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UniProtKB - P10721 (KIT_HUMAN)

Entry version 241 (02 Dec 2020)
Sequence version 1 (01 Jul 1989)
Previous versions | rss
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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%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Complete GO annotation on QuickGO ...

GO - Biological processi

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.10.1, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P10721

Reactome - a knowledgebase of biological pathways and processes

More...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
R-HSA-9669914, Dasatinib-resistant KIT mutants
R-HSA-9669917, Imatinib-resistant KIT mutants
R-HSA-9669921, KIT mutants bind TKIs
R-HSA-9669924, Masitinib-resistant KIT mutants
R-HSA-9669926, Nilotinib-resistant KIT mutants
R-HSA-9669929, Regorafenib-resistant KIT mutants
R-HSA-9669933, Signaling by kinase domain mutants of KIT
R-HSA-9669934, Sunitinib-resistant KIT mutants
R-HSA-9669935, Signaling by juxtamembrane domain KIT mutants
R-HSA-9669936, Sorafenib-resistant KIT mutants
R-HSA-9670439, Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants
R-HSA-9680187, Signaling by extracellular domain mutants of KIT

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

More...SignaLinki		P10721

SIGNOR Signaling Network Open Resource

More...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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 and Host Database Resources

More...EuPathDBi		HostDB:ENSG00000157404.15

Human Gene Nomenclature Database

More...HGNCi		HGNC:6342, KIT

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		164920, gene

neXtProt; the human protein knowledge platform

More...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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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%5Flocation%5Fsection">'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.
Related information in OMIM
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.
Related information in OMIM
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.
Related information in OMIM
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.
Related information in OMIM
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.
Related information in OMIM
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 PublicationCorresponds to variant dbSNP:rs753212327EnsemblClinVar.1
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 PublicationCorresponds to variant dbSNP:rs1057519709EnsemblClinVar.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_081065822N → I in MASTC; constitutively activated. 1 PublicationCorresponds to variant dbSNP:rs993022333EnsemblClinVar.1
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.
Related information in OMIM
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
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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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

More...DisGeNETi		3815

MalaCards human disease database

More...MalaCardsi		KIT
MIMi154800, phenotype
172800, phenotype
273300, phenotype
601626, phenotype
606764, phenotype

Open Targets

More...OpenTargetsi		ENSG00000157404

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

More...Orphaneti		566393, Acute mast cell leukemia
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
280785, Bullous diffuse cutaneous mastocytosis
566396, Chronic mast cell leukemia
79455, Cutaneous mastocytoma
44890, Gastrointestinal stromal tumor
158778, Isolated bone marrow mastocytosis
158772, Nodular urticaria pigmentosa
2884, Piebaldism
158769, Plaque-form urticaria pigmentosa
280794, Pseudoxanthomatous diffuse cutaneous mastocytosis
544260, Selection of therapeutic option in melanoma
158775, Smoldering systemic mastocytosis
98849, Systemic mastocytosis with associated hematologic neoplasm
90389, Telangiectasia macularis eruptiva perstans
842, Testicular seminomatous germ cell tumor
158766, Typical urticaria pigmentosa

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30128

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P10721, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1936

Drug and drug target database

More...DrugBanki		DB06080, ABT-869
DB12742, Amuvatinib
DB09103, Ancestim
DB15233, Avapritinib
DB01254, Dasatinib
DB12147, Erdafitinib
DB12010, Fostamatinib
DB00619, Imatinib
DB09078, Lenvatinib
DB06595, Midostaurin
DB04868, Nilotinib
DB05913, OSI-930
DB06589, Pazopanib
DB12978, Pexidartinib
DB01962, Phosphonotyrosine
DB08901, Ponatinib
DB08896, Regorafenib
DB14840, Ripretinib
DB00398, Sorafenib
DB01268, Sunitinib
DB05146, XL820

DrugCentral

More...DrugCentrali		P10721

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1805

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		KIT

Domain mapping of disease mutations (DMDM)

More...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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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%5Fprocessing%5Fsection">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

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P10721

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P10721

MaxQB - The MaxQuant DataBase

More...MaxQBi		P10721

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

More...PaxDbi		P10721

PeptideAtlas

More...PeptideAtlasi		P10721

PRoteomics IDEntifications database

More...PRIDEi		P10721

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		52640 [P10721-1]
52641 [P10721-2]
52642 [P10721-3]

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P10721

GlyConnect protein glycosylation platform

More...GlyConnecti		1492, 3 N-Linked glycans (2 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P10721, 10 sites, 1 N-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P10721

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

More...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 epithelium of mammary gland and 227 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P10721, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P10721, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000157404, Tissue enhanced (breast)

<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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details
P10721
With#Exp.IntAct
ABL1 [P00519]2EBI-1379503,EBI-375543
ABL2 [P42684]2EBI-1379503,EBI-1102694
BCAR3 [O75815]3EBI-1379503,EBI-702336
BLK [P51451]5EBI-1379503,EBI-2105445
BLNK [Q8WV28]2EBI-1379503,EBI-2623522
CRK [P46108]4EBI-1379503,EBI-886
FES [P07332]2EBI-1379503,EBI-1055635
FGR [P09769]2EBI-1379503,EBI-1383732
GRAP2 [O75791]2EBI-1379503,EBI-740418
GRB2 [P62993]6EBI-1379503,EBI-401755
GRB7 [Q14451]4EBI-1379503,EBI-970191
HCK [P08631]2EBI-1379503,EBI-346340
HSH2D [Q96JZ2]5EBI-1379503,EBI-3919324
KITLG [P21583]2EBI-1379503,EBI-1379527
LCK [P06239]8EBI-1379503,EBI-1348
LYN [P07948]7EBI-1379503,EBI-79452
NCK1 [P16333]3EBI-1379503,EBI-389883
NCK2 [O43639]2EBI-1379503,EBI-713635
PIK3R1 [P27986]19EBI-1379503,EBI-79464
PIK3R2 [O00459]19EBI-1379503,EBI-346930
PIK3R3 [Q92569]31EBI-1379503,EBI-79893
PLCG1 [P19174]31EBI-1379503,EBI-79387
PLCG2 [P16885]8EBI-1379503,EBI-617403
PTK6 [Q13882]4EBI-1379503,EBI-1383632
PTPN11 [Q06124]29EBI-1379503,EBI-297779
PTPRU [Q92729]2EBI-1379503,EBI-7052301
RASA1 [P20936]16EBI-1379503,EBI-1026476
SH2B3 [Q9UQQ2]2EBI-1379503,EBI-7879749
SH2D1B [O14796]8EBI-1379503,EBI-3923013
SH2D2A [Q9NP31]10EBI-1379503,EBI-490630
SH2D3C [Q8N5H7]4EBI-1379503,EBI-745980
SH3BP2 [P78314]3EBI-1379503,EBI-727062
SHB [Q15464]2EBI-1379503,EBI-4402156
SHC1 [P29353]8EBI-1379503,EBI-78835
SHC2 [P98077]5EBI-1379503,EBI-7256023
SHC3 [Q92529]3EBI-1379503,EBI-79084
SLA2 [Q9H6Q3]2EBI-1379503,EBI-1222854
SOCS2 [O14508]4EBI-1379503,EBI-617737
SOCS3 [O14543]3EBI-1379503,EBI-714146
SOCS6 [O14544]12EBI-1379503,EBI-3929549
SRC [P12931]5EBI-1379503,EBI-621482
STAP1 [Q9ULZ2]3EBI-1379503,EBI-6083058
TNS1 [Q9HBL0]2EBI-1379503,EBI-3389814
TNS2 [Q63HR2]2EBI-1379503,EBI-949753
TNS3 [Q68CZ2]5EBI-1379503,EBI-1220488
TXK [P42681]3EBI-1379503,EBI-7877438
YES1 [P07947]7EBI-1379503,EBI-515331
ZAP70 [P43403]2EBI-1379503,EBI-1211276
Mpdz [Q8VBX6] from Mus musculus.4EBI-1379503,EBI-8026435
Ptpn11 [P35235] from Mus musculus.2EBI-1379503,EBI-397236

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		110015, 62 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P10721

Database of interacting proteins

More...DIPi		DIP-1055N

Protein interaction database and analysis system

More...IntActi		P10721, 96 interactors

Molecular INTeraction database

More...MINTi		P10721

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000288135

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P10721

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P10721, protein

<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

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

More...SMRi		P10721

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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%5Fand%5Fdomains%5Fsection">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

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155626

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000288_49_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P10721

Identification of Orthologs from Complete Genome Data

More...OMAi		PSEMYQI

Database of Orthologous Groups

More...OrthoDBi		236292at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P10721

TreeFam database of animal gene trees

More...TreeFami		TF325768

Family and domain databases

Database of protein disorder

More...DisProti		DP02247

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, PK_Tyr_Ser-Thr, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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 <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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 PublicationCorresponds to variant dbSNP:rs753212327EnsemblClinVar.1
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:rs56094246EnsemblClinVar.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 PublicationCorresponds to variant dbSNP:rs1057519709EnsemblClinVar.1
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 PublicationCorresponds to variant dbSNP:rs993022333EnsemblClinVar.1
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:rs1057519713EnsemblClinVar.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.<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 Publications