UniProtKB - Q9BUT1 (BDH2_HUMAN)
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- BLAST>sp|Q9BUT1|BDH2_HUMAN 3-hydroxybutyrate dehydrogenase type 2 OS=Homo sapiens OX=9606 GN=BDH2 PE=1 SV=2 MGRLDGKVIILTAAAQGIGQAAALAFAREGAKVIATDINESKLQELEKYPGIQTRVLDVT KKKQIDQFANEVERLDVLFNVAGFVHHGTVLDCEEKDWDFSMNLNVRSMYLMIKAFLPKM LAQKSGNIINMSSVASSVKGVVNRCVYSTTKAAVIGLTKSVAADFIQQGIRCNCVCPGTV DTPSLQERIQARGNPEEARNDFLKRQKTGRFATAEEIAMLCVYLASDESAYVTGNPVIID GGWSL
- Align
3-hydroxybutyrate dehydrogenase type 2
BDH2
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.8"Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase."
Guo K., Lukacik P., Papagrigoriou E., Meier M., Lee W.H., Adamski J., Oppermann U.
J. Biol. Chem. 281:10291-10297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, SUBUNIT.
<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>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=60 µM for NAD1 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.8"Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase."
Guo K., Lukacik P., Papagrigoriou E., Meier M., Lee W.H., Adamski J., Oppermann U.
J. Biol. Chem. 281:10291-10297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, SUBUNIT.
- KM=10 mM for R-hydroxybutyrate1 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.8"Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase."
Guo K., Lukacik P., Papagrigoriou E., Meier M., Lee W.H., Adamski J., Oppermann U.
J. Biol. Chem. 281:10291-10297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, SUBUNIT.
- Vmax=82 nmol/min/mg enzyme (at 30 degrees Celsius)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.8"Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase."
Guo K., Lukacik P., Papagrigoriou E., Meier M., Lee W.H., Adamski J., Oppermann U.
J. Biol. Chem. 281:10291-10297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, SUBUNIT.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei
<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.8"Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase."
Guo K., Lukacik P., Papagrigoriou E., Meier M., Lee W.H., Adamski J., Oppermann U.
J. Biol. Chem. 281:10291-10297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, SUBUNIT.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Siderophore biosynthesis
This protein is involved in Siderophore biosynthesis.View all proteins of this organism that are known to be involved in Siderophore biosynthesis.
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 | 58 | NAD1 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 ‘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 | 144 | SubstrateCurated | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 147 | Proton acceptorPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 1 | |
| <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 | 151 | NAD1 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 ‘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 | 188 | SubstrateCurated | 1 | |
| <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 | 205 | SubstrateCurated | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 10 – 37 | NAD1 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
| 28 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 180 – 184 | NAD1 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
| 5 |
<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
- 3-hydroxybutyrate dehydrogenase activity Source: HGNC <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
- NAD binding Source: HGNC <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
- oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor Source: UniProtKB
<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
- epithelial cell differentiation 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
- fatty acid beta-oxidation Source: HGNC <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
- heme metabolic process Source: UniProtKB
- iron ion homeostasis Source: UniProtKB
- ketone body biosynthetic process Source: Reactome
- siderophore biosynthetic process Source: UniProtKB
<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 |
| Ligand | NAD |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS08987-MONOMER |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-77111 Synthesis of Ketone Bodies |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | Q9BUT1 |
<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 | |
| <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:BDH2 Synonyms:DHRS6, SDR15C1 ORF Names:UNQ6308/PRO20933 |
| <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:ENSG00000164039.14 |
Human Gene Nomenclature Database More...HGNCi | HGNC:32389 BDH2 |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9BUT1 |
<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
Other locations
- Cytoplasm 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.8"Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase."
Guo K., Lukacik P., Papagrigoriou E., Meier M., Lee W.H., Adamski J., Oppermann U.
J. Biol. Chem. 281:10291-10297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, SUBUNIT.
- Cytoplasm 1 Publication
Cytosol
- cytosol Source: HPA
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Other locations
- cytoplasm Source: HGNC <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
Cytoplasm<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
Organism-specific databases
DisGeNET More...DisGeNETi | 56898 |
Open Targets More...OpenTargetsi | ENSG00000164039 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA142672559 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | BDH2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 125987797 |
<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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000042580 | 1 – 245 | 3-hydroxybutyrate dehydrogenase type 2Add BLAST | 245 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9BUT1 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9BUT1 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9BUT1 |
PeptideAtlas More...PeptideAtlasi | Q9BUT1 |
PRoteomics IDEntifications database More...PRIDEi | Q9BUT1 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 79125 79126 [Q9BUT1-2] 79127 [Q9BUT1-3] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9BUT1 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9BUT1 |
<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 | ENSG00000164039 |
CleanEx database of gene expression profiles More...CleanExi | HS_BDH2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9BUT1 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9BUT1 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA036028 HPA036029 |
<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.8"Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase."
Guo K., Lukacik P., Papagrigoriou E., Meier M., Lee W.H., Adamski J., Oppermann U.
J. Biol. Chem. 281:10291-10297(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, SUBUNIT.
<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 |
|---|---|---|---|---|
| DIB1 | Q06819 | 3 | EBI-6137689,EBI-166 | From Saccharomyces cerevisiae (strain ATCC 204508 / S288c). |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 121228, 12 interactors |
Protein interaction database and analysis system More...IntActi | Q9BUT1, 2 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000296424 |
<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 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 | 3 – 6 | 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 | 8 – 13 | 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 | 6 | |
| <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 | 17 – 28 | 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 | |
| <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 – 38 | 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 | 40 – 43 | 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 | 44 – 48 | 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 | 52 – 56 | 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 | 62 – 71 | 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 | 10 | |
| <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 | 76 – 80 | 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 | 90 – 92 | 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 | 95 – 105 | 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 | 107 – 123 | 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 | 17 | |
| <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 | 126 – 131 | 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 | 6 | |
| <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 | 136 – 138 | 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 | 145 – 165 | 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 | 21 | |
| <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 | 166 – 168 | 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 | 170 – 178 | 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 | 9 | |
| <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 | 183 – 191 | 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 | 9 | |
| <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 | 192 – 194 | 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 | 195 – 204 | 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 | 10 | |
| <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 – 225 | 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 | |
| <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 | 227 – 229 | 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 | 236 – 239 | 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 | 243 – 245 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9BUT1 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9BUT1 |
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 | Q9BUT1 |
<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>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0725 Eukaryota COG1028 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000148965 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG002145 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9BUT1 |
KEGG Orthology (KO) More...KOi | K00019 |
Identification of Orthologs from Complete Genome Data More...OMAi | FPQWGAY |
Database of Orthologous Groups More...OrthoDBi | EOG091G0GO6 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9BUT1 |
TreeFam database of animal gene trees More...TreeFami | TF328795 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR036291 NAD(P)-bd_dom_sf IPR020904 Sc_DH/Rdtase_CS IPR002347 SDR_fam |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00081 GDHRDH PR00080 SDRFAMILY |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51735 SSF51735, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00061 ADH_SHORT, 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.
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
MGRLDGKVII LTAAAQGIGQ AAALAFAREG AKVIATDINE SKLQELEKYP
60 70 80 90 100
GIQTRVLDVT KKKQIDQFAN EVERLDVLFN VAGFVHHGTV LDCEEKDWDF
110 120 130 140 150
SMNLNVRSMY LMIKAFLPKM LAQKSGNIIN MSSVASSVKG VVNRCVYSTT
160 170 180 190 200
KAAVIGLTKS VAADFIQQGI RCNCVCPGTV DTPSLQERIQ ARGNPEEARN
210 220 230 240
DFLKRQKTGR FATAEEIAML CVYLASDESA YVTGNPVIID GGWSL
The sequence of this isoform differs from the canonical sequence as follows:
141-245: VVNRCVYSTT...PVIIDGGWSL → GSVSFRGLRCSYTHIIKSSAFGNRHSRDYNFKY
10 20 30 40 50
MGRLDGKVII LTAAAQGIGQ AAALAFAREG AKVIATDINE SKLQELEKYP
60 70 80 90 100
GIQTRVLDVT KKKQIDQFAN EVERLDVLFN VAGFVHHGTV LDCEEKDWDF
110 120 130 140 150
SMNLNVRSMY LMIKAFLPKM LAQKSGNIIN MSSVASSVKG GSVSFRGLRC
160 170
SYTHIIKSSA FGNRHSRDYN FKY
The sequence of this isoform differs from the canonical sequence as follows:
1-101: Missing.
10 20 30 40 50
MNLNVRSMYL MIKAFLPKML AQKSGNIINM SSVASSVKGV VNRCVYSTTK
60 70 80 90 100
AAVIGLTKSV AADFIQQGIR CNCVCPGTVD TPSLQERIQA RGNPEEARND
110 120 130 140
FLKRQKTGRF ATAEEIAMLC VYLASDESAY VTGNPVIIDG GWSL
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 | 95 | E → V in BAF82849 (PubMed:14702039).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 | 161 | V → L in AAQ89200 (PubMed:12975309).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 | 203 | L → P in BAF82849 (PubMed:14702039).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 | 230 | A → T in AAH95414 (PubMed:15489334).Curated | 1 |
Natural variant
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_039781 | 1 – 101 | 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
| 101 | |
| <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_015859 | 141 – 245 | VVNRC…GGWSL → GSVSFRGLRCSYTHIIKSSA FGNRHSRDYNFKY in isoform 2. 3 Publications <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
| 105 |
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 | AF164790 mRNA Translation: AAF80754.1 AY358841 mRNA Translation: AAQ89200.1 CR457309 mRNA Translation: CAG33590.1 AK023323 mRNA Translation: BAB14526.1 AK290160 mRNA Translation: BAF82849.1 AK300626 mRNA Translation: BAG62318.1 AC097485 Genomic DNA No translation available. BC037277 mRNA Translation: AAH37277.1 BC001953 mRNA Translation: AAH01953.1 BC095414 mRNA Translation: AAH95414.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS3663.1 [Q9BUT1-1] |
NCBI Reference Sequences More...RefSeqi | NP_064524.3, NM_020139.3 [Q9BUT1-1] XP_011530430.1, XM_011532128.2 [Q9BUT1-1] XP_016863951.1, XM_017008462.1 [Q9BUT1-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.124696 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000296424; ENSP00000296424; ENSG00000164039 [Q9BUT1-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 56898 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:56898 |
UCSC genome browser More...UCSCi | uc003hwz.4 human [Q9BUT1-1] |
<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 | |
|---|---|---|---|---|---|
| Q9BUT1 | 3-hydroxybutyrate dehydrogenase, type 2, isoform CRA_b | 245 | |||
| 3-hydroxybutyrate dehydrogenase 2 | 245 | ||||
| 3-hydroxybutyrate dehydrogenase 2 | 245 | ||||
| 3-hydroxybutyrate dehydrogenase 2 | 245 | ||||
| UPI000057D068 | 246 | ||||
| +1 | |||||
<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 | AF164790 mRNA Translation: AAF80754.1 AY358841 mRNA Translation: AAQ89200.1 CR457309 mRNA Translation: CAG33590.1 AK023323 mRNA Translation: BAB14526.1 AK290160 mRNA Translation: BAF82849.1 AK300626 mRNA Translation: BAG62318.1 AC097485 Genomic DNA No translation available. BC037277 mRNA Translation: AAH37277.1 BC001953 mRNA Translation: AAH01953.1 BC095414 mRNA Translation: AAH95414.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS3663.1 [Q9BUT1-1] |
NCBI Reference Sequences More...RefSeqi | NP_064524.3, NM_020139.3 [Q9BUT1-1] XP_011530430.1, XM_011532128.2 [Q9BUT1-1] XP_016863951.1, XM_017008462.1 [Q9BUT1-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.124696 |
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 |
| 2AG5 | X-ray | 1.84 | A/B/C/D | 1-245 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q9BUT1 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9BUT1 | |||||
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 | 121228, 12 interactors |
Protein interaction database and analysis system More...IntActi | Q9BUT1, 2 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000296424 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9BUT1 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9BUT1 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | BDH2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 125987797 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | Q9BUT1 |
MaxQB - The MaxQuant DataBase More...MaxQBi | Q9BUT1 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9BUT1 |
PeptideAtlas More...PeptideAtlasi | Q9BUT1 |
PRoteomics IDEntifications database More...PRIDEi | Q9BUT1 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 79125 79126 [Q9BUT1-2] 79127 [Q9BUT1-3] |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000296424; ENSP00000296424; ENSG00000164039 [Q9BUT1-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 56898 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:56898 |
UCSC genome browser More...UCSCi | uc003hwz.4 human [Q9BUT1-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 56898 |
DisGeNET More...DisGeNETi | 56898 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000164039.14 |
GeneCards: human genes, protein and diseases More...GeneCardsi | BDH2 |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0032960 |
Human Gene Nomenclature Database More...HGNCi | HGNC:32389 BDH2 |
Human Protein Atlas More...HPAi | HPA036028 HPA036029 |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9BUT1 |
Open Targets More...OpenTargetsi | ENSG00000164039 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA142672559 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0725 Eukaryota COG1028 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000148965 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG002145 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9BUT1 |
KEGG Orthology (KO) More...KOi | K00019 |
Identification of Orthologs from Complete Genome Data More...OMAi | FPQWGAY |
Database of Orthologous Groups More...OrthoDBi | EOG091G0GO6 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9BUT1 |
TreeFam database of animal gene trees More...TreeFami | TF328795 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS08987-MONOMER |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-77111 Synthesis of Ketone Bodies |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | Q9BUT1 |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9BUT1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 56898 |
Protein Ontology More...PROi | PR:Q9BUT1 |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000164039 |
CleanEx database of gene expression profiles More...CleanExi | HS_BDH2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9BUT1 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9BUT1 HS |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR036291 NAD(P)-bd_dom_sf IPR020904 Sc_DH/Rdtase_CS IPR002347 SDR_fam |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00081 GDHRDH PR00080 SDRFAMILY |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF51735 SSF51735, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00061 ADH_SHORT, 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 | BDH2_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 | Q9BUT1Primary (citable) accession number: Q9BUT1 Secondary accession number(s): A8K295 , B4DUF6, Q503A0, Q6IA46, Q6UWD3, Q9H8S8, Q9NRX8 | |
| <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: | October 11, 2005 |
| Last sequence update: | February 6, 2007 | |
| Last modified: | July 18, 2018 | |
| This is version 153 of the entry and version 2 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, Reference proteomeDocuments
- Human chromosome 4
Human chromosome 4: 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 - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
