dbPTM

ODPX_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ODPX_HUMAN
UniProt AC	O00330
Protein Name	Pyruvate dehydrogenase protein X component, mitochondrial
Gene Name	PDHX
Organism	Homo sapiens (Human).
Sequence Length	501
Subcellular Localization	Mitochondrion matrix.
Protein Description	Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex..
Protein Sequence	MAASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGANWRWFHSTQWLRGDPIKILMPSLSPTMEEGNIVKWLKKEGEAVSAGDALCEIETDKAVVTLDASDDGILAKIVVEEGSKNIRLGSLIGLIVEEGEDWKHVEIPKDVGPPPPVSKPSEPRPSPEPQISIPVKKEHIPGTLRFRLSPAARNILEKHSLDASQGTATGPRGIFTKEDALKLVQLKQTGKITESRPTPAPTATPTAPSPLQATAGPSYPRPVIPPVSTPGQPNAVGTFTEIPASNIRRVIAKRLTESKSTVPHAYATADCDLGAVLKVRQDLVKDDIKVSVNDFIIKAAAVTLKQMPDVNVSWDGEGPKQLPFIDISVAVATDKGLLTPIIKDAAAKGIQEIADSVKALSKKARDGKLLPEEYQGGSFSISNLGMFGIDEFTAVINPPQACILAVGRFRPVLKLTEDEEGNAKLQQRQLITVTMSSDSRVVDDELATRFLKSFKANLENPIRLA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MAASWRLGCDP ----CCCCCCCCCCH	11.82	24043423
9 (in isoform 3)	Phosphorylation	-	8.45	-
15 (in isoform 3)	Phosphorylation	-	27.60	-
16	Phosphorylation	CDPRLLRYLVGFPGR CCHHHHHHHHCCCCC	13.00	-
25	Phosphorylation	VGFPGRRSVGLVKGA HCCCCCCCHHCCCCC	21.12	-
31 (in isoform 3)	Phosphorylation	-	20.68	22210691
50 (in isoform 3)	Phosphorylation	-	39.97	22210691
52 (in isoform 3)	Phosphorylation	-	2.93	22210691
58	Acetylation	WLRGDPIKILMPSLS HHCCCCEEEEEECCC	34.86	25038526
63	Phosphorylation	PIKILMPSLSPTMEE CEEEEEECCCCCCCC	27.75	30108239
64	Ubiquitination	IKILMPSLSPTMEEG EEEEEECCCCCCCCC	6.15	29967540
65	Phosphorylation	KILMPSLSPTMEEGN EEEEECCCCCCCCCC	23.74	30108239
67	Phosphorylation	LMPSLSPTMEEGNIV EEECCCCCCCCCCCH	33.56	30108239
75	Acetylation	MEEGNIVKWLKKEGE CCCCCCHHHHHHCCC	42.91	26051181
79	Ubiquitination	NIVKWLKKEGEAVSA CCHHHHHHCCCCEEC	69.64	29967540
95	Phosphorylation	DALCEIETDKAVVTL CCEEEEECCCEEEEE	48.76	27251275
97	N6-lipoyllysine	LCEIETDKAVVTLDA EEEEECCCEEEEEEC	50.96	-
97	Lipoylation	LCEIETDKAVVTLDA EEEEECCCEEEEEEC	50.96	-
97	Lipoylation	LCEIETDKAVVTLDA EEEEECCCEEEEEEC	50.96	25525879
101	Phosphorylation	ETDKAVVTLDASDDG ECCCEEEEEECCCCC	16.60	27251275
105	Ubiquitination	AVVTLDASDDGILAK EEEEEECCCCCEEEE	35.58	29967540
105	Acetylation	AVVTLDASDDGILAK EEEEEECCCCCEEEE	35.58	-
120	Ubiquitination	IVVEEGSKNIRLGSL EEEECCCCCEEECHH	68.22	29967540
120	Acetylation	IVVEEGSKNIRLGSL EEEECCCCCEEECHH	68.22	25953088
139	Acetylation	VEEGEDWKHVEIPKD EEECCCCCCEECCCC	50.52	25038526
154	Phosphorylation	VGPPPPVSKPSEPRP CCCCCCCCCCCCCCC	44.62	27251275
157	Phosphorylation	PPPVSKPSEPRPSPE CCCCCCCCCCCCCCC	65.06	27251275
157	Ubiquitination	PPPVSKPSEPRPSPE CCCCCCCCCCCCCCC	65.06	29967540
158	Ubiquitination	PPVSKPSEPRPSPEP CCCCCCCCCCCCCCC	54.58	29967540
162	Phosphorylation	KPSEPRPSPEPQISI CCCCCCCCCCCCEEC	43.08	25159151
167	Ubiquitination	RPSPEPQISIPVKKE CCCCCCCEECEEECC	6.20	29967540
168	Phosphorylation	PSPEPQISIPVKKEH CCCCCCEECEEECCC	18.65	25159151
173	Ubiquitination	QISIPVKKEHIPGTL CEECEEECCCCCCEE	55.55	29967540
179	Acetylation	KKEHIPGTLRFRLSP ECCCCCCEEEEEECH	14.92	19608861
179	Acetylation	KKEHIPGTLRFRLSP ECCCCCCEEEEEECH	14.92	-
179	Phosphorylation	KKEHIPGTLRFRLSP ECCCCCCEEEEEECH	14.92	28857561
194	Acetylation	AARNILEKHSLDASQ HHHHHHHHHCCCCCC	34.74	19608861
196	Phosphorylation	RNILEKHSLDASQGT HHHHHHHCCCCCCCC	38.73	28857561
198	Ubiquitination	ILEKHSLDASQGTAT HHHHHCCCCCCCCCC	47.38	29967540
200	Phosphorylation	EKHSLDASQGTATGP HHHCCCCCCCCCCCC	28.89	28857561
208	Ubiquitination	QGTATGPRGIFTKED CCCCCCCCCEECHHH	52.78	29967540
208	Methylation	QGTATGPRGIFTKED CCCCCCCCCEECHHH	52.78	115486811
213	Ubiquitination	GPRGIFTKEDALKLV CCCCEECHHHHHHHH	42.73	29967540
218	Acetylation	FTKEDALKLVQLKQT ECHHHHHHHHHHHHH	48.62	25953088
223	Ubiquitination	ALKLVQLKQTGKITE HHHHHHHHHHCCCCC	28.82	29967540
223	Acetylation	ALKLVQLKQTGKITE HHHHHHHHHHCCCCC	28.82	25953088
297	Phosphorylation	RLTESKSTVPHAYAT HHCCCCCCCCCEEEC	41.62	30576142
304	Phosphorylation	TVPHAYATADCDLGA CCCCEEECCCCCHHH	15.45	30576142
307	Glutathionylation	HAYATADCDLGAVLK CEEECCCCCHHHEEH	4.28	22555962
310	Acetylation	ATADCDLGAVLKVRQ ECCCCCHHHEEHHHH	10.61	-
314	Ubiquitination	CDLGAVLKVRQDLVK CCHHHEEHHHHHHHC	28.86	-
321	Acetylation	KVRQDLVKDDIKVSV HHHHHHHCCCCEEEH	57.91	26210075
325	Acetylation	DLVKDDIKVSVNDFI HHHCCCCEEEHHHHH	35.14	23236377
364	Phosphorylation	QLPFIDISVAVATDK CCCEEEEEEEEECCC	10.56	25693802
369	Ubiquitination	DISVAVATDKGLLTP EEEEEEECCCCCCHH	31.48	29967540
369	Phosphorylation	DISVAVATDKGLLTP EEEEEEECCCCCCHH	31.48	25693802
375	Phosphorylation	ATDKGLLTPIIKDAA ECCCCCCHHHHHHHH	19.93	-
379	Succinylation	GLLTPIIKDAAAKGI CCCHHHHHHHHHHCH	41.87	23954790
379	2-Hydroxyisobutyrylation	GLLTPIIKDAAAKGI CCCHHHHHHHHHHCH	41.87	-
379	Acetylation	GLLTPIIKDAAAKGI CCCHHHHHHHHHHCH	41.87	-
379	Ubiquitination	GLLTPIIKDAAAKGI CCCHHHHHHHHHHCH	41.87	29967540
384	Ubiquitination	IIKDAAAKGIQEIAD HHHHHHHHCHHHHHH	52.39	29967540
384	2-Hydroxyisobutyrylation	IIKDAAAKGIQEIAD HHHHHHHHCHHHHHH	52.39	-
394	Succinylation	QEIADSVKALSKKAR HHHHHHHHHHHHHHC	47.78	-
394	Acetylation	QEIADSVKALSKKAR HHHHHHHHHHHHHHC	47.78	23236377
394	Succinylation	QEIADSVKALSKKAR HHHHHHHHHHHHHHC	47.78	27452117
394	Ubiquitination	QEIADSVKALSKKAR HHHHHHHHHHHHHHC	47.78	29967540
445	Ubiquitination	CILAVGRFRPVLKLT EEEEEEECCEEECCC	9.47	-
460	Ubiquitination	EDEEGNAKLQQRQLI CCCCCCCEEEEEEEE	51.32	-
468	Phosphorylation	LQQRQLITVTMSSDS EEEEEEEEEEECCCC	20.65	21406692
470	Phosphorylation	QRQLITVTMSSDSRV EEEEEEEEECCCCCC	11.59	21406692
472	Phosphorylation	QLITVTMSSDSRVVD EEEEEEECCCCCCCC	22.94	21406692
473	Phosphorylation	LITVTMSSDSRVVDD EEEEEECCCCCCCCH	28.87	21406692
475	Phosphorylation	TVTMSSDSRVVDDEL EEEECCCCCCCCHHH	28.99	21406692
476	Acetylation	VTMSSDSRVVDDELA EEECCCCCCCCHHHH	37.15	-
488	Acetylation	ELATRFLKSFKANLE HHHHHHHHHHHHHCC	51.65	25825284
489	Phosphorylation	LATRFLKSFKANLEN HHHHHHHHHHHHCCC	33.84	24719451
491	Malonylation	TRFLKSFKANLENPI HHHHHHHHHHCCCCC	43.38	26320211
491	Methylation	TRFLKSFKANLENPI HHHHHHHHHHCCCCC	43.38	7668025
491	Acetylation	TRFLKSFKANLENPI HHHHHHHHHHCCCCC	43.38	23749302

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
-	K	Ubiquitination	E3 ubiquitin ligase	SPOP	O43791	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
97	K	Lipoylation		25525879
Delipoylated at Lys-97 by SIRT4, delipoylation decreases the PHD complex activity.

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 ODPX_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATRAP_HUMAN	AGTRAP	physical	25416956
EP300_HUMAN	EP300	physical	11756538
NDF1_HUMAN	NEUROD1	physical	11756538
IF2M_HUMAN	MTIF2	physical	28514442
PPCEL_HUMAN	PREPL	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
245349	Pyruvate dehydrogenase E3-binding protein deficiency (PDHXD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ODPX_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-194, AND MASS SPECTROMETRY.	19608861 [Abstract]

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