TDO2

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

Catalytic activityⁱ

L-tryptophan
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O₂
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
N-formyl-L-kynurenine
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_03020
3 Publications
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.
EC:
1.13.11.11
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_03020
3 Publications
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.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
L-tryptophan
zoom
+
O₂
=
N-formyl-L-kynurenine
zoom

Cofactorⁱ

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

Kineticsⁱ

kcat is 0.54 sec(-1) with L-tryptophan as substrate.1 Publication

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 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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	144	SubstrateUniRule annotationCombined sources1 Publication	1
Metal bindingⁱ	328	Iron (heme axial ligand)UniRule annotationCombined sources1 Publication	1
Binding siteⁱ	342	SubstrateUniRule annotationCombined sources1 Publication	1

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Dioxygenase, Oxidoreductase
Biological process	Tryptophan catabolism
Ligand	Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	1.13.11.11, 2681 1.13.11.52, 2681
PathwayCommonsⁱ	P48775
Reactomeⁱ	R-HSA-71240, Tryptophan catabolism
SABIO-RKⁱ	P48775
SignaLinkⁱ	P48775
UniPathwayⁱ	UPA00333;UER00453

Names & Taxonomyⁱ

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
Gene namesⁱ	Name:TDO2UniRule annotation Synonyms:TDO
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
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
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 4

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:11708, TDO2
MIMⁱ	191070, gene
neXtProtⁱ	NX_P48775
VEuPathDBⁱ	HostDB:ENSG00000151790

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Hypertryptophanemia (HYPTRP)1 Publication

The disease is caused by variants affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive condition characterized by persistent hypertryptophanemia and hyperserotoninemia.

Related information in OMIM

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_080251	108	M → I in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization. 1 PublicationCorresponds to variant dbSNP:rs1553957997EnsemblClinVar.		1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	42	Y → A: Reduces enzyme activity by 99%. 1 Publication	1
Mutagenesisⁱ	45	Y → A: Reduces enzyme activity by 99%. 1 Publication	1
Mutagenesisⁱ	72	F → A: Abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	76	H → A: Abolishes enzyme activity. 1 Publication	1
Mutagenesisⁱ	140	F → A: Reduces enzyme activity by 99%. 1 Publication	1
Mutagenesisⁱ	144	R → A: Reduces enzyme activity by 99%. 1 Publication	1
Mutagenesisⁱ	151	S → A: Reduces enzyme activity by 90%. 1 Publication	1
Mutagenesisⁱ	175	Y → G: Reduces enzyme activity. 1 Publication	1
Mutagenesisⁱ	328	H → A: Abolishes enzyme activity. 1 Publication	1

Keywords - Diseaseⁱ

Disease variant

Organism-specific databases

DisGeNET More...DisGeNETⁱ	6999
MalaCards human disease database More...MalaCardsⁱ	TDO2
MIMⁱ	600627, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000151790
Orphanetⁱ	2224, Hypertryptophanemia
PharmGKBⁱ	PA36427

Miscellaneous databases

Pharosⁱ	P48775, Tchem

Pharosⁱ

P48775, Tchem

Chemistry databases

ChEMBLⁱ	CHEMBL2140
Drug and drug target database More...DrugBankⁱ	DB00779, Nalidixic acid DB00500, Tolmetin DB00150, Tryptophan
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2887

Genetic variation databases

BioMutaⁱ	TDO2
DMDMⁱ	1351188

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000072399	1 – 406	Tryptophan 2,3-dioxygenaseAdd BLAST		406

Proteomic databases

EPDⁱ	P48775
MassIVEⁱ	P48775
PaxDbⁱ	P48775
PeptideAtlas More...PeptideAtlasⁱ	P48775
PRIDEⁱ	P48775
ProteomicsDBⁱ	55947

PTM databases

iPTMnetⁱ	P48775
PhosphoSitePlusⁱ	P48775

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000151790, Expressed in liver and 137 other tissues
ExpressionAtlasⁱ	P48775, baseline and differential
Genevisibleⁱ	P48775, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000151790, Tissue enriched (liver)

HPAⁱ

ENSG00000151790, Tissue enriched (liver)

Interactionⁱ

Subunit structureⁱ

Homotetramer. Dimer of dimers.

UniRule annotation3 Publications

Binary interactionsⁱ

Hide details

P48775

With	#Exp.	IntAct
AHCYL1 [O43865]	3	EBI-743494,EBI-2371423
ASMTL [O95671]	11	EBI-743494,EBI-743231
CALR [P27797]	3	EBI-743494,EBI-1049597
CDH1 [P12830]	3	EBI-743494,EBI-727477
DLST [P36957]	3	EBI-743494,EBI-351007
DPM1 [O60762]	6	EBI-743494,EBI-719526
EIF4E [P06730]	4	EBI-743494,EBI-73440
LNX1 [Q8TBB1]	3	EBI-743494,EBI-739832
MOB1A [Q9H8S9]	6	EBI-743494,EBI-748229
MOB3C [Q70IA8]	3	EBI-743494,EBI-9679267
NEK7 [Q8TDX7]	3	EBI-743494,EBI-1055945
NGB [Q9NPG2]	6	EBI-743494,EBI-10311409
NMNAT1 [Q9HAN9]	4	EBI-743494,EBI-3917542
NR1D1 [P20393]	3	EBI-743494,EBI-2811738
PICK1 [Q9NRD5]	3	EBI-743494,EBI-79165
PM20D2 [Q8IYS1]	3	EBI-743494,EBI-11339910
SDCBP [O00560]	7	EBI-743494,EBI-727004
SDCBP2 [Q9H190]	4	EBI-743494,EBI-742426
itself	6	EBI-743494,EBI-743494
ZFYVE26 - isoform 5 [Q68DK2-5]	6	EBI-743494,EBI-8656416

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	112858, 27 interactors
IntActⁱ	P48775, 24 interactors
Molecular INTeraction database More...MINTⁱ	P48775
STRINGⁱ	9606.ENSP00000444788

Chemistry databases

BindingDBⁱ

P48775

Miscellaneous databases

RNActⁱ	P48775, protein

RNActⁱ

P48775, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	42 – 45	Combined sources	4
Helixⁱ	48 – 51	Combined sources	4
Helixⁱ	58 – 61	Combined sources	4
Helixⁱ	69 – 98	Combined sources	30
Helixⁱ	101 – 103	Combined sources	3
Helixⁱ	105 – 107	Combined sources	3
Helixⁱ	108 – 132	Combined sources	25
Helixⁱ	137 – 140	Combined sources	4
Turnⁱ	141 – 143	Combined sources	3
Helixⁱ	144 – 146	Combined sources	3
Turnⁱ	147 – 149	Combined sources	3
Helixⁱ	152 – 154	Combined sources	3
Helixⁱ	156 – 165	Combined sources	10
Helixⁱ	169 – 171	Combined sources	3
Helixⁱ	174 – 179	Combined sources	6
Helixⁱ	181 – 183	Combined sources	3
Helixⁱ	186 – 197	Combined sources	12
Helixⁱ	201 – 210	Combined sources	10
Turnⁱ	217 – 220	Combined sources	4
Helixⁱ	222 – 242	Combined sources	21
Helixⁱ	248 – 266	Combined sources	19
Helixⁱ	270 – 278	Combined sources	9
Helixⁱ	286 – 297	Combined sources	12
Turnⁱ	298 – 300	Combined sources	3
Helixⁱ	302 – 304	Combined sources	3
Helixⁱ	305 – 336	Combined sources	32
Helixⁱ	348 – 352	Combined sources	5
Helixⁱ	357 – 359	Combined sources	3
Helixⁱ	363 – 367	Combined sources	5
Helixⁱ	368 – 371	Combined sources	4
Helixⁱ	375 – 377	Combined sources	3
Helixⁱ	383 – 388	Combined sources	6

Show more details

3D structure databases

SMRⁱ	P48775
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	72 – 76	Substrate bindingUniRule annotationCombined sources1 Publication		5

Sequence similaritiesⁱ

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

Phylogenomic databases

eggNOGⁱ	KOG3906, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000008593
HOGENOMⁱ	CLU_045599_1_1_1
InParanoidⁱ	P48775
OMAⁱ	MLVPHRG
Database of Orthologous Groups More...OrthoDBⁱ	497681at2759
PhylomeDBⁱ	P48775
TreeFamⁱ	TF105827

Family and domain databases

HAMAPⁱ	MF_01972, T23O, 1 hit
InterProⁱ	View protein in InterPro IPR037217, Trp/Indoleamine_2_3_dOase-like IPR004981, Trp_2_3_dOase
PANTHERⁱ	PTHR10138, PTHR10138, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF03301, Trp_dioxygenase, 1 hit
SUPFAMⁱ	SSF140959, SSF140959, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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

P48775-1 [UniParc]FASTA Add 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

Checksum:ⁱ1B89901F445B79FE

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

D6RA50	D6RA50_HUMAN	Tryptophan 2,3-dioxygenase Tryptophan 2,3-dioxygenase	TDO2	65	Annotation score:
D6RB68	D6RB68_HUMAN	Tryptophan 2,3-dioxygenase Tryptophan 2,3-dioxygenase	TDO2	49	Annotation score:

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_080251	108	M → I in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization. 1 PublicationCorresponds to variant dbSNP:rs1553957997EnsemblClinVar.		1

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS34086.1
PIRⁱ	G02022
NCBI Reference Sequences More...RefSeqⁱ	NP_005642.1, NM_005651.3

Genome annotation databases

Ensemblⁱ	ENST00000536354; ENSP00000444788; ENSG00000151790 ENST00000573403; ENSP00000460086; ENSG00000262635
GeneIDⁱ	6999
KEGGⁱ	hsa:6999
MANE-Selectⁱ	ENST00000536354.3; ENSP00000444788.2; NM_005651.4; NP_005642.1
UCSC genome browser More...UCSCⁱ	uc003ipf.3, human

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P48775	Tryptophan 2,3-dioxygenase		PANPA		406	UniRef100_P48775
Tryptophan 2,3-dioxygenase		GORGO		406
Tryptophan 2,3-dioxygenase (Fragment)		HUMAN		49
TDO2 isoform 5 (Fragment)		PONAB		49
TDO2 isoform 4 (Fragment)		PANTR		49
+3

Protein	Similar proteins		Species	Score	Length	Source
P48775	Tryptophan 2,3-dioxygenase		BOVIN		406	UniRef90_P48775
Tryptophan 2,3-dioxygenase		PANPA		406
Tryptophan 2,3-dioxygenase		GORGO		406
Tryptophan 2,3-dioxygenase (Fragment)		HUMAN		49
TDO2 isoform 5 (Fragment)		PONAB		49
+81

Protein	Similar proteins		Species	Score	Length	Source
P48775	Tryptophan 2,3-dioxygenase		BOVIN		406	UniRef50_P48775
Tryptophan 2,3-dioxygenase		RAT		406
Tryptophan 2,3-dioxygenase		MOUSE		406
Tryptophan 2,3-dioxygenase A		DANRE		406
Tryptophan 2,3-dioxygenase		PANPA		406
+590

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
CCDSⁱ	CCDS34086.1
PIRⁱ	G02022
RefSeqⁱ	NP_005642.1, NM_005651.3

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 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	[»]
	6A4I	X-ray	2.65	A/B/C/D	19-388	[»]
	6PYY	X-ray	2.40	A/B/C/D	18-389	[»]
	6PYZ	X-ray	2.02	A/B/C/D	18-389	[»]
	6UD5	X-ray	2.05	A/B/C/D	18-389	[»]
	6VBN	X-ray	3.18	A/B/C/D	18-388	[»]
SMRⁱ	P48775
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	112858, 27 interactors
IntActⁱ	P48775, 24 interactors
MINTⁱ	P48775
STRINGⁱ	9606.ENSP00000444788

Chemistry databases

BindingDBⁱ	P48775
ChEMBLⁱ	CHEMBL2140
DrugBankⁱ	DB00779, Nalidixic acid DB00500, Tolmetin DB00150, Tryptophan
GuidetoPHARMACOLOGYⁱ	2887

PTM databases

iPTMnetⁱ	P48775
PhosphoSitePlusⁱ	P48775

Genetic variation databases

BioMutaⁱ	TDO2
DMDMⁱ	1351188

Proteomic databases

EPDⁱ	P48775
MassIVEⁱ	P48775
PaxDbⁱ	P48775
PeptideAtlasⁱ	P48775
PRIDEⁱ	P48775
ProteomicsDBⁱ	55947

Protocols and materials databases

Antibodypediaⁱ	28079, 311 antibodies from 25 providers
The DNASU plasmid repository More...DNASUⁱ	6999

Genome annotation databases

Ensemblⁱ	ENST00000536354; ENSP00000444788; ENSG00000151790 ENST00000573403; ENSP00000460086; ENSG00000262635
GeneIDⁱ	6999
KEGGⁱ	hsa:6999
MANE-Selectⁱ	ENST00000536354.3; ENSP00000444788.2; NM_005651.4; NP_005642.1
UCSCⁱ	uc003ipf.3, human

Organism-specific databases

CTDⁱ	6999
DisGeNETⁱ	6999
GeneCardsⁱ	TDO2
HGNCⁱ	HGNC:11708, TDO2
HPAⁱ	ENSG00000151790, Tissue enriched (liver)
MalaCardsⁱ	TDO2
MIMⁱ	191070, gene 600627, phenotype
neXtProtⁱ	NX_P48775
OpenTargetsⁱ	ENSG00000151790
Orphanetⁱ	2224, Hypertryptophanemia
PharmGKBⁱ	PA36427
VEuPathDBⁱ	HostDB:ENSG00000151790
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3906, Eukaryota
GeneTreeⁱ	ENSGT00390000008593
HOGENOMⁱ	CLU_045599_1_1_1
InParanoidⁱ	P48775
OMAⁱ	MLVPHRG
OrthoDBⁱ	497681at2759
PhylomeDBⁱ	P48775
TreeFamⁱ	TF105827

Enzyme and pathway databases

UniPathwayⁱ	UPA00333;UER00453
BRENDAⁱ	1.13.11.11, 2681 1.13.11.52, 2681
PathwayCommonsⁱ	P48775
Reactomeⁱ	R-HSA-71240, Tryptophan catabolism
SABIO-RKⁱ	P48775
SignaLinkⁱ	P48775

Miscellaneous databases

BioGRID-ORCSⁱ	6999, 11 hits in 1035 CRISPR screens
ChiTaRSⁱ	TDO2, human
GeneWikiⁱ	TDO2
GenomeRNAiⁱ	6999
Pharosⁱ	P48775, Tchem
Protein Ontology More...PROⁱ	PR:P48775
RNActⁱ	P48775, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000151790, Expressed in liver and 137 other tissues
ExpressionAtlasⁱ	P48775, baseline and differential
Genevisibleⁱ	P48775, HS

Family and domain databases

HAMAPⁱ	MF_01972, T23O, 1 hit
InterProⁱ	View protein in InterPro IPR037217, Trp/Indoleamine_2_3_dOase-like IPR004981, Trp_2_3_dOase
PANTHERⁱ	PTHR10138, PTHR10138, 1 hit
Pfamⁱ	View protein in Pfam PF03301, Trp_dioxygenase, 1 hit
SUPFAMⁱ	SSF140959, SSF140959, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	T23O_HUMAN
Accessionⁱ	P48775Primary (citable) accession number: P48775 Secondary accession number(s): A8K053
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
	Last sequence update:	February 1, 1996
	Last modified:	February 23, 2022
	This is version 180 of the entry and version 1 of the sequence. See complete history.
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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

Human chromosome 4
Human chromosome 4: entries, gene names and cross-references to MIM
Human entries with genetic variants
List of human entries with genetic variants
Human variants curated from literature reports
Index of human variants curated from literature reports
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

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UniProtKB - P48775 (T23O_HUMAN)

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Tryptophan 2,3-dioxygenase

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<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

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P48775

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

Pathwayⁱ: L-tryptophan degradation via kynurenine pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ