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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_HUMAN               Reviewed;         976 AA.
P10721; B5A956; D5LXN2; D5M931; F5H8F8; Q6IQ28; Q99662; Q9UM99;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
22-NOV-2017, entry version 215.
RecName: Full=Mast/stem cell growth factor receptor Kit;
Short=SCFR;
EC=2.7.10.1;
AltName: Full=Piebald trait protein;
Short=PBT;
AltName: Full=Proto-oncogene c-Kit;
AltName: Full=Tyrosine-protein kinase Kit;
AltName: Full=p145 c-kit;
AltName: Full=v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog;
AltName: CD_antigen=CD117;
Flags: Precursor;
Name=KIT; Synonyms=SCFR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY,
AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Fetal brain, and Term placenta;
PubMed=2448137;
Yarden Y., Kuang W.-J., Yang-Feng T., Coussens L., Munemitsu S.,
Dull T.J., Chen E., Schlessinger J., Francke U., Ullrich A.;
"Human proto-oncogene c-kit: a new cell surface receptor tyrosine
kinase for an unidentified ligand.";
EMBO J. 6:3341-3351(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
1 AND 2).
PubMed=1279499;
Giebel L.B., Strunk K.M., Holmes S.A., Spritz R.A.;
"Organization and nucleotide sequence of the human KIT (mast/stem cell
growth factor receptor) proto-oncogene.";
Oncogene 7:2207-2217(1992).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9027509; DOI=10.1006/geno.1996.4482;
Andre C., Hampe A., Lachaume P., Martin E., Wang X.P., Manus V.,
Hu W.X., Galibert F.;
"Sequence analysis of two genomic regions containing the KIT and the
FMS receptor tyrosine kinase genes.";
Genomics 39:216-226(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=18593464; DOI=10.1186/ar2447;
Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D.,
Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.;
"Novel splice variants derived from the receptor tyrosine kinase
superfamily are potential therapeutics for rheumatoid arthritis.";
Arthritis Res. Ther. 10:R73-R73(2008).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=20658618; DOI=10.1002/pbc.22603;
Neumann I., Foell J.L., Bremer M., Volkmer I., Korholz D., Burdach S.,
Staege M.S.;
"Retinoic acid enhances sensitivity of neuroblastoma cells for
imatinib mesylate.";
Pediatr. Blood Cancer 55:464-470(2010).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Staege M.S., Neumann I., Volkmer I.;
"Sequence of KIT mRNA from all-trans retinoic acid treated
neuroblastoma cell lines.";
Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
PubMed=7506248; DOI=10.1111/j.1349-7006.1993.tb02813.x;
Yamamoto K., Tojo A., Aoki N., Shibuya M.;
"Characterization of the promoter region of the human c-kit proto-
oncogene.";
Jpn. J. Cancer Res. 84:1136-1144(1993).
[11]
FUNCTION IN PHOSPHORYLATION OF PIK3R1; RAF1 AND MAPK1, INTERACTION
WITH GRB2; PIK3R1 AND PIK3 CATALYTIC SUBUNIT, ENZYME REGULATION, AND
PHOSPHORYLATION.
PubMed=7520444;
Blume-Jensen P., Ronnstrand L., Gout I., Waterfield M.D., Heldin C.H.;
"Modulation of Kit/stem cell factor receptor-induced signaling by
protein kinase C.";
J. Biol. Chem. 269:21793-21802(1994).
[12]
PHOSPHORYLATION AT SER-741; SER-746; SER-821 AND SER-959, ENZYME
REGULATION, PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS OF SER-741 AND
SER-746.
PubMed=7539802; DOI=10.1074/jbc.270.23.14192;
Blume-Jensen P., Wernstedt C., Heldin C.H., Ronnstrand L.;
"Identification of the major phosphorylation sites for protein kinase
C in kit/stem cell factor receptor in vitro and in intact cells.";
J. Biol. Chem. 270:14192-14200(1995).
[13]
INTERACTION WITH PIK3R1; MATK/CHK; FYN AND SHC1, AND PHOSPHORYLATION
AT TYR-568; TYR-570 AND TYR-721.
PubMed=9038210; DOI=10.1074/jbc.272.9.5915;
Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.;
"Direct association of Csk homologous kinase (CHK) with the
diphosphorylated site Tyr568/570 of the activated c-KIT in
megakaryocytes.";
J. Biol. Chem. 272:5915-5920(1997).
[14]
INTERACTION WITH LYN.
PubMed=9341198; DOI=10.1074/jbc.272.43.27450;
Linnekin D., DeBerry C.S., Mou S.;
"Lyn associates with the juxtamembrane region of c-Kit and is
activated by stem cell factor in hematopoietic cell lines and normal
progenitor cells.";
J. Biol. Chem. 272:27450-27455(1997).
[15]
INTERACTION WITH PTPN6, AUTOPHOSPHORYLATION, AND FUNCTION IN
PHOSPHORYLATION OF PTPN6.
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).
[16]
INTERACTION WITH GRB2 AND GRB7, PARTIAL PROTEIN SEQUENCE,
AUTOPHOSPHORYLATION, AND PHOSPHORYLATION AT TYR-703 AND TYR-936.
PubMed=10377264; DOI=10.1042/bj3410211;
Thommes K., Lennartsson J., Carlberg M., Ronnstrand L.;
"Identification of Tyr-703 and Tyr-936 as the primary association
sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor.";
Biochem. J. 341:211-216(1999).
[17]
INTERACTION WITH PTPRU, AND FUNCTION IN PHOSPHORYLATION OF PTPRU.
PubMed=10397721;
Taniguchi Y., London R., Schinkmann K., Jiang S., Avraham H.;
"The receptor protein tyrosine phosphatase, PTP-RO, is upregulated
during megakaryocyte differentiation and is associated with the c-Kit
receptor.";
Blood 94:539-549(1999).
[18]
INTERACTION WITH MPDZ, CHARACTERIZATION OF VARIANT VAL-816, AND
MUTAGENESIS OF LYS-623.
PubMed=11018522; DOI=10.1016/S0014-5793(00)02036-6;
Mancini A., Koch A., Stefan M., Niemann H., Tamura T.;
"The direct association of the multiple PDZ domain containing proteins
(MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine
kinase activity.";
FEBS Lett. 482:54-58(2000).
[19]
INTERACTION WITH LYN; TEC AND DOK1.
PubMed=11825908; DOI=10.1074/jbc.M200277200;
Liang X., Wisniewski D., Strife A., Shivakrupa R., Clarkson B.,
Resh M.D.;
"Phosphatidylinositol 3-kinase and Src family kinases are required for
phosphorylation and membrane recruitment of Dok-1 in c-Kit
signaling.";
J. Biol. Chem. 277:13732-13738(2002).
[20]
INTERACTION WITH SH2B2/APS, FUNCTION IN PHOSPHORYLATION OF SH2B2/APS,
AND MUTAGENESIS OF ILE-571 AND LEU-939.
PubMed=12444928; DOI=10.1042/BJ20020716;
Wollberg P., Lennartsson J., Gottfridsson E., Yoshimura A.,
Ronnstrand L.;
"The adapter protein APS associates with the multifunctional docking
sites Tyr-568 and Tyr-936 in c-Kit.";
Biochem. J. 370:1033-1038(2003).
[21]
PHOSPHORYLATION AT SER-891 AND TYR-900, PARTIAL PROTEIN SEQUENCE,
INTERACTION WITH CRK AND PIK3R1, FUNCTION IN PHOSPHORYLATION OF CRK;
AKT1 AND MAP KINASES, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12878163; DOI=10.1016/S0014-4827(03)00206-4;
Lennartsson J., Wernstedt C., Engstrom U., Hellman U., Ronnstrand L.;
"Identification of Tyr900 in the kinase domain of c-Kit as a Src-
dependent phosphorylation site mediating interaction with c-Crk.";
Exp. Cell Res. 288:110-118(2003).
[22]
FUNCTION, AND ALTERNATIVE SPLICING.
PubMed=12511554; DOI=10.1074/jbc.M211726200;
Voytyuk O., Lennartsson J., Mogi A., Caruana G., Courtneidge S.,
Ashman L.K., Ronnstrand L.;
"Src family kinases are involved in the differential signaling from
two splice forms of c-Kit.";
J. Biol. Chem. 278:9159-9166(2003).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[24]
INTERACTION WITH FES/FPS, AND CHARACTERIZATION OF VARIANT VAL-816.
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).
[25]
INTERACTION WITH GRB2 AND CBL, UBIQUITINATION, AND FUNCTION IN
PHOSPHORYLATION OF CBL.
PubMed=17904548; DOI=10.1016/j.yexcr.2007.08.021;
Sun J., Pedersen M., Bengtsson S., Ronnstrand L.;
"Grb2 mediates negative regulation of stem cell factor receptor/c-Kit
signaling by recruitment of Cbl.";
Exp. Cell Res. 313:3935-3942(2007).
[26]
FUNCTION IN ACTIVATION OF SIGNALING PATHWAYS AND CELL SURVIVAL,
FUNCTION IN PHOSPHORYLATION OF CBL, PHOSPHORYLATION AT TYR-568;
TYR-703; TYR-721 AND TYR-936, UBIQUITINATION, SUBCELLULAR LOCATION,
AND CHARACTERIZATION OF VARIANT VAL-816.
PubMed=19265199; DOI=10.1074/jbc.M808058200;
Sun J., Pedersen M., Ronnstrand L.;
"The D816V mutation of c-Kit circumvents a requirement for Src family
kinases in c-Kit signal transduction.";
J. Biol. Chem. 284:11039-11047(2009).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-959, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[28]
SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=20601678; DOI=10.1093/humrep/deq168;
Muciaccia B., Sette C., Paronetto M.P., Barchi M., Pensini S.,
D'Agostino A., Gandini L., Geremia R., Stefanini M., Rossi P.;
"Expression of a truncated form of KIT tyrosine kinase in human
spermatozoa correlates with sperm DNA integrity.";
Hum. Reprod. 25:2188-2202(2010).
[29]
PHOSPHORYLATION AT TYR-547; TYR-553; TYR-703; TYR-721; TYR-730;
TYR-823 AND TYR-900, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS
OF TYR-823, AND CHARACTERIZATION OF VARIANT HIS-816.
PubMed=20147452; DOI=10.1093/jb/mvq015;
DiNitto J.P., Deshmukh G.D., Zhang Y., Jacques S.L., Coli R.,
Worrall J.W., Diehl W., English J.M., Wu J.C.;
"Function of activation loop tyrosine phosphorylation in the mechanism
of c-Kit auto-activation and its implication in sunitinib
resistance.";
J. Biochem. 147:601-609(2010).
[30]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION,
SUBUNIT, AND CHARACTERIZATION OF VARIANT VAL-816.
PubMed=21640708; DOI=10.1016/j.bbrc.2011.05.111;
Kim S.Y., Kang J.J., Lee H.H., Kang J.J., Kim B., Kim C.G., Park T.K.,
Kang H.;
"Mechanism of activation of human c-KIT kinase by internal tandem
duplications of the juxtamembrane domain and point mutations at
aspartic acid 816.";
Biochem. Biophys. Res. Commun. 410:224-228(2011).
[31]
FUNCTION IN ACTIVATION AND PHOSPHORYLATION OF STAT1; STAT3; STAT5A AND
STAT5B.
PubMed=21135090; DOI=10.1074/jbc.M110.182642;
Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.;
"Mechanisms of STAT protein activation by oncogenic KIT mutants in
neoplastic mast cells.";
J. Biol. Chem. 286:5956-5966(2011).
[32]
REVIEW.
PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
Ronnstrand L.;
"Signal transduction via the stem cell factor receptor/c-Kit.";
Cell. Mol. Life Sci. 61:2535-2548(2004).
[33]
REVIEW ON KIT SIGNALING.
PubMed=16129412; DOI=10.1016/j.bbrc.2005.08.055;
Roskoski R. Jr.;
"Signaling by Kit protein-tyrosine kinase--the stem cell factor
receptor.";
Biochem. Biophys. Res. Commun. 337:1-13(2005).
[34]
REVIEW.
PubMed=15625120; DOI=10.1634/stemcells.2004-0117;
Lennartsson J., Jelacic T., Linnekin D., Shivakrupa R.;
"Normal and oncogenic forms of the receptor tyrosine kinase kit.";
Stem Cells 23:16-43(2005).
[35]
REVIEW.
PubMed=18381929; DOI=10.1158/1078-0432.CCR-07-5134;
Kent D., Copley M., Benz C., Dykstra B., Bowie M., Eaves C.;
"Regulation of hematopoietic stem cells by the steel factor/KIT
signaling pathway.";
Clin. Cancer Res. 14:1926-1930(2008).
[36]
REVIEW.
PubMed=21057534; DOI=10.1038/onc.2010.494;
Pittoni P., Piconese S., Tripodo C., Colombo M.P.;
"Tumor-intrinsic and -extrinsic roles of c-Kit: mast cells as the
primary off-target of tyrosine kinase inhibitors.";
Oncogene 30:757-769(2011).
[37]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 549-931 IN COMPLEX WITH ADP
AND MAGNESIUM IONS, SUBUNIT, PHOSPHORYLATION AT TYR-568 AND TYR-570,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12824176; DOI=10.1074/jbc.C300186200;
Mol C.D., Lim K.B., Sridhar V., Zou H., Chien E.Y., Sang B.C.,
Nowakowski J., Kassel D.B., Cronin C.N., McRee D.E.;
"Structure of a c-kit product complex reveals the basis for kinase
transactivation.";
J. Biol. Chem. 278:31461-31464(2003).
[38]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 565-935 IN COMPLEXES WITH
INHIBITOR IMATINIB AND PHOSPHATE, AND ENZYME REGULATION.
PubMed=15123710; DOI=10.1074/jbc.M403319200;
Mol C.D., Dougan D.R., Schneider T.R., Skene R.J., Kraus M.L.,
Scheibe D.N., Snell G.P., Zou H., Sang B.C., Wilson K.P.;
"Structural basis for the autoinhibition and STI-571 inhibition of c-
Kit tyrosine kinase.";
J. Biol. Chem. 279:31655-31663(2004).
[39]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-519 IN COMPLEX WITH
KITLG/SCF, INTERACTION WITH KITLG/SCF, SUBUNIT, DISULFIDE BONDS,
CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF ARG-381 AND
GLU-386, AND GLYCOSYLATION AT ASN-130; ASN-283; ASN-293; ASN-300;
ASN-320; ASN-352 AND ASN-367.
PubMed=17662946; DOI=10.1016/j.cell.2007.05.055;
Yuzawa S., Opatowsky Y., Zhang Z., Mandiyan V., Lax I.,
Schlessinger J.;
"Structural basis for activation of the receptor tyrosine kinase KIT
by stem cell factor.";
Cell 130:323-334(2007).
[40]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 544-935 IN COMPLEX WITH
SUNITINIB, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, CHARACTERIZATION
OF VARIANTS HIS-816 AND VAL-816, AND ENZYME REGULATION.
PubMed=19164557; DOI=10.1073/pnas.0812413106;
Gajiwala K.S., Wu J.C., Christensen J., Deshmukh G.D., Diehl W.,
DiNitto J.P., English J.M., Greig M.J., He Y.A., Jacques S.L.,
Lunney E.A., McTigue M., Molina D., Quenzer T., Wells P.A., Yu X.,
Zhang Y., Zou A., Emmett M.R., Marshall A.G., Zhang H.M.,
Demetri G.D.;
"KIT kinase mutants show unique mechanisms of drug resistance to
imatinib and sunitinib in gastrointestinal stromal tumor patients.";
Proc. Natl. Acad. Sci. U.S.A. 106:1542-1547(2009).
[41]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 564-574 IN COMPLEX WITH
SOCS6, AND PHOSPHORYLATION AT TYR-568.
PubMed=21030588; DOI=10.1074/jbc.M110.173526;
Zadjali F., Pike A.C., Vesterlund M., Sun J., Wu C., Li S.S.,
Ronnstrand L., Knapp S., Bullock A.N., Flores-Morales A.;
"Structural basis for c-KIT inhibition by the suppressor of cytokine
signaling 6 (SOCS6) ubiquitin ligase.";
J. Biol. Chem. 286:480-490(2011).
[42]
VARIANT PBT LYS-583.
PubMed=1376329; DOI=10.1172/JCI115772;
Fleischman R.A.;
"Human piebald trait resulting from a dominant negative mutant allele
of the c-kit membrane receptor gene.";
J. Clin. Invest. 89:1713-1717(1992).
[43]
VARIANT PBT LEU-584.
PubMed=1370874;
Spritz R.A., Giebel L.B., Holmes S.A.;
"Dominant negative and loss of function mutations of the c-kit
(mast/stem cell growth factor receptor) proto-oncogene in human
piebaldism.";
Am. J. Hum. Genet. 50:261-269(1992).
[44]
VARIANT PBT ARG-664.
PubMed=1717985; DOI=10.1073/pnas.88.19.8696;
Giebel L.B., Spritz R.A.;
"Mutation of the KIT (mast/stem cell growth factor receptor)
protooncogene in human piebaldism.";
Proc. Natl. Acad. Sci. U.S.A. 88:8696-8699(1991).
[45]
VARIANT MAST CELL LEUKEMIA VAL-816.
PubMed=7691885; DOI=10.1172/JCI116761;
Furitsu T., Tsujimura T., Tono T., Ikeda H., Kitayama H.,
Koshimizu U., Sugahara H., Butterfield J.H., Ashman L.K., Kanayama Y.,
Matsuzawa Y., Kitamura Y., Kanakura Y.;
"Identification of mutations in the coding sequence of the proto-
oncogene c-kit in a human mast cell leukemia cell line causing ligand-
independent activation of c-kit product.";
J. Clin. Invest. 92:1736-1744(1993).
[46]
VARIANTS PBT GLY-791 AND VAL-812.
PubMed=7687267; DOI=10.1111/1523-1747.ep12358440;
Spritz R.A., Holmes S.A., Itin P., Kuester W.;
"Novel mutations of the KIT (mast/stem cell growth factor receptor)
proto-oncogene in human piebaldism.";
J. Invest. Dermatol. 101:22-25(1993).
[47]
VARIANT PBT 893-GLU--PRO-896 DEL.
PubMed=8680409; DOI=10.1002/humu.1380060409;
Riva P., Milani N., Gandolfi P., Larizza L.;
"A 12-bp deletion (7818del12) in the c-kit protooncogene in a large
Italian kindred with piebaldism.";
Hum. Mutat. 6:343-345(1995).
[48]
VARIANT MAST CELL DISEASE GLY-820.
PubMed=9029028; DOI=10.1046/j.1365-2141.1997.d01-2042.x;
Pignon J.-M., Giraudier S., Duquesnoy P., Jouault H., Imbert M.,
Vainchenker W., Vernant J.-P., Tulliez M.;
"A new c-kit mutation in a case of aggressive mast cell disease.";
Br. J. Haematol. 96:374-376(1997).
[49]
VARIANT PBT GLY-796.
PubMed=9450866;
DOI=10.1002/(SICI)1096-8628(19980106)75:1<101::AID-AJMG20>3.0.CO;2-P;
Spritz R.A., Beighton P.;
"Piebaldism with deafness: molecular evidence for an expanded
syndrome.";
Am. J. Med. Genet. 75:101-103(1998).
[50]
VARIANT ACUTE MYELOID LEUKEMIA TYR-816.
PubMed=9657776;
Beghini A., Larizza L., Cairoli R., Morra E.;
"c-kit activating mutations and mast cell proliferation in human
leukemia.";
Blood 92:701-702(1998).
[51]
VARIANT PBT PRO-847.
PubMed=9699740; DOI=10.1046/j.1523-1747.1998.00269.x;
Nomura K., Hatayama I., Narita T., Kaneko T., Shiraishi M.;
"A novel KIT gene missense mutation in a Japanese family with
piebaldism.";
J. Invest. Dermatol. 111:337-338(1998).
[52]
VARIANT GIST VAL-559 DEL.
PubMed=9697690; DOI=10.1038/1209;
Nishida T., Hirota S., Taniguchi M., Hashimoto K., Isozaki K.,
Nakamura H., Kanakura Y., Tanaka T., Takabayashi A., Matsuda H.,
Kitamura Y.;
"Familial gastrointestinal stromal tumours with germline mutation of
the KIT gene.";
Nat. Genet. 19:323-324(1998).
[53]
VARIANTS GIST ILE-550; 550-LYS--LYS-558 DEL; 551-PRO--VAL-555 DEL;
ASP-559 AND 559-VAL-VAL-560 DEL.
PubMed=9438854; DOI=10.1126/science.279.5350.577;
Hirota S., Isozaki K., Moriyama Y., Hashimoto K., Nishida T.,
Ishiguro S., Kawano K., Hanada M., Kurata A., Takeda M.,
Muhammad Tunio G., Matsuzawa Y., Kanakura Y., Shinomura Y.,
Kitamura Y.;
"Gain-of-function mutations of c-kit in human gastrointestinal stromal
tumors.";
Science 279:577-580(1998).
[54]
VARIANT HIS-816, AND CHARACTERIZATION OF VARIANT HIS-816.
PubMed=10362788; DOI=10.1016/S0002-9440(10)65419-3;
Tian Q., Frierson H.F. Jr., Krystal G.W., Moskaluk C.A.;
"Activating c-kit gene mutations in human germ cell tumors.";
Am. J. Pathol. 154:1643-1647(1999).
[55]
VARIANTS MASTOCYTOSIS VAL-816; PHE-816; TYR-816 AND LYS-839, AND
CHARACTERIZATION OF VARIANTS MASTOCYTOSIS VAL-816; PHE-816; TYR-816
AND LYS-839.
PubMed=9990072; DOI=10.1073/pnas.96.4.1609;
Longley B.J. Jr., Metcalfe D.D., Tharp M., Wang X., Tyrrell L.,
Lu S.-Z., Heitjan D., Ma Y.;
"Activating and dominant inactivating c-KIT catalytic domain mutations
in distinct clinical forms of human mastocytosis.";
Proc. Natl. Acad. Sci. U.S.A. 96:1609-1614(1999).
[56]
VARIANTS PBT CYS-584; ARG-601 AND PRO-656.
PubMed=11074500;
DOI=10.1002/1096-8628(20001106)95:1<79::AID-AJMG16>3.0.CO;2-4;
Syrris P., Malik N.M., Murday V.A., Patton M.A., Carter N.D.,
Hughes H.E., Metcalfe K.;
"Three novel mutations of the proto-oncogene KIT cause human
piebaldism.";
Am. J. Med. Genet. 95:79-81(2000).
[57]
VARIANT GIST ALA-559.
PubMed=11505412;
DOI=10.1002/1097-0142(20010801)92:3<657::AID-CNCR1367>3.0.CO;2-D;
Beghini A., Tibiletti M.G., Roversi G., Chiaravalli A.M., Serio G.,
Capella C., Larizza L.;
"Germline mutation in the juxtamembrane domain of the kit gene in a
family with gastrointestinal stromal tumors and urticaria
pigmentosa.";
Cancer 92:657-662(2001).
[58]
VARIANT GIST 550-LYS--LYS-558 DEL.
PubMed=15824741; DOI=10.1038/sj.onc.1208587;
Chen L.L., Sabripour M., Wu E.F., Prieto V.G., Fuller G.N.,
Frazier M.L.;
"A mutation-created novel intra-exonic pre-mRNA splice site causes
constitutive activation of KIT in human gastrointestinal stromal
tumors.";
Oncogene 24:4271-4280(2005).
[59]
VARIANTS TYR-816; LYS-822 AND PRO-829.
PubMed=16175573; DOI=10.1002/gcc.20265;
Bignell G., Smith R., Hunter C., Stephens P., Davies H., Greenman C.,
Teague J., Butler A., Edkins S., Stevens C., O'meara S., Parker A.,
Avis T., Barthorpe S., Brackenbury L., Buck G., Clements J., Cole J.,
Dicks E., Edwards K., Forbes S., Gorton M., Gray K., Halliday K.,
Harrison R., Hills K., Hinton J., Jones D., Kosmidou V., Laman R.,
Lugg R., Menzies A., Perry J., Petty R., Raine K., Shepherd R.,
Small A., Solomon H., Stephens Y., Tofts C., Varian J., Webb A.,
West S., Widaa S., Yates A., Gillis A.J.M., Stoop H.J.,
van Gurp R.J.H.L.M., Oosterhuis J.W., Looijenga L.H.J., Futreal P.A.,
Wooster R., Stratton M.R.;
"Sequence analysis of the protein kinase gene family in human
testicular germ-cell tumors of adolescents and adults.";
Genes Chromosomes Cancer 45:42-46(2006).
[60]
VARIANTS [LARGE SCALE ANALYSIS] ILE-532; LEU-541; SER-691; ASN-715;
ASN-737; TRP-804; TYR-816; LYS-822 AND PRO-829.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- 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: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}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:17662946,
ECO:0000269|PubMed:19164557, ECO:0000269|PubMed:21640708,
ECO:0000269|PubMed:2448137}.
-!- ENZYME 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}.
-!- 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 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.
{ECO:0000250|UniProtKB:P05532, ECO:0000269|PubMed:10377264,
ECO:0000269|PubMed:10397721, ECO:0000269|PubMed:11018522,
ECO:0000269|PubMed:11825908, ECO:0000269|PubMed:12444928,
ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:12878163,
ECO:0000269|PubMed:17595334, ECO:0000269|PubMed:17662946,
ECO:0000269|PubMed:17904548, ECO:0000269|PubMed:19164557,
ECO:0000269|PubMed:21030588, ECO:0000269|PubMed:21640708,
ECO:0000269|PubMed:7520444, ECO:0000269|PubMed:9038210,
ECO:0000269|PubMed:9341198, ECO:0000269|PubMed:9528781}.
-!- INTERACTION:
P00519:ABL1; NbExp=2; IntAct=EBI-1379503, EBI-375543;
P42684:ABL2; NbExp=2; IntAct=EBI-1379503, EBI-1102694;
O75815:BCAR3; NbExp=3; IntAct=EBI-1379503, EBI-702336;
P51451:BLK; NbExp=5; IntAct=EBI-1379503, EBI-2105445;
Q8WV28:BLNK; NbExp=2; IntAct=EBI-1379503, EBI-2623522;
P46108:CRK; NbExp=4; IntAct=EBI-1379503, EBI-886;
P07332:FES; NbExp=2; IntAct=EBI-1379503, EBI-1055635;
P09769:FGR; NbExp=2; IntAct=EBI-1379503, EBI-1383732;
O75791:GRAP2; NbExp=2; IntAct=EBI-1379503, EBI-740418;
P62993:GRB2; NbExp=6; IntAct=EBI-1379503, EBI-401755;
Q14451:GRB7; NbExp=4; IntAct=EBI-1379503, EBI-970191;
P08631:HCK; NbExp=2; IntAct=EBI-1379503, EBI-346340;
Q96JZ2:HSH2D; NbExp=5; IntAct=EBI-1379503, EBI-3919324;
P21583:KITLG; NbExp=2; IntAct=EBI-1379503, EBI-1379527;
P06239:LCK; NbExp=8; IntAct=EBI-1379503, EBI-1348;
P07948:LYN; NbExp=7; IntAct=EBI-1379503, EBI-79452;
Q8VBX6:Mpdz (xeno); NbExp=4; IntAct=EBI-1379503, EBI-8026435;
P16333:NCK1; NbExp=3; IntAct=EBI-1379503, EBI-389883;
O43639:NCK2; NbExp=2; IntAct=EBI-1379503, EBI-713635;
P27986:PIK3R1; NbExp=19; IntAct=EBI-1379503, EBI-79464;
O00459:PIK3R2; NbExp=19; IntAct=EBI-1379503, EBI-346930;
Q92569:PIK3R3; NbExp=31; IntAct=EBI-1379503, EBI-79893;
P19174:PLCG1; NbExp=31; IntAct=EBI-1379503, EBI-79387;
P16885:PLCG2; NbExp=8; IntAct=EBI-1379503, EBI-617403;
Q13882:PTK6; NbExp=4; IntAct=EBI-1379503, EBI-1383632;
Q06124:PTPN11; NbExp=29; IntAct=EBI-1379503, EBI-297779;
P35235:Ptpn11 (xeno); NbExp=2; IntAct=EBI-1379503, EBI-397236;
Q92729:PTPRU; NbExp=2; IntAct=EBI-1379503, EBI-7052301;
P20936:RASA1; NbExp=16; IntAct=EBI-1379503, EBI-1026476;
Q9UQQ2:SH2B3; NbExp=2; IntAct=EBI-1379503, EBI-7879749;
O14796:SH2D1B; NbExp=8; IntAct=EBI-1379503, EBI-3923013;
Q9NP31:SH2D2A; NbExp=10; IntAct=EBI-1379503, EBI-490630;
Q8N5H7:SH2D3C; NbExp=4; IntAct=EBI-1379503, EBI-745980;
P78314:SH3BP2; NbExp=3; IntAct=EBI-1379503, EBI-727062;
Q15464:SHB; NbExp=2; IntAct=EBI-1379503, EBI-4402156;
P29353:SHC1; NbExp=8; IntAct=EBI-1379503, EBI-78835;
P98077:SHC2; NbExp=5; IntAct=EBI-1379503, EBI-7256023;
Q92529:SHC3; NbExp=3; IntAct=EBI-1379503, EBI-79084;
Q9H6Q3:SLA2; NbExp=2; IntAct=EBI-1379503, EBI-1222854;
O14508:SOCS2; NbExp=4; IntAct=EBI-1379503, EBI-617737;
O14543:SOCS3; NbExp=3; IntAct=EBI-1379503, EBI-714146;
O14544:SOCS6; NbExp=12; IntAct=EBI-1379503, EBI-3929549;
P12931:SRC; NbExp=5; IntAct=EBI-1379503, EBI-621482;
Q9ULZ2:STAP1; NbExp=3; IntAct=EBI-1379503, EBI-6083058;
Q9HBL0:TNS1; NbExp=2; IntAct=EBI-1379503, EBI-3389814;
Q63HR2:TNS2; NbExp=2; IntAct=EBI-1379503, EBI-949753;
Q68CZ2:TNS3; NbExp=5; IntAct=EBI-1379503, EBI-1220488;
P42681:TXK; NbExp=3; IntAct=EBI-1379503, EBI-7877438;
P07947:YES1; NbExp=7; IntAct=EBI-1379503, EBI-515331;
P43403:ZAP70; NbExp=2; IntAct=EBI-1379503, EBI-1211276;
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=GNNK(+), KitA(+);
IsoId=P10721-1; Sequence=Displayed;
Name=2; Synonyms=GNNK(-), Kit(+);
IsoId=P10721-2; Sequence=VSP_038385;
Name=3; Synonyms=TR-KIT;
IsoId=P10721-3; Sequence=VSP_041866, VSP_041867;
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:20601678, ECO:0000269|PubMed:2448137}.
-!- INDUCTION: Up-regulated by cis-retinoic acid in neuroblastoma cell
lines. {ECO:0000269|PubMed:20658618}.
-!- 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}.
-!- 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 mutations 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.
-!- 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}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/KITID127.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=CD117 entry;
URL="https://en.wikipedia.org/wiki/CD117";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=two's company - Issue
163 of August 2014;
URL="https://web.expasy.org/spotlight/back_issues/163/";
-----------------------------------------------------------------------
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EMBL; X06182; CAA29548.1; -; mRNA.
EMBL; X69301; CAA49159.1; -; Genomic_DNA.
EMBL; X69302; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69303; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69304; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69305; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69306; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69307; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69308; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69309; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69310; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69311; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69312; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69313; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69314; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69315; CAA49159.1; JOINED; Genomic_DNA.
EMBL; X69316; CAA49159.1; JOINED; Genomic_DNA.
EMBL; U63834; AAC50968.1; -; Genomic_DNA.
EMBL; U63834; AAC50969.1; -; Genomic_DNA.
EMBL; EU826594; ACF47630.1; -; mRNA.
EMBL; GU983671; ADF36702.1; -; mRNA.
EMBL; HM015525; ADF50068.1; -; mRNA.
EMBL; HM015526; ADF50069.1; -; mRNA.
EMBL; AK304031; BAG64945.1; -; mRNA.
EMBL; AC006552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC071593; AAH71593.1; -; mRNA.
EMBL; S67773; AAB29529.1; -; Genomic_DNA.
CCDS; CCDS3496.1; -. [P10721-1]
CCDS; CCDS47058.1; -. [P10721-2]
PIR; S01426; TVHUKT.
RefSeq; NP_000213.1; NM_000222.2. [P10721-1]
RefSeq; NP_001087241.1; NM_001093772.1. [P10721-2]
UniGene; Hs.479754; -.
PDB; 1PKG; X-ray; 2.90 A; A/B=549-935.
PDB; 1QZJ; Model; -; A=576-932.
PDB; 1QZK; Model; -; A=576-932.
PDB; 1R01; Model; -; A=576-932.
PDB; 1T45; X-ray; 1.90 A; A=547-693, A=754-935.
PDB; 1T46; X-ray; 1.60 A; A=565-693, A=754-935.
PDB; 2E9W; X-ray; 3.50 A; A/B=26-514.
PDB; 2EC8; X-ray; 3.00 A; A=1-519.
PDB; 2IUH; X-ray; 2.00 A; B=718-728.
PDB; 2VIF; X-ray; 1.45 A; P=564-574.
PDB; 3G0E; X-ray; 1.60 A; A=544-693, A=754-935.
PDB; 3G0F; X-ray; 2.60 A; A/B=544-693, A/B=754-935.
PDB; 4HVS; X-ray; 1.90 A; A=551-934.
PDB; 4K94; X-ray; 2.40 A; C=308-518.
PDB; 4K9E; X-ray; 2.70 A; C=308-518.
PDB; 4PGZ; X-ray; 2.40 A; A/B/C=308-518.
PDB; 4U0I; X-ray; 2.00 A; A=563-693, A=754-935.
PDBsum; 1PKG; -.
PDBsum; 1QZJ; -.
PDBsum; 1QZK; -.
PDBsum; 1R01; -.
PDBsum; 1T45; -.
PDBsum; 1T46; -.
PDBsum; 2E9W; -.
PDBsum; 2EC8; -.
PDBsum; 2IUH; -.
PDBsum; 2VIF; -.
PDBsum; 3G0E; -.
PDBsum; 3G0F; -.
PDBsum; 4HVS; -.
PDBsum; 4K94; -.
PDBsum; 4K9E; -.
PDBsum; 4PGZ; -.
PDBsum; 4U0I; -.
ProteinModelPortal; P10721; -.
SMR; P10721; -.
BioGrid; 110015; 50.
DIP; DIP-1055N; -.
IntAct; P10721; 66.
MINT; MINT-146746; -.
STRING; 9606.ENSP00000288135; -.
BindingDB; P10721; -.
ChEMBL; CHEMBL1936; -.
DrugBank; DB06080; ABT-869.
DrugBank; DB01254; Dasatinib.
DrugBank; DB00619; Imatinib.
DrugBank; DB09078; Lenvatinib.
DrugBank; DB05216; MP470.
DrugBank; DB04868; Nilotinib.
DrugBank; DB05913; OSI-930.
DrugBank; DB06589; Pazopanib.
DrugBank; DB01962; Phosphonotyrosine.
DrugBank; DB08901; Ponatinib.
DrugBank; DB08896; Regorafenib.
DrugBank; DB00398; Sorafenib.
DrugBank; DB01268; Sunitinib.
DrugBank; DB05153; XL184.
DrugBank; DB05146; XL820.
GuidetoPHARMACOLOGY; 1805; -.
iPTMnet; P10721; -.
PhosphoSitePlus; P10721; -.
BioMuta; KIT; -.
DMDM; 125472; -.
MaxQB; P10721; -.
PaxDb; P10721; -.
PeptideAtlas; P10721; -.
PRIDE; P10721; -.
DNASU; 3815; -.
Ensembl; ENST00000288135; ENSP00000288135; ENSG00000157404. [P10721-1]
Ensembl; ENST00000412167; ENSP00000390987; ENSG00000157404. [P10721-2]
GeneID; 3815; -.
KEGG; hsa:3815; -.
UCSC; uc010igr.4; human. [P10721-1]
CTD; 3815; -.
DisGeNET; 3815; -.
EuPathDB; HostDB:ENSG00000157404.15; -.
GeneCards; KIT; -.
HGNC; HGNC:6342; KIT.
HPA; CAB003288; -.
HPA; CAB068253; -.
HPA; CAB072867; -.
HPA; HPA004471; -.
HPA; HPA073252; -.
MalaCards; KIT; -.
MIM; 164920; gene.
MIM; 172800; phenotype.
MIM; 273300; phenotype.
MIM; 601626; phenotype.
MIM; 606764; phenotype.
neXtProt; NX_P10721; -.
OpenTargets; ENSG00000157404; -.
Orphanet; 98829; 'Acute myeloid leukemia with abnormal bone marrow eosinophils inv(16)(p13q22) or t(16;16)(p13;q22)'.
Orphanet; 102724; 'Acute myeloid leukemia with t(8;21)(q22;q22) translocation'.
Orphanet; 98834; Acute myeloblastic leukemia with maturation.
Orphanet; 158799; Aleukemic mast cell leukemia.
Orphanet; 280785; Bullous diffuse cutaneous mastocytosis.
Orphanet; 158796; Classic mast cell leukemia.
Orphanet; 79455; Cutaneous mastocytoma.
Orphanet; 44890; Gastrointestinal stromal tumor.
Orphanet; 158778; Isolated bone marrow mastocytosis.
Orphanet; 158793; Lymphoadenopathic mastocytosis with eosinophilia.
Orphanet; 158772; Nodular urticaria pigmentosa.
Orphanet; 2884; Piebaldism.
Orphanet; 158769; Plaque-form urticaria pigmentosa.
Orphanet; 280794; Pseudoxanthomatous diffuse cutaneous mastocytosis.
Orphanet; 158775; Smouldering systemic mastocytosis.
Orphanet; 98849; Systemic mastocytosis with an associated clonal hematologic non-mast cell lineage disease.
Orphanet; 90389; Telangiectasia macularis eruptiva perstans.
Orphanet; 158766; Typical urticaria pigmentosa.
PharmGKB; PA30128; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000112008; -.
HOVERGEN; HBG104348; -.
InParanoid; P10721; -.
KO; K05091; -.
OMA; PTFKQIV; -.
OrthoDB; EOG091G01TL; -.
PhylomeDB; P10721; -.
TreeFam; TF325768; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1433559; Regulation of KIT signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
SignaLink; P10721; -.
SIGNOR; P10721; -.
ChiTaRS; KIT; human.
EvolutionaryTrace; P10721; -.
GeneWiki; CD117; -.
GenomeRNAi; 3815; -.
PRO; PR:P10721; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000157404; -.
CleanEx; HS_KIT; -.
ExpressionAtlas; P10721; baseline and differential.
Genevisible; P10721; HS.
GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019955; F:cytokine binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:ProtInc.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0004716; F:signal transducer, downstream of receptor, with protein tyrosine kinase activity; TAS:ProtInc.
GO; GO:0005020; F:stem cell factor receptor activity; IEA:Ensembl.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; IDA:UniProtKB.
GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0002371; P:dendritic cell cytokine production; ISS:UniProtKB.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISS:UniProtKB.
GO; GO:0048565; P:digestive tract development; ISS:UniProtKB.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
GO; GO:0035162; P:embryonic hemopoiesis; ISS:UniProtKB.
GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0038162; P:erythropoietin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0038093; P:Fc receptor signaling pathway; IDA:UniProtKB.
GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
GO; GO:0006687; P:glycosphingolipid metabolic process; IEA:Ensembl.
GO; GO:0035701; P:hematopoietic stem cell migration; IEA:Ensembl.
GO; GO:0030097; P:hemopoiesis; TAS:UniProtKB.
GO; GO:0002327; P:immature B cell differentiation; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0038109; P:Kit signaling pathway; IDA:UniProtKB.
GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
GO; GO:0002320; P:lymphoid progenitor cell differentiation; IEA:Ensembl.
GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0002551; P:mast cell chemotaxis; IDA:UniProtKB.
GO; GO:0032762; P:mast cell cytokine production; IDA:UniProtKB.
GO; GO:0043303; P:mast cell degranulation; IMP:UniProtKB.
GO; GO:0060374; P:mast cell differentiation; ISS:UniProtKB.
GO; GO:0070662; P:mast cell proliferation; TAS:UniProtKB.
GO; GO:0035855; P:megakaryocyte development; ISS:UniProtKB.
GO; GO:0097326; P:melanocyte adhesion; ISS:UniProtKB.
GO; GO:0030318; P:melanocyte differentiation; ISS:UniProtKB.
GO; GO:0097324; P:melanocyte migration; ISS:UniProtKB.
GO; GO:0002318; P:myeloid progenitor cell differentiation; IEA:Ensembl.
GO; GO:0043069; P:negative regulation of programmed cell death; IEA:Ensembl.
GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0043473; P:pigmentation; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:1904343; P:positive regulation of colon smooth muscle contraction; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; IMP:UniProtKB.
GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; TAS:UniProtKB.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; TAS:UniProtKB.
GO; GO:0010863; P:positive regulation of phospholipase C activity; TAS:UniProtKB.
GO; GO:0031274; P:positive regulation of pseudopodium assembly; IEA:Ensembl.
GO; GO:0120072; P:positive regulation of pyloric antrum smooth muscle contraction; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:UniProtKB.
GO; GO:1904349; P:positive regulation of small intestine smooth muscle contraction; IEA:Ensembl.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:UniProtKB.
GO; GO:1905065; P:positive regulation of vascular smooth muscle cell differentiation; IDA:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:1904251; P:regulation of bile acid metabolic process; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; TAS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0048070; P:regulation of developmental pigmentation; IEA:Ensembl.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0048103; P:somatic stem cell division; IEA:Ensembl.
GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
GO; GO:0007286; P:spermatid development; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; TAS:UniProtKB.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
GO; GO:0043586; P:tongue development; IEA:Ensembl.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
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; 3.
SMART; SM00408; IGc2; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF56112; SSF56112; 2.
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;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Proto-oncogene; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 976 Mast/stem cell growth factor receptor
Kit.
/FTId=PRO_0000016754.
TOPO_DOM 26 524 Extracellular. {ECO:0000255}.
TRANSMEM 525 545 Helical. {ECO:0000255}.
TOPO_DOM 546 976 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 112 Ig-like C2-type 1.
DOMAIN 121 205 Ig-like C2-type 2.
DOMAIN 212 308 Ig-like C2-type 3.
DOMAIN 317 410 Ig-like C2-type 4.
DOMAIN 413 507 Ig-like C2-type 5.
DOMAIN 589 937 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 596 603 ATP.
NP_BIND 671 677 ATP.
REGION 568 570 Important for interaction with
phosphotyrosine-binding proteins.
ACT_SITE 792 792 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
METAL 568 568 Magnesium.
METAL 797 797 Magnesium.
METAL 810 810 Magnesium.
BINDING 623 623 ATP.
BINDING 796 796 ATP.
SITE 936 936 Important for interaction with
phosphotyrosine-binding proteins.
MOD_RES 547 547 Phosphotyrosine; by autocatalysis.
{ECO:0000305|PubMed:20147452}.
MOD_RES 553 553 Phosphotyrosine; by autocatalysis.
{ECO:0000305|PubMed:20147452}.
MOD_RES 568 568 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12824176,
ECO:0000269|PubMed:19265199,
ECO:0000269|PubMed:21030588,
ECO:0000269|PubMed:9038210}.
MOD_RES 570 570 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12824176,
ECO:0000269|PubMed:9038210}.
MOD_RES 703 703 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10377264,
ECO:0000269|PubMed:19265199,
ECO:0000269|PubMed:20147452}.
MOD_RES 721 721 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:19265199,
ECO:0000269|PubMed:20147452,
ECO:0000269|PubMed:9038210}.
MOD_RES 730 730 Phosphotyrosine; by autocatalysis.
{ECO:0000305|PubMed:20147452}.
MOD_RES 741 741 Phosphoserine; by PKC/PRKCA.
{ECO:0000269|PubMed:7539802}.
MOD_RES 746 746 Phosphoserine; by PKC/PRKCA.
{ECO:0000269|PubMed:7539802}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000269|PubMed:7539802}.
MOD_RES 823 823 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:20147452}.
MOD_RES 891 891 Phosphoserine.
{ECO:0000269|PubMed:12878163}.
MOD_RES 900 900 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12878163,
ECO:0000269|PubMed:20147452}.
MOD_RES 936 936 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10377264,
ECO:0000269|PubMed:19265199}.
MOD_RES 959 959 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:7539802}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:17662946}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17662946}.
CARBOHYD 293 293 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17662946}.
CARBOHYD 300 300 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17662946}.
CARBOHYD 320 320 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17662946}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17662946}.
CARBOHYD 367 367 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17662946}.
CARBOHYD 463 463 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 486 486 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 58 97 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17662946}.
DISULFID 136 186 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17662946}.
DISULFID 151 183 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17662946}.
DISULFID 233 290 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17662946}.
DISULFID 428 491 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17662946}.
VAR_SEQ 412 413 KP -> SL (in isoform 3).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_041866.
VAR_SEQ 414 976 Missing (in isoform 3).
{ECO:0000303|PubMed:18593464}.
/FTId=VSP_041867.
VAR_SEQ 510 513 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:20658618,
ECO:0000303|Ref.6}.
/FTId=VSP_038385.
VARIANT 532 532 V -> I (in dbSNP:rs55792975).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042021.
VARIANT 541 541 M -> L (in dbSNP:rs3822214).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042022.
VARIANT 541 541 M -> V (in dbSNP:rs3822214).
/FTId=VAR_061289.
VARIANT 550 558 Missing (in GIST; somatic mutation).
{ECO:0000269|PubMed:15824741,
ECO:0000269|PubMed:9438854}.
/FTId=VAR_033124.
VARIANT 550 550 K -> I (in GIST; somatic mutation).
{ECO:0000269|PubMed:9438854}.
/FTId=VAR_033123.
VARIANT 551 555 Missing (in GIST; somatic mutation).
{ECO:0000269|PubMed:9438854}.
/FTId=VAR_033125.
VARIANT 559 560 Missing (in GIST; somatic mutation).
{ECO:0000269|PubMed:9438854}.
/FTId=VAR_033128.
VARIANT 559 559 V -> A (in GIST; dbSNP:rs121913517).
{ECO:0000269|PubMed:11505412}.
/FTId=VAR_033126.
VARIANT 559 559 V -> D (in GIST; somatic mutation;
dbSNP:rs121913517).
{ECO:0000269|PubMed:9438854}.
/FTId=VAR_033127.
VARIANT 559 559 Missing (in GIST).
{ECO:0000269|PubMed:9697690}.
/FTId=VAR_007965.
VARIANT 583 583 E -> K (in PBT; dbSNP:rs121913680).
{ECO:0000269|PubMed:1376329}.
/FTId=VAR_004104.
VARIANT 584 584 F -> C (in PBT; dbSNP:rs28933371).
{ECO:0000269|PubMed:11074500}.
/FTId=VAR_033129.
VARIANT 584 584 F -> L (in PBT; dbSNP:rs794726671).
{ECO:0000269|PubMed:1370874}.
/FTId=VAR_004105.
VARIANT 601 601 G -> R (in PBT).
{ECO:0000269|PubMed:11074500}.
/FTId=VAR_033130.
VARIANT 656 656 L -> P (in PBT).
{ECO:0000269|PubMed:11074500}.
/FTId=VAR_033131.
VARIANT 664 664 G -> R (in PBT; dbSNP:rs121913679).
{ECO:0000269|PubMed:1717985}.
/FTId=VAR_004106.
VARIANT 691 691 C -> S (in dbSNP:rs35200131).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042023.
VARIANT 715 715 S -> N (in dbSNP:rs56094246).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042024.
VARIANT 737 737 D -> N (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs751005114).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042025.
VARIANT 791 791 R -> G (in PBT).
{ECO:0000269|PubMed:7687267}.
/FTId=VAR_004107.
VARIANT 796 796 R -> G (in PBT; with sensorineural
deafness; dbSNP:rs121913684).
{ECO:0000269|PubMed:9450866}.
/FTId=VAR_033132.
VARIANT 804 804 R -> W (in a colorectal adenocarcinoma
sample; somatic mutation;
dbSNP:rs145602440).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042026.
VARIANT 812 812 G -> V (in PBT).
{ECO:0000269|PubMed:7687267}.
/FTId=VAR_004108.
VARIANT 816 816 D -> F (in mastocytosis; requires 2
nucleotide substitutions; somatic
mutation; constitutively activated and is
much more rapidly autophosphorylated than
wild type). {ECO:0000269|PubMed:9990072}.
/FTId=VAR_033133.
VARIANT 816 816 D -> H (in a testicular tumor; seminoma;
somatic mutation; constitutively
activated; dbSNP:rs28933969).
{ECO:0000269|PubMed:10362788,
ECO:0000269|PubMed:19164557,
ECO:0000269|PubMed:20147452}.
/FTId=VAR_033134.
VARIANT 816 816 D -> V (in mast cell leukemia and
mastocytosis; somatic mutation;
constitutively activated; loss of
interaction with MPDZ;
dbSNP:rs121913507).
{ECO:0000269|PubMed:11018522,
ECO:0000269|PubMed:17595334,
ECO:0000269|PubMed:19164557,
ECO:0000269|PubMed:19265199,
ECO:0000269|PubMed:21640708,
ECO:0000269|PubMed:7691885,
ECO:0000269|PubMed:9990072}.
/FTId=VAR_004109.
VARIANT 816 816 D -> Y (in acute myeloid leukemia,
mastocytosis and a germ cell tumor of the
testis; somatic mutation; constitutively
activated; dbSNP:rs121913506).
{ECO:0000269|PubMed:16175573,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9657776,
ECO:0000269|PubMed:9990072}.
/FTId=VAR_023828.
VARIANT 820 820 D -> G (in mast cell disease; systemic;
dbSNP:rs121913682).
{ECO:0000269|PubMed:9029028}.
/FTId=VAR_033135.
VARIANT 822 822 N -> K (in a germ cell tumor of the
testis; somatic mutation;
dbSNP:rs121913514).
{ECO:0000269|PubMed:16175573,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_023829.
VARIANT 829 829 A -> P (in a germ cell tumor of the
testis; somatic mutation).
{ECO:0000269|PubMed:16175573,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_023830.
VARIANT 839 839 E -> K (in mastocytosis; somatic
mutation; dominant negative mutation;
loss of autophosphorylation;
dbSNP:rs121913509).
{ECO:0000269|PubMed:9990072}.
/FTId=VAR_033136.
VARIANT 847 847 T -> P (in PBT; dbSNP:rs121913687).
{ECO:0000269|PubMed:9699740}.
/FTId=VAR_033137.
VARIANT 893 896 Missing (in PBT; severe).
{ECO:0000269|PubMed:8680409}.
/FTId=VAR_004110.
MUTAGEN 381 381 R->A: Reduces autophosphorylation in
response to KITLG/SCF.
{ECO:0000269|PubMed:17662946}.
MUTAGEN 386 386 E->A: Reduces autophosphorylation in
response to KITLG/SCF.
{ECO:0000269|PubMed:17662946}.
MUTAGEN 571 571 I->A: Reduction in SH2B2/APS binding.
Abolishes SH2B2/APS binding; when
associated with A-939.
{ECO:0000269|PubMed:12444928}.
MUTAGEN 623 623 K->M: Stronger interaction with MPDZ.
{ECO:0000269|PubMed:11018522}.
MUTAGEN 741 741 S->A: Abolishes down-regulation of kinase
activity by PKC/PRKCA-mediated
phosphorylation; when associated with A-
746. {ECO:0000269|PubMed:7539802}.
MUTAGEN 746 746 S->A: Abolishes down-regulation of kinase
activity by PKC/PRKCA-mediated
phosphorylation; when associated with A-
741. {ECO:0000269|PubMed:7539802}.
MUTAGEN 823 823 Y->F: No decrease in activity. Leads to
autophosphorylation at Tyr-900.
{ECO:0000269|PubMed:20147452}.
MUTAGEN 939 939 L->A: Reduction in SH2B2/APS binding.
Abolishes SH2B2/APS binding; when
associated with A-571.
{ECO:0000269|PubMed:12444928}.
CONFLICT 764 764 L -> I (in Ref. 9; AAH71593).
{ECO:0000305}.
CONFLICT 838 838 P -> H (in Ref. 9; AAH71593).
{ECO:0000305}.
STRAND 38 41 {ECO:0000244|PDB:2EC8}.
STRAND 44 47 {ECO:0000244|PDB:2EC8}.
STRAND 54 59 {ECO:0000244|PDB:2EC8}.
STRAND 63 72 {ECO:0000244|PDB:2EC8}.
STRAND 75 77 {ECO:0000244|PDB:2EC8}.
STRAND 79 86 {ECO:0000244|PDB:2EC8}.
HELIX 89 91 {ECO:0000244|PDB:2E9W}.
STRAND 93 99 {ECO:0000244|PDB:2EC8}.
STRAND 104 110 {ECO:0000244|PDB:2EC8}.
STRAND 125 130 {ECO:0000244|PDB:2E9W}.
STRAND 132 134 {ECO:0000244|PDB:2EC8}.
STRAND 146 149 {ECO:0000244|PDB:2EC8}.
STRAND 151 153 {ECO:0000244|PDB:2EC8}.
STRAND 161 165 {ECO:0000244|PDB:2EC8}.
TURN 166 168 {ECO:0000244|PDB:2EC8}.
STRAND 169 174 {ECO:0000244|PDB:2EC8}.
HELIX 177 179 {ECO:0000244|PDB:2EC8}.
STRAND 183 188 {ECO:0000244|PDB:2EC8}.
STRAND 193 200 {ECO:0000244|PDB:2E9W}.
STRAND 203 205 {ECO:0000244|PDB:2E9W}.
STRAND 213 215 {ECO:0000244|PDB:2EC8}.
STRAND 219 224 {ECO:0000244|PDB:2EC8}.
STRAND 229 239 {ECO:0000244|PDB:2EC8}.
STRAND 243 248 {ECO:0000244|PDB:2EC8}.
STRAND 258 263 {ECO:0000244|PDB:2EC8}.
STRAND 265 267 {ECO:0000244|PDB:2EC8}.
STRAND 269 279 {ECO:0000244|PDB:2EC8}.
TURN 282 284 {ECO:0000244|PDB:2EC8}.
STRAND 286 293 {ECO:0000244|PDB:2EC8}.
STRAND 298 310 {ECO:0000244|PDB:2EC8}.
STRAND 312 319 {ECO:0000244|PDB:4K94}.
STRAND 321 325 {ECO:0000244|PDB:4K94}.
STRAND 331 341 {ECO:0000244|PDB:4K94}.
STRAND 344 350 {ECO:0000244|PDB:4K94}.
STRAND 356 364 {ECO:0000244|PDB:4K94}.
STRAND 367 369 {ECO:0000244|PDB:2EC8}.
STRAND 372 379 {ECO:0000244|PDB:4K94}.
HELIX 384 386 {ECO:0000244|PDB:4K94}.
STRAND 388 395 {ECO:0000244|PDB:4K94}.
STRAND 400 409 {ECO:0000244|PDB:4K94}.
STRAND 411 420 {ECO:0000244|PDB:4K94}.
HELIX 422 424 {ECO:0000244|PDB:4K94}.
STRAND 425 434 {ECO:0000244|PDB:4K94}.
STRAND 437 444 {ECO:0000244|PDB:4K94}.
STRAND 445 449 {ECO:0000244|PDB:4PGZ}.
STRAND 452 454 {ECO:0000244|PDB:4PGZ}.
STRAND 458 462 {ECO:0000244|PDB:4K94}.
STRAND 465 468 {ECO:0000244|PDB:4PGZ}.
STRAND 472 479 {ECO:0000244|PDB:4K94}.
HELIX 481 483 {ECO:0000244|PDB:4PGZ}.
STRAND 485 494 {ECO:0000244|PDB:4K94}.
STRAND 499 506 {ECO:0000244|PDB:4K94}.
STRAND 558 564 {ECO:0000244|PDB:3G0E}.
STRAND 567 570 {ECO:0000244|PDB:3G0E}.
TURN 573 575 {ECO:0000244|PDB:1T46}.
HELIX 580 582 {ECO:0000244|PDB:1T46}.
HELIX 586 588 {ECO:0000244|PDB:1T46}.
STRAND 589 597 {ECO:0000244|PDB:1T46}.
STRAND 599 613 {ECO:0000244|PDB:1T46}.
STRAND 617 625 {ECO:0000244|PDB:1T46}.
HELIX 631 647 {ECO:0000244|PDB:1T46}.
STRAND 656 660 {ECO:0000244|PDB:1T46}.
STRAND 662 665 {ECO:0000244|PDB:1T46}.
STRAND 667 671 {ECO:0000244|PDB:1T46}.
HELIX 678 684 {ECO:0000244|PDB:1T46}.
TURN 685 688 {ECO:0000244|PDB:1T46}.
STRAND 719 721 {ECO:0000244|PDB:2IUH}.
HELIX 754 756 {ECO:0000244|PDB:4HVS}.
STRAND 757 759 {ECO:0000244|PDB:4HVS}.
HELIX 760 762 {ECO:0000244|PDB:4HVS}.
HELIX 766 785 {ECO:0000244|PDB:1T46}.
STRAND 788 790 {ECO:0000244|PDB:3G0F}.
HELIX 795 797 {ECO:0000244|PDB:1T46}.
STRAND 798 801 {ECO:0000244|PDB:1T46}.
TURN 802 804 {ECO:0000244|PDB:1T46}.
STRAND 805 808 {ECO:0000244|PDB:1T46}.
HELIX 812 814 {ECO:0000244|PDB:1T46}.
HELIX 817 819 {ECO:0000244|PDB:3G0E}.
STRAND 823 825 {ECO:0000244|PDB:1T46}.
STRAND 827 831 {ECO:0000244|PDB:1T46}.
HELIX 833 835 {ECO:0000244|PDB:1T46}.
HELIX 838 843 {ECO:0000244|PDB:1T46}.
HELIX 848 863 {ECO:0000244|PDB:1T46}.
TURN 864 866 {ECO:0000244|PDB:1T46}.
HELIX 877 885 {ECO:0000244|PDB:1T46}.
HELIX 897 906 {ECO:0000244|PDB:1T46}.
HELIX 911 913 {ECO:0000244|PDB:1T46}.
HELIX 917 930 {ECO:0000244|PDB:1T46}.
TURN 931 933 {ECO:0000244|PDB:1T45}.
SEQUENCE 976 AA; 109865 MW; 81B0CD76817F3454 CRC64;
MRGARGAWDF LCVLLLLLRV QTGSSQPSVS PGEPSPPSIH PGKSDLIVRV GDEIRLLCTD
PGFVKWTFEI LDETNENKQN EWITEKAEAT NTGKYTCTNK HGLSNSIYVF VRDPAKLFLV
DRSLYGKEDN DTLVRCPLTD PEVTNYSLKG CQGKPLPKDL RFIPDPKAGI MIKSVKRAYH
RLCLHCSVDQ EGKSVLSEKF ILKVRPAFKA VPVVSVSKAS YLLREGEEFT VTCTIKDVSS
SVYSTWKREN SQTKLQEKYN SWHHGDFNYE RQATLTISSA RVNDSGVFMC YANNTFGSAN
VTTTLEVVDK GFINIFPMIN TTVFVNDGEN VDLIVEYEAF PKPEHQQWIY MNRTFTDKWE
DYPKSENESN IRYVSELHLT RLKGTEGGTY TFLVSNSDVN AAIAFNVYVN TKPEILTYDR
LVNGMLQCVA AGFPEPTIDW YFCPGTEQRC SASVLPVDVQ TLNSSGPPFG KLVVQSSIDS
SAFKHNGTVE CKAYNDVGKT SAYFNFAFKG NNKEQIHPHT LFTPLLIGFV IVAGMMCIIV
MILTYKYLQK PMYEVQWKVV EEINGNNYVY IDPTQLPYDH KWEFPRNRLS FGKTLGAGAF
GKVVEATAYG LIKSDAAMTV AVKMLKPSAH LTEREALMSE LKVLSYLGNH MNIVNLLGAC
TIGGPTLVIT EYCCYGDLLN FLRRKRDSFI CSKQEDHAEA ALYKNLLHSK ESSCSDSTNE
YMDMKPGVSY VVPTKADKRR SVRIGSYIER DVTPAIMEDD ELALDLEDLL SFSYQVAKGM
AFLASKNCIH RDLAARNILL THGRITKICD FGLARDIKND SNYVVKGNAR LPVKWMAPES
IFNCVYTFES DVWSYGIFLW ELFSLGSSPY PGMPVDSKFY KMIKEGFRML SPEHAPAEMY
DIMKTCWDAD PLKRPTFKQI VQLIEKQISE STNHIYSNLA NCSPNRQKPV VDHSVRINSV
GSTASSSQPL LVHDDV


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