FLT3
entrez
2322
canonical
uniprot
P36888
canonical
ensembl
ENSG00000122025
resolver
ensp
ENSP00000241453
resolver
genesymbol
FLT3
resolver
genesymbol_syn
CD135
resolver
genesymbol_syn
FLK2
resolver
genesymbol_syn
STK1
resolver
hgnc
HGNC:3765
resolver
uniprot
A0AVG9
resolver
uniprot
B7ZLT7
resolver
uniprot
B7ZLT8
resolver
uniprot
F5H0A0
resolver
uniprot
Q13414
resolver
uniprot_entry
FLT3_HUMAN
resolver
uniprot_sec
A0AVG9
resolver
uniprot_sec
B7ZLT7
resolver
uniprot_sec
B7ZLT8
resolver
uniprot_sec
F5H0A0
resolver
uniprot_sec
Q13414
resolver
activity_regulation
ACTIVITY REGULATION: Present in an inactive conformation in the absence of bound ligand. FLT3LG binding leads to dimerization and activation by autophosphorylation. {ECO:0000269|PubMed:14759363, ECO:0000269|PubMed:21516120}.
uniprot
proteins
amino_acid_sequence
MPALARDGGQLPLLVVFSAMIFGTITNQDLPVIKCVLINHKNNDSSVGKSSSYPMVSESPEDLGCALRPQSSGTVYEAAAVEVDVSASITLQVLVDAPGNISCLWVFKHSSLNCQPHFDLQNRGVVSMVILKMTETQAGEYLLFIQSEATNYTILFTVSIRNTLLYTLRRPYFRKMENQDALVCISESVPEPIVEWVLCDSQGESCKEESPAVVKKEEKVLHELFGTDIRCCARNELGRECTRLFTIDLNQTPQTTLPQLFLKVGEPLWIRCKAVHVNHGFGLTWELENKALEEGNYFEMSTYSTNRTMIRILFAFVSSVARNDTGYYTCSSSKHPSQSALVTIVEKGFINATNSSEDYEIDQYEEFCFSVRFKAYPQIRCTWTFSRKSFPCEQKGLDNGYSISKFCNHKHQPGEYIFHAENDDAQFTKMFTLNIRRKPQVLAEASASQASCFSDGYPLPSWTWKKCSDKSPNCTEEITEGVWNRKANRKVFGQWVSSSTLNMSEAIKGFLVKCCAYNSLGTSCETILLNSPGPFPFIQDNISFYATIGVCLLFIVVLTLLICHKYKKQFRYESQLQMVQVTGSSDNEYFYVDFREYEYDLKWEFPRENLEFGKVLGSGAFGKVMNATAYGISKTGVSIQVAVKMLKEKADSSEREALMSELKMMTQLGSHENIVNLLGACTLSGPIYLIFEYCCYGDLLNYLRSKREKFHRTWTEIFKEHNFSFYPTFQSHPNSSMPGSREVQIHPDSDQISGLHGNSFHSEDEIEYENQKRLEEEEDLNVLTFEDLLCFAYQVAKGMEFLEFKSCVHRDLAARNVLVTHGKVVKICDFGLARDIMSDSNYVVRGNARLPVKWMAPESLFEGIYTIKSDVWSYGILLWEIFSLGVNPYPGIPVDANFYKLIQNGFKMDQPFYATEEIYIIMQSCWAFDSRKRPSFPNLTSFLGCQLADAEEAMYQNVDGRVSECPHTYQNRRPFSREMDLGLLSPQAQVEDS
uniprot
proteins
disease_involvement
DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: 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. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. {ECO:0000269|PubMed:11090077, ECO:0000269|PubMed:11290608, ECO:0000269|PubMed:11442493, ECO:0000269|PubMed:14504097, ECO:0000269|PubMed:16266983, ECO:0000269|PubMed:18305215, ECO:0000269|PubMed:8946930, ECO:0000269|PubMed:9737679}. Note=The gene represented in this entry may be involved in disease pathogenesis. Somatic mutations that lead to constitutive activation of FLT3 are frequent in AML patients. These mutations fall into two classes, the most common being in-frame internal tandem duplications of variable length in the juxtamembrane region that disrupt the normal regulation of the kinase activity. Likewise, point mutations in the activation loop of the kinase domain can result in a constitutively activated kinase.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for the cytokine FLT3LG and regulates differentiation, proliferation and survival of hematopoietic progenitor cells and of dendritic cells. 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. {ECO:0000269|PubMed:10080542, ECO:0000269|PubMed:11090077, ECO:0000269|PubMed:14504097, ECO:0000269|PubMed:16266983, ECO:0000269|PubMed:16627759, ECO:0000269|PubMed:18490735, ECO:0000269|PubMed:20111072, ECO:0000269|PubMed:21067588, ECO:0000269|PubMed:21262971, ECO:0000269|PubMed:21516120, ECO:0000269|PubMed:7507245}.
uniprot
proteins
mass_dalton
112903
uniprot
proteins
mutagenesis
MUTAGEN 589; /note="Y->F: Reduced phosphorylation of the wild-type kinase in response to ligand binding. No effect on the phosphorylation of the constitutively activated mutant kinase variants. Abolishes activation of STAT5A."; /evidence="ECO:0000269|PubMed:16627759, ECO:0000269|PubMed:16684964, ECO:0000269|PubMed:9737679"; MUTAGEN 591; /note="Y->F: No significant effect on tyrosine phosphorylation. Abolishes activation of STAT5A."; /evidence="ECO:0000269|PubMed:16627759, ECO:0000269|PubMed:9737679"; MUTAGEN 599; /note="Y->F: Abolishes interaction with PTPN11/SHP2 and phosphorylation of PTPN11/SHP2."; /evidence="ECO:0000269|PubMed:16684964"; MUTAGEN 644; /note="K->A: Abolishes kinase activity."; /evidence="ECO:0000269|PubMed:15831474
uniprot
proteins
post_translational_modification
PTM: N-glycosylated, contains complex N-glycans with sialic acid. {ECO:0000269|PubMed:15831474, ECO:0000269|PubMed:21262971, ECO:0000269|PubMed:21389326}.; PTM: 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.; PTM: Rapidly ubiquitinated by UBE2L6 and the E3 ubiquitin-protein ligase SIAH1 after autophosphorylation, leading to its proteasomal degradation. {ECO:0000269|PubMed:20508617, ECO:0000269|PubMed:21262971}.
uniprot
proteins
protein_family
CSF-1/PDGF receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10080542
uniprot
proteins
pubmed
11090077
uniprot
proteins
pubmed
11290608
uniprot
proteins
pubmed
11442493
uniprot
proteins
pubmed
12951584
uniprot
proteins
pubmed
14504097
uniprot
proteins
pubmed
14759363
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15831474
uniprot
proteins
pubmed
16266983
uniprot
proteins
pubmed
16627759
uniprot
proteins
pubmed
16684964
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18305215
uniprot
proteins
pubmed
18490735
uniprot
proteins
pubmed
18987736
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19477218
uniprot
proteins
pubmed
19549778
uniprot
proteins
pubmed
2004790
uniprot
proteins
pubmed
20111072
uniprot
proteins
pubmed
20508617
uniprot
proteins
pubmed
21067588
uniprot
proteins
pubmed
21262971
uniprot
proteins
pubmed
21389326
uniprot
proteins
pubmed
21516120
uniprot
proteins
pubmed
29691342
uniprot
proteins
pubmed
7507245
uniprot
proteins
pubmed
8394751
uniprot
proteins
pubmed
8637232
uniprot
proteins
pubmed
8946930
uniprot
proteins
pubmed
9737679
uniprot
proteins
sequence_length
993
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Endoplasmic reticulum lumen. Note=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. The activated kinase is rapidly targeted for degradation.
uniprot
proteins
transmembrane_region
TRANSMEM 544..563; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins