ODBB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ODBB_HUMAN
• UniProt AC: P21953
• Protein Name: 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
• Gene Name: BCKDHB
• Organism: Homo sapiens (Human).
• Sequence Length: 392
• 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)..
• Protein Sequence: MAVVAAAAGWLLRLRAAGAEGHWRRLPGAGLARGFLHPAATVEDAAQRRQVAHFTFQPDPEPREYGQTQKMNLFQSVTSALDNSLAKDPTAVIFGEDVAFGGVFRCTVGLRDKYGKDRVFNTPLCEQGIVGFGIGIAVTGATAIAEIQFADYIFPAFDQIVNEAAKYRYRSGDLFNCGSLTIRSPWGCVGHGALYHSQSPEAFFAHCPGIKVVIPRSPFQAKGLLLSCIEDKNPCIFFEPKILYRAAAEEVPIEPYNIPLSQAEVIQEGSDVTLVAWGTQVHVIREVASMAKEKLGVSCEVIDLRTIIPWDVDTICKSVIKTGRLLISHEAPLTGGFASEISSTVQEECFLNLEAPISRVCGYDTPFPHIFEPFYIPDKWKCYDALRKMINY

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
179	Phosphorylation	GDLFNCGSLTIRSPW CCCEECCCEEEECCC	25.25	28634120
195	Phosphorylation	CVGHGALYHSQSPEA ECCCCHHCCCCCCHH	10.01	-
232	Acetylation	LLSCIEDKNPCIFFE HHHHHCCCCCEEEEC	50.42	26051181
232	Ubiquitination	LLSCIEDKNPCIFFE HHHHHCCCCCEEEEC	50.42	-
241	Acetylation	PCIFFEPKILYRAAA CEEEECHHHHHHHHH	37.84	19608861
294	Ubiquitination	VASMAKEKLGVSCEV HHHHHHHHHCCCEEE	50.24	-
294	Malonylation	VASMAKEKLGVSCEV HHHHHHHHHCCCEEE	50.24	26320211
294	Acetylation	VASMAKEKLGVSCEV HHHHHHHHHCCCEEE	50.24	25953088
317	Ubiquitination	WDVDTICKSVIKTGR CCHHHHHHHHHHHCC	43.86	-
318	Phosphorylation	DVDTICKSVIKTGRL CHHHHHHHHHHHCCE	25.35	22817900
321	Ubiquitination	TICKSVIKTGRLLIS HHHHHHHHHCCEEEE	42.65	-
328	Phosphorylation	KTGRLLISHEAPLTG HHCCEEEEECCCCCC	18.42	22817900
342	Phosphorylation	GGFASEISSTVQEEC CCCHHHHCHHHCHHH	18.86	22468782
363	Phosphorylation	PISRVCGYDTPFPHI CHHHHCCCCCCCCCC	16.12	-
383	Phosphorylation	IPDKWKCYDALRKMI CCCHHHHHHHHHHHH	10.67	22817900
392	Phosphorylation	ALRKMINY------- HHHHHHCC-------	14.70	-

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
318	S	Phosphorylation	Kinase	BCKDK	Q00972	PSP

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ODB2_HUMAN	DBT	physical	28514442
ODBA_HUMAN	BCKDHA	physical	28514442
SYLM_HUMAN	LARS2	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 248600: Maple syrup urine disease 1B (MSUD1B)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241, AND MASS SPECTROMETRY.
PubMed: 19608861