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Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene

PDHB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.2 Publications

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.1 Publication

Cofactori

thiamine diphosphate2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891Thiamine pyrophosphate1 Publication

GO - Molecular functioni

  • pyruvate dehydrogenase (acetyl-transferring) activity Source: ProtInc
  • pyruvate dehydrogenase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMetaCyc:HS09727-MONOMER.
ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_2071. Pyruvate metabolism.
REACT_267785. Signaling by Retinoic Acid.
SABIO-RKP11177.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (EC:1.2.4.1)
Short name:
PDHE1-B
Gene namesi
Name:PDHB
Synonyms:PHE1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:8808. PDHB.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • pyruvate dehydrogenase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Pyruvate dehydrogenase E1-beta deficiency (PDHBD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.

See also OMIM:614111
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321Y → C in PDHBD. 1 Publication
Corresponds to variant rs28935769 [ dbSNP | Ensembl ].
VAR_030954
Natural varianti344 – 3441P → S in PDHBD. 1 Publication
Corresponds to variant rs28933391 [ dbSNP | Ensembl ].
VAR_021058

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614111. phenotype.
Orphaneti255138. Pyruvate dehydrogenase E1-beta deficiency.
PharmGKBiPA33152.

Chemistry

DrugBankiDB00119. Pyruvic acid.

Polymorphism and mutation databases

BioMutaiPDHB.
DMDMi134044259.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Mitochondrion2 PublicationsAdd
BLAST
Chaini31 – 359329Pyruvate dehydrogenase E1 component subunit beta, mitochondrialPRO_0000020457Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671PhosphotyrosineBy similarity
Modified residuei354 – 3541N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP11177.
PaxDbiP11177.
PRIDEiP11177.

2D gel databases

REPRODUCTION-2DPAGEIPI00549885.
SWISS-2DPAGEP11177.
UCD-2DPAGEP11177.

PTM databases

PhosphoSiteiP11177.

Expressioni

Gene expression databases

BgeeiP11177.
CleanExiHS_PDHB.
ExpressionAtlasiP11177. baseline and differential.
GenevestigatoriP11177.

Organism-specific databases

HPAiCAB033794.
HPA036744.
HPA036745.

Interactioni

Subunit structurei

Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DLATP105157EBI-1035872,EBI-2959723

Protein-protein interaction databases

BioGridi111188. 50 interactions.
DIPiDIP-37651N.
IntActiP11177. 16 interactions.
MINTiMINT-3007546.
STRINGi9606.ENSP00000307241.

Structurei

Secondary structure

1
359
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 343Combined sources
Helixi35 – 4915Combined sources
Beta strandi53 – 575Combined sources
Turni58 – 614Combined sources
Turni69 – 724Combined sources
Helixi73 – 775Combined sources
Turni79 – 813Combined sources
Beta strandi82 – 843Combined sources
Helixi89 – 10113Combined sources
Beta strandi105 – 1095Combined sources
Helixi113 – 1197Combined sources
Helixi120 – 1245Combined sources
Turni125 – 1295Combined sources
Helixi130 – 1334Combined sources
Turni134 – 1363Combined sources
Beta strandi143 – 1475Combined sources
Helixi156 – 1583Combined sources
Helixi163 – 1675Combined sources
Beta strandi173 – 1753Combined sources
Helixi180 – 19213Combined sources
Beta strandi193 – 1953Combined sources
Beta strandi197 – 2015Combined sources
Turni203 – 2075Combined sources
Beta strandi209 – 2113Combined sources
Helixi214 – 2174Combined sources
Beta strandi229 – 2324Combined sources
Beta strandi235 – 2417Combined sources
Helixi245 – 25713Combined sources
Turni258 – 2603Combined sources
Beta strandi263 – 2675Combined sources
Beta strandi270 – 2723Combined sources
Helixi276 – 28611Combined sources
Beta strandi289 – 2924Combined sources
Helixi301 – 31111Combined sources
Helixi315 – 3173Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi329 – 3313Combined sources
Helixi336 – 3405Combined sources
Helixi346 – 35712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NI4X-ray1.95B/D31-359[»]
2OZLX-ray1.90B/D32-359[»]
3EXEX-ray1.98B/D/F/H31-359[»]
3EXFX-ray3.00B/D/F/H31-359[»]
3EXGX-ray3.012/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z31-359[»]
3EXHX-ray2.44B/D/F/H31-359[»]
3EXIX-ray2.20B31-359[»]
ProteinModelPortaliP11177.
SMRiP11177. Positions 30-359.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11177.

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0022.
GeneTreeiENSGT00530000063423.
HOGENOMiHOG000281450.
HOVERGENiHBG000917.
InParanoidiP11177.
KOiK00162.
OMAiAMKLAMR.
OrthoDBiEOG7KSX8S.
PhylomeDBiP11177.
TreeFamiTF105674.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERiPTHR11624:SF56. PTHR11624:SF56. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P11177-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAVSGLVRR PLREVSGLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD
60 70 80 90 100
EKVFLLGEEV AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA
110 120 130 140 150
MAGLRPICEF MTFNFSMQAI DQVINSAAKT YYMSGGLQPV PIVFRGPNGA
160 170 180 190 200
SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS EDAKGLIKSA IRDNNPVVVL
210 220 230 240 250
ENELMYGVPF EFPPEAQSKD FLIPIGKAKI ERQGTHITVV SHSRPVGHCL
260 270 280 290 300
EAAAVLSKEG VECEVINMRT IRPMDMETIE ASVMKTNHLV TVEGGWPQFG
310 320 330 340 350
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII

FAIKKTLNI
Length:359
Mass (Da):39,233
Last modified:March 6, 2007 - v3
Checksum:iAB459B1259FBDBD3
GO
Isoform 2 (identifier: P11177-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     16-33: Missing.

Note: No experimental confirmation available.

Show »
Length:341
Mass (Da):37,200
Checksum:iB4F137127819BB38
GO
Isoform 3 (identifier: P11177-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     135-152: Missing.

Note: No experimental confirmation available.

Show »
Length:341
Mass (Da):37,514
Checksum:i89F0A32D89507E9D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 135RRPLR → AETPS (PubMed:3422424).Curated
Sequence conflicti43 – 431M → G AA sequence (PubMed:7895732).Curated
Sequence conflicti160 – 1601Q → G (PubMed:3422424).Curated
Sequence conflicti213 – 2219PPEAQSKDF → LRKLSQKIL (PubMed:3422424).Curated
Sequence conflicti213 – 2131P → L in AAA88097 (PubMed:2377599).Curated
Sequence conflicti213 – 2131P → L in BAA14123 (PubMed:2377599).Curated
Sequence conflicti310 – 3123MEG → NGS (PubMed:3422424).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311L → V.2 Publications
VAR_004967
Natural varianti132 – 1321Y → C in PDHBD. 1 Publication
Corresponds to variant rs28935769 [ dbSNP | Ensembl ].
VAR_030954
Natural varianti344 – 3441P → S in PDHBD. 1 Publication
Corresponds to variant rs28933391 [ dbSNP | Ensembl ].
VAR_021058

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei16 – 3318Missing in isoform 2. 1 PublicationVSP_012675Add
BLAST
Alternative sequencei135 – 15218Missing in isoform 3. 1 PublicationVSP_043364Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34479 mRNA. Translation: AAA36428.1.
M19123 mRNA. Translation: AAA60052.1. Sequence problems.
M54788 mRNA. Translation: AAA60053.1.
M34055 mRNA. Translation: AAA60233.1.
M34056 mRNA. Translation: AAA60054.1.
D90086 Genomic DNA. Translation: BAA14123.1.
J03576 mRNA. Translation: AAA88097.1.
AL117618 mRNA. Translation: CAB56017.1.
CR541911 mRNA. Translation: CAG46709.1.
AK293153 mRNA. Translation: BAG56698.1.
AK313022 mRNA. Translation: BAG35857.1.
AC135507 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65371.1.
BC000439 mRNA. Translation: AAH00439.1.
BC001924 mRNA. Translation: AAH01924.1.
X57778 mRNA. Translation: CAA40924.1.
CCDSiCCDS2890.1. [P11177-1]
CCDS54602.1. [P11177-3]
PIRiJU0145. DEHUPB.
RefSeqiNP_000916.2. NM_000925.3. [P11177-1]
NP_001166939.1. NM_001173468.1. [P11177-3]
UniGeneiHs.161357.

Genome annotation databases

EnsembliENST00000302746; ENSP00000307241; ENSG00000168291. [P11177-1]
ENST00000383714; ENSP00000373220; ENSG00000168291. [P11177-2]
ENST00000485460; ENSP00000417267; ENSG00000168291. [P11177-3]
GeneIDi5162.
KEGGihsa:5162.
UCSCiuc003dke.4. human. [P11177-1]
uc003dkg.4. human. [P11177-2]
uc011bff.2. human. [P11177-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34479 mRNA. Translation: AAA36428.1.
M19123 mRNA. Translation: AAA60052.1. Sequence problems.
M54788 mRNA. Translation: AAA60053.1.
M34055 mRNA. Translation: AAA60233.1.
M34056 mRNA. Translation: AAA60054.1.
D90086 Genomic DNA. Translation: BAA14123.1.
J03576 mRNA. Translation: AAA88097.1.
AL117618 mRNA. Translation: CAB56017.1.
CR541911 mRNA. Translation: CAG46709.1.
AK293153 mRNA. Translation: BAG56698.1.
AK313022 mRNA. Translation: BAG35857.1.
AC135507 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65371.1.
BC000439 mRNA. Translation: AAH00439.1.
BC001924 mRNA. Translation: AAH01924.1.
X57778 mRNA. Translation: CAA40924.1.
CCDSiCCDS2890.1. [P11177-1]
CCDS54602.1. [P11177-3]
PIRiJU0145. DEHUPB.
RefSeqiNP_000916.2. NM_000925.3. [P11177-1]
NP_001166939.1. NM_001173468.1. [P11177-3]
UniGeneiHs.161357.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NI4X-ray1.95B/D31-359[»]
2OZLX-ray1.90B/D32-359[»]
3EXEX-ray1.98B/D/F/H31-359[»]
3EXFX-ray3.00B/D/F/H31-359[»]
3EXGX-ray3.012/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z31-359[»]
3EXHX-ray2.44B/D/F/H31-359[»]
3EXIX-ray2.20B31-359[»]
ProteinModelPortaliP11177.
SMRiP11177. Positions 30-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111188. 50 interactions.
DIPiDIP-37651N.
IntActiP11177. 16 interactions.
MINTiMINT-3007546.
STRINGi9606.ENSP00000307241.

Chemistry

DrugBankiDB00119. Pyruvic acid.

PTM databases

PhosphoSiteiP11177.

Polymorphism and mutation databases

BioMutaiPDHB.
DMDMi134044259.

2D gel databases

REPRODUCTION-2DPAGEIPI00549885.
SWISS-2DPAGEP11177.
UCD-2DPAGEP11177.

Proteomic databases

MaxQBiP11177.
PaxDbiP11177.
PRIDEiP11177.

Protocols and materials databases

DNASUi5162.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302746; ENSP00000307241; ENSG00000168291. [P11177-1]
ENST00000383714; ENSP00000373220; ENSG00000168291. [P11177-2]
ENST00000485460; ENSP00000417267; ENSG00000168291. [P11177-3]
GeneIDi5162.
KEGGihsa:5162.
UCSCiuc003dke.4. human. [P11177-1]
uc003dkg.4. human. [P11177-2]
uc011bff.2. human. [P11177-3]

Organism-specific databases

CTDi5162.
GeneCardsiGC03M058388.
HGNCiHGNC:8808. PDHB.
HPAiCAB033794.
HPA036744.
HPA036745.
MIMi179060. gene.
614111. phenotype.
neXtProtiNX_P11177.
Orphaneti255138. Pyruvate dehydrogenase E1-beta deficiency.
PharmGKBiPA33152.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0022.
GeneTreeiENSGT00530000063423.
HOGENOMiHOG000281450.
HOVERGENiHBG000917.
InParanoidiP11177.
KOiK00162.
OMAiAMKLAMR.
OrthoDBiEOG7KSX8S.
PhylomeDBiP11177.
TreeFamiTF105674.

Enzyme and pathway databases

BioCyciMetaCyc:HS09727-MONOMER.
ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_2071. Pyruvate metabolism.
REACT_267785. Signaling by Retinoic Acid.
SABIO-RKP11177.

Miscellaneous databases

ChiTaRSiPDHB. human.
EvolutionaryTraceiP11177.
GeneWikiiPyruvate_dehydrogenase_(lipoamide)_beta.
GenomeRNAii5162.
NextBioi19970.
PROiP11177.
SOURCEiSearch...

Gene expression databases

BgeeiP11177.
CleanExiHS_PDHB.
ExpressionAtlasiP11177. baseline and differential.
GenevestigatoriP11177.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERiPTHR11624:SF56. PTHR11624:SF56. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and cDNA sequence of the beta-subunit component of human pyruvate dehydrogenase complex."
    Ho L., Patel M.S.
    Gene 86:297-302(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Isolation, characterization and chromosomal localization of cDNA clones for the E1 beta subunit of the pyruvate dehydrogenase complex."
    Chun K., MacKay N., Willard H.F., Robinson B.H.
    Eur. J. Biochem. 194:587-592(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Characterization of two cDNA clones for pyruvate dehydrogenase E1 beta subunit and its regulation in tricarboxylic acid cycle-deficient fibroblast."
    Huh T.L., Casazza J.P., Huh J.W., Chi Y.T., Song B.J.
    J. Biol. Chem. 265:13320-13326(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-31.
  4. "Molecular cloning and characterization of human pyruvate dehydrogenase beta subunit gene."
    Koike K., Urata Y., Koike M.
    Proc. Natl. Acad. Sci. U.S.A. 87:5594-5597(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  5. "Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase."
    Koike K., Ohta S., Urata Y., Kagawa Y., Koike M.
    Proc. Natl. Acad. Sci. U.S.A. 85:41-45(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-31.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Brain cortex.
  9. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  12. "Identification of a cDNA clone for the beta-subunit of the pyruvate dehydrogenase component of human pyruvate dehydrogenase complex."
    Ho L., Javed A.A., Pepin R.A., Thekkumkara T.J., Raefsky C., Mole J.E., Caliendo A.M., Kwon M.S., Kerr D.S., Patel M.S.
    Biochem. Biophys. Res. Commun. 150:904-908(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 23-69.
  13. "The human myocardial two-dimensional gel protein database: update 1994."
    Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.
    Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-43.
    Tissue: Heart.
  14. "Isolation of tryptic fragment of antigen from mitochondrial inner membrane proteins reacting with antimitochondrial antibody in sera of patients with primary biliary cirrhosis."
    Muno D., Kominami E., Ishii H., Usui K., Saifuku K., Sakakibara Y., Namihisa T.
    Hepatology 11:16-23(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-55.
  15. "Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components."
    Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.
    J. Biol. Chem. 279:6921-6933(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase."
    Ciszak E.M., Korotchkina L.G., Dominiak P.M., Sidhu S., Patel M.S.
    J. Biol. Chem. 278:21240-21246(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 32-359 IN COMPLEX WITH THIAMINE PYROPHOSPHATE, COFACTOR.
  19. "Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex."
    Seifert F., Ciszak E., Korotchkina L., Golbik R., Spinka M., Dominiak P., Sidhu S., Brauer J., Patel M.S., Tittmann K.
    Biochemistry 46:6277-6287(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 32-359, SUBUNIT, FUNCTION.
  20. "Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops."
    Kato M., Wynn R.M., Chuang J.L., Tso S.C., Machius M., Li J., Chuang D.T.
    Structure 16:1849-1859(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 31-359, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, FUNCTION.
  21. "Mutations in the gene for the E1beta subunit: a novel cause of pyruvate dehydrogenase deficiency."
    Brown R.M., Head R.A., Boubriak I.I., Leonard J.V., Thomas N.H., Brown G.K.
    Hum. Genet. 115:123-127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PDHBD CYS-132 AND SER-344.

Entry informationi

Entry nameiODPB_HUMAN
AccessioniPrimary (citable) accession number: P11177
Secondary accession number(s): B2R7L0
, B4DDD7, Q6FH45, Q9BQ27, Q9UFK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 6, 2007
Last modified: May 27, 2015
This is version 181 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.