# CD135

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Protein found in humans

FLT3 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1RJB, 3QS7, 3QS9, 4RT7, 4XUF Identifiers Aliases FLT3, CD135, FLK-2, FLK2, STK1, fms related tyrosine kinase 3, fms related receptor tyrosine kinase 3 External IDs OMIM: 136351; MGI: 95559; HomoloGene: 3040; GeneCards: FLT3; OMA:FLT3 - orthologs Gene location (Human) Chr. Chromosome 13 (human)[1] Band 13q12.2 Start 28,003,274 bp[1] End 28,100,592 bp[1] Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5 86.88 cM|5 G3 Start 147,267,551 bp[2] End 147,337,299 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in testicle cerebellar hemisphere monocyte right hemisphere of cerebellum bone marrow cell lymph node granulocyte body of pancreas spleen appendix Top expressed in superior olivary complex facial motor nucleus red nucleus mesenteric lymph nodes set of nuclei of trapezoid body cochlear nuclei motor neuron medial preoptic nucleus Region IV of hippocampus proper Region II of hippocampus proper More reference expression data BioGPS More reference expression data Gene ontology Molecular function vascular endothelial growth factor-activated receptor activity nucleotide binding protein kinase activity transferase activity protein homodimerization activity kinase activity protein binding cytokine receptor activity transmembrane receptor protein tyrosine kinase activity protein tyrosine kinase activity ATP binding protein self-association protein-containing complex binding glucocorticoid receptor binding 1-phosphatidylinositol-3-kinase activity receptor tyrosine kinase transmembrane signaling receptor activity Cellular component cytoplasm integral component of membrane cytosol endoplasmic reticulum lumen membrane integral component of plasma membrane nucleus plasma membrane endoplasmic reticulum protein-containing complex receptor complex Biological process leukocyte homeostasis regulation of apoptotic process dendritic cell differentiation cell differentiation myeloid progenitor cell differentiation positive regulation of MAP kinase activity phosphorylation transmembrane receptor protein tyrosine kinase signaling pathway common myeloid progenitor cell proliferation positive regulation of tyrosine phosphorylation of STAT protein cellular response to cytokine stimulus positive regulation of phosphatidylinositol 3-kinase activity protein phosphorylation pro-B cell differentiation cellular response to glucocorticoid stimulus animal organ regeneration response to organonitrogen compound positive regulation of cell population proliferation lymphocyte proliferation protein autophosphorylation positive regulation of phosphatidylinositol 3-kinase signaling peptidyl-tyrosine phosphorylation B cell differentiation positive regulation of MAPK cascade vascular endothelial growth factor signaling pathway cytokine-mediated signaling pathway hemopoiesis MAPK cascade phosphatidylinositol-3-phosphate biosynthetic process negative regulation of signal transduction viral process negative regulation of apoptotic process positive regulation of ERK1 and ERK2 cascade hematopoietic progenitor cell differentiation leukocyte differentiation lymphocyte differentiation Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 2322 14255 Ensembl ENSG00000122025 ENSMUSG00000042817 UniProt P36888 Q00342 RefSeq (mRNA) NM_004119 NM_010229 RefSeq (protein) NP_004110 NP_034359 Location (UCSC) Chr 13: 28 – 28.1 Mb Chr 5: 147.27 – 147.34 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Cluster of differentiation antigen 135** (**CD135**) also known as **fms like tyrosine kinase 3** (**FLT-3** with fms standing for "feline McDonough sarcoma"), **receptor-type tyrosine-protein kinase FLT3**, or **fetal liver kinase-2** (Flk2) is a [protein](/source/Protein) that in humans is encoded by the *FLT3* [gene](/source/Gene). FLT3 is a [cytokine receptor](/source/Cytokine_receptor) which belongs to the receptor tyrosine kinase class III. CD135 is the receptor for the [cytokine](/source/Cytokine) [Flt3 ligand](/source/FMS-like_tyrosine_kinase_3_ligand) (FLT3L).

It is expressed on the surface of many [hematopoietic](/source/Hematopoietic) progenitor cells. Signalling of FLT3 is important for the normal development of haematopoietic stem cells and progenitor cells.

The *FLT3* gene is one of the most frequently mutated genes in [acute myeloid leukemia](/source/Acute_myeloid_leukemia) (AML).[5] High levels of wild-type FLT3 have been reported for blast cells of some AML patients without FLT3 mutations. These high levels may be associated with worse prognosis.

## Structure

FLT3 is composed of five extracellular [immunoglobulin-like domains](/source/Immunoglobulin_domain), an extracellular domain, a transmembrane domain, a juxtamembrane domain and a tyrosine-kinase domain consisting of 2 lobes that are connected by a tyrosine-kinase insert. Cytoplasmic FLT3 undergoes [glycosylation](/source/Glycosylation), which promotes localization of the receptor to the membrane.[6]

## Function

CD135 is a class III [receptor tyrosine kinase](/source/Receptor_tyrosine_kinase). When this receptor binds to [FLT3L](/source/Flt3L) a ternary complex is formed in which two FLT3 molecules are bridged by one (homodimeric) FLT3L.[7] The formation of such complex brings the two intracellular domains in close proximity to each other, eliciting initial trans-phosphorylation of each kinase domain. This initial phosphorylation event further activates the intrinsic tyrosine kinase activity, which in turn phosphorylates and activates signal transduction molecules that propagate the signal in the cell. Signaling through CD135 plays a role in cell survival, proliferation, and differentiation. CD135 is important for [lymphocyte](/source/Lymphocyte) ([B cell](/source/B_cell) and [T cell](/source/T_cell)) development.

Two cytokines that down modulate FLT3 activity (& block FLT3-induced hematopoietic activity) are:

- TNF-alpha ([Tumor necrosis factor-alpha](/source/Tumor_necrosis_factor-alpha))

- TGF-beta ([Transforming growth factor-beta](/source/Transforming_growth_factor-beta))

TGF-beta especially, decreases FLT3 protein levels and reverses the FLT3L-induced decrease in the time that hematopoietic progenitors spend in the G1-phase of the cell cycle.[6]

## Clinical significance

### Cell surface marker

[Cluster of differentiation](/source/Cluster_of_differentiation) (CD) molecules are markers on the cell surface, as recognized by specific sets of [antibodies](/source/Antibody), used to identify the cell type, stage of differentiation and activity of a cell. In mice, CD135 is expressed on several hematopoietic (blood) cells, including long- and short-term reconstituting [hematopoietic stem cells](/source/Hematopoietic_stem_cells) (HSC) and other progenitors like [multipotent progenitors](/source/Progenitor_cell) (MPPs) and [common lymphoid progenitors](/source/Common_lymphoid_progenitor) (CLP).[8]

### Role in cancer

CD135 is a [proto-oncogene](/source/Proto-oncogene), meaning that mutations of this protein can lead to cancer.[9] [Mutations](/source/Mutations) of the FLT3 receptor can lead to the development of [leukemia](/source/Leukemia), a cancer of bone marrow hematopoietic progenitors. Internal tandem duplications of FLT3 (FLT3-ITD) are the most common mutations associated with [acute myelogenous leukemia](/source/Acute_myelogenous_leukemia) (AML) and are a [prognostic indicator](/source/Prognosis) associated with adverse disease outcome.

### FLT3 inhibitors

[Gilteritinib](/source/Gilteritinib), a dual [FLT3](/source/FLT3)-AXL tyrosine kinase inhibitor[10] has completed a phase 3 trial of relapsed/refractory acute myeloid leukemia in patients with FLT3 ITD or TKD mutations.[11] In 2017, gilteritinib gained FDA [orphan drug status](/source/Orphan_drug_status) for AML.[12] In November 2018, the FDA approved gilteritinib (Xospata) for treatment of adult patients with relapsed or refractory acute myeloid leukemia (AML) with a FLT3 mutation as detected by an FDA-approved test.[13]

In July 2023, [quizartinib](/source/Quizartinib) (Vanflyta) was also approved for the treatment of newly diagnosed AML with FLT3 internal tandem duplication (ITD)-positive, as detected by an FDA-approved test.[14] Precisely, it should be used with standard cytarabine and anthracycline induction and cytarabine consolidation, and as maintenance monotherapy following consolidation chemotherapy.[14]

[Midostaurin](/source/Midostaurin) was approved by the FDA in April 2017 for the treatment of adult patients with newly diagnosed AML who are positive for oncogenic FLT3, in combination with chemotherapy.[15] The drug is approved for use with a companion diagnostic, the LeukoStrat CDx FLT3 Mutation Assay, which is used to detect the FLT3 mutation in patients with AML.

[Sorafenib](/source/Sorafenib) has been reported to show significant activity against Flt3-ITD positive [acute myelogenous leukemia](/source/Acute_myelogenous_leukemia).[16][17]

[Sunitinib](/source/Sunitinib) also inhibits Flt3.

[Lestaurtinib](/source/Lestaurtinib) is in clinical trials.

A paper published in Nature in April 2012 studied patients who developed resistance to FLT3 inhibitors, finding specific DNA sites contributing to that resistance and highlighting opportunities for future development of inhibitors that could take into account the resistance-conferring mutations for a more potent treatment.[18]

## See also

- [Cluster of differentiation](/source/Cluster_of_differentiation)

- [cytokine receptor](/source/Cytokine_receptor)

- [receptor tyrosine kinase](/source/Receptor_tyrosine_kinase)

- [tyrosine kinase](/source/Tyrosine_kinase)

- [oncogene](/source/Oncogene)

- [hematopoiesis](/source/Hematopoiesis)

- [Lymphopoiesis#Labeling lymphopoiesis](/source/Lymphopoiesis#Labeling_lymphopoiesis)

## References

1. ^ [***a***](#cite_ref-refGRCh38Ensembl_1-0) [***b***](#cite_ref-refGRCh38Ensembl_1-1) [***c***](#cite_ref-refGRCh38Ensembl_1-2) [GRCh38: Ensembl release 89: ENSG00000122025](http://May2017.archive.ensembl.org/Homo_sapiens/Gene/Summary?db=core;g=ENSG00000122025) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. ^ [***a***](#cite_ref-refGRCm38Ensembl_2-0) [***b***](#cite_ref-refGRCm38Ensembl_2-1) [***c***](#cite_ref-refGRCm38Ensembl_2-2) [GRCm38: Ensembl release 89: ENSMUSG00000042817](http://May2017.archive.ensembl.org/Mus_musculus/Gene/Summary?db=core;g=ENSMUSG00000042817) – [Ensembl](/source/Ensembl_genome_database_project), May 2017

1. **[^](#cite_ref-3)** ["Human PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=2322). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-4)** ["Mouse PubMed Reference:"](https://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Link&LinkName=gene_pubmed&from_uid=14255). *National Center for Biotechnology Information, U.S. National Library of Medicine*.

1. **[^](#cite_ref-pmid11290608_5-0)** Yamamoto Y, Kiyoi H, Nakano Y, Suzuki R, Kodera Y, Miyawaki S, Asou N, Kuriyama K, Yagasaki F, Shimazaki C, Akiyama H, Saito K, Nishimura M, Motoji T, Shinagawa K, Takeshita A, Saito H, Ueda R, Ohno R, Naoe T (April 2001). "Activating mutation of D835 within the activation loop of FLT3 in human hematologic malignancies". *Blood*. **97** (8): 2434–9. [doi](/source/Doi_(identifier)):[10.1182/blood.V97.8.2434](https://doi.org/10.1182%2Fblood.V97.8.2434). [PMID](/source/PMID_(identifier)) [11290608](https://pubmed.ncbi.nlm.nih.gov/11290608).

1. ^ [***a***](#cite_ref-urlPathway_Central:_FLT3_Signaling_6-0) [***b***](#cite_ref-urlPathway_Central:_FLT3_Signaling_6-1) ["FLT3 Signaling"](https://web.archive.org/web/20171111001721/http://sabiosciences.com/pathway.php?sn=FLT3_Signaling). *Pathway Central*. SABiosciences. Archived from [the original](http://www.sabiosciences.com/pathway.php?sn=FLT3_Signaling) on 2017-11-11. Retrieved 2012-12-18.

1. **[^](#cite_ref-pmid21389326_7-0)** Verstraete K, Vandriessche G, Januar M, Elegheert J, Shkumatov AV, Desfosses A, Van Craenenbroeck K, Svergun DI, Gutsche I, Vergauwen B, Savvides SN (February 2011). ["Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex"](https://doi.org/10.1182%2Fblood-2011-01-329532). *Blood*. **118** (1): 60–68. [doi](/source/Doi_(identifier)):[10.1182/blood-2011-01-329532](https://doi.org/10.1182%2Fblood-2011-01-329532). [PMID](/source/PMID_(identifier)) [21389326](https://pubmed.ncbi.nlm.nih.gov/21389326).

1. **[^](#cite_ref-8)** Mooney CJ, Cunningham A, Tsapogas P, Toellner KM, Brown G (May 2017). ["Selective Expression of Flt3 within the Mouse Hematopoietic Stem Cell Compartment"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5454949). *Int J Mol Sci*. **18** (5): 1037. [doi](/source/Doi_(identifier)):[10.3390/ijms18051037](https://doi.org/10.3390%2Fijms18051037). [PMC](/source/PMC_(identifier)) [5454949](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5454949). [PMID](/source/PMID_(identifier)) [28498310](https://pubmed.ncbi.nlm.nih.gov/28498310).

1. **[^](#cite_ref-urlFLT3_(FMS-like_tyrosine_kinase_3)_9-0)** Huret J-L. ["FLT3 (FMS-like tyrosine kinase 3)"](http://atlasgeneticsoncology.org/Genes/FLT3ID144.html). *Atlas of Genetics and Cytogenetics in Oncology and Haematology*. University Hospital of Poitiers.

1. **[^](#cite_ref-pmid32547718_10-0)** Chew S, Mackey MC, Jabbour E (2020). ["Gilteritinib in the treatment of relapsed and refractory acute myeloid leukemia with a FLT3 mutation"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7271272). Review. *Therapeutic Advances in Hematology*. **11** 2040620720930614. [doi](/source/Doi_(identifier)):[10.1177/2040620720930614](https://doi.org/10.1177%2F2040620720930614). [PMC](/source/PMC_(identifier)) [7271272](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7271272). [PMID](/source/PMID_(identifier)) [32547718](https://pubmed.ncbi.nlm.nih.gov/32547718).

1. **[^](#cite_ref-11)** Perl AE, Martinelli G, Cortes JE, Neubauer A, Berman E, Paolini S, et al. (October 2019). ["FLT3-Mutated AML"](https://doi.org/10.1056%2FNEJMoa1902688). *The New England Journal of Medicine*. **381** (18): 1728–1740. [doi](/source/Doi_(identifier)):[10.1056/NEJMoa1902688](https://doi.org/10.1056%2FNEJMoa1902688). [PMID](/source/PMID_(identifier)) [31665578](https://pubmed.ncbi.nlm.nih.gov/31665578).

1. **[^](#cite_ref-12)** ["Gilteritinib Granted Orphan Drug Status for Acute Myeloid Leukemia"](http://www.cancertherapyadvisor.com/hematologic-cancers/acute-leukemia-aml-gilteritinib-fda-orphan-drug-status/article/676474/). *Cancer Therapy Advisor*. 20 July 2017.

1. **[^](#cite_ref-13)** ["FDA approves gilteritinib for relapsed or refractory acute myeloid leukemia (AML) with a FLT3 mutatation"](https://web.archive.org/web/20190928083620/https://www.fda.gov/drugs/fda-approves-gilteritinib-relapsed-or-refractory-acute-myeloid-leukemia-aml-flt3-mutatation). *Drugs*. FDA. December 14, 2018. Archived from [the original](https://www.fda.gov/drugs/fda-approves-gilteritinib-relapsed-or-refractory-acute-myeloid-leukemia-aml-flt3-mutatation) on September 28, 2019. Retrieved July 21, 2023.

1. ^ [***a***](#cite_ref-:0_14-0) [***b***](#cite_ref-:0_14-1) ["FDA approves quizartinib for newly diagnosed acute myeloid leukemia"](https://web.archive.org/web/20230720225035/https://www.fda.gov/drugs/drug-approvals-and-databases/fda-approves-quizartinib-newly-diagnosed-acute-myeloid-leukemia). *Drugs*. FDA. July 20, 2023. Archived from [the original](https://www.fda.gov/drugs/drug-approvals-and-databases/fda-approves-quizartinib-newly-diagnosed-acute-myeloid-leukemia) on July 20, 2023. Retrieved July 21, 2023.

1. **[^](#cite_ref-15)** Office of the Commissioner. ["Press Announcements - FDA approves new combination treatment for acute myeloid leukemia"](https://web.archive.org/web/20170428190353/https://www.fda.gov/NewsEvents/Newsroom/PressAnnouncements/ucm555778.htm). *www.fda.gov*. Archived from [the original](https://www.fda.gov/newsevents/newsroom/pressannouncements/ucm555778.htm) on April 28, 2017. Retrieved 2017-05-04.

1. **[^](#cite_ref-pmid19389879_16-0)** Metzelder S, Wang Y, Wollmer E, Wanzel M, Teichler S, Chaturvedi A, Eilers M, Enghofer E, Neubauer A, Burchert A (June 2009). ["Compassionate use of sorafenib in FLT3-ITD-positive acute myeloid leukemia: sustained regression before and after allogeneic stem cell transplantation"](https://doi.org/10.1182%2Fblood-2009-03-208298). *Blood*. **113** (26): 6567–71. [doi](/source/Doi_(identifier)):[10.1182/blood-2009-03-208298](https://doi.org/10.1182%2Fblood-2009-03-208298). [PMID](/source/PMID_(identifier)) [19389879](https://pubmed.ncbi.nlm.nih.gov/19389879). [S2CID](/source/S2CID_(identifier)) [206878993](https://api.semanticscholar.org/CorpusID:206878993).

1. **[^](#cite_ref-pmid18230792_17-0)** Zhang W, Konopleva M, Shi YX, McQueen T, Harris D, Ling X, Estrov Z, Quintás-Cardama A, Small D, Cortes J, Andreeff M (February 2008). ["Mutant FLT3: a direct target of sorafenib in acute myelogenous leukemia"](https://doi.org/10.1093%2Fjnci%2Fdjm328). *J. Natl. Cancer Inst*. **100** (3): 184–98. [doi](/source/Doi_(identifier)):[10.1093/jnci/djm328](https://doi.org/10.1093%2Fjnci%2Fdjm328). [PMID](/source/PMID_(identifier)) [18230792](https://pubmed.ncbi.nlm.nih.gov/18230792).

1. **[^](#cite_ref-18)** Smith CC, Wang Q, Chin CS, Salerno S, Damon LE, Levis MJ, et al. (April 2012). ["Validation of ITD mutations in FLT3 as a therapeutic target in human acute myeloid leukaemia"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3390926). *Nature*. **485** (7397): 260–3. [Bibcode](/source/Bibcode_(identifier)):[2012Natur.485..260S](https://ui.adsabs.harvard.edu/abs/2012Natur.485..260S). [doi](/source/Doi_(identifier)):[10.1038/nature11016](https://doi.org/10.1038%2Fnature11016). [PMC](/source/PMC_(identifier)) [3390926](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3390926). [PMID](/source/PMID_(identifier)) [22504184](https://pubmed.ncbi.nlm.nih.gov/22504184).

## Further reading

- Kazi JU, Rönnstrand L (2019). ["FMS-like Tyrosine Kinase 3/FLT3: From Basic Science to Clinical Implications"](https://doi.org/10.1152%2Fphysrev.00029.2018). *Physiol Rev*. **99** (3): 1433–1466. [doi](/source/Doi_(identifier)):[10.1152/physrev.00029.2018](https://doi.org/10.1152%2Fphysrev.00029.2018). [PMID](/source/PMID_(identifier)) [31066629](https://pubmed.ncbi.nlm.nih.gov/31066629).

- Reilly JT (2003). "FLT3 and its role in the pathogenesis of acute myeloid leukaemia". *[Leuk. Lymphoma](/source/Leuk._Lymphoma)*. **44** (1): 1–7. [doi](/source/Doi_(identifier)):[10.1080/1042819021000040233](https://doi.org/10.1080%2F1042819021000040233). [PMID](/source/PMID_(identifier)) [12691136](https://pubmed.ncbi.nlm.nih.gov/12691136). [S2CID](/source/S2CID_(identifier)) [28533250](https://api.semanticscholar.org/CorpusID:28533250).

- Kottaridis PD, Gale RE, Linch DC (2003). "Prognostic implications of the presence of FLT3 mutations in patients with acute myeloid leukemia". *Leuk. Lymphoma*. **44** (6): 905–13. [doi](/source/Doi_(identifier)):[10.1080/1042819031000067503](https://doi.org/10.1080%2F1042819031000067503). [PMID](/source/PMID_(identifier)) [12854887](https://pubmed.ncbi.nlm.nih.gov/12854887). [S2CID](/source/S2CID_(identifier)) [44447515](https://api.semanticscholar.org/CorpusID:44447515).

- Gilliland DG (2004). "FLT3-activating mutations in acute promyelocytic leukaemia: a rationale for risk-adapted therapy with FLT3 inhibitors". *Best Practice & Research. Clinical Haematology*. **16** (3): 409–17. [doi](/source/Doi_(identifier)):[10.1016/S1521-6926(03)00063-X](https://doi.org/10.1016%2FS1521-6926%2803%2900063-X). [PMID](/source/PMID_(identifier)) [12935959](https://pubmed.ncbi.nlm.nih.gov/12935959).

- Drexler HG, Quentmeier H (2005). "FLT3: receptor and ligand". *[Growth Factors](/source/Growth_Factors_(journal))*. **22** (2): 71–3. [doi](/source/Doi_(identifier)):[10.1080/08977190410001700989](https://doi.org/10.1080%2F08977190410001700989). [PMID](/source/PMID_(identifier)) [15253381](https://pubmed.ncbi.nlm.nih.gov/15253381). [S2CID](/source/S2CID_(identifier)) [86614476](https://api.semanticscholar.org/CorpusID:86614476).

- Naoe T, Kiyoi H (2005). ["Normal and oncogenic FLT3"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11924486). *[Cell. Mol. Life Sci.](/source/Cell._Mol._Life_Sci.)* **61** (23): 2932–8. [doi](/source/Doi_(identifier)):[10.1007/s00018-004-4274-x](https://doi.org/10.1007%2Fs00018-004-4274-x). [PMC](/source/PMC_(identifier)) [11924486](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11924486). [PMID](/source/PMID_(identifier)) [15583855](https://pubmed.ncbi.nlm.nih.gov/15583855). [S2CID](/source/S2CID_(identifier)) [27189321](https://api.semanticscholar.org/CorpusID:27189321).

- Sternberg DW, Licht JD (2005). "Therapeutic intervention in leukemias that express the activated fms-like tyrosine kinase 3 (FLT3): opportunities and challenges". *Curr. Opin. Hematol*. **12** (1): 7–13. [doi](/source/Doi_(identifier)):[10.1097/01.moh.0000147891.06584.d7](https://doi.org/10.1097%2F01.moh.0000147891.06584.d7). [PMID](/source/PMID_(identifier)) [15604885](https://pubmed.ncbi.nlm.nih.gov/15604885). [S2CID](/source/S2CID_(identifier)) [1590938](https://api.semanticscholar.org/CorpusID:1590938).

- Marcucci G, Mrózek K, Bloomfield CD (2005). "Molecular heterogeneity and prognostic biomarkers in adults with acute myeloid leukemia and normal cytogenetics". *Curr. Opin. Hematol*. **12** (1): 68–75. [doi](/source/Doi_(identifier)):[10.1097/01.moh.0000149608.29685.d1](https://doi.org/10.1097%2F01.moh.0000149608.29685.d1). [PMID](/source/PMID_(identifier)) [15604894](https://pubmed.ncbi.nlm.nih.gov/15604894). [S2CID](/source/S2CID_(identifier)) [6183391](https://api.semanticscholar.org/CorpusID:6183391).

- Markovic A, MacKenzie KL, Lock RB (2005). "FLT-3: a new focus in the understanding of acute leukemia". *[Int. J. Biochem. Cell Biol.](/source/Int._J._Biochem._Cell_Biol.)* **37** (6): 1168–72. [doi](/source/Doi_(identifier)):[10.1016/j.biocel.2004.12.005](https://doi.org/10.1016%2Fj.biocel.2004.12.005). [PMID](/source/PMID_(identifier)) [15778081](https://pubmed.ncbi.nlm.nih.gov/15778081).

- Zheng R, Small D (2006). "Mutant FLT3 signaling contributes to a block in myeloid differentiation". *Leuk. Lymphoma*. **46** (12): 1679–87. [doi](/source/Doi_(identifier)):[10.1080/10428190500261740](https://doi.org/10.1080%2F10428190500261740). [PMID](/source/PMID_(identifier)) [16263569](https://pubmed.ncbi.nlm.nih.gov/16263569). [S2CID](/source/S2CID_(identifier)) [20518363](https://api.semanticscholar.org/CorpusID:20518363).

- Parcells BW, Ikeda AK, Simms-Waldrip T, et al. (2007). ["FMS-like tyrosine kinase 3 in normal hematopoiesis and acute myeloid leukemia"](https://doi.org/10.1634%2Fstemcells.2005-0519). *Stem Cells*. **24** (5): 1174–84. [doi](/source/Doi_(identifier)):[10.1634/stemcells.2005-0519](https://doi.org/10.1634%2Fstemcells.2005-0519). [PMID](/source/PMID_(identifier)) [16410383](https://pubmed.ncbi.nlm.nih.gov/16410383).

- Stubbs MC, Armstrong SA (2007). "FLT3 as a therapeutic target in childhood acute leukemia". *Current Drug Targets*. **8** (6): 703–14. [doi](/source/Doi_(identifier)):[10.2174/138945007780830782](https://doi.org/10.2174%2F138945007780830782). [PMID](/source/PMID_(identifier)) [17584026](https://pubmed.ncbi.nlm.nih.gov/17584026).

## External links

- [CD135+Antigen](https://meshb.nlm.nih.gov/record/ui?name=CD135+Antigen) at the U.S. National Library of Medicine [Medical Subject Headings](/source/Medical_Subject_Headings) (MeSH)

- Human [*FLT3*](https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&singleSearch=knownCanonical&position=FLT3) genome location and [*FLT3*](https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_type=knownGene&hgg_gene=FLT3) gene details page in the [UCSC Genome Browser](/source/UCSC_Genome_Browser).

- Overview of all the structural information available in the [PDB](/source/Protein_Data_Bank) for [UniProt](/source/UniProt): *[P36888](https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/P36888)* (Receptor-type tyrosine-protein kinase FLT3) at the [PDBe-KB](/source/PDBe-KB).

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation) 1–50 CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50 51–100 CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100 101–150 CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150 151–200 CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200 201–250 CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 CD248 CD249 251–300 CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299 301–350 CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350 351–371 CD351 CD352 CD353 CD354 CD355 CD357 CD358 CD360 CD361 CD362 CD363 CD364 CD365 CD366 CD367 CD368 CD369 CD370 CD371 Category Commons

v t e Tumor suppressor genes and oncogenes Ligand Growth factors ONCO c-Sis/PDGF HGF Receptor Wnt signaling pathway TSP CDH1 Hedgehog signaling pathway TSP PTCH1 TGF beta signaling pathway TSP TGF beta receptor 2 Receptor tyrosine kinase ONCO ErbB/c-ErbB HER2 HER3 c-Met c-Ret JAK-STAT signaling pathway ONCO c-Kit Flt3 Intracellular signaling P+Ps Wnt signaling pathway ONCO Beta-catenin TSP APC TGF beta signaling pathway TSP SMAD2 SMAD4 Akt/PKB signaling pathway ONCO c-Akt TSP PTEN Hippo signaling pathway TSP Neurofibromin 2/Merlin MAPK/ERK pathway ONCO c-Ras HRAS c-Raf TSP Neurofibromin 1 Other/unknown ONCO c-Src TSP Maspin Nucleus Cell cycle ONCO CDK4 Cyclin D Cyclin E TSP p53 pRb WT1 p16/p14arf DNA repair/Fanconi TSP BRCA1 BRCA2 Ubiquitin ligase ONCO CBL MDM2 TSP VHL Transcription factor ONCO AP-1 c-Fos c-Jun c-Myc TSP KLF6 Mitochondrion Apoptosis inhibitor SDHB SDHD Other/ungrouped c-Bcl-2 Notch Stathmin

v t e Protein kinases: tyrosine kinases (EC 2.7.10) Receptor tyrosine kinases (EC 2.7.10.1) Growth factor receptors EGF receptor family EGFR ERBB2 ERBB3 ERBB4 Insulin receptor family IGF1R INSR INSRR PDGF receptor family CSF1R FLT3 KIT PDGFR PDGFRA PDGFRB FGF receptor family FGFR1 FGFR2 FGFR3 FGFR4 VEGF receptor family VEGFR1 VEGFR2 VEGFR3 HGF receptor family MET RON Trk receptor family NTRK1 NTRK2 NTRK3 EPH receptor family EPHA1 EPHA2 EPHA3 EPHA4 EPHA5 EPHA6 EPHA7 EPHA8 EPHB1 EPHB2 EPHB3 EPHB4 EPHB5 EPHB6 EPHX LTK receptor family LTK ALK TIE receptor family TIE TEK ROR receptor family ROR1 ROR2 DDR receptor family DDR1 DDR2 PTK7 receptor family PTK7 RYK receptor family RYK MuSK receptor family MUSK ROS receptor family ROS1 AATYK receptor family AATYK AATYK2 AXL receptor family AXL MER TYRO3 RET receptor family RET uncategorised STYK1 Non-receptor tyrosine kinases (EC 2.7.10.2) ABL family ABL1 ARG ACK family ACK1 TNK1 CSK family CSK MATK FAK family FAK PYK2 FES family FES FER FRK family FRK BRK SRMS JAK family JAK1 JAK2 JAK3 TYK2 SRC-A family SRC FGR FYN YES1 SRC-B family BLK HCK LCK LYN TEC family TEC BMX BTK ITK TXK SYK family SYK ZAP70

v t e Enzymes Activity Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis Regulation Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator Classification EC number Enzyme superfamily Enzyme family List of enzymes Kinetics Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics Types EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

v t e Cytokine receptor modulators Chemokine See here instead. CSF Erythropoietin Agonists: ARA-290 Asialo erythropoietin Carbamylated erythropoietin CNTO-530 Darbepoetin alfa Epoetin alfa Epoetin beta Epoetin delta Epoetin epsilon Epoetin gamma Epoetin kappa Epoetin omega Epoetin theta Epoetin zeta Erythropoietin (EPO) Erythropoietin-Fc Methoxy polyethylene glycol-epoetin beta (CERA/Mircera) Peginesatide Pegol sihematide (EPO-018B) G-CSF (CSF3) Agonists: Filgrastim Granulocyte colony-stimulating factor Lenograstim Leridistim Lipegfilgrastim Nartograstim Pegfilgrastim Pegnartograstim GM-CSF (CSF2) Agonists: Ecogramostim Granulocyte-macrophage colony-stimulating factor Milodistim Molgramostim Regramostim Sargramostim Antibodies: Mavrilimumab Namilumab Otilimab M-CSF (CSF1) Agonists: Cilmostim Interleukin 34 Lanimostim Macrophage colony-stimulating factor Mirimostim Kinase inhibitors: Agerafenib SCF (c-Kit) See here instead. Thrombopoietin Agonists: Eltrombopag Pegacaristim Promegapoietin Romiplostim Avatrombopag Lusutrombopag Thrombopoietin (THPO, MGDF) Interferon IFNAR (α/β, I) Agonists: Albinterferon Interferon alpha (interferon alfa, IFN-α) Interferon alfa (IFNA1, IFNA2, IFNA4, IFNA5, IFNA6, IFNA7, IFNA8, IFNA10, IFNA13, IFNA14, IFNA16, IFNA17, IFNA21) Interferon alfa 2a Interferon alfa 2b Interferon alfa n1 Interferon alfacon-1 Interferon alpha-n3 Interferon beta (IFN-β) (IFNB1, IFNB3) Interferon beta 1a Interferon beta 1b Interferon kappa (IFN-ε/κ/τ/ζ, IFNK) Interferon omega (IFN-ω, IFNW1) Peginterferon alfa-2a Peginterferon alfa-2b Antibodies: Anifrolumab Faralimomab MEDI-545 Rontalizumab Sifalimumab Decoy receptors: Bifarcept IFNGR (γ, II) Agonists: Interferon gamma (IFN-γ) Interferon gamma 1b Antibodies: Emapalumab Fontolizumab IFNLR (λ, III) See IL-28R (IFNLR) here instead. Interleukin See here instead. TGFβ See here instead. TNF See here instead. Others JAK (inhibitors) JAK1 Abrocitinib Baricitinib Deuruxolitinib Filgotinib Momelotinib Oclacitinib Peficitinib Ruxolitinib Tofacitinib (tasocitinib) Upadacitinib JAK2 Atiprimod AZD-1480 Baricitinib CHZ868 Cucurbitacin I (elatericin B, JSI-124) CYT387 Deuruxolitinib Lestaurtinib NSC-7908 NSC-33994 Pacritinib Peficitinib Ruxolitinib SD-1008 Tofacitinib (tasocitinib) JAK3 Cercosporamide Decernotinib (VX-509) Peficitinib Ritlecitinib TCS-21311 Tofacitinib (tasocitinib) WHI-P 154 ZM-39923 ZM-449829 TYK2 Deucravacitinib Others Additional cytokines: Cardiotrophin 1 (CT-1) FMS-like tyrosine kinase 3 ligand (FLT3L) Leukemia/leukocyte inhibitory factor (LIF) Oncostatin M (OSM) Thymic stromal lymphopoietin (TSLP) Additional cytokine receptor modulators: Emfilermin Lestaurtinib Midostaurin Quizartinib Sorafenib Sunitinib

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Adapted from the Wikipedia article [CD135](https://en.wikipedia.org/wiki/CD135) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/CD135?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.