dbPTM

ODPA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ODPA_HUMAN
UniProt AC	P08559
Protein Name	Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
Gene Name	PDHA1
Organism	Homo sapiens (Human).
Sequence Length	390
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	MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVRGANQWIKFKSVS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	O-linked_Glycosylation	AAVSRVLSGASQKPA HHHHHHHHCCCCCCH	29.47	22121020
18	Acetylation	VLSGASQKPASRVLV HHHCCCCCCHHEEEE	39.80	63650805
18	Ubiquitination	VLSGASQKPASRVLV HHHCCCCCCHHEEEE	39.80	-
39	Acetylation	NDATFEIKKCDLHRL CCCEEEEEECCHHHC	39.90	2413493
39	Ubiquitination	NDATFEIKKCDLHRL CCCEEEEEECCHHHC	39.90	-
63	Acetylation	LTREDGLKYYRMMQT EECHHHHHHHHHHHH	45.85	25825284
63	Succinylation	LTREDGLKYYRMMQT EECHHHHHHHHHHHH	45.85	-
63	Succinylation	LTREDGLKYYRMMQT EECHHHHHHHHHHHH	45.85	-
63	Ubiquitination	LTREDGLKYYRMMQT EECHHHHHHHHHHHH	45.85	-
65	Phosphorylation	REDGLKYYRMMQTVR CHHHHHHHHHHHHHH	7.16	29496907
77	Acetylation	TVRRMELKADQLYKQ HHHHHHHCHHHHHHH	36.29	23954790
77	Malonylation	TVRRMELKADQLYKQ HHHHHHHCHHHHHHH	36.29	26320211
77	Succinylation	TVRRMELKADQLYKQ HHHHHHHCHHHHHHH	36.29	27452117
77	Ubiquitination	TVRRMELKADQLYKQ HHHHHHHCHHHHHHH	36.29	-
83	Acetylation	LKADQLYKQKIIRGF HCHHHHHHHHHHHHH	54.42	23236377
83	Succinylation	LKADQLYKQKIIRGF HCHHHHHHHHHHHHH	54.42	27452117
83	Ubiquitination	LKADQLYKQKIIRGF HCHHHHHHHHHHHHH	54.42	19608861
85	Acetylation	ADQLYKQKIIRGFCH HHHHHHHHHHHHHHH	35.63	23236377
115	Acetylation	INPTDHLITAYRAHG CCCCHHHHHHHHHCC	1.53	19608861
116	Phosphorylation	NPTDHLITAYRAHGF CCCHHHHHHHHHCCC	24.81	-
118	Phosphorylation	TDHLITAYRAHGFTF CHHHHHHHHHCCCEE	10.32	-
121	Acetylation	LITAYRAHGFTFTRG HHHHHHHCCCEECCC	23.93	19608861
130	Phosphorylation	FTFTRGLSVREILAE CEECCCCCHHHHHHH	23.19	24719451
139	Phosphorylation	REILAELTGRKGGCA HHHHHHHHCCCCCCC	26.84	20068231
145	S-palmitoylation	LTGRKGGCAKGKGGS HHCCCCCCCCCCCCC	4.88	21044946
152	Phosphorylation	CAKGKGGSMHMYAKN CCCCCCCCCEEEEEE	17.74	-
156	Phosphorylation	KGGSMHMYAKNFYGG CCCCCEEEEEEECCC	10.35	29496907
161	Phosphorylation	HMYAKNFYGGNGIVG EEEEEEECCCCCCCC	33.25	29496907
168	Phosphorylation	YGGNGIVGAQVPLGA CCCCCCCCCCCCCCC	14.36	24719451
227	Phosphorylation	FICENNRYGMGTSVE EEECCCCCCCCCHHH	17.37	26846344
231	Phosphorylation	NNRYGMGTSVERAAA CCCCCCCCHHHHHHC	22.25	29255136
232	Dephosphorylation	NRYGMGTSVERAAAS CCCCCCCHHHHHHCC	19.09	7782287
232	Phosphorylation	NRYGMGTSVERAAAS CCCCCCCHHHHHHCC	19.09	29255136
239	Phosphorylation	SVERAAASTDYYKRG HHHHHHCCCCHHHCC	19.65	28152594
240	Phosphorylation	VERAAASTDYYKRGD HHHHHCCCCHHHCCC	24.24	28152594
242	Phosphorylation	RAAASTDYYKRGDFI HHHCCCCHHHCCCCC	15.81	27273156
243	Phosphorylation	AAASTDYYKRGDFIP HHCCCCHHHCCCCCC	9.30	28152594
244	Acetylation	AASTDYYKRGDFIPG HCCCCHHHCCCCCCC	43.61	23236377
244	Malonylation	AASTDYYKRGDFIPG HCCCCHHHCCCCCCC	43.61	26320211
244	Succinylation	AASTDYYKRGDFIPG HCCCCHHHCCCCCCC	43.61	-
244	Succinylation	AASTDYYKRGDFIPG HCCCCHHHCCCCCCC	43.61	27452117
244	Ubiquitination	AASTDYYKRGDFIPG HCCCCHHHCCCCCCC	43.61	-
245	Methylation	ASTDYYKRGDFIPGL CCCCHHHCCCCCCCC	33.52	115486777
257	Sulfoxidation	PGLRVDGMDILCVRE CCCCCCCEEEEEEEH	2.21	21406390
261	Glutathionylation	VDGMDILCVREATRF CCCEEEEEEEHHHHH	2.50	22555962
269	Phosphorylation	VREATRFAAAYCRSG EEHHHHHHHHHHHCC	6.46	24719451
272	Phosphorylation	ATRFAAAYCRSGKGP HHHHHHHHHHCCCCC	5.44	28152594
273	Glutathionylation	TRFAAAYCRSGKGPI HHHHHHHHHCCCCCE	2.09	22555962
275	Phosphorylation	FAAAYCRSGKGPILM HHHHHHHCCCCCEEE	41.10	21406692
277	Acetylation	AAYCRSGKGPILMEL HHHHHCCCCCEEEEE	63.86	26051181
277	Succinylation	AAYCRSGKGPILMEL HHHHHCCCCCEEEEE	63.86	-
277	Succinylation	AAYCRSGKGPILMEL HHHHHCCCCCEEEEE	63.86	-
277	Ubiquitination	AAYCRSGKGPILMEL HHHHHCCCCCEEEEE	63.86	-
282 (in isoform 4)	Ubiquitination	-	5.10	-
286	Phosphorylation	PILMELQTYRYHGHS CEEEEEEEEEECCCC	23.69	26074081
287	Phosphorylation	ILMELQTYRYHGHSM EEEEEEEEEECCCCC	9.01	26074081
289	Phosphorylation	MELQTYRYHGHSMSD EEEEEEEECCCCCCC	11.18	22167270
290	Acetylation	ELQTYRYHGHSMSDP EEEEEEECCCCCCCC	20.63	19608861
293	Dephosphorylation	TYRYHGHSMSDPGVS EEEECCCCCCCCCCC	25.27	7782287
293	Phosphorylation	TYRYHGHSMSDPGVS EEEECCCCCCCCCCC	25.27	20201521
294	Sulfoxidation	YRYHGHSMSDPGVSY EEECCCCCCCCCCCH	4.34	28183972
295	Phosphorylation	RYHGHSMSDPGVSYR EECCCCCCCCCCCHH	43.60	29255136
300	Dephosphorylation	SMSDPGVSYRTREEI CCCCCCCCHHCHHHH	18.14	7782287
300	Phosphorylation	SMSDPGVSYRTREEI CCCCCCCCHHCHHHH	18.14	22167270
301	Phosphorylation	MSDPGVSYRTREEIQ CCCCCCCHHCHHHHH	17.38	22167270
303	Phosphorylation	DPGVSYRTREEIQEV CCCCCHHCHHHHHHH	33.91	25884760
305	Acetylation	GVSYRTREEIQEVRS CCCHHCHHHHHHHHH	59.86	19608861
312	Phosphorylation	EEIQEVRSKSDPIML HHHHHHHHCCCCEEH	41.51	20068231
313	Acetylation	EIQEVRSKSDPIMLL HHHHHHHCCCCEEHH	48.60	25825284
313	Malonylation	EIQEVRSKSDPIMLL HHHHHHHCCCCEEHH	48.60	26320211
313	Succinylation	EIQEVRSKSDPIMLL HHHHHHHCCCCEEHH	48.60	-
313	Succinylation	EIQEVRSKSDPIMLL HHHHHHHCCCCEEHH	48.60	-
313	Ubiquitination	EIQEVRSKSDPIMLL HHHHHHHCCCCEEHH	48.60	-
314	Phosphorylation	IQEVRSKSDPIMLLK HHHHHHCCCCEEHHH	50.28	26471730
318	Sulfoxidation	RSKSDPIMLLKDRMV HHCCCCEEHHHHHHH	4.34	21406390
321	Acetylation	SDPIMLLKDRMVNSN CCCEEHHHHHHHCCC	39.05	19608861
321	Malonylation	SDPIMLLKDRMVNSN CCCEEHHHHHHHCCC	39.05	26320211
321	Succinylation	SDPIMLLKDRMVNSN CCCEEHHHHHHHCCC	39.05	27452117
321	Ubiquitination	SDPIMLLKDRMVNSN CCCEEHHHHHHHCCC	39.05	19608861
328	Acetylation	KDRMVNSNLASVEEL HHHHHCCCCCCHHHH	34.13	19608861
331	Phosphorylation	MVNSNLASVEELKEI HHCCCCCCHHHHHHC	32.97	18691976
333	Phosphorylation	NSNLASVEELKEIDV CCCCCCHHHHHHCCH	55.93	24719451
336	Acetylation	LASVEELKEIDVEVR CCCHHHHHHCCHHHH	56.77	23954790
336	Ubiquitination	LASVEELKEIDVEVR CCCHHHHHHCCHHHH	56.77	-
338	Phosphorylation	SVEELKEIDVEVRKE CHHHHHHCCHHHHHH	7.41	24719451
339	Phosphorylation	VEELKEIDVEVRKEI HHHHHHCCHHHHHHH	31.45	27251275
341	Phosphorylation	ELKEIDVEVRKEIED HHHHCCHHHHHHHHH	32.62	27251275
343	Acetylation	KEIDVEVRKEIEDAA HHCCHHHHHHHHHHH	19.86	19608861
344	Ubiquitination	EIDVEVRKEIEDAAQ HCCHHHHHHHHHHHH	69.12	-
354	Ubiquitination	EDAAQFATADPEPPL HHHHHHHCCCCCCCH	32.64	21890473
359	Acetylation	FATADPEPPLEELGY HHCCCCCCCHHHHCC	44.13	19608861
366	Phosphorylation	PPLEELGYHIYSSDP CCHHHHCCEEECCCC	9.54	28064214
369	Phosphorylation	EELGYHIYSSDPPFE HHHCCEEECCCCCCE	6.71	18083107
374	Acetylation	HIYSSDPPFEVRGAN EEECCCCCCEECCCC	42.92	19608861
385	Acetylation	RGANQWIKFKSVS-- CCCCCEEEEEECC--	43.72	23236377
385	Methylation	RGANQWIKFKSVS-- CCCCCEEEEEECC--	43.72	2401739
385	Succinylation	RGANQWIKFKSVS-- CCCCCEEEEEECC--	43.72	-
385	Succinylation	RGANQWIKFKSVS-- CCCCCEEEEEECC--	43.72	-
385	Ubiquitination	RGANQWIKFKSVS-- CCCCCEEEEEECC--	43.72	-
392	Ubiquitination	KFKSVS--------- EEEECC---------		21890473
392	Ubiquitination	KFKSVS--------- EEEECC---------		21890473
392	Ubiquitination	KFKSVS--------- EEEECC---------		21890473
423	Ubiquitination	---------------------------------------- ----------------------------------------		21890473
423 (in isoform 4)	Ubiquitination	-		-

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
232	S	Phosphorylation	Kinase	PDHK1	Q15118	PSP
232	S	Phosphorylation	Kinase	PDK2	Q15119	GPS
232	S	Phosphorylation	Kinase	PDPK1	O15530	GPS
289	Y	Phosphorylation	Kinase	SRC	P12931	PSP
293	S	Phosphorylation	Kinase	PDHK1	Q15118	PSP
293	S	Phosphorylation	Kinase	PDHK2	Q15119	PSP
293	S	Phosphorylation	Kinase	PDHK3	Q15120	PSP
293	S	Phosphorylation	Kinase	PDHK4	Q16654	PSP
293	S	Phosphorylation	Kinase	PDPK1	O15530	GPS
300	S	Phosphorylation	Kinase	PDHK1	Q15118	PSP
300	S	Phosphorylation	Kinase	PDHK2	Q15119	PSP
300	S	Phosphorylation	Kinase	PDHK3	Q15120	PSP
300	S	Phosphorylation	Kinase	PDHK4	Q16654	PSP
300	S	Phosphorylation	Kinase	PDPK1	O15530	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
232	S	Phosphorylation	7782287
Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient.
293	S	Phosphorylation	7782287
Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient.
300	S	Phosphorylation	7782287
Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient.

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 ODPA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ODPB_HUMAN	PDHB	physical	22939629
ODPX_HUMAN	PDHX	physical	22939629
ARLY_HUMAN	ASL	physical	22863883
SLD5_HUMAN	GINS4	physical	22863883
IPP2_HUMAN	PPP1R2	physical	22863883
AT1B1_HUMAN	ATP1B1	physical	26344197
ODP2_HUMAN	DLAT	physical	26344197
RAB7A_HUMAN	RAB7A	physical	26344197
P5CR2_HUMAN	PYCR2	physical	29128334
ANXA2_HUMAN	ANXA2	physical	29128334
P5CR1_HUMAN	PYCR1	physical	29128334
RL32_HUMAN	RPL32	physical	29128334
H31T_HUMAN	HIST3H3	physical	29128334
ADAS_HUMAN	AGPS	physical	29128334
RL28_HUMAN	RPL28	physical	29128334
STML2_HUMAN	STOML2	physical	29128334
THIK_HUMAN	ACAA1	physical	29128334
SC22B_HUMAN	SEC22B	physical	29128334
CKAP4_HUMAN	CKAP4	physical	29128334
DHB4_HUMAN	HSD17B4	physical	29128334
MDHM_HUMAN	MDH2	physical	29128334
FUBP1_HUMAN	FUBP1	physical	29128334
MIC19_HUMAN	CHCHD3	physical	29128334
CHTOP_HUMAN	CHTOP	physical	29128334
NLTP_HUMAN	SCP2	physical	29128334
RL30_HUMAN	RPL30	physical	29128334
DREB_HUMAN	DBN1	physical	29128334
SFXN1_HUMAN	SFXN1	physical	29128334
RAB1B_HUMAN	RAB1B	physical	29128334
RL12_HUMAN	RPL12	physical	29128334
PHF5A_HUMAN	PHF5A	physical	29128334
H10_HUMAN	H1F0	physical	29128334
LRC59_HUMAN	LRRC59	physical	29128334
THOC4_HUMAN	ALYREF	physical	29128334
AMOT_HUMAN	AMOT	physical	29128334
KAD2_HUMAN	AK2	physical	29128334
ATD3A_HUMAN	ATAD3A	physical	29128334
RAB5C_HUMAN	RAB5C	physical	29128334
ROA1_HUMAN	HNRNPA1	physical	29128334
NDUS6_HUMAN	NDUFS6	physical	29128334
AIMP1_HUMAN	AIMP1	physical	29128334
ACOT8_HUMAN	ACOT8	physical	29128334
HSDL2_HUMAN	HSDL2	physical	29128334
ATP5H_HUMAN	ATP5H	physical	29128334
SND1_HUMAN	SND1	physical	29128334
ECI2_HUMAN	ECI2	physical	29128334
RAB1A_HUMAN	RAB1A	physical	29128334
HNRH3_HUMAN	HNRNPH3	physical	29128334
RBM8A_HUMAN	RBM8A	physical	29128334
TOM22_HUMAN	TOMM22	physical	29128334
RA1L2_HUMAN	HNRNPA1L2	physical	29128334
ODPB_HUMAN	PDHB	physical	29128334
GLYM_HUMAN	SHMT2	physical	29128334
EMD_HUMAN	EMD	physical	29128334
MIC60_HUMAN	IMMT	physical	29128334
SCAM3_HUMAN	SCAMP3	physical	29128334
ILF2_HUMAN	ILF2	physical	29128334
DHRS4_HUMAN	DHRS4	physical	29128334
ATRAP_HUMAN	AGTRAP	physical	29128334
RFA3_HUMAN	RPA3	physical	29128334
ELAV1_HUMAN	ELAVL1	physical	29128334
RAB7A_HUMAN	RAB7A	physical	29128334
H2B1J_HUMAN	HIST1H2BJ	physical	29128334
PDIP3_HUMAN	POLDIP3	physical	29128334
RB11A_HUMAN	RAB11A	physical	29128334
QCR1_HUMAN	UQCRC1	physical	29128334
MMGT1_HUMAN	MMGT1	physical	29128334
PABP2_HUMAN	PABPN1	physical	29128334
HNRDL_HUMAN	HNRNPDL	physical	29128334
EF1D_HUMAN	EEF1D	physical	29128334
CHCH2_HUMAN	CHCHD2	physical	29128334
AT1A1_HUMAN	ATP1A1	physical	29128334
GOGA2_HUMAN	GOLGA2	physical	29128334
ATPO_HUMAN	ATP5O	physical	29128334
TMEDA_HUMAN	TMED10	physical	29128334
TR150_HUMAN	THRAP3	physical	29128334
STX5_HUMAN	STX5	physical	29128334
TCPB_HUMAN	CCT2	physical	29128334
RL35_HUMAN	RPL35	physical	29128334
RFA1_HUMAN	RPA1	physical	29128334
IRS4_HUMAN	IRS4	physical	29128334
H2B1A_HUMAN	HIST1H2BA	physical	29128334
RHOA_HUMAN	RHOA	physical	29128334
DAZP1_HUMAN	DAZAP1	physical	29128334
HSPB1_HUMAN	HSPB1	physical	29128334
HAX1_HUMAN	HAX1	physical	29128334
SARNP_HUMAN	SARNP	physical	29128334
RPN2_HUMAN	RPN2	physical	29128334
DHX30_HUMAN	DHX30	physical	29128334
H1X_HUMAN	H1FX	physical	29128334
TOM40_HUMAN	TOMM40	physical	29128334
RL10A_HUMAN	RPL10A	physical	29128334
RM14_HUMAN	MRPL14	physical	29128334
ABCD3_HUMAN	ABCD3	physical	29128334
NB5R3_HUMAN	CYB5R3	physical	29128334
QCR2_HUMAN	UQCRC2	physical	29128334
TMED4_HUMAN	TMED4	physical	29128334
RM02_HUMAN	MRPL2	physical	29128334
TRAP1_HUMAN	TRAP1	physical	29128334
P53_HUMAN	TP53	physical	29128334
SRRT_HUMAN	SRRT	physical	29128334
DERL2_HUMAN	DERL2	physical	29128334
FUBP3_HUMAN	FUBP3	physical	29128334
PDIA3_HUMAN	PDIA3	physical	29128334
RPN1_HUMAN	RPN1	physical	29128334
RM13_HUMAN	MRPL13	physical	29128334
FMR1_HUMAN	FMR1	physical	29128334
PABP1_HUMAN	PABPC1	physical	29128334
RBM4_HUMAN	RBM4	physical	29128334
ATD3B_HUMAN	ATAD3B	physical	29128334
RED_HUMAN	IK	physical	29128334
PERI_HUMAN	PRPH	physical	29128334
LSM12_HUMAN	LSM12	physical	29128334
GOGB1_HUMAN	GOLGB1	physical	29128334
AINX_HUMAN	INA	physical	29128334
PININ_HUMAN	PNN	physical	29128334
SERPH_HUMAN	SERPINH1	physical	29128334
PSPC1_HUMAN	PSPC1	physical	29128334
PTBP1_HUMAN	PTBP1	physical	29128334
ROAA_HUMAN	HNRNPAB	physical	29128334
CWC15_HUMAN	CWC15	physical	29128334
G3BP1_HUMAN	G3BP1	physical	29128334
LMNB1_HUMAN	LMNB1	physical	29128334
COR1C_HUMAN	CORO1C	physical	29128334
SURF6_HUMAN	SURF6	physical	29128334
MPCP_HUMAN	SLC25A3	physical	29128334
AIFM1_HUMAN	AIFM1	physical	29128334
H2AY_HUMAN	H2AFY	physical	29128334
PRP19_HUMAN	PRPF19	physical	29128334
TFR1_HUMAN	TFRC	physical	29128334
AT2A2_HUMAN	ATP2A2	physical	29128334
NUP62_HUMAN	NUP62	physical	29128334
DNJA1_HUMAN	DNAJA1	physical	29128334
PQBP1_HUMAN	PQBP1	physical	29128334
PAIRB_HUMAN	SERBP1	physical	29128334
SRC8_HUMAN	CTTN	physical	29128334
LAP2A_HUMAN	TMPO	physical	29128334
LAP2B_HUMAN	TMPO	physical	29128334
THIL_HUMAN	ACAT1	physical	29128334
FLOT1_HUMAN	FLOT1	physical	29128334
TPM3_HUMAN	TPM3	physical	29128334
MYO6_HUMAN	MYO6	physical	29128334
EF1G_HUMAN	EEF1G	physical	29128334
IMB1_HUMAN	KPNB1	physical	29128334
RBM23_HUMAN	RBM23	physical	29128334
VDAC2_HUMAN	VDAC2	physical	29128334
ZC3HE_HUMAN	ZC3H14	physical	29128334
OST48_HUMAN	DDOST	physical	29128334
RM23_HUMAN	MRPL23	physical	29128334
EDC4_HUMAN	EDC4	physical	29128334
PR38A_HUMAN	PRPF38A	physical	29128334
DESM_HUMAN	DES	physical	29128334
SFXN3_HUMAN	SFXN3	physical	29128334
NUP93_HUMAN	NUP93	physical	29128334
SDHA_HUMAN	SDHA	physical	29128334
LDH6A_HUMAN	LDHAL6A	physical	29128334
PDIA1_HUMAN	P4HB	physical	29128334
MCA3_HUMAN	EEF1E1	physical	29128334
ACTN4_HUMAN	ACTN4	physical	29128334
GNL3_HUMAN	GNL3	physical	29128334
DSG2_HUMAN	DSG2	physical	29128334
FL2D_HUMAN	WTAP	physical	29128334
RL13A_HUMAN	RPL13A	physical	29128334
SRP68_HUMAN	SRP68	physical	29128334
SYRC_HUMAN	RARS	physical	29128334
CTNA1_HUMAN	CTNNA1	physical	29128334
PLEC_HUMAN	PLEC	physical	29128334
PRP6_HUMAN	PRPF6	physical	29128334
USO1_HUMAN	USO1	physical	29128334
DSRAD_HUMAN	ADAR	physical	29128334
ADDA_HUMAN	ADD1	physical	29128334
HNRL2_HUMAN	HNRNPUL2	physical	29128334
MYO1D_HUMAN	MYO1D	physical	29128334
LIMA1_HUMAN	LIMA1	physical	29128334
NCBP1_HUMAN	NCBP1	physical	29128334
ACINU_HUMAN	ACIN1	physical	29128334
TMF1_HUMAN	TMF1	physical	29128334
TCPQ_HUMAN	CCT8	physical	29128334
EIF3A_HUMAN	EIF3A	physical	29128334
HP1B3_HUMAN	HP1BP3	physical	29128334
RAGP1_HUMAN	RANGAP1	physical	29128334
FIP1_HUMAN	FIP1L1	physical	29128334
SYMC_HUMAN	MARS	physical	29128334
MTCH2_HUMAN	MTCH2	physical	29128334
IF2A_HUMAN	EIF2S1	physical	29128334
SYMPK_HUMAN	SYMPK	physical	29128334
IF4G1_HUMAN	EIF4G1	physical	29128334
SP16H_HUMAN	SUPT16H	physical	29128334
NEUL_HUMAN	NLN	physical	29128334
RBM27_HUMAN	RBM27	physical	29128334
PHF6_HUMAN	PHF6	physical	29128334
LUC7L_HUMAN	LUC7L	physical	29128334
CD11A_HUMAN	CDK11A	physical	29128334
CALD1_HUMAN	CALD1	physical	29128334
NEB2_HUMAN	PPP1R9B	physical	29128334
COPA_HUMAN	COPA	physical	29128334
DNJA2_HUMAN	DNAJA2	physical	29128334
M4K1_HUMAN	MAP4K1	physical	29128334
PDC6I_HUMAN	PDCD6IP	physical	29128334
SAFB1_HUMAN	SAFB	physical	29128334
NU107_HUMAN	NUP107	physical	29128334
RUVB2_HUMAN	RUVBL2	physical	29128334
RRBP1_HUMAN	RRBP1	physical	29128334
CPSF7_HUMAN	CPSF7	physical	29128334
GOGA3_HUMAN	GOLGA3	physical	29128334
AT2A1_HUMAN	ATP2A1	physical	29128334
PLRG1_HUMAN	PLRG1	physical	29128334
NOP58_HUMAN	NOP58	physical	29128334
MYO1B_HUMAN	MYO1B	physical	29128334
SEPT9_HUMAN	SEPT9	physical	29128334
LBR_HUMAN	LBR	physical	29128334
GT251_HUMAN	COLGALT1	physical	29128334
FAS_HUMAN	FASN	physical	29128334
SYIC_HUMAN	IARS	physical	29128334
VIGLN_HUMAN	HDLBP	physical	29128334
THOC1_HUMAN	THOC1	physical	29128334
LMNA_HUMAN	LMNA	physical	29128334
MTA2_HUMAN	MTA2	physical	29128334
CMC2_HUMAN	SLC25A13	physical	29128334
TOP1_HUMAN	TOP1	physical	29128334
CPT1A_HUMAN	CPT1A	physical	29128334
ZCCHV_HUMAN	ZC3HAV1	physical	29128334
CWC22_HUMAN	CWC22	physical	29128334
NFM_HUMAN	NEFM	physical	29128334
DYHC1_HUMAN	DYNC1H1	physical	29128334
MYH11_HUMAN	MYH11	physical	29128334
SMCA5_HUMAN	SMARCA5	physical	29128334
SC16A_HUMAN	SEC16A	physical	29128334
LPPRC_HUMAN	LRPPRC	physical	29128334
HORN_HUMAN	HRNR	physical	29128334
KDIS_HUMAN	KIDINS220	physical	29128334
CHD4_HUMAN	CHD4	physical	29128334
NUMA1_HUMAN	NUMA1	physical	29128334
TPR_HUMAN	TPR	physical	29128334
DESP_HUMAN	DSP	physical	29128334
H2A1B_HUMAN	HIST1H2AE	physical	29128334
ARPC4_HUMAN	ARPC4	physical	29128334
H31_HUMAN	HIST1H3A	physical	29128334
H33_HUMAN	H3F3A	physical	29128334
SMN_HUMAN	SMN1	physical	29128334
H2A2A_HUMAN	HIST2H2AA3	physical	29128334
H32_HUMAN	HIST2H3C	physical	29128334
AKAP2_HUMAN	AKAP2	physical	29128334

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
312170	Pyruvate dehydrogenase E1-alpha deficiency (PDHAD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ODPA_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-77; LYS-83; LYS-321 ANDLYS-336, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Structural basis for inactivation of the human pyruvate dehydrogenasecomplex by phosphorylation: role of disordered phosphorylationloops."; Kato M., Wynn R.M., Chuang J.L., Tso S.C., Machius M., Li J.,Chuang D.T.; Structure 16:1849-1859(2008). Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 30-390, ENZYME REGULATION,AND PHOSPHORYLATION AT SER-232; SER-293 AND SER-300 BY PDK4.	19081061 [Abstract]
"Phosphorylation of serine 264 impedes active site accessibility inthe E1 component of the human pyruvate dehydrogenase multienzymecomplex."; Seifert F., Ciszak E., Korotchkina L., Golbik R., Spinka M.,Dominiak P., Sidhu S., Brauer J., Patel M.S., Tittmann K.; Biochemistry 46:6277-6287(2007). Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-390, ENZYME REGULATION,AND PHOSPHORYLATION AT SER-293.	17474719 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-300, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-232 AND SER-293, ANDMASS SPECTROMETRY.	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-232; SER-293; SER-295AND SER-300, AND MASS SPECTROMETRY.	18220336 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-293, ANDMASS SPECTROMETRY.	18088087 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND MASSSPECTROMETRY.	17487921 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-231, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-231, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-289 AND TYR-301, ANDMASS SPECTROMETRY.	18083107 [Abstract]

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