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P36888

- FLT3_HUMAN

UniProt

P36888 - FLT3_HUMAN

Protein

Receptor-type tyrosine-protein kinase FLT3

Gene

FLT3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (21 Aug 2007)
      Previous versions | rss
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    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

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.1 PublicationPROSITE-ProRule annotation

    Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei644 – 6441ATPCurated
    Active sitei811 – 8111Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi616 – 6249ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cytokine receptor activity Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein homodimerization activity Source: UniProtKB
    5. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB
    6. vascular endothelial growth factor-activated receptor activity Source: ProtInc

    GO - Biological processi

    1. B cell differentiation Source: UniProtKB
    2. cellular response to cytokine stimulus Source: UniProtKB
    3. common myeloid progenitor cell proliferation Source: UniProtKB
    4. cytokine-mediated signaling pathway Source: UniProtKB
    5. dendritic cell differentiation Source: UniProtKB
    6. hemopoiesis Source: MGI
    7. leukocyte homeostasis Source: UniProtKB
    8. lymphocyte proliferation Source: UniProtKB
    9. myeloid progenitor cell differentiation Source: UniProtKB
    10. negative regulation of B cell differentiation Source: Ensembl
    11. negative regulation of cell proliferation Source: Ensembl
    12. peptidyl-tyrosine phosphorylation Source: UniProtKB
    13. positive regulation of cell proliferation Source: UniProtKB
    14. positive regulation of MAPK cascade Source: UniProtKB
    15. positive regulation of MAP kinase activity Source: UniProtKB
    16. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    17. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    18. positive regulation of tyrosine phosphorylation of STAT protein Source: UniProtKB
    19. pro-B cell differentiation Source: UniProtKB
    20. pro-T cell differentiation Source: Ensembl
    21. protein autophosphorylation Source: UniProtKB
    22. regulation of apoptotic process Source: UniProtKB
    23. transmembrane receptor protein tyrosine kinase signaling pathway Source: ProtInc
    24. vascular endothelial growth factor signaling pathway Source: GOC

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    SignaLinkiP36888.

    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
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:3765. FLT3.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    3. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.8 Publications
    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.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi589 – 5891Y → 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 Publications
    Mutagenesisi591 – 5911Y → F: No significant effect on tyrosine phosphorylation. Abolishes activation of STAT5A. 2 Publications
    Mutagenesisi599 – 5991Y → F: Abolishes interaction with PTPN11/SHP2 and phosphorylation of PTPN11/SHP2. 1 Publication
    Mutagenesisi644 – 6441K → A: Abolishes kinase activity. 1 Publication

    Keywords - Diseasei

    Disease mutation, Proto-oncogene

    Organism-specific databases

    MIMi601626. phenotype.
    Orphaneti98837. Acute biphenotypic leukemia.
    98834. Acute myeloblastic leukemia with maturation.
    98833. Acute myeloblastic leukemia without maturation.
    98829. 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.
    517. Acute myelomonocytic leukemia.
    98832. Minimally differentiated acute myeloblastic leukemia.
    99860. Precursor B-cell acute lymphoblastic leukemia.
    99861. Precursor T-cell acute lymphoblastic leukemia.
    PharmGKBiPA28181.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 993967Receptor-type tyrosine-protein kinase FLT3PRO_0000016778Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi35 ↔ 651 PublicationPROSITE-ProRule annotation
    Glycosylationi43 – 431N-linked (GlcNAc...)1 Publication
    Glycosylationi100 – 1001N-linked (GlcNAc...)1 Publication
    Disulfide bondi103 ↔ 1141 PublicationPROSITE-ProRule annotation
    Glycosylationi151 – 1511N-linked (GlcNAc...)1 Publication
    Disulfide bondi199 ↔ 2061 PublicationPROSITE-ProRule annotation
    Disulfide bondi232 ↔ 2411 PublicationPROSITE-ProRule annotation
    Disulfide bondi272 ↔ 3301 PublicationPROSITE-ProRule annotation
    Glycosylationi306 – 3061N-linked (GlcNAc...)1 Publication
    Glycosylationi323 – 3231N-linked (GlcNAc...)1 Publication
    Glycosylationi351 – 3511N-linked (GlcNAc...)1 Publication
    Glycosylationi354 – 3541N-linked (GlcNAc...)1 Publication
    Disulfide bondi368 ↔ 4071 PublicationPROSITE-ProRule annotation
    Disulfide bondi381 ↔ 3921 PublicationPROSITE-ProRule annotation
    Glycosylationi473 – 4731N-linked (GlcNAc...)
    Glycosylationi502 – 5021N-linked (GlcNAc...)
    Glycosylationi541 – 5411N-linked (GlcNAc...)Sequence Analysis
    Modified residuei572 – 5721Phosphotyrosine2 Publications
    Modified residuei574 – 5741Phosphoserine1 Publication
    Modified residuei589 – 5891Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei591 – 5911Phosphotyrosine; by autocatalysis5 Publications
    Modified residuei599 – 5991Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei726 – 7261Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei759 – 7591Phosphoserine1 Publication
    Modified residuei768 – 7681Phosphotyrosine2 Publications
    Modified residuei793 – 7931Phosphotyrosine2 Publications
    Modified residuei842 – 8421Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei955 – 9551Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei969 – 9691Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei993 – 9931Phosphoserine1 Publication

    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

    PaxDbiP36888.
    PRIDEiP36888.

    PTM databases

    PhosphoSiteiP36888.

    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

    ArrayExpressiP36888.
    BgeeiP36888.
    CleanExiHS_FLT3.
    GenevestigatoriP36888.

    Organism-specific databases

    HPAiCAB018358.

    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.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IKBKGQ9Y6K92EBI-3946257,EBI-81279
    PIK3R1P279862EBI-3946257,EBI-79464

    Protein-protein interaction databases

    BioGridi108610. 13 interactions.
    DIPiDIP-59769N.
    IntActiP36888. 3 interactions.
    MINTiMINT-7103562.
    STRINGi9606.ENSP00000241453.

    Structurei

    Secondary structure

    1
    993
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi575 – 5817
    Beta strandi583 – 5853
    Beta strandi589 – 5913
    Helixi594 – 5963
    Helixi601 – 6033
    Helixi607 – 6093
    Beta strandi610 – 6189
    Beta strandi620 – 63112
    Beta strandi633 – 6364
    Beta strandi638 – 6469
    Helixi656 – 66813
    Beta strandi677 – 6815
    Beta strandi683 – 6864
    Beta strandi688 – 6925
    Helixi699 – 7046
    Turni705 – 7084
    Helixi785 – 80420
    Beta strandi807 – 8093
    Helixi814 – 8163
    Beta strandi817 – 8204
    Turni821 – 8233
    Beta strandi824 – 8274
    Helixi831 – 8333
    Helixi836 – 8383
    Beta strandi842 – 8454
    Beta strandi848 – 8503
    Helixi852 – 8543
    Helixi857 – 8626
    Helixi867 – 88115
    Turni882 – 8843
    Helixi896 – 9038

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RJBX-ray2.10A564-907[»]
    3QS7X-ray4.30E/F/G/H27-436[»]
    3QS9X-ray7.80E/F/G/H27-540[»]
    DisProtiDP00312.
    ProteinModelPortaliP36888.
    SMRiP36888. Positions 79-529, 572-975.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36888.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini27 – 543517ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini564 – 993430CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei544 – 56320HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini253 – 34391Ig-like C2-typeAdd
    BLAST
    Domaini610 – 943334Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni591 – 5977Important for normal regulation of the kinase activity and for maintaining the kinase in an inactive state in the absence of bound ligand

    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
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG005735.
    KOiK05092.
    OrthoDBiEOG7H792D.
    PhylomeDBiP36888.
    TreeFamiTF325768.

    Family and domain databases

    Gene3Di2.60.40.10. 2 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013151. Immunoglobulin.
    IPR011009. Kinase-like_dom.
    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.
    IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
    IPR001824. Tyr_kinase_rcpt_3_CS.
    [Graphical view]
    PfamiPF00047. ig. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTiSM00409. IG. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS50835. 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.
    [Graphical view]

    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. Align

    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

    MPALARDGGQ LPLLVVFSAM IFGTITNQDL PVIKCVLINH KNNDSSVGKS    50
    SSYPMVSESP EDLGCALRPQ SSGTVYEAAA VEVDVSASIT LQVLVDAPGN 100
    ISCLWVFKHS SLNCQPHFDL QNRGVVSMVI LKMTETQAGE YLLFIQSEAT 150
    NYTILFTVSI RNTLLYTLRR PYFRKMENQD ALVCISESVP EPIVEWVLCD 200
    SQGESCKEES PAVVKKEEKV LHELFGTDIR CCARNELGRE CTRLFTIDLN 250
    QTPQTTLPQL FLKVGEPLWI RCKAVHVNHG FGLTWELENK ALEEGNYFEM 300
    STYSTNRTMI RILFAFVSSV ARNDTGYYTC SSSKHPSQSA LVTIVEKGFI 350
    NATNSSEDYE IDQYEEFCFS VRFKAYPQIR CTWTFSRKSF PCEQKGLDNG 400
    YSISKFCNHK HQPGEYIFHA ENDDAQFTKM FTLNIRRKPQ VLAEASASQA 450
    SCFSDGYPLP SWTWKKCSDK SPNCTEEITE GVWNRKANRK VFGQWVSSST 500
    LNMSEAIKGF LVKCCAYNSL GTSCETILLN SPGPFPFIQD NISFYATIGV 550
    CLLFIVVLTL LICHKYKKQF RYESQLQMVQ VTGSSDNEYF YVDFREYEYD 600
    LKWEFPRENL EFGKVLGSGA FGKVMNATAY GISKTGVSIQ VAVKMLKEKA 650
    DSSEREALMS ELKMMTQLGS HENIVNLLGA CTLSGPIYLI FEYCCYGDLL 700
    NYLRSKREKF HRTWTEIFKE HNFSFYPTFQ SHPNSSMPGS REVQIHPDSD 750
    QISGLHGNSF HSEDEIEYEN QKRLEEEEDL NVLTFEDLLC FAYQVAKGME 800
    FLEFKSCVHR DLAARNVLVT HGKVVKICDF GLARDIMSDS NYVVRGNARL 850
    PVKWMAPESL FEGIYTIKSD VWSYGILLWE IFSLGVNPYP GIPVDANFYK 900
    LIQNGFKMDQ PFYATEEIYI IMQSCWAFDS RKRPSFPNLT SFLGCQLADA 950
    EEAMYQNVDG RVSECPHTYQ NRRPFSREMD LGLLSPQAQV EDS 993
    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti8 – 81G → A in AAA18947. (PubMed:7507245)Curated
    Sequence conflicti10 – 112QL → TV in AAA18947. (PubMed:7507245)Curated
    Sequence conflicti71 – 711S → N in AAI44040. (PubMed:15489334)Curated
    Sequence conflicti78 – 781A → R in CAA81393. (PubMed:8394751)Curated
    Sequence conflicti346 – 3461E → G in AAA18947. (PubMed:7507245)Curated
    Sequence conflicti940 – 9401T → H in AAA35487. (PubMed:2004790)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71D → G.
    Corresponds to variant rs12872889 [ dbSNP | Ensembl ].
    VAR_034677
    Natural varianti158 – 1581V → A.1 Publication
    Corresponds to variant rs56321896 [ dbSNP | Ensembl ].
    VAR_042069
    Natural varianti194 – 1941V → M.1 Publication
    VAR_054149
    Natural varianti227 – 2271T → M.4 Publications
    Corresponds to variant rs1933437 [ dbSNP | Ensembl ].
    VAR_034678
    Natural varianti324 – 3241D → N.1 Publication
    Corresponds to variant rs35602083 [ dbSNP | Ensembl ].
    VAR_042070
    Natural varianti358 – 3581D → V.1 Publication
    Corresponds to variant rs34172843 [ dbSNP | Ensembl ].
    VAR_042071
    Natural varianti417 – 4171I → L.
    Corresponds to variant rs56090538 [ dbSNP | Ensembl ].
    VAR_061291
    Natural varianti557 – 5571V → I.1 Publication
    Corresponds to variant rs35958982 [ dbSNP | Ensembl ].
    VAR_042072
    Natural varianti835 – 8351D → E in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 2 Publications
    VAR_065679
    Natural varianti835 – 8351D → H in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 3 Publications
    VAR_065680
    Natural varianti835 – 8351D → N in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 1 Publication
    VAR_065681
    Natural varianti835 – 8351D → V in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 1 Publication
    VAR_065682
    Natural varianti835 – 8351D → Y in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 3 Publications
    VAR_065683
    Natural varianti836 – 8361I → M in acute lymphoblastic leukemia patients; somatic mutation. 1 Publication
    VAR_065684

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei807 – 84741Missing in isoform 2. 1 PublicationVSP_041796Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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]
    uc010tdn.2. human. [P36888-2]

    Polymorphism databases

    DMDMi156630887.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS31953.1. [P36888-1 ]
    PIRi A36873.
    A39061.
    RefSeqi NP_004110.2. NM_004119.2. [P36888-1 ]
    UniGenei Hs.507590.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RJB X-ray 2.10 A 564-907 [» ]
    3QS7 X-ray 4.30 E/F/G/H 27-436 [» ]
    3QS9 X-ray 7.80 E/F/G/H 27-540 [» ]
    DisProti DP00312.
    ProteinModelPortali P36888.
    SMRi P36888. Positions 79-529, 572-975.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108610. 13 interactions.
    DIPi DIP-59769N.
    IntActi P36888. 3 interactions.
    MINTi MINT-7103562.
    STRINGi 9606.ENSP00000241453.

    Chemistry

    BindingDBi P36888.
    ChEMBLi CHEMBL1974.
    DrugBanki DB00398. Sorafenib.
    DB01268. Sunitinib.
    GuidetoPHARMACOLOGYi 1807.

    PTM databases

    PhosphoSitei P36888.

    Polymorphism databases

    DMDMi 156630887.

    Proteomic databases

    PaxDbi P36888.
    PRIDEi P36888.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000241453 ; ENSP00000241453 ; ENSG00000122025 . [P36888-1 ]
    GeneIDi 2322.
    KEGGi hsa:2322.
    UCSCi uc001urw.3. human. [P36888-1 ]
    uc010tdn.2. human. [P36888-2 ]

    Organism-specific databases

    CTDi 2322.
    GeneCardsi GC13M028577.
    H-InvDB HIX0037338.
    HGNCi HGNC:3765. FLT3.
    HPAi CAB018358.
    MIMi 136351. gene.
    601626. phenotype.
    neXtProti NX_P36888.
    Orphaneti 98837. Acute biphenotypic leukemia.
    98834. Acute myeloblastic leukemia with maturation.
    98833. Acute myeloblastic leukemia without maturation.
    98829. 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.
    517. Acute myelomonocytic leukemia.
    98832. Minimally differentiated acute myeloblastic leukemia.
    99860. Precursor B-cell acute lymphoblastic leukemia.
    99861. Precursor T-cell acute lymphoblastic leukemia.
    PharmGKBi PA28181.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG005735.
    KOi K05092.
    OrthoDBi EOG7H792D.
    PhylomeDBi P36888.
    TreeFami TF325768.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    SignaLinki P36888.

    Miscellaneous databases

    EvolutionaryTracei P36888.
    GeneWikii CD135.
    GenomeRNAii 2322.
    NextBioi 9425.
    PROi P36888.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P36888.
    Bgeei P36888.
    CleanExi HS_FLT3.
    Genevestigatori P36888.

    Family and domain databases

    Gene3Di 2.60.40.10. 2 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013151. Immunoglobulin.
    IPR011009. Kinase-like_dom.
    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.
    IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
    IPR001824. Tyr_kinase_rcpt_3_CS.
    [Graphical view ]
    Pfami PF00047. ig. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTi SM00409. IG. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "STK-1, the human homolog of Flk-2/Flt-3, is selectively expressed in CD34+ human bone marrow cells and is involved in the proliferation of early progenitor/stem cells."
      Small D., Levenstein M., Kim E., Carow C., Amin S., Rockwell P., Witte L., Burrow C., Ratajczak M.Z., Gewirtz A.M., Civin C.I.
      Proc. Natl. Acad. Sci. U.S.A. 91:459-463(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Bone marrow.
    2. "Human FLT3/FLK2 gene: cDNA cloning and expression in hematopoietic cells."
      Rosnet O., Schiff C., Pebusque M.J., Marchetto S., Tonnelle C., Toiron Y., Birg F., Birnbaum D.
      Blood 82:1110-1119(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT MET-227.
      Tissue: Lymphocyte.
    3. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT MET-227.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT MET-227.
    6. "Isolation and chromosomal localization of a novel FMS-like tyrosine kinase gene."
      Rosnet O., Mattei M.-G., Marchetto S., Birnbaum D.
      Genomics 9:380-385(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 783-942 (ISOFORM 1).
      Tissue: Testis.
    7. "Human FLT3/FLK2 receptor tyrosine kinase is expressed at the surface of normal and malignant hematopoietic cells."
      Rosnet O., Buhring H.J., Marchetto S., Rappold I., Lavagna C., Sainty D., Arnoulet C., Chabannon C., Kanz L., Hannum C., Birnbaum D.
      Leukemia 10:238-248(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    8. "Internal tandem duplication of the flt3 gene found in acute myeloid leukemia."
      Nakao M., Yokota S., Iwai T., Kaneko H., Horiike S., Kashima K., Sonoda Y., Fujimoto T., Misawa S.
      Leukemia 10:1911-1918(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN AML.
    9. "Internal tandem duplication of the FLT3 gene is a novel modality of elongation mutation which causes constitutive activation of the product."
      Kiyoi H., Towatari M., Yokota S., Hamaguchi M., Ohno R., Saito H., Naoe T.
      Leukemia 12:1333-1337(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN AML, SUBUNIT, PHOSPHORYLATION, MUTAGENESIS OF TYR-589 AND TYR-591.
    10. "Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and their association with Grb2 and Shc in Baf3/Flt3 cells."
      Zhang S., Mantel C., Broxmeyer H.E.
      J. Leukoc. Biol. 65:372-380(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROMOTING PHOSPHORYLATION OF SHC1; PTPN6/SHP; PTPN11/SHP-2; MAPK1/ERK2; MAPK3/ERK1, AUTOPHOSPHORYLATION, INTERACTION WITH GRB2.
    11. "Flt3 mutations from patients with acute myeloid leukemia induce transformation of 32D cells mediated by the Ras and STAT5 pathways."
      Mizuki M., Fenski R., Halfter H., Matsumura I., Schmidt R., Muller C., Gruning W., Kratz-Albers K., Serve S., Steur C., Buchner T., Kienast J., Kanakura Y., Berdel W.E., Serve H.
      Blood 96:3907-3914(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIVATION OF AKT1; MAPK1/ERK2; MAPK3/ERK1; STAT5A AND STAT5B, PHOSPHORYLATION, FUNCTION IN ACTIVATION OF THE RAS PATHWAY, INVOLVEMENT IN AML.
    12. "Constitutive activation of Akt by Flt3 internal tandem duplications is necessary for increased survival, proliferation, and myeloid transformation."
      Brandts C.H., Sargin B., Rode M., Biermann C., Lindtner B., Schwable J., Buerger H., Muller-Tidow C., Choudhary C., McMahon M., Berdel W.E., Serve H.
      Cancer Res. 65:9643-9650(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIVATION OF AKT1, INVOLVEMENT IN AML.
    13. "Tyrosine phosphorylation regulates maturation of receptor tyrosine kinases."
      Schmidt-Arras D.E., Bohmer A., Markova B., Choudhary C., Serve H., Bohmer F.D.
      Mol. Cell. Biol. 25:3690-3703(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-591, DEPHOSPHORYLATION BY PTPN1; PTPN6/SHP-1 AND PTPN12, PROTEASOMAL DEGRADATION, GLYCOSYLATION, MUTAGENESIS OF LYS-644.
    14. "Roles of tyrosine 589 and 591 in STAT5 activation and transformation mediated by FLT3-ITD."
      Rocnik J.L., Okabe R., Yu J.C., Lee B.H., Giese N., Schenkein D.P., Gilliland D.G.
      Blood 108:1339-1345(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIVATION OF STAT5A AND/OR STAT5B, PHOSPHORYLATION AT TYR-591; TYR-726; TYR-842; TYR-955 AND TYR-969, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF TYR-589 AND TYR-591.
    15. "Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2."
      Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L.
      Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPN11/SHP2; LYN; FGR; HCK AND SRC, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-589 AND TYR-599, PHOSPHORYLATION AT TYR-572; SER-574; TYR-589; TYR-591 AND TYR-599.
    16. Cited for: REGION INVOLVED IN REGULATION OF KINASE ACTIVITY, AUTOREGULATORY DOMAIN, INVOLVEMENT IN AML.
    17. "Human Flt3 is expressed at the hematopoietic stem cell and the granulocyte/macrophage progenitor stages to maintain cell survival."
      Kikushige Y., Yoshimoto G., Miyamoto T., Iino T., Mori Y., Iwasaki H., Niiro H., Takenaka K., Nagafuji K., Harada M., Ishikawa F., Akashi K.
      J. Immunol. 180:7358-7367(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    18. "Oncogenic Flt3 receptors display different specificity and kinetics of autophosphorylation."
      Razumovskaya E., Masson K., Khan R., Bengtsson S., Ronnstrand L.
      Exp. Hematol. 37:979-989(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-589; TYR-591; TYR-599; TYR-726; TYR-768; TYR-793; TYR-842 AND TYR-955.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759 AND SER-993, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: FUNCTION IN ACTIVATION OF FES AND FER, INTERACTION WITH FES AND FER.
    21. "Ubiquitin conjugase UBCH8 targets active FMS-like tyrosine kinase 3 for proteasomal degradation."
      Buchwald M., Pietschmann K., Muller J.P., Bohmer F.D., Heinzel T., Kramer O.H.
      Leukemia 24:1412-1421(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    22. "mTOR signaling is activated by FLT3 kinase and promotes survival of FLT3-mutated acute myeloid leukemia cells."
      Chen W., Drakos E., Grammatikakis I., Schlette E.J., Li J., Leventaki V., Staikou-Drakopoulou E., Patsouris E., Panayiotidis P., Medeiros L.J., Rassidakis G.Z.
      Mol. Cancer 9:292-292(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. Cited for: INTERACTION WITH PTPRJ/DEP1, FUNCTION IN ACTIVATION OF MAPK1/ERK2; MAPK3/ERK1; PLCG1; STAT5A AND/OR STAT5B, GLYCOSYLATION, UBIQUITINATION, PHOSPHORYLATION AT TYR-572; TYR-589; TYR-591; TYR-599; TYR-768; TYR-793; TYR-842 AND TYR-955.
    24. "Further activation of FLT3 mutants by FLT3 ligand."
      Zheng R., Bailey E., Nguyen B., Yang X., Piloto O., Levis M., Small D.
      Oncogene 30:4004-4014(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
    25. "The role of FLT3 in haematopoietic malignancies."
      Stirewalt D.L., Radich J.P.
      Nat. Rev. Cancer 3:650-665(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    26. "Structural and functional alterations of FLT3 in acute myeloid leukemia."
      Meshinchi S., Appelbaum F.R.
      Clin. Cancer Res. 15:4263-4269(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    27. "The structural basis for autoinhibition of FLT3 by the juxtamembrane domain."
      Griffith J., Black J., Faerman C., Swenson L., Wynn M., Lu F., Lippke J., Saxena K.
      Mol. Cell 13:169-178(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 564-958, ENZYME REGULATION.
    28. "Structural insights into the extracellular assembly of the hematopoietic Flt3 signaling complex."
      Verstraete K., Vandriessche G., Januar M., Elegheert J., Shkumatov A.V., Desfosses A., Van Craenenbroeck K., Svergun D.I., Gutsche I., Vergauwen B., Savvides S.N.
      Blood 118:60-68(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (4.3 ANGSTROMS) OF 27-436 IN COMPLEX WITH FLT3LG, SUBUNIT, INTERACTION WITH FLT3LG, GLYCOSYLATION AT ASN-43; ASN-100; ASN-151; ASN-306; ASN-323; ASN-351 AND ASN-354, IDENTIFICATION BY MASS SPECTROMETRY, DISULFIDE BONDS.
    29. "Identification of novel FLT-3 Asp835 mutations in adult acute myeloid leukaemia."
      Abu-Duhier F.M., Goodeve A.C., Wilson G.A., Care R.S., Peake I.R., Reilly J.T.
      Br. J. Haematol. 113:983-988(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TYR-835 DEL; HIS-835 AND TYR-835, INVOLVEMENT IN AML.
    30. Cited for: VARIANTS ASN-835; GLU-835; HIS-835; VAL-835 AND TYR-835, CHARACTERIZATION OF VARIANTS ASN-835; GLU-835; HIS-835; VAL-835 AND TYR-835, PHOSPHORYLATION, INVOLVEMENT IN AML.
    31. "FLT3 mutations in the activation loop of tyrosine kinase domain are frequently found in infant ALL with MLL rearrangements and pediatric ALL with hyperdiploidy."
      Taketani T., Taki T., Sugita K., Furuichi Y., Ishii E., Hanada R., Tsuchida M., Sugita K., Ida K., Hayashi Y.
      Blood 103:1085-1088(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLU-835; HIS-835; TYR-835; ILE-836 DEL AND MET-836, FUNCTION IN ACTIVATION OF STAT5A AND/OR STAT5B, PHOSPHORYLATION, INVOLVEMENT IN AML.
    32. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-158; MET-227; ASN-324; VAL-358 AND ILE-557.
    33. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-194.

    Entry informationi

    Entry nameiFLT3_HUMAN
    AccessioniPrimary (citable) accession number: P36888
    Secondary accession number(s): A0AVG9
    , B7ZLT7, B7ZLT8, F5H0A0, Q13414
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [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

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3