UniProtKB - P48775 (T23O_HUMAN)

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

Align
Format
Add to basket Added to basket
History
Entry version 161 (07 Nov 2018)
Sequence version 1 (01 Feb 1996)
Previous versions | rss
Other tutorials and videos
Help video
Feedback

Protein

Tryptophan 2,3-dioxygenase

Gene

TDO2

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

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 + O₂ = N-formyl-L-kynurenine.UniRule annotation3 Publications

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
Proteins known to be involved in the 2 steps of the subpathway in this organism are:

Indoleamine 2,3-dioxygenase 1 (IDO1), Indoleamine 2,3-dioxygenase 2 (IDO2), Tryptophan 2,3-dioxygenase (TDO2)
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 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

amino acid binding Source: Ensembl
heme binding
Source: UniProtKB
Inferred from direct assayⁱ
- 27762317
- 28285122
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 25416956
metal ion binding Source: UniProtKB-KW
oxygen binding Source: Ensembl
tryptophan 2,3-dioxygenase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 27762317
- 28285122

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

protein homotetramerization
Source: UniProtKB
Inferred from direct assayⁱ
- 27762317
- 28285122
response to nitroglycerin Source: Ensembl
tryptophan catabolic process Source: Reactome
tryptophan catabolic process to acetyl-CoA
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
tryptophan catabolic process to kynurenine
Source: UniProtKB
Inferred from direct assayⁱ
- 27762317

View the complete GO annotation on QuickGO ...

Keywordsⁱ

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

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS07771-MONOMER
BRENDAⁱ	1.13.11.11 2681
Reactomeⁱ	R-HSA-71240 Tryptophan catabolism
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

EuPathDBⁱ	HostDB:ENSG00000151790.8
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:11708 TDO2
MIMⁱ	191070 gene
neXtProtⁱ	NX_P48775

Subcellular locationⁱ

GO - Cellular component

Pathology & Biotechⁱ

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.

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 mutation

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

Chemistry databases

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

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

PTM databases

iPTMnetⁱ	P48775
PhosphoSitePlusⁱ	P48775

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000151790 Expressed in 118 organ(s), highest expression level in liver
CleanExⁱ	HS_TDO2
ExpressionAtlasⁱ	P48775 baseline and differential
Genevisibleⁱ	P48775 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA039611

HPAⁱ

HPA039611

Interactionⁱ

Subunit structureⁱ

Homotetramer. Dimer of dimers.UniRule annotation3 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
itself		3	EBI-743494,EBI-743494
ASMTL	O95671	8	EBI-743494,EBI-743231
DPM1	O60762	6	EBI-743494,EBI-719526
EIF4E	P06730	3	EBI-743494,EBI-73440
MOB1A	Q9H8S9	5	EBI-743494,EBI-748229
MOB3C	Q70IA8	3	EBI-743494,EBI-9679267
NGB	Q9NPG2	5	EBI-743494,EBI-10311409
PICK1	Q9NRD5	4	EBI-743494,EBI-79165
PM20D2	Q8IYS1	4	EBI-743494,EBI-11339910
SDCBP	O00560	7	EBI-743494,EBI-727004
SDCBP2	Q9H190	3	EBI-743494,EBI-742426
ZFYVE26	Q68DK2-5	5	EBI-743494,EBI-8656416

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- 25416956

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	112858, 23 interactors
IntActⁱ	P48775, 19 interactors
Molecular INTeraction database More...MINTⁱ	P48775
STRINGⁱ	9606.ENSP00000444788

Chemistry databases

BindingDBⁱ

P48775

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	68 – 98	Combined sources	31
Helixⁱ	101 – 103	Combined sources	3
Helixⁱ	105 – 107	Combined sources	3
Helixⁱ	108 – 127	Combined sources	20
Helixⁱ	129 – 132	Combined sources	4
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
Turnⁱ	169 – 171	Combined sources	3
Helixⁱ	174 – 177	Combined sources	4
Helixⁱ	186 – 197	Combined sources	12
Helixⁱ	201 – 210	Combined sources	10
Turnⁱ	217 – 220	Combined sources	4
Helixⁱ	222 – 243	Combined sources	22
Beta strandⁱ	246 – 248	Combined sources	3
Helixⁱ	252 – 266	Combined sources	15
Helixⁱ	270 – 276	Combined sources	7
Turnⁱ	277 – 280	Combined sources	4
Helixⁱ	286 – 297	Combined sources	12
Turnⁱ	298 – 300	Combined sources	3
Helixⁱ	302 – 336	Combined sources	35
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

ProteinModelPortalⁱ	P48775
SMRⁱ	P48775
ModBaseⁱ	Search...
MobiDBⁱ	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 COG3483 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000008593
HOGENOMⁱ	HOG000221584
HOVERGENⁱ	HBG003043
InParanoidⁱ	P48775
KEGG Orthology (KO) More...KOⁱ	K00453
OMAⁱ	YWDLYQL
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G080K
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

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 Publication		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
UniGeneⁱ	Hs.183671 Hs.593955

Genome annotation databases

Ensemblⁱ	ENST00000536354; ENSP00000444788; ENSG00000151790 ENST00000573403; ENSP00000460086; ENSG00000262635
GeneIDⁱ	6999
KEGGⁱ	hsa:6999
UCSC genome browser More...UCSCⁱ	uc003ipf.3 human

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		PANPA		406	UniRef90_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
+42

Protein	Similar proteins		Species	Score	Length	Source
P48775	Tryptophan 2,3-dioxygenase		XENLA		406	UniRef50_P48775
Tryptophan 2,3-dioxygenase		XENTR		406
Tryptophan 2,3-dioxygenase B		DANRE		407
Tryptophan 2,3-dioxygenase		RAT		406
Tryptophan 2,3-dioxygenase		MOUSE		406
+309

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
UniGeneⁱ	Hs.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 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	[»]
ProteinModelPortalⁱ	P48775
SMRⁱ	P48775
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	112858, 23 interactors
IntActⁱ	P48775, 19 interactors
MINTⁱ	P48775
STRINGⁱ	9606.ENSP00000444788

Chemistry databases

BindingDBⁱ	P48775
ChEMBLⁱ	CHEMBL2140
DrugBankⁱ	DB00150 L-Tryptophan DB00779 Nalidixic Acid DB00500 Tolmetin
GuidetoPHARMACOLOGYⁱ	2887

PTM databases

iPTMnetⁱ	P48775
PhosphoSitePlusⁱ	P48775

Polymorphism and mutation databases

BioMutaⁱ	TDO2
DMDMⁱ	1351188

Proteomic databases

EPDⁱ	P48775
PaxDbⁱ	P48775
PeptideAtlasⁱ	P48775
PRIDEⁱ	P48775
ProteomicsDBⁱ	55947

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	6999
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000536354; ENSP00000444788; ENSG00000151790 ENST00000573403; ENSP00000460086; ENSG00000262635
GeneIDⁱ	6999
KEGGⁱ	hsa:6999
UCSCⁱ	uc003ipf.3 human

Organism-specific databases

CTDⁱ	6999
DisGeNETⁱ	6999
EuPathDBⁱ	HostDB:ENSG00000151790.8
GeneCardsⁱ	TDO2
HGNCⁱ	HGNC:11708 TDO2
HPAⁱ	HPA039611
MalaCardsⁱ	TDO2
MIMⁱ	191070 gene 600627 phenotype
neXtProtⁱ	NX_P48775
OpenTargetsⁱ	ENSG00000151790
Orphanetⁱ	2224 Hypertryptophanemia
PharmGKBⁱ	PA36427
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3906 Eukaryota COG3483 LUCA
GeneTreeⁱ	ENSGT00390000008593
HOGENOMⁱ	HOG000221584
HOVERGENⁱ	HBG003043
InParanoidⁱ	P48775
KOⁱ	K00453
OMAⁱ	YWDLYQL
OrthoDBⁱ	EOG091G080K
PhylomeDBⁱ	P48775
TreeFamⁱ	TF105827

Enzyme and pathway databases

UniPathwayⁱ	UPA00333;UER00453
BioCycⁱ	MetaCyc:HS07771-MONOMER
BRENDAⁱ	1.13.11.11 2681
Reactomeⁱ	R-HSA-71240 Tryptophan catabolism

Miscellaneous databases

ChiTaRSⁱ	TDO2 human
GeneWikiⁱ	TDO2
GenomeRNAiⁱ	6999
Protein Ontology More...PROⁱ	PR:P48775
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000151790 Expressed in 118 organ(s), highest expression level in liver
CleanExⁱ	HS_TDO2
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
ProtoNetⁱ	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:	November 7, 2018
	This is version 161 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, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P48775 (T23O_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Tryptophan 2,3-dioxygenase

TDO2

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>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>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

Sites

<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

GO - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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

<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

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

Proteomic databases

PTM databases

<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

Organism-specific databases

<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

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

<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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Natural variant

Sequence databases

Genome annotation databases

<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

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<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 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

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

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