UniProtKB - P11177 (ODPB_HUMAN)
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- BLAST>sp|P11177|ODPB_HUMAN Pyruvate dehydrogenase E1 component subunit beta, mitochondrial OS=Homo sapiens OX=9606 GN=PDHB PE=1 SV=3 MAAVSGLVRRPLREVSGLLKRRFHWTAPAALQVTVRDAINQGMDEELERDEKVFLLGEEV AQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAI DQVINSAAKTYYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNS EDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVV SHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFG VGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAIKKTLNI
- Align
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
PDHB
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.21"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. - Ref.22"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.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.22"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.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.20"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. - Ref.22"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.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 89 | Thiamine pyrophosphate1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 319 | Important for interaction with DLAT1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- pyruvate dehydrogenase (acetyl-transferring) activity Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- pyruvate dehydrogenase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- glucose metabolic process Source: UniProtKB-KW
- mitochondrial acetyl-CoA biosynthetic process from pyruvate Source: MGI <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence <br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ic">GO evidence code guide</a></p> Inferred by curatori
- tricarboxylic acid cycle Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Oxidoreductase |
| Biological process | Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle |
| Ligand | Pyruvate, Thiamine pyrophosphate |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS09727-MONOMER |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-204174 Regulation of pyruvate dehydrogenase (PDH) complex R-HSA-389661 Glyoxylate metabolism and glycine degradation R-HSA-5362517 Signaling by Retinoic Acid R-HSA-70268 Pyruvate metabolism |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P11177 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (EC:1.2.4.1)Short name: PDHE1-B |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:PDHB Synonyms:PHE1B |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000168291.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:8808 PDHB |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 179060 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P11177 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Mitochondrion
Mitochondrion
- mitochondrial matrix Source: Reactome
- mitochondrion Source: HPA
Nucleus
- nucleoplasm Source: HPA
- nucleus Source: UniProtKBInferred from high throughput direct assayi
Other locations
- pyruvate dehydrogenase complex Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Mitochondrion<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Pyruvate dehydrogenase E1-beta deficiency (PDHBD)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.23"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.
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]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_030954 | 132 | Y → C in PDHBD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_021058 | 344 | P → S in PDHBD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 259 | E → A or Q: Does not affect interaction with DLAT. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 262 | E → A or Q: Does not affect interaction with DLAT. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 264 | E → A or Q: Does not affect interaction with DLAT. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 319 | D → A: Inhibits interaction with DLAT. Does not affect pyruvate decarboxylase activity. Loss of multienzyme pyruvate dehydrogenase complex activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 319 | D → N: Reduces interaction with DLAT. Reduces multienzyme pyruvate dehydrogenase complex activity. Does not affect pyruvate decarboxylase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 359 | I → A: Reduces pyruvate decarboxylase and multienzyme pyruvate dehydrogenase complex activity. Does not affect interaction with DLAT. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 359 | Missing : Reduces pyruvate decarboxylase and multienzyme pyruvate dehydrogenase complex activity. Does not affect interaction with DLAT. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 5162 |
MalaCards human disease database More...MalaCardsi | PDHB |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 614111 phenotype |
Open Targets More...OpenTargetsi | ENSG00000168291 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 255138 Pyruvate dehydrogenase E1-beta deficiency |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33152 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB00157 NADH DB00119 Pyruvic acid |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PDHB |
Domain mapping of disease mutations (DMDM) More...DMDMi | 134044259 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei | 1 – 30 | Mitochondrion2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 30 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000020457 | 31 – 359 | Pyruvate dehydrogenase E1 component subunit beta, mitochondrialAdd BLAST | 329 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 67 | PhosphotyrosineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 354 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P11177 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P11177 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P11177 |
PeptideAtlas More...PeptideAtlasi | P11177 |
PRoteomics IDEntifications database More...PRIDEi | P11177 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 52715 52716 [P11177-2] 52717 [P11177-3] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P11177-1 [P11177-1] |
2D gel databases
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00549885 |
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P11177 |
University College Dublin 2-DE Proteome Database More...UCD-2DPAGEi | P11177 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P11177 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P11177 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P11177 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000168291 |
CleanEx database of gene expression profiles More...CleanExi | HS_PDHB |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P11177 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P11177 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB033794 HPA036744 HPA036745 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.16"Interaction of E1 and E3 components with the core proteins of the human pyruvate dehydrogenase complex."
Patel M.S., Korotchkina L.G., Sidhu S.
J. Mol. Catal., B Enzym. 61:2-6(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH DLAT, MUTAGENESIS OF GLU-259; GLU-262; GLU-264; ASP-319 AND ILE-359. - Ref.20"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. - Ref.21"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. - Ref.22"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.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| DLAT | P10515 | 7 | EBI-1035872,EBI-2959723 | |
| PDHA1 | P08559 | 3 | EBI-1035872,EBI-715747 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 111188, 72 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-376 Pyruvate dehydrogenase E1 heterotetramer |
Database of interacting proteins More...DIPi | DIP-37651N |
Protein interaction database and analysis system More...IntActi | P11177, 30 interactors |
Molecular INTeraction database More...MINTi | P11177 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000307241 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 32 – 34 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 35 – 49 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 53 – 57 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 58 – 61 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 69 – 72 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 73 – 77 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 79 – 81 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 82 – 84 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 89 – 101 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 105 – 109 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 113 – 119 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 120 – 124 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 125 – 129 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 130 – 133 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 134 – 136 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 143 – 147 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 156 – 158 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 163 – 167 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 173 – 175 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 180 – 192 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 193 – 195 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 197 – 201 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 203 – 207 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 209 – 211 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 214 – 217 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 229 – 232 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 235 – 241 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 245 – 257 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 258 – 260 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 263 – 267 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 270 – 272 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 276 – 286 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 289 – 292 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 301 – 311 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 315 – 317 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 323 – 325 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 329 – 331 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 336 – 340 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 346 – 357 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P11177 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P11177 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P11177 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Transit peptidePhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0524 Eukaryota COG0022 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000063423 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000281450 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000917 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P11177 |
KEGG Orthology (KO) More...KOi | K00162 |
Identification of Orthologs from Complete Genome Data More...OMAi | SRMRHHC |
Database of Orthologous Groups More...OrthoDBi | EOG091G0D37 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P11177 |
TreeFam database of animal gene trees More...TreeFami | TF105674 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.50.920, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029061 THDP-binding IPR009014 Transketo_C/PFOR_II IPR005475 Transketolase-like_Pyr-bd IPR033248 Transketolase_C |
Pfam protein domain database More...Pfami | View protein in Pfam PF02779 Transket_pyr, 1 hit PF02780 Transketolase_C, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00861 Transket_pyr, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52518 SSF52518, 1 hit SSF52922 SSF52922, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded 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.
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
The sequence of this isoform differs from the canonical sequence as follows:
16-33: Missing.
10 20 30 40 50
MAAVSGLVRR PLREVTVRDA INQGMDEELE RDEKVFLLGE EVAQYDGAYK
60 70 80 90 100
VSRGLWKKYG DKRIIDTPIS EMGFAGIAVG AAMAGLRPIC EFMTFNFSMQ
110 120 130 140 150
AIDQVINSAA KTYYMSGGLQ PVPIVFRGPN GASAGVAAQH SQCFAAWYGH
160 170 180 190 200
CPGLKVVSPW NSEDAKGLIK SAIRDNNPVV VLENELMYGV PFEFPPEAQS
210 220 230 240 250
KDFLIPIGKA KIERQGTHIT VVSHSRPVGH CLEAAAVLSK EGVECEVINM
260 270 280 290 300
RTIRPMDMET IEASVMKTNH LVTVEGGWPQ FGVGAEICAR IMEGPAFNFL
310 320 330 340
DAPAVRVTGA DVPMPYAKIL EDNSIPQVKD IIFAIKKTLN I
The sequence of this isoform differs from the canonical sequence as follows:
135-152: Missing.
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 YYMSGVAAQH SQCFAAWYGH
160 170 180 190 200
CPGLKVVSPW NSEDAKGLIK SAIRDNNPVV VLENELMYGV PFEFPPEAQS
210 220 230 240 250
KDFLIPIGKA KIERQGTHIT VVSHSRPVGH CLEAAAVLSK EGVECEVINM
260 270 280 290 300
RTIRPMDMET IEASVMKTNH LVTVEGGWPQ FGVGAEICAR IMEGPAFNFL
310 320 330 340
DAPAVRVTGA DVPMPYAKIL EDNSIPQVKD IIFAIKKTLN I
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 9 – 13 | RRPLR → AETPS (PubMed:3422424).Curated | 5 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 43 | M → G AA sequence (PubMed:7895732).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 160 | Q → G (PubMed:3422424).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 213 – 221 | PPEAQSKDF → LRKLSQKIL (PubMed:3422424).Curated | 9 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 213 | P → L in AAA88097 (PubMed:2377599).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 213 | P → L in BAA14123 (PubMed:2377599).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 310 – 312 | MEG → NGS (PubMed:3422424).Curated | 3 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_004967 | 31 | L → V2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_030954 | 132 | Y → C in PDHBD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_021058 | 344 | P → S in PDHBD. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_012675 | 16 – 33 | Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 18 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_043364 | 135 – 152 | Missing in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 18 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS2890.1 [P11177-1] CCDS54602.1 [P11177-3] CCDS82795.1 [P11177-2] |
Protein sequence database of the Protein Information Resource More...PIRi | JU0145 DEHUPB |
NCBI Reference Sequences More...RefSeqi | NP_000916.2, NM_000925.3 [P11177-1] NP_001166939.1, NM_001173468.1 [P11177-3] NP_001302465.1, NM_001315536.1 [P11177-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.161357 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000302746; ENSP00000307241; ENSG00000168291 [P11177-1] ENST00000383714; ENSP00000373220; ENSG00000168291 [P11177-2] ENST00000485460; ENSP00000417267; ENSG00000168291 [P11177-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5162 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5162 |
UCSC genome browser More...UCSCi | uc003dkf.4 human [P11177-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P11177 | PDHB isoform 2 | 359 | |||
| Pyruvate dehydrogenase E1 beta subunit | 359 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 359 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 359 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 359 | ||||
| +2 | |||||
| P11177-2 | PDHB isoform 2 | 341 | |||
| PDHB isoform 1 | 341 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 341 | ||||
| P11177-3 | PDHB isoform 8 | 341 | |||
| Pyruvate dehydrogenase E1 beta subunit | 341 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 341 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 341 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 341 | ||||
| +1 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P11177 | PDHB isoform 2 | 359 | |||
| Pyruvate dehydrogenase E1 beta subunit | 359 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 359 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 359 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 359 | ||||
| +152 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P11177 | PDHB isoform 2 | 359 | |||
| Pyruvate dehydrogenase E1 beta subunit | 359 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 359 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 359 | ||||
| Pyruvate dehydrogenase E1 beta subunit | 359 | ||||
| +1193 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS2890.1 [P11177-1] CCDS54602.1 [P11177-3] CCDS82795.1 [P11177-2] |
Protein sequence database of the Protein Information Resource More...PIRi | JU0145 DEHUPB |
NCBI Reference Sequences More...RefSeqi | NP_000916.2, NM_000925.3 [P11177-1] NP_001166939.1, NM_001173468.1 [P11177-3] NP_001302465.1, NM_001315536.1 [P11177-2] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.161357 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB 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 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P11177 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P11177 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 111188, 72 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-376 Pyruvate dehydrogenase E1 heterotetramer |
Database of interacting proteins More...DIPi | DIP-37651N |
Protein interaction database and analysis system More...IntActi | P11177, 30 interactors |
Molecular INTeraction database More...MINTi | P11177 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000307241 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB00157 NADH DB00119 Pyruvic acid |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P11177 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P11177 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P11177 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | PDHB |
Domain mapping of disease mutations (DMDM) More...DMDMi | 134044259 |
2D gel databases
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00549885 |
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P11177 |
University College Dublin 2-DE Proteome Database More...UCD-2DPAGEi | P11177 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P11177 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P11177 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P11177 |
PeptideAtlas More...PeptideAtlasi | P11177 |
PRoteomics IDEntifications database More...PRIDEi | P11177 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 52715 52716 [P11177-2] 52717 [P11177-3] |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P11177-1 [P11177-1] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 5162 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000302746; ENSP00000307241; ENSG00000168291 [P11177-1] ENST00000383714; ENSP00000373220; ENSG00000168291 [P11177-2] ENST00000485460; ENSP00000417267; ENSG00000168291 [P11177-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 5162 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:5162 |
UCSC genome browser More...UCSCi | uc003dkf.4 human [P11177-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 5162 |
DisGeNET More...DisGeNETi | 5162 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000168291.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | PDHB |
Human Gene Nomenclature Database More...HGNCi | HGNC:8808 PDHB |
Human Protein Atlas More...HPAi | CAB033794 HPA036744 HPA036745 |
MalaCards human disease database More...MalaCardsi | PDHB |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 179060 gene 614111 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P11177 |
Open Targets More...OpenTargetsi | ENSG00000168291 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 255138 Pyruvate dehydrogenase E1-beta deficiency |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33152 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0524 Eukaryota COG0022 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000063423 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000281450 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000917 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P11177 |
KEGG Orthology (KO) More...KOi | K00162 |
Identification of Orthologs from Complete Genome Data More...OMAi | SRMRHHC |
Database of Orthologous Groups More...OrthoDBi | EOG091G0D37 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P11177 |
TreeFam database of animal gene trees More...TreeFami | TF105674 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS09727-MONOMER |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-204174 Regulation of pyruvate dehydrogenase (PDH) complex R-HSA-389661 Glyoxylate metabolism and glycine degradation R-HSA-5362517 Signaling by Retinoic Acid R-HSA-70268 Pyruvate metabolism |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P11177 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | PDHB human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P11177 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Pyruvate_dehydrogenase_(lipoamide)_beta |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 5162 |
Protein Ontology More...PROi | PR:P11177 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000168291 |
CleanEx database of gene expression profiles More...CleanExi | HS_PDHB |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P11177 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P11177 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.40.50.920, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029061 THDP-binding IPR009014 Transketo_C/PFOR_II IPR005475 Transketolase-like_Pyr-bd IPR033248 Transketolase_C |
Pfam protein domain database More...Pfami | View protein in Pfam PF02779 Transket_pyr, 1 hit PF02780 Transketolase_C, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00861 Transket_pyr, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF52518 SSF52518, 1 hit SSF52922 SSF52922, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | ODPB_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P11177Primary (citable) accession number: P11177 Secondary accession number(s): B2R7L0 , B4DDD7, Q6FH45, Q9BQ27, Q9UFK3 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
| Last sequence update: | March 6, 2007 | |
| Last modified: | July 18, 2018 | |
| This is version 212 of the entry and version 3 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references
