ODP2_HUMAN - dbPTM
ODP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ODP2_HUMAN
UniProt AC P10515
Protein Name Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Gene Name DLAT
Organism Homo sapiens (Human).
Sequence Length 647
Subcellular Localization Mitochondrion matrix.
Protein Description The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle..
Protein Sequence MWRVCARRAQNVAPWAGLEARWTALQEVPGTPRVTSRSGPAPARRNSVTTGYGGVRALCGWTPSSGATPRNRLLLQLLGSPGRRYYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEAFKNYTLDSSAAPTPQAAPAPTPAATASPPTPSAQAPGSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLEKPITMLL
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
35PhosphorylationVPGTPRVTSRSGPAP
CCCCCCCCCCCCCCC		21.50-
47PhosphorylationPAPARRNSVTTGYGG
CCCCCCCCCCCCCCC		21.0128348404
50PhosphorylationARRNSVTTGYGGVRA
CCCCCCCCCCCCCHH		26.6730576142
52PhosphorylationRNSVTTGYGGVRALC
CCCCCCCCCCCHHHC		14.4930576142
64PhosphorylationALCGWTPSSGATPRN
HHCCCCCCCCCCCCH		33.7530576142
80PhosphorylationLLLQLLGSPGRRYYS
HHHHHHCCCCCCCCC		24.9329978859
85PhosphorylationLGSPGRRYYSLPPHQ
HCCCCCCCCCCCCCC		8.9529978859
86PhosphorylationGSPGRRYYSLPPHQK
CCCCCCCCCCCCCCC		11.2629978859
87PhosphorylationSPGRRYYSLPPHQKV
CCCCCCCCCCCCCCC		26.0129978859
93AcetylationYSLPPHQKVPLPSLS
CCCCCCCCCCCCCCC		42.6730585923
98PhosphorylationHQKVPLPSLSPTMQA
CCCCCCCCCCCCCCC		49.5130108239
100PhosphorylationKVPLPSLSPTMQAGT
CCCCCCCCCCCCCCC		23.7430108239
102PhosphorylationPLPSLSPTMQAGTIA
CCCCCCCCCCCCCCE		20.6630108239
107PhosphorylationSPTMQAGTIARWEKK
CCCCCCCCCEEEECC		17.9323186163
132N6-lipoyllysineIAEVETDKATVGFES
EEEEECCCCEECCCH		54.07-
132LipoylationIAEVETDKATVGFES
EEEEECCCCEECCCH		54.073191998
132LipoylationIAEVETDKATVGFES
EEEEECCCCEECCCH		54.07-
154PhosphorylationKILVAEGTRDVPIGA
HHHHCCCCCCCCEEE		18.4019664995
169AcetylationIICITVGKPEDIEAF
EEEEEECCHHHHHHH		40.6825038526
259LipoylationLAEIETDKATIGFEV
EEEEECCCCEEEEEE		55.65-
259LipoylationLAEIETDKATIGFEV
EEEEECCCCEEEEEE		55.653191998
259N6-lipoyllysineLAEIETDKATIGFEV
EEEEECCCCEEEEEE		55.65-
271PhosphorylationFEVQEEGYLAKILVP
EEECCCCEEEEEECC		13.53-
281PhosphorylationKILVPEGTRDVPLGT
EEECCCCCCCCCCCC		23.26-
288PhosphorylationTRDVPLGTPLCIIVE
CCCCCCCCCEEEEEE		22.29-
291GlutathionylationVPLGTPLCIIVEKEA
CCCCCCEEEEEECCC		1.7822555962
312PhosphorylationDYRPTEVTDLKPQVP
CCCCCCCCCCCCCCC		29.4018491316
322PhosphorylationKPQVPPPTPPPVAAV
CCCCCCCCCCCCCCC		54.9527251275
332PhosphorylationPVAAVPPTPQPLAPT
CCCCCCCCCCCCCCC		28.6127251275
339PhosphorylationTPQPLAPTPSAPCPA
CCCCCCCCCCCCCCC		25.0327251275
341PhosphorylationQPLAPTPSAPCPATP
CCCCCCCCCCCCCCC		47.5227251275
347PhosphorylationPSAPCPATPAGPKGR
CCCCCCCCCCCCCCC		9.9827251275
358PhosphorylationPKGRVFVSPLAKKLA
CCCCEEECHHHHHHH		11.6123312004
362SuccinylationVFVSPLAKKLAVEKG
EEECHHHHHHHHHCC		56.8823954790
362AcetylationVFVSPLAKKLAVEKG
EEECHHHHHHHHHCC		56.8825953088
363UbiquitinationFVSPLAKKLAVEKGI
EECHHHHHHHHHCCC		35.75-
368AcetylationAKKLAVEKGIDLTQV
HHHHHHHCCCCCEEE		55.3525953088
376AcetylationGIDLTQVKGTGPDGR
CCCCEEECCCCCCCC		40.7225953088
376SuccinylationGIDLTQVKGTGPDGR
CCCCEEECCCCCCCC		40.7223954790
376UbiquitinationGIDLTQVKGTGPDGR
CCCCEEECCCCCCCC		40.72-
378PhosphorylationDLTQVKGTGPDGRIT
CCEEECCCCCCCCCC		39.5622210691
387AcetylationPDGRITKKDIDSFVP
CCCCCCHHHHHHHCC		51.7923749302
391PhosphorylationITKKDIDSFVPSKVA
CCHHHHHHHCCCCCC		28.6021712546
426PhosphorylationVFTDIPISNIRRVIA
EECCCCHHHHHHHHH		22.3524719451
462AcetylationGEVLLVRKELNKILE
CCEEEEHHHHHHHHC		60.1025038526
466AcetylationLVRKELNKILEGRSK
EEHHHHHHHHCCCCC		62.3819608861
466MalonylationLVRKELNKILEGRSK
EEHHHHHHHHCCCCC		62.3826320211
466SuccinylationLVRKELNKILEGRSK
EEHHHHHHHHCCCCC		62.3827452117
466UbiquitinationLVRKELNKILEGRSK
EEHHHHHHHHCCCCC		62.3819608861
4662-HydroxyisobutyrylationLVRKELNKILEGRSK
EEHHHHHHHHCCCCC		62.38-
472PhosphorylationNKILEGRSKISVNDF
HHHHCCCCCCCHHHH		45.2423312004
473SuccinylationKILEGRSKISVNDFI
HHHCCCCCCCHHHHH		37.33-
473MalonylationKILEGRSKISVNDFI
HHHCCCCCCCHHHHH		37.3326320211
473SuccinylationKILEGRSKISVNDFI
HHHCCCCCCCHHHHH		37.33-
4732-HydroxyisobutyrylationKILEGRSKISVNDFI
HHHCCCCCCCHHHHH		37.33-
473UbiquitinationKILEGRSKISVNDFI
HHHCCCCCCCHHHHH		37.33-
473AcetylationKILEGRSKISVNDFI
HHHCCCCCCCHHHHH		37.3325953088
475PhosphorylationLEGRSKISVNDFIIK
HCCCCCCCHHHHHHH		20.7128857561
490AcetylationASALACLKVPEANSS
HHHHHHHCCCCCCCC		56.4825953088
496PhosphorylationLKVPEANSSWMDTVI
HCCCCCCCCHHHHHH		32.2128857561
497PhosphorylationKVPEANSSWMDTVIR
CCCCCCCCHHHHHHH		26.6528857561
501PhosphorylationANSSWMDTVIRQNHV
CCCCHHHHHHHCCCE		11.1728857561
543PhosphorylationTIANDVVSLATKARE
HHHHHHHHHHHHHHC		16.4924641631
546PhosphorylationNDVVSLATKAREGKL
HHHHHHHHHHHCCCC		30.4524641631
547SuccinylationDVVSLATKAREGKLQ
HHHHHHHHHHCCCCC		39.58-
547SuccinylationDVVSLATKAREGKLQ
HHHHHHHHHHCCCCC		39.58-
547UbiquitinationDVVSLATKAREGKLQ
HHHHHHHHHHCCCCC		39.58-
547AcetylationDVVSLATKAREGKLQ
HHHHHHHHHHCCCCC		39.5825953088
552AcetylationATKAREGKLQPHEFQ
HHHHHCCCCCCCEEC		38.9125953088
637MalonylationQWLAEFRKYLEKPIT
HHHHHHHHHHHCCCE		60.5526320211
637AcetylationQWLAEFRKYLEKPIT
HHHHHHHHHHHCCCE		60.5525038526
641AcetylationEFRKYLEKPITMLL-
HHHHHHHCCCEECC-		38.8426051181
6412-HydroxyisobutyrylationEFRKYLEKPITMLL-
HHHHHHHCCCEECC-		38.84-
641UbiquitinationEFRKYLEKPITMLL-
HHHHHHHCCCEECC-		38.84-
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 ODP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
132KLipoylation

3191998
259KLipoylation

3191998
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 ODP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ODPX_HUMANPDHXphysical
14638692
ODPB_HUMANPDHBphysical
14638692
PDK3_HUMANPDK3physical
11978179
PDK2_HUMANPDK2physical
11978179
PDK1_HUMANPDK1physical
11978179
ODPX_HUMANPDHXphysical
22939629
ODPA_HUMANPDHA1physical
22939629
ODPAT_HUMANPDHA2physical
22939629
RM01_HUMANMRPL1physical
22939629
ODPX_HUMANPDHXphysical
21988832
KPCD3_HUMANPRKD3physical
21988832
CISY_HUMANCSphysical
26344197
CY1_HUMANCYC1physical
26344197
DLDH_HUMANDLDphysical
26344197
ODO2_HUMANDLSTphysical
26344197
LMAN1_HUMANLMAN1physical
26344197
NDUS2_HUMANNDUFS2physical
26344197
ODPB_HUMANPDHBphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=Primary biliary cirrhosis 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. Patients with primary biliary cirrhosis show autoantibodies against the E2 component of pyruvate dehydrogenase complex.
245348
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ODP2_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-466, AND MASS SPECTROMETRY.

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