ODO2_HUMAN - dbPTM
ODO2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
3O-linked_Glycosylation-----MLSRSRCVSR
-----CCCHHHHHHH
27.2330379171
5O-linked_Glycosylation---MLSRSRCVSRAF
---CCCHHHHHHHHH
27.0130379171
53PhosphorylationRKVVINNSVFSVRFF
CEEEEECCEEEEEEE
21.7629083192
56PhosphorylationVINNSVFSVRFFRTT
EEECCEEEEEEEEEE
15.3829083192
74SuccinylationKDDLVTVKTPAFAES
CCCEEEECCHHHHCC
39.1523954790
74UbiquitinationKDDLVTVKTPAFAES
CCCEEEECCHHHHCC
39.15-
75PhosphorylationDDLVTVKTPAFAESV
CCEEEECCHHHHCCC
18.6027251275
81PhosphorylationKTPAFAESVTEGDVR
CCHHHHCCCCCCCCC
30.8025693802
83PhosphorylationPAFAESVTEGDVRWE
HHHHCCCCCCCCCHH
43.4630108239
108PhosphorylationEVVCEIETDKTSVQV
EEEEEEECCCCEEEC
48.7528060719
110LipoylationVCEIETDKTSVQVPS
EEEEECCCCEEECCC
50.55-
110N6-lipoyllysineVCEIETDKTSVQVPS
EEEEECCCCEEECCC
50.55-
111PhosphorylationCEIETDKTSVQVPSP
EEEECCCCEEECCCC
36.6228060719
112PhosphorylationEIETDKTSVQVPSPA
EEECCCCEEECCCCC
19.1228060719
117PhosphorylationKTSVQVPSPANGVIE
CCEEECCCCCCCEEE
37.4828060719
138PhosphorylationGGKVEGGTPLFTLRK
CCEECCCCCCEEEEE
27.8921406692
142PhosphorylationEGGTPLFTLRKTGAA
CCCCCCEEEEECCCC
33.0824719451
154MalonylationGAAPAKAKPAEAPAA
CCCCCCCCCCCCCCC
44.0126320211
154AcetylationGAAPAKAKPAEAPAA
CCCCCCCCCCCCCCC
44.01-
203MalonylationGKPVSAVKPTVAPPL
CCCCCCCCCCCCCCC
34.3926320211
203UbiquitinationGKPVSAVKPTVAPPL
CCCCCCCCCCCCCCC
34.39-
205PhosphorylationPVSAVKPTVAPPLAE
CCCCCCCCCCCCCCC
24.4720068231
217UbiquitinationLAEPGAGKGLRSEHR
CCCCCCCCCCCHHHH
54.9921890473
221AcetylationGAGKGLRSEHREKMN
CCCCCCCHHHHHHHH
42.68-
221UbiquitinationGAGKGLRSEHREKMN
CCCCCCCHHHHHHHH
42.68-
221PhosphorylationGAGKGLRSEHREKMN
CCCCCCCHHHHHHHH
42.6820068231
267SuccinylationQEMRARHKEAFLKKH
HHHHHHHHHHHHHHH
45.2227452117
267UbiquitinationQEMRARHKEAFLKKH
HHHHHHHHHHHHHHH
45.22-
2672-HydroxyisobutyrylationQEMRARHKEAFLKKH
HHHHHHHHHHHHHHH
45.22-
267MalonylationQEMRARHKEAFLKKH
HHHHHHHHHHHHHHH
45.2226320211
267UbiquitinationQEMRARHKEAFLKKH
HHHHHHHHHHHHHHH
45.2219608861
267AcetylationQEMRARHKEAFLKKH
HHHHHHHHHHHHHHH
45.2219608861
272AcetylationRHKEAFLKKHNLKLG
HHHHHHHHHHCCCHH
45.6019608861
273AcetylationHKEAFLKKHNLKLGF
HHHHHHHHHCCCHHH
39.612402213
277UbiquitinationFLKKHNLKLGFMSAF
HHHHHCCCHHHHHHH
52.46-
277AcetylationFLKKHNLKLGFMSAF
HHHHHCCCHHHHHHH
52.4623954790
277MalonylationFLKKHNLKLGFMSAF
HHHHHCCCHHHHHHH
52.4626320211
282PhosphorylationNLKLGFMSAFVKASA
CCCHHHHHHHHHHHH
19.12-
307UbiquitinationAVIDDTTKEVVYRDY
EEECCCCCEEEEECC
51.0821906983
307AcetylationAVIDDTTKEVVYRDY
EEECCCCCEEEEECC
51.0823236377
323PhosphorylationDISVAVATPRGLVVP
CEEEEEECCCCEEEE
13.61-
338SulfoxidationVIRNVEAMNFADIER
EECCHHHCCHHHHHH
2.4121406390
353UbiquitinationTITELGEKARKNELA
HHHHHHHHHHHCCCE
52.2521906983
437MethylationREAVTFLRKIKAAVE
HHHHHHHHHHHHHHC
34.17-
4402-HydroxyisobutyrylationVTFLRKIKAAVEDPR
HHHHHHHHHHHCCCC
33.07-

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 ODO2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ODO2_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 ODO2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DLG5_HUMANDLG5physical
16169070
PROF2_HUMANPFN2physical
16169070
ZHX1_HUMANZHX1physical
16169070
ZBT16_HUMANZBTB16physical
16169070
SIAH2_HUMANSIAH2physical
15466852
RM39_HUMANMRPL39physical
22939629
RM40_HUMANMRPL40physical
22939629
RM15_HUMANMRPL15physical
22939629
RM49_HUMANMRPL49physical
22939629
ODB2_HUMANDBTphysical
26344197
STML2_HUMANSTOML2physical
26344197
FLOT1_HUMANFLOT1physical
29128334
SQSTM_HUMANSQSTM1physical
29128334
CHTOP_HUMANCHTOPphysical
29128334
NOP10_HUMANNOP10physical
29128334
P53_HUMANTP53physical
29128334
PPIA_HUMANPPIAphysical
29128334
FLOT2_HUMANFLOT2physical
29128334
PROF1_HUMANPFN1physical
29128334
KCRB_HUMANCKBphysical
29128334
CKAP4_HUMANCKAP4physical
29128334
TOP1_HUMANTOP1physical
29128334
NHP2_HUMANNHP2physical
29128334
H2AV_HUMANH2AFVphysical
29128334
DHB4_HUMANHSD17B4physical
29128334
PDIA3_HUMANPDIA3physical
29128334
DDX23_HUMANDDX23physical
29128334
RBM8A_HUMANRBM8Aphysical
29128334
SAP18_HUMANSAP18physical
29128334
NOP58_HUMANNOP58physical
29128334
H1X_HUMANH1FXphysical
29128334
FBRL_HUMANFBLphysical
29128334
NOP56_HUMANNOP56physical
29128334
ATPG_HUMANATP5C1physical
29128334
CHM4B_HUMANCHMP4Bphysical
29128334
SFXN1_HUMANSFXN1physical
29128334
ENPL_HUMANHSP90B1physical
29128334
1433E_HUMANYWHAEphysical
29128334
DKC1_HUMANDKC1physical
29128334
SERPH_HUMANSERPINH1physical
29128334
H10_HUMANH1F0physical
29128334
MIC19_HUMANCHCHD3physical
29128334
TAGL2_HUMANTAGLN2physical
29128334
RAB1B_HUMANRAB1Bphysical
29128334
MDHM_HUMANMDH2physical
29128334
LMNA_HUMANLMNAphysical
29128334
RAB5C_HUMANRAB5Cphysical
29128334
TCPB_HUMANCCT2physical
29128334
LMNB1_HUMANLMNB1physical
29128334
MIC60_HUMANIMMTphysical
29128334
CAAP1_HUMANCAAP1physical
29128334
NH2L1_HUMANNHP2L1physical
29128334
DESM_HUMANDESphysical
29128334
H2A1D_HUMANHIST1H2ADphysical
29128334
HCD2_HUMANHSD17B10physical
29128334
PDIA6_HUMANPDIA6physical
29128334
ATD3A_HUMANATAD3Aphysical
29128334
RA1L2_HUMANHNRNPA1L2physical
29128334
RAP1A_HUMANRAP1Aphysical
29128334
ANXA2_HUMANANXA2physical
29128334
RMXL2_HUMANRBMXL2physical
29128334
CDK1_HUMANCDK1physical
29128334
RM12_HUMANMRPL12physical
29128334
PGAM1_HUMANPGAM1physical
29128334
EMD_HUMANEMDphysical
29128334
STML2_HUMANSTOML2physical
29128334
PININ_HUMANPNNphysical
29128334
RAB1A_HUMANRAB1Aphysical
29128334
IF5A1_HUMANEIF5Aphysical
29128334
RAB7A_HUMANRAB7Aphysical
29128334
BAG2_HUMANBAG2physical
29128334
UBA1_HUMANUBA1physical
29128334
H2AY_HUMANH2AFYphysical
29128334
EF2_HUMANEEF2physical
29128334
HMGA2_HUMANHMGA2physical
29128334
ACOT9_HUMANACOT9physical
29128334
CHM2A_HUMANCHMP2Aphysical
29128334
UCHL1_HUMANUCHL1physical
29128334
RL30_HUMANRPL30physical
29128334
TOP2A_HUMANTOP2Aphysical
29128334
ODPB_HUMANPDHBphysical
29128334
MYH14_HUMANMYH14physical
29128334
PR38A_HUMANPRPF38Aphysical
29128334
SF3B6_HUMANSF3B6physical
29128334
NTPCR_HUMANNTPCRphysical
29128334
ETFB_HUMANETFBphysical
29128334
RHOA_HUMANRHOAphysical
29128334
RT11_HUMANMRPS11physical
29128334
MYL1_HUMANMYL1physical
29128334
RT17_HUMANMRPS17physical
29128334
RANG_HUMANRANBP1physical
29128334
PERI_HUMANPRPHphysical
29128334
HSPB1_HUMANHSPB1physical
29128334
GSTP1_HUMANGSTP1physical
29128334
EF1D_HUMANEEF1Dphysical
29128334
TPIS_HUMANTPI1physical
29128334
1A02_HUMANHLA-Aphysical
29128334
1A03_HUMANHLA-Aphysical
29128334
1A01_HUMANHLA-Aphysical
29128334
1A26_HUMANHLA-Aphysical
29128334
IMDH2_HUMANIMPDH2physical
29128334
VDAC2_HUMANVDAC2physical
29128334
ADT2_HUMANSLC25A5physical
29128334
QCR2_HUMANUQCRC2physical
29128334
PIMT_HUMANPCMT1physical
29128334
TAXB1_HUMANTAX1BP1physical
29128334
HP1B3_HUMANHP1BP3physical
29128334
MYO6_HUMANMYO6physical
29128334
1433T_HUMANYWHAQphysical
29128334
1433Z_HUMANYWHAZphysical
29128334
PAL4A_HUMANPPIAL4Bphysical
29128334
FSCN1_HUMANFSCN1physical
29128334
TIF1B_HUMANTRIM28physical
29128334
LDHB_HUMANLDHBphysical
29128334
PRP19_HUMANPRPF19physical
29128334
PRDX3_HUMANPRDX3physical
29128334
HNRH3_HUMANHNRNPH3physical
29128334
DREB_HUMANDBN1physical
29128334
DESP_HUMANDSPphysical
29128334
ADT3_HUMANSLC25A6physical
29128334
SND1_HUMANSND1physical
29128334
RPN1_HUMANRPN1physical
29128334
RNPS1_HUMANRNPS1physical
29128334
PRS6B_HUMANPSMC4physical
29128334
ATPO_HUMANATP5Ophysical
29128334
P5CR2_HUMANPYCR2physical
29128334
RAB5A_HUMANRAB5Aphysical
29128334
TCPH_HUMANCCT7physical
29128334
EF1G_HUMANEEF1Gphysical
29128334
MYO1D_HUMANMYO1Dphysical
29128334
PLEC_HUMANPLECphysical
29128334
AP3D1_HUMANAP3D1physical
29128334
TRAP1_HUMANTRAP1physical
29128334
CALX_HUMANCANXphysical
29128334
RABL6_HUMANRABL6physical
29128334
XRCC6_HUMANXRCC6physical
29128334
1433G_HUMANYWHAGphysical
29128334
AINX_HUMANINAphysical
29128334
IMB1_HUMANKPNB1physical
29128334
MYO1B_HUMANMYO1Bphysical
29128334
RT14_HUMANMRPS14physical
29128334
NP1L1_HUMANNAP1L1physical
29128334
MYH11_HUMANMYH11physical
29128334
AK17A_HUMANAKAP17Aphysical
29128334
TOM22_HUMANTOMM22physical
29128334
THIL_HUMANACAT1physical
29128334
CAZA2_HUMANCAPZA2physical
29128334
PDC6I_HUMANPDCD6IPphysical
29128334
MLEC_HUMANMLECphysical
29128334
OAT_HUMANOATphysical
29128334
RM02_HUMANMRPL2physical
29128334
TECR_HUMANTECRphysical
29128334
GELS_HUMANGSNphysical
29128334
COR1C_HUMANCORO1Cphysical
29128334
SFSWA_HUMANSFSWAPphysical
29128334
TR150_HUMANTHRAP3physical
29128334
SFXN3_HUMANSFXN3physical
29128334
RM49_HUMANMRPL49physical
29128334
CHRD1_HUMANCHORDC1physical
29128334
FAS_HUMANFASNphysical
29128334
LAP2A_HUMANTMPOphysical
29128334
LAP2B_HUMANTMPOphysical
29128334
COPZ1_HUMANCOPZ1physical
29128334
RBM4_HUMANRBM4physical
29128334
SAFB1_HUMANSAFBphysical
29128334
LUC7L_HUMANLUC7Lphysical
29128334
KINH_HUMANKIF5Bphysical
29128334
2AAA_HUMANPPP2R1Aphysical
29128334
TAP1_HUMANTAP1physical
29128334
DHX8_HUMANDHX8physical
29128334
RPN2_HUMANRPN2physical
29128334
PUR6_HUMANPAICSphysical
29128334
ODP2_HUMANDLATphysical
29128334
GAR1_HUMANGAR1physical
29128334
ENOB_HUMANENO3physical
29128334
THOC1_HUMANTHOC1physical
29128334
CWC15_HUMANCWC15physical
29128334
KNOP1_HUMANKNOP1physical
29128334
RRBP1_HUMANRRBP1physical
29128334
PRP6_HUMANPRPF6physical
29128334
TPM4_HUMANTPM4physical
29128334
SYEP_HUMANEPRSphysical
29128334
PLRG1_HUMANPLRG1physical
29128334
RAD50_HUMANRAD50physical
29128334
SMCA5_HUMANSMARCA5physical
29128334
ACINU_HUMANACIN1physical
29128334
GNL3_HUMANGNL3physical
29128334
PHRF1_HUMANPHRF1physical
29128334
ZN512_HUMANZNF512physical
29128334
TPM1_HUMANTPM1physical
29128334
RALYL_HUMANRALYLphysical
29128334
MAGD2_HUMANMAGED2physical
29128334
LBR_HUMANLBRphysical
29128334
SRP68_HUMANSRP68physical
29128334
FMR1_HUMANFMR1physical
29128334
EFTS_HUMANTSFMphysical
29128334
BRD7_HUMANBRD7physical
29128334
SYAM_HUMANAARS2physical
29128334
MY18A_HUMANMYO18Aphysical
29128334
NEUL_HUMANNLNphysical
29128334
H2AW_HUMANH2AFY2physical
29128334
SNF5_HUMANSMARCB1physical
29128334
ILF2_HUMANILF2physical
29128334
DDX21_HUMANDDX21physical
29128334
CING_HUMANCGNphysical
29128334
IF4G1_HUMANEIF4G1physical
29128334
IF4A3_HUMANEIF4A3physical
29128334
ATD3C_HUMANATAD3Cphysical
29128334
HSDL2_HUMANHSDL2physical
29128334
ACL6A_HUMANACTL6Aphysical
29128334
PRS4_HUMANPSMC1physical
29128334
HYOU1_HUMANHYOU1physical
29128334
AT2A1_HUMANATP2A1physical
29128334
SYDC_HUMANDARSphysical
29128334
PUR2_HUMANGARTphysical
29128334
E2AK2_HUMANEIF2AK2physical
29128334
DSG2_HUMANDSG2physical
29128334
NCOA5_HUMANNCOA5physical
29128334
RAGP1_HUMANRANGAP1physical
29128334
LMNB2_HUMANLMNB2physical
29128334
PABP1_HUMANPABPC1physical
29128334
PICAL_HUMANPICALMphysical
29128334
TTBK1_HUMANTTBK1physical
29128334
DYHC1_HUMANDYNC1H1physical
29128334
MTA2_HUMANMTA2physical
29128334
CMC2_HUMANSLC25A13physical
29128334
MTA1_HUMANMTA1physical
29128334
YTDC1_HUMANYTHDC1physical
29128334
TAF5_HUMANTAF5physical
29128334
NOC3L_HUMANNOC3Lphysical
29128334
MCM3_HUMANMCM3physical
29128334
TOP2B_HUMANTOP2Bphysical
29128334
NUP93_HUMANNUP93physical
29128334
CRNL1_HUMANCRNKL1physical
29128334
ZO1_HUMANTJP1physical
29128334
SYMC_HUMANMARSphysical
29128334
CCD80_HUMANCCDC80physical
29128334
BPTF_HUMANBPTFphysical
29128334
MDC1_HUMANMDC1physical
29128334
MYO1C_HUMANMYO1Cphysical
29128334
HPS5_HUMANHPS5physical
29128334
TNR6C_HUMANTNRC6Cphysical
29128334
H2A1B_HUMANHIST1H2AEphysical
29128334
HBA_HUMANHBA1physical
29128334
BOLA2_HUMANBOLA2physical
29128334

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ODO2_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-267, AND MASS SPECTROMETRY.

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