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P11177 (ODPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Short name=PDHE1-B
EC=1.2.4.1
Gene names
Name:PDHB
Synonyms:PHE1B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.18 Ref.19

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. Ref.19

Cofactor

Thiamine pyrophosphate. Ref.17 Ref.19

Subunit structure

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. Ref.15 Ref.18 Ref.19

Subcellular location

Mitochondrion matrix.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
Tricarboxylic acid cycle
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacetyl-CoA biosynthetic process from pyruvate

Inferred from direct assay Ref.19. Source: UniProtKB

cellular metabolic process

Traceable author statement. Source: Reactome

glucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

pyruvate metabolic process

Traceable author statement. Source: Reactome

regulation of acetyl-CoA biosynthetic process from pyruvate

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

tricarboxylic acid cycle

Inferred from direct assay Ref.19. Source: UniProtKB

   Cellular_componentmitochondrial matrix

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

pyruvate dehydrogenase complex

Inferred from direct assay Ref.19. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 18206651. Source: IntAct

pyruvate dehydrogenase (acetyl-transferring) activity

Traceable author statement Ref.3. Source: ProtInc

pyruvate dehydrogenase activity

Inferred from direct assay Ref.19. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DLATP105157EBI-1035872,EBI-2959723

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11177-1)

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.
Isoform 2 (identifier: P11177-2)

The sequence of this isoform differs from the canonical sequence as follows:
     16-33: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P11177-3)

The sequence of this isoform differs from the canonical sequence as follows:
     135-152: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3030Mitochondrion Ref.13 Ref.14
Chain31 – 359329Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
PRO_0000020457

Sites

Binding site891Thiamine pyrophosphate

Amino acid modifications

Modified residue671Phosphotyrosine By similarity
Modified residue3541N6-acetyllysine By similarity

Natural variations

Alternative sequence16 – 3318Missing in isoform 2.
VSP_012675
Alternative sequence135 – 15218Missing in isoform 3.
VSP_043364
Natural variant311L → V. Ref.3 Ref.5
VAR_004967
Natural variant1321Y → C in PDHBD. Ref.20
Corresponds to variant rs28935769 [ dbSNP | Ensembl ].
VAR_030954
Natural variant3441P → S in PDHBD. Ref.20
Corresponds to variant rs28933391 [ dbSNP | Ensembl ].
VAR_021058

Experimental info

Sequence conflict9 – 135RRPLR → AETPS Ref.5
Sequence conflict431M → G AA sequence Ref.13
Sequence conflict1601Q → G Ref.5
Sequence conflict213 – 2219PPEAQSKDF → LRKLSQKIL Ref.5
Sequence conflict2131P → L in AAA88097. Ref.4
Sequence conflict2131P → L in BAA14123. Ref.4
Sequence conflict310 – 3123MEG → NGS Ref.5

Secondary structure

..................................................................... 359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 6, 2007. Version 3.
Checksum: AB459B1259FBDBD3

FASTA35939,233
        10         20         30         40         50         60 
MAAVSGLVRR PLREVSGLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD EKVFLLGEEV 

        70         80         90        100        110        120 
AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI 

       130        140        150        160        170        180 
DQVINSAAKT YYMSGGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS 

       190        200        210        220        230        240 
EDAKGLIKSA IRDNNPVVVL ENELMYGVPF EFPPEAQSKD FLIPIGKAKI ERQGTHITVV 

       250        260        270        280        290        300 
SHSRPVGHCL EAAAVLSKEG VECEVINMRT IRPMDMETIE ASVMKTNHLV TVEGGWPQFG 

       310        320        330        340        350 
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII FAIKKTLNI 

« Hide

Isoform 2 [UniParc].

Checksum: B4F137127819BB38
Show »

FASTA34137,200
Isoform 3 [UniParc].

Checksum: 89F0A32D89507E9D
Show »

FASTA34137,514

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2890.1. [P11177-1]
CCDS54602.1. [P11177-3]
PIRDEHUPB. JU0145.
RefSeqNP_000916.2. NM_000925.3. [P11177-1]
NP_001166939.1. NM_001173468.1. [P11177-3]
UniGeneHs.161357.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP11177.
SMRP11177. Positions 30-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111188. 34 interactions.
DIPDIP-37651N.
IntActP11177. 15 interactions.
MINTMINT-3007546.
STRING9606.ENSP00000307241.

Chemistry

DrugBankDB00157. NADH.
DB00119. Pyruvic acid.

PTM databases

PhosphoSiteP11177.

Polymorphism databases

DMDM134044259.

2D gel databases

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

Proteomic databases

MaxQBP11177.
PaxDbP11177.
PRIDEP11177.

Protocols and materials databases

DNASU5162.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302746; ENSP00000307241; ENSG00000168291. [P11177-1]
ENST00000383714; ENSP00000373220; ENSG00000168291. [P11177-2]
ENST00000485460; ENSP00000417267; ENSG00000168291. [P11177-3]
GeneID5162.
KEGGhsa:5162.
UCSCuc003dke.4. human. [P11177-1]
uc003dkg.4. human. [P11177-2]
uc011bff.2. human. [P11177-3]

Organism-specific databases

CTD5162.
GeneCardsGC03M058388.
HGNCHGNC:8808. PDHB.
HPAHPA036744.
MIM179060. gene.
614111. phenotype.
neXtProtNX_P11177.
Orphanet255138. Pyruvate dehydrogenase E1-beta deficiency.
PharmGKBPA33152.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0022.
HOGENOMHOG000281450.
HOVERGENHBG000917.
InParanoidP11177.
KOK00162.
OMADPKVFVM.
OrthoDBEOG7KSX8S.
PhylomeDBP11177.
TreeFamTF105674.

Enzyme and pathway databases

BioCycMetaCyc:HS09727-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP11177.

Gene expression databases

ArrayExpressP11177.
BgeeP11177.
CleanExHS_PDHB.
GenevestigatorP11177.

Family and domain databases

Gene3D3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProIPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERPTHR11624:SF56. PTHR11624:SF56. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPDHB. human.
EvolutionaryTraceP11177.
GeneWikiPyruvate_dehydrogenase_(lipoamide)_beta.
GenomeRNAi5162.
NextBio19970.
PROP11177.
SOURCESearch...

Entry information

Entry nameODPB_HUMAN
AccessionPrimary (citable) accession number: P11177
Secondary accession number(s): B2R7L0 expand/collapse secondary AC list , B4DDD7, Q6FH45, Q9BQ27, Q9UFK3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM