KIT
entrez
3815
canonical
uniprot
P10721
canonical
ensembl
ENSG00000157404
resolver
ensp
ENSP00000288135
resolver
ensp
ENSP00000390987
resolver
ensp
ENSP00000508733
resolver
ensp
ENSP00000508831
resolver
ensp
ENSP00000509084
resolver
ensp
ENSP00000509371
resolver
ensp
ENSP00000509450
resolver
ensp
ENSP00000509704
resolver
enst
ENST00000412167
resolver
enst
ENST00000686011
resolver
enst
ENST00000687109
resolver
enst
ENST00000689832
resolver
enst
ENST00000690543
resolver
enst
ENST00000692783
resolver
genesymbol
KIT
resolver
genesymbol_syn
SCFR
resolver
hgnc
HGNC:6342
resolver
uniprot
A0A0U2N547
resolver
uniprot
A0A8I5KQL9
resolver
uniprot
A0A8I5KQZ6
resolver
uniprot
A0A8I5KS03
resolver
uniprot
A0A8I5QKL5
resolver
uniprot
A0A8I5QKP7
resolver
uniprot
A0A8J8Z860
resolver
uniprot
B5A956
resolver
uniprot
D5LXN2
resolver
uniprot
D5M931
resolver
uniprot
F5H8F8
resolver
uniprot
Q6IQ28
resolver
uniprot
Q99662
resolver
uniprot
Q9UM99
resolver
uniprot_entry
A0A0U2N547_HUMAN
resolver
uniprot_entry
A0A8I5KQL9_HUMAN
resolver
uniprot_entry
A0A8I5KQZ6_HUMAN
resolver
uniprot_entry
A0A8I5KS03_HUMAN
resolver
uniprot_entry
A0A8I5QKL5_HUMAN
resolver
uniprot_entry
A0A8I5QKP7_HUMAN
resolver
uniprot_entry
A0A8J8Z860_HUMAN
resolver
uniprot_entry
KIT_HUMAN
resolver
uniprot_sec
B5A956
resolver
uniprot_sec
D5LXN2
resolver
uniprot_sec
D5M931
resolver
uniprot_sec
F5H8F8
resolver
uniprot_sec
Q6IQ28
resolver
uniprot_sec
Q99662
resolver
uniprot_sec
Q9UM99
resolver
activity_regulation
ACTIVITY REGULATION: 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. {ECO:0000269|PubMed:15123710, ECO:0000269|PubMed:19164557, ECO:0000269|PubMed:21640708, ECO:0000269|PubMed:7520444, ECO:0000269|PubMed:7539802}.
uniprot
proteins
amino_acid_sequence
MRGARGAWDFLCVLLLLLRVQTGSSQPSVSPGEPSPPSIHPGKSDLIVRVGDEIRLLCTDPGFVKWTFEILDETNENKQNEWITEKAEATNTGKYTCTNKHGLSNSIYVFVRDPAKLFLVDRSLYGKEDNDTLVRCPLTDPEVTNYSLKGCQGKPLPKDLRFIPDPKAGIMIKSVKRAYHRLCLHCSVDQEGKSVLSEKFILKVRPAFKAVPVVSVSKASYLLREGEEFTVTCTIKDVSSSVYSTWKRENSQTKLQEKYNSWHHGDFNYERQATLTISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMINTTVFVNDGENVDLIVEYEAFPKPEHQQWIYMNRTFTDKWEDYPKSENESNIRYVSELHLTRLKGTEGGTYTFLVSNSDVNAAIAFNVYVNTKPEILTYDRLVNGMLQCVAAGFPEPTIDWYFCPGTEQRCSASVLPVDVQTLNSSGPPFGKLVVQSSIDSSAFKHNGTVECKAYNDVGKTSAYFNFAFKGNNKEQIHPHTLFTPLLIGFVIVAGMMCIIVMILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSKESSCSDSTNEYMDMKPGVSYVVPTKADKRRSVRIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHIYSNLANCSPNRQKPVVDHSVRINSVGSTASSSQPLLVHDDV
uniprot
proteins
disease_involvement
DISEASE: Piebald trait (PBT) [MIM:172800]: Autosomal dominant genetic developmental abnormality of pigmentation characterized by congenital patches of white skin and hair that lack melanocytes. {ECO:0000269|PubMed:11074500, ECO:0000269|PubMed:1370874, ECO:0000269|PubMed:1376329, ECO:0000269|PubMed:1717985, ECO:0000269|PubMed:7687267, ECO:0000269|PubMed:8680409, ECO:0000269|PubMed:9450866, ECO:0000269|PubMed:9699740}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: 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. {ECO:0000269|PubMed:11505412, ECO:0000269|PubMed:15824741, ECO:0000269|PubMed:9438854, ECO:0000269|PubMed:9697690}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: 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.; DISEASE: 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.; DISEASE: Mastocytosis, cutaneous (MASTC) [MIM:154800]: A form of mastocytosis, a heterogeneous group of disorders associated with abnormal proliferation and accumulation of mast cells in various tissues, especially in the skin and hematopoietic organs. MASTC is an autosomal dominant form characterized by macules, papules, nodules, or diffuse infiltration of the skin, often associated with localized hyperpigmentation. Gentle rubbing of the lesions induces histamine release from mechanically activated mast cells, causing local wheals, erythema, and often pruritus, a phenomenon termed Darier sign. {ECO:0000269|PubMed:15173254, ECO:0000269|PubMed:19865100, ECO:0000269|PubMed:21689725, ECO:0000269|PubMed:24289326, ECO:0000269|PubMed:9990072}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Mastocytosis, systemic (MASTSYS) [MIM:154800]: A severe form of mastocytosis characterized by abnormal proliferation and accumulation of mast cells in several organs, resulting in a systemic disease that may affect bone, gastrointestinal tract, lymphatics, spleen, and liver. In some cases, it is associated with a clonal hematologic non-mast-cell lineage disease, such as a myelodysplastic or myeloproliferative disorder. It can also lead to mast cell leukemia, which carries a high risk of mortality. {ECO:0000269|PubMed:9990072}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Tyrosine-protein kinase that acts as a 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. {ECO:0000269|PubMed:10397721, ECO:0000269|PubMed:12444928, ECO:0000269|PubMed:12511554, ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:17904548, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:21640708, ECO:0000269|PubMed:7520444, ECO:0000269|PubMed:9528781}.
uniprot
proteins
mass_dalton
109865
uniprot
proteins
mutagenesis
MUTAGEN 381; /note="R->A: Reduces autophosphorylation in response to KITLG/SCF."; /evidence="ECO:0000269|PubMed:17662946"; MUTAGEN 386; /note="E->A: Reduces autophosphorylation in response to KITLG/SCF."; /evidence="ECO:0000269|PubMed:17662946"; MUTAGEN 571; /note="I->A: Reduction in SH2B2/APS binding. Abolishes SH2B2/APS binding; when associated with A-939."; /evidence="ECO:0000269|PubMed:12444928"; MUTAGEN 623; /note="K->M: Stronger interaction with MPDZ."; /evidence="ECO:0000269|PubMed:11018522"; MUTAGEN 741; /note="S->A: Abolishes down-regulation of kinase activity by PKC/PRKCA-mediated phosphorylation; when associated with A-746."; /evidence="ECO:0000269|PubMed:7539802"; MUTAGEN 746; /note="S->A: Abolishes down-regulation of kinase activity by PKC/PRKCA-mediated phosphorylation; when associated with A-741."; /evidence="ECO:0000269|PubMed:7539802"; MUTAGEN 823; /note="Y->F: No decrease in activity. Leads to autophosphorylation at Tyr-900."; /evidence="ECO:0000269|PubMed:20147452"; MUTAGEN 939; /note="L->A: Reduction in SH2B2/APS binding. Abolishes SH2B2/APS binding; when associated with A-571."; /evidence="ECO:0000269|PubMed:12444928
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation. {ECO:0000269|PubMed:17904548, ECO:0000269|PubMed:19265199}.; PTM: 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. {ECO:0000269|PubMed:10377264, ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:20147452, ECO:0000269|PubMed:21030588, ECO:0000269|PubMed:9038210}.
uniprot
proteins
protein_family
CSF-1/PDGF receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10362788
uniprot
proteins
pubmed
10377264
uniprot
proteins
pubmed
10397721
uniprot
proteins
pubmed
11018522
uniprot
proteins
pubmed
11074500
uniprot
proteins
pubmed
11505412
uniprot
proteins
pubmed
11825908
uniprot
proteins
pubmed
12444928
uniprot
proteins
pubmed
12511554
uniprot
proteins
pubmed
1279499
uniprot
proteins
pubmed
12824176
uniprot
proteins
pubmed
12878163
uniprot
proteins
pubmed
1370874
uniprot
proteins
pubmed
1376329
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15039213
uniprot
proteins
pubmed
15123710
uniprot
proteins
pubmed
15173254
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15526160
uniprot
proteins
pubmed
15625120
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15824741
uniprot
proteins
pubmed
16129412
uniprot
proteins
pubmed
16175573
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
1717985
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17595334
uniprot
proteins
pubmed
17662946
uniprot
proteins
pubmed
17904548
uniprot
proteins
pubmed
18381929
uniprot
proteins
pubmed
18593464
uniprot
proteins
pubmed
19164557
uniprot
proteins
pubmed
19265199
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19865100
uniprot
proteins
pubmed
20147452
uniprot
proteins
pubmed
20601678
uniprot
proteins
pubmed
20658618
uniprot
proteins
pubmed
21030588
uniprot
proteins
pubmed
21057534
uniprot
proteins
pubmed
21135090
uniprot
proteins
pubmed
21640708
uniprot
proteins
pubmed
21689725
uniprot
proteins
pubmed
24289326
uniprot
proteins
pubmed
2448137
uniprot
proteins
pubmed
7505199
uniprot
proteins
pubmed
7506248
uniprot
proteins
pubmed
7520444
uniprot
proteins
pubmed
7539802
uniprot
proteins
pubmed
7687267
uniprot
proteins
pubmed
7691885
uniprot
proteins
pubmed
8680409
uniprot
proteins
pubmed
9027509
uniprot
proteins
pubmed
9029028
uniprot
proteins
pubmed
9038210
uniprot
proteins
pubmed
9341198
uniprot
proteins
pubmed
9438854
uniprot
proteins
pubmed
9450866
uniprot
proteins
pubmed
9528781
uniprot
proteins
pubmed
9657776
uniprot
proteins
pubmed
9697690
uniprot
proteins
pubmed
9699740
uniprot
proteins
pubmed
9990072
uniprot
proteins
sequence_length
976
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:20601678}. Note=Detected in the cytoplasm of spermatozoa, especially in the equatorial and subacrosomal region of the sperm head. {ECO:0000269|PubMed:20601678}.
uniprot
proteins
transmembrane_region
TRANSMEM 525..545; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins