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Protein Page:
PDHB (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
PDHB the beta subunit of pyruvate dehydrogenase (PDH), a 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. Defects in PDHB are a cause of pyruvate dehydrogenase E1 component deficiency (PDHE1 deficiency), the most common enzyme defect in patients with primary lactic acidosis. It is associated with variable clinical phenotypes ranging from neonatal death to prolonged survival complicated by developmental delay, seizures, ataxia, apnea, and in some cases to an X-linked form of Leigh syndrome (LS). Two alternatively spliced human isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Carbohydrate Metabolism - citrate (TCA) cycle; Carbohydrate Metabolism - butanoate; Oxidoreductase; Carbohydrate Metabolism - glycolysis and gluconeogenesis; EC 1.2.4.1; Mitochondrial; Carbohydrate Metabolism - pyruvate; Amino Acid Metabolism - valine, leucine and isoleucine biosynthesis
Cellular Component: mitochondrial matrix; pyruvate dehydrogenase complex; nucleus
Molecular Function: pyruvate dehydrogenase activity; protein binding; pyruvate dehydrogenase (acetyl-transferring) activity
Biological Process: acetyl-CoA biosynthetic process from pyruvate; cellular metabolic process; tricarboxylic acid cycle; glucose metabolic process; regulation of acetyl-CoA biosynthetic process from pyruvate; pyruvate metabolic process
Reference #:  P11177 (UniProtKB)
Alt. Names/Synonyms: DKFZp564K0164; ODPB; PDHB; PDHE1-B; PHE1B; pyruvate dehydrogenase (lipoamide) beta; Pyruvate dehydrogenase E1 component subunit beta, mitochondrial; pyruvate dehydrogenase, E1 beta polypeptide
Gene Symbols: PDHB
Molecular weight: 39,233 Da
Basal Isoelectric point: 6.2  Predict pI for various phosphorylation states
CST Pathways:  Warburg Effect
Select Structure to View Below

PDHB

Protein Structure Not Found.


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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 T26-p LKRRFHWtAPAALQV
0 1 T34-p APAALQVtVRDAINQ
0 1 K52 EELERDEKVFLLGEE
0 1 K52 EELERDEKVFLLGEE
0 5 Y63-p LGEEVAQyDGAYkVS
0 1 Y67 VAQyDGAYkVSRGLW
0 2 K68-ac AQyDGAYkVSRGLWK
0 1 K184 PWNSEDAKGLIKSAI
0 2 K227 DFLIPIGKAKIERQG
0 1 K227 DFLIPIGKAKIERQG
0 1 K227 DFLIPIGKAKIERQG
0 1 T270-p CEVINMRtIRPMDME
0 1 T278-p IRPMDMEtIEAsVMK
0 1 S282-p DMEtIEAsVMKTNHL
0 2 K336-ac DVPMPYAkILEDNSI
0 2 K336-ub DVPMPYAkILEDNSI
0 1 K336 DVPMPYAKILEDNSI
0 2 K347-ac DNSIPQVkDIIFAIk
0 1 K347-sc DNSIPQVkDIIFAIk
0 38 K354-ac kDIIFAIkKTLNI__
0 1 K354-sc kDIIFAIkKTLNI__
  mouse

 
S26 LKRRFHRSAPAAVQL
T34 APAAVQLTVREAINQ
K52-ac EELERDEkVFLLGEE
K52-sc EELERDEkVFLLGEE
Y63 LGEEVAQYDGAykVS
Y67-p VAQYDGAykVSRGLW
K68-ac AQYDGAykVSRGLWK
K184-ub PWNSEDAkGLIKSAI
K227 DFLIPIGKAKIERQG
K227-ub DFLIPIGkAKIERQG
K227-sc DFLIPIGkAKIERQG
T270 CEVINLRTIRPMDIE
A278 IRPMDIEAIEASVMK
S282 DIEAIEASVMKTNHL
K336-ac DVPMPYAkVLEDNSV
K336-ub DVPMPYAkVLEDNSV
K336-sc DVPMPYAkVLEDNSV
K347-ac DNSVPQVkDIIFAVk
K347-sc DNSVPQVkDIIFAVk
K354-ac kDIIFAVkKTLNI__
K354-sc kDIIFAVkKTLNI__
  rat

 
S26 LKRRFHRSAPAAVQL
T34 APAAVQLTVREAINQ
K52 EELERDEKVFLLGEE
K52 EELERDEKVFLLGEE
Y63 LGEEVAQYDGAYKVS
Y67 VAQYDGAYKVSRGLW
K68 AQYDGAYKVSRGLWK
K184 PWNSEDAKGLIKSAI
K227-ac DFLIPIGkAKIERQG
K227 DFLIPIGKAKIERQG
K227 DFLIPIGKAKIERQG
T270 CEVINLRTIRPMDIE
A278 IRPMDIEAIEASVMK
S282 DIEAIEASVMKTNHL
K336 DVPMPYAKILEDNSI
K336 DVPMPYAKILEDNSI
K336 DVPMPYAKILEDNSI
K347 DNSIPQVKDIIFAIk
K347 DNSIPQVKDIIFAIk
K354-ac KDIIFAIkKTLNI__
K354 KDIIFAIKKTLNI__
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