ODO2_MOUSE - dbPTM
ODO2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ODO2_MOUSE
UniProt AC Q9D2G2
Protein Name Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Gene Name Dlst
Organism Mus musculus (Mouse).
Sequence Length 454
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. 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 (By similarity)..
Protein Sequence MLSRSRCVSRAFSRSLSAFQKGNCPLGRRSLPGVSLCRGPGYPDNRKMVINSGSVFRVRFFQTTAVCKNDVITVQTPAFAESVTEGDVRWEKAVGDAVAEDEVVCEIETDKTSVQVPSPANGIIEALLVPDGGKVEGGTPLFTLRKTGAAPAKAKPAETPAPAHKAEPAAPAAPPPPAAPVLTQMPPVPSPSQPPSSKPVSAIKPTAAPPLAEAGAAKGLRSEHREKMNRMRQRIAQRLKEAQNTCAMLTTFNEVDMSNIQEMRARHKDAFLKKHNLKLGFMSAFVKASAFALQEQPVVNAVIDDATKEVVYRDYIDISVAVATPRGLVVPVIRNVETMNYADIERTINELGEKARKNELAIEDMDGGTFTISNGGVFGSLFGTPIINPPQSAILGMHAIFDRPVAVGGKVEVRPMMYVALTYDHRLIDGREAVTFLRKIKAAVEDPRVLLLDL
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
76PhosphorylationNDVITVQTPAFAESV
CCEEEECCHHHHCCC		16.5519060867
82PhosphorylationQTPAFAESVTEGDVR
CCHHHHCCCCCCCCC		30.8023684622
84PhosphorylationPAFAESVTEGDVRWE
HHHHCCCCCCCCCHH		43.4623984901
111N6-lipoyllysineVCEIETDKTSVQVPS
EEEEECCCCEEECCC		50.55-
111LipoylationVCEIETDKTSVQVPS
EEEEECCCCEEECCC		50.55-
112PhosphorylationCEIETDKTSVQVPSP
EEEECCCCEEECCCC		36.6225777480
113PhosphorylationEIETDKTSVQVPSPA
EEECCCCEEECCCCC		19.1225777480
118PhosphorylationKTSVQVPSPANGIIE
CCEEECCCCCCCEEE		37.4825777480
139PhosphorylationGGKVEGGTPLFTLRK
CCEECCCCCCEEEEE		27.8925777480
143PhosphorylationEGGTPLFTLRKTGAA
CCCCCCEEEEECCCC		33.0825777480
147PhosphorylationPLFTLRKTGAAPAKA
CCEEEEECCCCCCCC		26.1428059163
153AcetylationKTGAAPAKAKPAETP
ECCCCCCCCCCCCCC		56.7523576753
155SuccinylationGAAPAKAKPAETPAP
CCCCCCCCCCCCCCC		44.0123806337
155AcetylationGAAPAKAKPAETPAP
CCCCCCCCCCCCCCC		44.0123576753
159PhosphorylationAKAKPAETPAPAHKA
CCCCCCCCCCCCCCC		27.1923684622
183PhosphorylationPPAAPVLTQMPPVPS
CCCCCCCCCCCCCCC		24.0523140645
190PhosphorylationTQMPPVPSPSQPPSS
CCCCCCCCCCCCCCC		37.1023140645
192PhosphorylationMPPVPSPSQPPSSKP
CCCCCCCCCCCCCCC		60.7123140645
196PhosphorylationPSPSQPPSSKPVSAI
CCCCCCCCCCCCCCC		58.6423140645
197PhosphorylationSPSQPPSSKPVSAIK
CCCCCCCCCCCCCCC		46.9123140645
201PhosphorylationPPSSKPVSAIKPTAA
CCCCCCCCCCCCCCC		32.5723140645
206PhosphorylationPVSAIKPTAAPPLAE
CCCCCCCCCCCCHHH		30.3723140645
227AcetylationLRSEHREKMNRMRQR
CCHHHHHHHHHHHHH		41.246569221
246S-nitrosocysteineLKEAQNTCAMLTTFN
HHHHHHHHHHHEECC		2.48-
246S-nitrosylationLKEAQNTCAMLTTFN
HHHHHHHHHHHEECC		2.4821278135
268MalonylationQEMRARHKDAFLKKH
HHHHHHCHHHHHHHH		45.2426320211
268AcetylationQEMRARHKDAFLKKH
HHHHHHCHHHHHHHH		45.2423576753
268SuccinylationQEMRARHKDAFLKKH
HHHHHHCHHHHHHHH		45.2423954790
273AcetylationRHKDAFLKKHNLKLG
HCHHHHHHHHCCCHH		45.6023576753
273SuccinylationRHKDAFLKKHNLKLG
HCHHHHHHHHCCCHH		45.6024315375
274AcetylationHKDAFLKKHNLKLGF
CHHHHHHHHCCCHHH		39.6123576753
278AcetylationFLKKHNLKLGFMSAF
HHHHHCCCHHHHHHH		52.4623576753
278SuccinylationFLKKHNLKLGFMSAF
HHHHHCCCHHHHHHH		52.4624315375
283PhosphorylationNLKLGFMSAFVKASA
CCCHHHHHHHHHHHH		19.1222817900
308AcetylationAVIDDATKEVVYRDY
EEECCCCCCEEEECC		50.6723576753
308SuccinylationAVIDDATKEVVYRDY
EEECCCCCCEEEECC		50.6724315375
354SuccinylationTINELGEKARKNELA
HHHHHHHHHHHCCCE		52.2523806337
354AcetylationTINELGEKARKNELA
HHHHHHHHHHHCCCE		52.2523806337
418PhosphorylationVEVRPMMYVALTYDH
EEEECCEEEEEEECC		4.0228978645
422PhosphorylationPMMYVALTYDHRLID
CCEEEEEEECCCCCC		19.7128978645
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ODO2_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ODO2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ODO2_MOUSE

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Related Literatures of Post-Translational Modification

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