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Protein Page:
PDHA2 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PDHA2 a testis-specific mitochondrial matrix enzyme that catalyzes the oxidative decarboxylation of pyruvate, producing acetyl-CoA and CO2. A key enzyme in controlling the balance between lipid and glucose oxidation depending on substrate availability. The pyruvate dehydrogenase (PDH) holoenzyme is a multi-enzyme complex (PDHC) that contains 20-30 copies of pyruvate decarboxylase tetramers (2 alpha:2 beta)(E1), 60 copies of dihydrolipoamide acetyltransferase (E2), six homodimers of dihydrolipoamide dehydrogenase (E3), plus E3 binding proteins. The activity of PDH is tightly regulated by phosphorylation. The phosphorylation of at least one of three specific serine residues in E1 subunit by PDHK inactivates the PDHC, while dephosphorylation by PDP restores its activity. Expressed in postmeiotic spermatogenic cells. Note: This description may include information from UniProtKB.
Protein type: EC 1.2.4.1; Oxidoreductase; Carbohydrate Metabolism - glycolysis and gluconeogenesis; Carbohydrate Metabolism - citrate (TCA) cycle; Amino Acid Metabolism - valine, leucine and isoleucine biosynthesis; Mitochondrial; Carbohydrate Metabolism - pyruvate; Carbohydrate Metabolism - butanoate
Chromosomal Location of Human Ortholog: 4q22-q23
Cellular Component: nucleus
Molecular Function: pyruvate dehydrogenase (acetyl-transferring) activity
Biological Process: pyruvate metabolic process
Reference #:  P29803 (UniProtKB)
Alt. Names/Synonyms: MGC149517; MGC149518; ODPAT; PDHA2; PDHAL; PDHE1-A type II; pyruvate dehydrogenase (lipoamide) alpha 2; pyruvate dehydrogenase E1 alpha 2; Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial; pyruvate dehydrogenase, E1-alpha polypeptide, testis specific
Gene Symbols: PDHA2
Molecular weight: 42,933 Da
Basal Isoelectric point: 8.76  Predict pI for various phosphorylation states
CST Pathways:  Warburg Effect
Select Structure to View Below

PDHA2

Protein Structure Not Found.


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Sites Implicated In
enzymatic activity, induced: S291‑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



 LTP 

LTP: 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.


 HTP 

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


       human

 
0 1 K16‑sm VLRRVAQkSARRVLV
0 1 A24 SARRVLVASRNSSND
0 2 K37‑ac NDATFEIkKCDLyLL
0 1 Y42‑p EIkKCDLyLLEEGPP
0 1 K61 LTRAEGLKyyRMMLT
0 1 Y62‑p TRAEGLKyyRMMLTV
0 1 Y63‑p RAEGLKyyRMMLTVR
0 15 K75‑ac TVRRMELkADQLYkQ
0 11 K81‑ac LkADQLYkQKFIRGF
0 2 K81‑sc LkADQLYkQKFIRGF
0 1 K83 ADQLYkQKFIRGFCH
0 1 R130 YTRGLSVRSILAELT
0 3 Y154‑p KGGSMHMyTKNFYGG
1 0 S230‑p NLYGMGTsTERAAAS
0 1 K242 AASPDYYKRGNFIPG
0 24 K275‑ac ANYCRSGkGPILMEL
0 386 Y287‑p MELQTYRyHGHsMsD
1 657 S291‑p TYRyHGHsMsDPGVs
0 229 S293‑p RyHGHsMsDPGVsyR
1 448 S298‑p sMsDPGVsyRTREEI
0 1181 Y299‑p MsDPGVsyRTREEIQ
0 1 K311 EIQEVRSKRDPIIIL
0 1 K334 LATVEELKEIGAEVR
0 2 R341 KEIGAEVRKEIDDAA
0 1 P380 FEVRGANPWIKFKSV
  mouse

 
K19 VFSGMVQKPALRGLL
S27‑p PALRGLLsSLKFSND
K40‑ac NDATCDIkKCDLYRL
Y45 DIkKCDLYRLEEGPP
K64 LTRAEALKYYRTMQV
Y65 TRAEALKYYRTMQVI
Y66 RAEALKYYRTMQVIR
K78‑ac VIRRMELkADQLYkQ
K84‑ac LkADQLYkQkFIRGF
K84‑sc LkADQLYkQkFIRGF
K86‑ac ADQLYkQkFIRGFCH
K133 YTRGLSVKSILAELT
Y157‑p KGGSMHMyGKNFYGG
S233 NLYGMGTSNERSAAS
K245‑ac AASTDYHkKGFIIPG
K278 ADHCRSGKGPIVMEL
Y290 MELQTYRYHGHsMsD
S294‑p TYRYHGHsMsDPGIs
S296‑p RYHGHsMsDPGIsYR
S301‑p sMsDPGIsYRSREEV
Y302 MsDPGIsYRSREEVH
K314 EVHNVRSKSDPIMLL
K337 LSNIEELKEIDADVk
K344‑ac KEIDADVkKEVEDAA
K383 FEVRGAHKWLKYKSH
  rat

 
K19 VFSGMVQKPALRGLL
S27 PALRGLLSSLKFSND
K40 NDATCDIKKCDLYLL
Y45 DIKKCDLYLLEQGPP
K64‑ac LTREEALkYYRNMQV
Y65 TREEALkYYRNMQVI
Y66 REEALkYYRNMQVIR
K78‑ac VIRRMELkADQLYkQ
K84‑ac LkADQLYkQKFIRGF
K84 LkADQLYKQKFIRGF
K86 ADQLYkQKFIRGFCH
K133‑ac YTRGLSVkSILAELT
Y157 KGGSMHMYAKNFYGG
A233 NRYGMGTAIERSAAS
K245 AASTDYHKKGFVIPG
K278 ADHCRSGKGPIVMEL
Y290 MELQTYRYHGHsMSD
S294‑p TYRYHGHsMSDPGIS
S296 RYHGHsMSDPGISYR
S301 sMSDPGISYRTREEV
Y302 MSDPGISYRTREEVQ
K314‑ac EVQNVRSkSDPIMLL
K337‑ac LSSVEELkEIDADVk
K344‑ac kEIDADVkKEVEEAA
K383‑ac FEVRGAHkWLKFKSV
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