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IDO1 (indoleamine 2,3-dioxygenase 1)

Written2009-03Mee Young Chang, Alexander J Muller, George C Prendergast
Lankenau Institute for Medical Research, 100 Lancaster Avenue, Wynnewood PA 19096, USA

(Note : for Links provided by Atlas : click)


Alias (NCBI)CD107B
HGNC (Hugo) IDO1
HGNC Previous nameIDO
HGNC Previous nameindoleamine-pyrrole 2,3 dioxygenase
LocusID (NCBI) 3620
Atlas_Id 40973
Location 8p11.21  [Link to chromosome band 8p11]
Location_base_pair Starts at 39913891 and ends at 39928790 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping IDO1.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
EXOC1 (4q12)::IDO1 (8p11.21)EXOSC10 (1p36.22)::IDO1 (8p11.21)IDO1 (8p11.21)::IPO4 (14q12)
IDO1 (8p11.21)::NUFIP2 (17q11.2)PTPRD (9p24.1)::IDO1 (8p11.21)


Description The human IDO1 gene is encoded on 10 exons which span 14,163 bps at chromosome 8p12-p11 (nucleotides 39,890,485-39,905,107). The murine IDO1 gene is similarly sized and localized to a syntenic locus on mouse chromosome 8A2.
Transcription Transcription of the human IDO1 gene produces a full-length mRNA transcript of 1,572 nt. The promoter includes transcription factor sites that confer responsiveness to type I and type II interferons (IFN-alpha / IFN-beta and IFN-gamma respectively), most potently to IFN-gamma. Many cell types strongly increase IDO transcription after exposure to IFN-gamma, including myeloid cells (monocyte/macrophages and dentritic cells), fibroblasts, endothelial cells, epithelial cells and many tumor cell lines. STAT and IRF transcription factors function cooperatively to mediate induction of IDO1 expression by IFN-gamma, and mice lacking either IFN-gamma or IRF1 function are deficient in IDO1 expression during infections.
Pseudogene None known.


Description The IDO1 gene encodes a full-length protein of 403 amino acids with a predicted molecular weight of 45,332 Daltons. The open reading frame is preceded by a long, untranslated sequence. There is no Kozak consensus sequence present at the ATG start site in the open reading frame.
Expression IDO1 is widely expressed in the body. High expression is seen in placental trophoblast giant cells of fetal origin, epididymis, gut (distal ileum and colon), lymph nodes, spleen, thymus and lung. IDO activity in many of these locations is markedly increased in vivo by LPS treatment. With the exception of epididymis, a common feature of sites of expression are extensive mucosal surfaces and/or large lymphoid compartments with immunoregulatory roles. IDO1 is overexpressed in many human diseases including cancer, chronic infectious disease, allergy, autoimmune disease and other disorders characterized by local immune suppression.
Localisation IDO1 is a cytosolic enzyme with no known secreted or extracellular form.
Function IDO1 is a single-chain oxidoreductase catalyzing the first, rate-limiting step of tryptophan degradation in biosynthesis of the central metabolic regulator nicotinamide adenine dinucleotide (NAD) along the kynurenine pathway. In mammals, IDO1 does not catabolyze excess dietary tryptophan, which is carried out by the liver enzyme TDO2, and NAD levels are not maintained by synthesis but by salvage from the diet. Thus, the role of IDO1 in mammals was obscure until it was discovered to be strongly induced by IFN-gamma and linked to immune control. The function of IDO1 in immune control is based on broad evidence that tryptophan depletion and/or kynurenine production suppresses T cell-mediated immunity. In particular, IDO1-mediated tryptophan catabolism in antigen-presenting dendritic cells appears to be an important mechanism to generate immune tolerance to cross-presented neoantigens, such as those that arise during allogeneic pregnancy or cancer.
Antiproliferation : Tryptophan catabolism by IDO1 has been suggested to mediate antiproliferative effects during infection, including directly on infectious microorganisms that may rely on tryptophan for growth. With regard to the function of IDO1 in immune regulation, tryptophan depletion in the vicinity of an antigen presentation event has been suggested to limit T cell activation by preventing the cell division required by T cells to become activated upon appropriate presentation of antigen. Dendritic cells arising from monocytes acquire the ability to act as regulatory cells that suppress T cell proliferation through tryptophan catabolism by IDO1. The 1-methyl analogue of tryptophan (1MT) has been used widely to block IDO activity. When T cells are deprived of tryptophan, they arrest at a mid-G1 phase of the cell cycle. Restoring tryptophan does not restore the activation process, which requires a second round of T cell receptor signaling along with tryptophan. Together this information has suggested that antigen-presenting cells can employ IDO1 to restrict T cell activation by blocking T cell proliferation, due to tryptophan catabolism.
Apoptosis : The products of tryptophan catabolism by IDO1 include kynurenine and downstream products of the so-called kynurenine pathway that can induce apoptosis of thymocytes and Th1 but not Th2 helper T cells. Apoptosis induced by these products does not require Fas/Fas ligand interactions but are associated with activation of caspase-8 and the release of cytochrome c from mitochondria. When administered in vivo, some kynurenines can deplete specific thymocyte subsets like dexamethasone. Thus, the selective deletion of T lymphocytes by kynurenine production has been suggested as one mechanism through which tryptophan catabolism could blunt immunity under pathologic conditions.
Immune tolerance : Many studies illustrate how IDO1 overexpression can blunt immune responses to neoantigens. Cell lines overexpressing IDO1 limit antigen-specific T cell responses in vitro. In murine tumor cell lines, IDO1 overexpression renders tumor allografts resistant to immune rejection in vivo. Adenoviral-mediated IDO1 gene transfer into pancreatic islet cells is reported to prolong survival in allogeneic hosts. Similarly, ectopic expression of IDO1 is found to protect allogeneic lung transplants from rejection. CTLA-4 signaling induces IDO and pre-treatment of mice with CTLA-4-Ig to induce IDO expression suppresses rejection of pancreatic islet allografts. In a model of graft-versus-host disease, IDO1 overexpression completely blocks clonal expansion of alloreactive T-cell receptor (TCR)-transgenic T cells. Studies in other tissue allograft models confirm that IDO is a potent regulator of adaptive immune response. A consistent picture is provided by studies employing the pharmacological agent 1MT as an IDO inhibitor. 1MT exacerbates symptoms of experimental autoimmune encephalomyelitis and abrogates the tolerogenic effects of CTLA4-Ig treatment in an islet-cell transplant model. Similarly, 1MT increases disease severity and mortality in a T cell-dependent colitis model, suggesting the role of IDO in the downregulation of Th1 responses within the gastrointestinal tract. Lastly, as discussed in more detail below, 1MT corrects immune escape mediated by IDO in a variety of allograft and transgenic (autochthonous) mouse models of cancer.
Maintenance of Pregnancy : IDO1 has been suggested to mediate immune tolerance during pregnancy on the basis of the ability of IDO inhibitor 1MT to act as an abortifacient in allogeneic but not syngeneic mice. IDO1 gene knockout studies do not replicate this effect suggesting a compensatory genetic effect or an IDO1-dependent effect of 1MT. Indeed, 1MT is no longer active in IDO1 knockout mice, demonstrating that 1MT must target IDO1 mediate its effects.
Null phenotype in mouse : IDO1-deficient mice are viable and fertile. in vitro generation of antigen-presenting dendritic cells (DCs) from IDO1-deficient bone marrow precursors appeared to be affected in the presence of GM-CSF, however, changing growth factor and adherence conditions abolished the observed differences (Flt3L and low-adherence dishes). Moreover, IDO1-deficient mice display a normal DC compartment in vivo and do not develop lethal autoimmune or lymphoproliferative disorders. Consistent with this observation, mice treated systemically for up to 28 days with 1MT or other IDO inhibitors do not appear to develop spontaneous autoimmunity. Together these observations imply that IDO1 is non-essential for self tolerance. In contrast, skin carcinogenesis studies reveal that IDO1-deficient mice are resistant to cancer initiation and carcinoma progression, due to an apparent inability to develop tumor tolerance.
Homology Human IDO1 has 62% identity (77% similarity) with mouse IDO1 and 44% identity (64% similarity) with mouse IDO2. Human IDO1 has 44% identity (63% similarity) with human IDO2 and mouse IDO1 has 44% identity (64% similarity) with mouse IDO2.

Implicated in

Entity Cancer
Note IDO1 is observed to be highly expressed in many human cancer at the level of the tumor and/or the tumor-draining lymph node. Elevated tryptophan catabolism in the urine and blood of tumor-bearing patients has been recognized for many decades, perhaps explained by the discovery of common IDO1 overexpression in tumors.
Entity Leukemia
Note Patients with acute myeloid leukemia (AML) exhibit an increased ratio of Kyn/Trp in the serum and patients with higher Kyn/Trp ratios display a dramatically reduced survival. In adult T-cell leukemia/lymphoma (ATLL) that is caused by HTLV-1 infection, the serum kynurenine concentrations, Kyn/Trp ratio, and level of IDO mRNA expression are all significantly increased relative to healthy subjects. Interestingly, after chemotherapy, serum kynurenine concentrations are significantly reduced and tryptophan concentrations are significantly increased.
Entity Breast cancer
Note IDO1 expression has been reported in all breast cancer and non-cancer specimens as determined by semiquantitative RT-PCR, with higher levels observed in cancer specimens compared to non-cancer specimens. In this malignancy IDO1 has not been found to correlate to histologic classification, tumor size, lymph nodes metastasis, and survival rate after surgery. However, its expression has been reported to correlate to clinical stage and the serum level of immunosuppressive acidic protein (IAP) in breast cancer patient. In MMTV-Neu transgenic mice, an established mouse model of breast cancer, the IDO1 inhibitor 1MT slows tumor growth but does not arrest it. In contrast, 1MT cooperates strongly with paclitaxel, cisplatin, cyclophosphamide, or doxyrubicin (all widely used in breast cancer treatment) to trigger regression of established tumors that are otherwise refractory to single-agent therapy.
Entity Lung cancer
Note IDO1 expression has been reported to be higher in cases of lung cancer and autologous non-malignant lung tissues than in lung cancer cell lines by quantitative real-time RT-PCR. No significant correlations between IDO1 expression and clinicopathological parameters have been observed. In human non-small-cell lung cancer (NSCLC), immunohistochemical analysis suggests that IDO1 is expressed not by tumor cells but by eosinophilic granulocytes. IDO1 protein in NSCLC is enzymatically active, implying that IDO-positive eosinophils may be competent to exert local immunosuppression. A significant relationship is found between the amount of IDO1-positive infiltrate and overall survival by follow-up analysis of lung cancer patients.
Entity Skin cancer
Note In the classical two-stage mouse model of skin carcinogenesis, phorbol myristate acetate (PMA) induces plasmacytoid dendritic cells (pDCs) in local draining lymph nodes to express IDO1, which confers suppressor activity to the pDCs. Significantly, IDO1-deficient mice display a tumor-resistant phenotype in this model of carcinogenesis.
Entity Colon cancer
Note IDO1 expression in human colon carcinoma cell lines dependent on IFN-gamma induction. Immunohistochemical analysis of colon tumors indicated that IDO1 overexpression is associated with a significant reduction of CD3+ infiltrating T cells and higher occurrence of liver metastases in colorectal cancer patients. Conversely, no correlation was seen with tumor stage, tumor size, histologic grade, nodal status, gender, or age.
Entity Pancreatic ductal adenocarcinoma (PDA)
Note IDO1 is upregulated in metastatic PDA cells and associated with an increased number of FoxP3+ T regulatory cells (Tregs) in tumors. No correlation of IDO1 expression is observed with tumor histologic grade in PDA. In contrast, while non-metastatic PDAs are negative or only focally positive for IDO1, higher and broader expression of IDO1 is seen in both primary and metastatic tumors in patients with lymph node metastases (with stronger staining in metastatic foci).
Entity Liver cancer
Note In human hepatocarcinomas, immunohistochemical analysis revealed that IDO1 was strongly expressed in 36% of cases and weakly expressed in 64% of cases examined. In this study, IDO1 overexpression was significantly correlated with high rates of metastasis and poor prognosis.
Entity Ovarian cancer
Note IDO1 was found to be overexpressed in serous-type ovarian cancer where it was associated with decreased patient survival. IDO1 overexpression was also associated with resistance to paclitaxel.
Entity Renal cell carcinoma
Note Elevated levels of IDO1 mRNA were detected in >75% of clear cell type renal carcinoma, compared to normal kidney. In this study, IDO1 expression was associated with vascular cells in tumors and it correlated with improved long-term survival.
Entity Cervical cancer
Note IDO1 is expressed in cervical intraepithelial neoplasia (CIN) and invasive cervical cancer. Immunohistochemical analysis suggests IDO1 expression in antigen-presenting cells in both primary and invasive lesions. FoxP3+CD4+CD25+ Tregs appear in CIN and are increased in invasive cancer. No significant differences were observed in the proportion of Tregs in the stroma or epithelium (or between metastatic and non-metastatic cancers), but there was a significant increase in Tregs associated with IDO1 overexrpression in metastatic lymph nodes as compared to non-metastatic lymph modes.
Entity Endometrial cancer
Note High expression of IDO1 correlated with a reduced number of tumor-infiltrating lymphocytes (TILs) and natural killer (NK) cells in endometrial cancer. IDO1 overexpression was also positively correlated with myometrial invasion, nodal metastasis, and lymph-vascular space involvement, all of which contribute to disease progression and lower progression-free survival.
Entity Uveal melanoma
Note Primary uveal melanoma from tumor-bearing eyes and metastatic uveal melanoma from liver were not found to express IDO1 in situ. Also, IDO1 was not expressed in either primary or metastatic uveal melanoma cell lines unless they were stimulated by IFN-gamma. Addition of 1MT to IFN-gamma-treated uveal melanoma cell lines significantly diminished kynurenine levels. Together these findings suggested that in settings of IFN-gamma expression IDO1 upregulation may promote escape from T cell-mediated immune surveilance in uveal melanoma.
Entity Inflammatory bowel disease (IBD)
Note IDO1 mRNA is markedly induced in lesional colonic biopsies of IBD patients, being primarily expressed in CD123(+) mononuclear cells that infiltrate the submucosal areas of inflamed lesions. In Crohn's disease (CD), IDO1 is also strongly expressed in perifollicular regions of lymphoid follicles, with increased kynurenine and Kyn/Trp ratioes in colonic explant cultures (CECs) from CD patients. Immunohistochemical analysis of colonic biopsies taken from CD patients prior and after treatment with the TNF-blocking antibody infliximab caused a reduction in IDO1 expression in patients with good clinical response to infliximab, consistent with a potential benefit to IDO1 reduction in this disease.
Entity Primary biliary cirrhosis (PBL)
Note PBL is a chronic autoimmune cholestatic liver disease characterized by inflammatory destruction of the small bile ducts within the liver that eventually leads to cirrhosis. One study found a defective Treg compartment and an impaired IDO1 induction by IFN-gamma in peripheral monocytes isolated from patients with PBL.
Entity HIV infection
Note Infection of HIV or Simian immunodeficiency virus (SIV) increases IDO1 expression and functional IDO enzymatic activity both in vitro and in vivo. It is reported that patients infected with HIV have chronically reduced levels of plasma tryptophan and increased levels of kynurenine, suggesting the possibility of IDO1 activation. IDO1-expressing cells may protect HIV from clearance by allowing virally infected cells to become resistant to attack by T cell, or indirectly by promoting induction of acquired, antigen-specific tolerance to HIV antigens.
Entity Depression
Note Evidence exists of a link between IDO activity and mood. In serotonergic nerve terminals tryptophan is hydroxylated before conversion to serotonin (5HT). Lower levels of serotonin in the brain are associated with depressed mood. Tryptophan availability limits de novo synthesis of serotonin and tryptophan depletion has been associated with depressive symptoms in patients with remitted major depressive disorder, resulting in a disturbance of mood in subjects with a family history of affective illness.
Given the proposed role of IDO in maintaining pregnancy, the linkage between IDO activity and mood may be relevant to postpartum depression. Typically this phenomenon occurs within a few days after delivery until the tenth day postpartum. An association has been noted between Kyn/Trp ratio and the severity of depressive symptoms in the early puerperium, suggesting that an increased degradation of typtophan relates to the occurrence of postpartum blues. Conversely, a decrease in Kyn/Trp ratioes has been reported in women with stable mood after delivery.
Some evidence exists that inflammatory changes in the brain that may be associated with IDO1 expression are pathological features of both depression and dementia. Pathological changes have been associated with a reduction in the neuroprotective components of the kynurenine pathway (e.g. kynurenic acid) and an increase in the neurodegenerative components (e.g. 3-hydroxykynurenine acid and quinolinic acid). These changes are postulated to cause neuronal damage and predispose chronically depressed patients to dementia. In Alzheimer's patients, plasma Kyn/Trp ratioes have been observed to correlate with the degree of cognitive deficit. Also, immunohistochemical analysis suggests that IDO1 is abundant in the brains of Alzheimer's patients compared to controls. Similarly, relative elevations in Kyn/Trp ratio have been found in plasma from patients with Huntington's or Parkinson's disease compared to controls. Notably, depressive symptoms affect up to 50% of Alzheimer's patients, 41% of Huntington's patients, and 40% of Parkinson's patients.
Further support for a link between IDO1 elevation and depressed mood are found in patients with autoimmune diseases, where symptoms have been associated with increased tryptophan catabolism. Enhanced tryptophan degradation was found in systemic lupus erythromatosus, rheumatoid arthritis, sarcoidosis, and a mouse model of multiple sclerosis. It has also been noted that a higher proportion of patients infected with Hepatitis C virus (HCV) have lower serum tryptophan concentrations and depression relative to healthy volunteers.
Entity Defense against mycoplasm infection
Note IDO1 has been implicated in host defence against certain pathogens such as Chlamydia pneumoniae, Toxoplasma gondii, group B streptococci, and mycobacteria through its ability to deplete tryptophan and thereby inhibit pathogen replication. IDO1 has also been observed to inhibit the replication of cytomegalovirus and herpes simplex virus in vitro.


Inhibition of human herpes simplex virus type 2 by interferon gamma and tumor necrosis factor alpha is mediated by indoleamine 2,3-dioxygenase.
Adams O, Besken K, Oberdorfer C, MacKenzie CR, Russing D, Daubener W.
Microbes Infect. 2004 Jul;6(9):806-12.
PMID 15374002
Eosinophil granulocytes account for indoleamine 2,3-dioxygenase-mediated immune escape in human non-small cell lung cancer.
Astigiano S, Morandi B, Costa R, Mastracci L, D'Agostino A, Ratto GB, Melioli G, Frumento G.
Neoplasia. 2005 Apr;7(4):390-6.
PMID 15967116
Proteomic analysis of cytokine induced proteins in human intestinal epithelial cells: implications for inflammatory bowel diseases.
Barcelo-Batllori S, Andre M, Servis C, Levy N, Takikawa O, Michetti P, Reymond M, Felley-Bosco E.
Proteomics. 2002 May;2(5):551-60.
PMID 11987129
Cyclooxygenase-2 inhibitor enhances the efficacy of a breast cancer vaccine: role of IDO.
Basu GD, Tinder TL, Bradley JM, Tu T, Hattrup CL, Pockaj BA, Mukherjee P.
J Immunol. 2006 Aug 15;177(4):2391-402.
PMID 16888001
Expression of indoleamine 2,3-dioxygenase (IDO) by endothelial cells: implications for the control of alloresponses.
Beutelspacher SC, Tan PH, McClure MO, Larkin DF, Lechler RI, George AJ.
Am J Transplant. 2006 Jun;6(6):1320-30.
PMID 16686756
Clinical relevance of indoleamine 2,3-dioxygenase for alloimmunity and transplantation.
Brandacher G, Margreiter R, Fuchs D.
Curr Opin Organ Transplant. 2008 Feb;13(1):10-5.
PMID 18660700
A two-step induction of indoleamine 2,3 dioxygenase (IDO) activity during dendritic-cell maturation.
Braun D, Longman RS, Albert ML.
Blood. 2005 Oct 1;106(7):2375-81. Epub 2005 Jun 9.
PMID 15947091
The role of serine 167 in human indoleamine 2,3-dioxygenase: a comparison with tryptophan 2,3-dioxygenase.
Chauhan N, Basran J, Efimov I, Svistunenko DA, Seward HE, Moody PC, Raven EL.
Biochemistry. 2008 Apr 22;47(16):4761-9. Epub 2008 Mar 28.
PMID 18370410
The indoleamine 2,3-dioxygenase pathway is essential for human plasmacytoid dendritic cell-induced adaptive T regulatory cell generation.
Chen W, Liang X, Peterson AJ, Munn DH, Blazar BR.
J Immunol. 2008 Oct 15;181(8):5396-404.
PMID 18832696
Reduced uterine indoleamine 2,3-dioxygenase versus increased Th1/Th2 cytokine ratios as a basis for occult and clinical pregnancy failure in mice and humans.
Clark DA, Blois S, Kandil J, Handjiski B, Manuel J, Arck PC.
Am J Reprod Immunol. 2005 Oct;54(4):203-16.
PMID 16135011
Low serum tryptophan levels, reduced macrophage IDO activity and high frequency of psychopathology in HCV patients.
Cozzi A, Zignego AL, Carpendo R, Biagiotti T, Aldinucci A, Monti M, Giannini C, Rosselli M, Laffi G, Moroni F.
J Viral Hepat. 2006 Jun;13(6):402-8.
PMID 16842443
Induction of indoleamine 2,3-dioxygenase in vascular smooth muscle cells by interferon-gamma contributes to medial immunoprivilege.
Cuffy MC, Silverio AM, Qin L, Wang Y, Eid R, Brandacher G, Lakkis FG, Fuchs D, Pober JS, Tellides G.
J Immunol. 2007 Oct 15;179(8):5246-54.
PMID 17911610
Acute myeloid leukemia cells constitutively express the immunoregulatory enzyme indoleamine 2,3-dioxygenase.
Curti A, Aluigi M, Pandolfi S, Ferri E, Isidori A, Salvestrini V, Durelli I, Horenstein AL, Fiore F, Massaia M, Piccioli M, Pileri SA, Zavatto E, D'Addio A, Baccarani M, Lemoli RM.
Leukemia. 2007 Feb;21(2):353-5. Epub 2006 Dec 14.
PMID 17170728
CD4(+)CD25(+) regulatory lymphocytes require interleukin 10 to interrupt colon carcinogenesis in mice.
Erdman SE, Rao VP, Poutahidis T, Ihrig MM, Ge Z, Feng Y, Tomczak M, Rogers AB, Horwitz BH, Fox JG.
Cancer Res. 2003 Sep 15;63(18):6042-50.
PMID 14522933
CD4+CD25+ regulatory lymphocytes induce regression of intestinal tumors in ApcMin/+ mice.
Erdman SE, Sohn JJ, Rao VP, Nambiar PR, Ge Z, Fox JG, Schauer DB.
Cancer Res. 2005 May 15;65(10):3998-4004.
PMID 15899788
Differential immunosuppressive effect of indoleamine 2,3-dioxygenase (IDO) on primary human CD4+ and CD8+ T cells.
Forouzandeh F, Jalili RB, Germain M, Duronio V, Ghahary A.
Mol Cell Biochem. 2008 Feb;309(1-2):1-7. Epub 2007 Nov 16.
PMID 18008147
Rabbit antithymocyte globulin inhibits monocyte-derived dendritic cells maturation in vitro and polarizes monocyte-derived dendritic cells towards tolerogenic dendritic cells expressing indoleamine 2,3-dioxygenase.
Gillet-Hladky S, de Carvalho CM, Bernaud J, Bendahou C, Bloy C, Rigal D.
Transplantation. 2006 Oct 15;82(7):965-74.
PMID 17038913
Inhibition of indoleamine 2,3-dioxygenase activity in IFN-gamma stimulated astroglioma cells decreases intracellular NAD levels.
Grant R, Kapoor V.
Biochem Pharmacol. 2003 Sep 15;66(6):1033-6.
PMID 12963490
Antimicrobial and immunoregulatory effects mediated by human lung cells: role of IFN-gamma-induced tryptophan degradation.
Heseler K, Spekker K, Schmidt SK, MacKenzie CR, Daubener W.
FEMS Immunol Med Microbiol. 2008 Mar;52(2):273-81. Epub 2008 Jan 16.
PMID 18205804
Heme oxygenase-1 inhibits rat and human breast cancer cell proliferation: mutual cross inhibition with indoleamine 2,3-dioxygenase.
Hill M, Pereira V, Chauveau C, Zagani R, Remy S, Tesson L, Mazal D, Ubillos L, Brion R, Asghar K, Mashreghi MF, Kotsch K, Moffett J, Doebis C, Seifert M, Boczkowski J, Osinaga E, Anegon I.
FASEB J. 2005 Dec;19(14):1957-68.
PMID 16319139
Indoleamine 2,3-dioxygenase is highly expressed in human adult T-cell leukemia/lymphoma and chemotherapy changes tryptophan catabolism in serum and reduced activity.
Hoshi M, Ito H, Fujigaki H, Takemura M, Takahashi T, Tomita E, Ohyama M, Tanaka R, Saito K, Seishima M.
Leuk Res. 2009 Jan;33(1):39-45. Epub 2008 Jul 17.
PMID 18639341
Nitric oxide-mediated regulation of gamma interferon-induced bacteriostasis: inhibition and degradation of human indoleamine 2,3-dioxygenase.
Hucke C, MacKenzie CR, Adjogble KD, Takikawa O, Daubener W.
Infect Immun. 2004 May;72(5):2723-30.
PMID 15102781
Indoleamine 2,3-dioxygenase is necessary for cytolytic activity of natural killer cells.
Kai S, Goto S, Tahara K, Sasaki A, Tone S, Kitano S.
Scand J Immunol. 2004 Feb;59(2):177-82.
PMID 14871294
IDO and clinical conditions associated with depressive symptoms.
Kohl C, Sperner-Unterweger B.
Curr Drug Metab. 2007 Apr;8(3):283-7. (REVIEW)
PMID 17430116
Mechanisms regulating the expression of indoleamine 2,3-dioxygenase during decidualization of human endometrium.
Kudo Y, Hara T, Katsuki T, Toyofuku A, Katsura Y, Takikawa O, Fujii T, Ohama K.
Hum Reprod. 2004 May;19(5):1222-30. Epub 2004 Apr 7.
PMID 15070879
Upregulation of indoleamine 2,3-dioxygenase in hepatitis C virus infection.
Larrea E, Riezu-Boj JI, Gil-Guerrero L, Casares N, Aldabe R, Sarobe P, Civeira MP, Heeney JL, Rollier C, Verstrepen B, Wakita T, Borras-Cuesta F, Lasarte JJ, Prieto J.
J Virol. 2007 Apr;81(7):3662-6. Epub 2007 Jan 17.
PMID 17229698
Upregulation of placental indoleamine 2,3-dioxygenase by human chorionic gonadotropin.
Lei ZM, Yang M, Li X, Takikawa O, Rao CV.
Biol Reprod. 2007 Apr;76(4):639-44. Epub 2006 Dec 20.
PMID 17182891
Cell surface expression of MHC class I antigen is suppressed in indoleamine 2,3-dioxygenase genetically modified keratinocytes: implications in allogeneic skin substitute engraftment.
Li Y, Tredget EE, Ghahary A.
Hum Immunol. 2004 Feb;65(2):114-23.
PMID 14969766
Localisation of indoleamine 2,3-dioxygenase and kynurenine hydroxylase in the human placenta and decidua: implications for role of the kynurenine pathway in pregnancy.
Ligam P, Manuelpillai U, Wallace EM, Walker D.
Placenta. 2005 Jul;26(6):498-504.
PMID 15950064
Asp274 and his346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase.
Littlejohn TK, Takikawa O, Truscott RJ, Walker MJ.
J Biol Chem. 2003 Aug 8;278(32):29525-31. Epub 2003 May 24.
PMID 12766158
Nonviral gene delivery with indoleamine 2,3-dioxygenase targeting pulmonary endothelium protects against ischemia-reperfusion injury.
Liu H, Liu L, Visner GA.
Am J Transplant. 2007 Oct;7(10):2291-300. Epub 2007 Aug 16.
PMID 17711549
Are indoleamine-2,3-dioxygenase producing human dendritic cells a tool for suppression of allogeneic T-cell responses?
Lob S, Ebner S, Wagner S, Weinreich J, Schafer R, Konigsrainer A.
Transplantation. 2007 Feb 27;83(4):468-73.
PMID 17318080
Levo- but not dextro-1-methyl tryptophan abrogates the IDO activity of human dendritic cells.
Lob S, Konigsrainer A, Schafer R, Rammensee HG, Opelz G, Terness P.
Blood. 2008 Feb 15;111(4):2152-4. Epub 2007 Nov 28.
PMID 18045970
Cytochrome b5, not superoxide anion radical, is a major reductant of indoleamine 2,3-dioxygenase in human cells.
Maghzal GJ, Thomas SR, Hunt NH, Stocker R.
J Biol Chem. 2008 May 2;283(18):12014-25. Epub 2008 Feb 25.
PMID 18299324
IL-8 and IDO expression by human gingival fibroblasts via TLRs.
Mahanonda R, Sa-Ard-Iam N, Montreekachon P, Pimkhaokham A, Yongvanichit K, Fukuda MM, Pichyangkul S.
J Immunol. 2007 Jan 15;178(2):1151-7.
PMID 17202379
HIV-activated human plasmacytoid DCs induce Tregs through an indoleamine 2,3-dioxygenase-dependent mechanism.
Manches O, Munn D, Fallahi A, Lifson J, Chaperot L, Plumas J, Bhardwaj N.
J Clin Invest. 2008 Oct;118(10):3431-9.
PMID 18776940
Sputum indoleamine-2, 3-dioxygenase activity is increased in asthmatic airways by using inhaled corticosteroids.
Maneechotesuwan K, Supawita S, Kasetsinsombat K, Wongkajornsilp A, Barnes PJ.
J Allergy Clin Immunol. 2008 Jan;121(1):43-50. Epub 2007 Nov 26.
PMID 18036645
Human bone marrow stromal cells inhibit allogeneic T-cell responses by indoleamine 2,3-dioxygenase-mediated tryptophan degradation.
Meisel R, Zibert A, Laryea M, Gobel U, Daubener W, Dilloo D.
Blood. 2004 Jun 15;103(12):4619-21. Epub 2004 Mar 4.
PMID 15001472
Cutting edge: induced indoleamine 2,3 dioxygenase expression in dendritic cell subsets suppresses T cell clonal expansion.
Mellor AL, Baban B, Chandler P, Marshall B, Jhaver K, Hansen A, Koni PA, Iwashima M, Munn DH.
J Immunol. 2003 Aug 15;171(4):1652-5.
PMID 12902462
IDO expression by dendritic cells: tolerance and tryptophan catabolism.
Mellor AL, Munn DH.
Nat Rev Immunol. 2004 Oct;4(10):762-74. (REVIEW)
PMID 15459668
IDO expression on decidual and peripheral blood dendritic cells and monocytes/macrophages after treatment with CTLA-4 or interferon-gamma increase in normal pregnancy but decrease in spontaneous abortion.
Miwa N, Hayakawa S, Miyazaki S, Myojo S, Sasaki Y, Sakai M, Takikawa O, Saito S.
Mol Hum Reprod. 2005 Dec;11(12):865-70. Epub 2006 Jan 18.
PMID 16421220
Inhibition of indoleamine 2,3-dioxygenase, an immunoregulatory target of the cancer suppression gene Bin1, potentiates cancer chemotherapy.
Muller AJ, DuHadaway JB, Donover PS, Sutanto-Ward E, Prendergast GC.
Nat Med. 2005 Mar;11(3):312-9. Epub 2005 Feb 13.
PMID 15711557
Marrying immunotherapy with chemotherapy: why say IDO?
Muller AJ, Prendergast GC.
Cancer Res. 2005 Sep 15;65(18):8065-8. (REVIEW)
PMID 16166276
Targeting the mechanisms of tumoral immune tolerance with small-molecule inhibitors.
Muller AJ, Scherle PA.
Nat Rev Cancer. 2006 Aug;6(8):613-25.
PMID 16862192
Indoleamine 2,3-dioxygenase and tumor-induced tolerance.
Munn DH, Mellor AL.
J Clin Invest. 2007 May;117(5):1147-54. (REVIEW)
PMID 17476344
Expression of indoleamine 2,3-dioxygenase by plasmacytoid dendritic cells in tumor-draining lymph nodes.
Munn DH, Sharma MD, Hou D, Baban B, Lee JR, Antonia SJ, Messina JL, Chandler P, Koni PA, Mellor AL.
J Clin Invest. 2004 Jul;114(2):280-90.
PMID 15254595
Expression of indoleamine 2, 3-dioxygenase and the recruitment of Foxp3-expressing regulatory T cells in the development and progression of uterine cervical cancer.
Nakamura T, Shima T, Saeki A, Hidaka T, Nakashima A, Takikawa O, Saito S.
Cancer Sci. 2007 Jun;98(6):874-81. Epub 2007 Apr 13.
PMID 17433037
Indoleamine 2,3-dioxygenase mediates cell type-specific anti-measles virus activity of gamma interferon.
Obojes K, Andres O, Kim KS, Daubener W, Schneider-Schaulies J.
J Virol. 2005 Jun;79(12):7768-76.
PMID 15919929
Crystallization and preliminary crystallographic studies of human indoleamine 2,3-dioxygenase.
Oda S, Sugimoto H, Yoshida T, Shiro Y.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt 3):221-3. Epub 2006 Feb 10.
PMID 16511306
Cutting edge: human eosinophils regulate T cell subset selection through indoleamine 2,3-dioxygenase.
Odemuyiwa SO, Ghahary A, Li Y, Puttagunta L, Lee JE, Musat-Marcu S, Ghahary A, Moqbel R.
J Immunol. 2004 Nov 15;173(10):5909-13.
PMID 15528322
Impaired indoleamine 2,3-dioxygenase production contributes to the development of autoimmunity in primary biliary cirrhosis.
Oertelt-Prigione S, Mao TK, Selmi C, Tsuneyama K, Ansari AA, Coppel RL, Invernizzi P, Podda M, Gershwin ME.
Autoimmunity. 2008 Feb;41(1):92-9.
PMID 18176870
Induction of indoleamine 2,3-dioxygenase: a mechanism of the antitumor activity of interferon gamma.
Ozaki Y, Edelstein MP, Duch DS.
Proc Natl Acad Sci U S A. 1988 Feb;85(4):1242-6.
PMID 3124115
Expression and prognosis role of indoleamine 2,3-dioxygenase in hepatocellular carcinoma.
Pan K, Wang H, Chen MS, Zhang HK, Weng DS, Zhou J, Huang W, Li JJ, Song HF, Xia JC.
J Cancer Res Clin Oncol. 2008 Nov;134(11):1247-53. Epub 2008 Apr 26.
PMID 18438685
Indoleamine 2,3-dioxygenase activity in nonagenarians is markedly increased and predicts mortality.
Pertovaara M, Raitala A, Lehtimaki T, Karhunen PJ, Oja SS, Jylha M, Hervonen A, Hurme M.
Mech Ageing Dev. 2006 May;127(5):497-9. Epub 2006 Feb 28.
PMID 16513157
Immune escape as a fundamental trait of cancer: focus on IDO.
Prendergast GC.
Oncogene. 2008 Jun 26;27(28):3889-900. Epub 2008 Mar 3. (REVIEW)
PMID 18317452
On watching the watchers: IDO and type I/II IFN.
Puccetti P.
Eur J Immunol. 2007 Apr;37(4):876-9.
PMID 17393386
Synergistic transcriptional activation of indoleamine dioxygenase by IFN-gamma and tumor necrosis factor-alpha.
Robinson CM, Shirey KA, Carlin JM.
J Interferon Cytokine Res. 2003 Aug;23(8):413-21.
PMID 13678429
Interactions between nitric oxide and indoleamine 2,3-dioxygenase.
Samelson-Jones BJ, Yeh SR.
Biochemistry. 2006 Jul 18;45(28):8527-38.
PMID 16834326
Induction of indoleamine 2,3-dioxygenase by interferon-gamma in human islets.
Sarkar SA, Wong R, Hackl SI, Moua O, Gill RG, Wiseman A, Davidson HW, Hutton JC.
Diabetes. 2007 Jan;56(1):72-9.
PMID 17192467
Immune cell proliferation is suppressed by the interferon-gamma-induced indoleamine 2,3-dioxygenase expression of fibroblasts populated in collagen gel (FPCG).
Sarkhosh K, Tredget EE, Karami A, Uludag H, Iwashina T, Kilani RT, Ghahary A.
J Cell Biochem. 2003 Sep 1;90(1):206-17.
PMID 12938169
Indoleamine 2,3-dioxygenase (IDO): the antagonist of type I interferon-driven skin inflammation?
Scheler M, Wenzel J, Tuting T, Takikawa O, Bieber T, von Bubnoff D.
Am J Pathol. 2007 Dec;171(6):1936-43. Epub 2007 Nov 30.
PMID 18055547
Mesenchymal stem cells inhibit natural killer-cell proliferation, cytotoxicity, and cytokine production: role of indoleamine 2,3-dioxygenase and prostaglandin E2.
Spaggiari GM, Capobianco A, Abdelrazik H, Becchetti F, Mingari MC, Moretta L.
Blood. 2008 Feb 1;111(3):1327-33. Epub 2007 Oct 19.
PMID 17951526
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. 2006 Feb 21;103(8):2611-6. Epub 2006 Feb 13.
PMID 16477023
Astrocyte indoleamine 2,3-dioxygenase is induced by the TLR3 ligand poly(I:C): mechanism of induction and role in antiviral response.
Suh HS, Zhao ML, Rivieccio M, Choi S, Connolly E, Zhao Y, Takikawa O, Brosnan CF, Lee SC.
J Virol. 2007 Sep;81(18):9838-50. Epub 2007 Jul 11.
PMID 17626075
Biochemical and medical aspects of the indoleamine 2,3-dioxygenase-initiated L-tryptophan metabolism.
Takikawa O.
Biochem Biophys Res Commun. 2005 Dec 9;338(1):12-9. Epub 2005 Sep 15.
PMID 16176799
Relationship between interferon-gamma, indoleamine 2,3-dioxygenase, and tryptophan catabolism.
Taylor MW, Feng GS.
FASEB J. 1991 Aug;5(11):2516-22. (REVIEW)
PMID 1907934
The heme environment of recombinant human indoleamine 2,3-dioxygenase. Structural properties and substrate-ligand interactions.
Terentis AC, Thomas SR, Takikawa O, Littlejohn TK, Truscott RJ, Armstrong RS, Yeh SR, Stocker R.
J Biol Chem. 2002 May 3;277(18):15788-94. Epub 2002 Feb 26.
PMID 11867636
Inhibition of allogeneic T cell proliferation by indoleamine 2,3-dioxygenase-expressing dendritic cells: mediation of suppression by tryptophan metabolites.
Terness P, Bauer TM, Rose L, Dufter C, Watzlik A, Simon H, Opelz G.
J Exp Med. 2002 Aug 19;196(4):447-57.
PMID 12186837
The immunoregulatory role of IDO-producing human dendritic cells revisited.
Terness P, Chuang JJ, Opelz G.
Trends Immunol. 2006 Feb;27(2):68-73. Epub 2006 Jan 10.
PMID 16406698
Post-translational regulation of human indoleamine 2,3-dioxygenase activity by nitric oxide.
Thomas SR, Terentis AC, Cai H, Takikawa O, Levina A, Lay PA, Freewan M, Stocker R.
J Biol Chem. 2007 Aug 17;282(33):23778-87. Epub 2007 May 29.
PMID 17535808
Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3-dioxygenase.
Uyttenhove C, Pilotte L, Theate I, Stroobant V, Colau D, Parmentier N, Boon T, Van den Eynde BJ.
Nat Med. 2003 Oct;9(10):1269-74. Epub 2003 Sep 21.
PMID 14502282
Suppression of cytotoxic and proliferative xenogeneic T-cell responses by transgenic expression of indoleamine 2,3-dioxygenase.
Wee JL, Christiansen D, Li YQ, Boyle W, Sandrin MS.
Immunol Cell Biol. 2008 Jul;86(5):460-5. Epub 2008 Mar 11.
PMID 18332894
Expression of indoleamine 2,3-dioxygenase in metastatic pancreatic ductal adenocarcinoma recruits regulatory T cells to avoid immune detection.
Witkiewicz A, Williams TK, Cozzitorto J, Durkan B, Showalter SL, Yeo CJ, Brody JR.
J Am Coll Surg. 2008 May;206(5):849-54; discussion 854-6. Epub 2008 Mar 4.
PMID 18471709
Overexpression of indoleamine 2,3-dioxygenase in human endometrial carcinoma cells induces rapid tumor growth in a mouse xenograft model.
Yoshida N, Ino K, Ishida Y, Kajiyama H, Yamamoto E, Shibata K, Terauchi M, Nawa A, Akimoto H, Takikawa O, Isobe K, Kikkawa F.
Clin Cancer Res. 2008 Nov 15;14(22):7251-9.
PMID 19010841
A putative mechanism on remission of multiple sclerosis during pregnancy: estrogen-induced indoleamine 2,3-dioxygenase by dendritic cells.
Zhu WH, Lu CZ, Huang YM, Link H, Xiao BG.
Mult Scler. 2007 Jan;13(1):33-40.
PMID 17294609
Normal development and function of dendritic cells in mice lacking IDO-1 expression.
de Faudeur G, de Trez C, Muraille E, Leo O.
Immunol Lett. 2008 Jun 15;118(1):21-9. Epub 2008 Mar 14.
PMID 18384884
Intralesional expression of mRNA of interferon- gamma , tumor necrosis factor- alpha , interleukin-10, nitric oxide synthase, indoleamine-2,3-dioxygenase, and RANTES is a major immune effector in Mediterranean spotted fever rickettsiosis.
de Sousa R, Ismail N, Nobrega SD, Franca A, Amaro M, Anes M, Pocas J, Coelho R, Torgal J, Bacellar F, Walker DH.
J Infect Dis. 2007 Sep 1;196(5):770-81. Epub 2007 Jul 20.
PMID 17674321
IFN-gamma amplifies IL-6 and IL-8 responses by airway epithelial-like cells via indoleamine 2,3-dioxygenase.
van Wissen M, Snoek M, Smids B, Jansen HM, Lutter R.
J Immunol. 2002 Dec 15;169(12):7039-44.
PMID 12471139
Human epidermal langerhans cells express the immunoregulatory enzyme indoleamine 2,3-dioxygenase.
von Bubnoff D, Bausinger H, Matz H, Koch S, Hacker G, Takikawa O, Bieber T, Hanau D, de la Salle H.
J Invest Dermatol. 2004 Aug;123(2):298-304.
PMID 15245429
Indoleamine-dioxygenase is expressed in human decidua at the time maternal tolerance is established.
von Rango U, Krusche CA, Beier HM, Classen-Linke I.
J Reprod Immunol. 2007 Jun;74(1-2):34-45. Epub 2007 Feb 26.
PMID 17321596


This paper should be referenced as such :
Chang, MY ; Muller, AJ ; Prendergast, GC
IDO1 (indoleamine 2,3-dioxygenase 1)
Atlas Genet Cytogenet Oncol Haematol. 2010;14(2):141-148.
Free journal version : [ pdf ]   [ DOI ]

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]
  Subcutaneous panniculitis-like T-cell lymphoma

External links


HGNC (Hugo)IDO1   6059
Entrez_Gene (NCBI)IDO1    indoleamine 2,3-dioxygenase 1
AliasesIDO; IDO-1; INDO
GeneCards (Weizmann)IDO1
Ensembl hg19 (Hinxton)ENSG00000131203 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000131203 [Gene_View]  ENSG00000131203 [Sequence]  chr8:39913891-39928790 [Contig_View]  IDO1 [Vega]
ICGC DataPortalENSG00000131203
TCGA cBioPortalIDO1
AceView (NCBI)IDO1
Genatlas (Paris)IDO1
SOURCE (Princeton)IDO1
Genetics Home Reference (NIH)IDO1
Genomic and cartography
GoldenPath hg38 (UCSC)IDO1  -     chr8:39913891-39928790 +  8p11.21   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)IDO1  -     8p11.21   [Description]    (hg19-Feb_2009)
GoldenPathIDO1 - 8p11.21 [CytoView hg19]  IDO1 - 8p11.21 [CytoView hg38]
Genome Data Viewer NCBIIDO1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AK313259 AU137351 AY221100 BC027882 BF094375
RefSeq transcript (Entrez)NM_002164
Consensus coding sequences : CCDS (NCBI)IDO1
Gene ExpressionIDO1 [ NCBI-GEO ]   IDO1 [ EBI - ARRAY_EXPRESS ]   IDO1 [ SEEK ]   IDO1 [ MEM ]
Gene Expression Viewer (FireBrowse)IDO1 [ Firebrowse - Broad ]
GenevisibleExpression of IDO1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)3620
GTEX Portal (Tissue expression)IDO1
Human Protein AtlasENSG00000131203-IDO1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP14902   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP14902  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP14902
Domaine pattern : Prosite (Expaxy)IDO_1 (PS00876)    IDO_2 (PS00877)   
Domains : Interpro (EBI)Indolamine_dOase    Trp/Indoleamine_2_3_dOase-like   
Domain families : Pfam (Sanger)IDO (PF01231)   
Domain families : Pfam (NCBI)pfam01231   
Conserved Domain (NCBI)IDO1
PDB (RSDB)2D0T    2D0U    4PK5    4PK6    4U72    4U74    5EK2    5EK3    5EK4    5ETW    5WHR    5WMU    5WMV    5WMW    5WMX    5WN8    5XE1    6AZU    6AZV    6AZW    6CXU    6CXV    6DPQ    6DPR    6E35    6E40    6E41    6E42    6E43    6E44    6E45    6E46    6F0A    6KOF    6KPS    6KW7    6MQ6    6O3I    6PU7    6PZ1    6R63    6TUE    6V52    6WJY   
PDB Europe2D0T    2D0U    4PK5    4PK6    4U72    4U74    5EK2    5EK3    5EK4    5ETW    5WHR    5WMU    5WMV    5WMW    5WMX    5WN8    5XE1    6AZU    6AZV    6AZW    6CXU    6CXV    6DPQ    6DPR    6E35    6E40    6E41    6E42    6E43    6E44    6E45    6E46    6F0A    6KOF    6KPS    6KW7    6MQ6    6O3I    6PU7    6PZ1    6R63    6TUE    6V52    6WJY   
PDB (PDBSum)2D0T    2D0U    4PK5    4PK6    4U72    4U74    5EK2    5EK3    5EK4    5ETW    5WHR    5WMU    5WMV    5WMW    5WMX    5WN8    5XE1    6AZU    6AZV    6AZW    6CXU    6CXV    6DPQ    6DPR    6E35    6E40    6E41    6E42    6E43    6E44    6E45    6E46    6F0A    6KOF    6KPS    6KW7    6MQ6    6O3I    6PU7    6PZ1    6R63    6TUE    6V52    6WJY   
PDB (IMB)2D0T    2D0U    4PK5    4PK6    4U72    4U74    5EK2    5EK3    5EK4    5ETW    5WHR    5WMU    5WMV    5WMW    5WMX    5WN8    5XE1    6AZU    6AZV    6AZW    6CXU    6CXV    6DPQ    6DPR    6E35    6E40    6E41    6E42    6E43    6E44    6E45    6E46    6F0A    6KOF    6KPS    6KW7    6MQ6    6O3I    6PU7    6PZ1    6R63    6TUE    6V52    6WJY   
Structural Biology KnowledgeBase2D0T    2D0U    4PK5    4PK6    4U72    4U74    5EK2    5EK3    5EK4    5ETW    5WHR    5WMU    5WMV    5WMW    5WMX    5WN8    5XE1    6AZU    6AZV    6AZW    6CXU    6CXV    6DPQ    6DPR    6E35    6E40    6E41    6E42    6E43    6E44    6E45    6E46    6F0A    6KOF    6KPS    6KW7    6MQ6    6O3I    6PU7    6PZ1    6R63    6TUE    6V52    6WJY   
SCOP (Structural Classification of Proteins)2D0T    2D0U    4PK5    4PK6    4U72    4U74    5EK2    5EK3    5EK4    5ETW    5WHR    5WMU    5WMV    5WMW    5WMX    5WN8    5XE1    6AZU    6AZV    6AZW    6CXU    6CXV    6DPQ    6DPR    6E35    6E40    6E41    6E42    6E43    6E44    6E45    6E46    6F0A    6KOF    6KPS    6KW7    6MQ6    6O3I    6PU7    6PZ1    6R63    6TUE    6V52    6WJY   
CATH (Classification of proteins structures)2D0T    2D0U    4PK5    4PK6    4U72    4U74    5EK2    5EK3    5EK4    5ETW    5WHR    5WMU    5WMV    5WMW    5WMX    5WN8    5XE1    6AZU    6AZV    6AZW    6CXU    6CXV    6DPQ    6DPR    6E35    6E40    6E41    6E42    6E43    6E44    6E45    6E46    6F0A    6KOF    6KPS    6KW7    6MQ6    6O3I    6PU7    6PZ1    6R63    6TUE    6V52    6WJY   
AlphaFold pdb e-kbP14902   
Human Protein Atlas [tissue]ENSG00000131203-IDO1 [tissue]
Protein Interaction databases
IntAct (EBI)P14902
Ontologies - Pathways
Ontology : AmiGOimmune system process  tryptophan 2,3-dioxygenase activity  cytoplasm  cytosol  tryptophan catabolic process  female pregnancy  electron transfer activity  tryptophan catabolic process to kynurenine  tryptophan catabolic process to kynurenine  heme binding  electron transport chain  indoleamine 2,3-dioxygenase activity  indoleamine 2,3-dioxygenase activity  'de novo' NAD biosynthetic process from tryptophan  regulation of activated T cell proliferation  metal ion binding  positive regulation of T cell apoptotic process  
Ontology : EGO-EBIimmune system process  tryptophan 2,3-dioxygenase activity  cytoplasm  cytosol  tryptophan catabolic process  female pregnancy  electron transfer activity  tryptophan catabolic process to kynurenine  tryptophan catabolic process to kynurenine  heme binding  electron transport chain  indoleamine 2,3-dioxygenase activity  indoleamine 2,3-dioxygenase activity  'de novo' NAD biosynthetic process from tryptophan  regulation of activated T cell proliferation  metal ion binding  positive regulation of T cell apoptotic process  
Pathways : KEGGTryptophan metabolism    African trypanosomiasis   
REACTOMEP14902 [protein]
REACTOME PathwaysR-HSA-71240 [pathway]   
NDEx NetworkIDO1
Atlas of Cancer Signalling NetworkIDO1
Wikipedia pathwaysIDO1
Orthology - Evolution
GeneTree (enSembl)ENSG00000131203
Phylogenetic Trees/Animal Genes : TreeFamIDO1
Homologs : HomoloGeneIDO1
Homology/Alignments : Family Browser (UCSC)IDO1
Gene fusions - Rearrangements
Fusion : MitelmanEXOC1::IDO1 [4q12/8p11.21]  
Fusion : MitelmanPTPRD::IDO1 [9p24.1/8p11.21]  
Fusion : FusionGDB1.13.11.52   
Fusion : QuiverIDO1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerIDO1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)IDO1
Exome Variant ServerIDO1
GNOMAD BrowserENSG00000131203
Varsome BrowserIDO1
ACMGIDO1 variants
Genomic Variants (DGV)IDO1 [DGVbeta]
DECIPHERIDO1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisIDO1 
ICGC Data PortalIDO1 
TCGA Data PortalIDO1 
Broad Tumor PortalIDO1
OASIS PortalIDO1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICIDO1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DIDO1
Mutations and Diseases : HGMDIDO1
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)IDO1
DoCM (Curated mutations)IDO1
CIViC (Clinical Interpretations of Variants in Cancer)IDO1
NCG (London)IDO1
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry IDO1
NextProtP14902 [Medical]
Target ValidationIDO1
Huge Navigator IDO1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDIDO1
Pharm GKB GenePA29869
Clinical trialIDO1
DataMed IndexIDO1
PubMed439 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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