SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P14902

- I23O1_HUMAN

UniProt

P14902 - I23O1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Indoleamine 2,3-dioxygenase 1
Gene
IDO1, IDO, INDO
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the cleavage of the pyrrol ring of tryptophan and incorporates both atoms of a molecule of oxygen.1 Publication

Catalytic activityi

D-tryptophan + O2 = N-formyl-D-kynurenine.1 Publication
L-tryptophan + O2 = N-formyl-L-kynurenine.1 Publication

Cofactori

Binds 1 heme group per subunit.

Enzyme regulationi

Activity is inhibited by and MTH-trp (methylthiohydantoin-DL-tryptophan), modestly inhibited by L-1MT (1-methyl-L-tryptophan) but not D-1MT (1-methyl-D-tryptophan).1 Publication

Kineticsi

Catalytic efficiency for L-tryptophan is 150 times higher than for D-tryptophan.

  1. KM=21.23 µM for L-tryptophan1 Publication
  2. KM=4.6 mM for D-tryptophan

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi346 – 3461Iron (heme proximal ligand)

GO - Molecular functioni

  1. electron carrier activity Source: UniProtKB
  2. heme binding Source: InterPro
  3. indoleamine 2,3-dioxygenase activity Source: UniProtKB-EC
  4. metal ion binding Source: UniProtKB-KW
  5. tryptophan 2,3-dioxygenase activity Source: Reactome

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. cytokine production involved in inflammatory response Source: Ensembl
  3. female pregnancy Source: ProtInc
  4. kynurenic acid biosynthetic process Source: Ensembl
  5. multicellular organismal response to stress Source: Ensembl
  6. negative regulation of T cell apoptotic process Source: Ensembl
  7. negative regulation of activated T cell proliferation Source: Ensembl
  8. negative regulation of interleukin-10 production Source: Ensembl
  9. positive regulation of T cell tolerance induction Source: Ensembl
  10. positive regulation of apoptotic process Source: Ensembl
  11. positive regulation of chronic inflammatory response Source: Ensembl
  12. positive regulation of interleukin-12 production Source: Ensembl
  13. positive regulation of type 2 immune response Source: Ensembl
  14. response to lipopolysaccharide Source: Ensembl
  15. small molecule metabolic process Source: Reactome
  16. swimming behavior Source: Ensembl
  17. tryptophan catabolic process Source: Reactome
  18. tryptophan catabolic process to kynurenine Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS05502-MONOMER.
BRENDAi1.13.11.11. 2681.
ReactomeiREACT_916. Tryptophan catabolism.
SABIO-RKP14902.
UniPathwayiUPA00333; UER00453.

Names & Taxonomyi

Protein namesi
Recommended name:
Indoleamine 2,3-dioxygenase 1 (EC:1.13.11.52)
Short name:
IDO-1
Alternative name(s):
Indoleamine-pyrrole 2,3-dioxygenase
Gene namesi
Name:IDO1
Synonyms:IDO, INDO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:6059. IDO1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. smooth muscle contractile fiber Source: Ensembl
  3. stereocilium bundle Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29869.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Indoleamine 2,3-dioxygenase 1
PRO_0000215204Add
BLAST

Proteomic databases

PaxDbiP14902.
PRIDEiP14902.

PTM databases

PhosphoSiteiP14902.

Expressioni

Inductioni

By IFNG/IFN-gamma.2 Publications

Gene expression databases

ArrayExpressiP14902.
BgeeiP14902.
GenevestigatoriP14902.

Organism-specific databases

HPAiHPA023072.
HPA023149.
HPA027772.

Interactioni

Protein-protein interaction databases

BioGridi109832. 4 interactions.
IntActiP14902. 3 interactions.
MINTiMINT-1414454.
STRINGi9606.ENSP00000253513.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 163
Turni19 – 213
Helixi34 – 363
Helixi37 – 448
Helixi46 – 516
Helixi55 – 617
Helixi73 – 9220
Beta strandi95 – 973
Beta strandi101 – 1033
Helixi105 – 11814
Helixi126 – 1294
Beta strandi132 – 1387
Helixi145 – 1473
Beta strandi148 – 1514
Helixi160 – 17819
Helixi181 – 1899
Helixi193 – 21422
Helixi217 – 2204
Helixi223 – 2286
Helixi230 – 2334
Beta strandi237 – 2393
Helixi241 – 2433
Beta strandi247 – 2493
Turni250 – 2523
Helixi264 – 2663
Helixi268 – 2769
Beta strandi284 – 2863
Helixi287 – 2959
Helixi296 – 2983
Helixi301 – 31111
Helixi316 – 3216
Turni322 – 3243
Helixi326 – 35328
Helixi355 – 3584
Helixi382 – 39716

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D0TX-ray2.30A/B1-403[»]
2D0UX-ray3.40A/B1-403[»]
ProteinModelPortaliP14902.
SMRiP14902. Positions 11-403.

Miscellaneous databases

EvolutionaryTraceiP14902.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG73554.
HOGENOMiHOG000203926.
HOVERGENiHBG006100.
InParanoidiP14902.
KOiK00463.
OMAiEAYDACV.
PhylomeDBiP14902.
TreeFamiTF330978.

Family and domain databases

InterProiIPR000898. Indolamine_dOase.
[Graphical view]
PfamiPF01231. IDO. 1 hit.
[Graphical view]
PROSITEiPS00876. IDO_1. 1 hit.
PS00877. IDO_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14902-1 [UniParc]FASTAAdd to Basket

« Hide

MAHAMENSWT ISKEYHIDEE VGFALPNPQE NLPDFYNDWM FIAKHLPDLI    50
ESGQLRERVE KLNMLSIDHL TDHKSQRLAR LVLGCITMAY VWGKGHGDVR 100
KVLPRNIAVP YCQLSKKLEL PPILVYADCV LANWKKKDPN KPLTYENMDV 150
LFSFRDGDCS KGFFLVSLLV EIAAASAIKV IPTVFKAMQM QERDTLLKAL 200
LEIASCLEKA LQVFHQIHDH VNPKAFFSVL RIYLSGWKGN PQLSDGLVYE 250
GFWEDPKEFA GGSAGQSSVF QCFDVLLGIQ QTAGGGHAAQ FLQDMRRYMP 300
PAHRNFLCSL ESNPSVREFV LSKGDAGLRE AYDACVKALV SLRSYHLQIV 350
TKYILIPASQ QPKENKTSED PSKLEAKGTG GTDLMNFLKT VRSTTEKSLL 400
KEG 403
Length:403
Mass (Da):45,326
Last modified:April 1, 1990 - v1
Checksum:iE92CF57AD0D0BA8D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti4 – 41A → T.
Corresponds to variant rs35059413 [ dbSNP | Ensembl ].
VAR_053368

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34455 mRNA. Translation: AAA36081.1.
X17668 mRNA. Translation: CAA35663.1.
M86472 Genomic DNA. No translation available.
M86473 Genomic DNA. No translation available.
M86474 Genomic DNA. No translation available.
M86475 Genomic DNA. No translation available.
M86476 Genomic DNA. No translation available.
M86477 Genomic DNA. No translation available.
M86478 Genomic DNA. No translation available.
M86479 Genomic DNA. No translation available.
M86480 Genomic DNA. No translation available.
M86481 Genomic DNA. No translation available.
AY221100 mRNA. Translation: AAO34405.1.
AK313259 mRNA. Translation: BAG36069.1.
BC027882 mRNA. Translation: AAH27882.1.
CCDSiCCDS47847.1.
PIRiPC1161.
RefSeqiNP_002155.1. NM_002164.5.
UniGeneiHs.840.

Genome annotation databases

EnsembliENST00000518237; ENSP00000430950; ENSG00000131203.
ENST00000522495; ENSP00000430505; ENSG00000131203.
GeneIDi3620.
KEGGihsa:3620.
UCSCiuc003xnm.3. human.

Polymorphism databases

DMDMi123948.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34455 mRNA. Translation: AAA36081.1 .
X17668 mRNA. Translation: CAA35663.1 .
M86472 Genomic DNA. No translation available.
M86473 Genomic DNA. No translation available.
M86474 Genomic DNA. No translation available.
M86475 Genomic DNA. No translation available.
M86476 Genomic DNA. No translation available.
M86477 Genomic DNA. No translation available.
M86478 Genomic DNA. No translation available.
M86479 Genomic DNA. No translation available.
M86480 Genomic DNA. No translation available.
M86481 Genomic DNA. No translation available.
AY221100 mRNA. Translation: AAO34405.1 .
AK313259 mRNA. Translation: BAG36069.1 .
BC027882 mRNA. Translation: AAH27882.1 .
CCDSi CCDS47847.1.
PIRi PC1161.
RefSeqi NP_002155.1. NM_002164.5.
UniGenei Hs.840.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2D0T X-ray 2.30 A/B 1-403 [» ]
2D0U X-ray 3.40 A/B 1-403 [» ]
ProteinModelPortali P14902.
SMRi P14902. Positions 11-403.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109832. 4 interactions.
IntActi P14902. 3 interactions.
MINTi MINT-1414454.
STRINGi 9606.ENSP00000253513.

Chemistry

BindingDBi P14902.
ChEMBLi CHEMBL4685.
DrugBanki DB00150. L-Tryptophan.

PTM databases

PhosphoSitei P14902.

Polymorphism databases

DMDMi 123948.

Proteomic databases

PaxDbi P14902.
PRIDEi P14902.

Protocols and materials databases

DNASUi 3620.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000518237 ; ENSP00000430950 ; ENSG00000131203 .
ENST00000522495 ; ENSP00000430505 ; ENSG00000131203 .
GeneIDi 3620.
KEGGi hsa:3620.
UCSCi uc003xnm.3. human.

Organism-specific databases

CTDi 3620.
GeneCardsi GC08P039771.
HGNCi HGNC:6059. IDO1.
HPAi HPA023072.
HPA023149.
HPA027772.
MIMi 147435. gene.
neXtProti NX_P14902.
PharmGKBi PA29869.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG73554.
HOGENOMi HOG000203926.
HOVERGENi HBG006100.
InParanoidi P14902.
KOi K00463.
OMAi EAYDACV.
PhylomeDBi P14902.
TreeFami TF330978.

Enzyme and pathway databases

UniPathwayi UPA00333 ; UER00453 .
BioCyci MetaCyc:HS05502-MONOMER.
BRENDAi 1.13.11.11. 2681.
Reactomei REACT_916. Tryptophan catabolism.
SABIO-RK P14902.

Miscellaneous databases

ChiTaRSi IDO1. human.
EvolutionaryTracei P14902.
GeneWikii Indoleamine_2,3-dioxygenase.
GenomeRNAii 3620.
NextBioi 14159.
PROi P14902.
SOURCEi Search...

Gene expression databases

ArrayExpressi P14902.
Bgeei P14902.
Genevestigatori P14902.

Family and domain databases

InterProi IPR000898. Indolamine_dOase.
[Graphical view ]
Pfami PF01231. IDO. 1 hit.
[Graphical view ]
PROSITEi PS00876. IDO_1. 1 hit.
PS00877. IDO_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, sequencing and expression of human interferon-gamma-inducible indoleamine 2,3-dioxygenase cDNA."
    Dai W., Gupta S.L.
    Biochem. Biophys. Res. Commun. 168:1-8(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION BY IFNG.
    Tissue: Fibroblast.
  2. "Primary structure of human indoleamine 2,3-dioxygenase deduced from the nucleotide sequence of its cDNA."
    Tone S., Takikawa O., Habara-Ohkubo A., Kadoya A., Yoshida R., Kido R.
    Nucleic Acids Res. 18:367-367(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Lung.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Human indoleamine 2,3-dioxygenase from peripheral blood."
    He X., Xu L., Liu Y., Zeng Y.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Peripheral blood.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  7. "Novel tryptophan catabolic enzyme IDO2 is the preferred biochemical target of the antitumor indoleamine 2,3-dioxygenase inhibitory compound D-1-methyl-tryptophan."
    Metz R., Duhadaway J.B., Kamasani U., Laury-Kleintop L., Muller A.J., Prendergast G.C.
    Cancer Res. 67:7082-7087(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY.
  8. Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  9. "Crystal structure of human indoleamine 2,3-dioxygenase: catalytic mechanism of O2 incorporation by a heme-containing dioxygenase."
    Sugimoto H., Oda S., Otsuki T., Hino T., Yoshida T., Shiro Y.
    Proc. Natl. Acad. Sci. U.S.A. 103:2611-2616(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiI23O1_HUMAN
AccessioniPrimary (citable) accession number: P14902
Secondary accession number(s): Q540B4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 3, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi