SCOT1_HUMAN - dbPTM
SCOT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCOT1_HUMAN
UniProt AC P55809
Protein Name Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
Gene Name OXCT1
Organism Homo sapiens (Human).
Sequence Length 520
Subcellular Localization Mitochondrion matrix.
Protein Description Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate..
Protein Sequence MAALKLLSSGLRLCASARGSGATWYKGCVCSFSTSAHRHTKFYTDPVEAVKDIPDGATVLVGGFGLCGIPENLIDALLKTGVKGLTAVSNNAGVDNFGLGLLLRSKQIKRMVSSYVGENAEFERQYLSGELEVELTPQGTLAERIRAGGAGVPAFYTPTGYGTLVQEGGSPIKYNKDGSVAIASKPREVREFNGQHFILEEAITGDFALVKAWKADRAGNVIFRKSARNFNLPMCKAAETTVVEVEEIVDIGAFAPEDIHIPQIYVHRLIKGEKYEKRIERLSIRKEGDGEAKSAKPGDDVRERIIKRAALEFEDGMYANLGIGIPLLASNFISPNITVHLQSENGVLGLGPYPRQHEADADLINAGKETVTILPGASFFSSDESFAMIRGGHVDLTMLGAMQVSKYGDLANWMIPGKMVKGMGGAMDLVSSAKTKVVVTMEHSAKGNAHKIMEKCTLPLTGKQCVNRIITEKAVFDVDKKKGLTLIELWEGLTVDDVQKSTGCDFAVSPKLMPMQQIAN
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
24UbiquitinationARGSGATWYKGCVCS
HCCCCCCEECCEEEE		7.72-
24AcetylationARGSGATWYKGCVCS
HCCCCCCEECCEEEE		7.72-
43NitrationAHRHTKFYTDPVEAV
CCCCCCEECCHHHHH		16.28-
58AcetylationKDIPDGATVLVGGFG
CCCCCCCEEEECCCC		21.65-
86PhosphorylationKTGVKGLTAVSNNAG
HHCCCHHHCCCCCCC		33.41-
114PhosphorylationQIKRMVSSYVGENAE
HHHHHHHHHCCCCHH		16.66-
115PhosphorylationIKRMVSSYVGENAEF
HHHHHHHHCCCCHHH		12.64-
115NitrationIKRMVSSYVGENAEF
HHHHHHHHCCCCHHH		12.64-
126PhosphorylationNAEFERQYLSGELEV
CHHHHHHHHCCEEEE		14.73-
146MethylationGTLAERIRAGGAGVP
CCHHHHHHHCCCCCC		33.14115486113
156PhosphorylationGAGVPAFYTPTGYGT
CCCCCEEECCCCCCC		17.5727080861
157PhosphorylationAGVPAFYTPTGYGTL
CCCCEEECCCCCCCE		14.1227080861
159PhosphorylationVPAFYTPTGYGTLVQ
CCEEECCCCCCCEEE		34.9226074081
161PhosphorylationAFYTPTGYGTLVQEG
EEECCCCCCCEEEEC		14.9327080861
163PhosphorylationYTPTGYGTLVQEGGS
ECCCCCCCEEEECCC		18.4427050516
170PhosphorylationTLVQEGGSPIKYNKD
CEEEECCCCCEECCC		34.0225159151
173UbiquitinationQEGGSPIKYNKDGSV
EECCCCCEECCCCCE		46.2719608861
173AcetylationQEGGSPIKYNKDGSV
EECCCCCEECCCCCE		46.2719608861
174PhosphorylationEGGSPIKYNKDGSVA
ECCCCCEECCCCCEE		28.3221712546
176MalonylationGSPIKYNKDGSVAIA
CCCCEECCCCCEEEE		61.4526320211
176SuccinylationGSPIKYNKDGSVAIA
CCCCEECCCCCEEEE		61.4527452117
176AcetylationGSPIKYNKDGSVAIA
CCCCEECCCCCEEEE		61.4527452117
176UbiquitinationGSPIKYNKDGSVAIA
CCCCEECCCCCEEEE		61.45-
179PhosphorylationIKYNKDGSVAIASKP
CEECCCCCEEEECCC		20.6423403867
184PhosphorylationDGSVAIASKPREVRE
CCCEEEECCCCEEEE		36.7621406692
185SuccinylationGSVAIASKPREVREF
CCEEEECCCCEEEEE		38.7927452117
185MalonylationGSVAIASKPREVREF
CCEEEECCCCEEEEE		38.7932601280
185AcetylationGSVAIASKPREVREF
CCEEEECCCCEEEEE		38.7923749302
185SuccinylationGSVAIASKPREVREF
CCEEEECCCCEEEEE		38.79-
185UbiquitinationGSVAIASKPREVREF
CCEEEECCCCEEEEE		38.79-
225AcetylationAGNVIFRKSARNFNL
CCCEEEEECCCCCCC		37.4030585259
283PhosphorylationEKRIERLSIRKEGDG
HHHHHHHCCEECCCC		26.9429449344
294PhosphorylationEGDGEAKSAKPGDDV
CCCCCCCCCCCCCHH		48.88-
296AcetylationDGEAKSAKPGDDVRE
CCCCCCCCCCCHHHH		57.5323236377
368AcetylationADLINAGKETVTILP
HHHHHCCCCEEEECC		48.0425038526
381PhosphorylationLPGASFFSSDESFAM
CCCCCCCCCCCCEEE		34.56-
406AcetylationLGAMQVSKYGDLANW
ECCEEEHHHCCHHCC		55.1625038526
407PhosphorylationGAMQVSKYGDLANWM
CCEEEHHHCCHHCCC		14.36-
418AcetylationANWMIPGKMVKGMGG
HCCCCCCCCCCCCCH		34.8623954790
418MalonylationANWMIPGKMVKGMGG
HCCCCCCCCCCCCCH		34.8626320211
418SuccinylationANWMIPGKMVKGMGG
HCCCCCCCCCCCCCH		34.8627452117
418SuccinylationANWMIPGKMVKGMGG
HCCCCCCCCCCCCCH		34.86-
421SuccinylationMIPGKMVKGMGGAMD
CCCCCCCCCCCHHHH		39.4227452117
421MalonylationMIPGKMVKGMGGAMD
CCCCCCCCCCCHHHH		39.4226320211
421AcetylationMIPGKMVKGMGGAMD
CCCCCCCCCCCHHHH		39.4223954790
421SuccinylationMIPGKMVKGMGGAMD
CCCCCCCCCCCHHHH		39.42-
4212-HydroxyisobutyrylationMIPGKMVKGMGGAMD
CCCCCCCCCCCHHHH		39.42-
421UbiquitinationMIPGKMVKGMGGAMD
CCCCCCCCCCCHHHH		39.42-
431PhosphorylationGGAMDLVSSAKTKVV
CHHHHHHHHCCCEEE		31.69-
432PhosphorylationGAMDLVSSAKTKVVV
HHHHHHHHCCCEEEE		26.72-
4342-HydroxyisobutyrylationMDLVSSAKTKVVVTM
HHHHHHCCCEEEEEE		51.32-
435PhosphorylationDLVSSAKTKVVVTME
HHHHHCCCEEEEEEC		28.87-
4362-HydroxyisobutyrylationLVSSAKTKVVVTMEH
HHHHCCCEEEEEECC		32.12-
4462-HydroxyisobutyrylationVTMEHSAKGNAHKIM
EEECCCCCCCHHHHH		56.57-
446MalonylationVTMEHSAKGNAHKIM
EEECCCCCCCHHHHH		56.5726320211
446UbiquitinationVTMEHSAKGNAHKIM
EEECCCCCCCHHHHH		56.57-
446AcetylationVTMEHSAKGNAHKIM
EEECCCCCCCHHHHH		56.5725953088
446SuccinylationVTMEHSAKGNAHKIM
EEECCCCCCCHHHHH		56.5727452117
4512-HydroxyisobutyrylationSAKGNAHKIMEKCTL
CCCCCHHHHHHHCCC		41.14-
451SuccinylationSAKGNAHKIMEKCTL
CCCCCHHHHHHHCCC		41.1427452117
455SuccinylationNAHKIMEKCTLPLTG
CHHHHHHHCCCCCCC		18.35-
455AcetylationNAHKIMEKCTLPLTG
CHHHHHHHCCCCCCC		18.3523954790
455SuccinylationNAHKIMEKCTLPLTG
CHHHHHHHCCCCCCC		18.35-
455MalonylationNAHKIMEKCTLPLTG
CHHHHHHHCCCCCCC		18.3526320211
457PhosphorylationHKIMEKCTLPLTGKQ
HHHHHHCCCCCCCHH		42.3429496963
461PhosphorylationEKCTLPLTGKQCVNR
HHCCCCCCCHHHHHH		40.1529496963
463UbiquitinationCTLPLTGKQCVNRII
CCCCCCCHHHHHHHH		34.98-
463MalonylationCTLPLTGKQCVNRII
CCCCCCCHHHHHHHH		34.9826320211
4632-HydroxyisobutyrylationCTLPLTGKQCVNRII
CCCCCCCHHHHHHHH		34.98-
463SuccinylationCTLPLTGKQCVNRII
CCCCCCCHHHHHHHH		34.9827452117
463AcetylationCTLPLTGKQCVNRII
CCCCCCCHHHHHHHH		34.9825953088
473SuccinylationVNRIITEKAVFDVDK
HHHHHHHCCEEECCC		41.0027452117
4732-HydroxyisobutyrylationVNRIITEKAVFDVDK
HHHHHHHCCEEECCC		41.00-
473MalonylationVNRIITEKAVFDVDK
HHHHHHHCCEEECCC		41.0026320211
473AcetylationVNRIITEKAVFDVDK
HHHHHHHCCEEECCC		41.0025953088
473UbiquitinationVNRIITEKAVFDVDK
HHHHHHHCCEEECCC		41.00-
4802-HydroxyisobutyrylationKAVFDVDKKKGLTLI
CCEEECCCCCCCEEE		57.12-
480AcetylationKAVFDVDKKKGLTLI
CCEEECCCCCCCEEE		57.1225953088
480UbiquitinationKAVFDVDKKKGLTLI
CCEEECCCCCCCEEE		57.12-
481MalonylationAVFDVDKKKGLTLIE
CEEECCCCCCCEEEE		47.8426320211
481AcetylationAVFDVDKKKGLTLIE
CEEECCCCCCCEEEE		47.8425953088
482AcetylationVFDVDKKKGLTLIEL
EEECCCCCCCEEEEE		65.967675267
500AcetylationLTVDDVQKSTGCDFA
CCHHHHHHHCCCCCE		50.2425038526
501PhosphorylationTVDDVQKSTGCDFAV
CHHHHHHHCCCCCEE		16.9721712546
502PhosphorylationVDDVQKSTGCDFAVS
HHHHHHHCCCCCEEC		49.1921712546
509PhosphorylationTGCDFAVSPKLMPMQ
CCCCCEECCCCCCHH		16.9428985074
511AcetylationCDFAVSPKLMPMQQI
CCCEECCCCCCHHHH		50.3325953088
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 SCOT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCOT1_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 SCOT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TMEM9_HUMANTMEM9physical
22939629
SVIL_HUMANSVILphysical
22939629
UBXN7_HUMANUBXN7physical
22939629
VMA21_HUMANVMA21physical
22939629
TCOF_HUMANTCOF1physical
22939629
TOIP1_HUMANTOR1AIP1physical
22939629
SUCB1_HUMANSUCLA2physical
22939629
UPAR_HUMANPLAURphysical
22939629
SDHF2_HUMANSDHAF2physical
22939629
SUCA_HUMANSUCLG1physical
22939629
SFR15_HUMANSCAF4physical
22939629
SEP11_HUMANSEPT11physical
22939629
UCRI_HUMANUQCRFS1physical
22939629
TM189_HUMANTMEM189physical
22939629
VAPB_HUMANVAPBphysical
22939629
TIM9_HUMANTIMM9physical
22939629
TM177_HUMANTMEM177physical
22939629
SRC8_HUMANCTTNphysical
22939629
SPHM_HUMANSGSHphysical
22939629
PURA2_HUMANADSSphysical
22863883
CH60_HUMANHSPD1physical
22863883
IDHC_HUMANIDH1physical
22863883
MTPN_HUMANMTPNphysical
22863883
NDKA_HUMANNME1physical
22863883
PTMS_HUMANPTMSphysical
22863883
PTN11_HUMANPTPN11physical
22863883
RBBP7_HUMANRBBP7physical
22863883
SMAP_HUMANC11orf58physical
22863883
THOP1_HUMANTHOP1physical
22863883
WDR1_HUMANWDR1physical
22863883
AHNK_HUMANAHNAKphysical
26344197
FUMH_HUMANFHphysical
26344197
HINT1_HUMANHINT1physical
26344197
HSPB1_HUMANHSPB1physical
26344197
LYPA1_HUMANLYPLA1physical
26344197
MDHC_HUMANMDH1physical
26344197
RAE1L_HUMANRAE1physical
26344197
SODC_HUMANSOD1physical
26344197
TALDO_HUMANTALDO1physical
26344197
TPIS_HUMANTPI1physical
26344197
SCOT1_HUMANOXCT1physical
27499296
SCOT2_HUMANOXCT2physical
27499296
C1QBP_HUMANC1QBPphysical
27499296
SCOT2_HUMANOXCT2physical
28514442
EPS15_HUMANEPS15physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
3-oxoacid CoA transferase deficiency (SCOTD)Succinyl-CoA
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00139Succinic acid
Regulatory Network of SCOT1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory