PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr0604155; PubMed=17203969 [NCBI, ExPASy, EBI, Israel, Japan]
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry.";
J. Proteome Res. 6:250-262(2007).

Comments

FUNCTION: Incorporates oxygen into the indole moiety of tryptophan. Has a broad specificity towards tryptamine and derivatives including D- and L-tryptophan, 5-hydroxytryptophan and serotonin (By similarity).
CATALYTIC ACTIVITY: L-tryptophan + O₂ = N-formyl-L-kynurenine.
COFACTOR: Binds 2 heme groups per tetramer. The hemes are protoheme IV (By similarity).
PATHWAY: Amino-acid degradation; L-tryptophan degradation via kynurenine pathway; L-kynurenine from L-tryptophan: step 1/2 .
SUBUNIT: Homotetramer (By similarity).
SIMILARITY: Belongs to the tryptophan 2,3-dioxygenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U24493; AAB60491.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

UniGene

Mm.258622

3D structure databases

ModBase

P48776.

PTM databases

PhosphoSite

P48776; -.

Organism-specific databases

MGI

MGI:1928486; Tdo2.

Gene expression databases

ArrayExpress

P48776; -.

CleanEx

MM_TDO2; -.

GermOnline

ENSMUSG00000028011; Mus musculus.

Family and domain databases

InterPro

IPR004981; Trp_2_3_dOase.
Graphical view of domain structure.

PANTHER

PTHR10138; Trp_2_3_dOase; 1.

Pfam

PF03301; Trp_dioxygenase; 1.
Pfam graphical view of domain structure.

BLOCKS

P48776.

Genome annotation databases

Ensembl

ENSMUSG00000028011; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

P48776; -.

HOVERGEN

P48776; -.

Other

Tdo2; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Dioxygenase; Heme; Iron; Metal-binding; Oxidoreductase; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 406`	`406`	`Tryptophan 2,3-dioxygenase.`	`PRO_0000072400`
`MOD_RES`	`19 19`		`Phosphoserine.`
`MOD_RES`	`155 155`		`Phosphoserine (By similarity).`
`VARIANT`	`18 18`	`1`	`L -> V.`

Sequence information

Length: 406 AA [This is the length of the unprocessed precursor]

Molecular weight: 47784 Da [This is the MW of the unprocessed precursor]

CRC64: 1E0A96095920D0F3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGCPFAGNS VGYTLKNLSM EDNEEDRAQT GVNRASKGGL IYGNYLQLEK ILNAQELQSE 

        70         80         90        100        110        120 
VKGNKIHDEH LFIITHQAYE LWFKQILWEL DSVREIFQNG HVRDERNMLK VIARMHRVVV 

       130        140        150        160        170        180 
IFKLLVQQFS VLETMTALDF NDFREYLSPA SGFQSLQFRL LENKIGVLQS LRVPYNRKHY 

       190        200        210        220        230        240 
RDNFGGDYNE LLLKSEQEQT LLQLVEAWLE RTPGLEPNGF NFWGKFEKKI LKGLEEEFLK 

       250        260        270        280        290        300 
IQAKKDSEEK EEQMAEFRKQ KEVLLCLFDE KRHDYLLSKG ERRLSYRALQ GALMIYFYRE 

       310        320        330        340        350        360 
EPRFQVPFQL LTSLMDIDTL MTKWRYNHVC MVHRMLGTKA GTGGSSGYHY LRSTVSDRYK 

       370        380        390        400 
VFVDLFNLST YLVPRHWVPK MNPIIHKFLY TAEYSDSSYF SSDESD

P48776 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools