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UniProtKB - P48775 (T23O_HUMAN)

Protein

Tryptophan 2,3-dioxygenase

Gene

TDO2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

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>

<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

Heme-dependent dioxygenase that catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring and converts L-tryptophan to N-formyl-L-kynurenine. Catalyzes the oxidative cleavage of the indole moiety.UniRule annotation3 Publications

<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. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

hemeUniRule annotation3 PublicationsNote: Binds 1 heme group per subunit.UniRule annotation1 Publication

<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

Kcat is 0.54 sec(-1) with L-tryptophan as substrate.1 Publication
  1. KM=0.135 mM for L-tryptophan1 Publication
  2. KM=0.132 mM for L-tryptophan1 Publication

    <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 annotation2 Publications
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Indoleamine 2,3-dioxygenase 2 (IDO2), Tryptophan 2,3-dioxygenase (TDO2), Indoleamine 2,3-dioxygenase 1 (IDO1)
    2. Kynurenine formamidase (AFMID)
    This subpathway is part of the pathway L-tryptophan degradation via kynurenine pathway, which is itself part of Amino-acid degradation.
    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 keyPosition(s)DescriptionActionsGraphical viewLength
    <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 sitei144SubstrateUniRule annotationCombined sources1 Publication1
    <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 bindingi328Iron (heme axial ligand)UniRule annotationCombined sources1 Publication1
    Binding sitei342SubstrateUniRule annotationCombined sources1 Publication1

    <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
    • identical protein binding Source: IntAct
    • metal ion binding Source: UniProtKB-KW
    • oxygen binding Source: Ensembl
    • tryptophan 2,3-dioxygenase activity Source: UniProtKB
    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    <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 functionDioxygenase, Oxidoreductase
    Biological processTryptophan catabolism
    LigandHeme, 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 (EC:1.13.11.11UniRule annotation3 Publications)
    Short name:
    TDOUniRule annotation
    Alternative name(s):
    Tryptamin 2,3-dioxygenaseUniRule annotation
    Tryptophan oxygenaseUniRule annotation
    Short name:
    TOUniRule annotation
    Short name:
    TRPOUniRule annotation
    Tryptophan pyrrolaseUniRule annotation
    TryptophanaseUniRule annotation
    <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
    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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

    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

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    <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
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn autosomal recessive condition characterized by persistent hypertryptophanemia and hyperserotoninemia.
    See also OMIM:600627
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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_080251108M → I in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization. 1 Publication1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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>Mutagenesisi42Y → A: Reduces enzyme activity by 99%. 1 Publication1
    Mutagenesisi45Y → A: Reduces enzyme activity by 99%. 1 Publication1
    Mutagenesisi72F → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi76H → A: Abolishes enzyme activity. 1 Publication1
    Mutagenesisi140F → A: Reduces enzyme activity by 99%. 1 Publication1
    Mutagenesisi144R → A: Reduces enzyme activity by 99%. 1 Publication1
    Mutagenesisi151S → A: Reduces enzyme activity by 90%. 1 Publication1
    Mutagenesisi175Y → G: Reduces enzyme activity. 1 Publication1
    Mutagenesisi328H → A: Abolishes enzyme activity. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		6999

    MalaCards human disease database

    More...    MalaCardsi    		TDO2
    MIMi600627 phenotype

    Open Targets

    More...    OpenTargetsi    		ENSG00000151790

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...    Orphaneti    		2224 Hypertryptophanemia

    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 keyPosition(s)DescriptionActionsGraphical viewLength
    <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_00000723991 – 406Tryptophan 2,3-dioxygenaseAdd BLAST406

    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 Expressed in 118 organ(s), highest expression level in liver

    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

    Homotetramer. Dimer of dimers.UniRule annotation3 Publications

    <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

    GO - Molecular functioni

    View the complete GO annotation on QuickGO ...

    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, 19 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

    1406
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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 keyPosition(s)DescriptionActionsGraphical viewLength
    <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>Regioni72 – 76Substrate bindingUniRule annotationCombined sources1 Publication5

    <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

    Belongs to the tryptophan 2,3-dioxygenase family.UniRule annotation

    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, 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>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

    P48775-1 [UniParc]FASTAAdd to basket
    « Hide
            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
    Length:406
    Mass (Da):47,872
    Last modified:February 1, 1996 - v1
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1B89901F445B79FE
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    D6RA50D6RA50_HUMAN
    Tryptophan 2,3-dioxygenase
    TDO2
    		65Annotation score:

    Annotation score:1 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>
    D6RB68D6RB68_HUMAN
    Tryptophan 2,3-dioxygenase
    TDO2
    		49Annotation score:

    Annotation score:1 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>

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_080251108M → I in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization. 1 Publication1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links 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

    <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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		U32989 mRNA Translation: AAB08514.1
    AK289418 mRNA Translation: BAF82107.1
    CH471056 Genomic DNA Translation: EAX04885.1
    BC005355 mRNA Translation: AAH05355.1
    CCDSiCCDS34086.1
    PIRiG02022
    RefSeqiNP_005642.1, NM_005651.3
    UniGeneiHs.183671
    Hs.593955

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4PW8X-ray2.90A/B/C/D/E/F/G/H19-388[»]
    5TI9X-ray2.50A/B/C/D18-389[»]
    5TIAX-ray2.44A/B/C/D18-389[»]
    6A4IX-ray2.65A/B/C/D19-388[»]
    ProteinModelPortaliP48775
    SMRiP48775
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi112858, 23 interactors
    IntActiP48775, 19 interactors
    MINTiP48775
    STRINGi9606.ENSP00000444788

    Chemistry databases

    BindingDBiP48775
    ChEMBLiCHEMBL2140
    DrugBankiDB00150 L-Tryptophan
    DB00779 Nalidixic Acid
    DB00500 Tolmetin
    GuidetoPHARMACOLOGYi2887

    PTM databases

    iPTMnetiP48775
    PhosphoSitePlusiP48775

    Polymorphism and mutation databases

    BioMutaiTDO2
    DMDMi1351188

    Proteomic databases

    EPDiP48775
    PaxDbiP48775
    PeptideAtlasiP48775
    PRIDEiP48775
    ProteomicsDBi55947

    Protocols and materials databases

    The DNASU plasmid repository

    More...    DNASUi    		6999
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000536354; ENSP00000444788; ENSG00000151790
    ENST00000573403; ENSP00000460086; ENSG00000262635
    GeneIDi6999
    KEGGihsa:6999
    UCSCiuc003ipf.3 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		6999
    DisGeNETi6999
    EuPathDBiHostDB:ENSG00000151790.8

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		TDO2
    HGNCiHGNC:11708 TDO2
    HPAiHPA039611
    MalaCardsiTDO2
    MIMi191070 gene
    600627 phenotype
    neXtProtiNX_P48775
    OpenTargetsiENSG00000151790
    Orphaneti2224 Hypertryptophanemia
    PharmGKBiPA36427

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG3906 Eukaryota
    COG3483 LUCA
    GeneTreeiENSGT00390000008593
    HOGENOMiHOG000221584
    HOVERGENiHBG003043
    InParanoidiP48775
    KOiK00453
    OMAiYWDLYQL
    OrthoDBiEOG091G080K
    PhylomeDBiP48775
    TreeFamiTF105827

    Enzyme and pathway databases

    UniPathwayi
    UPA00333;UER00453

    BioCyciMetaCyc:HS07771-MONOMER
    BRENDAi1.13.11.11 2681
    ReactomeiR-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

    BgeeiENSG00000151790 Expressed in 118 organ(s), highest expression level in liver
    CleanExiHS_TDO2
    ExpressionAtlasiP48775 baseline and differential
    GenevisibleiP48775 HS

    Family and domain databases

    HAMAPiMF_01972 T23O, 1 hit
    InterProiView protein in InterPro
    IPR037217 Trp/Indoleamine_2_3_dOase-like
    IPR004981 Trp_2_3_dOase
    PANTHERiPTHR10138 PTHR10138, 1 hit
    PfamiView protein in Pfam
    PF03301 Trp_dioxygenase, 1 hit
    SUPFAMiSSF140959 SSF140959, 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 nameiT23O_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>AccessioniPrimary (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 historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: December 5, 2018
    This is version 162 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 statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    7. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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