UniProtKB - P16152 (CBR1_HUMAN)
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- BLAST>sp|P16152|CBR1_HUMAN Carbonyl reductase [NADPH] 1 OS=Homo sapiens OX=9606 GN=CBR1 PE=1 SV=3 MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFH QLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRD VCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTK KGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKA TKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW
- Align
Carbonyl reductase [NADPH] 1
CBR1
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.14"Inhibition of polymorphic human carbonyl reductase 1 (CBR1) by the cardioprotectant flavonoid 7-monohydroxyethyl rutoside (monoHER)."
Gonzalez-Covarrubias V., Kalabus J.L., Blanco J.G.
Pharm. Res. 25:1730-1734(2008) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION, FUNCTION. - Ref.17"An unbiased cell morphology-based screen for new, biologically active small molecules."
Tanaka M., Bateman R., Rauh D., Vaisberg E., Ramachandani S., Zhang C., Hansen K.C., Burlingame A.L., Trautman J.K., Shokat K.M., Adams C.L.
PLoS Biol. 3:E128-E128(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 2-276 IN COMPLEX WITH THE SYNTHETIC INHIBITOR HYDROXY-PP AND NADP, IDENTIFICATION BY MASS SPECTROMETRY, PARTIAL PROTEIN SEQUENCE, FUNCTION. - Ref.18"Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane adduct."
Bateman R., Rauh D., Shokat K.M.
Org. Biomol. Chem. 5:3363-3367(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP AND FORMALDEHYDE-GLUTATHIONE ADDUCT, FUNCTION. - Ref.19"Human carbonyl reductase 1 is an S-nitrosoglutathione reductase."
Bateman R.L., Rauh D., Tavshanjian B., Shokat K.M.
J. Biol. Chem. 283:35756-35762(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP, SUBSTRATE ANALOGS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
<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 an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<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.14"Inhibition of polymorphic human carbonyl reductase 1 (CBR1) by the cardioprotectant flavonoid 7-monohydroxyethyl rutoside (monoHER)."
Gonzalez-Covarrubias V., Kalabus J.L., Blanco J.G.
Pharm. Res. 25:1730-1734(2008) [PubMed] [Europe PMC] [Abstract]Cited for: ENZYME REGULATION, FUNCTION. - Ref.20"A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity."
Gonzalez-Covarrubias V., Ghosh D., Lakhman S.S., Pendyala L., Blanco J.G.
Drug Metab. Dispos. 35:973-980(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ILE-88, CHARACTERIZATION OF VARIANT ILE-88, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
<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=30 µM for S-nitrosoglutathione2 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
- Ref.19"Human carbonyl reductase 1 is an S-nitrosoglutathione reductase."
Bateman R.L., Rauh D., Tavshanjian B., Shokat K.M.
J. Biol. Chem. 283:35756-35762(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP, SUBSTRATE ANALOGS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.20"A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity."
Gonzalez-Covarrubias V., Ghosh D., Lakhman S.S., Pendyala L., Blanco J.G.
Drug Metab. Dispos. 35:973-980(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ILE-88, CHARACTERIZATION OF VARIANT ILE-88, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
- KM=22 µM for menadione2 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
- Ref.19"Human carbonyl reductase 1 is an S-nitrosoglutathione reductase."
Bateman R.L., Rauh D., Tavshanjian B., Shokat K.M.
J. Biol. Chem. 283:35756-35762(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP, SUBSTRATE ANALOGS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.20"A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity."
Gonzalez-Covarrubias V., Ghosh D., Lakhman S.S., Pendyala L., Blanco J.G.
Drug Metab. Dispos. 35:973-980(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ILE-88, CHARACTERIZATION OF VARIANT ILE-88, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
- KM=309 µM for prostaglandin E22 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
- Ref.19"Human carbonyl reductase 1 is an S-nitrosoglutathione reductase."
Bateman R.L., Rauh D., Tavshanjian B., Shokat K.M.
J. Biol. Chem. 283:35756-35762(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP, SUBSTRATE ANALOGS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.20"A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity."
Gonzalez-Covarrubias V., Ghosh D., Lakhman S.S., Pendyala L., Blanco J.G.
Drug Metab. Dispos. 35:973-980(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ILE-88, CHARACTERIZATION OF VARIANT ILE-88, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
- KM=173 µM for daunorubicin2 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
- Ref.19"Human carbonyl reductase 1 is an S-nitrosoglutathione reductase."
Bateman R.L., Rauh D., Tavshanjian B., Shokat K.M.
J. Biol. Chem. 283:35756-35762(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP, SUBSTRATE ANALOGS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.20"A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity."
Gonzalez-Covarrubias V., Ghosh D., Lakhman S.S., Pendyala L., Blanco J.G.
Drug Metab. Dispos. 35:973-980(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ILE-88, CHARACTERIZATION OF VARIANT ILE-88, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
- KM=247 µM for NADPH2 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
- Ref.19"Human carbonyl reductase 1 is an S-nitrosoglutathione reductase."
Bateman R.L., Rauh D., Tavshanjian B., Shokat K.M.
J. Biol. Chem. 283:35756-35762(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP, SUBSTRATE ANALOGS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.20"A functional genetic polymorphism on human carbonyl reductase 1 (CBR1 V88I) impacts on catalytic activity and NADPH binding affinity."
Gonzalez-Covarrubias V., Ghosh D., Lakhman S.S., Pendyala L., Blanco J.G.
Drug Metab. Dispos. 35:973-980(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT ILE-88, CHARACTERIZATION OF VARIANT ILE-88, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
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 | 90 | NADP; via carbonyl oxygen3 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 ‘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 | 106 | Glutathione | 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 | 140 | Substrate | 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 | 194 | Proton acceptor | 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 – 34 | NADP3 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
| 25 | |
| <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 | 63 – 64 | NADP3 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
| 2 | |
| <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 | 194 – 198 | NADP3 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
| 5 | |
| <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 | 231 – 233 | NADP3 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
| 3 |
<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
- 15-hydroxyprostaglandin dehydrogenase (NADP+) activity Source: UniProtKB-EC
- carbonyl reductase (NADPH) 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
- oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor 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
- prostaglandin-E2 9-reductase activity Source: Reactome
<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
- cyclooxygenase pathway Source: Reactome
- drug metabolic process 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
- epithelial cell differentiation Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patterni
- oxidation-reduction process 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
- vitamin K metabolic process 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 |
| Ligand | NADP |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.1.1.184 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2162123 Synthesis of Prostaglandins (PG) and Thromboxanes (TX) |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P16152 |
<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:CBR1 Synonyms:CBR, CRN, SDR21C1 |
| <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:ENSG00000159228.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:1548 CBR1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 114830 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P16152 |
<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
Cytosol
- cytosol Source: Reactome
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- extracellular vesicle Source: UniProtKBInferred from high throughput 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 | 873 |
Open Targets More...OpenTargetsi | ENSG00000159228 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA26121 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5586 |
Drug and drug target database More...DrugBanki | DB00414 Acetohexamide DB00997 Doxorubicin DB00502 Haloperidol DB01046 Lubiprostone DB05197 Sofalcone DB04844 Tetrabenazine |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1383 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | CBR1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 118519 |
<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined 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
| |||
| <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_0000054602 | 2 – 277 | Carbonyl reductase [NADPH] 1Add BLAST | 276 |
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 | 2 | N-acetylserineCombined 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
| 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 | 2 | PhosphoserineBy 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 | 30 | PhosphoserineBy 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 | 239 | N6-1-carboxyethyl lysine1 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 - PTMi
Acetylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P16152 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P16152 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P16152 |
PeptideAtlas More...PeptideAtlasi | P16152 |
PRoteomics IDEntifications database More...PRIDEi | P16152 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 53298 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P16152-1 [P16152-1] |
2D gel databases
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00295386 |
University College Dublin 2-DE Proteome Database More...UCD-2DPAGEi | P16152 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P16152 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P16152 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P16152 |
<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 | ENSG00000159228 |
CleanEx database of gene expression profiles More...CleanExi | HS_CBR1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P16152 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P16152 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA018433 |
<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.17"An unbiased cell morphology-based screen for new, biologically active small molecules."
Tanaka M., Bateman R., Rauh D., Vaisberg E., Ramachandani S., Zhang C., Hansen K.C., Burlingame A.L., Trautman J.K., Shokat K.M., Adams C.L.
PLoS Biol. 3:E128-E128(2005) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 2-276 IN COMPLEX WITH THE SYNTHETIC INHIBITOR HYDROXY-PP AND NADP, IDENTIFICATION BY MASS SPECTROMETRY, PARTIAL PROTEIN SEQUENCE, FUNCTION. - Ref.18"Glutathione traps formaldehyde by formation of a bicyclo[4.4.1]undecane adduct."
Bateman R., Rauh D., Shokat K.M.
Org. Biomol. Chem. 5:3363-3367(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP AND FORMALDEHYDE-GLUTATHIONE ADDUCT, FUNCTION. - Ref.19"Human carbonyl reductase 1 is an S-nitrosoglutathione reductase."
Bateman R.L., Rauh D., Tavshanjian B., Shokat K.M.
J. Biol. Chem. 283:35756-35762(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-277 IN COMPLEX WITH NADP, SUBSTRATE ANALOGS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
<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 |
|---|---|---|---|---|
| PRKAB1 | Q9Y478 | 2 | EBI-351348,EBI-719769 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 107319, 38 interactors |
Database of interacting proteins More...DIPi | DIP-33136N |
Protein interaction database and analysis system More...IntActi | P16152, 41 interactors |
Molecular INTeraction database More...MINTi | P16152 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000290349 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P16152 |
<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 | 7 – 12 | 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 | 16 – 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 | 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 | 29 – 39 | 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 | 40 – 52 | 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 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 67 – 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 | 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 | 82 – 89 | 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 | 8 | |
| <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 | 103 – 114 | 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 | 116 – 125 | 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 | 126 – 128 | 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 | 129 – 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 | 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 | 141 – 148 | 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 | 8 | |
| <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 | 152 – 159 | 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 | 8 | |
| <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 | 165 – 180 | 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 | 16 | |
| <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 | 184 – 188 | 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 | 193 – 215 | 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 | 23 | |
| <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 | 222 – 227 | 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 | 234 – 236 | 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 | 244 – 247 | 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 | 249 – 255 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 268 – 270 | 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 | 273 – 275 | 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 | P16152 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P16152 |
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 | P16152 |
<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
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 95 – 97 | Glutathione binding | 3 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 193 – 194 | Glutathione binding | 2 |
<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 | KOG1208 Eukaryota COG1028 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00510000046499 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG001909 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P16152 |
KEGG Orthology (KO) More...KOi | K00079 |
Identification of Orthologs from Complete Genome Data More...OMAi | SVEFSHM |
Database of Orthologous Groups More...OrthoDBi | EOG091G0V7L |
Database for complete collections of gene phylogenies More...PhylomeDBi | P16152 |
TreeFam database of animal gene trees More...TreeFami | TF329359 |
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 |
Pfam protein domain database More...Pfami | View protein in Pfam PF00106 adh_short, 1 hit |
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 (2)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 2 <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
MSSGIHVALV TGGNKGIGLA IVRDLCRLFS GDVVLTARDV TRGQAAVQQL
60 70 80 90 100
QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLDVLVNN AGIAFKVADP
110 120 130 140 150
TPFHIQAEVT MKTNFFGTRD VCTELLPLIK PQGRVVNVSS IMSVRALKSC
160 170 180 190 200
SPELQQKFRS ETITEEELVG LMNKFVEDTK KGVHQKEGWP SSAYGVTKIG
210 220 230 240 250
VTVLSRIHAR KLSEQRKGDK ILLNACCPGW VRTDMAGPKA TKSPEEGAET
260 270
PVYLALLPPD AEGPHGQFVS EKRVEQW
The sequence of this isoform differs from the canonical sequence as follows:
133-173: GRVVNVSSIM...TEEELVGLMN → ASCVLSAWSC...ICRCLTLGPF
174-277: Missing.
10 20 30 40 50
MSSGIHVALV TGGNKGIGLA IVRDLCRLFS GDVVLTARDV TRGQAAVQQL
60 70 80 90 100
QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLDVLVNN AGIAFKVADP
110 120 130 140 150
TPFHIQAEVT MKTNFFGTRD VCTELLPLIK PQASCVLSAW SCLSQNPSGG
160 170
KSKPLAWFTE MSIICRCLTL GPF
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_059053 | 88 | V → I Reduced affinity for NADPH and reduced activity towards daunorubicin and prostaglandin E2. 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_031706 | 131 | P → S1 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
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 | J04056 mRNA Translation: AAA52070.1 M62420 Genomic DNA Translation: AAA17881.1 AB003151 Genomic DNA Translation: BAA33498.1 AP000688 Genomic DNA Translation: BAA89424.1 AB124848 mRNA Translation: BAE45940.1 BT019843 mRNA Translation: AAV38646.1 CR541708 mRNA Translation: CAG46509.1 AK294142 mRNA Translation: BAG57468.1 AK314879 mRNA Translation: BAG37394.1 EF141836 Genomic DNA Translation: ABK97430.1 AP001724 Genomic DNA Translation: BAA95508.1 CH471079 Genomic DNA Translation: EAX09754.1 CH471079 Genomic DNA Translation: EAX09755.1 BC002511 mRNA Translation: AAH02511.1 BC015640 mRNA Translation: AAH15640.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS13641.1 [P16152-1] CCDS68202.1 [P16152-2] |
Protein sequence database of the Protein Information Resource More...PIRi | A61271 RDHUCB |
NCBI Reference Sequences More...RefSeqi | NP_001273718.1, NM_001286789.1 [P16152-2] NP_001748.1, NM_001757.3 [P16152-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.88778 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000290349; ENSP00000290349; ENSG00000159228 [P16152-1] ENST00000530908; ENSP00000434613; ENSG00000159228 [P16152-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 873 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:873 |
UCSC genome browser More...UCSCi | uc002yvb.3 human [P16152-1] |
<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 | |
|---|---|---|---|---|---|
| P16152 | CBR1 isoform 2 | 277 | |||
| Carbonyl reductase 1 | 277 | ||||
| Carbonyl reductase 1 | 277 | ||||
| UPI00001292D3 | 276 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P16152 | CBR1 isoform 2 | 277 | |||
| Carbonyl reductase 1 | 277 | ||||
| Carbonyl reductase 1 | 277 | ||||
| UPI00001292D3 | 276 | ||||
| Carbonyl reductase 1 | 290 | ||||
| +42 | |||||
| P16152-2 | Carbonyl reductase 1 | 174 | |||
| Carbonyl reductase 1 | 173 | ||||
| Carbonyl reductase 1 | 173 | ||||
| CBR1 isoform 2 | 173 | ||||
| Carbonyl reductase 3 | 173 | ||||
| +6 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P16152 | CBR1 isoform 2 | 277 | |||
| Carbonyl reductase 1 | 277 | ||||
| Carbonyl reductase 1 | 277 | ||||
| UPI00001292D3 | 276 | ||||
| Carbonyl reductase 1 | 290 | ||||
| +357 | |||||
| P16152-2 | Carbonyl reductase 1 | 174 | |||
| CBR1 isoform 2 | 173 | ||||
| Carbonyl reductase 3 | 173 | ||||
| Carbonyl reductase 1 | 173 | ||||
| Carbonyl reductase [NADPH] 1 | 173 | ||||
| +32 | |||||
<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
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| SeattleSNPs |
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 | J04056 mRNA Translation: AAA52070.1 M62420 Genomic DNA Translation: AAA17881.1 AB003151 Genomic DNA Translation: BAA33498.1 AP000688 Genomic DNA Translation: BAA89424.1 AB124848 mRNA Translation: BAE45940.1 BT019843 mRNA Translation: AAV38646.1 CR541708 mRNA Translation: CAG46509.1 AK294142 mRNA Translation: BAG57468.1 AK314879 mRNA Translation: BAG37394.1 EF141836 Genomic DNA Translation: ABK97430.1 AP001724 Genomic DNA Translation: BAA95508.1 CH471079 Genomic DNA Translation: EAX09754.1 CH471079 Genomic DNA Translation: EAX09755.1 BC002511 mRNA Translation: AAH02511.1 BC015640 mRNA Translation: AAH15640.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS13641.1 [P16152-1] CCDS68202.1 [P16152-2] |
Protein sequence database of the Protein Information Resource More...PIRi | A61271 RDHUCB |
NCBI Reference Sequences More...RefSeqi | NP_001273718.1, NM_001286789.1 [P16152-2] NP_001748.1, NM_001757.3 [P16152-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.88778 |
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 |
| 1WMA | X-ray | 1.24 | A | 2-277 | [»] | |
| 2PFG | X-ray | 1.54 | A | 2-277 | [»] | |
| 3BHI | X-ray | 2.27 | A | 2-277 | [»] | |
| 3BHJ | X-ray | 1.77 | A | 2-277 | [»] | |
| 3BHM | X-ray | 1.80 | A | 2-277 | [»] | |
| 4Z3D | X-ray | 1.80 | A/B/C/D | 2-277 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P16152 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P16152 | |||||
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 | 107319, 38 interactors |
Database of interacting proteins More...DIPi | DIP-33136N |
Protein interaction database and analysis system More...IntActi | P16152, 41 interactors |
Molecular INTeraction database More...MINTi | P16152 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000290349 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P16152 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5586 |
Drug and drug target database More...DrugBanki | DB00414 Acetohexamide DB00997 Doxorubicin DB00502 Haloperidol DB01046 Lubiprostone DB05197 Sofalcone DB04844 Tetrabenazine |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1383 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P16152 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P16152 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P16152 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | CBR1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 118519 |
2D gel databases
REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEi | IPI00295386 |
University College Dublin 2-DE Proteome Database More...UCD-2DPAGEi | P16152 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P16152 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P16152 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P16152 |
PeptideAtlas More...PeptideAtlasi | P16152 |
PRoteomics IDEntifications database More...PRIDEi | P16152 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 53298 |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P16152-1 [P16152-1] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 873 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000290349; ENSP00000290349; ENSG00000159228 [P16152-1] ENST00000530908; ENSP00000434613; ENSG00000159228 [P16152-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 873 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:873 |
UCSC genome browser More...UCSCi | uc002yvb.3 human [P16152-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 873 |
DisGeNET More...DisGeNETi | 873 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000159228.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | CBR1 |
Human Gene Nomenclature Database More...HGNCi | HGNC:1548 CBR1 |
Human Protein Atlas More...HPAi | HPA018433 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 114830 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P16152 |
Open Targets More...OpenTargetsi | ENSG00000159228 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA26121 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG1208 Eukaryota COG1028 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00510000046499 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG001909 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P16152 |
KEGG Orthology (KO) More...KOi | K00079 |
Identification of Orthologs from Complete Genome Data More...OMAi | SVEFSHM |
Database of Orthologous Groups More...OrthoDBi | EOG091G0V7L |
Database for complete collections of gene phylogenies More...PhylomeDBi | P16152 |
TreeFam database of animal gene trees More...TreeFami | TF329359 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.1.1.184 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2162123 Synthesis of Prostaglandins (PG) and Thromboxanes (TX) |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P16152 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | CBR1 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P16152 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | CBR1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 873 |
Protein Ontology More...PROi | PR:P16152 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000159228 |
CleanEx database of gene expression profiles More...CleanExi | HS_CBR1 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P16152 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P16152 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 |
Pfam protein domain database More...Pfami | View protein in Pfam PF00106 adh_short, 1 hit |
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 | CBR1_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 | P16152Primary (citable) accession number: P16152 Secondary accession number(s): B2RBZ7, B4DFK7, Q3LHW8 | |
| <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: | April 1, 1990 |
| Last sequence update: | January 23, 2007 | |
| Last modified: | July 18, 2018 | |
| This is version 200 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 21
Human chromosome 21: 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 - SIMILARITY comments
Index of protein domains and families
