ODB2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ODB2_MOUSE
• UniProt AC: P53395
• Protein Name: Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
• Gene Name: Dbt
• Organism: Mus musculus (Mouse).
• 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: MAAARVLRTWSQNAVRLTCVRYFQTFNSARVLKPKCVCSVGYPLFKYSQPRHSLRTAAVLQGQVVQFKLSDIGEGIREVTIKEWYVKEGDTVSQFDSICEVQSDKASVTITSRYDGVIKRLYYNLDDIAYVGKPLIDIETEALKDSEEDVVETPAVSHDEHTHQEIKGQKTLATPAVRRLAMENNIKLSEVVGSGKDGRILKEDILSFLEKQTGAILPPSPKSEITPPPPQPKDRTFPTPIAKPPVFTGKDRTEPVTGFQKAMVKTMSAALKIPHFGYCDEIDLTQLVKLREELKPVALARGIKLSFMPFFLKAASLGLLQFPILNASVDENCQNITYKASHNIGIAMDTELGLIVPNVKNVQVRSVFEIAMELNRLQKLGSSGQLGTTDLTGGTFTLSNIGSIGGTYAKPVILPPEVAIGALGAIKALPRFDQKGDVYKAQIMNVSWSADHRVIDGATMSRFSNLWKSYLENPAFMLLDLK

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
68	Acetylation	QGQVVQFKLSDIGEG CCCEEEEEHHHHCCC	29.95	23576753
68	Succinylation	QGQVVQFKLSDIGEG CCCEEEEEHHHHCCC	29.95	24315375
82	Acetylation	GIREVTIKEWYVKEG CEEEEEEEEEEEECC	32.59	23864654
105	Lipoylation	ICEVQSDKASVTITS EEEEECCCCEEEEEE	48.05	-
105	N6-lipoyllysine	ICEVQSDKASVTITS EEEEECCCCEEEEEE	48.05	-
114	Phosphorylation	SVTITSRYDGVIKRL EEEEEECCCHHHEEE	19.47	29899451
119	Acetylation	SRYDGVIKRLYYNLD ECCCHHHEEEEEEHH	33.66	23576753
133	Succinylation	DDIAYVGKPLIDIET HHCEEECCCEEEECH	26.97	-
133	Succinylation	DDIAYVGKPLIDIET HHCEEECCCEEEECH	26.97	23806337
133	Acetylation	DDIAYVGKPLIDIET HHCEEECCCEEEECH	26.97	23806337
140	Phosphorylation	KPLIDIETEALKDSE CCEEEECHHHHCCCC	27.22	-
144	Acetylation	DIETEALKDSEEDVV EECHHHHCCCCCCCC	67.28	23954790
157	Phosphorylation	VVETPAVSHDEHTHQ CCCCCCCCCCCCCCH	27.59	25521595
162	Phosphorylation	AVSHDEHTHQEIKGQ CCCCCCCCCHHHCCC	24.17	23684622
170	Succinylation	HQEIKGQKTLATPAV CHHHCCCHHCCCHHH	54.92	24315375
170	Malonylation	HQEIKGQKTLATPAV CHHHCCCHHCCCHHH	54.92	26320211
189	Phosphorylation	MENNIKLSEVVGSGK HHCCCCHHHHCCCCC	24.28	-
196	Acetylation	SEVVGSGKDGRILKE HHHCCCCCCCCCCHH	59.72	23576753
196	Succinylation	SEVVGSGKDGRILKE HHHCCCCCCCCCCHH	59.72	-
196	Succinylation	SEVVGSGKDGRILKE HHHCCCCCCCCCCHH	59.72	23806337
202	Succinylation	GKDGRILKEDILSFL CCCCCCCHHHHHHHH	51.47	24315375
202	Acetylation	GKDGRILKEDILSFL CCCCCCCHHHHHHHH	51.47	23576753
211	Acetylation	DILSFLEKQTGAILP HHHHHHHHCCCCCCC	56.13	23806337
211	Succinylation	DILSFLEKQTGAILP HHHHHHHHCCCCCCC	56.13	23806337
213	Phosphorylation	LSFLEKQTGAILPPS HHHHHHCCCCCCCCC	39.38	22324799
220	Phosphorylation	TGAILPPSPKSEITP CCCCCCCCCCCCCCC	42.91	29472430
223	Phosphorylation	ILPPSPKSEITPPPP CCCCCCCCCCCCCCC	37.30	25521595
233	Acetylation	TPPPPQPKDRTFPTP CCCCCCCCCCCCCCC	55.37	23576753
233	Succinylation	TPPPPQPKDRTFPTP CCCCCCCCCCCCCCC	55.37	24315375
243	Succinylation	TFPTPIAKPPVFTGK CCCCCCCCCCCCCCC	51.04	24315375
243	Acetylation	TFPTPIAKPPVFTGK CCCCCCCCCCCCCCC	51.04	23576753
250	Succinylation	KPPVFTGKDRTEPVT CCCCCCCCCCCCCCC	40.76	24315375
250	Acetylation	KPPVFTGKDRTEPVT CCCCCCCCCCCCCCC	40.76	23576753
261	Succinylation	EPVTGFQKAMVKTMS CCCCHHHHHHHHHHH	35.87	-
261	Acetylation	EPVTGFQKAMVKTMS CCCCHHHHHHHHHHH	35.87	23864654
261	Succinylation	EPVTGFQKAMVKTMS CCCCHHHHHHHHHHH	35.87	23806337
265	Acetylation	GFQKAMVKTMSAALK HHHHHHHHHHHHHHC	25.98	23806337
265	Succinylation	GFQKAMVKTMSAALK HHHHHHHHHHHHHHC	25.98	23806337
272	Acetylation	KTMSAALKIPHFGYC HHHHHHHCCCCCCCC	49.84	30985801
279	S-nitrosylation	KIPHFGYCDEIDLTQ CCCCCCCCCCCCHHH	3.76	21278135
279	S-palmitoylation	KIPHFGYCDEIDLTQ CCCCCCCCCCCCHHH	3.76	28526873
279	S-nitrosocysteine	KIPHFGYCDEIDLTQ CCCCCCCCCCCCHHH	3.76	-
289	Succinylation	IDLTQLVKLREELKP CCHHHHHHHHHHHHH	50.88	23806337
289	Acetylation	IDLTQLVKLREELKP CCHHHHHHHHHHHHH	50.88	23576753
289	Succinylation	IDLTQLVKLREELKP CCHHHHHHHHHHHHH	50.88	-
295	Acetylation	VKLREELKPVALARG HHHHHHHHHHHHHHC	40.50	23576753
295	Succinylation	VKLREELKPVALARG HHHHHHHHHHHHHHC	40.50	23954790
304	Acetylation	VALARGIKLSFMPFF HHHHHCCCHHHHHHH	40.68	23576753
304	Succinylation	VALARGIKLSFMPFF HHHHHCCCHHHHHHH	40.68	24315375
333	S-palmitoylation	NASVDENCQNITYKA CCCCCCCCCCCCEEH	2.85	28526873
333	S-nitrosocysteine	NASVDENCQNITYKA CCCCCCCCCCCCEEH	2.85	-
333	S-nitrosylation	NASVDENCQNITYKA CCCCCCCCCCCCEEH	2.85	21278135
379	Succinylation	MELNRLQKLGSSGQL HHHHHHHHHCCCCCC	60.45	24315375
379	Acetylation	MELNRLQKLGSSGQL HHHHHHHHHCCCCCC	60.45	23576753
410	Acetylation	SIGGTYAKPVILPPE CCCCEECCCEECCHH	29.42	23806337
410	Succinylation	SIGGTYAKPVILPPE CCCCEECCCEECCHH	29.42	23806337
427	Acetylation	IGALGAIKALPRFDQ HHHHHHHHHCCCCCC	43.25	22826441
435	Acetylation	ALPRFDQKGDVYKAQ HCCCCCCCCCEEEEE	59.95	23576753
435	Succinylation	ALPRFDQKGDVYKAQ HCCCCCCCCCEEEEE	59.95	23806337
440	Succinylation	DQKGDVYKAQIMNVS CCCCCEEEEEEECEE	33.39	23806337
440	Acetylation	DQKGDVYKAQIMNVS CCCCCEEEEEEECEE	33.39	23576753
440	Succinylation	DQKGDVYKAQIMNVS CCCCCEEEEEEECEE	33.39	-
482	Acetylation	AFMLLDLK------- EEEEEECC-------	58.94	2389847

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ODB2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ODB2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ODB2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ODB2_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.