
ATP5H_HUMANATP5Hphysical
26344197
COX5A_HUMANCOX5Aphysical
26344197
CY1_HUMANCYC1physical
26344197
ODP2_HUMANDLATphysical
26344197
ODO2_HUMANDLSTphysical
26344197
NDUS4_HUMANNDUFS4physical
26344197
ODPA_HUMANPDHA1physical
26344197
SUCB2_HUMANSUCLG2physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00313Valproic Acid
Regulatory Network of ODO1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-970, AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-534, AND MASSSPECTROMETRY.

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