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Protein Page:
PDP1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PDP1 a protein phosphoserine phosphatase associated with the mitochondrial matrix that activates phosphorylated pyruvate dehydrogenase complex by dephosphorylation. The PDPs play crucial roles in switching metabolic flux from glycolysis towards oxidative phosphorylation. Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex . PDP1 is composed of a catalytic subunit and a regulatory subunit (PDPR). Heterodimer of a catalytic subunit and a FAD protein of unknown function . Defects in PDP1 are the cause of pyruvate dehydrogenase phosphatase deficiency (PDP deficiency). PDP deficiency results in lactic acidosis leading to neurological dysfunction. Belongs to the PP2C family. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Protein phosphatase, Ser/Thr (non-receptor); Mitochondrial; EC 3.1.3.43
Cellular Component: mitochondrial matrix
Molecular Function: [pyruvate dehydrogenase (lipoamide)] phosphatase activity; metal ion binding; protein serine/threonine phosphatase activity
Biological Process: cellular metabolic process; regulation of acetyl-CoA biosynthetic process from pyruvate; pyruvate metabolic process
Reference #:  Q9P0J1 (UniProtKB)
Alt. Names/Synonyms: [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial; FLJ32517; FLJ56179; MGC119646; PDH; PDP; PDP 1; PDP1; PDPC; PDPC 1; PPM2C; Protein phosphatase 2C; protein phosphatase 2C, magnesium-dependent, catalytic subunit; pyruvate dehydrogenase (Lipoamide) phosphatase-phosphatase; Pyruvate dehydrogenase phosphatase catalytic subunit 1; pyruvate dehyrogenase phosphatase catalytic subunit 1
Gene Symbols: PDP1
Molecular weight: 61,054 Da
Basal Isoelectric point: 6.2  Predict pI for various phosphorylation states
Select Structure to View Below

PDP1

Protein Structure Not Found.


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Sites Implicated In
cell growth, induced: K202‑ac
molecular association, regulation: K202‑ac, Y381‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 R43-m1 SSYIPQSrLRyTPHP
1 2 Y46-p IPQSrLRyTPHPAYA
0 1 K77-ub RYASTPQkFyLTPPQ
1 1 Y79-p ASTPQkFyLTPPQVN
0 1 K90-ub PQVNSILkANEySFk
2 1 Y94-p SILkANEySFkVPEF
0 1 K97-ub kANEySFkVPEFDGk
1 1 K104-ac kVPEFDGkNVSSILG
0 1 K104-ub kVPEFDGkNVSSILG
0 1 K194-ub LPILQWHkHPNDYFS
2 2 K202-ac HPNDYFSkEASkLYF
0 2 K202-ub HPNDYFSkEASkLYF
0 1 K206-ub YFSkEASkLYFNSLR
0 2 K241-ac EALINAFkRLDNDIS
0 1 K241-ub EALINAFkRLDNDIS
0 1 K326-ac ERELERLkLEHPkSE
0 1 K326-ub ERELERLkLEHPkSE
0 1 K331-ac RLkLEHPkSEAkSVV
0 1 K335-ac EHPkSEAkSVVkQDR
0 1 K335-ub EHPkSEAkSVVkQDR
0 1 K339-ub SEAkSVVkQDRLLGL
1 1 K357-ac FRAFGDVkFkWSIDL
0 3 K357-ub FRAFGDVkFkWSIDL
0 1 K359-ub AFGDVkFkWSIDLQk
0 1 K366-ub kWSIDLQkRVIESGP
2 1 Y381-p DQLNDNEyTkFIPPN
0 1 K383-ub LNDNEyTkFIPPNYH
0 1 K411-ub HRLRPQDkFLVLATD
0 1 K452-ub PIAVGGYkVTLGQMH
1 1 K468-ac LLTERRTkMSSVFED
0 1 K468-ub LLTERRTkMSSVFED
1 1 K502-ac VDHERLSkMLSLPEE
0 2 K502-ub VDHERLSkMLSLPEE
0 2 Y514 PEELARMYRDDITII
  mouse

 
R43 PPYIPQNRLRYTPHP
Y46 IPQNRLRYTPHPAYA
K77 RYASTPQKFYLTPPQ
Y79 ASTPQKFYLTPPQVN
K90 PQVNSILKANEYSFK
Y94 SILKANEYSFKVPEF
K97 KANEYSFKVPEFDGK
K104 KVPEFDGKNVSSILG
K104 KVPEFDGKNVSSILG
K194 LPILQWHKHPNDYFS
K202 HPNDYFSKEASKLYF
K202 HPNDYFSKEASKLYF
K206 YFSKEASKLYFNSLR
K241-ac EALINAFkRLDNDIS
K241 EALINAFKRLDNDIS
K326 ERELERLKLEHPKNE
K326 ERELERLKLEHPKNE
K331 RLKLEHPKNEAKSVV
K335 EHPKNEAKSVVKQDR
K335 EHPKNEAKSVVKQDR
K339 NEAKSVVKQDRLLGL
K357 FRAFGDVKFKWSIDL
K357 FRAFGDVKFKWSIDL
K359 AFGDVKFKWSIDLQK
K366 KWSIDLQKRVIESGP
Y381 DQLNDNEYTKFIPPN
K383 LNDNEYTKFIPPNYH
K411 HRLRPQDKFLVLATD
K452 PIAVGGYKVTLGQMH
K468 LLTERRAKMSSVFED
K468 LLTERRAKMSSVFED
K502 VDHERLSKMLSLPEE
K502-ub VDHERLSkMLSLPEE
Y514 PEELARMYRDDITII
  rat

 
R43 PPYIPQNRLRYTPHP
Y46 IPQNRLRYTPHPAYA
K77 RYASTPQKFYLTPPQ
Y79 ASTPQKFYLTPPQVN
K90 PQVNSILKANEYSFK
Y94 SILKANEYSFKVPEF
K97 KANEYSFKVPEFDGK
K104 KVPEFDGKNVSSILG
K104 KVPEFDGKNVSSILG
K194 LPILQWHKHPNDYFS
K202 HPNDYFSKEASKLYF
K202 HPNDYFSKEASKLYF
K206 YFSKEASKLYFNGLR
K241 EALINAFKRLDNDIS
K241 EALINAFKRLDNDIS
K326 ERELQRLKLEHPKNE
K326 ERELQRLKLEHPKNE
K331 RLKLEHPKNEAKSVV
K335 EHPKNEAKSVVKQDR
K335 EHPKNEAKSVVKQDR
K339 NEAKSVVKQDRLLGL
K357 FRAFGDVKFKWSIDL
K357 FRAFGDVKFKWSIDL
K359 AFGDVKFKWSIDLQK
K366 KWSIDLQKRVIESGP
Y381 DQLNDNEYTKFIPPN
K383 LNDNEYTKFIPPNYH
K411 HRLRPQDKFLVLATD
K452 PIAVGGYKVTLGQMH
K468 LLTERRAKMSSVFED
K468 LLTERRAKMSSVFED
K502 VDHERLSKMLSLPEE
K502 VDHERLSKMLSLPEE
Y514-p PEELARMyRDDITII
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