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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-Experimental evidence at protein leveli

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

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation4 Publications

Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi568 – 5681Magnesium
Binding sitei623 – 6231ATP
Active sitei792 – 7921Proton acceptorPROSITE-ProRule annotation
Binding sitei796 – 7961ATP
Metal bindingi797 – 7971Magnesium
Metal bindingi810 – 8101Magnesium
Sitei936 – 9361Important for interaction with phosphotyrosine-binding proteins

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi596 – 6038ATP
Nucleotide bindingi671 – 6777ATP

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cytokine binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: UniProtKB
  • protein tyrosine kinase activity Source: ProtInc
  • receptor signaling protein tyrosine kinase activity Source: ProtInc
  • stem cell factor receptor activity Source: Ensembl
  • transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • activation of MAPK activity Source: UniProtKB
  • cell chemotaxis Source: UniProtKB
  • cellular response to thyroid hormone stimulus Source: Ensembl
  • cytokine-mediated signaling pathway Source: UniProtKB
  • dendritic cell cytokine production Source: UniProtKB
  • detection of mechanical stimulus involved in sensory perception of sound Source: UniProtKB
  • digestive tract development Source: UniProtKB
  • ectopic germ cell programmed cell death Source: Ensembl
  • embryonic hemopoiesis Source: UniProtKB
  • epidermal growth factor receptor signaling pathway Source: Reactome
  • epithelial cell proliferation Source: Ensembl
  • erythrocyte differentiation Source: UniProtKB
  • erythropoietin-mediated signaling pathway Source: UniProtKB
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • Fc receptor signaling pathway Source: UniProtKB
  • fibroblast growth factor receptor signaling pathway Source: Reactome
  • germ cell migration Source: Ensembl
  • glycosphingolipid metabolic process Source: Ensembl
  • hemopoiesis Source: UniProtKB
  • immature B cell differentiation Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • innate immune response Source: Reactome
  • Kit signaling pathway Source: UniProtKB
  • lamellipodium assembly Source: UniProtKB
  • lymphoid progenitor cell differentiation Source: Ensembl
  • male gonad development Source: UniProtKB
  • mast cell chemotaxis Source: UniProtKB
  • mast cell cytokine production Source: UniProtKB
  • mast cell degranulation Source: UniProtKB
  • mast cell differentiation Source: UniProtKB
  • mast cell proliferation Source: UniProtKB
  • megakaryocyte development Source: UniProtKB
  • melanocyte adhesion Source: UniProtKB
  • melanocyte differentiation Source: UniProtKB
  • melanocyte migration Source: UniProtKB
  • myeloid progenitor cell differentiation Source: Ensembl
  • negative regulation of programmed cell death Source: Ensembl
  • neurotrophin TRK receptor signaling pathway Source: Reactome
  • ovarian follicle development Source: UniProtKB
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • phosphatidylinositol-mediated signaling Source: Reactome
  • pigmentation Source: UniProtKB
  • positive regulation of cell migration Source: Ensembl
  • positive regulation of cell proliferation Source: Ensembl
  • positive regulation of gene expression Source: Ensembl
  • positive regulation of JAK-STAT cascade Source: UniProtKB
  • positive regulation of long-term neuronal synaptic plasticity Source: Ensembl
  • positive regulation of MAPK cascade Source: UniProtKB
  • positive regulation of Notch signaling pathway Source: Ensembl
  • positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • positive regulation of phospholipase C activity Source: UniProtKB
  • positive regulation of pseudopodium assembly Source: Ensembl
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • positive regulation of tyrosine phosphorylation of Stat1 protein Source: UniProtKB
  • positive regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  • positive regulation of tyrosine phosphorylation of Stat5 protein Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of developmental pigmentation Source: Ensembl
  • signal transduction Source: ProtInc
  • signal transduction by phosphorylation Source: GOC
  • somatic stem cell division Source: Ensembl
  • somatic stem cell maintenance Source: Ensembl
  • spermatid development Source: Ensembl
  • spermatogenesis Source: UniProtKB
  • stem cell differentiation Source: UniProtKB
  • stem cell maintenance Source: UniProtKB
  • T cell differentiation Source: UniProtKB
  • visual learning Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_111225. Regulation of KIT signaling.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_75829. PIP3 activates AKT signaling.
SignaLinkiP10721.

Names & Taxonomyi

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
Gene namesi
Name:KIT
Synonyms:SCFR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:6342. KIT.

Subcellular locationi

Isoform 3 :
  • Cytoplasm

  • Note: Detected in the cytoplasm of spermatozoa, especially in the equatorial and subacrosomal region of the sperm head.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 524499ExtracellularSequence AnalysisAdd
BLAST
Transmembranei525 – 54521HelicalSequence AnalysisAdd
BLAST
Topological domaini546 – 976431CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • acrosomal vesicle Source: Ensembl
  • cell-cell junction Source: Ensembl
  • cytoplasmic side of plasma membrane Source: Ensembl
  • external side of plasma membrane Source: Ensembl
  • extracellular space Source: BHF-UCL
  • integral component of membrane Source: UniProtKB-KW
  • mast cell granule Source: GOC
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti583 – 5831E → K in PBT. 1 Publication
VAR_004104
Natural varianti584 – 5841F → C in PBT. 1 Publication
Corresponds to variant rs28933371 [ dbSNP | Ensembl ].
VAR_033129
Natural varianti584 – 5841F → L in PBT. 1 Publication
VAR_004105
Natural varianti601 – 6011G → R in PBT. 1 Publication
VAR_033130
Natural varianti656 – 6561L → P in PBT. 1 Publication
VAR_033131
Natural varianti664 – 6641G → R in PBT. 1 Publication
VAR_004106
Natural varianti791 – 7911R → G in PBT. 1 Publication
VAR_004107
Natural varianti796 – 7961R → G in PBT; with sensorineural deafness. 1 Publication
VAR_033132
Natural varianti812 – 8121G → V in PBT. 1 Publication
VAR_004108
Natural varianti847 – 8471T → P in PBT. 1 Publication
VAR_033137
Natural varianti893 – 8964Missing in PBT; severe. 1 Publication
VAR_004110
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti550 – 5589Missing in GIST; somatic mutation. 2 Publications
VAR_033124
Natural varianti550 – 5501K → I in GIST; somatic mutation. 1 Publication
Corresponds to variant rs28933968 [ dbSNP | Ensembl ].
VAR_033123
Natural varianti551 – 5555Missing in GIST; somatic mutation. 1 Publication
VAR_033125
Natural varianti559 – 5602Missing in GIST; somatic mutation. 1 Publication
VAR_033128
Natural varianti559 – 5591V → A in GIST. 1 Publication
VAR_033126
Natural varianti559 – 5591V → D in GIST; somatic mutation. 1 Publication
VAR_033127
Natural varianti559 – 5591Missing in GIST. 1 Publication
VAR_007965
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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi381 – 3811R → A: Reduces autophosphorylation in response to KITLG/SCF. 1 Publication
Mutagenesisi386 – 3861E → A: Reduces autophosphorylation in response to KITLG/SCF. 1 Publication
Mutagenesisi571 – 5711I → A: Reduction in SH2B2/APS binding. Abolishes SH2B2/APS binding; when associated with A-939. 1 Publication
Mutagenesisi623 – 6231K → M: Stronger interaction with MPDZ. 1 Publication
Mutagenesisi741 – 7411S → A: Abolishes down-regulation of kinase activity by PKC/PRKCA-mediated phosphorylation; when associated with A-746. 1 Publication
Mutagenesisi746 – 7461S → A: Abolishes down-regulation of kinase activity by PKC/PRKCA-mediated phosphorylation; when associated with A-741. 1 Publication
Mutagenesisi823 – 8231Y → F: No decrease in activity. Leads to autophosphorylation at Tyr-900. 1 Publication
Mutagenesisi939 – 9391L → A: Reduction in SH2B2/APS binding. Abolishes SH2B2/APS binding; when associated with A-571. 1 Publication

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

MIMi172800. phenotype.
273300. phenotype.
601626. phenotype.
606764. phenotype.
Orphaneti98829. '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'.
98834. Acute myeloblastic leukemia with maturation.
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.
158766. Typical urticaria pigmentosa.
PharmGKBiPA30128.

Chemistry

DrugBankiDB01254. Dasatinib.
DB00619. Imatinib.
DB04868. Nilotinib.
DB06589. Pazopanib.
DB08901. Ponatinib.
DB08896. Regorafenib.
DB00398. Sorafenib.
DB01268. Sunitinib.

Polymorphism and mutation databases

BioMutaiKIT.
DMDMi125472.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 976951Mast/stem cell growth factor receptor KitPRO_0000016754Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 ↔ 97PROSITE-ProRule annotation1 Publication
Glycosylationi130 – 1301N-linked (GlcNAc...)2 Publications
Disulfide bondi136 ↔ 186PROSITE-ProRule annotation1 Publication
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi151 ↔ 183PROSITE-ProRule annotation1 Publication
Disulfide bondi233 ↔ 290PROSITE-ProRule annotation1 Publication
Glycosylationi283 – 2831N-linked (GlcNAc...)1 Publication
Glycosylationi293 – 2931N-linked (GlcNAc...)1 Publication
Glycosylationi300 – 3001N-linked (GlcNAc...)1 Publication
Glycosylationi320 – 3201N-linked (GlcNAc...)1 Publication
Glycosylationi352 – 3521N-linked (GlcNAc...)1 Publication
Glycosylationi367 – 3671N-linked (GlcNAc...)1 Publication
Disulfide bondi428 ↔ 491PROSITE-ProRule annotation1 Publication
Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi486 – 4861N-linked (GlcNAc...)Sequence Analysis
Modified residuei547 – 5471Phosphotyrosine; by autocatalysis1 Publication
Modified residuei553 – 5531Phosphotyrosine; by autocatalysis1 Publication
Modified residuei568 – 5681Phosphotyrosine; by autocatalysis4 Publications
Modified residuei570 – 5701Phosphotyrosine; by autocatalysis2 Publications
Modified residuei703 – 7031Phosphotyrosine; by autocatalysis3 Publications
Modified residuei721 – 7211Phosphotyrosine; by autocatalysis3 Publications
Modified residuei730 – 7301Phosphotyrosine; by autocatalysis1 Publication
Modified residuei741 – 7411Phosphoserine; by PKC/PRKCA1 Publication
Modified residuei746 – 7461Phosphoserine; by PKC/PRKCA1 Publication
Modified residuei821 – 8211Phosphoserine1 Publication
Modified residuei823 – 8231Phosphotyrosine; by autocatalysis1 Publication
Modified residuei891 – 8911Phosphoserine1 Publication
Modified residuei900 – 9001Phosphotyrosine; by autocatalysis2 Publications
Modified residuei936 – 9361Phosphotyrosine; by autocatalysis2 Publications
Modified residuei959 – 9591Phosphoserine2 Publications

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

MaxQBiP10721.
PaxDbiP10721.
PRIDEiP10721.

PTM databases

PhosphoSiteiP10721.

Expressioni

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

Inductioni

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

Gene expression databases

BgeeiP10721.
CleanExiHS_KIT.
ExpressionAtlasiP10721. baseline and differential.
GenevestigatoriP10721.

Organism-specific databases

HPAiCAB003288.
CAB068253.
HPA004471.

Interactioni

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.17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005192EBI-1379503,EBI-375543
ABL2P426842EBI-1379503,EBI-1102694
BCAR3O758153EBI-1379503,EBI-702336
BLKP514515EBI-1379503,EBI-2105445
BLNKQ8WV282EBI-1379503,EBI-2623522
CRKP461084EBI-1379503,EBI-886
FESP073322EBI-1379503,EBI-1055635
FGRP097692EBI-1379503,EBI-1383732
GRAP2O757912EBI-1379503,EBI-740418
GRB2P629936EBI-1379503,EBI-401755
GRB7Q144514EBI-1379503,EBI-970191
HCKP086312EBI-1379503,EBI-346340
HSH2DQ96JZ25EBI-1379503,EBI-3919324
KITLGP215832EBI-1379503,EBI-1379527
LCKP062398EBI-1379503,EBI-1348
LYNP079487EBI-1379503,EBI-79452
MpdzQ8VBX64EBI-1379503,EBI-8026435From a different organism.
NCK1P163333EBI-1379503,EBI-389883
NCK2O436392EBI-1379503,EBI-713635
PIK3R1P2798619EBI-1379503,EBI-79464
PIK3R2O0045919EBI-1379503,EBI-346930
PIK3R3Q9256931EBI-1379503,EBI-79893
PLCG1P1917431EBI-1379503,EBI-79387
PLCG2P168858EBI-1379503,EBI-617403
PTK6Q138824EBI-1379503,EBI-1383632
PTPN11Q0612429EBI-1379503,EBI-297779
Ptpn11P352352EBI-1379503,EBI-397236From a different organism.
PTPRUQ927292EBI-1379503,EBI-7052301
RASA1P2093616EBI-1379503,EBI-1026476
SH2B3Q9UQQ22EBI-1379503,EBI-7879749
SH2D1BO147968EBI-1379503,EBI-3923013
SH2D2AQ9NP3110EBI-1379503,EBI-490630
SH2D3CQ8N5H74EBI-1379503,EBI-745980
SH3BP2P783143EBI-1379503,EBI-727062
SHBQ154642EBI-1379503,EBI-4402156
SHC1P293538EBI-1379503,EBI-78835
SHC2P980775EBI-1379503,EBI-7256023
SHC3Q925293EBI-1379503,EBI-79084
SLA2Q9H6Q32EBI-1379503,EBI-1222854
SOCS2O145084EBI-1379503,EBI-617737
SOCS3O145433EBI-1379503,EBI-714146
SOCS6O1454412EBI-1379503,EBI-3929549
SRCP129315EBI-1379503,EBI-621482
STAP1Q9ULZ23EBI-1379503,EBI-6083058
TENC1Q63HR22EBI-1379503,EBI-949753
TNS1Q9HBL02EBI-1379503,EBI-3389814
TNS3Q68CZ25EBI-1379503,EBI-1220488
TXKP426813EBI-1379503,EBI-7877438
YES1P079477EBI-1379503,EBI-515331
ZAP70P434032EBI-1379503,EBI-1211276

Protein-protein interaction databases

BioGridi110015. 44 interactions.
DIPiDIP-1055N.
IntActiP10721. 64 interactions.
MINTiMINT-146746.
STRINGi9606.ENSP00000288135.

Structurei

Secondary structure

1
976
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 414Combined sources
Beta strandi44 – 474Combined sources
Beta strandi54 – 596Combined sources
Beta strandi63 – 7210Combined sources
Beta strandi75 – 773Combined sources
Beta strandi79 – 868Combined sources
Helixi89 – 913Combined sources
Beta strandi93 – 997Combined sources
Beta strandi104 – 1107Combined sources
Beta strandi125 – 1306Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi146 – 1494Combined sources
Beta strandi151 – 1533Combined sources
Beta strandi161 – 1655Combined sources
Turni166 – 1683Combined sources
Beta strandi169 – 1746Combined sources
Helixi177 – 1793Combined sources
Beta strandi183 – 1886Combined sources
Beta strandi193 – 2008Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi213 – 2153Combined sources
Beta strandi219 – 2246Combined sources
Beta strandi229 – 23911Combined sources
Beta strandi243 – 2486Combined sources
Beta strandi258 – 2636Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi269 – 27911Combined sources
Turni282 – 2843Combined sources
Beta strandi286 – 2938Combined sources
Beta strandi298 – 31013Combined sources
Beta strandi312 – 3198Combined sources
Beta strandi321 – 3255Combined sources
Beta strandi331 – 34111Combined sources
Beta strandi344 – 3507Combined sources
Beta strandi356 – 3649Combined sources
Beta strandi367 – 3693Combined sources
Beta strandi372 – 3798Combined sources
Helixi384 – 3863Combined sources
Beta strandi388 – 3958Combined sources
Beta strandi400 – 40910Combined sources
Beta strandi411 – 42010Combined sources
Helixi422 – 4243Combined sources
Beta strandi425 – 43410Combined sources
Beta strandi437 – 4448Combined sources
Beta strandi458 – 4625Combined sources
Beta strandi468 – 4703Combined sources
Beta strandi472 – 4798Combined sources
Beta strandi485 – 49410Combined sources
Beta strandi499 – 5068Combined sources
Beta strandi558 – 5647Combined sources
Beta strandi567 – 5704Combined sources
Turni573 – 5753Combined sources
Helixi580 – 5823Combined sources
Helixi586 – 5883Combined sources
Beta strandi589 – 5979Combined sources
Beta strandi599 – 61315Combined sources
Beta strandi617 – 6259Combined sources
Helixi631 – 64717Combined sources
Beta strandi656 – 6605Combined sources
Beta strandi662 – 6654Combined sources
Beta strandi667 – 6715Combined sources
Helixi678 – 6847Combined sources
Turni685 – 6884Combined sources
Beta strandi757 – 7593Combined sources
Helixi760 – 7623Combined sources
Helixi766 – 78520Combined sources
Beta strandi788 – 7903Combined sources
Helixi795 – 7973Combined sources
Beta strandi798 – 8014Combined sources
Turni802 – 8043Combined sources
Beta strandi805 – 8084Combined sources
Helixi812 – 8143Combined sources
Helixi817 – 8193Combined sources
Beta strandi823 – 8253Combined sources
Beta strandi827 – 8315Combined sources
Helixi833 – 8353Combined sources
Helixi838 – 8436Combined sources
Helixi848 – 86316Combined sources
Turni864 – 8663Combined sources
Helixi877 – 8859Combined sources
Helixi897 – 90610Combined sources
Helixi911 – 9133Combined sources
Helixi917 – 93014Combined sources
Turni931 – 9333Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PKGX-ray2.90A/B549-935[»]
1QZJmodel-A576-932[»]
1QZKmodel-A576-932[»]
1R01model-A576-932[»]
1T45X-ray1.90A547-693[»]
1T46X-ray1.60A565-693[»]
2E9WX-ray3.50A/B26-514[»]
2EC8X-ray3.00A1-519[»]
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[»]
ProteinModelPortaliP10721.
SMRiP10721. Positions 33-507, 547-933.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10721.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 11286Ig-like C2-type 1Add
BLAST
Domaini121 – 20585Ig-like C2-type 2Add
BLAST
Domaini212 – 30897Ig-like C2-type 3Add
BLAST
Domaini317 – 41094Ig-like C2-type 4Add
BLAST
Domaini413 – 50795Ig-like C2-type 5Add
BLAST
Domaini589 – 937349Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni568 – 5703Important for interaction with phosphotyrosine-binding proteins

Sequence similaritiesi

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

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000112008.
HOVERGENiHBG104348.
InParanoidiP10721.
KOiK05091.
OMAiYFCPGTE.
OrthoDBiEOG7S7SCZ.
PhylomeDBiP10721.
TreeFamiTF325768.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
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.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500951. SCGF_recepter. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P10721-1) [UniParc]FASTAAdd to basket

Also known as: GNNK(+), Kit(+)

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
Checksum:i81B0CD76817F3454
GO
Isoform 2 (identifier: P10721-2) [UniParc]FASTAAdd to basket

Also known as: GNNK(-), KitA(+)

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti764 – 7641L → I in AAH71593 (PubMed:15489334).Curated
Sequence conflicti838 – 8381P → H in AAH71593 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti532 – 5321V → I.1 Publication
Corresponds to variant rs55792975 [ dbSNP | Ensembl ].
VAR_042021
Natural varianti541 – 5411M → L.1 Publication
Corresponds to variant rs3822214 [ dbSNP | Ensembl ].
VAR_042022
Natural varianti541 – 5411M → V.
Corresponds to variant rs3822214 [ dbSNP | Ensembl ].
VAR_061289
Natural varianti550 – 5589Missing in GIST; somatic mutation. 2 Publications
VAR_033124
Natural varianti550 – 5501K → I in GIST; somatic mutation. 1 Publication
Corresponds to variant rs28933968 [ dbSNP | Ensembl ].
VAR_033123
Natural varianti551 – 5555Missing in GIST; somatic mutation. 1 Publication
VAR_033125
Natural varianti559 – 5602Missing in GIST; somatic mutation. 1 Publication
VAR_033128
Natural varianti559 – 5591V → A in GIST. 1 Publication
VAR_033126
Natural varianti559 – 5591V → D in GIST; somatic mutation. 1 Publication
VAR_033127
Natural varianti559 – 5591Missing in GIST. 1 Publication
VAR_007965
Natural varianti583 – 5831E → K in PBT. 1 Publication
VAR_004104
Natural varianti584 – 5841F → C in PBT. 1 Publication
Corresponds to variant rs28933371 [ dbSNP | Ensembl ].
VAR_033129
Natural varianti584 – 5841F → L in PBT. 1 Publication
VAR_004105
Natural varianti601 – 6011G → R in PBT. 1 Publication
VAR_033130
Natural varianti656 – 6561L → P in PBT. 1 Publication
VAR_033131
Natural varianti664 – 6641G → R in PBT. 1 Publication
VAR_004106
Natural varianti691 – 6911C → S.1 Publication
Corresponds to variant rs35200131 [ dbSNP | Ensembl ].
VAR_042023
Natural varianti715 – 7151S → N.1 Publication
Corresponds to variant rs56094246 [ dbSNP | Ensembl ].
VAR_042024
Natural varianti737 – 7371D → N in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042025
Natural varianti791 – 7911R → G in PBT. 1 Publication
VAR_004107
Natural varianti796 – 7961R → G in PBT; with sensorineural deafness. 1 Publication
VAR_033132
Natural varianti804 – 8041R → W in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042026
Natural varianti812 – 8121G → V in PBT. 1 Publication
VAR_004108
Natural varianti816 – 8161D → F in mastocytosis; requires 2 nucleotide substitutions; somatic mutation; constitutively activated and is much more rapidly autophosphorylated than wild type. 1 Publication
VAR_033133
Natural varianti816 – 8161D → H in a testicular tumor; seminoma; somatic mutation; constitutively activated. 3 Publications
Corresponds to variant rs28933969 [ dbSNP | Ensembl ].
VAR_033134
Natural varianti816 – 8161D → V in mast cell leukemia and mastocytosis; somatic mutation; constitutively activated; loss of interaction with MPDZ. 7 Publications
VAR_004109
Natural varianti816 – 8161D → Y in acute myeloid leukemia, mastocytosis and a germ cell tumor of the testis; somatic mutation; constitutively activated. 4 Publications
VAR_023828
Natural varianti820 – 8201D → G in mast cell disease; systemic. 1 Publication
VAR_033135
Natural varianti822 – 8221N → K in a germ cell tumor of the testis; somatic mutation. 2 Publications
VAR_023829
Natural varianti829 – 8291A → P in a germ cell tumor of the testis; somatic mutation. 2 Publications
VAR_023830
Natural varianti839 – 8391E → K in mastocytosis; somatic mutation; dominant negative mutation; loss of autophosphorylation. 1 Publication
VAR_033136
Natural varianti847 – 8471T → P in PBT. 1 Publication
VAR_033137
Natural varianti893 – 8964Missing in PBT; severe. 1 Publication
VAR_004110

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei412 – 4132KP → SL in isoform 3. 1 PublicationVSP_041866
Alternative sequencei414 – 976563Missing in isoform 3. 1 PublicationVSP_041867Add
BLAST
Alternative sequencei510 – 5134Missing in isoform 2. 3 PublicationsVSP_038385

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.

Genome annotation databases

EnsembliENST00000288135; ENSP00000288135; ENSG00000157404. [P10721-1]
ENST00000412167; ENSP00000390987; ENSG00000157404. [P10721-2]
GeneIDi3815.
KEGGihsa:3815.
UCSCiuc010igr.3. human. [P10721-1]
uc010igs.3. human. [P10721-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

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:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PKGX-ray2.90A/B549-935[»]
1QZJmodel-A576-932[»]
1QZKmodel-A576-932[»]
1R01model-A576-932[»]
1T45X-ray1.90A547-693[»]
1T46X-ray1.60A565-693[»]
2E9WX-ray3.50A/B26-514[»]
2EC8X-ray3.00A1-519[»]
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[»]
ProteinModelPortaliP10721.
SMRiP10721. Positions 33-507, 547-933.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110015. 44 interactions.
DIPiDIP-1055N.
IntActiP10721. 64 interactions.
MINTiMINT-146746.
STRINGi9606.ENSP00000288135.

Chemistry

BindingDBiP10721.
ChEMBLiCHEMBL1936.
DrugBankiDB01254. Dasatinib.
DB00619. Imatinib.
DB04868. Nilotinib.
DB06589. Pazopanib.
DB08901. Ponatinib.
DB08896. Regorafenib.
DB00398. Sorafenib.
DB01268. Sunitinib.
GuidetoPHARMACOLOGYi1805.

PTM databases

PhosphoSiteiP10721.

Polymorphism and mutation databases

BioMutaiKIT.
DMDMi125472.

Proteomic databases

MaxQBiP10721.
PaxDbiP10721.
PRIDEiP10721.

Protocols and materials databases

DNASUi3815.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000288135; ENSP00000288135; ENSG00000157404. [P10721-1]
ENST00000412167; ENSP00000390987; ENSG00000157404. [P10721-2]
GeneIDi3815.
KEGGihsa:3815.
UCSCiuc010igr.3. human. [P10721-1]
uc010igs.3. human. [P10721-2]

Organism-specific databases

CTDi3815.
GeneCardsiGC04P055524.
HGNCiHGNC:6342. KIT.
HPAiCAB003288.
CAB068253.
HPA004471.
MIMi164920. gene.
172800. phenotype.
273300. phenotype.
601626. phenotype.
606764. phenotype.
neXtProtiNX_P10721.
Orphaneti98829. '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'.
98834. Acute myeloblastic leukemia with maturation.
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.
158766. Typical urticaria pigmentosa.
PharmGKBiPA30128.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000112008.
HOVERGENiHBG104348.
InParanoidiP10721.
KOiK05091.
OMAiYFCPGTE.
OrthoDBiEOG7S7SCZ.
PhylomeDBiP10721.
TreeFamiTF325768.

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_111225. Regulation of KIT signaling.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_75829. PIP3 activates AKT signaling.
SignaLinkiP10721.

Miscellaneous databases

ChiTaRSiKIT. human.
EvolutionaryTraceiP10721.
GeneWikiiCD117.
GenomeRNAii3815.
NextBioi14995.
PROiP10721.
SOURCEiSearch...

Gene expression databases

BgeeiP10721.
CleanExiHS_KIT.
ExpressionAtlasiP10721. baseline and differential.
GenevestigatoriP10721.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
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.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view]
PfamiPF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500951. SCGF_recepter. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human proto-oncogene c-kit: a new cell surface receptor tyrosine kinase for an unidentified ligand."
    Yarden Y., Kuang W.-J., Yang-Feng T., Coussens L., Munemitsu S., Dull T.J., Chen E., Schlessinger J., Francke U., Ullrich A.
    EMBO J. 6:3341-3351(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Fetal brain and Term placenta.
  2. "Organization and nucleotide sequence of the human KIT (mast/stem cell growth factor receptor) proto-oncogene."
    Giebel L.B., Strunk K.M., Holmes S.A., Spritz R.A.
    Oncogene 7:2207-2217(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
  3. "Sequence analysis of two genomic regions containing the KIT and the FMS receptor tyrosine kinase genes."
    Andre C., Hampe A., Lachaume P., Martin E., Wang X.P., Manus V., Hu W.X., Galibert F.
    Genomics 39:216-226(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
    Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
    Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  5. "Retinoic acid enhances sensitivity of neuroblastoma cells for imatinib mesylate."
    Neumann I., Foell J.L., Bremer M., Volkmer I., Korholz D., Burdach S., Staege M.S.
    Pediatr. Blood Cancer 55:464-470(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, INDUCTION.
  6. "Sequence of KIT mRNA from all-trans retinoic acid treated neuroblastoma cell lines."
    Staege M.S., Neumann I., Volkmer I.
    Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Trachea.
  8. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  10. "Characterization of the promoter region of the human c-kit proto-oncogene."
    Yamamoto K., Tojo A., Aoki N., Shibuya M.
    Jpn. J. Cancer Res. 84:1136-1144(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
  11. "Modulation of Kit/stem cell factor receptor-induced signaling by protein kinase C."
    Blume-Jensen P., Ronnstrand L., Gout I., Waterfield M.D., Heldin C.H.
    J. Biol. Chem. 269:21793-21802(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PIK3R1; RAF1 AND MAPK1, INTERACTION WITH GRB2; PIK3R1 AND PIK3 CATALYTIC SUBUNIT, ENZYME REGULATION, PHOSPHORYLATION.
  12. "Identification of the major phosphorylation sites for protein kinase C in kit/stem cell factor receptor in vitro and in intact cells."
    Blume-Jensen P., Wernstedt C., Heldin C.H., Ronnstrand L.
    J. Biol. Chem. 270:14192-14200(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-741; SER-746; SER-821 AND SER-959, ENZYME REGULATION, PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF SER-741 AND SER-746.
  13. "Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes."
    Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.
    J. Biol. Chem. 272:5915-5920(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIK3R1; MATK/CHK; FYN AND SHC1, PHOSPHORYLATION AT TYR-568; TYR-570 AND TYR-721.
  14. "Lyn associates with the juxtamembrane region of c-Kit and is activated by stem cell factor in hematopoietic cell lines and normal progenitor cells."
    Linnekin D., DeBerry C.S., Mou S.
    J. Biol. Chem. 272:27450-27455(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LYN.
  15. "SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain."
    Kozlowski M., Larose L., Lee F., Le D.M., Rottapel R., Siminovitch K.A.
    Mol. Cell. Biol. 18:2089-2099(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPN6, AUTOPHOSPHORYLATION, FUNCTION IN PHOSPHORYLATION OF PTPN6.
  16. "Identification of Tyr-703 and Tyr-936 as the primary association sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor."
    Thommes K., Lennartsson J., Carlberg M., Ronnstrand L.
    Biochem. J. 341:211-216(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRB2 AND GRB7, PARTIAL PROTEIN SEQUENCE, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-703 AND TYR-936.
  17. "The receptor protein tyrosine phosphatase, PTP-RO, is upregulated during megakaryocyte differentiation and is associated with the c-Kit receptor."
    Taniguchi Y., London R., Schinkmann K., Jiang S., Avraham H.
    Blood 94:539-549(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTPRU, FUNCTION IN PHOSPHORYLATION OF PTPRU.
  18. "The direct association of the multiple PDZ domain containing proteins (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase activity."
    Mancini A., Koch A., Stefan M., Niemann H., Tamura T.
    FEBS Lett. 482:54-58(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MPDZ, CHARACTERIZATION OF VARIANT VAL-816, MUTAGENESIS OF LYS-623.
  19. "Phosphatidylinositol 3-kinase and Src family kinases are required for phosphorylation and membrane recruitment of Dok-1 in c-Kit signaling."
    Liang X., Wisniewski D., Strife A., Shivakrupa R., Clarkson B., Resh M.D.
    J. Biol. Chem. 277:13732-13738(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LYN; TEC AND DOK1.
  20. "The adapter protein APS associates with the multifunctional docking sites Tyr-568 and Tyr-936 in c-Kit."
    Wollberg P., Lennartsson J., Gottfridsson E., Yoshimura A., Ronnstrand L.
    Biochem. J. 370:1033-1038(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SH2B2/APS, FUNCTION IN PHOSPHORYLATION OF SH2B2/APS, MUTAGENESIS OF ILE-571 AND LEU-939.
  21. "Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent phosphorylation site mediating interaction with c-Crk."
    Lennartsson J., Wernstedt C., Engstrom U., Hellman U., Ronnstrand L.
    Exp. Cell Res. 288:110-118(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-891 AND TYR-900, PARTIAL PROTEIN SEQUENCE, INTERACTION WITH CRK AND PIK3R1, FUNCTION IN PHOSPHORYLATION OF CRK; AKT1 AND MAP KINASES, IDENTIFICATION BY MASS SPECTROMETRY.
  22. "Src family kinases are involved in the differential signaling from two splice forms of c-Kit."
    Voytyuk O., Lennartsson J., Mogi A., Caruana G., Courtneidge S., Ashman L.K., Ronnstrand L.
    J. Biol. Chem. 278:9159-9166(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE SPLICING.
  23. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130.
    Tissue: Plasma.
  24. "The tyrosine kinase FES is an essential effector of KITD816V proliferation signal."
    Voisset E., Lopez S., Dubreuil P., De Sepulveda P.
    Blood 110:2593-2599(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FES/FPS, CHARACTERIZATION OF VARIANT VAL-816.
  25. "Grb2 mediates negative regulation of stem cell factor receptor/c-Kit signaling by recruitment of Cbl."
    Sun J., Pedersen M., Bengtsson S., Ronnstrand L.
    Exp. Cell Res. 313:3935-3942(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRB2 AND CBL, UBIQUITINATION, FUNCTION IN PHOSPHORYLATION OF CBL.
  26. "The D816V mutation of c-Kit circumvents a requirement for Src family kinases in c-Kit signal transduction."
    Sun J., Pedersen M., Ronnstrand L.
    J. Biol. Chem. 284:11039-11047(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF SIGNALING PATHWAYS AND CELL SURVIVAL, FUNCTION IN PHOSPHORYLATION OF CBL, PHOSPHORYLATION AT TYR-568; TYR-703; TYR-721 AND TYR-936, UBIQUITINATION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT VAL-816.
  27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-959, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Expression of a truncated form of KIT tyrosine kinase in human spermatozoa correlates with sperm DNA integrity."
    Muciaccia B., Sette C., Paronetto M.P., Barchi M., Pensini S., D'Agostino A., Gandini L., Geremia R., Stefanini M., Rossi P.
    Hum. Reprod. 25:2188-2202(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  29. "Function of activation loop tyrosine phosphorylation in the mechanism of c-Kit auto-activation and its implication in sunitinib resistance."
    DiNitto J.P., Deshmukh G.D., Zhang Y., Jacques S.L., Coli R., Worrall J.W., Diehl W., English J.M., Wu J.C.
    J. Biochem. 147:601-609(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-547; TYR-553; TYR-703; TYR-721; TYR-730; TYR-823 AND TYR-900, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF TYR-823, CHARACTERIZATION OF VARIANT HIS-816.
  30. "Mechanism of activation of human c-KIT kinase by internal tandem duplications of the juxtamembrane domain and point mutations at aspartic acid 816."
    Kim S.Y., Kang J.J., Lee H.H., Kang J.J., Kim B., Kim C.G., Park T.K., Kang H.
    Biochem. Biophys. Res. Commun. 410:224-228(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, SUBUNIT, CHARACTERIZATION OF VARIANT VAL-816.
  31. "Mechanisms of STAT protein activation by oncogenic KIT mutants in neoplastic mast cells."
    Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.
    J. Biol. Chem. 286:5956-5966(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION AND PHOSPHORYLATION OF STAT1; STAT3; STAT5A AND STAT5B.
  32. "Signal transduction via the stem cell factor receptor/c-Kit."
    Ronnstrand L.
    Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  33. "Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor."
    Roskoski R. Jr.
    Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON KIT SIGNALING.
  34. "Normal and oncogenic forms of the receptor tyrosine kinase kit."
    Lennartsson J., Jelacic T., Linnekin D., Shivakrupa R.
    Stem Cells 23:16-43(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  35. "Regulation of hematopoietic stem cells by the steel factor/KIT signaling pathway."
    Kent D., Copley M., Benz C., Dykstra B., Bowie M., Eaves C.
    Clin. Cancer Res. 14:1926-1930(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  36. "Tumor-intrinsic and -extrinsic roles of c-Kit: mast cells as the primary off-target of tyrosine kinase inhibitors."
    Pittoni P., Piconese S., Tripodo C., Colombo M.P.
    Oncogene 30:757-769(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  37. "Structure of a c-kit product complex reveals the basis for kinase transactivation."
    Mol C.D., Lim K.B., Sridhar V., Zou H., Chien E.Y., Sang B.C., Nowakowski J., Kassel D.B., Cronin C.N., McRee D.E.
    J. Biol. Chem. 278:31461-31464(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 549-931 IN COMPLEX WITH ADP AND MAGNESIUM IONS, SUBUNIT, PHOSPHORYLATION AT TYR-568 AND TYR-570, IDENTIFICATION BY MASS SPECTROMETRY.
  38. "Structural basis for the autoinhibition and STI-571 inhibition of c-Kit tyrosine kinase."
    Mol C.D., Dougan D.R., Schneider T.R., Skene R.J., Kraus M.L., Scheibe D.N., Snell G.P., Zou H., Sang B.C., Wilson K.P.
    J. Biol. Chem. 279:31655-31663(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 565-935 IN COMPLEXES WITH INHIBITOR IMATINIB AND PHOSPHATE, ENZYME REGULATION.
  39. "Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor."
    Yuzawa S., Opatowsky Y., Zhang Z., Mandiyan V., Lax I., Schlessinger J.
    Cell 130:323-334(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-519 IN COMPLEX WITH KITLG/SCF, INTERACTION WITH KITLG/SCF, SUBUNIT, DISULFIDE BONDS, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF ARG-381 AND GLU-386, GLYCOSYLATION AT ASN-130; ASN-283; ASN-293; ASN-300; ASN-320; ASN-352 AND ASN-367.
  40. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 544-935 IN COMPLEX WITH SUNITINIB, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, CHARACTERIZATION OF VARIANTS HIS-816 AND VAL-816, ENZYME REGULATION.
  41. "Structural basis for c-KIT inhibition by the suppressor of cytokine signaling 6 (SOCS6) ubiquitin ligase."
    Zadjali F., Pike A.C., Vesterlund M., Sun J., Wu C., Li S.S., Ronnstrand L., Knapp S., Bullock A.N., Flores-Morales A.
    J. Biol. Chem. 286:480-490(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 564-574 IN COMPLEX WITH SOCS6, PHOSPHORYLATION AT TYR-568.
  42. "Human piebald trait resulting from a dominant negative mutant allele of the c-kit membrane receptor gene."
    Fleischman R.A.
    J. Clin. Invest. 89:1713-1717(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PBT LYS-583.
  43. "Dominant negative and loss of function mutations of the c-kit (mast/stem cell growth factor receptor) proto-oncogene in human piebaldism."
    Spritz R.A., Giebel L.B., Holmes S.A.
    Am. J. Hum. Genet. 50:261-269(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PBT LEU-584.
  44. "Mutation of the KIT (mast/stem cell growth factor receptor) protooncogene in human piebaldism."
    Giebel L.B., Spritz R.A.
    Proc. Natl. Acad. Sci. U.S.A. 88:8696-8699(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PBT ARG-664.
  45. "Identification of mutations in the coding sequence of the proto-oncogene c-kit in a human mast cell leukemia cell line causing ligand-independent activation of c-kit product."
    Furitsu T., Tsujimura T., Tono T., Ikeda H., Kitayama H., Koshimizu U., Sugahara H., Butterfield J.H., Ashman L.K., Kanayama Y., Matsuzawa Y., Kitamura Y., Kanakura Y.
    J. Clin. Invest. 92:1736-1744(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MAST CELL LEUKEMIA VAL-816.
  46. "Novel mutations of the KIT (mast/stem cell growth factor receptor) proto-oncogene in human piebaldism."
    Spritz R.A., Holmes S.A., Itin P., Kuester W.
    J. Invest. Dermatol. 101:22-25(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PBT GLY-791 AND VAL-812.
  47. "A 12-bp deletion (7818del12) in the c-kit protooncogene in a large Italian kindred with piebaldism."
    Riva P., Milani N., Gandolfi P., Larizza L.
    Hum. Mutat. 6:343-345(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PBT 893-GLU--PRO-896 DEL.
  48. Cited for: VARIANT MAST CELL DISEASE GLY-820.
  49. "Piebaldism with deafness: molecular evidence for an expanded syndrome."
    Spritz R.A., Beighton P.
    Am. J. Med. Genet. 75:101-103(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PBT GLY-796.
  50. "c-kit activating mutations and mast cell proliferation in human leukemia."
    Beghini A., Larizza L., Cairoli R., Morra E.
    Blood 92:701-702(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ACUTE MYELOID LEUKEMIA TYR-816.
  51. "A novel KIT gene missense mutation in a Japanese family with piebaldism."
    Nomura K., Hatayama I., Narita T., Kaneko T., Shiraishi M.
    J. Invest. Dermatol. 111:337-338(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PBT PRO-847.
  52. Cited for: VARIANT GIST VAL-559 DEL.
  53. Cited for: VARIANTS GIST ILE-550; 550-LYS--LYS-558 DEL; 551-PRO--VAL-555 DEL; ASP-559 AND 559-VAL-VAL-560 DEL.
  54. "Activating c-kit gene mutations in human germ cell tumors."
    Tian Q., Frierson H.F. Jr., Krystal G.W., Moskaluk C.A.
    Am. J. Pathol. 154:1643-1647(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIS-816, CHARACTERIZATION OF VARIANT HIS-816.
  55. "Activating and dominant inactivating c-KIT catalytic domain mutations in distinct clinical forms of human mastocytosis."
    Longley B.J. Jr., Metcalfe D.D., Tharp M., Wang X., Tyrrell L., Lu S.-Z., Heitjan D., Ma Y.
    Proc. Natl. Acad. Sci. U.S.A. 96:1609-1614(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MASTOCYTOSIS VAL-816; PHE-816; TYR-816 AND LYS-839, CHARACTERIZATION OF VARIANTS MASTOCYTOSIS VAL-816; PHE-816; TYR-816 AND LYS-839.
  56. "Three novel mutations of the proto-oncogene KIT cause human piebaldism."
    Syrris P., Malik N.M., Murday V.A., Patton M.A., Carter N.D., Hughes H.E., Metcalfe K.
    Am. J. Med. Genet. 95:79-81(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PBT CYS-584; ARG-601 AND PRO-656.
  57. "Germline mutation in the juxtamembrane domain of the kit gene in a family with gastrointestinal stromal tumors and urticaria pigmentosa."
    Beghini A., Tibiletti M.G., Roversi G., Chiaravalli A.M., Serio G., Capella C., Larizza L.
    Cancer 92:657-662(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GIST ALA-559.
  58. "A mutation-created novel intra-exonic pre-mRNA splice site causes constitutive activation of KIT in human gastrointestinal stromal tumors."
    Chen L.L., Sabripour M., Wu E.F., Prieto V.G., Fuller G.N., Frazier M.L.
    Oncogene 24:4271-4280(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GIST 550-LYS--LYS-558 DEL.
  59. "Sequence analysis of the protein kinase gene family in human testicular germ-cell tumors of adolescents an