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Receptor-type tyrosine-protein kinase FLT3 (EC 2.7.10.1) (FL cytokine receptor) (Fetal liver kinase-2) (FLK-2) (Fms-like tyrosine kinase 3) (FLT-3) (Stem cell tyrosine kinase 1) (STK-1) (CD antigen CD135)

 FLT3_HUMAN              Reviewed;         993 AA.
P36888; A0AVG9; B7ZLT7; B7ZLT8; F5H0A0; Q13414;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
21-AUG-2007, sequence version 2.
22-NOV-2017, entry version 178.
RecName: Full=Receptor-type tyrosine-protein kinase FLT3;
EC=2.7.10.1;
AltName: Full=FL cytokine receptor;
AltName: Full=Fetal liver kinase-2;
Short=FLK-2;
AltName: Full=Fms-like tyrosine kinase 3;
Short=FLT-3;
AltName: Full=Stem cell tyrosine kinase 1;
Short=STK-1;
AltName: CD_antigen=CD135;
Flags: Precursor;
Name=FLT3; Synonyms=CD135, FLK2, STK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Bone marrow;
PubMed=7507245; DOI=10.1073/pnas.91.2.459;
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.;
"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.";
Proc. Natl. Acad. Sci. U.S.A. 91:459-463(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT MET-227.
TISSUE=Lymphocyte;
PubMed=8394751;
Rosnet O., Schiff C., Pebusque M.J., Marchetto S., Tonnelle C.,
Toiron Y., Birg F., Birnbaum D.;
"Human FLT3/FLK2 gene: cDNA cloning and expression in hematopoietic
cells.";
Blood 82:1110-1119(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
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.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-227.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
MET-227.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 783-942 (ISOFORM 1).
TISSUE=Testis;
PubMed=2004790; DOI=10.1016/0888-7543(91)90270-O;
Rosnet O., Mattei M.-G., Marchetto S., Birnbaum D.;
"Isolation and chromosomal localization of a novel FMS-like tyrosine
kinase gene.";
Genomics 9:380-385(1991).
[7]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=8637232;
Rosnet O., Buhring H.J., Marchetto S., Rappold I., Lavagna C.,
Sainty D., Arnoulet C., Chabannon C., Kanz L., Hannum C., Birnbaum D.;
"Human FLT3/FLK2 receptor tyrosine kinase is expressed at the surface
of normal and malignant hematopoietic cells.";
Leukemia 10:238-248(1996).
[8]
INVOLVEMENT IN AML.
PubMed=8946930;
Nakao M., Yokota S., Iwai T., Kaneko H., Horiike S., Kashima K.,
Sonoda Y., Fujimoto T., Misawa S.;
"Internal tandem duplication of the flt3 gene found in acute myeloid
leukemia.";
Leukemia 10:1911-1918(1996).
[9]
INVOLVEMENT IN AML, SUBUNIT, PHOSPHORYLATION, AND MUTAGENESIS OF
TYR-589 AND TYR-591.
PubMed=9737679; DOI=10.1038/sj.leu.2401130;
Kiyoi H., Towatari M., Yokota S., Hamaguchi M., Ohno R., Saito H.,
Naoe T.;
"Internal tandem duplication of the FLT3 gene is a novel modality of
elongation mutation which causes constitutive activation of the
product.";
Leukemia 12:1333-1337(1998).
[10]
FUNCTION IN PROMOTING PHOSPHORYLATION OF SHC1; PTPN6/SHP;
PTPN11/SHP-2; MAPK1/ERK2; MAPK3/ERK1, AUTOPHOSPHORYLATION, AND
INTERACTION WITH GRB2.
PubMed=10080542;
Zhang S., Mantel C., Broxmeyer H.E.;
"Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and
their association with Grb2 and Shc in Baf3/Flt3 cells.";
J. Leukoc. Biol. 65:372-380(1999).
[11]
FUNCTION IN ACTIVATION OF AKT1; MAPK1/ERK2; MAPK3/ERK1; STAT5A AND
STAT5B, PHOSPHORYLATION, FUNCTION IN ACTIVATION OF THE RAS PATHWAY,
AND INVOLVEMENT IN AML.
PubMed=11090077;
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.;
"Flt3 mutations from patients with acute myeloid leukemia induce
transformation of 32D cells mediated by the Ras and STAT5 pathways.";
Blood 96:3907-3914(2000).
[12]
FUNCTION IN ACTIVATION OF AKT1, AND INVOLVEMENT IN AML.
PubMed=16266983; DOI=10.1158/0008-5472.CAN-05-0422;
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.;
"Constitutive activation of Akt by Flt3 internal tandem duplications
is necessary for increased survival, proliferation, and myeloid
transformation.";
Cancer Res. 65:9643-9650(2005).
[13]
SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-591,
DEPHOSPHORYLATION BY PTPN1; PTPN6/SHP-1 AND PTPN12, PROTEASOMAL
DEGRADATION, GLYCOSYLATION, AND MUTAGENESIS OF LYS-644.
PubMed=15831474; DOI=10.1128/MCB.25.9.3690-3703.2005;
Schmidt-Arras D.E., Bohmer A., Markova B., Choudhary C., Serve H.,
Bohmer F.D.;
"Tyrosine phosphorylation regulates maturation of receptor tyrosine
kinases.";
Mol. Cell. Biol. 25:3690-3703(2005).
[14]
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, AND MUTAGENESIS OF TYR-589 AND TYR-591.
PubMed=16627759; DOI=10.1182/blood-2005-11-011429;
Rocnik J.L., Okabe R., Yu J.C., Lee B.H., Giese N., Schenkein D.P.,
Gilliland D.G.;
"Roles of tyrosine 589 and 591 in STAT5 activation and transformation
mediated by FLT3-ITD.";
Blood 108:1339-1345(2006).
[15]
INTERACTION WITH PTPN11/SHP2; LYN; FGR; HCK AND SRC,
AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-589 AND TYR-599, AND
PHOSPHORYLATION AT TYR-572; SER-574; TYR-589; TYR-591 AND TYR-599.
PubMed=16684964; DOI=10.1182/blood-2005-07-008896;
Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S.,
Ronnstrand L.;
"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.";
Blood 108:1542-1550(2006).
[16]
REGION INVOLVED IN REGULATION OF KINASE ACTIVITY, AUTOREGULATORY
DOMAIN, AND INVOLVEMENT IN AML.
PubMed=18305215; DOI=10.1182/blood-2008-01-117770;
Meshinchi S., Stirewalt D.L., Alonzo T.A., Boggon T.J., Gerbing R.B.,
Rocnik J.L., Lange B.J., Gilliland D.G., Radich J.P.;
"Structural and numerical variation of FLT3/ITD in pediatric AML.";
Blood 111:4930-4933(2008).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18490735; DOI=10.4049/jimmunol.180.11.7358;
Kikushige Y., Yoshimoto G., Miyamoto T., Iino T., Mori Y., Iwasaki H.,
Niiro H., Takenaka K., Nagafuji K., Harada M., Ishikawa F., Akashi K.;
"Human Flt3 is expressed at the hematopoietic stem cell and the
granulocyte/macrophage progenitor stages to maintain cell survival.";
J. Immunol. 180:7358-7367(2008).
[18]
PHOSPHORYLATION AT TYR-589; TYR-591; TYR-599; TYR-726; TYR-768;
TYR-793; TYR-842 AND TYR-955.
PubMed=19477218; DOI=10.1016/j.exphem.2009.05.008;
Razumovskaya E., Masson K., Khan R., Bengtsson S., Ronnstrand L.;
"Oncogenic Flt3 receptors display different specificity and kinetics
of autophosphorylation.";
Exp. Hematol. 37:979-989(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759 AND SER-993, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[20]
FUNCTION IN ACTIVATION OF FES AND FER, AND INTERACTION WITH FES AND
FER.
PubMed=20111072; DOI=10.1038/leu.2009.301;
Voisset E., Lopez S., Chaix A., Georges C., Hanssens K., Prebet T.,
Dubreuil P., De Sepulveda P.;
"FES kinases are required for oncogenic FLT3 signaling.";
Leukemia 24:721-728(2010).
[21]
UBIQUITINATION.
PubMed=20508617; DOI=10.1038/leu.2010.114;
Buchwald M., Pietschmann K., Muller J.P., Bohmer F.D., Heinzel T.,
Kramer O.H.;
"Ubiquitin conjugase UBCH8 targets active FMS-like tyrosine kinase 3
for proteasomal degradation.";
Leukemia 24:1412-1421(2010).
[22]
FUNCTION.
PubMed=21067588; DOI=10.1186/1476-4598-9-292;
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.;
"mTOR signaling is activated by FLT3 kinase and promotes survival of
FLT3-mutated acute myeloid leukemia cells.";
Mol. Cancer 9:292-292(2010).
[23]
INTERACTION WITH PTPRJ/DEP1, FUNCTION IN ACTIVATION OF MAPK1/ERK2;
MAPK3/ERK1; PLCG1; STAT5A AND/OR STAT5B, GLYCOSYLATION,
UBIQUITINATION, AND PHOSPHORYLATION AT TYR-572; TYR-589; TYR-591;
TYR-599; TYR-768; TYR-793; TYR-842 AND TYR-955.
PubMed=21262971; DOI=10.1074/jbc.M110.205021;
Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K.,
Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D.,
Muller J.P.;
"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase
FLT3 signaling.";
J. Biol. Chem. 286:10918-10929(2011).
[24]
FUNCTION, AND ENZYME REGULATION.
PubMed=21516120; DOI=10.1038/onc.2011.110;
Zheng R., Bailey E., Nguyen B., Yang X., Piloto O., Levis M.,
Small D.;
"Further activation of FLT3 mutants by FLT3 ligand.";
Oncogene 30:4004-4014(2011).
[25]
REVIEW.
PubMed=12951584; DOI=10.1038/nrc1169;
Stirewalt D.L., Radich J.P.;
"The role of FLT3 in haematopoietic malignancies.";
Nat. Rev. Cancer 3:650-665(2003).
[26]
REVIEW.
PubMed=19549778; DOI=10.1158/1078-0432.CCR-08-1123;
Meshinchi S., Appelbaum F.R.;
"Structural and functional alterations of FLT3 in acute myeloid
leukemia.";
Clin. Cancer Res. 15:4263-4269(2009).
[27]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 564-958, AND ENZYME
REGULATION.
PubMed=14759363; DOI=10.1016/S1097-2765(03)00505-7;
Griffith J., Black J., Faerman C., Swenson L., Wynn M., Lu F.,
Lippke J., Saxena K.;
"The structural basis for autoinhibition of FLT3 by the juxtamembrane
domain.";
Mol. Cell 13:169-178(2004).
[28]
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, AND DISULFIDE BONDS.
PubMed=21389326; DOI=10.1182/blood-2011-01-329532;
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.;
"Structural insights into the extracellular assembly of the
hematopoietic Flt3 signaling complex.";
Blood 118:60-68(2011).
[29]
VARIANTS TYR-835 DEL; HIS-835 AND TYR-835, AND INVOLVEMENT IN AML.
PubMed=11442493; DOI=10.1046/j.1365-2141.2001.02850.x;
Abu-Duhier F.M., Goodeve A.C., Wilson G.A., Care R.S., Peake I.R.,
Reilly J.T.;
"Identification of novel FLT-3 Asp835 mutations in adult acute myeloid
leukaemia.";
Br. J. Haematol. 113:983-988(2001).
[30]
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, AND INVOLVEMENT IN AML.
PubMed=11290608; DOI=10.1182/blood.V97.8.2434;
Yamamoto Y., Kiyoi H., Nakano Y., Suzuki R., Kodera Y., Miyawaki S.,
Asou N., Kuriyama K., Yagasaki F., Shimazaki C., Akiyama H., Saito K.,
Nishimura M., Motoji T., Shinagawa K., Takeshita A., Saito H.,
Ueda R., Ohno R., Naoe T.;
"Activating mutation of D835 within the activation loop of FLT3 in
human hematologic malignancies.";
Blood 97:2434-2439(2001).
[31]
VARIANTS GLU-835; HIS-835; TYR-835; ILE-836 DEL AND MET-836, FUNCTION
IN ACTIVATION OF STAT5A AND/OR STAT5B, PHOSPHORYLATION, AND
INVOLVEMENT IN AML.
PubMed=14504097; DOI=10.1182/blood-2003-02-0418;
Taketani T., Taki T., Sugita K., Furuichi Y., Ishii E., Hanada R.,
Tsuchida M., Sugita K., Ida K., Hayashi Y.;
"FLT3 mutations in the activation loop of tyrosine kinase domain are
frequently found in infant ALL with MLL rearrangements and pediatric
ALL with hyperdiploidy.";
Blood 103:1085-1088(2004).
[32]
VARIANTS [LARGE SCALE ANALYSIS] ALA-158; MET-227; ASN-324; VAL-358 AND
ILE-557.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[33]
VARIANT [LARGE SCALE ANALYSIS] MET-194.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
-!- FUNCTION: 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.
{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}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:15831474}.
-!- ENZYME 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}.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:Q00342, ECO:0000269|PubMed:10080542,
ECO:0000269|PubMed:16684964, ECO:0000269|PubMed:20111072,
ECO:0000269|PubMed:21262971, ECO:0000269|PubMed:21389326,
ECO:0000269|PubMed:9737679}.
-!- INTERACTION:
Q9Y6K9:IKBKG; NbExp=2; IntAct=EBI-3946257, EBI-81279;
P27986:PIK3R1; NbExp=2; IntAct=EBI-3946257, EBI-79464;
Q12913:PTPRJ; NbExp=3; IntAct=EBI-3946257, EBI-2264500;
P43405:SYK; NbExp=21; IntAct=EBI-3946257, EBI-78302;
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P36888-1; Sequence=Displayed;
Name=2;
IsoId=P36888-2; Sequence=VSP_041796;
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:18490735, ECO:0000269|PubMed:7507245,
ECO:0000269|PubMed:8394751, ECO:0000269|PubMed:8637232}.
-!- DOMAIN: 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.
-!- 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}.
-!- 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.
-!- MISCELLANEOUS: Can be used as diagnostic tool to establish the
exact cause of acute myeloid leukemia, and to determine the
optimal therapy.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FLT3ID144.html";
-----------------------------------------------------------------------
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EMBL; U02687; AAA18947.1; -; mRNA.
EMBL; Z26652; CAA81393.1; -; mRNA.
EMBL; AL356915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL445262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL591024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08424.1; -; Genomic_DNA.
EMBL; BC126350; AAI26351.1; -; mRNA.
EMBL; BC144039; AAI44040.1; -; mRNA.
EMBL; BC144040; AAI44041.1; -; mRNA.
EMBL; L36162; AAA35487.1; -; mRNA.
CCDS; CCDS31953.1; -. [P36888-1]
PIR; A36873; A36873.
PIR; A39061; A39061.
RefSeq; NP_004110.2; NM_004119.2. [P36888-1]
UniGene; Hs.507590; -.
PDB; 1RJB; X-ray; 2.10 A; A=564-907.
PDB; 3QS7; X-ray; 4.30 A; E/F/G/H=27-436.
PDB; 3QS9; X-ray; 7.80 A; E/F/G/H=27-540.
PDB; 4RT7; X-ray; 3.10 A; A=564-958.
PDB; 4XUF; X-ray; 3.20 A; A/B=600-947.
PDBsum; 1RJB; -.
PDBsum; 3QS7; -.
PDBsum; 3QS9; -.
PDBsum; 4RT7; -.
PDBsum; 4XUF; -.
ProteinModelPortal; P36888; -.
SMR; P36888; -.
BioGrid; 108610; 13.
DIP; DIP-59769N; -.
IntAct; P36888; 6.
MINT; MINT-7103562; -.
STRING; 9606.ENSP00000241453; -.
BindingDB; P36888; -.
ChEMBL; CHEMBL1974; -.
DrugBank; DB06080; ABT-869.
DrugBank; DB05213; AC220.
DrugBank; DB05465; MLN-518.
DrugBank; DB05216; MP470.
DrugBank; DB09079; Nintedanib.
DrugBank; DB08901; Ponatinib.
DrugBank; DB00398; Sorafenib.
DrugBank; DB01268; Sunitinib.
DrugBank; DB05014; XL999.
GuidetoPHARMACOLOGY; 1807; -.
iPTMnet; P36888; -.
PhosphoSitePlus; P36888; -.
BioMuta; FLT3; -.
DMDM; 156630887; -.
MaxQB; P36888; -.
PaxDb; P36888; -.
PeptideAtlas; P36888; -.
PRIDE; P36888; -.
Ensembl; ENST00000241453; ENSP00000241453; ENSG00000122025. [P36888-1]
GeneID; 2322; -.
KEGG; hsa:2322; -.
UCSC; uc001urw.3; human. [P36888-1]
CTD; 2322; -.
DisGeNET; 2322; -.
EuPathDB; HostDB:ENSG00000122025.14; -.
GeneCards; FLT3; -.
H-InvDB; HIX0037338; -.
HGNC; HGNC:3765; FLT3.
HPA; HPA047539; -.
MalaCards; FLT3; -.
MIM; 136351; gene.
MIM; 601626; phenotype.
neXtProt; NX_P36888; -.
OpenTargets; ENSG00000122025; -.
Orphanet; 98829; 'Acute myeloid leukemia with abnormal bone marrow eosinophils inv(16)(p13q22) or t(16;16)(p13;q22)'.
Orphanet; 102724; 'Acute myeloid leukemia with t(8;21)(q22;q22) translocation'.
Orphanet; 98837; Acute biphenotypic leukemia.
Orphanet; 98834; Acute myeloblastic leukemia with maturation.
Orphanet; 98833; Acute myeloblastic leukemia without maturation.
Orphanet; 98832; Minimally differentiated acute myeloblastic leukemia.
Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
PharmGKB; PA28181; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOVERGEN; HBG005735; -.
InParanoid; P36888; -.
KO; K05092; -.
OMA; FHRTWTE; -.
OrthoDB; EOG091G01TL; -.
PhylomeDB; P36888; -.
TreeFam; TF325768; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-449836; Other interleukin signaling.
SignaLink; P36888; -.
SIGNOR; P36888; -.
EvolutionaryTrace; P36888; -.
GeneWiki; CD135; -.
GenomeRNAi; 2322; -.
PRO; PR:P36888; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000122025; -.
CleanEx; HS_FLT3; -.
ExpressionAtlas; P36888; baseline and differential.
Genevisible; P36888; HS.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004896; F:cytokine receptor activity; ISS:UniProtKB.
GO; GO:0035259; F:glucocorticoid receptor binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
GO; GO:0043621; F:protein self-association; IMP:CAFA.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:UniProtKB.
GO; GO:0005021; F:vascular endothelial growth factor-activated receptor activity; TAS:ProtInc.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEA:Ensembl.
GO; GO:0035726; P:common myeloid progenitor cell proliferation; ISS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0097028; P:dendritic cell differentiation; ISS:UniProtKB.
GO; GO:0030097; P:hemopoiesis; IDA:MGI.
GO; GO:0001776; P:leukocyte homeostasis; ISS:UniProtKB.
GO; GO:0046651; P:lymphocyte proliferation; ISS:UniProtKB.
GO; GO:0002318; P:myeloid progenitor cell differentiation; ISS:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; TAS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:UniProtKB.
GO; GO:0043406; P:positive regulation of MAP kinase activity; TAS:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; TAS:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; TAS:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; TAS:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; TAS:UniProtKB.
GO; GO:0002328; P:pro-B cell differentiation; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; TAS:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR030118; FLT3.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
PANTHER; PTHR24416:SF356; PTHR24416:SF356; 1.
Pfam; PF00047; ig; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Disease mutation; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Polymorphism; Proto-oncogene; Receptor;
Reference proteome; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 993 Receptor-type tyrosine-protein kinase
FLT3.
/FTId=PRO_0000016778.
TOPO_DOM 27 543 Extracellular. {ECO:0000255}.
TRANSMEM 544 563 Helical. {ECO:0000255}.
TOPO_DOM 564 993 Cytoplasmic. {ECO:0000255}.
DOMAIN 253 343 Ig-like C2-type.
DOMAIN 610 943 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 616 624 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 591 597 Important for normal regulation of the
kinase activity and for maintaining the
kinase in an inactive state in the
absence of bound ligand.
ACT_SITE 811 811 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 644 644 ATP. {ECO:0000305}.
MOD_RES 572 572 Phosphotyrosine.
{ECO:0000269|PubMed:16684964,
ECO:0000269|PubMed:21262971}.
MOD_RES 574 574 Phosphoserine.
{ECO:0000269|PubMed:16684964}.
MOD_RES 589 589 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16684964,
ECO:0000269|PubMed:19477218,
ECO:0000269|PubMed:21262971}.
MOD_RES 591 591 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:15831474,
ECO:0000269|PubMed:16627759,
ECO:0000269|PubMed:16684964,
ECO:0000269|PubMed:19477218,
ECO:0000269|PubMed:21262971}.
MOD_RES 599 599 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16684964,
ECO:0000269|PubMed:19477218,
ECO:0000269|PubMed:21262971}.
MOD_RES 726 726 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16627759,
ECO:0000269|PubMed:19477218}.
MOD_RES 759 759 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 768 768 Phosphotyrosine.
{ECO:0000269|PubMed:19477218,
ECO:0000269|PubMed:21262971}.
MOD_RES 793 793 Phosphotyrosine.
{ECO:0000269|PubMed:19477218,
ECO:0000269|PubMed:21262971}.
MOD_RES 842 842 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16627759,
ECO:0000269|PubMed:19477218,
ECO:0000269|PubMed:21262971}.
MOD_RES 955 955 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16627759,
ECO:0000269|PubMed:19477218,
ECO:0000269|PubMed:21262971}.
MOD_RES 969 969 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16627759}.
MOD_RES 993 993 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21389326}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21389326}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21389326}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21389326}.
CARBOHYD 323 323 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21389326}.
CARBOHYD 351 351 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21389326}.
CARBOHYD 354 354 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21389326}.
CARBOHYD 473 473 N-linked (GlcNAc...) asparagine.
CARBOHYD 502 502 N-linked (GlcNAc...) asparagine.
CARBOHYD 541 541 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 65 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21389326}.
DISULFID 103 114 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21389326}.
DISULFID 199 206 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21389326}.
DISULFID 232 241 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21389326}.
DISULFID 272 330 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21389326}.
DISULFID 368 407 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21389326}.
DISULFID 381 392 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21389326}.
VAR_SEQ 807 847 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041796.
VARIANT 7 7 D -> G (in dbSNP:rs12872889).
/FTId=VAR_034677.
VARIANT 158 158 V -> A (in dbSNP:rs56321896).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042069.
VARIANT 194 194 V -> M (in dbSNP:rs146030737).
{ECO:0000269|PubMed:18987736}.
/FTId=VAR_054149.
VARIANT 227 227 T -> M (in dbSNP:rs1933437).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8394751,
ECO:0000269|Ref.4}.
/FTId=VAR_034678.
VARIANT 324 324 D -> N (in dbSNP:rs35602083).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042070.
VARIANT 358 358 D -> V (in dbSNP:rs34172843).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042071.
VARIANT 417 417 I -> L (in dbSNP:rs56090538).
/FTId=VAR_061291.
VARIANT 557 557 V -> I (in dbSNP:rs35958982).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042072.
VARIANT 835 835 D -> E (in acute lymphoblastic leukemia
patients and acute myelogenous leukemia
patients; somatic mutation;
constitutively activated;
dbSNP:rs121913487).
{ECO:0000269|PubMed:11290608,
ECO:0000269|PubMed:14504097}.
/FTId=VAR_065679.
VARIANT 835 835 D -> H (in acute lymphoblastic leukemia
patients and in acute myelogenous
leukemia patients; somatic mutation;
constitutively activated;
dbSNP:rs121913488).
{ECO:0000269|PubMed:11290608,
ECO:0000269|PubMed:11442493,
ECO:0000269|PubMed:14504097}.
/FTId=VAR_065680.
VARIANT 835 835 D -> N (in acute lymphoblastic leukemia
patients and in acute myelogenous
leukemia patients; somatic mutation;
constitutively activated;
dbSNP:rs121913488).
{ECO:0000269|PubMed:11290608}.
/FTId=VAR_065681.
VARIANT 835 835 D -> V (in acute lymphoblastic leukemia
patients and in acute myelogenous
leukemia patients; somatic mutation;
constitutively activated;
dbSNP:rs121909646).
{ECO:0000269|PubMed:11290608}.
/FTId=VAR_065682.
VARIANT 835 835 D -> Y (in acute lymphoblastic leukemia
patients and in acute myelogenous
leukemia patients; somatic mutation;
constitutively activated;
dbSNP:rs121913488).
{ECO:0000269|PubMed:11290608,
ECO:0000269|PubMed:11442493,
ECO:0000269|PubMed:14504097}.
/FTId=VAR_065683.
VARIANT 836 836 I -> M (in acute lymphoblastic leukemia
patients; somatic mutation;
dbSNP:rs121913232).
{ECO:0000269|PubMed:14504097}.
/FTId=VAR_065684.
MUTAGEN 589 589 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. {ECO:0000269|PubMed:16627759,
ECO:0000269|PubMed:16684964,
ECO:0000269|PubMed:9737679}.
MUTAGEN 591 591 Y->F: No significant effect on tyrosine
phosphorylation. Abolishes activation of
STAT5A. {ECO:0000269|PubMed:16627759,
ECO:0000269|PubMed:9737679}.
MUTAGEN 599 599 Y->F: Abolishes interaction with
PTPN11/SHP2 and phosphorylation of
PTPN11/SHP2.
{ECO:0000269|PubMed:16684964}.
MUTAGEN 644 644 K->A: Abolishes kinase activity.
{ECO:0000269|PubMed:15831474}.
CONFLICT 8 8 G -> A (in Ref. 1; AAA18947).
{ECO:0000305}.
CONFLICT 10 11 QL -> TV (in Ref. 1; AAA18947).
{ECO:0000305}.
CONFLICT 71 71 S -> N (in Ref. 5; AAI44040).
{ECO:0000305}.
CONFLICT 78 78 A -> R (in Ref. 2; CAA81393).
{ECO:0000305}.
CONFLICT 346 346 E -> G (in Ref. 1; AAA18947).
{ECO:0000305}.
CONFLICT 940 940 T -> H (in Ref. 6; AAA35487).
{ECO:0000305}.
STRAND 575 581 {ECO:0000244|PDB:1RJB}.
STRAND 583 585 {ECO:0000244|PDB:1RJB}.
STRAND 589 591 {ECO:0000244|PDB:1RJB}.
HELIX 594 596 {ECO:0000244|PDB:1RJB}.
HELIX 601 603 {ECO:0000244|PDB:1RJB}.
HELIX 607 609 {ECO:0000244|PDB:1RJB}.
STRAND 610 618 {ECO:0000244|PDB:1RJB}.
STRAND 620 631 {ECO:0000244|PDB:1RJB}.
STRAND 633 636 {ECO:0000244|PDB:1RJB}.
STRAND 638 646 {ECO:0000244|PDB:1RJB}.
HELIX 656 668 {ECO:0000244|PDB:1RJB}.
STRAND 677 681 {ECO:0000244|PDB:1RJB}.
STRAND 683 686 {ECO:0000244|PDB:1RJB}.
STRAND 688 692 {ECO:0000244|PDB:1RJB}.
HELIX 699 704 {ECO:0000244|PDB:1RJB}.
TURN 705 708 {ECO:0000244|PDB:1RJB}.
HELIX 785 804 {ECO:0000244|PDB:1RJB}.
STRAND 807 809 {ECO:0000244|PDB:1RJB}.
HELIX 814 816 {ECO:0000244|PDB:1RJB}.
STRAND 817 820 {ECO:0000244|PDB:1RJB}.
TURN 821 823 {ECO:0000244|PDB:1RJB}.
STRAND 824 827 {ECO:0000244|PDB:1RJB}.
HELIX 831 833 {ECO:0000244|PDB:1RJB}.
HELIX 836 838 {ECO:0000244|PDB:1RJB}.
STRAND 842 845 {ECO:0000244|PDB:1RJB}.
STRAND 848 850 {ECO:0000244|PDB:1RJB}.
HELIX 852 854 {ECO:0000244|PDB:1RJB}.
HELIX 857 862 {ECO:0000244|PDB:1RJB}.
HELIX 867 881 {ECO:0000244|PDB:1RJB}.
TURN 882 884 {ECO:0000244|PDB:1RJB}.
HELIX 896 903 {ECO:0000244|PDB:1RJB}.
HELIX 916 924 {ECO:0000244|PDB:4RT7}.
HELIX 930 932 {ECO:0000244|PDB:4RT7}.
HELIX 936 949 {ECO:0000244|PDB:4RT7}.
SEQUENCE 993 AA; 112903 MW; 6C1995718F352ECE CRC64;
MPALARDGGQ LPLLVVFSAM IFGTITNQDL PVIKCVLINH KNNDSSVGKS SSYPMVSESP
EDLGCALRPQ SSGTVYEAAA VEVDVSASIT LQVLVDAPGN ISCLWVFKHS SLNCQPHFDL
QNRGVVSMVI LKMTETQAGE YLLFIQSEAT NYTILFTVSI RNTLLYTLRR PYFRKMENQD
ALVCISESVP EPIVEWVLCD SQGESCKEES PAVVKKEEKV LHELFGTDIR CCARNELGRE
CTRLFTIDLN QTPQTTLPQL FLKVGEPLWI RCKAVHVNHG FGLTWELENK ALEEGNYFEM
STYSTNRTMI RILFAFVSSV ARNDTGYYTC SSSKHPSQSA LVTIVEKGFI NATNSSEDYE
IDQYEEFCFS VRFKAYPQIR CTWTFSRKSF PCEQKGLDNG YSISKFCNHK HQPGEYIFHA
ENDDAQFTKM FTLNIRRKPQ VLAEASASQA SCFSDGYPLP SWTWKKCSDK SPNCTEEITE
GVWNRKANRK VFGQWVSSST LNMSEAIKGF LVKCCAYNSL GTSCETILLN SPGPFPFIQD
NISFYATIGV CLLFIVVLTL LICHKYKKQF RYESQLQMVQ VTGSSDNEYF YVDFREYEYD
LKWEFPRENL EFGKVLGSGA FGKVMNATAY GISKTGVSIQ VAVKMLKEKA DSSEREALMS
ELKMMTQLGS HENIVNLLGA CTLSGPIYLI FEYCCYGDLL NYLRSKREKF HRTWTEIFKE
HNFSFYPTFQ SHPNSSMPGS REVQIHPDSD QISGLHGNSF HSEDEIEYEN QKRLEEEEDL
NVLTFEDLLC FAYQVAKGME FLEFKSCVHR DLAARNVLVT HGKVVKICDF GLARDIMSDS
NYVVRGNARL PVKWMAPESL FEGIYTIKSD VWSYGILLWE IFSLGVNPYP GIPVDANFYK
LIQNGFKMDQ PFYATEEIYI IMQSCWAFDS RKRPSFPNLT SFLGCQLADA EEAMYQNVDG
RVSECPHTYQ NRRPFSREMD LGLLSPQAQV EDS


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