Skip Header

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

Receptor-type tyrosine-protein kinase FLT3

Gene

FLT3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Tyrosine-protein kinase that acts as 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.11 Publications

Miscellaneous

Can be used as diagnostic tool to establish the exact cause of acute myeloid leukemia, and to determine the optimal therapy.

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation1 Publication

Activity regulationi

Present in an inactive conformation in the absence of bound ligand. FLT3LG binding leads to dimerization and activation by autophosphorylation.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei644ATPCurated1
Active sitei811Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi616 – 624ATPPROSITE-ProRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processHost-virus interaction
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-HSA-109704 PI3K Cascade
R-HSA-449836 Other interleukin signaling
R-HSA-5673001 RAF/MAP kinase cascade
SignaLinkiP36888
SIGNORiP36888

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein kinase FLT3 (EC:2.7.10.1)
Alternative name(s):
FL cytokine receptor
Fetal liver kinase-2
Short name:
FLK-2
Fms-like tyrosine kinase 3
Short name:
FLT-3
Stem cell tyrosine kinase 1
Short name:
STK-1
CD_antigen: CD135
Gene namesi
Name:FLT3
Synonyms:CD135, FLK2, STK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

EuPathDBiHostDB:ENSG00000122025.14
HGNCiHGNC:3765 FLT3
MIMi136351 gene
neXtProtiNX_P36888

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini27 – 543ExtracellularSequence analysisAdd BLAST517
Transmembranei544 – 563HelicalSequence analysisAdd BLAST20
Topological domaini564 – 993CytoplasmicSequence analysisAdd BLAST430

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Leukemia, acute myelogenous (AML)8 Publications
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.
Disease descriptionA 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.
See also OMIM:601626

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi589Y → 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. 3 Publications1
Mutagenesisi591Y → F: No significant effect on tyrosine phosphorylation. Abolishes activation of STAT5A. 2 Publications1
Mutagenesisi599Y → F: Abolishes interaction with PTPN11/SHP2 and phosphorylation of PTPN11/SHP2. 1 Publication1
Mutagenesisi644K → A: Abolishes kinase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNETi2322
MalaCardsiFLT3
MIMi601626 phenotype
OpenTargetsiENSG00000122025
Orphaneti98829 'Acute myeloid leukemia with abnormal bone marrow eosinophils inv(16)(p13q22) or t(16;16)(p13;q22)'
102724 'Acute myeloid leukemia with t(8;21)(q22;q22) translocation'
98837 Acute biphenotypic leukemia
98834 Acute myeloblastic leukemia with maturation
98833 Acute myeloblastic leukemia without maturation
98832 Minimally differentiated acute myeloblastic leukemia
99860 Precursor B-cell acute lymphoblastic leukemia
99861 Precursor T-cell acute lymphoblastic leukemia
PharmGKBiPA28181

Chemistry databases

ChEMBLiCHEMBL1974
DrugBankiDB06080 ABT-869
DB05213 AC220
DB05465 MLN-518
DB05216 MP470
DB09079 Nintedanib
DB08901 Ponatinib
DB00398 Sorafenib
DB01268 Sunitinib
DB05014 XL999
GuidetoPHARMACOLOGYi1807

Polymorphism and mutation databases

BioMutaiFLT3
DMDMi156630887

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000001677827 – 993Receptor-type tyrosine-protein kinase FLT3Add BLAST967

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi35 ↔ 65PROSITE-ProRule annotation1 Publication
Glycosylationi43N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi100N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi103 ↔ 114PROSITE-ProRule annotation1 Publication
Glycosylationi151N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi199 ↔ 206PROSITE-ProRule annotation1 Publication
Disulfide bondi232 ↔ 241PROSITE-ProRule annotation1 Publication
Disulfide bondi272 ↔ 330PROSITE-ProRule annotation1 Publication
Glycosylationi306N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi323N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi351N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi354N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi368 ↔ 407PROSITE-ProRule annotation1 Publication
Disulfide bondi381 ↔ 392PROSITE-ProRule annotation1 Publication
Glycosylationi473N-linked (GlcNAc...) asparagine1
Glycosylationi502N-linked (GlcNAc...) asparagine1
Glycosylationi541N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei572Phosphotyrosine2 Publications1
Modified residuei574Phosphoserine1 Publication1
Modified residuei589Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei591Phosphotyrosine; by autocatalysis5 Publications1
Modified residuei599Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei726Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei759PhosphoserineCombined sources1
Modified residuei768Phosphotyrosine2 Publications1
Modified residuei793Phosphotyrosine2 Publications1
Modified residuei842Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei955Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei969Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei993PhosphoserineCombined sources1

Post-translational modificationi

N-glycosylated, contains complex N-glycans with sialic acid.3 Publications
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.
Rapidly ubiquitinated by UBE2L6 and the E3 ubiquitin-protein ligase SIAH1 after autophosphorylation, leading to its proteasomal degradation.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP36888
PaxDbiP36888
PeptideAtlasiP36888
PRIDEiP36888
ProteomicsDBi55226
55227 [P36888-2]

PTM databases

iPTMnetiP36888
PhosphoSitePlusiP36888

Expressioni

Tissue specificityi

Detected in bone marrow, in hematopoietic stem cells, in myeloid progenitor cells and in granulocyte/macrophage progenitor cells (at protein level). Detected in bone marrow, liver, thymus, spleen and lymph node, and at low levels in kidney and pancreas. Highly expressed in T-cell leukemia.4 Publications

Gene expression databases

BgeeiENSG00000122025 Expressed in 100 organ(s), highest expression level in cerebellar hemisphere
CleanExiHS_FLT3
ExpressionAtlasiP36888 baseline and differential
GenevisibleiP36888 HS

Organism-specific databases

HPAiHPA047539

Interactioni

Subunit structurei

Monomer in the absence of bound FLT3LG. Homodimer in the presence of bound FLT3LG. Interacts with FIZ1 following ligand activation (By similarity). Interacts with FES, FER, LYN, FGR, HCK, SRC and GRB2. Interacts with PTPRJ/DEP-1 and PTPN11/SHP2. Interacts with RNF115 and RNF126 (By similarity).By similarity6 Publications
(Microbial infection) Interacts with human cytomegalovirus protein UL7.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi108610, 14 interactors
DIPiDIP-59769N
IntActiP36888, 7 interactors
MINTiP36888
STRINGi9606.ENSP00000241453

Chemistry databases

BindingDBiP36888

Structurei

Secondary structure

1993
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP36888
SMRiP36888
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36888

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini253 – 343Ig-like C2-typeAdd BLAST91
Domaini610 – 943Protein kinasePROSITE-ProRule annotationAdd BLAST334

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni591 – 597Important for normal regulation of the kinase activity and for maintaining the kinase in an inactive state in the absence of bound ligand7

Domaini

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.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00760000118923
HOVERGENiHBG005735
InParanoidiP36888
KOiK05092
OMAiFHRTWTE
OrthoDBiEOG091G01TL
PhylomeDBiP36888
TreeFamiTF325768

Family and domain databases

Gene3Di2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR030118 FLT3
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013151 Immunoglobulin
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR001824 Tyr_kinase_rcpt_3_CS
PANTHERiPTHR24416:SF356 PTHR24416:SF356, 1 hit
PfamiView protein in Pfam
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit
SMARTiView protein in SMART
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 1 hit
SSF56112 SSF56112, 2 hits
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS00240 RECEPTOR_TYR_KIN_III, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P36888-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MPALARDGGQ LPLLVVFSAM IFGTITNQDL PVIKCVLINH KNNDSSVGKS
60 70 80 90 100
SSYPMVSESP EDLGCALRPQ SSGTVYEAAA VEVDVSASIT LQVLVDAPGN
110 120 130 140 150
ISCLWVFKHS SLNCQPHFDL QNRGVVSMVI LKMTETQAGE YLLFIQSEAT
160 170 180 190 200
NYTILFTVSI RNTLLYTLRR PYFRKMENQD ALVCISESVP EPIVEWVLCD
210 220 230 240 250
SQGESCKEES PAVVKKEEKV LHELFGTDIR CCARNELGRE CTRLFTIDLN
260 270 280 290 300
QTPQTTLPQL FLKVGEPLWI RCKAVHVNHG FGLTWELENK ALEEGNYFEM
310 320 330 340 350
STYSTNRTMI RILFAFVSSV ARNDTGYYTC SSSKHPSQSA LVTIVEKGFI
360 370 380 390 400
NATNSSEDYE IDQYEEFCFS VRFKAYPQIR CTWTFSRKSF PCEQKGLDNG
410 420 430 440 450
YSISKFCNHK HQPGEYIFHA ENDDAQFTKM FTLNIRRKPQ VLAEASASQA
460 470 480 490 500
SCFSDGYPLP SWTWKKCSDK SPNCTEEITE GVWNRKANRK VFGQWVSSST
510 520 530 540 550
LNMSEAIKGF LVKCCAYNSL GTSCETILLN SPGPFPFIQD NISFYATIGV
560 570 580 590 600
CLLFIVVLTL LICHKYKKQF RYESQLQMVQ VTGSSDNEYF YVDFREYEYD
610 620 630 640 650
LKWEFPRENL EFGKVLGSGA FGKVMNATAY GISKTGVSIQ VAVKMLKEKA
660 670 680 690 700
DSSEREALMS ELKMMTQLGS HENIVNLLGA CTLSGPIYLI FEYCCYGDLL
710 720 730 740 750
NYLRSKREKF HRTWTEIFKE HNFSFYPTFQ SHPNSSMPGS REVQIHPDSD
760 770 780 790 800
QISGLHGNSF HSEDEIEYEN QKRLEEEEDL NVLTFEDLLC FAYQVAKGME
810 820 830 840 850
FLEFKSCVHR DLAARNVLVT HGKVVKICDF GLARDIMSDS NYVVRGNARL
860 870 880 890 900
PVKWMAPESL FEGIYTIKSD VWSYGILLWE IFSLGVNPYP GIPVDANFYK
910 920 930 940 950
LIQNGFKMDQ PFYATEEIYI IMQSCWAFDS RKRPSFPNLT SFLGCQLADA
960 970 980 990
EEAMYQNVDG RVSECPHTYQ NRRPFSREMD LGLLSPQAQV EDS
Length:993
Mass (Da):112,903
Last modified:August 21, 2007 - v2
Checksum:i6C1995718F352ECE
GO
Isoform 2 (identifier: P36888-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     807-847: Missing.

Show »
Length:952
Mass (Da):108,378
Checksum:i1C384B292EDEB144
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7ER61E7ER61_HUMAN
Receptor-type tyrosine-protein kina...
FLT3
739Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti8G → A in AAA18947 (PubMed:7507245).Curated1
Sequence conflicti10 – 11QL → TV in AAA18947 (PubMed:7507245).Curated2
Sequence conflicti71S → N in AAI44040 (PubMed:15489334).Curated1
Sequence conflicti78A → R in CAA81393 (PubMed:8394751).Curated1
Sequence conflicti346E → G in AAA18947 (PubMed:7507245).Curated1
Sequence conflicti940T → H in AAA35487 (PubMed:2004790).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0346777D → G. Corresponds to variant dbSNP:rs12872889Ensembl.1
Natural variantiVAR_042069158V → A1 PublicationCorresponds to variant dbSNP:rs56321896Ensembl.1
Natural variantiVAR_054149194V → M1 PublicationCorresponds to variant dbSNP:rs146030737EnsemblClinVar.1
Natural variantiVAR_034678227T → M4 PublicationsCorresponds to variant dbSNP:rs1933437EnsemblClinVar.1
Natural variantiVAR_042070324D → N1 PublicationCorresponds to variant dbSNP:rs35602083EnsemblClinVar.1
Natural variantiVAR_042071358D → V1 PublicationCorresponds to variant dbSNP:rs34172843EnsemblClinVar.1
Natural variantiVAR_061291417I → L. Corresponds to variant dbSNP:rs56090538EnsemblClinVar.1
Natural variantiVAR_042072557V → I1 PublicationCorresponds to variant dbSNP:rs35958982EnsemblClinVar.1
Natural variantiVAR_065679835D → E in acute lymphoblastic leukemia patients and acute myelogenous leukemia patients; somatic mutation; constitutively activated. 2 PublicationsCorresponds to variant dbSNP:rs121913487EnsemblClinVar.1
Natural variantiVAR_065680835D → H in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 3 PublicationsCorresponds to variant dbSNP:rs121913488EnsemblClinVar.1
Natural variantiVAR_065681835D → N in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 1 PublicationCorresponds to variant dbSNP:rs121913488EnsemblClinVar.1
Natural variantiVAR_065682835D → V in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 1 PublicationCorresponds to variant dbSNP:rs121909646EnsemblClinVar.1
Natural variantiVAR_065683835D → Y in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 3 PublicationsCorresponds to variant dbSNP:rs121913488EnsemblClinVar.1
Natural variantiVAR_065684836I → M in acute lymphoblastic leukemia patients; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913232EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_041796807 – 847Missing in isoform 2. 1 PublicationAdd BLAST41

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02687 mRNA Translation: AAA18947.1
Z26652 mRNA Translation: CAA81393.1
AL356915 Genomic DNA No translation available.
AL445262 Genomic DNA No translation available.
AL591024 Genomic DNA No translation available.
CH471075 Genomic DNA Translation: EAX08424.1
BC126350 mRNA Translation: AAI26351.1
BC144039 mRNA Translation: AAI44040.1
BC144040 mRNA Translation: AAI44041.1
L36162 mRNA Translation: AAA35487.1
CCDSiCCDS31953.1 [P36888-1]
PIRiA36873
A39061
RefSeqiNP_004110.2, NM_004119.2 [P36888-1]
UniGeneiHs.507590

Genome annotation databases

EnsembliENST00000241453; ENSP00000241453; ENSG00000122025 [P36888-1]
GeneIDi2322
KEGGihsa:2322
UCSCiuc001urw.3 human [P36888-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02687 mRNA Translation: AAA18947.1
Z26652 mRNA Translation: CAA81393.1
AL356915 Genomic DNA No translation available.
AL445262 Genomic DNA No translation available.
AL591024 Genomic DNA No translation available.
CH471075 Genomic DNA Translation: EAX08424.1
BC126350 mRNA Translation: AAI26351.1
BC144039 mRNA Translation: AAI44040.1
BC144040 mRNA Translation: AAI44041.1
L36162 mRNA Translation: AAA35487.1
CCDSiCCDS31953.1 [P36888-1]
PIRiA36873
A39061
RefSeqiNP_004110.2, NM_004119.2 [P36888-1]
UniGeneiHs.507590

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RJBX-ray2.10A564-958[»]
3QS7X-ray4.30E/F/G/H27-436[»]
3QS9X-ray7.80E/F/G/H27-540[»]
4RT7X-ray3.10A564-958[»]
4XUFX-ray3.20A/B600-947[»]
5X02X-ray2.40A564-958[»]
ProteinModelPortaliP36888
SMRiP36888
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108610, 14 interactors
DIPiDIP-59769N
IntActiP36888, 7 interactors
MINTiP36888
STRINGi9606.ENSP00000241453

Chemistry databases

BindingDBiP36888
ChEMBLiCHEMBL1974
DrugBankiDB06080 ABT-869
DB05213 AC220
DB05465 MLN-518
DB05216 MP470
DB09079 Nintedanib
DB08901 Ponatinib
DB00398 Sorafenib
DB01268 Sunitinib
DB05014 XL999
GuidetoPHARMACOLOGYi1807

PTM databases

iPTMnetiP36888
PhosphoSitePlusiP36888

Polymorphism and mutation databases

BioMutaiFLT3
DMDMi156630887

Proteomic databases

MaxQBiP36888
PaxDbiP36888
PeptideAtlasiP36888
PRIDEiP36888
ProteomicsDBi55226
55227 [P36888-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000241453; ENSP00000241453; ENSG00000122025 [P36888-1]
GeneIDi2322
KEGGihsa:2322
UCSCiuc001urw.3 human [P36888-1]

Organism-specific databases

CTDi2322
DisGeNETi2322
EuPathDBiHostDB:ENSG00000122025.14
GeneCardsiFLT3
H-InvDBiHIX0037338
HGNCiHGNC:3765 FLT3
HPAiHPA047539
MalaCardsiFLT3
MIMi136351 gene
601626 phenotype
neXtProtiNX_P36888
OpenTargetsiENSG00000122025
Orphaneti98829 'Acute myeloid leukemia with abnormal bone marrow eosinophils inv(16)(p13q22) or t(16;16)(p13;q22)'
102724 'Acute myeloid leukemia with t(8;21)(q22;q22) translocation'
98837 Acute biphenotypic leukemia
98834 Acute myeloblastic leukemia with maturation
98833 Acute myeloblastic leukemia without maturation
98832 Minimally differentiated acute myeloblastic leukemia
99860 Precursor B-cell acute lymphoblastic leukemia
99861 Precursor T-cell acute lymphoblastic leukemia
PharmGKBiPA28181
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00760000118923
HOVERGENiHBG005735
InParanoidiP36888
KOiK05092
OMAiFHRTWTE
OrthoDBiEOG091G01TL
PhylomeDBiP36888
TreeFamiTF325768

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-HSA-109704 PI3K Cascade
R-HSA-449836 Other interleukin signaling
R-HSA-5673001 RAF/MAP kinase cascade
SignaLinkiP36888
SIGNORiP36888

Miscellaneous databases

ChiTaRSiFLT3 human
EvolutionaryTraceiP36888
GeneWikiiCD135
GenomeRNAii2322
PROiPR:P36888
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000122025 Expressed in 100 organ(s), highest expression level in cerebellar hemisphere
CleanExiHS_FLT3
ExpressionAtlasiP36888 baseline and differential
GenevisibleiP36888 HS

Family and domain databases

Gene3Di2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR030118 FLT3
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013151 Immunoglobulin
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR001824 Tyr_kinase_rcpt_3_CS
PANTHERiPTHR24416:SF356 PTHR24416:SF356, 1 hit
PfamiView protein in Pfam
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit
SMARTiView protein in SMART
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 1 hit
SSF56112 SSF56112, 2 hits
PROSITEiView protein in PROSITE
PS50835 IG_LIKE, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS00240 RECEPTOR_TYR_KIN_III, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiFLT3_HUMAN
AccessioniPrimary (citable) accession number: P36888
Secondary accession number(s): A0AVG9
, B7ZLT7, B7ZLT8, F5H0A0, Q13414
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: August 21, 2007
Last modified: September 12, 2018
This is version 185 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  4. SIMILARITY comments
    Index of protein domains and families
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  7. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  8. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again