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Promotes phosphorylation of SHC1 and AKT1, and activation of the downstream effector MTOR. Promotes activation of RAS signaling and phosphorylation of downstream kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation of FES, FER, PTPN6/SHP, PTPN11/SHP-2, PLCG1, and STAT5A and/or STAT5B. Activation of wild-type FLT3 causes only marginal activation of STAT5A or STAT5B. Mutations that cause constitutive kinase activity promote cell proliferation and resistance to apoptosis via the activation of multiple signaling pathways"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10596"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20101"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:61978"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.10.1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10028"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15831474"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14759363"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21516120"}],"value":"Present in an inactive conformation in the absence of bound ligand. 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Interacts with RNF115 and RNF126 (By similarity)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29691342"}],"value":"(Microbial infection) Interacts with human cytomegalovirus protein UL7"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P36888","intActId":"EBI-3946257"},"interactantTwo":{"uniProtKBAccession":"P00519","geneName":"ABL1","intActId":"EBI-375543"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P36888","intActId":"EBI-3946257"},"interactantTwo":{"uniProtKBAccession":"P42684","geneName":"ABL2","intActId":"EBI-1102694"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P36888","intActId":"EBI-3946257"},"interactantTwo":{"uniProtKBAccession":"P46108","geneName":"CRK","intActId":"EBI-886"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P36888","intActId":"EBI-3946257"},"interactantTwo":{"uniProtKBAccession":"P46109","geneName":"CRKL","intActId":"EBI-910"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P36888","intActId":"EBI-3946257"},"interactantTwo":{"uniProtKBAccession":"P06241","geneName":"FYN","intActId":"EBI-515315"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P36888","intActId":"EBI-3946257"},"interactantTwo":{"uniProtKBAccession":"Q13322","geneName":"GRB10","intActId":"EBI-80275"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P36888","intActId":"EBI-3946257"},"interactantTwo":{"uniProtKBAccession":"Q9Y6K9","geneName":"IKBKG","intActId":"EBI-81279"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P36888","intActId":"EBI-3946257"},"interactantTwo":{"uniProtKBAccession":"P06239","geneName":"LCK","intActId":"EBI-1348"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P36888","intActId":"EBI-3946257"},"interactantTwo":{"uniProtKBAccession":"P27986","geneName":"PIK3R1","intActId":"EBI-79464"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P36888","intActId":"EBI-3946257"},"interactantTwo":{"uniProtKBAccession":"P20936","geneName":"RASA1","intActId":"EBI-1026476"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P36888","intActId":"EBI-3946257"},"interactantTwo":{"uniProtKBAccession":"P43405","geneName":"SYK","intActId":"EBI-78302"},"numberOfExperiments":22,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P36888","intActId":"EBI-3946257"},"interactantTwo":{"uniProtKBAccession":"Q8R4L0","geneName":"Sla2","intActId":"EBI-20766300"},"numberOfExperiments":14,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"value":"Constitutively activated mutant forms with internal tandem duplications are less efficiently transported to the cell surface and a significant proportion is retained in an immature form in the endoplasmic reticulum lumen. 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Detected in bone marrow, liver, thymus, spleen and lymph node, and at low levels in kidney and pancreas. Highly expressed in T-cell leukemia"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"value":"The juxtamembrane autoregulatory region is important for normal regulation of the kinase activity and for maintaining the kinase in an inactive state in the absence of bound ligand. Upon tyrosine phosphorylation, it mediates interaction with the SH2 domains of numerous signaling partners. In-frame internal tandem duplications (ITDs) result in constitutive activation of the kinase. The activity of the mutant kinase can be stimulated further by FLT3LG binding"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15831474"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21262971"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21389326"}],"value":"N-glycosylated, contains complex N-glycans with sialic acid"}],"commentType":"PTM"},{"texts":[{"value":"Autophosphorylated on several tyrosine residues in response to FLT3LG binding. FLT3LG binding also increases phosphorylation of mutant kinases that are constitutively activated. Dephosphorylated by PTPRJ/DEP-1, PTPN1, PTPN6/SHP-1, and to a lesser degree by PTPN12. Dephosphorylation is important for export from the endoplasmic reticulum and location at the cell membrane"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20508617"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21262971"}],"value":"Rapidly ubiquitinated by UBE2L6 and the E3 ubiquitin-protein ligase SIAH1 after autophosphorylation, leading to its proteasomal degradation"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Leukemia, acute myelogenous","diseaseAccession":"DI-01171","acronym":"AML","description":"A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. 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