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Q00342

- FLT3_MOUSE

UniProt

Q00342 - FLT3_MOUSE

Protein

Receptor-type tyrosine-protein kinase FLT3

Gene

Flt3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      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.5 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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei645 – 6451ATPPROSITE-ProRule annotation
    Active sitei814 – 8141Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi617 – 6259ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cytokine receptor activity Source: UniProtKB
    3. phosphatidylinositol 3-kinase binding Source: MGI
    4. protein binding Source: MGI
    5. protein tyrosine kinase activity Source: MGI
    6. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB-EC

    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 differentiation Source: MGI
    9. lymphocyte proliferation Source: UniProtKB
    10. lymphoid progenitor cell differentiation Source: MGI
    11. myeloid progenitor cell differentiation Source: UniProtKB
    12. negative regulation of B cell differentiation Source: MGI
    13. negative regulation of cell proliferation Source: MGI
    14. peptidyl-tyrosine phosphorylation Source: GOC
    15. positive regulation of protein phosphorylation Source: MGI
    16. pro-B cell differentiation Source: UniProtKB
    17. pro-T cell differentiation Source: MGI
    18. protein autophosphorylation Source: MGI
    19. transmembrane receptor protein tyrosine kinase signaling pathway Source: InterPro

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.

    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
    Tyrosine-protein kinase receptor flk-2
    CD_antigen: CD135
    Gene namesi
    Name:Flt3
    Synonyms:Flk-2, Flt-3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:95559. Flt3.

    Subcellular locationi

    Membrane; Single-pass type I membrane protein. Endoplasmic reticulum lumen By similarity
    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 By similarity.By similarity

    GO - Cellular componenti

    1. cell surface Source: MGI
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    3. external side of plasma membrane Source: MGI
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Mice are born at the expected Mendelian rate, develop normally and are fertile. They show normal blood cell counts, excepting reduced levels of primitive B-cell progenitors. Mice lacking both Flt3 and Kit show a reduction in both lymphoid and myeloid cell lineages. They appear normal, but are born at a lower frequency than expected and exhibit severely reduced viability after 3 weeks, none surviving more than six weeks.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi645 – 6451K → A: Loss of kinase activity; no effect on FIZ1-binding. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 992965Receptor-type tyrosine-protein kinase FLT3PRO_0000016779Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi36 ↔ 66PROSITE-ProRule annotation
    Glycosylationi44 – 441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi104 ↔ 115PROSITE-ProRule annotation
    Glycosylationi133 – 1331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi200 ↔ 207PROSITE-ProRule annotation
    Disulfide bondi233 ↔ 242PROSITE-ProRule annotation
    Disulfide bondi273 ↔ 331PROSITE-ProRule annotation
    Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi352 – 3521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi369 ↔ 408PROSITE-ProRule annotation
    Disulfide bondi382 ↔ 393PROSITE-ProRule annotation
    Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi474 – 4741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi503 – 5031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi542 – 5421N-linked (GlcNAc...)Sequence Analysis
    Modified residuei573 – 5731PhosphotyrosineBy similarity
    Modified residuei575 – 5751PhosphoserineBy similarity
    Modified residuei590 – 5901Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei592 – 5921Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei600 – 6001PhosphotyrosineBy similarity
    Modified residuei727 – 7271Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei760 – 7601PhosphoserineBy similarity
    Modified residuei769 – 7691PhosphotyrosineBy similarity
    Modified residuei796 – 7961PhosphotyrosineBy similarity
    Modified residuei845 – 8451Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei992 – 9921PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ00342.
    PRIDEiQ00342.

    PTM databases

    PhosphoSiteiQ00342.

    Expressioni

    Tissue specificityi

    Hematopoietic stem and progenitor cell-enriched populations. Found in brain, placenta and testis.

    Gene expression databases

    CleanExiMM_FLT3.
    GenevestigatoriQ00342.

    Interactioni

    Subunit structurei

    Monomer in the absence of bound FLT3LG. Homodimer in the presence of bound FLT3LG. Interacts with FIZ1 following ligand activation. Interacts with FES, FER, LYN, FGR, HCK, SRC and GRB2. Interacts with PTPRJ/DEP-1 and PTPN11/SHP2 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi199707. 4 interactions.
    MINTiMINT-85239.

    Structurei

    3D structure databases

    ProteinModelPortaliQ00342.
    SMRiQ00342. Positions 80-530, 573-953.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini28 – 544517ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini565 – 992428CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei545 – 56420HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini254 – 34491Ig-like C2-typeAdd
    BLAST
    Domaini611 – 946336Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni592 – 5987Important for normal regulation of the kinase activity and for maintaining the kinase in an inactive state in the absence of ligand bindingBy similarity

    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 By similarity.By similarity

    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.
    InParanoidiQ00342.
    KOiK05092.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    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. 2 hits.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    Q00342-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRALAQRSDR RLLLLVVLSV MILETVTNQD LPVIKCVLIS HENNGSSAGK    50
    PSSYRMVRGS PEDLQCTPRR QSEGTVYEAA TVEVAESGSI TLQVQLATPG 100
    DLSCLWVFKH SSLGCQPHFD LQNRGIVSMA ILNVTETQAG EYLLHIQSER 150
    ANYTVLFTVN VRDTQLYVLR RPYFRKMENQ DALLCISEGV PEPTVEWVLC 200
    SSHRESCKEE GPAVVRKEEK VLHELFGTDI RCCARNALGR ECTKLFTIDL 250
    NQAPQSTLPQ LFLKVGEPLW IRCKAIHVNH GFGLTWELED KALEEGSYFE 300
    MSTYSTNRTM IRILLAFVSS VGRNDTGYYT CSSSKHPSQS ALVTILEKGF 350
    INATSSQEEY EIDPYEKFCF SVRFKAYPRI RCTWIFSQAS FPCEQRGLED 400
    GYSISKFCDH KNKPGEYIFY AENDDAQFTK MFTLNIRKKP QVLANASASQ 450
    ASCSSDGYPL PSWTWKKCSD KSPNCTEEIP EGVWNKKANR KVFGQWVSSS 500
    TLNMSEAGKG LLVKCCAYNS MGTSCETIFL NSPGPFPFIQ DNISFYATIG 550
    LCLPFIVVLI VLICHKYKKQ FRYESQLQMI QVTGPLDNEY FYVDFRDYEY 600
    DLKWEFPREN LEFGKVLGSG AFGRVMNATA YGISKTGVSI QVAVKMLKEK 650
    ADSCEKEALM SELKMMTHLG HHDNIVNLLG ACTLSGPVYL IFEYCCYGDL 700
    LNYLRSKREK FHRTWTEIFK EHNFSSYPTF QAHSNSSMPG SREVQLHPPL 750
    DQLSGFNGNS IHSEDEIEYE NQKRLAEEEE EDLNVLTFED LLCFAYQVAK 800
    GMEFLEFKSC VHRDLAARNV LVTHGKVVKI CDFGLARDIL SDSSYVVRGN 850
    ARLPVKWMAP ESLFEGIYTI KSDVWSYGIL LWEIFSLGVN PYPGIPVDAN 900
    FYKLIQSGFK MEQPFYATEG IYFVMQSCWA FDSRKRPSFP NLTSFLGCQL 950
    AEAEEACIRT SIHLPKQAAP QQRGGLRAQS PQRQVKIHRE RS 992
    Length:992
    Mass (Da):112,640
    Last modified:April 1, 1993 - v1
    Checksum:i407A087853372100
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti150 – 1501R → A in CAA42041. (PubMed:1656368)Curated
    Sequence conflicti242 – 2421C → S in CAA42041. (PubMed:1656368)Curated
    Sequence conflicti726 – 7261S → F in CAA42041. (PubMed:1656368)Curated
    Sequence conflicti957 – 97923CIRTS…GLRAQ → MYQNMGGNVPEHPSIYQNRR PLSREAGSEPP in CAA42041. (PubMed:1656368)CuratedAdd
    BLAST
    Sequence conflicti983 – 9831R → A in CAA42041. (PubMed:1656368)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64689 mRNA. Translation: AAA37634.1.
    X59398 mRNA. Translation: CAA42041.1.
    PIRiA39931.
    S18827.
    RefSeqiNP_034359.2. NM_010229.2.
    UniGeneiMm.194.

    Genome annotation databases

    GeneIDi14255.
    KEGGimmu:14255.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64689 mRNA. Translation: AAA37634.1 .
    X59398 mRNA. Translation: CAA42041.1 .
    PIRi A39931.
    S18827.
    RefSeqi NP_034359.2. NM_010229.2.
    UniGenei Mm.194.

    3D structure databases

    ProteinModelPortali Q00342.
    SMRi Q00342. Positions 80-530, 573-953.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199707. 4 interactions.
    MINTi MINT-85239.

    Chemistry

    ChEMBLi CHEMBL2034796.

    PTM databases

    PhosphoSitei Q00342.

    Proteomic databases

    PaxDbi Q00342.
    PRIDEi Q00342.

    Protocols and materials databases

    DNASUi 14255.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 14255.
    KEGGi mmu:14255.

    Organism-specific databases

    CTDi 2322.
    MGIi MGI:95559. Flt3.

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG005735.
    InParanoidi Q00342.
    KOi K05092.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.

    Miscellaneous databases

    NextBioi 285583.
    PROi Q00342.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_FLT3.
    Genevestigatori Q00342.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    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. 2 hits.
    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. "A receptor tyrosine kinase specific to hematopoietic stem and progenitor cell-enriched populations."
      Matthews W., Jordan C.T., Wiegand G.W., Pardoll D., Lemischka I.R.
      Cell 65:1143-1152(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Murine Flt3, a gene encoding a novel tyrosine kinase receptor of the PDGFR/CSF1R family."
      Rosnet O., Marchetto S., Delapeyriere O., Birnbaum D.
      Oncogene 6:1641-1650(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Biochemical characterization and analysis of the transforming potential of the FLT3/FLK2 receptor tyrosine kinase."
      Maroc N., Rottapel R., Rosnet O., Marchetto S., Lavezzi C., Mannoni P., Birnbaum D., Dubreuil P.
      Oncogene 8:909-918(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    4. "Targeted disruption of the flk2/flt3 gene leads to deficiencies in primitive hematopoietic progenitors."
      Mackarehtschian K., Hardin J.D., Moore K.A., Boast S., Goff S.P., Lemischka I.R.
      Immunity 3:147-161(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    5. "Dramatic increase in the numbers of functionally mature dendritic cells in Flt3 ligand-treated mice: multiple dendritic cell subpopulations identified."
      Maraskovsky E., Brasel K., Teepe M., Roux E.R., Lyman S.D., Shortman K., McKenna H.J.
      J. Exp. Med. 184:1953-1962(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF DENDRITIC CELL DEVELOPMENT.
    6. "Fiz1, a novel zinc finger protein interacting with the receptor tyrosine kinase Flt3."
      Wolf I., Rohrschneider L.R.
      J. Biol. Chem. 274:21478-21484(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FIZ1, MUTAGENESIS OF LYS-645.
    7. "The receptor tyrosine kinase Flt3 is required for dendritic cell development in peripheral lymphoid tissues."
      Waskow C., Liu K., Darrasse-Jeze G., Guermonprez P., Ginhoux F., Merad M., Shengelia T., Yao K., Nussenzweig M.
      Nat. Immunol. 9:676-683(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: FUNCTION.
    9. "Flt3 permits survival during infection by rendering dendritic cells competent to activate NK cells."
      Eidenschenk C., Crozat K., Krebs P., Arens R., Popkin D., Arnold C.N., Blasius A.L., Benedict C.A., Moresco E.M., Xia Y., Beutler B.
      Proc. Natl. Acad. Sci. U.S.A. 107:9759-9764(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF DENDRITIC CELL DEVELOPMENT.
    10. "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, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, DOMAIN, ENZYME REGULATION.

    Entry informationi

    Entry nameiFLT3_MOUSE
    AccessioniPrimary (citable) accession number: Q00342
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3