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Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117)

 KIT_MOUSE               Reviewed;         979 AA.
P05532; Q61415; Q61416; Q61417; Q6LEE9; Q6QJB7; Q6QJB8; Q7TS86; Q8C8K9;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
19-OCT-2011, sequence version 3.
17-JUN-2020, entry version 213.
RecName: Full=Mast/stem cell growth factor receptor Kit;
Short=SCFR;
EC=2.7.10.1;
AltName: Full=Proto-oncogene c-Kit;
AltName: Full=Tyrosine-protein kinase Kit;
AltName: CD_antigen=CD117;
Flags: Precursor;
Name=Kit; Synonyms=Sl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT GLU-207.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=2456920; DOI=10.1002/j.1460-2075.1988.tb02907.x;
Qiu F., Ray P., Brown K., Barker P.E., Jhanwar S., Ruddle F.H., Besmer P.;
"Primary structure of c-kit: relationship with the CSF-1/PDGF receptor
kinase family -- oncogenic activation of v-kit involves deletion of
extracellular domain and C-terminus.";
EMBO J. 7:1003-1011(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
PubMed=1709486; DOI=10.1093/nar/19.6.1267;
Hayashi S., Kunisada T., Ogawa M., Yamaguchi K., Nishikawa S.;
"Exon skipping by mutation of an authentic splice site of c-kit gene in W/W
mouse.";
Nucleic Acids Res. 19:1267-1271(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), AND TISSUE
SPECIFICITY.
STRAIN=ICR;
PubMed=1378413; DOI=10.1016/0012-1606(92)90172-d;
Rossi P., Marziali G., Albanesi C., Charlesworth A., Geremia R.,
Sorrentino V.;
"A novel c-kit transcript, potentially encoding a truncated receptor,
originates within a kit gene intron in mouse spermatids.";
Dev. Biol. 152:203-207(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND MUTAGENESIS OF PHE-860.
STRAIN=C57BL/6J;
PubMed=15731517; DOI=10.1534/genetics.104.027177;
Ruan H.B., Zhang N., Gao X.;
"Identification of a novel point mutation of mouse proto-oncogene c-kit
through N-ethyl-N-nitrosourea mutagenesis.";
Genetics 169:819-831(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of the
mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
STRAIN=BALB/cJ;
PubMed=7682073; DOI=10.1006/bbrc.1993.1301;
Yasuda H., Galli S.J., Geissler E.N.;
"Cloning and functional analysis of the mouse c-kit promoter.";
Biochem. Biophys. Res. Commun. 191:893-901(1993).
[8]
FUNCTION, AND SUBUNIT.
PubMed=1698611; DOI=10.1002/j.1460-2075.1990.tb07528.x;
Tan J.C., Buck J., Levi E., Besmer P.;
"Candidate ligand for the c-kit transmembrane kinase receptor: KL, a
fibroblast derived growth factor stimulates mast cells and erythroid
progenitors.";
EMBO J. 9:3287-3294(1990).
[9]
FUNCTION IN ACTIVATION OF PLCG1, INTERACTION WITH PLCG1, ALTERNATIVE
SPLICING, PHOSPHORYLATION, GLYCOSYLATION, AND CHARACTERIZATION OF VARIANTS
W37 LYS-586 AND W41 MET-835.
PubMed=1714377; DOI=10.1002/j.1460-2075.1991.tb07784.x;
Reith A.D., Ellis C., Lyman S.D., Anderson D.M., Williams D.E.,
Bernstein A., Pawson T.;
"Signal transduction by normal isoforms and W mutant variants of the Kit
receptor tyrosine kinase.";
EMBO J. 10:2451-2459(1991).
[10]
INTERACTION WITH PIK3R1, AND FUNCTION IN PHOSPHORYLATION OF PIK3R1.
PubMed=7509796;
Serve H., Hsu Y.C., Besmer P.;
"Tyrosine residue 719 of the c-kit receptor is essential for binding of the
P85 subunit of phosphatidylinositol (PI) 3-kinase and for c-kit-associated
PI 3-kinase activity in COS-1 cells.";
J. Biol. Chem. 269:6026-6030(1994).
[11]
UBIQUITINATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, PHOSPHORYLATION
AT TYR-825, INTERACTION WITH PIK3R1, CHARACTERIZATION OF VARIANT W42
ASN-794, MUTAGENESIS OF TYR-723, AND TISSUE SPECIFICITY.
PubMed=7527401;
Yee N.S., Hsiau C.W., Serve H., Vosseller K., Besmer P.;
"Mechanism of down-regulation of c-kit receptor. Roles of receptor tyrosine
kinase, phosphatidylinositol 3'-kinase, and protein kinase C.";
J. Biol. Chem. 269:31991-31998(1994).
[12]
ALTERNATIVE SPLICING, AND FUNCTION IN ACTIVATION OF PLCG1.
PubMed=9722617; DOI=10.1083/jcb.142.4.1063;
Sette C., Bevilacqua A., Geremia R., Rossi P.;
"Involvement of phospholipase Cgamma1 in mouse egg activation induced by a
truncated form of the C-kit tyrosine kinase present in spermatozoa.";
J. Cell Biol. 142:1063-1074(1998).
[13]
INTERACTION WITH PTPN6/SHP-1 AND PTPN11/SHP-2, FUNCTION IN PHOSPHORYLATION
OF PTPN6/SHP-1, AND MUTAGENESIS OF TYR-571 AND TYR-573.
PubMed=9528781; DOI=10.1128/mcb.18.4.2089;
Kozlowski M., Larose L., Lee F., Le D.M., Rottapel R., Siminovitch K.A.;
"SHP-1 binds and negatively modulates the c-Kit receptor by interaction
with tyrosine 569 in the c-Kit juxtamembrane domain.";
Mol. Cell. Biol. 18:2089-2099(1998).
[14]
REVIEW ON ROLE IN SPERMATOGENESIS AND FERTILITY.
PubMed=12558531; DOI=10.1046/j.1439-0272.2003.00539.x;
Rossi P., Dolci S., Sette C., Geremia R.;
"Molecular mechanisms utilized by alternative c-kit gene products in the
control of spermatogonial proliferation and sperm-mediated egg
activation.";
Andrologia 35:71-78(2003).
[15]
INTERACTION WITH FES/FPS.
PubMed=17595334; DOI=10.1182/blood-2007-02-076471;
Voisset E., Lopez S., Dubreuil P., De Sepulveda P.;
"The tyrosine kinase FES is an essential effector of KITD816V proliferation
signal.";
Blood 110:2593-2599(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-571; TYR-573; TYR-706 AND
TYR-938, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[17]
FUNCTION IN MAST CELL MIGRATION, AND IN SIGNALING VIA FYN.
PubMed=18725415; DOI=10.1074/jbc.m804077200;
Samayawardhena L.A., Pallen C.J.;
"Protein-tyrosine phosphatase alpha regulates stem cell factor-dependent c-
Kit activation and migration of mast cells.";
J. Biol. Chem. 283:29175-29185(2008).
[18]
ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=18447649; DOI=10.1089/scd.2007.0101;
Zayas J., Spassov D.S., Nachtman R.G., Jurecic R.;
"Murine hematopoietic stem cells and multipotent progenitors express
truncated intracellular form of c-kit receptor.";
Stem Cells Dev. 17:343-353(2008).
[19]
FUNCTION IN MAST CELL DEGRANULATION.
PubMed=21037083; DOI=10.2353/ajpath.2010.100369;
Chen S., Burgin S., McDaniel A., Li X., Yuan J., Chen M., Khalaf W.,
Clapp D.W., Yang F.C.;
"Nf1-/- Schwann cell-conditioned medium modulates mast cell degranulation
by c-Kit-mediated hyperactivation of phosphatidylinositol 3-kinase.";
Am. J. Pathol. 177:3125-3132(2010).
[20]
INTERACTION WITH IL1RL1 AND IL1RAP, AND SUBUNIT.
PubMed=20200353; DOI=10.1182/blood-2009-10-247411;
Drube S., Heink S., Walter S., Loehn T., Grusser M., Gerbaulet A.,
Berod L., Schons J., Dudeck A., Freitag J., Grotha S., Reich D.,
Rudeschko O., Norgauer J., Hartmann K., Roers A., Kamradt T.;
"The receptor tyrosine kinase c-Kit controls IL-33 receptor signaling in
mast cells.";
Blood 115:3899-3906(2010).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and expression.";
Cell 143:1174-1189(2010).
[22]
VARIANT GLU-207.
Jawad-Alam J.;
Unpublished observations (APR-2010).
[23]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-314 IN COMPLEX WITH KITLG/SCF,
DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-296 AND ASN-303.
PubMed=17255936; DOI=10.1038/sj.emboj.7601545;
Liu H., Chen X., Focia P.J., He X.;
"Structural basis for stem cell factor-KIT signaling and activation of
class III receptor tyrosine kinases.";
EMBO J. 26:891-901(2007).
[24]
VARIANT W42 ASN-794.
PubMed=1688471; DOI=10.1126/science.1688471;
Tan J.C., Nocka K., Ray P., Traktman P., Besmer P.;
"The dominant W42 spotting phenotype results from a missense mutation in
the c-kit receptor kinase.";
Science 247:209-212(1990).
[25]
VARIANTS W37 LYS-586; WV MET-664 AND W41 MET-835.
PubMed=1693331; DOI=10.1002/j.1460-2075.1990.tb08305.x;
Nocka K., Tan J.C., Chiu E., Chu T.Y., Ray P., Traktman P., Besmer P.;
"Molecular bases of dominant negative and loss of function mutations at the
murine c-kit/white spotting locus: W37, Wv, W41 and W.";
EMBO J. 9:1805-1813(1990).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:1698611, ECO:0000269|PubMed:1714377,
ECO:0000269|PubMed:18725415, ECO:0000269|PubMed:21037083,
ECO:0000269|PubMed:7509796, ECO:0000269|PubMed:9528781,
ECO:0000269|PubMed:9722617}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
ECO:0000269|PubMed:7527401};
-!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
of bound ligand. KITLG/SCF binding leads to dimerization and activation
by autophosphorylation.
-!- SUBUNIT: 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 the
protein phosphatases PTPN6/SHP-1 (via SH2 domain), PTPN11/SHP-2 (via
SH2 domain) and PTPRU. Interacts with DOK1 and TEC (By similarity).
Interacts with the protein kinase FES/FPS. Interacts with PLCG1.
Interacts (via phosphorylated tyrosine residues) with PIK3R1 and PIK3
catalytic subunit. 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. {ECO:0000250|UniProtKB:P10721,
ECO:0000269|PubMed:1698611, ECO:0000269|PubMed:1714377,
ECO:0000269|PubMed:17255936, ECO:0000269|PubMed:17595334,
ECO:0000269|PubMed:20200353, ECO:0000269|PubMed:7509796,
ECO:0000269|PubMed:7527401, ECO:0000269|PubMed:9528781}.
-!- INTERACTION:
P05532; P26955: Csf2rb; NbExp=4; IntAct=EBI-8559255, EBI-1810026;
-!- 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. Note=Detected in the
cytoplasm of spermatozoa, especially in the equatorial and subacrosomal
region of the sperm head. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=GNNK(+), KitA(+);
IsoId=P05532-1; Sequence=Displayed;
Name=2; Synonyms=GNNK(-), Kit(+);
IsoId=P05532-2; Sequence=VSP_041870;
Name=3; Synonyms=Tr-kit, Truncated;
IsoId=P05532-3; Sequence=VSP_041868, VSP_041869;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are detected in bone marrow
cells, spermatogonia and spermatocytes, but not in round spermatids,
elongating spermatids and spermatozoa. Isoform 3 is detected in round
spermatids, elongating spermatids and spermatozoa, but not in
spermatogonia and spermatocytes (at protein level). Isoform 1 is widely
expressed and detected in fetal liver and bone marrow. Isoform 3 is
detected in bone marrow cells enriched in hematopoietic stem cells.
{ECO:0000269|PubMed:1378413, ECO:0000269|PubMed:18447649,
ECO:0000269|PubMed:7527401}.
-!- PTM: Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after
autophosphorylation induced by KITLG/SCF binding, leading to
internalization and degradation (By similarity). {ECO:0000250}.
-!- PTM: Autophosphorylated on tyrosine residues. KITLG/SCF binding
promotes autophosphorylation of isoform 1 and isoform 2. Isoform 1
shows low levels of tyrosine phosphorylation in the absence of added
KITLG/SCF, while isoform 2 requires stimulation by KITLG/SCF for
phosphorylation (in vitro). Phosphorylation of Tyr-573 is required for
interaction with PTPN6/SHP-1. Phosphorylation of Tyr-571 is required
for interaction with PTPN11/SHP-2. Phosphorylated tyrosine residues are
important for interaction with specific binding partners.
{ECO:0000269|PubMed:1714377, ECO:0000269|PubMed:7527401}.
-!- DISEASE: Note=Defects in Kit are the cause of the white-spotting
phenotype (W). White-spotting variants induces severe effects on
pigmentation, gametogenesis and hematopoiesis. Mice homozygous for W42
die perinatally of macrocytic anemia.
-!- 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.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; Y00864; CAA68772.1; -; mRNA.
EMBL; AK046795; BAC32872.1; -; mRNA.
EMBL; X65997; CAA46798.1; -; mRNA.
EMBL; X65998; CAA46799.1; ALT_SEQ; Genomic_DNA.
EMBL; X65998; CAA46800.1; -; Genomic_DNA.
EMBL; AY536430; AAS45606.1; -; mRNA.
EMBL; AY536431; AAS45607.1; -; mRNA.
EMBL; AC013622; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC115853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC052457; AAH52457.1; -; mRNA.
EMBL; BC075716; AAH75716.1; -; mRNA.
EMBL; L11358; AAA37420.1; -; Genomic_DNA.
CCDS; CCDS51525.1; -. [P05532-1]
CCDS; CCDS80302.1; -. [P05532-2]
PIR; A44876; A44876.
PIR; S00474; TVMSKT.
PIR; S24667; S24667.
PIR; S34435; S34435.
RefSeq; NP_001116205.1; NM_001122733.1. [P05532-1]
RefSeq; NP_066922.2; NM_021099.3. [P05532-2]
PDB; 2O26; X-ray; 2.50 A; U/W/X/Y=25-314.
PDBsum; 2O26; -.
SMR; P05532; -.
BioGRID; 200957; 20.
CORUM; P05532; -.
DIP; DIP-59622N; -.
IntAct; P05532; 5.
MINT; P05532; -.
STRING; 10090.ENSMUSP00000005815; -.
BindingDB; P05532; -.
ChEMBL; CHEMBL2034798; -.
iPTMnet; P05532; -.
PhosphoSitePlus; P05532; -.
MaxQB; P05532; -.
PaxDb; P05532; -.
PRIDE; P05532; -.
ABCD; P05532; 1 sequenced antibody.
Antibodypedia; 1392; 5150 antibodies.
Ensembl; ENSMUST00000005815; ENSMUSP00000005815; ENSMUSG00000005672. [P05532-1]
Ensembl; ENSMUST00000144270; ENSMUSP00000116465; ENSMUSG00000005672. [P05532-2]
GeneID; 16590; -.
KEGG; mmu:16590; -.
UCSC; uc008xug.2; mouse. [P05532-1]
UCSC; uc012dxj.1; mouse. [P05532-2]
CTD; 3815; -.
MGI; MGI:96677; Kit.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00940000155626; -.
HOGENOM; CLU_000288_49_0_1; -.
InParanoid; P05532; -.
KO; K05091; -.
OMA; PSEMYQI; -.
OrthoDB; 236292at2759; -.
TreeFam; TF325768; -.
BRENDA; 2.7.10.1; 3474.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-1433559; Regulation of KIT signaling.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
BioGRID-ORCS; 16590; 1 hit in 12 CRISPR screens.
ChiTaRS; Kit; mouse.
EvolutionaryTrace; P05532; -.
PRO; PR:P05532; -.
Proteomes; UP000000589; Chromosome 5.
RNAct; P05532; protein.
Bgee; ENSMUSG00000005672; Expressed in lung and 379 other tissues.
Genevisible; P05532; MM.
GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0043235; C:receptor complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019955; F:cytokine binding; ISS:UniProtKB.
GO; GO:0019838; F:growth factor binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; ISO:MGI.
GO; GO:0042169; F:SH2 domain binding; IPI:BHF-UCL.
GO; GO:0005020; F:stem cell factor receptor activity; IDA:MGI.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; ISO:MGI.
GO; GO:0030183; P:B cell differentiation; IBA:GO_Central.
GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; TAS:MGI.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IDA:UniProtKB.
GO; GO:0006935; P:chemotaxis; TAS:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
GO; GO:0002371; P:dendritic cell cytokine production; IMP:UniProtKB.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:UniProtKB.
GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
GO; GO:0048565; P:digestive tract development; IMP:UniProtKB.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IGI:MGI.
GO; GO:0035162; P:embryonic hemopoiesis; IMP:UniProtKB.
GO; GO:0050673; P:epithelial cell proliferation; ISO:MGI.
GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
GO; GO:0038162; P:erythropoietin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0038093; P:Fc receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007281; P:germ cell development; TAS:MGI.
GO; GO:0008354; P:germ cell migration; ISO:MGI.
GO; GO:0006687; P:glycosphingolipid metabolic process; IMP:MGI.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IBA:GO_Central.
GO; GO:0035701; P:hematopoietic stem cell migration; IMP:MGI.
GO; GO:0030097; P:hemopoiesis; IMP:MGI.
GO; GO:0002327; P:immature B cell differentiation; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; IMP:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
GO; GO:0038109; P:Kit signaling pathway; ISO:MGI.
GO; GO:0030032; P:lamellipodium assembly; IDA:UniProtKB.
GO; GO:0002320; P:lymphoid progenitor cell differentiation; IGI:MGI.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0002551; P:mast cell chemotaxis; ISO:MGI.
GO; GO:0032762; P:mast cell cytokine production; ISS:UniProtKB.
GO; GO:0043303; P:mast cell degranulation; ISS:UniProtKB.
GO; GO:0060374; P:mast cell differentiation; IMP:UniProtKB.
GO; GO:0035855; P:megakaryocyte development; IMP:UniProtKB.
GO; GO:0097326; P:melanocyte adhesion; IDA:UniProtKB.
GO; GO:0030318; P:melanocyte differentiation; IMP:UniProtKB.
GO; GO:0097324; P:melanocyte migration; IMP:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0002573; P:myeloid leukocyte differentiation; IMP:MGI.
GO; GO:0002318; P:myeloid progenitor cell differentiation; IGI:MGI.
GO; GO:0043069; P:negative regulation of programmed cell death; IMP:MGI.
GO; GO:0001541; P:ovarian follicle development; IMP:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0043473; P:pigmentation; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
GO; GO:1904343; P:positive regulation of colon smooth muscle contraction; ISO:MGI.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; ISO:MGI.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IGI:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; ISO:MGI.
GO; GO:0031274; P:positive regulation of pseudopodium assembly; ISO:MGI.
GO; GO:0120072; P:positive regulation of pyloric antrum smooth muscle contraction; ISO:MGI.
GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
GO; GO:1904349; P:positive regulation of small intestine smooth muscle contraction; ISO:MGI.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
GO; GO:1905065; P:positive regulation of vascular smooth muscle cell differentiation; ISO:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:1904251; P:regulation of bile acid metabolic process; ISO:MGI.
GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0009314; P:response to radiation; IMP:MGI.
GO; GO:0048103; P:somatic stem cell division; ISO:MGI.
GO; GO:0035019; P:somatic stem cell population maintenance; ISO:MGI.
GO; GO:0007286; P:spermatid development; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
GO; GO:0030217; P:T cell differentiation; IMP:UniProtKB.
GO; GO:0043586; P:tongue development; IEA:Ensembl.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
GO; GO:0008542; P:visual learning; ISO:MGI.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR027263; SCGF_receptor.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR001824; Tyr_kinase_rcpt_3_CS.
Pfam; PF00047; ig; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF500951; SCGF_recepter; 1.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 4.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane; Cytoplasm;
Disease mutation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Proto-oncogene; Receptor; Reference proteome; Repeat;
Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1..24
/evidence="ECO:0000255"
CHAIN 25..979
/note="Mast/stem cell growth factor receptor Kit"
/id="PRO_0000016755"
TOPO_DOM 25..527
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 528..548
/note="Helical"
/evidence="ECO:0000255"
TOPO_DOM 549..979
/note="Cytoplasmic"
/evidence="ECO:0000255"
DOMAIN 31..117
/note="Ig-like C2-type 1"
DOMAIN 126..210
/note="Ig-like C2-type 2"
DOMAIN 217..315
/note="Ig-like C2-type 3"
DOMAIN 324..417
/note="Ig-like C2-type 4"
DOMAIN 420..514
/note="Ig-like C2-type 5"
DOMAIN 592..939
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 599..606
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 674..680
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
REGION 571..573
/note="Important for interaction with phosphotyrosine-
binding proteins"
/evidence="ECO:0000250"
ACT_SITE 794
/note="Proton acceptor"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
ECO:0000255|PROSITE-ProRule:PRU10028"
METAL 571
/note="Magnesium"
/evidence="ECO:0000250"
METAL 799
/note="Magnesium"
/evidence="ECO:0000250"
METAL 812
/note="Magnesium"
/evidence="ECO:0000250"
BINDING 626
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
BINDING 798
/note="ATP"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SITE 938
/note="Important for interaction with phosphotyrosine-
binding proteins"
/evidence="ECO:0000250"
MOD_RES 550
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P10721"
MOD_RES 556
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P10721"
MOD_RES 571
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:17947660"
MOD_RES 573
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:17947660"
MOD_RES 706
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:17947660"
MOD_RES 720
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:21183079"
MOD_RES 723
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P10721"
MOD_RES 732
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P10721"
MOD_RES 743
/note="Phosphoserine; by PKC/PRKCA"
/evidence="ECO:0000250|UniProtKB:P10721"
MOD_RES 748
/note="Phosphoserine; by PKC/PRKCA"
/evidence="ECO:0000250|UniProtKB:P10721"
MOD_RES 823
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10721"
MOD_RES 825
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:7527401"
MOD_RES 893
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10721"
MOD_RES 902
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000250|UniProtKB:P10721"
MOD_RES 938
/note="Phosphotyrosine"
/evidence="ECO:0000244|PubMed:17947660"
MOD_RES 962
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P10721"
CARBOHYD 146
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 296
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:17255936"
CARBOHYD 303
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000269|PubMed:17255936"
CARBOHYD 323
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 355
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 370
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 466
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 489
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 58..98
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17255936"
DISULFID 137..187
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17255936"
DISULFID 152..184
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17255936"
DISULFID 234..293
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17255936"
DISULFID 431..494
/evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
VAR_SEQ 1..12
/note="MRGARGAWDLLC -> MAVAVFPFLPQQ (in isoform 3)"
/evidence="ECO:0000303|PubMed:1378413"
/id="VSP_041868"
VAR_SEQ 13..789
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:1378413"
/id="VSP_041869"
VAR_SEQ 512..515
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15731517, ECO:0000303|PubMed:2456920"
/id="VSP_041870"
VARIANT 207
/note="A -> E (loss-of-function mutation abolishing ligand
binding)"
/evidence="ECO:0000269|PubMed:2456920, ECO:0000269|Ref.22"
VARIANT 586
/note="E -> K (in W37 spotting; impaired protein stability
and loss of kinase activity)"
/evidence="ECO:0000269|PubMed:1693331,
ECO:0000269|PubMed:1714377"
VARIANT 664
/note="T -> M (in Wv spotting)"
/evidence="ECO:0000269|PubMed:1693331"
VARIANT 794
/note="D -> N (in W42 spotting; loss of kinase activity and
impaired internalization after exposure to KITLG/SCF)"
/evidence="ECO:0000269|PubMed:1688471,
ECO:0000269|PubMed:7527401"
VARIANT 835
/note="V -> M (in W41 spotting; decreased kinase activity)"
/evidence="ECO:0000269|PubMed:1693331,
ECO:0000269|PubMed:1714377"
MUTAGEN 571
/note="Y->F: Abolishes interaction with PTPN11/SHP-2."
/evidence="ECO:0000269|PubMed:9528781"
MUTAGEN 573
/note="Y->F: Abolishes interaction with PTPN6/SHP-1."
/evidence="ECO:0000269|PubMed:9528781"
MUTAGEN 573
/note="Missing: Abolishes interaction with PTPN6/SHP-1."
/evidence="ECO:0000269|PubMed:9528781"
MUTAGEN 723
/note="Y->F: Abolishes interaction with PIK3R1."
/evidence="ECO:0000269|PubMed:7527401"
MUTAGEN 860
/note="F->S: Mice display white fur, hearing loss, anemia
and mast cell deficiency, plus sterility in both males and
females."
/evidence="ECO:0000269|PubMed:15731517"
CONFLICT 551
/note="L -> F (in Ref. 6; AAH52457)"
/evidence="ECO:0000305"
CONFLICT 781
/note="G -> A (in Ref. 1; CAA68772 and 2; CAA46799)"
/evidence="ECO:0000305"
CONFLICT 860
/note="F -> S (in Ref. 4; AAS45607)"
/evidence="ECO:0000305"
STRAND 38..41
/evidence="ECO:0000244|PDB:2O26"
STRAND 43..49
/evidence="ECO:0000244|PDB:2O26"
STRAND 54..59
/evidence="ECO:0000244|PDB:2O26"
STRAND 63..69
/evidence="ECO:0000244|PDB:2O26"
STRAND 71..73
/evidence="ECO:0000244|PDB:2O26"
STRAND 75..78
/evidence="ECO:0000244|PDB:2O26"
STRAND 80..85
/evidence="ECO:0000244|PDB:2O26"
HELIX 90..92
/evidence="ECO:0000244|PDB:2O26"
STRAND 94..103
/evidence="ECO:0000244|PDB:2O26"
STRAND 105..113
/evidence="ECO:0000244|PDB:2O26"
STRAND 125..128
/evidence="ECO:0000244|PDB:2O26"
STRAND 133..135
/evidence="ECO:0000244|PDB:2O26"
STRAND 145..151
/evidence="ECO:0000244|PDB:2O26"
STRAND 162..166
/evidence="ECO:0000244|PDB:2O26"
TURN 167..169
/evidence="ECO:0000244|PDB:2O26"
STRAND 170..175
/evidence="ECO:0000244|PDB:2O26"
HELIX 178..180
/evidence="ECO:0000244|PDB:2O26"
STRAND 184..191
/evidence="ECO:0000244|PDB:2O26"
STRAND 194..197
/evidence="ECO:0000244|PDB:2O26"
STRAND 201..206
/evidence="ECO:0000244|PDB:2O26"
STRAND 214..216
/evidence="ECO:0000244|PDB:2O26"
STRAND 230..240
/evidence="ECO:0000244|PDB:2O26"
STRAND 244..256
/evidence="ECO:0000244|PDB:2O26"
STRAND 264..268
/evidence="ECO:0000244|PDB:2O26"
STRAND 271..282
/evidence="ECO:0000244|PDB:2O26"
STRAND 285..287
/evidence="ECO:0000244|PDB:2O26"
STRAND 289..296
/evidence="ECO:0000244|PDB:2O26"
STRAND 301..308
/evidence="ECO:0000244|PDB:2O26"
SEQUENCE 979 AA; 109343 MW; 03FB4D672248585E CRC64;
MRGARGAWDL LCVLLVLLRG QTATSQPSAS PGEPSPPSIH PAQSELIVEA GDTLSLTCID
PDFVRWTFKT YFNEMVENKK NEWIQEKAEA TRTGTYTCSN SNGLTSSIYV FVRDPAKLFL
VGLPLFGKED SDALVRCPLT DPQVSNYSLI ECDGKSLPTD LTFVPNPKAG ITIKNVKRAY
HRLCVRCAAQ RDGTWLHSDK FTLKVRAAIK AIPVVSVPET SHLLKKGDTF TVVCTIKDVS
TSVNSMWLKM NPQPQHIAQV KHNSWHRGDF NYERQETLTI SSARVDDSGV FMCYANNTFG
SANVTTTLKV VEKGFINISP VKNTTVFVTD GENVDLVVEY EAYPKPEHQQ WIYMNRTSAN
KGKDYVKSDN KSNIRYVNQL RLTRLKGTEG GTYTFLVSNS DASASVTFNV YVNTKPEILT
YDRLINGMLQ CVAEGFPEPT IDWYFCTGAE QRCTTPVSPV DVQVQNVSVS PFGKLVVQSS
IDSSVFRHNG TVECKASNDV GKSSAFFNFA FKGNNKEQIQ AHTLFTPLLI GFVVAAGAMG
IIVMVLTYKY LQKPMYEVQW KVVEEINGNN YVYIDPTQLP YDHKWEFPRN RLSFGKTLGA
GAFGKVVEAT AYGLIKSDAA MTVAVKMLKP SAHLTEREAL MSELKVLSYL GNHMNIVNLL
GACTVGGPTL VITEYCCYGD LLNFLRRKRD SFIFSKQEEQ AEAALYKNLL HSTEPSCDSS
NEYMDMKPGV SYVVPTKTDK RRSARIDSYI ERDVTPAIME DDELALDLDD LLSFSYQVAK
GMAFLASKNC IHRDLAARNI LLTHGRITKI CDFGLARDIR NDSNYVVKGN ARLPVKWMAP
ESIFSCVYTF ESDVWSYGIF LWELFSLGSS PYPGMPVDSK FYKMIKEGFR MVSPEHAPAE
MYDVMKTCWD ADPLKRPTFK QVVQLIEKQI SDSTKHIYSN LANCNPNPEN PVVVDHSVRV
NSVGSSASST QPLLVHEDA


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Pathways :
WP2328: Allograft rejection
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP313: Signaling of Hepatocyte Growth Factor Receptor
WP810: Signaling of Hepatocyte Growth Factor Receptor
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP193: Signaling of Hepatocyte Growth Factor Receptor
WP927: Signaling of Hepatocyte Growth Factor Receptor
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP444: Signaling of Hepatocyte Growth Factor Receptor
WP94: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP2272: Pathogenic Escherichia coli infection
WP352: T Cell Receptor Signaling Pathway
WP23: B Cell Receptor Signaling Pathway
WP1025: B Cell Receptor Signaling Pathway
WP894: T Cell Receptor Signaling Pathway
WP1345: T Cell Receptor Signaling Pathway
WP285: B Cell Receptor Signaling Pathway
WP1493: Carbon assimilation C4 pathway
WP794: B Cell Receptor Signaling Pathway
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP1130: T Cell Receptor Signaling Pathway
WP2292: Chemokine signaling pathway
WP274: B Cell Receptor Signaling Pathway
WP908: B Cell Receptor Signaling Pathway

Related Genes :
[KIT SCFR] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Piebald trait protein) (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)
[Kit Sl] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117)
[KIT] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117)
[KIT] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117)
[KIT] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117)
[KIT] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117)
[KIT] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117)
[KIT] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (CD antigen CD117)
[KIT] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit)
[kita kit sparse] Mast/stem cell growth factor receptor kita (SCFR) (EC 2.7.10.1) (Tyrosine-protein kinase Kit)
[Kitlg Kitl Mgf Sl Slf] Kit ligand (Hematopoietic growth factor KL) (Mast cell growth factor) (MGF) (Steel factor) (Stem cell factor) (SCF) (c-Kit ligand) [Cleaved into: Soluble KIT ligand (sKITLG)]
[kit krk1] Mast/stem cell growth factor receptor-related protein Kit (EC 2.7.10.1) (Kit-related kinase 1) (xKrk1) (Tyrosine-protein kinase kit)
[KITLG MGF SCF] Kit ligand (Mast cell growth factor) (MGF) (Stem cell factor) (SCF) (c-Kit ligand) [Cleaved into: Soluble KIT ligand (sKITLG)]
[Kitlg Kitl Mgf] Kit ligand (Hematopoietic growth factor KL) (Mast cell growth factor) (MGF) (Stem cell factor) (SCF) (c-Kit ligand) [Cleaved into: Soluble KIT ligand (sKITLG)]
[FGFR1 BFGFR CEK FGFBR FLG FLT2 HBGFR] Fibroblast growth factor receptor 1 (FGFR-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (BFGFR) (bFGF-R-1) (Fms-like tyrosine kinase 2) (FLT-2) (N-sam) (Proto-oncogene c-Fgr) (CD antigen CD331)
[KITLG MGF] Kit ligand (Mast cell growth factor) (MGF) (Stem cell factor) (SCF) (c-Kit ligand) [Cleaved into: Soluble KIT ligand (sKITLG)]
[FES FPS] Tyrosine-protein kinase Fes/Fps (EC 2.7.10.2) (Feline sarcoma/Fujinami avian sarcoma oncogene homolog) (Proto-oncogene c-Fes) (Proto-oncogene c-Fps) (p93c-fes)
[Erbb2 Neu] Receptor tyrosine-protein kinase erbB-2 (EC 2.7.10.1) (Epidermal growth factor receptor-related protein) (Proto-oncogene Neu) (Proto-oncogene c-ErbB-2) (p185erbB2) (p185neu) (CD antigen CD340)
[EGFR ERBB ERBB1 HER1] Epidermal growth factor receptor (EC 2.7.10.1) (Proto-oncogene c-ErbB-1) (Receptor tyrosine-protein kinase erbB-1)
[Fyn] Tyrosine-protein kinase Fyn (EC 2.7.10.2) (Proto-oncogene c-Fyn) (p59-Fyn)
[ERBB2 HER2 MLN19 NEU NGL] Receptor tyrosine-protein kinase erbB-2 (EC 2.7.10.1) (Metastatic lymph node gene 19 protein) (MLN 19) (Proto-oncogene Neu) (Proto-oncogene c-ErbB-2) (Tyrosine kinase-type cell surface receptor HER2) (p185erbB2) (CD antigen CD340)
[LCK] Tyrosine-protein kinase Lck (EC 2.7.10.2) (Leukocyte C-terminal Src kinase) (LSK) (Lymphocyte cell-specific protein-tyrosine kinase) (Protein YT16) (Proto-oncogene Lck) (T cell-specific protein-tyrosine kinase) (p56-LCK)
[ABL1 ABL JTK7] Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150)
[PDGFRA PDGFR2 RHEPDGFRA] Platelet-derived growth factor receptor alpha (PDGF-R-alpha) (PDGFR-alpha) (EC 2.7.10.1) (Alpha platelet-derived growth factor receptor) (Alpha-type platelet-derived growth factor receptor) (CD140 antigen-like family member A) (CD140a antigen) (Platelet-derived growth factor alpha receptor) (Platelet-derived growth factor receptor 2) (PDGFR-2) (CD antigen CD140a)
[SRC SRC1] Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)
[Lyn] Tyrosine-protein kinase Lyn (EC 2.7.10.2) (V-yes-1 Yamaguchi sarcoma viral related oncogene homolog) (p53Lyn) (p56Lyn)
[MET] Hepatocyte growth factor receptor (HGF receptor) (EC 2.7.10.1) (HGF/SF receptor) (Proto-oncogene c-Met) (Scatter factor receptor) (SF receptor) (Tyrosine-protein kinase Met)
[LYN JTK8] Tyrosine-protein kinase Lyn (EC 2.7.10.2) (Lck/Yes-related novel protein tyrosine kinase) (V-yes-1 Yamaguchi sarcoma viral related oncogene homolog) (p53Lyn) (p56Lyn)
[SRC] Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)
[Ros1 Ros Ros-1] Proto-oncogene tyrosine-protein kinase ROS (EC 2.7.10.1) (Proto-oncogene c-Ros) (Proto-oncogene c-Ros-1) (Receptor tyrosine kinase c-ros oncogene 1) (c-Ros receptor tyrosine kinase)

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