ODP2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ODP2_MOUSE
• UniProt AC: Q8BMF4
• Protein Name: Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
• Gene Name: Dlat
• Organism: Mus musculus (Mouse).
• Sequence Length: 642
• 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: MWRVCARRARSAVPRDGFRARWAALKEGPGAPCGSPRIGPAAVRCGSGIPRYGVRSLCGWSSGSGTVPRNRLLRQLLGSPSRRSYSLPPHQKVPLPSLSPTMQAGTIARWEKKEGEKISEGDLIAEVETDKATVGFESLEECYMAKILVPEGTRDVPVGSIICITVEKPQDIEAFKNYTLDLAAAAAPQAAPAAAPAPAAAPAAPSASAPGSSYPTHMQIVLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGAPLCIIVEKQEDIAAFADYRPTEVTSLKPQAAPPAPPPVAAVPPTPQPVAPTPSAAPAGPKGRVFVSPLAKKLAAEKGIDLTQVKGTGPEGRIIKKDIDSFVPSKAAPAAAAAMAPPGPRVAPAPAGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSVDVNMGEVLLVRKELNKMLEGKGKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGLETIASDVVSLASKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLIPADNEKGFDVASVMSVTLSCDHRVVDGAVGAQWLAEFKKYLEKPITMLL

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
35	Phosphorylation	GPGAPCGSPRIGPAA CCCCCCCCCCCCCCH	20.09	20495213
52	Phosphorylation	CGSGIPRYGVRSLCG CCCCCCCCCHHHHCC	18.02	-
56	Phosphorylation	IPRYGVRSLCGWSSG CCCCCHHHHCCCCCC	26.13	-
66	Phosphorylation	GWSSGSGTVPRNRLL CCCCCCCCCCHHHHH	29.09	-
79	Phosphorylation	LLRQLLGSPSRRSYS HHHHHHCCCCCCCCC	21.48	28066266
81	Phosphorylation	RQLLGSPSRRSYSLP HHHHCCCCCCCCCCC	41.86	28066266
97	Phosphorylation	HQKVPLPSLSPTMQA CCCCCCCCCCCCCCC	49.51	26745281
99	Phosphorylation	KVPLPSLSPTMQAGT CCCCCCCCCCCCCCC	23.74	26745281
101	Phosphorylation	PLPSLSPTMQAGTIA CCCCCCCCCCCCCCE	20.66	26745281
106	Phosphorylation	SPTMQAGTIARWEKK CCCCCCCCCEEEEHH	17.93	26745281
131	Lipoylation	IAEVETDKATVGFES EEEEECCCCEECCCC	54.07	-
131	N6-lipoyllysine	IAEVETDKATVGFES EEEEECCCCEECCCC	54.07	-
163	S-nitrosocysteine	VPVGSIICITVEKPQ CCCCEEEEEEECCCC	1.71	-
163	S-nitrosylation	VPVGSIICITVEKPQ CCCCEEEEEEECCCC	1.71	21278135
258	N6-lipoyllysine	LAEIETDKATIGFEV EEEEECCCCEEEEEE	55.65	-
258	Lipoylation	LAEIETDKATIGFEV EEEEECCCCEEEEEE	55.65	-
290	S-nitrosylation	VPLGAPLCIIVEKQE CCCCCCEEEEEECCC	1.62	22588120
290	S-nitrosocysteine	VPLGAPLCIIVEKQE CCCCCCEEEEEECCC	1.62	-
311	Phosphorylation	DYRPTEVTSLKPQAA CCCCCCCCCCCCCCC	23.31	23140645
312	Phosphorylation	YRPTEVTSLKPQAAP CCCCCCCCCCCCCCC	39.30	23140645
331	Phosphorylation	PVAAVPPTPQPVAPT CCCCCCCCCCCCCCC	28.61	23140645
357	Methylation	VFVSPLAKKLAAEKG EEECHHHHHHHHHHC	56.88	-
358	Succinylation	FVSPLAKKLAAEKGI EECHHHHHHHHHHCC	37.44	26388266
358	Acetylation	FVSPLAKKLAAEKGI EECHHHHHHHHHHCC	37.44	23201123
358	Methylation	FVSPLAKKLAAEKGI EECHHHHHHHHHHCC	37.44	-
363	Acetylation	AKKLAAEKGIDLTQV HHHHHHHHCCCCEEE	57.34	23236377
363	Methylation	AKKLAAEKGIDLTQV HHHHHHHHCCCCEEE	57.34	-
371	Succinylation	GIDLTQVKGTGPEGR CCCCEEECCCCCCCC	40.72	23806337
371	Acetylation	GIDLTQVKGTGPEGR CCCCEEECCCCCCCC	40.72	23806337
382	Acetylation	PEGRIIKKDIDSFVP CCCCEEECCHHHCCC	49.89	24062335
391	Succinylation	IDSFVPSKAAPAAAA HHHCCCCCCCHHHHH	42.36	26388266
416	Phosphorylation	PAPAGVFTDIPISNI CCCCCCCCCCCHHHH	30.52	26026062
421	Phosphorylation	VFTDIPISNIRRVIA CCCCCCHHHHHHHHH	22.35	25195567
461	Succinylation	LVRKELNKMLEGKGK EEHHHHHHHHCCCCC	58.44	23806337
461	Acetylation	LVRKELNKMLEGKGK EEHHHHHHHHCCCCC	58.44	23864654
468	Acetylation	KMLEGKGKISVNDFI HHHCCCCCEEHHHHH	34.98	23806337
468	Succinylation	KMLEGKGKISVNDFI HHHCCCCCEEHHHHH	34.98	23806337
468	Succinylation	KMLEGKGKISVNDFI HHHCCCCCEEHHHHH	34.98	-
468	Ubiquitination	KMLEGKGKISVNDFI HHHCCCCCEEHHHHH	34.98	-
470	Phosphorylation	LEGKGKISVNDFIIK HCCCCCEEHHHHHHH	20.53	27742792
483	S-nitrosocysteine	IKASALACLKVPEAN HHHHHHHHHCCCCCC	3.82	-
483	S-nitrosylation	IKASALACLKVPEAN HHHHHHHHHCCCCCC	3.82	21278135
531	Phosphorylation	AHIKGLETIASDVVS HHHCCHHHHHHHHHH	27.21	29899451
534	Phosphorylation	KGLETIASDVVSLAS CCHHHHHHHHHHHHH	27.39	29899451
538	Phosphorylation	TIASDVVSLASKARE HHHHHHHHHHHHHHC	20.33	29899451
542	Succinylation	DVVSLASKAREGKLQ HHHHHHHHHHCCCCC	45.94	-
542	Acetylation	DVVSLASKAREGKLQ HHHHHHHHHHCCCCC	45.94	23806337
542	Succinylation	DVVSLASKAREGKLQ HHHHHHHHHHCCCCC	45.94	23806337
581	S-nitrosylation	IINPPQACILAIGAS ECCCCCCEEEEEECC	1.89	21278135
581	S-nitrosocysteine	IINPPQACILAIGAS ECCCCCCEEEEEECC	1.89	-
613	S-nitrosylation	VMSVTLSCDHRVVDG EEEEEEECCCCEECC	6.01	21278135
613	S-nitrosocysteine	VMSVTLSCDHRVVDG EEEEEEECCCCEECC	6.01	-
631	Acetylation	AQWLAEFKKYLEKPI HHHHHHHHHHHCCCC	31.82	23954790
632	Acetylation	QWLAEFKKYLEKPIT HHHHHHHHHHCCCCE	61.46	24062335
636	Acetylation	EFKKYLEKPITMLL- HHHHHHCCCCEECC-	38.84	22826441
636	Ubiquitination	EFKKYLEKPITMLL- HHHHHHCCCCEECC-	38.84	22790023

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

Oops, there are no upstream regulatory protein records of ODP2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
131	K	Lipoylation	Delipoylated at Lys-131 and Lys-258 by SIRT4, delipoylation decreases the PHD complex activity.	-
258	K	Lipoylation	Delipoylated at Lys-131 and Lys-258 by SIRT4, delipoylation decreases the PHD complex activity.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ODP2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ODP2_MOUSE !!

Drug and Disease Associations

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