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P36888

- FLT3_HUMAN

UniProt

P36888 - FLT3_HUMAN

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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

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 homodimerization activity Source: UniProtKB
  4. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB
  5. 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
Complete GO annotation...

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. endoplasmic reticulum Source: UniProtKB-KW
  2. external side of plasma membrane Source: Ensembl
  3. integral component of plasma membrane Source: ProtInc
Complete GO annotation...

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

BgeeiP36888.
CleanExiHS_FLT3.
ExpressionAtlasiP36888. baseline and differential.
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. Interacts with RNF115 and RNF126 (By similarity).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.
GeneTreeiENSGT00760000118923.
HOVERGENiHBG005735.
InParanoidiP36888.
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

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

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

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

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 DB08901. Ponatinib.
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.
GeneTreei ENSGT00760000118923.
HOVERGENi HBG005735.
InParanoidi P36888.
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

Bgeei P36888.
CleanExi HS_FLT3.
ExpressionAtlasi P36888. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 150 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