ODB2_HUMAN - dbPTM
ODB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ODB2_HUMAN
UniProt AC P11182
Protein Name Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
Gene Name DBT
Organism Homo sapiens (Human).
Sequence Length 482
Subcellular Localization Mitochondrion matrix.
Protein Description The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component..
Protein Sequence MAAVRMLRTWSRNAGKLICVRYFQTCGNVHVLKPNYVCFFGYPSFKYSHPHHFLKTTAALRGQVVQFKLSDIGEGIREVTVKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKKLYYNLDDIAYVGKPLVDIETEALKDSEEDVVETPAVSHDEHTHQEIKGRKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILNYLEKQTGAILPPSPKVEIMPPPPKPKDMTVPILVSKPPVFTGKDKTEPIKGFQKAMVKTMSAALKIPHFGYCDEIDLTELVKLREELKPIAFARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTEQGLIVPNVKNVQICSIFDIATELNRLQKLGSVGQLSTTDLTGGTFTLSNIGSIGGTFAKPVIMPPEVAIGALGSIKAIPRFNQKGEVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDLK
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
56PhosphorylationHPHHFLKTTAALRGQ
CCHHHHHHHHHHCCC		24.6620068231
57PhosphorylationPHHFLKTTAALRGQV
CHHHHHHHHHHCCCE		14.3520068231
68AcetylationRGQVVQFKLSDIGEG
CCCEEEEEHHHHCCC		29.9526051181
70PhosphorylationQVVQFKLSDIGEGIR
CEEEEEHHHHCCCEE		27.9820068231
80PhosphorylationGEGIREVTVKEWYVK
CCCEEEEEEEEEEEE		22.5520068231
82AcetylationGIREVTVKEWYVKEG
CEEEEEEEEEEEECC		32.9126051181
105N6-lipoyllysineICEVQSDKASVTITS
EEEEECCCCEEEEEE		48.05-
105LipoylationICEVQSDKASVTITS
EEEEECCCCEEEEEE		48.05-
105LipoylationICEVQSDKASVTITS
EEEEECCCCEEEEEE		48.05-
133SuccinylationDDIAYVGKPLVDIET
HHCEEECCCEEECCC		25.74-
133SuccinylationDDIAYVGKPLVDIET
HHCEEECCCEEECCC		25.74-
140PhosphorylationKPLVDIETEALKDSE
CCEEECCCHHHCCCC		27.2224275569
153PhosphorylationSEEDVVETPAVSHDE
CCCCCCCCCCCCCCC		12.63-
170UbiquitinationHQEIKGRKTLATPAV
CHHHCCCHHCCCHHH		57.4724816145
171PhosphorylationQEIKGRKTLATPAVR
HHHCCCHHCCCHHHH		21.9220068231
174PhosphorylationKGRKTLATPAVRRLA
CCCHHCCCHHHHHHH		18.2020068231
189PhosphorylationMENNIKLSEVVGSGK
HHCCCCHHHCCCCCC		24.2829743597
196SuccinylationSEVVGSGKDGRILKE
HHCCCCCCCCCCCHH		59.72-
196MalonylationSEVVGSGKDGRILKE
HHCCCCCCCCCCCHH		59.7226320211
196AcetylationSEVVGSGKDGRILKE
HHCCCCCCCCCCCHH		59.7226051181
1962-HydroxyisobutyrylationSEVVGSGKDGRILKE
HHCCCCCCCCCCCHH		59.72-
196SuccinylationSEVVGSGKDGRILKE
HHCCCCCCCCCCCHH		59.72-
202AcetylationGKDGRILKEDILNYL
CCCCCCCHHHHHHHH		51.4726051181
202UbiquitinationGKDGRILKEDILNYL
CCCCCCCHHHHHHHH		51.4729967540
2022-HydroxyisobutyrylationGKDGRILKEDILNYL
CCCCCCCHHHHHHHH		51.47-
213PhosphorylationLNYLEKQTGAILPPS
HHHHHHHCCCCCCCC		39.38-
220PhosphorylationTGAILPPSPKVEIMP
CCCCCCCCCCCEECC		35.1030108239
231AcetylationEIMPPPPKPKDMTVP
EECCCCCCCCCCEEE		71.1626051181
235SulfoxidationPPPKPKDMTVPILVS
CCCCCCCCEEEEEEE		5.2021406390
243AcetylationTVPILVSKPPVFTGK
EEEEEEECCCCCCCC		45.95-
250MalonylationKPPVFTGKDKTEPIK
CCCCCCCCCCCCCCC		53.6626320211
250AcetylationKPPVFTGKDKTEPIK
CCCCCCCCCCCCCCC		53.66-
261SuccinylationEPIKGFQKAMVKTMS
CCCCHHHHHHHHHHH		35.87-
261SuccinylationEPIKGFQKAMVKTMS
CCCCHHHHHHHHHHH		35.87-
261AcetylationEPIKGFQKAMVKTMS
CCCCHHHHHHHHHHH		35.8726051181
265AcetylationGFQKAMVKTMSAALK
HHHHHHHHHHHHHHC		25.9825953088
265MalonylationGFQKAMVKTMSAALK
HHHHHHHHHHHHHHC		25.9832601280
289MethylationIDLTELVKLREELKP
CCHHHHHHHHHHHHH		55.22-
289SuccinylationIDLTELVKLREELKP
CCHHHHHHHHHHHHH		55.22-
289SuccinylationIDLTELVKLREELKP
CCHHHHHHHHHHHHH		55.22-
289AcetylationIDLTELVKLREELKP
CCHHHHHHHHHHHHH		55.22-
295MalonylationVKLREELKPIAFARG
HHHHHHHHHHHHHCC		37.3426320211
295AcetylationVKLREELKPIAFARG
HHHHHHHHHHHHHCC		37.3419608861
304AcetylationIAFARGIKLSFMPFF
HHHHCCCCHHHHHHH		40.6826051181
350PhosphorylationNIGIAMDTEQGLIVP
EEEEEEECCCCEECC		19.6822210691
366PhosphorylationVKNVQICSIFDIATE
CCCCEEEEHHHHHHH		28.1122210691
372PhosphorylationCSIFDIATELNRLQK
EEHHHHHHHHHHHHH		41.1422210691
392PhosphorylationQLSTTDLTGGTFTLS
CCEECCCCCCEEEEE		36.05-
403PhosphorylationFTLSNIGSIGGTFAK
EEEECCCCCCCEECC		17.79-
410AcetylationSIGGTFAKPVIMPPE
CCCCEECCCEECCHH		35.3125038526
435SuccinylationAIPRFNQKGEVYKAQ
ECCCCCCCCCEEEEE		59.1327452117
435MalonylationAIPRFNQKGEVYKAQ
ECCCCCCCCCEEEEE		59.1326320211
435UbiquitinationAIPRFNQKGEVYKAQ
ECCCCCCCCCEEEEE		59.1329967540
435AcetylationAIPRFNQKGEVYKAQ
ECCCCCCCCCEEEEE		59.1326822725
440MalonylationNQKGEVYKAQIMNVS
CCCCCEEEEEEECEE		38.7026320211
440SuccinylationNQKGEVYKAQIMNVS
CCCCCEEEEEEECEE		38.7027452117
440SuccinylationNQKGEVYKAQIMNVS
CCCCCEEEEEEECEE		38.70-
440AcetylationNQKGEVYKAQIMNVS
CCCCCEEEEEEECEE		38.7023954790
447PhosphorylationKAQIMNVSWSADHRV
EEEEECEEECCCCCC		15.43-
459PhosphorylationHRVIDGATMSRFSNL
CCCCCHHHHHHHHHH		22.6220068231
461PhosphorylationVIDGATMSRFSNLWK
CCCHHHHHHHHHHHH		26.3120068231
464PhosphorylationGATMSRFSNLWKSYL
HHHHHHHHHHHHHHH		29.8729978859
469PhosphorylationRFSNLWKSYLENPAF
HHHHHHHHHHHCCEE		24.3029978859
470PhosphorylationFSNLWKSYLENPAFM
HHHHHHHHHHCCEEE		17.8229978859
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 ODB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ODB2_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 ODB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ODB2_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
0000269|PubMedNote=Patients with primary biliary cirrhosis (PBC) show autoantibodies against the E2 component of branched-chain alpha-keto acid dehydrogenase complex. PBC is a chronic, progressive cholestatic liver disease characterized by the presence of antimitochondrial autoantibodies in patients serum. It manifests with inflammatory obliteration of intra-hepatic bile duct, leading to liver cell damage and cirrhosis. {ECO
248600
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ODB2_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-295, AND MASS SPECTROMETRY.

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