dbPTM

BCKD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BCKD_HUMAN
UniProt AC	O14874
Protein Name	[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial
Gene Name	BCKDK
Organism	Homo sapiens (Human).
Sequence Length	412
Subcellular Localization	Mitochondrion matrix. Mitochondrion .
Protein Description	Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex..
Protein Sequence	MILASVLRSGPGGGLPLRPLLGPALALRARSTSATDTHHVEMARERSKTVTSFYNQSAIDAAAEKPSVRLTPTMMLYAGRSQDGSHLLKSARYLQQELPVRIAHRIKGFRCLPFIIGCNPTILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHIEDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARRLCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVITIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRISPLFGHLDMHSGAQSGPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
31	Phosphorylation	ALALRARSTSATDTH HHHHHCCCCCCCCCH	26.23	22167270
32	Phosphorylation	LALRARSTSATDTHH HHHHCCCCCCCCCHH	19.48	22167270
33	Phosphorylation	ALRARSTSATDTHHV HHHCCCCCCCCCHHH	30.34	22167270
35	Phosphorylation	RARSTSATDTHHVEM HCCCCCCCCCHHHHH	40.99	22167270
37	Phosphorylation	RSTSATDTHHVEMAR CCCCCCCCHHHHHHH	14.99	23927012
47	Phosphorylation	VEMARERSKTVTSFY HHHHHHHHCCHHHHC	28.11	-
48	Ubiquitination	EMARERSKTVTSFYN HHHHHHHCCHHHHCC	53.92	21890473
48	Ubiquitination	EMARERSKTVTSFYN HHHHHHHCCHHHHCC	53.92	21890473
48	Ubiquitination	EMARERSKTVTSFYN HHHHHHHCCHHHHCC	53.92	21890473
52	Phosphorylation	ERSKTVTSFYNQSAI HHHCCHHHHCCHHHH	22.77	19060867
57	Phosphorylation	VTSFYNQSAIDAAAE HHHHCCHHHHHHHHC	24.45	28857561
71	Phosphorylation	EKPSVRLTPTMMLYA CCCCCEECCCEEEEC	13.22	29978859
73	Phosphorylation	PSVRLTPTMMLYAGR CCCEECCCEEEECCC	15.24	29978859
77	Phosphorylation	LTPTMMLYAGRSQDG ECCCEEEECCCCCCH	6.79	25884760
81	Phosphorylation	MMLYAGRSQDGSHLL EEEECCCCCCHHHHH	31.53	28857561
85	Phosphorylation	AGRSQDGSHLLKSAR CCCCCCHHHHHHHHH	21.17	29978859
89	Acetylation	QDGSHLLKSARYLQQ CCHHHHHHHHHHHHH	48.72	25953088
89	Methylation	QDGSHLLKSARYLQQ CCHHHHHHHHHHHHH	48.72	-
90	Phosphorylation	DGSHLLKSARYLQQE CHHHHHHHHHHHHHH	20.25	29978859
93	Phosphorylation	HLLKSARYLQQELPV HHHHHHHHHHHHCCH	14.47	28152594
184	Acetylation	RKHIEDEKLVRYFLD HHHCCHHHHHHHHHH	65.68	19608861
184	Succinylation	RKHIEDEKLVRYFLD HHHCCHHHHHHHHHH	65.68	23954790
192	Acetylation	LVRYFLDKTLTSRLG HHHHHHHHHHHHHHH	47.80	19608861
192	Acetylation	LVRYFLDKTLTSRLG HHHHHHHHHHHHHHH	47.80	-
192	2-Hydroxyisobutyrylation	LVRYFLDKTLTSRLG HHHHHHHHHHHHHHH	47.80	-
226	Phosphorylation	GIICTRLSPKKIIEK EEEECCCCHHHHHHH	31.23	26091039
233	Acetylation	SPKKIIEKWVDFARR CHHHHHHHHHHHHHH	41.95	19608861
245	Acetylation	ARRLCEHKYGNAPRV HHHHHHHHCCCCCEE	32.34	19608861
246	Phosphorylation	RRLCEHKYGNAPRVR HHHHHHHCCCCCEEE	19.95	-
284	Phosphorylation	LKNAMRATMESHLDT HHHHHHHHHHHHCCC	15.88	22210691
287	Phosphorylation	AMRATMESHLDTPYN HHHHHHHHHCCCCCC	20.66	22210691
301	Phosphorylation	NVPDVVITIANNDVD CCCCEEEEEECCCCE	11.48	22210691
331	Phosphorylation	DLDRVMDYHFTTAEA CHHHHHHEEEECHHC	4.82	23312004
334	Phosphorylation	RVMDYHFTTAEASTQ HHHHEEEECHHCCCC	16.28	28857561
335	Phosphorylation	VMDYHFTTAEASTQD HHHEEEECHHCCCCC	22.89	28857561
339	Phosphorylation	HFTTAEASTQDPRIS EEECHHCCCCCCCCC	20.36	28857561
340	Phosphorylation	FTTAEASTQDPRISP EECHHCCCCCCCCCH	44.00	28857561
356	Phosphorylation	FGHLDMHSGAQSGPM CCCCCCCCCCCCCCC	29.23	24719451
360	Phosphorylation	DMHSGAQSGPMHGFG CCCCCCCCCCCCCCC	44.31	24719451

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
246	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BCKD_HUMAN !!

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 BCKD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAB39_HUMAN	CAB39	physical	17353931
CB39L_HUMAN	CAB39L	physical	17353931
ODBA_HUMAN	BCKDHA	physical	17353931
RN219_HUMAN	RNF219	physical	17353931
FA98B_HUMAN	FAM98B	physical	17353931
RTCA_HUMAN	RTCA	physical	17353931
A4_HUMAN	APP	physical	21832049
STAT3_HUMAN	STAT3	physical	21988832
EPS8_HUMAN	EPS8	physical	21988832
LSM8_HUMAN	LSM8	physical	21988832
CETN3_HUMAN	CETN3	physical	26186194
WDTC1_HUMAN	WDTC1	physical	26186194
CETN2_HUMAN	CETN2	physical	26186194
LG3BP_HUMAN	LGALS3BP	physical	28514442
CETN3_HUMAN	CETN3	physical	28514442
CETN2_HUMAN	CETN2	physical	28514442
WDTC1_HUMAN	WDTC1	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614923	Branched-chain ketoacid dehydrogenase kinase deficiency (BCKDKD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of BCKD_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-184; LYS-192; LYS-233 ANDLYS-245, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND MASSSPECTROMETRY.	18220336 [Abstract]