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UniProtKB - P36888 (FLT3_HUMAN)

Entry version 189 (13 Feb 2019)
Sequence version 2 (21 Aug 2007)
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Protein

Receptor-type tyrosine-protein kinase FLT3

Gene

FLT3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Tyrosine-protein kinase that acts as cell-surface receptor for the cytokine FLT3LG and regulates differentiation, proliferation and survival of hematopoietic progenitor cells and of dendritic cells. Promotes phosphorylation of SHC1 and AKT1, and activation of the downstream effector MTOR. Promotes activation of RAS signaling and phosphorylation of downstream kinases, including MAPK1/ERK2 and/or MAPK3/ERK1. Promotes phosphorylation of FES, FER, PTPN6/SHP, PTPN11/SHP-2, PLCG1, and STAT5A and/or STAT5B. Activation of wild-type FLT3 causes only marginal activation of STAT5A or STAT5B. Mutations that cause constitutive kinase activity promote cell proliferation and resistance to apoptosis via the activation of multiple signaling pathways.11 Publications

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei644ATPCurated1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei811Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi616 – 624ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.10.1 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-109704 PI3K Cascade
R-HSA-449836 Other interleukin signaling
R-HSA-5673001 RAF/MAP kinase cascade

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P36888

SIGNOR Signaling Network Open Resource

More...SIGNORi		P36888

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FLT3
Synonyms:CD135, FLK2, STK1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000122025.14

Human Gene Nomenclature Database

More...HGNCi		HGNC:3765 FLT3

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		136351 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P36888

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini27 – 543ExtracellularSequence analysisAdd BLAST517
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei544 – 563HelicalSequence analysisAdd BLAST20
Topological domaini564 – 993CytoplasmicSequence analysisAdd BLAST430

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Leukemia, acute myelogenous (AML)8 Publications
The gene represented in this entry may be involved in disease pathogenesis. Somatic mutations that lead to constitutive activation of FLT3 are frequent in AML patients. These mutations fall into two classes, the most common being in-frame internal tandem duplications of variable length in the juxtamembrane region that disrupt the normal regulation of the kinase activity. Likewise, point mutations in the activation loop of the kinase domain can result in a constitutively activated kinase.
Disease descriptionA subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes.
See also OMIM:601626

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi589Y → F: Reduced phosphorylation of the wild-type kinase in response to ligand binding. No effect on the phosphorylation of the constitutively activated mutant kinase variants. Abolishes activation of STAT5A. 3 Publications1
Mutagenesisi591Y → F: No significant effect on tyrosine phosphorylation. Abolishes activation of STAT5A. 2 Publications1
Mutagenesisi599Y → F: Abolishes interaction with PTPN11/SHP2 and phosphorylation of PTPN11/SHP2. 1 Publication1
Mutagenesisi644K → A: Abolishes kinase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		2322

MalaCards human disease database

More...MalaCardsi		FLT3
MIMi601626 phenotype

Open Targets

More...OpenTargetsi		ENSG00000122025

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...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)
98832 Acute myeloid leukemia with minimal differentiation
102724 Acute myeloid leukemia with t(8;21)(q22;q22) translocation
99860 Precursor B-cell acute lymphoblastic leukemia
99861 Precursor T-cell acute lymphoblastic leukemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28181

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1974

Drug and drug target database

More...DrugBanki		DB06080 ABT-869
DB05213 AC220
DB05465 MLN-518
DB05216 MP470
DB09079 Nintedanib
DB08901 Ponatinib
DB00398 Sorafenib
DB01268 Sunitinib
DB05014 XL999

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1807

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		FLT3

Domain mapping of disease mutations (DMDM)

More...DMDMi		156630887

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 26Sequence analysisAdd BLAST26
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001677827 – 993Receptor-type tyrosine-protein kinase FLT3Add BLAST967

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi35 ↔ 65PROSITE-ProRule annotation1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi43N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi100N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi103 ↔ 114PROSITE-ProRule annotation1 Publication
Glycosylationi151N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi199 ↔ 206PROSITE-ProRule annotation1 Publication
Disulfide bondi232 ↔ 241PROSITE-ProRule annotation1 Publication
Disulfide bondi272 ↔ 330PROSITE-ProRule annotation1 Publication
Glycosylationi306N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi323N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi351N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi354N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi368 ↔ 407PROSITE-ProRule annotation1 Publication
Disulfide bondi381 ↔ 392PROSITE-ProRule annotation1 Publication
Glycosylationi473N-linked (GlcNAc...) asparagine1
Glycosylationi502N-linked (GlcNAc...) asparagine1
Glycosylationi541N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei572Phosphotyrosine2 Publications1
Modified residuei574Phosphoserine1 Publication1
Modified residuei589Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei591Phosphotyrosine; by autocatalysis5 Publications1
Modified residuei599Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei726Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei759PhosphoserineCombined sources1
Modified residuei768Phosphotyrosine2 Publications1
Modified residuei793Phosphotyrosine2 Publications1
Modified residuei842Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei955Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei969Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei993PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P36888

MaxQB - The MaxQuant DataBase

More...MaxQBi		P36888

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P36888

PeptideAtlas

More...PeptideAtlasi		P36888

PRoteomics IDEntifications database

More...PRIDEi		P36888

ProteomicsDB human proteome resource

More...ProteomicsDBi		55226
55227 [P36888-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P36888

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P36888

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000122025 Expressed in 100 organ(s), highest expression level in cerebellar hemisphere

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P36888 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P36888 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA047539

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		108610, 14 interactors

Database of interacting proteins

More...DIPi		DIP-59769N

Protein interaction database and analysis system

More...IntActi		P36888, 24 interactors

Molecular INTeraction database

More...MINTi		P36888

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000241453

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P36888

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RJBX-ray2.10A564-958[»]
3QS7X-ray4.30E/F/G/H27-436[»]
3QS9X-ray7.80E/F/G/H27-540[»]
4RT7X-ray3.10A564-958[»]
4XUFX-ray3.20A/B600-947[»]
5X02X-ray2.40A564-958[»]
6IL3X-ray2.50A564-958[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P36888

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P36888

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P36888

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini253 – 343Ig-like C2-typeAdd BLAST91
Domaini610 – 943Protein kinasePROSITE-ProRule annotationAdd BLAST334

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni591 – 597Important for normal regulation of the kinase activity and for maintaining the kinase in an inactive state in the absence of bound ligand7

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0200 Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160575

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG005735

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P36888

KEGG Orthology (KO)

More...KOi		K05092

Identification of Orthologs from Complete Genome Data

More...OMAi		YFYIDFR

Database of Orthologous Groups

More...OrthoDBi		236292at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P36888

TreeFam database of animal gene trees

More...TreeFami		TF325768

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR030118 FLT3
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013151 Immunoglobulin
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR001824 Tyr_kinase_rcpt_3_CS

The PANTHER Classification System

More...PANTHERi		PTHR24416:SF356 PTHR24416:SF356, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48726 SSF48726, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50835 IG_LIKE, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS00240 RECEPTOR_TYR_KIN_III, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

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

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

« Hide
        10         20         30         40         50
MPALARDGGQ LPLLVVFSAM IFGTITNQDL PVIKCVLINH KNNDSSVGKS 
        60         70         80         90        100
SSYPMVSESP EDLGCALRPQ SSGTVYEAAA VEVDVSASIT LQVLVDAPGN 
       110        120        130        140        150
ISCLWVFKHS SLNCQPHFDL QNRGVVSMVI LKMTETQAGE YLLFIQSEAT 
       160        170        180        190        200
NYTILFTVSI RNTLLYTLRR PYFRKMENQD ALVCISESVP EPIVEWVLCD 
       210        220        230        240        250
SQGESCKEES PAVVKKEEKV LHELFGTDIR CCARNELGRE CTRLFTIDLN 
       260        270        280        290        300
QTPQTTLPQL FLKVGEPLWI RCKAVHVNHG FGLTWELENK ALEEGNYFEM 
       310        320        330        340        350
STYSTNRTMI RILFAFVSSV ARNDTGYYTC SSSKHPSQSA LVTIVEKGFI 
       360        370        380        390        400
NATNSSEDYE IDQYEEFCFS VRFKAYPQIR CTWTFSRKSF PCEQKGLDNG 
       410        420        430        440        450
YSISKFCNHK HQPGEYIFHA ENDDAQFTKM FTLNIRRKPQ VLAEASASQA 
       460        470        480        490        500
SCFSDGYPLP SWTWKKCSDK SPNCTEEITE GVWNRKANRK VFGQWVSSST 
       510        520        530        540        550
LNMSEAIKGF LVKCCAYNSL GTSCETILLN SPGPFPFIQD NISFYATIGV 
       560        570        580        590        600
CLLFIVVLTL LICHKYKKQF RYESQLQMVQ VTGSSDNEYF YVDFREYEYD 
       610        620        630        640        650
LKWEFPRENL EFGKVLGSGA FGKVMNATAY GISKTGVSIQ VAVKMLKEKA 
       660        670        680        690        700
DSSEREALMS ELKMMTQLGS HENIVNLLGA CTLSGPIYLI FEYCCYGDLL 
       710        720        730        740        750
NYLRSKREKF HRTWTEIFKE HNFSFYPTFQ SHPNSSMPGS REVQIHPDSD 
       760        770        780        790        800
QISGLHGNSF HSEDEIEYEN QKRLEEEEDL NVLTFEDLLC FAYQVAKGME 
       810        820        830        840        850
FLEFKSCVHR DLAARNVLVT HGKVVKICDF GLARDIMSDS NYVVRGNARL 
       860        870        880        890        900
PVKWMAPESL FEGIYTIKSD VWSYGILLWE IFSLGVNPYP GIPVDANFYK 
       910        920        930        940        950
LIQNGFKMDQ PFYATEEIYI IMQSCWAFDS RKRPSFPNLT SFLGCQLADA 
       960        970        980        990 
EEAMYQNVDG RVSECPHTYQ NRRPFSREMD LGLLSPQAQV EDS
Length:993
Mass (Da):112,903
Last modified:August 21, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

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

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti8G → A in AAA18947 (PubMed:7507245).Curated1
Sequence conflicti10 – 11QL → TV in AAA18947 (PubMed:7507245).Curated2
Sequence conflicti71S → N in AAI44040 (PubMed:15489334).Curated1
Sequence conflicti78A → R in CAA81393 (PubMed:8394751).Curated1
Sequence conflicti346E → G in AAA18947 (PubMed:7507245).Curated1
Sequence conflicti940T → H in AAA35487 (PubMed:2004790).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_0346777D → G. Corresponds to variant dbSNP:rs12872889Ensembl.1
Natural variantiVAR_042069158V → A1 PublicationCorresponds to variant dbSNP:rs56321896Ensembl.1
Natural variantiVAR_054149194V → M1 PublicationCorresponds to variant dbSNP:rs146030737EnsemblClinVar.1
Natural variantiVAR_034678227T → M4 PublicationsCorresponds to variant dbSNP:rs1933437EnsemblClinVar.1
Natural variantiVAR_042070324D → N1 PublicationCorresponds to variant dbSNP:rs35602083EnsemblClinVar.1
Natural variantiVAR_042071358D → V1 PublicationCorresponds to variant dbSNP:rs34172843EnsemblClinVar.1
Natural variantiVAR_061291417I → L. Corresponds to variant dbSNP:rs56090538EnsemblClinVar.1
Natural variantiVAR_042072557V → I1 PublicationCorresponds to variant dbSNP:rs35958982EnsemblClinVar.1
Natural variantiVAR_065679835D → E in acute lymphoblastic leukemia patients and acute myelogenous leukemia patients; somatic mutation; constitutively activated. 2 PublicationsCorresponds to variant dbSNP:rs121913487EnsemblClinVar.1
Natural variantiVAR_065680835D → H in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 3 PublicationsCorresponds to variant dbSNP:rs121913488EnsemblClinVar.1
Natural variantiVAR_065681835D → N in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 1 PublicationCorresponds to variant dbSNP:rs121913488EnsemblClinVar.1
Natural variantiVAR_065682835D → V in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 1 PublicationCorresponds to variant dbSNP:rs121909646EnsemblClinVar.1
Natural variantiVAR_065683835D → Y in acute lymphoblastic leukemia patients and in acute myelogenous leukemia patients; somatic mutation; constitutively activated. 3 PublicationsCorresponds to variant dbSNP:rs121913488EnsemblClinVar.1
Natural variantiVAR_065684836I → M in acute lymphoblastic leukemia patients; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913232EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041796807 – 847Missing in isoform 2. 1 PublicationAdd BLAST41

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U02687 mRNA Translation: AAA18947.1
Z26652 mRNA Translation: CAA81393.1
AL356915 Genomic DNA No translation available.
AL445262 Genomic DNA No translation available.
AL591024 Genomic DNA No translation available.
CH471075 Genomic DNA Translation: EAX08424.1
BC126350 mRNA Translation: AAI26351.1
BC144039 mRNA Translation: AAI44040.1
BC144040 mRNA Translation: AAI44041.1
L36162 mRNA Translation: AAA35487.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS31953.1 [P36888-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A36873
A39061

NCBI Reference Sequences

More...RefSeqi		NP_004110.2, NM_004119.2 [P36888-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.507590

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000241453; ENSP00000241453; ENSG00000122025 [P36888-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2322

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2322

UCSC genome browser

More...UCSCi		uc001urw.3 human [P36888-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RJBX-ray2.10A564-958[»]
3QS7X-ray4.30E/F/G/H27-436[»]
3QS9X-ray7.80E/F/G/H27-540[»]
4RT7X-ray3.10A564-958[»]
4XUFX-ray3.20A/B600-947[»]
5X02X-ray2.40A564-958[»]
6IL3X-ray2.50A564-958[»]
ProteinModelPortaliP36888
SMRiP36888
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108610, 14 interactors
DIPiDIP-59769N
IntActiP36888, 24 interactors
MINTiP36888
STRINGi9606.ENSP00000241453

Chemistry databases

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

PTM databases

iPTMnetiP36888
PhosphoSitePlusiP36888

Polymorphism and mutation databases

BioMutaiFLT3
DMDMi156630887

Proteomic databases

jPOSTiP36888
MaxQBiP36888
PaxDbiP36888
PeptideAtlasiP36888
PRIDEiP36888
ProteomicsDBi55226
55227 [P36888-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2322
DisGeNETi2322
EuPathDBiHostDB:ENSG00000122025.14

GeneCards: human genes, protein and diseases

More...GeneCardsi		FLT3

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0037338
HGNCiHGNC:3765 FLT3
HPAiHPA047539
MalaCardsiFLT3
MIMi136351 gene
601626 phenotype
neXtProtiNX_P36888
OpenTargetsiENSG00000122025
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)
98832 Acute myeloid leukemia with minimal differentiation
102724 Acute myeloid leukemia with t(8;21)(q22;q22) translocation
99860 Precursor B-cell acute lymphoblastic leukemia
99861 Precursor T-cell acute lymphoblastic leukemia
PharmGKBiPA28181

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000160575
HOVERGENiHBG005735
InParanoidiP36888
KOiK05092
OMAiYFYIDFR
OrthoDBi236292at2759
PhylomeDBiP36888
TreeFamiTF325768

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		FLT3 human
EvolutionaryTraceiP36888

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CD135

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		2322

Protein Ontology

More...PROi		PR:P36888

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

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

Family and domain databases

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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFLT3_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P36888
Secondary accession number(s): A0AVG9
, B7ZLT7, B7ZLT8, F5H0A0, Q13414
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: August 21, 2007
Last modified: February 13, 2019
This is version 189 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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