PDP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PDP1_HUMAN
• UniProt AC: Q9P0J1
• Protein Name: [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial
• Gene Name: PDP1
• Organism: Homo sapiens (Human).
• Sequence Length: 537
• Subcellular Localization: Mitochondrion matrix.
• Protein Description: Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex..
• Protein Sequence: MPAPTQLFFPLIRNCELSRIYGTACYCHHKHLCCSSSYIPQSRLRYTPHPAYATFCRPKENWWQYTQGRRYASTPQKFYLTPPQVNSILKANEYSFKVPEFDGKNVSSILGFDSNQLPANAPIEDRRSAATCLQTRGMLLGVFDGHAGCACSQAVSERLFYYIAVSLLPHETLLEIENAVESGRALLPILQWHKHPNDYFSKEASKLYFNSLRTYWQELIDLNTGESTDIDVKEALINAFKRLDNDISLEAQVGDPNSFLNYLVLRVAFSGATACVAHVDGVDLHVANTGDSRAMLGVQEEDGSWSAVTLSNDHNAQNERELERLKLEHPKSEAKSVVKQDRLLGLLMPFRAFGDVKFKWSIDLQKRVIESGPDQLNDNEYTKFIPPNYHTPPYLTAEPEVTYHRLRPQDKFLVLATDGLWETMHRQDVVRIVGEYLTGMHHQQPIAVGGYKVTLGQMHGLLTERRTKMSSVFEDQNAATHLIRHAVGNNEFGTVDHERLSKMLSLPEELARMYRDDITIIVVQFNSHVVGAYQNQE

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
43	Methylation	SSYIPQSRLRYTPHP CCCCCHHHCCCCCCC	20.24	24411441
46	Phosphorylation	IPQSRLRYTPHPAYA CCHHHCCCCCCCCCC	29.25	18083107
59	Ubiquitination	YATFCRPKENWWQYT CCCEECCCCCCCCCC	44.31	-
74	Phosphorylation	QGRRYASTPQKFYLT CCCCCCCCCCEEECC	22.90	28985074
77	Ubiquitination	RYASTPQKFYLTPPQ CCCCCCCEEECCCHH	36.86	21906983
79	Phosphorylation	ASTPQKFYLTPPQVN CCCCCEEECCCHHHH	19.39	-
87	Phosphorylation	LTPPQVNSILKANEY CCCHHHHHHHHHCCC	30.37	24719451
87	O-linked_Glycosylation	LTPPQVNSILKANEY CCCHHHHHHHHHCCC	30.37	29351928
90	Ubiquitination	PQVNSILKANEYSFK HHHHHHHHHCCCEEE	47.71	21906983
94	Phosphorylation	SILKANEYSFKVPEF HHHHHCCCEEECCCC	21.15	-
97	Ubiquitination	KANEYSFKVPEFDGK HHCCCEEECCCCCCC	51.44	21906983
97	Acetylation	KANEYSFKVPEFDGK HHCCCEEECCCCCCC	51.44	25038526
104	Acetylation	KVPEFDGKNVSSILG ECCCCCCCCHHHHHC	56.89	63650813
104	Ubiquitination	KVPEFDGKNVSSILG ECCCCCCCCHHHHHC	56.89	21906983
194	Ubiquitination	LPILQWHKHPNDYFS HHHHHHCCCCCCCCC	58.77	21906983
199	Phosphorylation	WHKHPNDYFSKEASK HCCCCCCCCCHHHHH	19.18	-
202	Ubiquitination	HPNDYFSKEASKLYF CCCCCCCHHHHHHHH	47.61	21906983
202	Acetylation	HPNDYFSKEASKLYF CCCCCCCHHHHHHHH	47.61	19608861
206	Ubiquitination	YFSKEASKLYFNSLR CCCHHHHHHHHHHHH	55.01	21906983
227	Ubiquitination	IDLNTGESTDIDVKE HHCCCCCCCCCHHHH	32.50	19608861
227	Acetylation	IDLNTGESTDIDVKE HHCCCCCCCCCHHHH	32.50	19608861
233	Ubiquitination	ESTDIDVKEALINAF CCCCCHHHHHHHHHH	33.26	-
241	Ubiquitination	EALINAFKRLDNDIS HHHHHHHHHCCCCCC	50.03	21906983
241	Acetylation	EALINAFKRLDNDIS HHHHHHHHHCCCCCC	50.03	30591195
292	Phosphorylation	HVANTGDSRAMLGVQ EEEECCCCCCEEEEE	24.23	-
326	Ubiquitination	ERELERLKLEHPKSE HHHHHHHHCCCCHHH	59.04	21906983
326	Acetylation	ERELERLKLEHPKSE HHHHHHHHCCCCHHH	59.04	22362505
331	Acetylation	RLKLEHPKSEAKSVV HHHCCCCHHHHHHHH	63.94	22362515
331	Ubiquitination	RLKLEHPKSEAKSVV HHHCCCCHHHHHHHH	63.94	-
335	Ubiquitination	EHPKSEAKSVVKQDR CCCHHHHHHHHCHHH	39.47	21906983
335	Acetylation	EHPKSEAKSVVKQDR CCCHHHHHHHHCHHH	39.47	22362525
339	Ubiquitination	SEAKSVVKQDRLLGL HHHHHHHCHHHHHHH	44.30	21906983
357	Ubiquitination	FRAFGDVKFKWSIDL CHHHCCCEEEEEEEH	46.06	21906983
357	Acetylation	FRAFGDVKFKWSIDL CHHHCCCEEEEEEEH	46.06	63650811
359	Ubiquitination	AFGDVKFKWSIDLQK HHCCCEEEEEEEHHH	34.02	21906983
366	Sumoylation	KWSIDLQKRVIESGP EEEEEHHHHHHHHCC	56.80	-
366	Ubiquitination	KWSIDLQKRVIESGP EEEEEHHHHHHHHCC	56.80	21906983
381	Phosphorylation	DQLNDNEYTKFIPPN CCCCCCCCCCCCCCC	22.83	-
383	Ubiquitination	LNDNEYTKFIPPNYH CCCCCCCCCCCCCCC	40.15	21906983
411	Ubiquitination	HRLRPQDKFLVLATD ECCCCCCEEEEEECC	35.04	21906983
411	Acetylation	HRLRPQDKFLVLATD ECCCCCCEEEEEECC	35.04	25038526
452	Ubiquitination	PIAVGGYKVTLGQMH CEEECCEEEEHHHHC	31.83	21906983
468	Ubiquitination	LLTERRTKMSSVFED HHHHHHHHHHHHCCC	34.67	21906983
468	Acetylation	LLTERRTKMSSVFED HHHHHHHHHHHHCCC	34.67	63650807
502	Ubiquitination	VDHERLSKMLSLPEE CCHHHHHHHHCCHHH	48.75	21906983
502	Acetylation	VDHERLSKMLSLPEE CCHHHHHHHHCCHHH	48.75	63650809

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
381	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
381	Y	Phosphorylation	Kinase	FGFR1	P11362	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PDP1_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 PDP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ODPA_HUMAN	PDHA1	physical	24486017
THIL_HUMAN	ACAT1	physical	24486017
SIR3_HUMAN	SIRT3	physical	24486017
FGFR1_HUMAN	FGFR1	physical	24486017
EGFR_HUMAN	EGFR	physical	24486017
COR1C_HUMAN	CORO1C	physical	27880917
PDPR_HUMAN	PDPR	physical	27880917
MPPA_HUMAN	PMPCA	physical	27880917
MPPB_HUMAN	PMPCB	physical	27880917
SPTN1_HUMAN	SPTAN1	physical	27880917
SPTB2_HUMAN	SPTBN1	physical	27880917

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 608782: Pyruvate dehydrogenase phosphatase deficiency (PDP deficiency)
• 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-202, AND MASS SPECTROMETRY.
PubMed: 19608861