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Protein

Mast/stem cell growth factor receptor Kit

Gene

KIT

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 KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KITLG/SCF binding, KIT can activate several signaling pathways. Phosphorylates PIK3R1, PLCG1, SH2B2/APS and CBL. Activates the AKT1 signaling pathway by phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase. Activated KIT also transmits signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. Promotes activation of STAT family members STAT1, STAT3, STAT5A and STAT5B. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KIT signaling is modulated by protein phosphatases, and by rapid internalization and degradation of the receptor. Activated KIT promotes phosphorylation of the protein phosphatases PTPN6/SHP-1 and PTPRU, and of the transcription factors STAT1, STAT3, STAT5A and STAT5B. Promotes phosphorylation of PIK3R1, CBL, CRK (isoform Crk-II), LYN, MAPK1/ERK2 and/or MAPK3/ERK1, PLCG1, SRC and SHC1.10 Publications

Miscellaneous

Numerous proteins are phosphorylated in response to KIT signaling, but it is not evident to determine which are directly phosphorylated by KIT under in vivo conditions.

<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. KITLG/SCF binding leads to dimerization and activation by autophosphorylation on tyrosine residues. Activity is down-regulated by PRKCA-mediated phosphorylation on serine residues. Inhibited by imatinib/STI-571 (Gleevec) and sunitinib; these compounds maintain the kinase in an inactive conformation.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi568Magnesium1
<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 sitei623ATP1
<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 sitei792Proton acceptorPROSITE-ProRule annotation1
Binding sitei796ATP1
Metal bindingi797Magnesium1
Metal bindingi810Magnesium1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei936Important for interaction with phosphotyrosine-binding proteins1

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 bindingi596 – 603ATP8
Nucleotide bindingi671 – 677ATP7

<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

GO - Biological processi

<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
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.10.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-1433557 Signaling by SCF-KIT
R-HSA-1433559 Regulation of KIT signaling
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8866910 TFAP2 (AP-2) family regulates transcription of growth factors and their receptors

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

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SignaLinki
P10721

SIGNOR Signaling Network Open Resource

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SIGNORi
P10721

<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:
Mast/stem cell growth factor receptor Kit (EC:2.7.10.1)
Short name:
SCFR
Alternative name(s):
Piebald trait protein
Short name:
PBT
Proto-oncogene c-Kit
Tyrosine-protein kinase Kit
p145 c-kit
v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog
CD_antigen: CD117
<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:KIT
Synonyms:SCFR
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 4

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000157404.15

Human Gene Nomenclature Database

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HGNCi
HGNC:6342 KIT

Online Mendelian Inheritance in Man (OMIM)

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MIMi
164920 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P10721

<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 domaini26 – 524ExtracellularSequence analysisAdd BLAST499
<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>Transmembranei525 – 545HelicalSequence analysisAdd BLAST21
Topological domaini546 – 976CytoplasmicSequence analysisAdd BLAST431

Keywords - Cellular componenti

Cell membrane, Cytoplasm, 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

Piebald trait (PBT)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant genetic developmental abnormality of pigmentation characterized by congenital patches of white skin and hair that lack melanocytes.
See also OMIM:172800
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_004104583E → K in PBT. 1 PublicationCorresponds to variant dbSNP:rs121913680EnsemblClinVar.1
Natural variantiVAR_033129584F → C in PBT. 1 PublicationCorresponds to variant dbSNP:rs28933371EnsemblClinVar.1
Natural variantiVAR_004105584F → L in PBT. 1 PublicationCorresponds to variant dbSNP:rs794726671EnsemblClinVar.1
Natural variantiVAR_033130601G → R in PBT. 1 Publication1
Natural variantiVAR_033131656L → P in PBT. 1 Publication1
Natural variantiVAR_004106664G → R in PBT. 1 PublicationCorresponds to variant dbSNP:rs121913679EnsemblClinVar.1
Natural variantiVAR_004107791R → G in PBT. 1 Publication1
Natural variantiVAR_033132796R → G in PBT; with sensorineural deafness. 1 PublicationCorresponds to variant dbSNP:rs121913684EnsemblClinVar.1
Natural variantiVAR_004108812G → V in PBT. 1 Publication1
Natural variantiVAR_033137847T → P in PBT. 1 PublicationCorresponds to variant dbSNP:rs121913687EnsemblClinVar.1
Natural variantiVAR_004110893 – 896Missing in PBT; severe. 1 Publication4
Gastrointestinal stromal tumor (GIST)4 Publications
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionCommon mesenchymal neoplasms arising in the gastrointestinal tract, most often in the stomach. They are histologically, immunohistochemically, and genetically different from typical leiomyomas, leiomyosarcomas, and schwannomas. Most GISTs are composed of a fairly uniform population of spindle-shaped cells. Some tumors are dominated by epithelioid cells or contain a mixture of spindle and epithelioid morphologies. Primary GISTs in the gastrointestinal tract commonly metastasize in the omentum and mesenteries, often as multiple nodules. However, primary tumors may also occur outside of the gastrointestinal tract, in other intra-abdominal locations, especially in the omentum and mesentery.
See also OMIM:606764
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033124550 – 558Missing in GIST; somatic mutation. 2 Publications9
Natural variantiVAR_033123550K → I in GIST; somatic mutation. 1 Publication1
Natural variantiVAR_033125551 – 555Missing in GIST; somatic mutation. 1 Publication5
Natural variantiVAR_033128559 – 560Missing in GIST; somatic mutation. 1 Publication2
Natural variantiVAR_033126559V → A in GIST. 1 PublicationCorresponds to variant dbSNP:rs121913517EnsemblClinVar.1
Natural variantiVAR_033127559V → D in GIST; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913517EnsemblClinVar.1
Natural variantiVAR_007965559Missing in GIST. 1 Publication1
Testicular germ cell tumor (TGCT)
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma.
See also OMIM:273300
Leukemia, acute myelogenous (AML)
The gene represented in this entry is involved in disease pathogenesis. Somatic mutations that lead to constitutive activation of KIT are detected 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 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
Mastocytosis, cutaneous (MASTC)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mastocytosis, a heterogeneous group of disorders associated with abnormal proliferation and accumulation of mast cells in various tissues, especially in the skin and hematopoietic organs. MASTC is an autosomal dominant form characterized by macules, papules, nodules, or diffuse infiltration of the skin, often associated with localized hyperpigmentation. Gentle rubbing of the lesions induces histamine release from mechanically activated mast cells, causing local wheals, erythema, and often pruritus, a phenomenon termed Darier sign.
See also OMIM:154800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_081062451S → C in MASTC; unknown pathological significance. 1 Publication1
Natural variantiVAR_081063533A → D in MASTC; unknown pathological significance. 1 Publication1
Natural variantiVAR_033133816D → F in MASTC; sporadic case; somatic mutation; requires 2 nucleotide substitutions; constitutively activated and is much more rapidly autophosphorylated than wild type. 1 Publication1
Natural variantiVAR_081064816D → I in MASTC; somatic mutation; constitutively activated; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_081065822N → I in MASTC; constitutively activated. 1 Publication1
Natural variantiVAR_033136839E → K in MASTC; sporadic case; somatic mutation; dominant negative mutation; loss of autophosphorylation. 1 PublicationCorresponds to variant dbSNP:rs121913509EnsemblClinVar.1
Mastocytosis, systemic (MASTSYS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe form of mastocytosis characterized by abnormal proliferation and accumulation of mast cells in several organs, resulting in a systemic disease that may affect bone, gastrointestinal tract, lymphatics, spleen, and liver. In some cases, it is associated with a clonal hematologic non-mast-cell lineage disease, such as a myelodysplastic or myeloproliferative disorder. It can also lead to mast cell leukemia, which carries a high risk of mortality.
See also OMIM:154800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004109816D → V in MASTSYS, MASTC and mast cell leukemia; somatic mutation; constitutively activated; loss of interaction with MPDZ. 8 PublicationsCorresponds to variant dbSNP:rs121913507EnsemblClinVar.1

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>Mutagenesisi381R → A: Reduces autophosphorylation in response to KITLG/SCF. 1 Publication1
Mutagenesisi386E → A: Reduces autophosphorylation in response to KITLG/SCF. 1 Publication1
Mutagenesisi571I → A: Reduction in SH2B2/APS binding. Abolishes SH2B2/APS binding; when associated with A-939. 1 Publication1
Mutagenesisi623K → M: Stronger interaction with MPDZ. 1 Publication1
Mutagenesisi741S → A: Abolishes down-regulation of kinase activity by PKC/PRKCA-mediated phosphorylation; when associated with A-746. 1 Publication1
Mutagenesisi746S → A: Abolishes down-regulation of kinase activity by PKC/PRKCA-mediated phosphorylation; when associated with A-741. 1 Publication1
Mutagenesisi823Y → F: No decrease in activity. Leads to autophosphorylation at Tyr-900. 1 Publication1
Mutagenesisi939L → A: Reduction in SH2B2/APS binding. Abolishes SH2B2/APS binding; when associated with A-571. 1 Publication1

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
3815

MalaCards human disease database

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MalaCardsi
KIT
MIMi154800 phenotype
172800 phenotype
273300 phenotype
601626 phenotype
606764 phenotype

Open Targets

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OpenTargetsi
ENSG00000157404

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

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Orphaneti
98834 Acute myeloblastic leukemia with 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
158799 Aleukemic mast cell leukemia
280785 Bullous diffuse cutaneous mastocytosis
158796 Classic mast cell leukemia
79455 Cutaneous mastocytoma
44890 Gastrointestinal stromal tumor
158778 Isolated bone marrow mastocytosis
158793 Lymphoadenopathic mastocytosis with eosinophilia
158772 Nodular urticaria pigmentosa
2884 Piebaldism
158769 Plaque-form urticaria pigmentosa
280794 Pseudoxanthomatous diffuse cutaneous mastocytosis
158775 Smouldering systemic mastocytosis
98849 Systemic mastocytosis with an associated clonal hematologic non-mast cell lineage disease
90389 Telangiectasia macularis eruptiva perstans
842 Testicular seminomatous germ cell tumor
158766 Typical urticaria pigmentosa

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30128

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1936

Drug and drug target database

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DrugBanki
DB06080 ABT-869
DB01254 Dasatinib
DB00619 Imatinib
DB09078 Lenvatinib
DB05216 MP470
DB04868 Nilotinib
DB05913 OSI-930
DB06589 Pazopanib
DB01962 Phosphonotyrosine
DB08901 Ponatinib
DB08896 Regorafenib
DB00398 Sorafenib
DB01268 Sunitinib
DB05153 XL184
DB05146 XL820

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1805

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
KIT

Domain mapping of disease mutations (DMDM)

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DMDMi
125472

<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 – 25Sequence analysisAdd BLAST25
<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_000001675426 – 976Mast/stem cell growth factor receptor KitAdd BLAST951

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 bondi58 ↔ 97PROSITE-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>Glycosylationi130N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi136 ↔ 186PROSITE-ProRule annotation1 Publication
Glycosylationi145N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi151 ↔ 183PROSITE-ProRule annotation1 Publication
Disulfide bondi233 ↔ 290PROSITE-ProRule annotation1 Publication
Glycosylationi283N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi293N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi300N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi320N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi352N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi367N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi428 ↔ 491PROSITE-ProRule annotation1 Publication
Glycosylationi463N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi486N-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 residuei547Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei553Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei568Phosphotyrosine; by autocatalysis4 Publications1
Modified residuei570Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei703Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei721Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei730Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei741Phosphoserine; by PKC/PRKCA1 Publication1
Modified residuei746Phosphoserine; by PKC/PRKCA1 Publication1
Modified residuei821Phosphoserine1 Publication1
Modified residuei823Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei891Phosphoserine1 Publication1
Modified residuei900Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei936Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei959PhosphoserineCombined sources1 Publication1

<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

Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation.2 Publications
Autophosphorylated on tyrosine residues. KITLG/SCF binding enhances autophosphorylation. Isoform 1 shows low levels of tyrosine phosphorylation in the absence of added KITLG/SCF (in vitro). Kinase activity is down-regulated by phosphorylation on serine residues by protein kinase C family members. Phosphorylation at Tyr-568 is required for interaction with PTPN11/SHP-2, CRK (isoform Crk-II) and members of the SRC tyrosine-protein kinase family. Phosphorylation at Tyr-570 is required for interaction with PTPN6/SHP-1. Phosphorylation at Tyr-703, Tyr-823 and Tyr-936 is important for interaction with GRB2. Phosphorylation at Tyr-721 is important for interaction with PIK3R1. Phosphorylation at Tyr-823 and Tyr-936 is important for interaction with GRB7.6 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P10721

MaxQB - The MaxQuant DataBase

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MaxQBi
P10721

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

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PaxDbi
P10721

PeptideAtlas

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PeptideAtlasi
P10721

PRoteomics IDEntifications database

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PRIDEi
P10721

ProteomicsDB human proteome resource

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ProteomicsDBi
52640
52641 [P10721-2]
52642 [P10721-3]

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P10721

GlyConnect protein glycosylation platform

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GlyConnecti
1492

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P10721

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

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PhosphoSitePlusi
P10721

<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

Isoform 1 and isoform 2 are detected in spermatogonia and Leydig cells. Isoform 3 is detected in round spermatids, elongating spermatids and spermatozoa (at protein level). Widely expressed. Detected in the hematopoietic system, the gastrointestinal system, in melanocytes and in germ cells.2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by cis-retinoic acid in neuroblastoma cell lines.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000157404 Expressed in 214 organ(s), highest expression level in epithelium of mammary gland

CleanEx database of gene expression profiles

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CleanExi
HS_KIT

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P10721 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P10721 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB003288
CAB068253
CAB072867
HPA004471
HPA073252

<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 KITLG/SCF. Homodimer in the presence of bound KITLG/SCF, forming a heterotetramer with two KITLG/SCF molecules. Interacts (via phosphorylated tyrosine residues) with the adapter proteins GRB2 and GRB7 (via SH2 domain), and SH2B2/APS. Interacts (via C-terminus) with MPDZ (via the tenth PDZ domain). Interacts (via phosphorylated tyrosine residues) with PIK3R1 and PIK3 catalytic subunit. Interacts (via phosphorylated tyrosine) with CRK (isoform Crk-II), FYN, SHC1 and MATK/CHK (via SH2 domain). Interacts with LYN and FES/FPS. Interacts (via phosphorylated tyrosine residues) with the protein phosphatases PTPN6/SHP-1 (via SH2 domain), PTPN11/SHP-2 (via SH2 domain) and PTPRU. Interacts with PLCG1. Interacts with DOK1 and TEC. Interacts (KITLG/SCF-bound) with IL1RL1. Interacts with IL1RAP (independent of stimulation with KITLG/SCF). A mast cell-specific KITLG/SCF-induced interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and MYD88.By similarity17 Publications

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110015, 53 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P10721

Database of interacting proteins

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DIPi
DIP-1055N

Protein interaction database and analysis system

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IntActi
P10721, 66 interactors

Molecular INTeraction database

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MINTi
P10721

STRING: functional protein association networks

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STRINGi
9606.ENSP00000288135

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P10721

<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

1976
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P10721

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

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SMRi
P10721

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P10721

<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>Domaini27 – 112Ig-like C2-type 1Add BLAST86
Domaini121 – 205Ig-like C2-type 2Add BLAST85
Domaini212 – 308Ig-like C2-type 3Add BLAST97
Domaini317 – 410Ig-like C2-type 4Add BLAST94
Domaini413 – 507Ig-like C2-type 5Add BLAST95
Domaini589 – 937Protein kinasePROSITE-ProRule annotationAdd BLAST349

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>Regioni568 – 570Important for interaction with phosphotyrosine-binding proteins3

<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, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0200 Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155626

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000112008

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG004335

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P10721

KEGG Orthology (KO)

More...
KOi
K05091

Identification of Orthologs from Complete Genome Data

More...
OMAi
YMNRTST

Database of Orthologous Groups

More...
OrthoDBi
EOG091G01TL

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P10721

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, 5 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013151 Immunoglobulin
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR027263 SCGF_receptor
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR001824 Tyr_kinase_rcpt_3_CS

Pfam protein domain database

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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF500951 SCGF_recepter, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48726 SSF48726, 3 hits
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 (3)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 3 <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
Isoform 1 (identifier: P10721-1) [UniParc]FASTAAdd to basket
Also known as: GNNK(+), KitA(+)

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
MRGARGAWDF LCVLLLLLRV QTGSSQPSVS PGEPSPPSIH PGKSDLIVRV
60 70 80 90 100
GDEIRLLCTD PGFVKWTFEI LDETNENKQN EWITEKAEAT NTGKYTCTNK
110 120 130 140 150
HGLSNSIYVF VRDPAKLFLV DRSLYGKEDN DTLVRCPLTD PEVTNYSLKG
160 170 180 190 200
CQGKPLPKDL RFIPDPKAGI MIKSVKRAYH RLCLHCSVDQ EGKSVLSEKF
210 220 230 240 250
ILKVRPAFKA VPVVSVSKAS YLLREGEEFT VTCTIKDVSS SVYSTWKREN
260 270 280 290 300
SQTKLQEKYN SWHHGDFNYE RQATLTISSA RVNDSGVFMC YANNTFGSAN
310 320 330 340 350
VTTTLEVVDK GFINIFPMIN TTVFVNDGEN VDLIVEYEAF PKPEHQQWIY
360 370 380 390 400
MNRTFTDKWE DYPKSENESN IRYVSELHLT RLKGTEGGTY TFLVSNSDVN
410 420 430 440 450
AAIAFNVYVN TKPEILTYDR LVNGMLQCVA AGFPEPTIDW YFCPGTEQRC
460 470 480 490 500
SASVLPVDVQ TLNSSGPPFG KLVVQSSIDS SAFKHNGTVE CKAYNDVGKT
510 520 530 540 550
SAYFNFAFKG NNKEQIHPHT LFTPLLIGFV IVAGMMCIIV MILTYKYLQK
560 570 580 590 600
PMYEVQWKVV EEINGNNYVY IDPTQLPYDH KWEFPRNRLS FGKTLGAGAF
610 620 630 640 650
GKVVEATAYG LIKSDAAMTV AVKMLKPSAH LTEREALMSE LKVLSYLGNH
660 670 680 690 700
MNIVNLLGAC TIGGPTLVIT EYCCYGDLLN FLRRKRDSFI CSKQEDHAEA
710 720 730 740 750
ALYKNLLHSK ESSCSDSTNE YMDMKPGVSY VVPTKADKRR SVRIGSYIER
760 770 780 790 800
DVTPAIMEDD ELALDLEDLL SFSYQVAKGM AFLASKNCIH RDLAARNILL
810 820 830 840 850
THGRITKICD FGLARDIKND SNYVVKGNAR LPVKWMAPES IFNCVYTFES
860 870 880 890 900
DVWSYGIFLW ELFSLGSSPY PGMPVDSKFY KMIKEGFRML SPEHAPAEMY
910 920 930 940 950
DIMKTCWDAD PLKRPTFKQI VQLIEKQISE STNHIYSNLA NCSPNRQKPV
960 970
VDHSVRINSV GSTASSSQPL LVHDDV
Length:976
Mass (Da):109,865
Last modified:July 1, 1989 - v1
<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:i81B0CD76817F3454
GO
Isoform 2 (identifier: P10721-2) [UniParc]FASTAAdd to basket
Also known as: GNNK(-), Kit(+)

The sequence of this isoform differs from the canonical sequence as follows:
     510-513: Missing.

Show »
Length:972
Mass (Da):109,451
Checksum:iD59DEFE9AF761FDA
GO
Isoform 3 (identifier: P10721-3) [UniParc]FASTAAdd to basket
Also known as: TR-KIT

The sequence of this isoform differs from the canonical sequence as follows:
     412-413: KP → SL
     414-976: Missing.

Show »
Length:413
Mass (Da):46,658
Checksum:i08B327362CEF1B7E
GO

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 conflicti764L → I in AAH71593 (PubMed:15489334).Curated1
Sequence conflicti838P → H in AAH71593 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_081062451S → C in MASTC; unknown pathological significance. 1 Publication1
Natural variantiVAR_042021532V → I1 PublicationCorresponds to variant dbSNP:rs55792975EnsemblClinVar.1
Natural variantiVAR_081063533A → D in MASTC; unknown pathological significance. 1 Publication1
Natural variantiVAR_042022541M → L2 PublicationsCorresponds to variant dbSNP:rs3822214EnsemblClinVar.1
Natural variantiVAR_061289541M → V. Corresponds to variant dbSNP:rs3822214EnsemblClinVar.1
Natural variantiVAR_033124550 – 558Missing in GIST; somatic mutation. 2 Publications9
Natural variantiVAR_033123550K → I in GIST; somatic mutation. 1 Publication1
Natural variantiVAR_033125551 – 555Missing in GIST; somatic mutation. 1 Publication5
Natural variantiVAR_033128559 – 560Missing in GIST; somatic mutation. 1 Publication2
Natural variantiVAR_033126559V → A in GIST. 1 PublicationCorresponds to variant dbSNP:rs121913517EnsemblClinVar.1
Natural variantiVAR_033127559V → D in GIST; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121913517EnsemblClinVar.1
Natural variantiVAR_007965559Missing in GIST. 1 Publication1
Natural variantiVAR_004104583E → K in PBT. 1 PublicationCorresponds to variant dbSNP:rs121913680EnsemblClinVar.1
Natural variantiVAR_033129584F → C in PBT. 1 PublicationCorresponds to variant dbSNP:rs28933371EnsemblClinVar.1
Natural variantiVAR_004105584F → L in PBT. 1 PublicationCorresponds to variant dbSNP:rs794726671EnsemblClinVar.1
Natural variantiVAR_033130601G → R in PBT. 1 Publication1
Natural variantiVAR_033131656L → P in PBT. 1 Publication1
Natural variantiVAR_004106664G → R in PBT. 1 PublicationCorresponds to variant dbSNP:rs121913679EnsemblClinVar.1
Natural variantiVAR_042023691C → S1 PublicationCorresponds to variant dbSNP:rs35200131Ensembl.1
Natural variantiVAR_042024715S → N1 PublicationCorresponds to variant dbSNP:rs56094246Ensembl.1
Natural variantiVAR_042025737D → N in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs751005114EnsemblClinVar.1
Natural variantiVAR_004107791R → G in PBT. 1 Publication1
Natural variantiVAR_033132796R → G in PBT; with sensorineural deafness. 1 PublicationCorresponds to variant dbSNP:rs121913684EnsemblClinVar.1
Natural variantiVAR_042026804R → W in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs145602440EnsemblClinVar.1
Natural variantiVAR_004108812G → V in PBT. 1 Publication1
Natural variantiVAR_033133816D → F in MASTC; sporadic case; somatic mutation; requires 2 nucleotide substitutions; constitutively activated and is much more rapidly autophosphorylated than wild type. 1 Publication1
Natural variantiVAR_033134816D → H in a testicular tumor; seminoma; somatic mutation; constitutively activated. 3 PublicationsCorresponds to variant dbSNP:rs121913506EnsemblClinVar.1
Natural variantiVAR_081064816D → I in MASTC; somatic mutation; constitutively activated; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_004109816D → V in MASTSYS, MASTC and mast cell leukemia; somatic mutation; constitutively activated; loss of interaction with MPDZ. 8 PublicationsCorresponds to variant dbSNP:rs121913507EnsemblClinVar.1
Natural variantiVAR_023828816D → Y in MASTSYS and MASTC; also found in acute myeloid leukemia and a germ cell tumor of the testis; somatic mutation; constitutively activated. 5 PublicationsCorresponds to variant dbSNP:rs121913506EnsemblClinVar.1
Natural variantiVAR_033135820D → G in mast cell disease; systemic. 1 PublicationCorresponds to variant dbSNP:rs121913682EnsemblClinVar.1
Natural variantiVAR_081065822N → I in MASTC; constitutively activated. 1 Publication1
Natural variantiVAR_023829822N → K in a germ cell tumor of the testis; somatic mutation. 2 PublicationsCorresponds to variant dbSNP:rs121913514EnsemblClinVar.1
Natural variantiVAR_023830829A → P in a germ cell tumor of the testis; somatic mutation. 2 PublicationsCorresponds to variant dbSNP:rs1057519713Ensembl.1
Natural variantiVAR_033136839E → K in MASTC; sporadic case; somatic mutation; dominant negative mutation; loss of autophosphorylation. 1 PublicationCorresponds to variant dbSNP:rs121913509EnsemblClinVar.1
Natural variantiVAR_033137847T → P in PBT. 1 PublicationCorresponds to variant dbSNP:rs121913687EnsemblClinVar.1
Natural variantiVAR_004110893 – 896Missing in PBT; severe. 1 Publication4

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_041866412 – 413KP → SL in isoform 3. 1 Publication2
Alternative sequenceiVSP_041867414 – 976Missing in isoform 3. 1 PublicationAdd BLAST563
Alternative sequenceiVSP_038385510 – 513Missing in isoform 2. 3 Publications4

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
X06182 mRNA Translation: CAA29548.1
X69301
, X69302, X69303, X69304, X69305, X69306, X69307, X69308, X69309, X69310, X69311, X69312, X69313, X69314, X69315, X69316 Genomic DNA Translation: CAA49159.1
U63834 Genomic DNA Translation: AAC50968.1
U63834 Genomic DNA Translation: AAC50969.1
EU826594 mRNA Translation: ACF47630.1
GU983671 mRNA Translation: ADF36702.1
HM015525 mRNA Translation: ADF50068.1
HM015526 mRNA Translation: ADF50069.1
AK304031 mRNA Translation: BAG64945.1
AC006552 Genomic DNA No translation available.
AC092545 Genomic DNA No translation available.
BC071593 mRNA Translation: AAH71593.1
S67773 Genomic DNA Translation: AAB29529.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS3496.1 [P10721-1]
CCDS47058.1 [P10721-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
S01426 TVHUKT

NCBI Reference Sequences

More...
RefSeqi
NP_000213.1, NM_000222.2 [P10721-1]
NP_001087241.1, NM_001093772.1 [P10721-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.479754

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000288135; ENSP00000288135; ENSG00000157404 [P10721-1]
ENST00000412167; ENSP00000390987; ENSG00000157404 [P10721-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3815

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3815

UCSC genome browser

More...
UCSCi
uc010igr.4 human [P10721-1]

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
Wikipedia

CD117 entry

Protein Spotlight

two's company - Issue 163 of August 2014

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06182 mRNA Translation: CAA29548.1
X69301
, X69302, X69303, X69304, X69305, X69306, X69307, X69308, X69309, X69310, X69311, X69312, X69313, X69314, X69315, X69316 Genomic DNA Translation: CAA49159.1
U63834 Genomic DNA Translation: AAC50968.1
U63834 Genomic DNA Translation: AAC50969.1
EU826594 mRNA Translation: ACF47630.1
GU983671 mRNA Translation: ADF36702.1
HM015525 mRNA Translation: ADF50068.1
HM015526 mRNA Translation: ADF50069.1
AK304031 mRNA Translation: BAG64945.1
AC006552 Genomic DNA No translation available.
AC092545 Genomic DNA No translation available.
BC071593 mRNA Translation: AAH71593.1
S67773 Genomic DNA Translation: AAB29529.1
CCDSiCCDS3496.1 [P10721-1]
CCDS47058.1 [P10721-2]
PIRiS01426 TVHUKT
RefSeqiNP_000213.1, NM_000222.2 [P10721-1]
NP_001087241.1, NM_001093772.1 [P10721-2]
UniGeneiHs.479754

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
1PKGX-ray2.90A/B549-935[»]
1QZJmodel-A576-932[»]
1QZKmodel-A576-932[»]
1R01model-A576-932[»]
1T45X-ray1.90A547-693[»]
A754-935[»]
1T46X-ray1.60A565-693[»]
A754-935[»]
2E9WX-ray3.50A/B26-514[»]
2EC8X-ray3.00A1-519[»]
2IUHX-ray2.00B718-728[»]
2VIFX-ray1.45P564-574[»]
3G0EX-ray1.60A544-693[»]
A754-935[»]
3G0FX-ray2.60A/B544-693[»]
A/B754-935[»]
4HVSX-ray1.90A551-934[»]
4K94X-ray2.40C308-518[»]
4K9EX-ray2.70C308-518[»]
4PGZX-ray2.40A/B/C308-518[»]
4U0IX-ray2.00A563-693[»]
A754-935[»]
6GQJX-ray2.33A/B551-933[»]
6GQKX-ray2.31A/B551-687[»]
A/B771-934[»]
6GQLX-ray2.01A/B551-934[»]
6GQMX-ray2.00A/B551-934[»]
ProteinModelPortaliP10721
SMRiP10721
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110015, 53 interactors
CORUMiP10721
DIPiDIP-1055N
IntActiP10721, 66 interactors
MINTiP10721
STRINGi9606.ENSP00000288135

Chemistry databases

BindingDBiP10721
ChEMBLiCHEMBL1936
DrugBankiDB06080 ABT-869
DB01254 Dasatinib
DB00619 Imatinib
DB09078 Lenvatinib
DB05216 MP470
DB04868 Nilotinib
DB05913 OSI-930
DB06589 Pazopanib
DB01962 Phosphonotyrosine
DB08901 Ponatinib
DB08896 Regorafenib
DB00398 Sorafenib
DB01268 Sunitinib
DB05153 XL184
DB05146 XL820
GuidetoPHARMACOLOGYi1805

PTM databases

CarbonylDBiP10721
GlyConnecti1492
iPTMnetiP10721
PhosphoSitePlusiP10721

Polymorphism and mutation databases

BioMutaiKIT
DMDMi125472

Proteomic databases

EPDiP10721
MaxQBiP10721
PaxDbiP10721
PeptideAtlasiP10721
PRIDEiP10721
ProteomicsDBi52640
52641 [P10721-2]
52642 [P10721-3]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
3815
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000288135; ENSP00000288135; ENSG00000157404 [P10721-1]
ENST00000412167; ENSP00000390987; ENSG00000157404 [P10721-2]
GeneIDi3815
KEGGihsa:3815
UCSCiuc010igr.4 human [P10721-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
3815
DisGeNETi3815
EuPathDBiHostDB:ENSG00000157404.15

GeneCards: human genes, protein and diseases

More...
GeneCardsi
KIT
HGNCiHGNC:6342 KIT
HPAiCAB003288
CAB068253
CAB072867
HPA004471
HPA073252
MalaCardsiKIT
MIMi154800 phenotype
164920 gene
172800 phenotype
273300 phenotype
601626 phenotype
606764 phenotype
neXtProtiNX_P10721
OpenTargetsiENSG00000157404
Orphaneti98834 Acute myeloblastic leukemia with 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
158799 Aleukemic mast cell leukemia
280785 Bullous diffuse cutaneous mastocytosis
158796 Classic mast cell leukemia
79455 Cutaneous mastocytoma
44890 Gastrointestinal stromal tumor
158778 Isolated bone marrow mastocytosis
158793 Lymphoadenopathic mastocytosis with eosinophilia
158772 Nodular urticaria pigmentosa
2884 Piebaldism
158769 Plaque-form urticaria pigmentosa
280794 Pseudoxanthomatous diffuse cutaneous mastocytosis
158775 Smouldering systemic mastocytosis
98849 Systemic mastocytosis with an associated clonal hematologic non-mast cell lineage disease
90389 Telangiectasia macularis eruptiva perstans
842 Testicular seminomatous germ cell tumor
158766 Typical urticaria pigmentosa
PharmGKBiPA30128

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0200 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000155626
HOGENOMiHOG000112008
HOVERGENiHBG004335
InParanoidiP10721
KOiK05091
OMAiYMNRTST
OrthoDBiEOG091G01TL
PhylomeDBiP10721
TreeFamiTF325768

Enzyme and pathway databases

BRENDAi2.7.10.1 2681
ReactomeiR-HSA-1257604 PIP3 activates AKT signaling
R-HSA-1433557 Signaling by SCF-KIT
R-HSA-1433559 Regulation of KIT signaling
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8866910 TFAP2 (AP-2) family regulates transcription of growth factors and their receptors
SignaLinkiP10721
SIGNORiP10721

Miscellaneous databases

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

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ChiTaRSi
KIT human
EvolutionaryTraceiP10721

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
CD117

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

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GenomeRNAii
3815

Protein Ontology

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PROi
PR:P10721

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000157404 Expressed in 214 organ(s), highest expression level in epithelium of mammary gland
CleanExiHS_KIT
ExpressionAtlasiP10721 baseline and differential
GenevisibleiP10721 HS

Family and domain databases

Gene3Di2.60.40.10, 5 hits
InterProiView protein in InterPro
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013151 Immunoglobulin
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR027263 SCGF_receptor
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR001824 Tyr_kinase_rcpt_3_CS
PfamiView protein in Pfam
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PIRSFiPIRSF500951 SCGF_recepter, 1 hit
SMARTiView protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF48726 SSF48726, 3 hits
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

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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 nameiKIT_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: P10721
Secondary accession number(s): B5A956
, D5LXN2, D5M931, F5H8F8, Q6IQ28, Q99662, Q9UM99
<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: July 1, 1989
Last sequence update: July 1, 1989
Last modified: December 5, 2018
This is version 225 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  8. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  9. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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