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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)DescriptionActionsGraphical viewLength
Metal bindingi568Magnesium1
Binding sitei623ATP1
Active sitei792Proton acceptorPROSITE-ProRule annotation1
Binding sitei796ATP1
Metal bindingi797Magnesium1
Metal bindingi810Magnesium1
Sitei936Important for interaction with phosphotyrosine-binding proteins1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi596 – 603ATP8
Nucleotide bindingi671 – 677ATP7

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cytokine binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
  • protein homodimerization activity Source: UniProtKB
  • protein tyrosine kinase activity Source: ProtInc
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome
  • 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
  • epithelial cell proliferation Source: Ensembl
  • erythrocyte differentiation Source: UniProtKB
  • erythropoietin-mediated signaling pathway Source: UniProtKB
  • Fc receptor signaling pathway Source: UniProtKB
  • germ cell migration Source: Ensembl
  • glycosphingolipid metabolic process Source: Ensembl
  • hematopoietic stem cell migration Source: Ensembl
  • hemopoiesis Source: UniProtKB
  • immature B cell differentiation Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • Kit signaling pathway Source: UniProtKB
  • lamellipodium assembly Source: UniProtKB
  • lymphoid progenitor cell differentiation Source: Ensembl
  • male gonad development Source: UniProtKB
  • MAPK cascade Source: Reactome
  • 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
  • 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
  • positive regulation of vascular smooth muscle cell differentiation Source: BHF-UCL
  • protein autophosphorylation Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of developmental pigmentation Source: Ensembl
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • signal transduction Source: ProtInc
  • somatic stem cell division Source: Ensembl
  • somatic stem cell population maintenance Source: Ensembl
  • spermatid development Source: Ensembl
  • spermatogenesis Source: UniProtKB
  • stem cell differentiation Source: UniProtKB
  • stem cell population 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

BioCyciZFISH:HS08211-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-1433559. Regulation of KIT signaling.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8866910. TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
SignaLinkiP10721.
SIGNORiP10721.

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
Proteomesi
  • UP000005640 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)DescriptionActionsGraphical viewLength
Topological domaini26 – 524ExtracellularSequence analysisAdd BLAST499
Transmembranei525 – 545HelicalSequence analysisAdd BLAST21
Topological domaini546 – 976CytoplasmicSequence analysisAdd BLAST431

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_004104583E → K in PBT. 1 PublicationCorresponds to variant rs121913680dbSNPEnsembl.1
Natural variantiVAR_033129584F → C in PBT. 1 PublicationCorresponds to variant rs28933371dbSNPEnsembl.1
Natural variantiVAR_004105584F → L in PBT. 1 PublicationCorresponds to variant rs794726671dbSNPEnsembl.1
Natural variantiVAR_033130601G → R in PBT. 1 Publication1
Natural variantiVAR_033131656L → P in PBT. 1 Publication1
Natural variantiVAR_004106664G → R in PBT. 1 PublicationCorresponds to variant rs121913679dbSNPEnsembl.1
Natural variantiVAR_004107791R → G in PBT. 1 Publication1
Natural variantiVAR_033132796R → G in PBT; with sensorineural deafness. 1 PublicationCorresponds to variant rs121913684dbSNPEnsembl.1
Natural variantiVAR_004108812G → V in PBT. 1 Publication1
Natural variantiVAR_033137847T → P in PBT. 1 PublicationCorresponds to variant rs121913687dbSNPEnsembl.1
Natural variantiVAR_004110893 – 896Missing in PBT; severe. 1 Publication4
Gastrointestinal stromal tumor (GIST)4 Publications
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionCommon mesenchymal neoplasms arising in the gastrointestinal tract, most often in the stomach. They are histologically, immunohistochemically, and genetically different from typical leiomyomas, leiomyosarcomas, and schwannomas. Most GISTs are composed of a fairly uniform population of spindle-shaped cells. Some tumors are dominated by epithelioid cells or contain a mixture of spindle and epithelioid morphologies. Primary GISTs in the gastrointestinal tract commonly metastasize in the omentum and mesenteries, often as multiple nodules. However, primary tumors may also occur outside of the gastrointestinal tract, in other intra-abdominal locations, especially in the omentum and mesentery.
See also OMIM:606764
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_033124550 – 558Missing in GIST; somatic mutation. 2 Publications9
Natural variantiVAR_033123550K → I in GIST; somatic mutation. 1 PublicationCorresponds to variant rs28933968dbSNPEnsembl.1
Natural variantiVAR_033125551 – 555Missing in GIST; somatic mutation. 1 Publication5
Natural variantiVAR_033128559 – 560Missing in GIST; somatic mutation. 1 Publication2
Natural variantiVAR_033126559V → A in GIST. 1 PublicationCorresponds to variant rs121913517dbSNPEnsembl.1
Natural variantiVAR_033127559V → D in GIST; somatic mutation. 1 PublicationCorresponds to variant rs121913517dbSNPEnsembl.1
Natural variantiVAR_007965559Missing in GIST. 1 Publication1
Testicular germ cell tumor (TGCT)
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma.
See also OMIM:273300
Leukemia, acute myelogenous (AML)
The gene represented in this entry is involved in disease pathogenesis. Somatic mutations that lead to constitutive activation of KIT are detected in AML patients. These mutations fall into two classes, the most common being in-frame internal tandem duplications of variable length in the juxtamembrane region that disrupt the normal regulation of the kinase activity. Likewise, point mutations in the kinase domain can result in a constitutively activated kinase.
Disease descriptionA subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes.
See also OMIM:601626

Mutagenesis

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

Keywords - Diseasei

Disease mutation, Proto-oncogene

Organism-specific databases

DisGeNETi3815.
MalaCardsiKIT.
MIMi172800. phenotype.
273300. phenotype.
601626. phenotype.
606764. phenotype.
OpenTargetsiENSG00000157404.
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 databases

ChEMBLiCHEMBL1936.
DrugBankiDB01254. Dasatinib.
DB00619. Imatinib.
DB09078. Lenvatinib.
DB04868. Nilotinib.
DB06589. Pazopanib.
DB08901. Ponatinib.
DB08896. Regorafenib.
DB00398. Sorafenib.
DB01268. Sunitinib.
GuidetoPHARMACOLOGYi1805.

Polymorphism and mutation databases

BioMutaiKIT.
DMDMi125472.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000001675426 – 976Mast/stem cell growth factor receptor KitAdd BLAST951

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi58 ↔ 97PROSITE-ProRule annotation1 Publication
Glycosylationi130N-linked (GlcNAc...)2 Publications1
Disulfide bondi136 ↔ 186PROSITE-ProRule annotation1 Publication
Glycosylationi145N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi151 ↔ 183PROSITE-ProRule annotation1 Publication
Disulfide bondi233 ↔ 290PROSITE-ProRule annotation1 Publication
Glycosylationi283N-linked (GlcNAc...)1 Publication1
Glycosylationi293N-linked (GlcNAc...)1 Publication1
Glycosylationi300N-linked (GlcNAc...)1 Publication1
Glycosylationi320N-linked (GlcNAc...)1 Publication1
Glycosylationi352N-linked (GlcNAc...)1 Publication1
Glycosylationi367N-linked (GlcNAc...)1 Publication1
Disulfide bondi428 ↔ 491PROSITE-ProRule annotation1 Publication
Glycosylationi463N-linked (GlcNAc...)Sequence analysis1
Glycosylationi486N-linked (GlcNAc...)Sequence analysis1
Modified residuei547Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei553Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei568Phosphotyrosine; by autocatalysis4 Publications1
Modified residuei570Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei703Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei721Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei730Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei741Phosphoserine; by PKC/PRKCA1 Publication1
Modified residuei746Phosphoserine; by PKC/PRKCA1 Publication1
Modified residuei821Phosphoserine1 Publication1
Modified residuei823Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei891Phosphoserine1 Publication1
Modified residuei900Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei936Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei959PhosphoserineCombined sources1 Publication1

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.
PeptideAtlasiP10721.
PRIDEiP10721.

PTM databases

iPTMnetiP10721.
PhosphoSitePlusiP10721.

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

BgeeiENSG00000157404.
CleanExiHS_KIT.
ExpressionAtlasiP10721. baseline and differential.
GenevisibleiP10721. HS.

Organism-specific databases

HPAiCAB003288.
CAB068253.
CAB072867.
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. Interacts (KITLG/SCF-bound) with IL1RL1. Interacts with IL1RAP (independent of stimulation with KITLG/SCF). A mast cell-specific KITLG/SCF-induced interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and MYD88.By similarity17 Publications

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
TNS1Q9HBL02EBI-1379503,EBI-3389814
TNS2Q63HR22EBI-1379503,EBI-949753
TNS3Q68CZ25EBI-1379503,EBI-1220488
TXKP426813EBI-1379503,EBI-7877438
YES1P079477EBI-1379503,EBI-515331
ZAP70P434032EBI-1379503,EBI-1211276

GO - Molecular functioni

  • cytokine binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi110015. 43 interactors.
DIPiDIP-1055N.
IntActiP10721. 65 interactors.
MINTiMINT-146746.
STRINGi9606.ENSP00000288135.

Chemistry databases

BindingDBiP10721.

Structurei

Secondary structure

1976
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 41Combined sources4
Beta strandi44 – 47Combined sources4
Beta strandi54 – 59Combined sources6
Beta strandi63 – 72Combined sources10
Beta strandi75 – 77Combined sources3
Beta strandi79 – 86Combined sources8
Helixi89 – 91Combined sources3
Beta strandi93 – 99Combined sources7
Beta strandi104 – 110Combined sources7
Beta strandi125 – 130Combined sources6
Beta strandi132 – 134Combined sources3
Beta strandi146 – 149Combined sources4
Beta strandi151 – 153Combined sources3
Beta strandi161 – 165Combined sources5
Turni166 – 168Combined sources3
Beta strandi169 – 174Combined sources6
Helixi177 – 179Combined sources3
Beta strandi183 – 188Combined sources6
Beta strandi193 – 200Combined sources8
Beta strandi203 – 205Combined sources3
Beta strandi213 – 215Combined sources3
Beta strandi219 – 224Combined sources6
Beta strandi229 – 239Combined sources11
Beta strandi243 – 248Combined sources6
Beta strandi258 – 263Combined sources6
Beta strandi265 – 267Combined sources3
Beta strandi269 – 279Combined sources11
Turni282 – 284Combined sources3
Beta strandi286 – 293Combined sources8
Beta strandi298 – 310Combined sources13
Beta strandi312 – 319Combined sources8
Beta strandi321 – 325Combined sources5
Beta strandi331 – 341Combined sources11
Beta strandi344 – 350Combined sources7
Beta strandi356 – 364Combined sources9
Beta strandi367 – 369Combined sources3
Beta strandi372 – 379Combined sources8
Helixi384 – 386Combined sources3
Beta strandi388 – 395Combined sources8
Beta strandi400 – 409Combined sources10
Beta strandi411 – 420Combined sources10
Helixi422 – 424Combined sources3
Beta strandi425 – 434Combined sources10
Beta strandi437 – 444Combined sources8
Beta strandi445 – 449Combined sources5
Beta strandi452 – 454Combined sources3
Beta strandi458 – 462Combined sources5
Beta strandi465 – 468Combined sources4
Beta strandi472 – 479Combined sources8
Helixi481 – 483Combined sources3
Beta strandi485 – 494Combined sources10
Beta strandi499 – 506Combined sources8
Beta strandi558 – 564Combined sources7
Beta strandi567 – 570Combined sources4
Turni573 – 575Combined sources3
Helixi580 – 582Combined sources3
Helixi586 – 588Combined sources3
Beta strandi589 – 597Combined sources9
Beta strandi599 – 613Combined sources15
Beta strandi617 – 625Combined sources9
Helixi631 – 647Combined sources17
Beta strandi656 – 660Combined sources5
Beta strandi662 – 665Combined sources4
Beta strandi667 – 671Combined sources5
Helixi678 – 684Combined sources7
Turni685 – 688Combined sources4
Beta strandi719 – 721Combined sources3
Beta strandi757 – 759Combined sources3
Helixi760 – 762Combined sources3
Helixi766 – 785Combined sources20
Beta strandi788 – 790Combined sources3
Helixi795 – 797Combined sources3
Beta strandi798 – 801Combined sources4
Turni802 – 804Combined sources3
Beta strandi805 – 808Combined sources4
Helixi812 – 814Combined sources3
Helixi817 – 819Combined sources3
Beta strandi823 – 825Combined sources3
Beta strandi827 – 831Combined sources5
Helixi833 – 835Combined sources3
Helixi838 – 843Combined sources6
Helixi848 – 863Combined sources16
Turni864 – 866Combined sources3
Helixi877 – 885Combined sources9
Helixi897 – 906Combined sources10
Helixi911 – 913Combined sources3
Helixi917 – 930Combined sources14
Turni931 – 933Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PKGX-ray2.90A/B549-935[»]
1QZJmodel-A576-932[»]
1QZKmodel-A576-932[»]
1R01model-A576-932[»]
1T45X-ray1.90A547-693[»]
A754-935[»]
1T46X-ray1.60A565-693[»]
A754-935[»]
2E9WX-ray3.50A/B26-514[»]
2EC8X-ray3.00A1-519[»]
2IUHX-ray2.00B718-728[»]
2VIFX-ray1.45P564-574[»]
3G0EX-ray1.60A544-693[»]
A754-935[»]
3G0FX-ray2.60A/B544-693[»]
A/B754-935[»]
4HVSX-ray1.90A551-934[»]
4K94X-ray2.40C308-518[»]
4K9EX-ray2.70C308-518[»]
4PGZX-ray2.40A/B/C308-518[»]
4U0IX-ray2.00A563-693[»]
A754-935[»]
ProteinModelPortaliP10721.
SMRiP10721.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10721.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 112Ig-like C2-type 1Add BLAST86
Domaini121 – 205Ig-like C2-type 2Add BLAST85
Domaini212 – 308Ig-like C2-type 3Add BLAST97
Domaini317 – 410Ig-like C2-type 4Add BLAST94
Domaini413 – 507Ig-like C2-type 5Add BLAST95
Domaini589 – 937Protein kinasePROSITE-ProRule annotationAdd BLAST349

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni568 – 570Important for interaction with phosphotyrosine-binding proteins3

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

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000112008.
HOVERGENiHBG104348.
InParanoidiP10721.
KOiK05091.
OMAiYFCPGTE.
OrthoDBiEOG091G01TL.
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. 3 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF56112. 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(+), KitA(+)

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

« Hide

        10         20         30         40         50
MRGARGAWDF LCVLLLLLRV QTGSSQPSVS PGEPSPPSIH PGKSDLIVRV
60 70 80 90 100
GDEIRLLCTD PGFVKWTFEI LDETNENKQN EWITEKAEAT NTGKYTCTNK
110 120 130 140 150
HGLSNSIYVF VRDPAKLFLV DRSLYGKEDN DTLVRCPLTD PEVTNYSLKG
160 170 180 190 200
CQGKPLPKDL RFIPDPKAGI MIKSVKRAYH RLCLHCSVDQ EGKSVLSEKF
210 220 230 240 250
ILKVRPAFKA VPVVSVSKAS YLLREGEEFT VTCTIKDVSS SVYSTWKREN
260 270 280 290 300
SQTKLQEKYN SWHHGDFNYE RQATLTISSA RVNDSGVFMC YANNTFGSAN
310 320 330 340 350
VTTTLEVVDK GFINIFPMIN TTVFVNDGEN VDLIVEYEAF PKPEHQQWIY
360 370 380 390 400
MNRTFTDKWE DYPKSENESN IRYVSELHLT RLKGTEGGTY TFLVSNSDVN
410 420 430 440 450
AAIAFNVYVN TKPEILTYDR LVNGMLQCVA AGFPEPTIDW YFCPGTEQRC
460 470 480 490 500
SASVLPVDVQ TLNSSGPPFG KLVVQSSIDS SAFKHNGTVE CKAYNDVGKT
510 520 530 540 550
SAYFNFAFKG NNKEQIHPHT LFTPLLIGFV IVAGMMCIIV MILTYKYLQK
560 570 580 590 600
PMYEVQWKVV EEINGNNYVY IDPTQLPYDH KWEFPRNRLS FGKTLGAGAF
610 620 630 640 650
GKVVEATAYG LIKSDAAMTV AVKMLKPSAH LTEREALMSE LKVLSYLGNH
660 670 680 690 700
MNIVNLLGAC TIGGPTLVIT EYCCYGDLLN FLRRKRDSFI CSKQEDHAEA
710 720 730 740 750
ALYKNLLHSK ESSCSDSTNE YMDMKPGVSY VVPTKADKRR SVRIGSYIER
760 770 780 790 800
DVTPAIMEDD ELALDLEDLL SFSYQVAKGM AFLASKNCIH RDLAARNILL
810 820 830 840 850
THGRITKICD FGLARDIKND SNYVVKGNAR LPVKWMAPES IFNCVYTFES
860 870 880 890 900
DVWSYGIFLW ELFSLGSSPY PGMPVDSKFY KMIKEGFRML SPEHAPAEMY
910 920 930 940 950
DIMKTCWDAD PLKRPTFKQI VQLIEKQISE STNHIYSNLA NCSPNRQKPV
960 970
VDHSVRINSV GSTASSSQPL LVHDDV
Length:976
Mass (Da):109,865
Last modified:July 1, 1989 - v1
Checksum:i81B0CD76817F3454
GO
Isoform 2 (identifier: P10721-2) [UniParc]FASTAAdd to basket
Also known as: GNNK(-), Kit(+)

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

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

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

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti764L → I in AAH71593 (PubMed:15489334).Curated1
Sequence conflicti838P → H in AAH71593 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_042021532V → I.1 PublicationCorresponds to variant rs55792975dbSNPEnsembl.1
Natural variantiVAR_042022541M → L.1 PublicationCorresponds to variant rs3822214dbSNPEnsembl.1
Natural variantiVAR_061289541M → V.Corresponds to variant rs3822214dbSNPEnsembl.1
Natural variantiVAR_033124550 – 558Missing in GIST; somatic mutation. 2 Publications9
Natural variantiVAR_033123550K → I in GIST; somatic mutation. 1 PublicationCorresponds to variant rs28933968dbSNPEnsembl.1
Natural variantiVAR_033125551 – 555Missing in GIST; somatic mutation. 1 Publication5
Natural variantiVAR_033128559 – 560Missing in GIST; somatic mutation. 1 Publication2
Natural variantiVAR_033126559V → A in GIST. 1 PublicationCorresponds to variant rs121913517dbSNPEnsembl.1
Natural variantiVAR_033127559V → D in GIST; somatic mutation. 1 PublicationCorresponds to variant rs121913517dbSNPEnsembl.1
Natural variantiVAR_007965559Missing in GIST. 1 Publication1
Natural variantiVAR_004104583E → K in PBT. 1 PublicationCorresponds to variant rs121913680dbSNPEnsembl.1
Natural variantiVAR_033129584F → C in PBT. 1 PublicationCorresponds to variant rs28933371dbSNPEnsembl.1
Natural variantiVAR_004105584F → L in PBT. 1 PublicationCorresponds to variant rs794726671dbSNPEnsembl.1
Natural variantiVAR_033130601G → R in PBT. 1 Publication1
Natural variantiVAR_033131656L → P in PBT. 1 Publication1
Natural variantiVAR_004106664G → R in PBT. 1 PublicationCorresponds to variant rs121913679dbSNPEnsembl.1
Natural variantiVAR_042023691C → S.1 PublicationCorresponds to variant rs35200131dbSNPEnsembl.1
Natural variantiVAR_042024715S → N.1 PublicationCorresponds to variant rs56094246dbSNPEnsembl.1
Natural variantiVAR_042025737D → N in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs751005114dbSNPEnsembl.1
Natural variantiVAR_004107791R → G in PBT. 1 Publication1
Natural variantiVAR_033132796R → G in PBT; with sensorineural deafness. 1 PublicationCorresponds to variant rs121913684dbSNPEnsembl.1
Natural variantiVAR_042026804R → W in a colorectal adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs145602440dbSNPEnsembl.1
Natural variantiVAR_004108812G → V in PBT. 1 Publication1
Natural variantiVAR_033133816D → F in mastocytosis; requires 2 nucleotide substitutions; somatic mutation; constitutively activated and is much more rapidly autophosphorylated than wild type. 1 Publication1
Natural variantiVAR_033134816D → H in a testicular tumor; seminoma; somatic mutation; constitutively activated. 3 PublicationsCorresponds to variant rs28933969dbSNPEnsembl.1
Natural variantiVAR_004109816D → V in mast cell leukemia and mastocytosis; somatic mutation; constitutively activated; loss of interaction with MPDZ. 7 PublicationsCorresponds to variant rs121913507dbSNPEnsembl.1
Natural variantiVAR_023828816D → Y in acute myeloid leukemia, mastocytosis and a germ cell tumor of the testis; somatic mutation; constitutively activated. 4 PublicationsCorresponds to variant rs121913506dbSNPEnsembl.1
Natural variantiVAR_033135820D → G in mast cell disease; systemic. 1 PublicationCorresponds to variant rs121913682dbSNPEnsembl.1
Natural variantiVAR_023829822N → K in a germ cell tumor of the testis; somatic mutation. 2 PublicationsCorresponds to variant rs121913514dbSNPEnsembl.1
Natural variantiVAR_023830829A → P in a germ cell tumor of the testis; somatic mutation. 2 Publications1
Natural variantiVAR_033136839E → K in mastocytosis; somatic mutation; dominant negative mutation; loss of autophosphorylation. 1 PublicationCorresponds to variant rs121913509dbSNPEnsembl.1
Natural variantiVAR_033137847T → P in PBT. 1 PublicationCorresponds to variant rs121913687dbSNPEnsembl.1
Natural variantiVAR_004110893 – 896Missing in PBT; severe. 1 Publication4

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_041866412 – 413KP → SL in isoform 3. 1 Publication2
Alternative sequenceiVSP_041867414 – 976Missing in isoform 3. 1 PublicationAdd BLAST563
Alternative sequenceiVSP_038385510 – 513Missing in isoform 2. 3 Publications4

Sequence databases

Select the link destinations:
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.4. human. [P10721-1]

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1PKGX-ray2.90A/B549-935[»]
1QZJmodel-A576-932[»]
1QZKmodel-A576-932[»]
1R01model-A576-932[»]
1T45X-ray1.90A547-693[»]
A754-935[»]
1T46X-ray1.60A565-693[»]
A754-935[»]
2E9WX-ray3.50A/B26-514[»]
2EC8X-ray3.00A1-519[»]
2IUHX-ray2.00B718-728[»]
2VIFX-ray1.45P564-574[»]
3G0EX-ray1.60A544-693[»]
A754-935[»]
3G0FX-ray2.60A/B544-693[»]
A/B754-935[»]
4HVSX-ray1.90A551-934[»]
4K94X-ray2.40C308-518[»]
4K9EX-ray2.70C308-518[»]
4PGZX-ray2.40A/B/C308-518[»]
4U0IX-ray2.00A563-693[»]
A754-935[»]
ProteinModelPortaliP10721.
SMRiP10721.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110015. 43 interactors.
DIPiDIP-1055N.
IntActiP10721. 65 interactors.
MINTiMINT-146746.
STRINGi9606.ENSP00000288135.

Chemistry databases

BindingDBiP10721.
ChEMBLiCHEMBL1936.
DrugBankiDB01254. Dasatinib.
DB00619. Imatinib.
DB09078. Lenvatinib.
DB04868. Nilotinib.
DB06589. Pazopanib.
DB08901. Ponatinib.
DB08896. Regorafenib.
DB00398. Sorafenib.
DB01268. Sunitinib.
GuidetoPHARMACOLOGYi1805.

PTM databases

iPTMnetiP10721.
PhosphoSitePlusiP10721.

Polymorphism and mutation databases

BioMutaiKIT.
DMDMi125472.

Proteomic databases

MaxQBiP10721.
PaxDbiP10721.
PeptideAtlasiP10721.
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.4. human. [P10721-1]

Organism-specific databases

CTDi3815.
DisGeNETi3815.
GeneCardsiKIT.
HGNCiHGNC:6342. KIT.
HPAiCAB003288.
CAB068253.
CAB072867.
HPA004471.
MalaCardsiKIT.
MIMi164920. gene.
172800. phenotype.
273300. phenotype.
601626. phenotype.
606764. phenotype.
neXtProtiNX_P10721.
OpenTargetsiENSG00000157404.
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

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000112008.
HOVERGENiHBG104348.
InParanoidiP10721.
KOiK05091.
OMAiYFCPGTE.
OrthoDBiEOG091G01TL.
PhylomeDBiP10721.
TreeFamiTF325768.

Enzyme and pathway databases

BioCyciZFISH:HS08211-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-1433559. Regulation of KIT signaling.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8866910. TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
SignaLinkiP10721.
SIGNORiP10721.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000157404.
CleanExiHS_KIT.
ExpressionAtlasiP10721. baseline and differential.
GenevisibleiP10721. HS.

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. 3 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF56112. 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...

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: November 2, 2016
This is version 206 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  9. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.