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P10721

- KIT_HUMAN

UniProt

P10721 - KIT_HUMAN

Protein

Mast/stem cell growth factor receptor Kit

Gene

KIT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 182 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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.4 PublicationsPROSITE-ProRule annotation

    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

    1. ATP binding Source: UniProtKB-KW
    2. cytokine binding Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. protein homodimerization activity Source: UniProtKB
    6. protein tyrosine kinase activity Source: ProtInc
    7. receptor signaling protein tyrosine kinase activity Source: ProtInc
    8. stem cell factor receptor activity Source: Ensembl
    9. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. activation of MAPK activity Source: UniProtKB
    3. cell chemotaxis Source: UniProtKB
    4. cellular response to thyroid hormone stimulus Source: Ensembl
    5. cytokine-mediated signaling pathway Source: UniProtKB
    6. dendritic cell cytokine production Source: UniProtKB
    7. detection of mechanical stimulus involved in sensory perception of sound Source: UniProtKB
    8. digestive tract development Source: UniProtKB
    9. ectopic germ cell programmed cell death Source: Ensembl
    10. embryonic hemopoiesis Source: UniProtKB
    11. epidermal growth factor receptor signaling pathway Source: Reactome
    12. epithelial cell proliferation Source: Ensembl
    13. erythrocyte differentiation Source: UniProtKB
    14. erythropoietin-mediated signaling pathway Source: UniProtKB
    15. Fc-epsilon receptor signaling pathway Source: Reactome
    16. Fc receptor signaling pathway Source: UniProtKB
    17. fibroblast growth factor receptor signaling pathway Source: Reactome
    18. germ cell migration Source: Ensembl
    19. glycosphingolipid metabolic process Source: Ensembl
    20. hemopoiesis Source: UniProtKB
    21. immature B cell differentiation Source: UniProtKB
    22. inflammatory response Source: UniProtKB
    23. innate immune response Source: Reactome
    24. Kit signaling pathway Source: UniProtKB
    25. lamellipodium assembly Source: UniProtKB
    26. lymphoid progenitor cell differentiation Source: Ensembl
    27. male gonad development Source: UniProtKB
    28. mast cell chemotaxis Source: UniProtKB
    29. mast cell cytokine production Source: UniProtKB
    30. mast cell degranulation Source: UniProtKB
    31. mast cell differentiation Source: UniProtKB
    32. mast cell proliferation Source: UniProtKB
    33. megakaryocyte development Source: UniProtKB
    34. melanocyte adhesion Source: UniProtKB
    35. melanocyte differentiation Source: UniProtKB
    36. melanocyte migration Source: UniProtKB
    37. myeloid progenitor cell differentiation Source: Ensembl
    38. negative regulation of programmed cell death Source: Ensembl
    39. neurotrophin TRK receptor signaling pathway Source: Reactome
    40. ovarian follicle development Source: UniProtKB
    41. peptidyl-tyrosine phosphorylation Source: UniProtKB
    42. phosphatidylinositol-mediated signaling Source: Reactome
    43. pigmentation Source: UniProtKB
    44. positive regulation of cell migration Source: Ensembl
    45. positive regulation of cell proliferation Source: Ensembl
    46. positive regulation of gene expression Source: Ensembl
    47. positive regulation of JAK-STAT cascade Source: UniProtKB
    48. positive regulation of long-term neuronal synaptic plasticity Source: Ensembl
    49. positive regulation of MAPK cascade Source: UniProtKB
    50. positive regulation of Notch signaling pathway Source: Ensembl
    51. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    52. positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    53. positive regulation of phospholipase C activity Source: UniProtKB
    54. positive regulation of pseudopodium assembly Source: Ensembl
    55. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    56. positive regulation of tyrosine phosphorylation of Stat1 protein Source: UniProtKB
    57. positive regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
    58. positive regulation of tyrosine phosphorylation of Stat5 protein Source: UniProtKB
    59. protein autophosphorylation Source: UniProtKB
    60. regulation of cell proliferation Source: UniProtKB
    61. regulation of cell shape Source: UniProtKB
    62. regulation of developmental pigmentation Source: Ensembl
    63. signal transduction Source: ProtInc
    64. signal transduction by phosphorylation Source: GOC
    65. somatic stem cell division Source: Ensembl
    66. somatic stem cell maintenance Source: Ensembl
    67. spermatid development Source: Ensembl
    68. spermatogenesis Source: UniProtKB
    69. stem cell differentiation Source: UniProtKB
    70. stem cell maintenance Source: UniProtKB
    71. T cell differentiation Source: UniProtKB
    72. visual learning Source: Ensembl

    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 PI3K/AKT Signaling 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: 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.

    GO - Cellular componenti

    1. acrosomal vesicle Source: Ensembl
    2. cytoplasmic side of plasma membrane Source: Ensembl
    3. external side of plasma membrane Source: Ensembl
    4. extracellular space Source: BHF-UCL
    5. integral component of membrane Source: UniProtKB-KW
    6. mast cell granule Source: GOC
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Piebald trait (PBT) [MIM:172800]: Autosomal dominant genetic developmental abnormality of pigmentation characterized by congenital patches of white skin and hair that lack melanocytes.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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) [MIM:606764]: Common 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.4 Publications
    Note: The gene represented in this entry is involved in disease pathogenesis.
    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.
    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) [MIM:273300]: A 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.
    Note: The gene represented in this entry may be involved in disease pathogenesis.
    Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes.
    Note: 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.

    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.
    Orphaneti98834. Acute myeloblastic leukemia with maturation.
    98829. Acute myeloid leukemia with abnormal bone marrow eosinophils inv(16)(p13q22) or t(16;16)(p13;q22).
    102724. Acute myeloid leukemia with t(8;21)(q22;q22) translocation.
    158799. Aleukemic mast cell leukemia.
    280785. Bullous diffuse cutaneous mastocytosis.
    158796. Classic mast cell leukemia.
    79455. Cutaneous mastocytoma.
    44890. Gastrointestinal stromal tumor.
    158778. Isolated bone marrow mastocytosis.
    158793. Lymphoadenopathic mastocytosis with eosinophilia.
    158772. Nodular urticaria pigmentosa.
    2884. Piebaldism.
    158769. Plaque-form urticaria pigmentosa.
    280794. Pseudoxanthomatous diffuse cutaneous mastocytosis.
    158775. Smouldering systemic mastocytosis.
    98849. Systemic mastocytosis with an associated clonal hematologic non-mast cell lineage disease.
    90389. Telangiectasia macularis eruptiva perstans.
    158766. Typical urticaria pigmentosa.
    PharmGKBiPA30128.

    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 ↔ 971 PublicationPROSITE-ProRule annotation
    Glycosylationi130 – 1301N-linked (GlcNAc...)2 Publications
    Disulfide bondi136 ↔ 1861 PublicationPROSITE-ProRule annotation
    Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi151 ↔ 1831 PublicationPROSITE-ProRule annotation
    Disulfide bondi233 ↔ 2901 PublicationPROSITE-ProRule annotation
    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 ↔ 4911 PublicationPROSITE-ProRule annotation
    Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi486 – 4861N-linked (GlcNAc...)Sequence Analysis
    Modified residuei547 – 5471Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei553 – 5531Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei568 – 5681Phosphotyrosine; by autocatalysis5 Publications
    Modified residuei570 – 5701Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei703 – 7031Phosphotyrosine; by autocatalysis4 Publications
    Modified residuei721 – 7211Phosphotyrosine; by autocatalysis4 Publications
    Modified residuei730 – 7301Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei741 – 7411Phosphoserine; by PKC/PRKCA2 Publications
    Modified residuei746 – 7461Phosphoserine; by PKC/PRKCA2 Publications
    Modified residuei821 – 8211Phosphoserine2 Publications
    Modified residuei823 – 8231Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei891 – 8911Phosphoserine2 Publications
    Modified residuei900 – 9001Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei936 – 9361Phosphotyrosine; by autocatalysis3 Publications
    Modified residuei959 – 9591Phosphoserine3 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

    ArrayExpressiP10721.
    BgeeiP10721.
    CleanExiHS_KIT.
    GenevestigatoriP10721.

    Organism-specific databases

    HPAiCAB003288.
    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
    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. 63 interactions.
    MINTiMINT-146746.
    STRINGi9606.ENSP00000288135.

    Structurei

    Secondary structure

    1
    976
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 414
    Beta strandi44 – 474
    Beta strandi54 – 596
    Beta strandi63 – 7210
    Beta strandi75 – 773
    Beta strandi79 – 868
    Helixi89 – 913
    Beta strandi93 – 997
    Beta strandi104 – 1107
    Beta strandi125 – 1306
    Beta strandi132 – 1343
    Beta strandi146 – 1494
    Beta strandi151 – 1533
    Beta strandi161 – 1655
    Turni166 – 1683
    Beta strandi169 – 1746
    Helixi177 – 1793
    Beta strandi183 – 1886
    Beta strandi193 – 2008
    Beta strandi203 – 2053
    Beta strandi213 – 2153
    Beta strandi219 – 2246
    Beta strandi229 – 23911
    Beta strandi243 – 2486
    Beta strandi258 – 2636
    Beta strandi265 – 2673
    Beta strandi269 – 27911
    Turni282 – 2843
    Beta strandi286 – 2938
    Beta strandi298 – 31013
    Beta strandi312 – 3198
    Beta strandi321 – 3255
    Beta strandi331 – 34111
    Beta strandi344 – 3507
    Beta strandi356 – 3649
    Beta strandi367 – 3693
    Beta strandi372 – 3798
    Helixi384 – 3863
    Beta strandi388 – 3958
    Beta strandi400 – 40910
    Beta strandi411 – 42010
    Helixi422 – 4243
    Beta strandi425 – 43410
    Beta strandi437 – 4448
    Beta strandi458 – 4625
    Beta strandi468 – 4703
    Beta strandi472 – 4798
    Beta strandi485 – 49410
    Beta strandi499 – 5068
    Beta strandi558 – 5647
    Beta strandi567 – 5704
    Turni573 – 5753
    Helixi580 – 5823
    Helixi586 – 5883
    Beta strandi589 – 5979
    Beta strandi599 – 61315
    Beta strandi617 – 6259
    Helixi631 – 64717
    Beta strandi656 – 6605
    Beta strandi662 – 6654
    Beta strandi667 – 6715
    Helixi678 – 6847
    Turni685 – 6884
    Beta strandi757 – 7593
    Helixi760 – 7623
    Helixi766 – 78520
    Beta strandi788 – 7903
    Helixi795 – 7973
    Beta strandi798 – 8014
    Turni802 – 8043
    Beta strandi805 – 8084
    Helixi812 – 8143
    Helixi817 – 8193
    Beta strandi823 – 8264
    Beta strandi829 – 8313
    Helixi833 – 8353
    Helixi838 – 8436
    Helixi848 – 86316
    Turni864 – 8663
    Helixi877 – 8848
    Helixi897 – 90610
    Helixi911 – 9133
    Helixi917 – 93014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    ProteinModelPortaliP10721.
    SMRiP10721. Positions 33-507, 547-931.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10721.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei525 – 54521HelicalSequence AnalysisAdd
    BLAST

    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.
    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. Align

    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

    MRGARGAWDF LCVLLLLLRV QTGSSQPSVS PGEPSPPSIH PGKSDLIVRV    50
    GDEIRLLCTD PGFVKWTFEI LDETNENKQN EWITEKAEAT NTGKYTCTNK 100
    HGLSNSIYVF VRDPAKLFLV DRSLYGKEDN DTLVRCPLTD PEVTNYSLKG 150
    CQGKPLPKDL RFIPDPKAGI MIKSVKRAYH RLCLHCSVDQ EGKSVLSEKF 200
    ILKVRPAFKA VPVVSVSKAS YLLREGEEFT VTCTIKDVSS SVYSTWKREN 250
    SQTKLQEKYN SWHHGDFNYE RQATLTISSA RVNDSGVFMC YANNTFGSAN 300
    VTTTLEVVDK GFINIFPMIN TTVFVNDGEN VDLIVEYEAF PKPEHQQWIY 350
    MNRTFTDKWE DYPKSENESN IRYVSELHLT RLKGTEGGTY TFLVSNSDVN 400
    AAIAFNVYVN TKPEILTYDR LVNGMLQCVA AGFPEPTIDW YFCPGTEQRC 450
    SASVLPVDVQ TLNSSGPPFG KLVVQSSIDS SAFKHNGTVE CKAYNDVGKT 500
    SAYFNFAFKG NNKEQIHPHT LFTPLLIGFV IVAGMMCIIV MILTYKYLQK 550
    PMYEVQWKVV EEINGNNYVY IDPTQLPYDH KWEFPRNRLS FGKTLGAGAF 600
    GKVVEATAYG LIKSDAAMTV AVKMLKPSAH LTEREALMSE LKVLSYLGNH 650
    MNIVNLLGAC TIGGPTLVIT EYCCYGDLLN FLRRKRDSFI CSKQEDHAEA 700
    ALYKNLLHSK ESSCSDSTNE YMDMKPGVSY VVPTKADKRR SVRIGSYIER 750
    DVTPAIMEDD ELALDLEDLL SFSYQVAKGM AFLASKNCIH RDLAARNILL 800
    THGRITKICD FGLARDIKND SNYVVKGNAR LPVKWMAPES IFNCVYTFES 850
    DVWSYGIFLW ELFSLGSSPY PGMPVDSKFY KMIKEGFRML SPEHAPAEMY 900
    DIMKTCWDAD PLKRPTFKQI VQLIEKQISE STNHIYSNLA NCSPNRQKPV 950
    VDHSVRINSV GSTASSSQPL LVHDDV 976
    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.
    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. 1 Publication
    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. 2 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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi125472.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Wikipedia

    CD117 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS3496.1. [P10721-1 ]
    CCDS47058.1. [P10721-2 ]
    PIRi S01426. TVHUKT.
    RefSeqi NP_000213.1. NM_000222.2. [P10721-1 ]
    NP_001087241.1. NM_001093772.1. [P10721-2 ]
    UniGenei Hs.479754.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PKG X-ray 2.90 A/B 549-935 [» ]
    1QZJ model - A 576-932 [» ]
    1QZK model - A 576-932 [» ]
    1R01 model - A 576-932 [» ]
    1T45 X-ray 1.90 A 547-693 [» ]
    1T46 X-ray 1.60 A 565-693 [» ]
    2E9W X-ray 3.50 A/B 26-514 [» ]
    2EC8 X-ray 3.00 A 1-519 [» ]
    2VIF X-ray 1.45 P 564-574 [» ]
    3G0E X-ray 1.60 A 544-693 [» ]
    A 754-935 [» ]
    3G0F X-ray 2.60 A/B 544-693 [» ]
    A/B 754-935 [» ]
    4HVS X-ray 1.90 A 551-934 [» ]
    4K94 X-ray 2.40 C 308-518 [» ]
    4K9E X-ray 2.70 C 308-518 [» ]
    ProteinModelPortali P10721.
    SMRi P10721. Positions 33-507, 547-931.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110015. 44 interactions.
    DIPi DIP-1055N.
    IntActi P10721. 63 interactions.
    MINTi MINT-146746.
    STRINGi 9606.ENSP00000288135.

    Chemistry

    BindingDBi P10721.
    ChEMBLi CHEMBL1936.
    DrugBanki DB01254. Dasatinib.
    DB00619. Imatinib.
    DB00398. Sorafenib.
    DB01268. Sunitinib.
    GuidetoPHARMACOLOGYi 1805.

    PTM databases

    PhosphoSitei P10721.

    Polymorphism databases

    DMDMi 125472.

    Proteomic databases

    MaxQBi P10721.
    PaxDbi P10721.
    PRIDEi P10721.

    Protocols and materials databases

    DNASUi 3815.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000288135 ; ENSP00000288135 ; ENSG00000157404 . [P10721-1 ]
    ENST00000412167 ; ENSP00000390987 ; ENSG00000157404 . [P10721-2 ]
    GeneIDi 3815.
    KEGGi hsa:3815.
    UCSCi uc010igr.3. human. [P10721-1 ]
    uc010igs.3. human. [P10721-2 ]

    Organism-specific databases

    CTDi 3815.
    GeneCardsi GC04P055524.
    HGNCi HGNC:6342. KIT.
    HPAi CAB003288.
    HPA004471.
    MIMi 164920. gene.
    172800. phenotype.
    273300. phenotype.
    601626. phenotype.
    606764. phenotype.
    neXtProti NX_P10721.
    Orphaneti 98834. Acute myeloblastic leukemia with maturation.
    98829. Acute myeloid leukemia with abnormal bone marrow eosinophils inv(16)(p13q22) or t(16;16)(p13;q22).
    102724. Acute myeloid leukemia with t(8;21)(q22;q22) translocation.
    158799. Aleukemic mast cell leukemia.
    280785. Bullous diffuse cutaneous mastocytosis.
    158796. Classic mast cell leukemia.
    79455. Cutaneous mastocytoma.
    44890. Gastrointestinal stromal tumor.
    158778. Isolated bone marrow mastocytosis.
    158793. Lymphoadenopathic mastocytosis with eosinophilia.
    158772. Nodular urticaria pigmentosa.
    2884. Piebaldism.
    158769. Plaque-form urticaria pigmentosa.
    280794. Pseudoxanthomatous diffuse cutaneous mastocytosis.
    158775. Smouldering systemic mastocytosis.
    98849. Systemic mastocytosis with an associated clonal hematologic non-mast cell lineage disease.
    90389. Telangiectasia macularis eruptiva perstans.
    158766. Typical urticaria pigmentosa.
    PharmGKBi PA30128.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000112008.
    HOVERGENi HBG104348.
    InParanoidi P10721.
    KOi K05091.
    OMAi YFCPGTE.
    OrthoDBi EOG7S7SCZ.
    PhylomeDBi P10721.
    TreeFami TF325768.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_111225. Regulation of KIT signaling.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinki P10721.

    Miscellaneous databases

    EvolutionaryTracei P10721.
    GeneWikii CD117.
    GenomeRNAii 3815.
    NextBioi 14995.
    PROi P10721.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10721.
    Bgeei P10721.
    CleanExi HS_KIT.
    Genevestigatori P10721.

    Family and domain databases

    Gene3Di 2.60.40.10. 5 hits.
    InterProi IPR007110. 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 ]
    Pfami PF00047. ig. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500951. SCGF_recepter. 1 hit.
    PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTi SM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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 and adults."
      Bignell G., Smith R., Hunter C., Stephens P., Davies H., Greenman C., Teague J., Butler A., Edkins S., Stevens C., O'meara S., Parker A., Avis T., Barthorpe S., Brackenbury L., Buck G., Clements J., Cole J.
      , Dicks E., Edwards K., Forbes S., Gorton M., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jones D., Kosmidou V., Laman R., Lugg R., Menzies A., Perry J., Petty R., Raine K., Shepherd R., Small A., Solomon H., Stephens Y., Tofts C., Varian J., Webb A., West S., Widaa S., Yates A., Gillis A.J.M., Stoop H.J., van Gurp R.J.H.L.M., Oosterhuis J.W., Looijenga L.H.J., Futreal P.A., Wooster R., Stratton M.R.
      Genes Chromosomes Cancer 45:42-46(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TYR-816; LYS-822 AND PRO-829.
    60. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-532; LEU-541; SER-691; ASN-715; ASN-737; TRP-804; TYR-816; LYS-822 AND PRO-829.

    Entry informationi

    Entry nameiKIT_HUMAN
    AccessioniPrimary (citable) accession number: P10721
    Secondary accession number(s): B5A956
    , D5LXN2, D5M931, F5H8F8, Q6IQ28, Q99662, Q9UM99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 182 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3