ODPB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ODPB_MOUSE
• UniProt AC: Q9D051
• Protein Name: Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
• Gene Name: Pdhb
• Organism: Mus musculus (Mouse).
• Sequence Length: 359
• 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: MAVVAGLVRGPLRQASGLLKRRFHRSAPAAVQLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVMLENELMYGVAFELPAEAQSKDFLIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKVLEDNSVPQVKDIIFAVKKTLNI

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
52	Acetylation	EELERDEKVFLLGEE HHHHHHCEEEECCHH	42.44	23954790
52	Succinylation	EELERDEKVFLLGEE HHHHHHCEEEECCHH	42.44	26388266
63	Phosphorylation	LGEEVAQYDGAYKVS CCHHHHHCCCCCEEC	13.45	25195567
67	Phosphorylation	VAQYDGAYKVSRGLW HHHCCCCCEECCCHH	19.90	22817900
68	Acetylation	AQYDGAYKVSRGLWK HHCCCCCEECCCHHH	32.95	23236377
184	Ubiquitination	PWNSEDAKGLIKSAI CCCCHHHHHHHHHHH	67.58	22790023
227	Ubiquitination	DFLIPIGKAKIERQG CEEEEECCCEEEECC	47.42	27667366
227	Succinylation	DFLIPIGKAKIERQG CEEEEECCCEEEECC	47.42	23954790
258	Acetylation	EAAAVLSKEGIECEV HHHHHHCCCCCEEEE	56.66	23576753
263	S-nitrosocysteine	LSKEGIECEVINLRT HCCCCCEEEEEECCE	4.84	-
263	S-palmitoylation	LSKEGIECEVINLRT HCCCCCEEEEEECCE	4.84	28526873
263	S-nitrosylation	LSKEGIECEVINLRT HCCCCCEEEEEECCE	4.84	21278135
263	Glutathionylation	LSKEGIECEVINLRT HCCCCCEEEEEECCE	4.84	24333276
306	S-nitrosylation	FGVGAEICARIMEGP CCCCHHHHHHHHHCC	1.24	21278135
306	S-nitrosocysteine	FGVGAEICARIMEGP CCCCHHHHHHHHHCC	1.24	-
336	Ubiquitination	DVPMPYAKVLEDNSV CCCCCCHHHCCCCCC	41.32	-
336	Acetylation	DVPMPYAKVLEDNSV CCCCCCHHHCCCCCC	41.32	23864654
336	Succinylation	DVPMPYAKVLEDNSV CCCCCCHHHCCCCCC	41.32	23954790
347	Acetylation	DNSVPQVKDIIFAVK CCCCCCHHHHHHHHH	37.65	23864654
347	Succinylation	DNSVPQVKDIIFAVK CCCCCCHHHHHHHHH	37.65	26388266
354	Succinylation	KDIIFAVKKTLNI-- HHHHHHHHHHCCC--	36.29	23806337
354	Acetylation	KDIIFAVKKTLNI-- HHHHHHHHHHCCC--	36.29	23576753
355	Succinylation	DIIFAVKKTLNI--- HHHHHHHHHCCC---	52.20	26388266

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ODPB_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 ODPB_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ODPB_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, AND MASSSPECTROMETRY.
PubMed: 18034455