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P11177

- ODPB_HUMAN

UniProt

P11177 - ODPB_HUMAN

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Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene

PDHB

Organism
Homo sapiens (Human)
Status
Reviewed - 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 pyrophosphate.2 Publications

Sites

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

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: ProtInc
  2. pyruvate dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
  2. cellular metabolic process Source: Reactome
  3. glucose metabolic process Source: UniProtKB-KW
  4. pyruvate metabolic process Source: Reactome
  5. regulation of acetyl-CoA biosynthetic process from pyruvate Source: Reactome
  6. small molecule metabolic process Source: Reactome
  7. tricarboxylic acid cycle Source: UniProtKB
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.
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: Chromosome 3

Organism-specific databases

HGNCiHGNC:8808. PDHB.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrial matrix Source: Reactome
  3. nucleus Source: UniProt
  4. pyruvate dehydrogenase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Pyruvate dehydrogenase E1-beta deficiency (PDHBD) [MIM:614111]: An 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.

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

HPAiHPA036744.

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. 52 interactions.
DIPiDIP-37651N.
IntActiP11177. 15 interactions.
MINTiMINT-3007546.
STRINGi9606.ENSP00000307241.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiDPKVFVM.
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. Align

Isoform 1 (identifier: P11177) [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:
EMBL
GenBank
DDBJ
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]

Polymorphism databases

DMDMi134044259.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2890.1. [P11177-1 ]
CCDS54602.1. [P11177-3 ]
PIRi JU0145. DEHUPB.
RefSeqi NP_000916.2. NM_000925.3. [P11177-1 ]
NP_001166939.1. NM_001173468.1. [P11177-3 ]
UniGenei Hs.161357.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NI4 X-ray 1.95 B/D 31-359 [» ]
2OZL X-ray 1.90 B/D 32-359 [» ]
3EXE X-ray 1.98 B/D/F/H 31-359 [» ]
3EXF X-ray 3.00 B/D/F/H 31-359 [» ]
3EXG X-ray 3.01 2/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z 31-359 [» ]
3EXH X-ray 2.44 B/D/F/H 31-359 [» ]
3EXI X-ray 2.20 B 31-359 [» ]
ProteinModelPortali P11177.
SMRi P11177. Positions 30-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111188. 52 interactions.
DIPi DIP-37651N.
IntActi P11177. 15 interactions.
MINTi MINT-3007546.
STRINGi 9606.ENSP00000307241.

Chemistry

DrugBanki DB00119. Pyruvic acid.

PTM databases

PhosphoSitei P11177.

Polymorphism databases

DMDMi 134044259.

2D gel databases

REPRODUCTION-2DPAGE IPI00549885.
SWISS-2DPAGE P11177.
UCD-2DPAGE P11177.

Proteomic databases

MaxQBi P11177.
PaxDbi P11177.
PRIDEi P11177.

Protocols and materials databases

DNASUi 5162.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302746 ; ENSP00000307241 ; ENSG00000168291 . [P11177-1 ]
ENST00000383714 ; ENSP00000373220 ; ENSG00000168291 . [P11177-2 ]
ENST00000485460 ; ENSP00000417267 ; ENSG00000168291 . [P11177-3 ]
GeneIDi 5162.
KEGGi hsa:5162.
UCSCi uc003dke.4. human. [P11177-1 ]
uc003dkg.4. human. [P11177-2 ]
uc011bff.2. human. [P11177-3 ]

Organism-specific databases

CTDi 5162.
GeneCardsi GC03M058388.
HGNCi HGNC:8808. PDHB.
HPAi HPA036744.
MIMi 179060. gene.
614111. phenotype.
neXtProti NX_P11177.
Orphaneti 255138. Pyruvate dehydrogenase E1-beta deficiency.
PharmGKBi PA33152.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0022.
GeneTreei ENSGT00530000063423.
HOGENOMi HOG000281450.
HOVERGENi HBG000917.
InParanoidi P11177.
KOi K00162.
OMAi DPKVFVM.
OrthoDBi EOG7KSX8S.
PhylomeDBi P11177.
TreeFami TF105674.

Enzyme and pathway databases

BioCyci MetaCyc:HS09727-MONOMER.
Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_2071. Pyruvate metabolism.
SABIO-RK P11177.

Miscellaneous databases

ChiTaRSi PDHB. human.
EvolutionaryTracei P11177.
GeneWikii Pyruvate_dehydrogenase_(lipoamide)_beta.
GenomeRNAii 5162.
NextBioi 19970.
PROi P11177.
SOURCEi Search...

Gene expression databases

Bgeei P11177.
CleanExi HS_PDHB.
ExpressionAtlasi P11177. baseline and differential.
Genevestigatori P11177.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProi IPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view ]
PANTHERi PTHR11624:SF56. PTHR11624:SF56. 1 hit.
Pfami PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view ]
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNeti Search...

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. "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.
  18. "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.
  19. "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.
  20. "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: October 29, 2014
This is version 174 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