UniProtKB - P48775 (T23O_HUMAN)
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- BLAST>sp|P48775|T23O_HUMAN Tryptophan 2,3-dioxygenase OS=Homo sapiens OX=9606 GN=TDO2 PE=1 SV=1 MSGCPFLGNNFGYTFKKLPVEGSEEDKSQTGVNRASKGGLIYGNYLHLEKVLNAQELQSE TKGNKIHDEHLFIITHQAYELWFKQILWELDSVREIFQNGHVRDERNMLKVVSRMHRVSV ILKLLVQQFSILETMTALDFNDFREYLSPASGFQSLQFRLLENKIGVLQNMRVPYNRRHY RDNFKGEENELLLKSEQEKTLLELVEAWLERTPGLEPHGFNFWGKLEKNITRGLEEEFIR IQAKEESEEKEEQVAEFQKQKEVLLSLFDEKRHEHLLSKGERRLSYRALQGALMIYFYRE EPRFQVPFQLLTSLMDIDSLMTKWRYNHVCMVHRMLGSKAGTGGSSGYHYLRSTVSDRYK VFVDLFNLSTYLIPRHWIPKMNPTIHKFLYTAEYCDSSYFSSDESD
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Tryptophan 2,3-dioxygenase
TDO2
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>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
3 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.5"Hypertryptophanemia due to tryptophan 2,3-dioxygenase deficiency."
Ferreira P., Shin I., Sosova I., Dornevil K., Jain S., Dewey D., Liu F., Liu A.
Mol. Genet. Metab. 120:317-324(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HYPTRP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, VARIANT HYPTRP ILE-108, CHARACTERIZATION OF VARIANT HYPTRP ILE-108. - Ref.6"Structural and functional analyses of human tryptophan 2,3-dioxygenase."
Meng B., Wu D., Gu J., Ouyang S., Ding W., Liu Z.J.
Proteins 82:3210-3216(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 19-388 OF APOPROTEIN, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-42; TYR-45; PHE-72; HIS-76; PHE-140; ARG-144; SER-151 AND HIS-328. - Ref.7"Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase."
Lewis-Ballester A., Forouhar F., Kim S.M., Lew S., Wang Y., Karkashon S., Seetharaman J., Batabyal D., Chiang B.Y., Hussain M., Correia M.A., Yeh S.R., Tong L.
Sci. Rep. 6:35169-35169(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 18-389 IN COMPLEX WITH HEME AND TRYPTOPHAN, COFACTOR, SUBUNIT, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF TYR-175.
<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>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
3 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.5"Hypertryptophanemia due to tryptophan 2,3-dioxygenase deficiency."
Ferreira P., Shin I., Sosova I., Dornevil K., Jain S., Dewey D., Liu F., Liu A.
Mol. Genet. Metab. 120:317-324(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HYPTRP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, VARIANT HYPTRP ILE-108, CHARACTERIZATION OF VARIANT HYPTRP ILE-108. - Ref.6"Structural and functional analyses of human tryptophan 2,3-dioxygenase."
Meng B., Wu D., Gu J., Ouyang S., Ding W., Liu Z.J.
Proteins 82:3210-3216(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 19-388 OF APOPROTEIN, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-42; TYR-45; PHE-72; HIS-76; PHE-140; ARG-144; SER-151 AND HIS-328. - Ref.7"Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase."
Lewis-Ballester A., Forouhar F., Kim S.M., Lew S., Wang Y., Karkashon S., Seetharaman J., Batabyal D., Chiang B.Y., Hussain M., Correia M.A., Yeh S.R., Tong L.
Sci. Rep. 6:35169-35169(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 18-389 IN COMPLEX WITH HEME AND TRYPTOPHAN, COFACTOR, SUBUNIT, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF TYR-175.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
<p>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
3 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.5"Hypertryptophanemia due to tryptophan 2,3-dioxygenase deficiency."
Ferreira P., Shin I., Sosova I., Dornevil K., Jain S., Dewey D., Liu F., Liu A.
Mol. Genet. Metab. 120:317-324(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HYPTRP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, VARIANT HYPTRP ILE-108, CHARACTERIZATION OF VARIANT HYPTRP ILE-108. - Ref.6"Structural and functional analyses of human tryptophan 2,3-dioxygenase."
Meng B., Wu D., Gu J., Ouyang S., Ding W., Liu Z.J.
Proteins 82:3210-3216(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 19-388 OF APOPROTEIN, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-42; TYR-45; PHE-72; HIS-76; PHE-140; ARG-144; SER-151 AND HIS-328. - Ref.7"Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase."
Lewis-Ballester A., Forouhar F., Kim S.M., Lew S., Wang Y., Karkashon S., Seetharaman J., Batabyal D., Chiang B.Y., Hussain M., Correia M.A., Yeh S.R., Tong L.
Sci. Rep. 6:35169-35169(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 18-389 IN COMPLEX WITH HEME AND TRYPTOPHAN, COFACTOR, SUBUNIT, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF TYR-175.
<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 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.7"Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase."
Lewis-Ballester A., Forouhar F., Kim S.M., Lew S., Wang Y., Karkashon S., Seetharaman J., Batabyal D., Chiang B.Y., Hussain M., Correia M.A., Yeh S.R., Tong L.
Sci. Rep. 6:35169-35169(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 18-389 IN COMPLEX WITH HEME AND TRYPTOPHAN, COFACTOR, SUBUNIT, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF TYR-175.
<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
<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.5"Hypertryptophanemia due to tryptophan 2,3-dioxygenase deficiency."
Ferreira P., Shin I., Sosova I., Dornevil K., Jain S., Dewey D., Liu F., Liu A.
Mol. Genet. Metab. 120:317-324(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HYPTRP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, VARIANT HYPTRP ILE-108, CHARACTERIZATION OF VARIANT HYPTRP ILE-108.
- KM=0.135 mM for L-tryptophan1 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.6"Structural and functional analyses of human tryptophan 2,3-dioxygenase."
Meng B., Wu D., Gu J., Ouyang S., Ding W., Liu Z.J.
Proteins 82:3210-3216(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 19-388 OF APOPROTEIN, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-42; TYR-45; PHE-72; HIS-76; PHE-140; ARG-144; SER-151 AND HIS-328.
- KM=0.132 mM for L-tryptophan1 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.5"Hypertryptophanemia due to tryptophan 2,3-dioxygenase deficiency."
Ferreira P., Shin I., Sosova I., Dornevil K., Jain S., Dewey D., Liu F., Liu A.
Mol. Genet. Metab. 120:317-324(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HYPTRP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, VARIANT HYPTRP ILE-108, CHARACTERIZATION OF VARIANT HYPTRP ILE-108.
<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: L-tryptophan degradation via kynurenine pathway
This protein is involved in step 1 of the subpathway that synthesizes L-kynurenine from L-tryptophan.UniRule 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
2 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.6"Structural and functional analyses of human tryptophan 2,3-dioxygenase."
Meng B., Wu D., Gu J., Ouyang S., Ding W., Liu Z.J.
Proteins 82:3210-3216(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 19-388 OF APOPROTEIN, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-42; TYR-45; PHE-72; HIS-76; PHE-140; ARG-144; SER-151 AND HIS-328. - Ref.7"Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase."
Lewis-Ballester A., Forouhar F., Kim S.M., Lew S., Wang Y., Karkashon S., Seetharaman J., Batabyal D., Chiang B.Y., Hussain M., Correia M.A., Yeh S.R., Tong L.
Sci. Rep. 6:35169-35169(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 18-389 IN COMPLEX WITH HEME AND TRYPTOPHAN, COFACTOR, SUBUNIT, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF TYR-175.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
- Indoleamine 2,3-dioxygenase 1 (IDO1), Tryptophan 2,3-dioxygenase (TDO2), Indoleamine 2,3-dioxygenase 2 (IDO2)
- Kynurenine formamidase (AFMID)
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-kynurenine from L-tryptophan, the pathway L-tryptophan degradation via kynurenine pathway and in Amino-acid degradation.
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 | 144 | SubstrateUniRule 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 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 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 ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 328 | Iron (heme axial ligand)UniRule 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 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 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 ‘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 | 342 | SubstrateUniRule 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 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 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>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
- amino acid binding Source: Ensembl
- heme binding 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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- metal ion binding Source: UniProtKB-KW
- oxygen binding Source: Ensembl
- tryptophan 2,3-dioxygenase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- protein homotetramerization 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
- tryptophan catabolic process Source: Reactome
- tryptophan catabolic process to acetyl-CoA Source: GO_Central
- tryptophan catabolic process to kynurenine 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 | Dioxygenase, Oxidoreductase |
| Biological process | Tryptophan catabolism |
| Ligand | Heme, Iron, Metal-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS07771-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.13.11.11 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-71240 Tryptophan catabolism |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00333; UER00453 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Tryptophan 2,3-dioxygenaseUniRule 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 (EC:1.13.11.11UniRule 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 3 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
Short name: TDOUniRule 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 Alternative name(s): Tryptamin 2,3-dioxygenaseUniRule 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 Tryptophan oxygenaseUniRule 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 Short name: TOUniRule 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 Short name: TRPOUniRule 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 Tryptophan pyrrolaseUniRule 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 TryptophanaseUniRule 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 |
| <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:TDO2UniRule 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 Synonyms:TDO |
| <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 |
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Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000151790.8 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11708 TDO2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 191070 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P48775 |
<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
Cytosol
- cytosol Source: Reactome
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Hypertryptophanemia (HYPTRP)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.5"Hypertryptophanemia due to tryptophan 2,3-dioxygenase deficiency."
Ferreira P., Shin I., Sosova I., Dornevil K., Jain S., Dewey D., Liu F., Liu A.
Mol. Genet. Metab. 120:317-324(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HYPTRP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, VARIANT HYPTRP ILE-108, CHARACTERIZATION OF VARIANT HYPTRP ILE-108.
Ferreira P., Shin I., Sosova I., Dornevil K., Jain S., Dewey D., Liu F., Liu A.
Mol. Genet. Metab. 120:317-324(2017) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_080251 | 108 | M → I in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 42 | Y → A: Reduces enzyme activity by 99%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 45 | Y → A: Reduces enzyme activity by 99%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 72 | F → A: Abolishes enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 76 | H → A: Abolishes enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 140 | F → A: Reduces enzyme activity by 99%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 144 | R → A: Reduces enzyme activity by 99%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 151 | S → A: Reduces enzyme activity by 90%. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 175 | Y → G: Reduces enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 328 | H → A: Abolishes enzyme activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 6999 |
MalaCards human disease database More...MalaCardsi | TDO2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600627 phenotype |
Open Targets More...OpenTargetsi | ENSG00000151790 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA36427 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2140 |
Drug and drug target database More...DrugBanki | DB00150 L-Tryptophan DB00779 Nalidixic Acid DB00500 Tolmetin |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2887 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | TDO2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 1351188 |
<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_0000072399 | 1 – 406 | Tryptophan 2,3-dioxygenaseAdd BLAST | 406 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P48775 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P48775 |
PeptideAtlas More...PeptideAtlasi | P48775 |
PRoteomics IDEntifications database More...PRIDEi | P48775 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 55947 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P48775 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P48775 |
<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 | ENSG00000151790 |
CleanEx database of gene expression profiles More...CleanExi | HS_TDO2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P48775 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P48775 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA039611 |
<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>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
3 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.5"Hypertryptophanemia due to tryptophan 2,3-dioxygenase deficiency."
Ferreira P., Shin I., Sosova I., Dornevil K., Jain S., Dewey D., Liu F., Liu A.
Mol. Genet. Metab. 120:317-324(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN HYPTRP, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, VARIANT HYPTRP ILE-108, CHARACTERIZATION OF VARIANT HYPTRP ILE-108. - Ref.6"Structural and functional analyses of human tryptophan 2,3-dioxygenase."
Meng B., Wu D., Gu J., Ouyang S., Ding W., Liu Z.J.
Proteins 82:3210-3216(2014) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 19-388 OF APOPROTEIN, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-42; TYR-45; PHE-72; HIS-76; PHE-140; ARG-144; SER-151 AND HIS-328. - Ref.7"Molecular basis for catalysis and substrate-mediated cellular stabilization of human tryptophan 2,3-dioxygenase."
Lewis-Ballester A., Forouhar F., Kim S.M., Lew S., Wang Y., Karkashon S., Seetharaman J., Batabyal D., Chiang B.Y., Hussain M., Correia M.A., Yeh S.R., Tong L.
Sci. Rep. 6:35169-35169(2016) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 18-389 IN COMPLEX WITH HEME AND TRYPTOPHAN, COFACTOR, SUBUNIT, CATALYTIC ACTIVITY, PATHWAY, MUTAGENESIS OF TYR-175.
<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
<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
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 112858, 23 interactors |
Protein interaction database and analysis system More...IntActi | P48775, 25 interactors |
Molecular INTeraction database More...MINTi | P48775 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000444788 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P48775 |
<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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 42 – 45 | 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 | 48 – 51 | 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 | 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 | 68 – 98 | 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 | 31 | |
| <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 | 101 – 103 | 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 | 105 – 107 | 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 | 108 – 127 | 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 | 20 | |
| <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 | 129 – 132 | 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 | 137 – 140 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 141 – 143 | 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 | 144 – 146 | 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 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 | 147 – 149 | 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 | 152 – 154 | 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 | 156 – 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 | 10 | |
| <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 | 169 – 171 | 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 | 174 – 177 | 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 | 186 – 197 | 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 | 201 – 210 | 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 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 | 217 – 220 | 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 | 222 – 243 | 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 | 22 | |
| <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 | 246 – 248 | 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 | 252 – 266 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 270 – 276 | 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 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 | 277 – 280 | 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 | 286 – 297 | 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 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 | 298 – 300 | 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 | 302 – 336 | 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 | 35 | |
| <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 | 348 – 352 | 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 | 357 – 359 | 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 | 363 – 367 | 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 | 368 – 371 | 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 | 375 – 377 | 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 | 383 – 388 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P48775 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P48775 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<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 | 72 – 76 | Substrate bindingUniRule 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 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 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
| 5 |
<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
<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
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3906 Eukaryota COG3483 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000008593 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000221584 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG003043 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P48775 |
KEGG Orthology (KO) More...KOi | K00453 |
Identification of Orthologs from Complete Genome Data More...OMAi | YWDLYQL |
Database of Orthologous Groups More...OrthoDBi | EOG091G080K |
Database for complete collections of gene phylogenies More...PhylomeDBi | P48775 |
TreeFam database of animal gene trees More...TreeFami | TF105827 |
Family and domain databases
HAMAP database of protein families More...HAMAPi | MF_01972 T23O, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR037217 Trp/Indoleamine_2_3_dOase-like IPR004981 Trp_2_3_dOase |
The PANTHER Classification System More...PANTHERi | PTHR10138 PTHR10138, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03301 Trp_dioxygenase, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF140959 SSF140959, 2 hits |
<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>Sequencei
<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.
10 20 30 40 50
MSGCPFLGNN FGYTFKKLPV EGSEEDKSQT GVNRASKGGL IYGNYLHLEK
60 70 80 90 100
VLNAQELQSE TKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG
110 120 130 140 150
HVRDERNMLK VVSRMHRVSV ILKLLVQQFS ILETMTALDF NDFREYLSPA
160 170 180 190 200
SGFQSLQFRL LENKIGVLQN MRVPYNRRHY RDNFKGEENE LLLKSEQEKT
210 220 230 240 250
LLELVEAWLE RTPGLEPHGF NFWGKLEKNI TRGLEEEFIR IQAKEESEEK
260 270 280 290 300
EEQVAEFQKQ KEVLLSLFDE KRHEHLLSKG ERRLSYRALQ GALMIYFYRE
310 320 330 340 350
EPRFQVPFQL LTSLMDIDSL MTKWRYNHVC MVHRMLGSKA GTGGSSGYHY
360 370 380 390 400
LRSTVSDRYK VFVDLFNLST YLIPRHWIPK MNPTIHKFLY TAEYCDSSYF
SSDESD
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_080251 | 108 | M → I in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization. 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 |
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 | U32989 mRNA Translation: AAB08514.1 AK289418 mRNA Translation: BAF82107.1 CH471056 Genomic DNA Translation: EAX04885.1 BC005355 mRNA Translation: AAH05355.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS34086.1 |
Protein sequence database of the Protein Information Resource More...PIRi | G02022 |
NCBI Reference Sequences More...RefSeqi | NP_005642.1, NM_005651.3 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.183671 Hs.593955 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000536354; ENSP00000444788; ENSG00000151790 ENST00000573403; ENSP00000460086; ENSG00000262635 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6999 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6999 |
UCSC genome browser More...UCSCi | uc003ipf.3 human |
<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 | |
|---|---|---|---|---|---|
| P48775 | Tryptophan 2,3-dioxygenase | 406 | |||
| Tryptophan 2,3-dioxygenase | 406 | ||||
| Tryptophan 2,3-dioxygenase (Fragment) | 49 | ||||
| TDO2 isoform 5 (Fragment) | 49 | ||||
| TDO2 isoform 4 (Fragment) | 49 | ||||
| +3 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P48775 | Tryptophan 2,3-dioxygenase | 406 | |||
| Tryptophan 2,3-dioxygenase | 406 | ||||
| Tryptophan 2,3-dioxygenase (Fragment) | 49 | ||||
| TDO2 isoform 5 (Fragment) | 49 | ||||
| TDO2 isoform 4 (Fragment) | 49 | ||||
| +99 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P48775 | Tryptophan 2,3-dioxygenase | 406 | |||
| Tryptophan 2,3-dioxygenase | 406 | ||||
| Tryptophan 2,3-dioxygenase (Fragment) | 49 | ||||
| TDO2 isoform 5 (Fragment) | 49 | ||||
| TDO2 isoform 4 (Fragment) | 49 | ||||
| +295 | |||||
<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 | U32989 mRNA Translation: AAB08514.1 AK289418 mRNA Translation: BAF82107.1 CH471056 Genomic DNA Translation: EAX04885.1 BC005355 mRNA Translation: AAH05355.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS34086.1 |
Protein sequence database of the Protein Information Resource More...PIRi | G02022 |
NCBI Reference Sequences More...RefSeqi | NP_005642.1, NM_005651.3 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.183671 Hs.593955 |
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 |
| 4PW8 | X-ray | 2.90 | A/B/C/D/E/F/G/H | 19-388 | [»] | |
| 5TI9 | X-ray | 2.50 | A/B/C/D | 18-389 | [»] | |
| 5TIA | X-ray | 2.44 | A/B/C/D | 18-389 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P48775 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P48775 | |||||
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 | 112858, 23 interactors |
Protein interaction database and analysis system More...IntActi | P48775, 25 interactors |
Molecular INTeraction database More...MINTi | P48775 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000444788 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P48775 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2140 |
Drug and drug target database More...DrugBanki | DB00150 L-Tryptophan DB00779 Nalidixic Acid DB00500 Tolmetin |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2887 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P48775 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P48775 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | TDO2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 1351188 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P48775 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P48775 |
PeptideAtlas More...PeptideAtlasi | P48775 |
PRoteomics IDEntifications database More...PRIDEi | P48775 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 55947 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 6999 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000536354; ENSP00000444788; ENSG00000151790 ENST00000573403; ENSP00000460086; ENSG00000262635 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 6999 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:6999 |
UCSC genome browser More...UCSCi | uc003ipf.3 human |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 6999 |
DisGeNET More...DisGeNETi | 6999 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000151790.8 |
GeneCards: human genes, protein and diseases More...GeneCardsi | TDO2 |
Human Gene Nomenclature Database More...HGNCi | HGNC:11708 TDO2 |
Human Protein Atlas More...HPAi | HPA039611 |
MalaCards human disease database More...MalaCardsi | TDO2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 191070 gene 600627 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P48775 |
Open Targets More...OpenTargetsi | ENSG00000151790 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA36427 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3906 Eukaryota COG3483 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00390000008593 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000221584 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG003043 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P48775 |
KEGG Orthology (KO) More...KOi | K00453 |
Identification of Orthologs from Complete Genome Data More...OMAi | YWDLYQL |
Database of Orthologous Groups More...OrthoDBi | EOG091G080K |
Database for complete collections of gene phylogenies More...PhylomeDBi | P48775 |
TreeFam database of animal gene trees More...TreeFami | TF105827 |
Enzyme and pathway databases
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00333; UER00453 |
BioCyc Collection of Pathway/Genome Databases More...BioCyci | MetaCyc:HS07771-MONOMER |
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 1.13.11.11 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-71240 Tryptophan catabolism |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | TDO2 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | TDO2 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 6999 |
Protein Ontology More...PROi | PR:P48775 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000151790 |
CleanEx database of gene expression profiles More...CleanExi | HS_TDO2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P48775 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P48775 HS |
Family and domain databases
HAMAP database of protein families More...HAMAPi | MF_01972 T23O, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR037217 Trp/Indoleamine_2_3_dOase-like IPR004981 Trp_2_3_dOase |
The PANTHER Classification System More...PANTHERi | PTHR10138 PTHR10138, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03301 Trp_dioxygenase, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF140959 SSF140959, 2 hits |
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 | T23O_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 | P48775Primary (citable) accession number: P48775 Secondary accession number(s): A8K053 | |
| <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: | February 1, 1996 |
| Last sequence update: | February 1, 1996 | |
| Last modified: | July 18, 2018 | |
| This is version 158 of the entry and version 1 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 - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - 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
