Reviewed, UniProtKB/Swiss-Prot P10721 (KIT_HUMAN)

Names and origin

Protein names

Recommended name:
    Mast/stem cell growth factor receptor
      Short name=SCFR
    EC=2.7.10.1
Alternative name(s):
    Proto-oncogene tyrosine-protein kinase Kit
      Short name=c-kit
    CD_antigen=CD117

Gene names

Name:

KIT

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	976 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is the receptor for stem cell factor (mast cell growth factor). It has a tyrosine-protein kinase activity. Binding of the ligands leads to the autophosphorylation of KIT and its association with substrates such as phosphatidylinositol 3-kinase (Pi3K).
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Subunit structure	Interacts with APS. Interacts with MPDZ (via the tenth PDZ domain). Interacts with PTPRU. Ref.5 Ref.6 Ref.7
Subcellular location	Membrane; Single-pass type I membrane protein.
Involvement in disease	Defects in KIT are a cause of piebaldism [MIM:172800]. Piebaldism is an autosomal dominant genetic developmental abnormality of pigmentation characterized by congenital patches of white skin and hair that lack melanocytes. Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.24 Defects in KIT are a cause of gastrointestinal stromal tumor (GIST) [MIM:606764]. Ref.16 Ref.20 Ref.21 Ref.25 Ref.26 Defects in KIT have been associated with testicular tumors [MIM:273300]. It includes germ cell tumor (GCT) or testicular germ cell tumor (TGCT). Ref.16 Ref.22
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily. Contains 5 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation Proto-oncogene
Domain	Immunoglobulin domain Repeat Signal Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	transmembrane receptor protein tyrosine kinase signaling pathway Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from direct assay. Source: HPA extracellular space Inferred from direct assay. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct receptor signaling protein tyrosine kinase activity Ref.21 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KITLG	P21583	1	EBI-1379503,EBI-1379527
PTPRJ	Q12913	1	EBI-1379503,EBI-2264500

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential

Chain

26 – 976

951

Mast/stem cell growth factor receptor

PRO_0000016754

Regions

Topological domain

26 – 524

499

Extracellular Potential

Transmembrane

525 – 545

21

Potential

Topological domain

546 – 976

431

Cytoplasmic Potential

Domain

27 – 112

86

Ig-like C2-type 1

Domain

121 – 205

85

Ig-like C2-type 2

Domain

212 – 308

97

Ig-like C2-type 3

Domain

317 – 410

94

Ig-like C2-type 4

Domain

413 – 507

95

Ig-like C2-type 5

Domain

589 – 937

349

Protein kinase

Nucleotide binding

595 – 603

9

ATP By similarity

Sites

Active site

792

1

Proton acceptor By similarity

Binding site

623

1

ATP By similarity

Site

568

1

Interaction with APS

Site

936

1

Interaction with APS

Amino acid modifications

Modified residue

568

1

Phosphotyrosine By similarity

Modified residue

570

1

Phosphotyrosine By similarity

Modified residue

703

1

Phosphotyrosine By similarity

Modified residue

823

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

936

1

Phosphotyrosine Ref.9

Glycosylation

130

1

N-linked (GlcNAc...) Ref.8

Glycosylation

145

1

N-linked (GlcNAc...) Potential

Glycosylation

283

1

N-linked (GlcNAc...) Potential

Glycosylation

293

1

N-linked (GlcNAc...) Potential

Glycosylation

300

1

N-linked (GlcNAc...) Potential

Glycosylation

320

1

N-linked (GlcNAc...) Potential

Glycosylation

352

1

N-linked (GlcNAc...) Potential

Glycosylation

367

1

N-linked (GlcNAc...) Potential

Glycosylation

463

1

N-linked (GlcNAc...) Potential

Glycosylation

486

1

N-linked (GlcNAc...) Potential

Disulfide bond

58 ↔ 97

By similarity

Disulfide bond

151 ↔ 183

By similarity

Disulfide bond

233 ↔ 290

By similarity

Disulfide bond

428 ↔ 491

By similarity

Natural variations

Natural variant

532

1

V → I Ref.28

VAR_042021

Natural variant

541

1

M → L Ref.28

VAR_042022

Natural variant

550 – 558

9

Missing in GIST; somatic mutation. Ref.21 Ref.26

VAR_033124

Natural variant

550

1

K → I in GIST; somatic mutation. Ref.21

VAR_033123

Natural variant

551 – 555

5

Missing in GIST; somatic mutation. Ref.21

VAR_033125

Natural variant

559 – 560

2

Missing in GIST; somatic mutation. Ref.20 Ref.21 Ref.25

VAR_033128

Natural variant

559

1

V → A in GIST. Ref.20 Ref.21 Ref.25

VAR_033126

Natural variant

559

1

V → D in GIST; somatic mutation. Ref.20 Ref.21 Ref.25

VAR_033127

Natural variant

559

1

Missing in GIST. Ref.20 Ref.21 Ref.25

VAR_007965

Natural variant

583

1

E → K in piebaldism. Ref.10

VAR_004104

Natural variant

584

1

F → C in piebaldism. Ref.11 Ref.24

VAR_033129

Natural variant

584

1

F → L in piebaldism. Ref.11 Ref.24

VAR_004105

Natural variant

601

1

G → R in piebaldism. Ref.24

VAR_033130

Natural variant

656

1

L → P in piebaldism. Ref.24

VAR_033131

Natural variant

664

1

G → R in piebaldism. Ref.12

VAR_004106

Natural variant

691

1

C → S Ref.28

VAR_042023

Natural variant

715

1

S → N Ref.28

VAR_042024

Natural variant

737

1

D → N in a colorectal adenocarcinoma sample; somatic mutation. Ref.28

VAR_042025

Natural variant

791

1

R → G in piebaldism. Ref.14

VAR_004107

Natural variant

796

1

R → G in piebaldism; with sensorineural deafness. Ref.17

VAR_033132

Natural variant

804

1

R → W in a colorectal adenocarcinoma sample; somatic mutation. Ref.28

VAR_042026

Natural variant

812

1

G → V in piebaldism. Ref.14

VAR_004108

Natural variant

816

1

D → F in mastocytosis; requires 2 nucleotide substitutions; somatic mutation; constitutively activated. Ref.6 Ref.22 Ref.28 Ref.13 Ref.18 Ref.23 Ref.27

VAR_033133

Natural variant

816

1

D → H in GCT; somatic mutation; constitutively activated. Ref.22

VAR_033134

Natural variant

816

1

D → V in mast cell leukemia and mastocytosis; somatic mutation; constitutively activated; loss of interaction with MPDZ. Ref.6 Ref.22 Ref.28 Ref.13 Ref.18 Ref.23 Ref.27

VAR_004109

Natural variant

816

1

D → Y in acute myeloid leukemia, mastocytosis and TGCT; somatic mutation; constitutively activated. Ref.6 Ref.22 Ref.28 Ref.13 Ref.18 Ref.23 Ref.27

VAR_023828

Natural variant

820

1

D → G in mast cell disease; systemic. Ref.16

VAR_033135

Natural variant

822

1

N → K in TGCT; somatic mutation. Ref.27

VAR_023829

Natural variant

829

1

A → P in TGCT; somatic mutation. Ref.27

VAR_023830

Natural variant

839

1

E → K in mastocytosis; somatic mutation; dominant negative mutation; loss of autophosphorylation. Ref.23

VAR_033136

Natural variant

847

1

T → P in piebaldism. Ref.19

VAR_033137

Natural variant

893 – 896

4

Missing in piebaldism; severe. Ref.15

VAR_004110

Experimental info

Mutagenesis

571

1

I → A: Reduction in APS binding. Abolishes APS binding; when associated with A-939. Ref.7

Mutagenesis

623

1

K → M: Stronger interaction with MPDZ. Ref.6

Mutagenesis

939

1

L → A: Reduction in APS binding. Abolishes APS binding; when associated with A-571. Ref.7

Secondary structure

1

.

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976

Helix Strand Turn

Details...

Beta strand

556 – 560

5

Helix

580 – 582

3

Helix

586 – 588

3

Beta strand

589 – 597

9

Beta strand

599 – 613

15

Beta strand

617 – 625

9

Helix

631 – 647

17

Beta strand

656 – 660

5

Beta strand

662 – 665

4

Beta strand

667 – 671

5

Helix

678 – 690

13

Helix

766 – 785

20

Helix

795 – 797

3

Beta strand

798 – 801

4

Helix

802 – 804

3

Beta strand

805 – 808

4

Helix

812 – 814

3

Helix

817 – 819

3

Beta strand

823 – 831

9

Helix

833 – 835

3

Helix

838 – 843

6

Helix

848 – 863

16

Helix

877 – 885

9

Helix

897 – 906

10

Helix

911 – 913

3

Helix

917 – 930

14

Turn

931 – 933

3

Sequences

	Sequence		Length	Mass (Da)
	P10721-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 81B0CD76817F3454	FASTA	976	109,865
	10 20 30 40 50 60 MRGARGAWDF LCVLLLLLRV QTGSSQPSVS PGEPSPPSIH PGKSDLIVRV GDEIRLLCTD 70 80 90 100 110 120 PGFVKWTFEI LDETNENKQN EWITEKAEAT NTGKYTCTNK HGLSNSIYVF VRDPAKLFLV 130 140 150 160 170 180 DRSLYGKEDN DTLVRCPLTD PEVTNYSLKG CQGKPLPKDL RFIPDPKAGI MIKSVKRAYH 190 200 210 220 230 240 RLCLHCSVDQ EGKSVLSEKF ILKVRPAFKA VPVVSVSKAS YLLREGEEFT VTCTIKDVSS 250 260 270 280 290 300 SVYSTWKREN SQTKLQEKYN SWHHGDFNYE RQATLTISSA RVNDSGVFMC YANNTFGSAN 310 320 330 340 350 360 VTTTLEVVDK GFINIFPMIN TTVFVNDGEN VDLIVEYEAF PKPEHQQWIY MNRTFTDKWE 370 380 390 400 410 420 DYPKSENESN IRYVSELHLT RLKGTEGGTY TFLVSNSDVN AAIAFNVYVN TKPEILTYDR 430 440 450 460 470 480 LVNGMLQCVA AGFPEPTIDW YFCPGTEQRC SASVLPVDVQ TLNSSGPPFG KLVVQSSIDS 490 500 510 520 530 540 SAFKHNGTVE CKAYNDVGKT SAYFNFAFKG NNKEQIHPHT LFTPLLIGFV IVAGMMCIIV 550 560 570 580 590 600 MILTYKYLQK PMYEVQWKVV EEINGNNYVY IDPTQLPYDH KWEFPRNRLS FGKTLGAGAF 610 620 630 640 650 660 GKVVEATAYG LIKSDAAMTV AVKMLKPSAH LTEREALMSE LKVLSYLGNH MNIVNLLGAC 670 680 690 700 710 720 TIGGPTLVIT EYCCYGDLLN FLRRKRDSFI CSKQEDHAEA ALYKNLLHSK ESSCSDSTNE 730 740 750 760 770 780 YMDMKPGVSY VVPTKADKRR SVRIGSYIER DVTPAIMEDD ELALDLEDLL SFSYQVAKGM 790 800 810 820 830 840 AFLASKNCIH RDLAARNILL THGRITKICD FGLARDIKND SNYVVKGNAR LPVKWMAPES 850 860 870 880 890 900 IFNCVYTFES DVWSYGIFLW ELFSLGSSPY PGMPVDSKFY KMIKEGFRML SPEHAPAEMY 910 920 930 940 950 960 DIMKTCWDAD PLKRPTFKQI VQLIEKQISE STNHIYSNLA NCSPNRQKPV VDHSVRINSV 970 GSTASSSQPL LVHDDV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human proto-oncogene c-kit: a new cell surface receptor tyrosine kinase for an unidentified ligand." Yarden Y., Kuang W.-J., Yang-Feng T., Coussens L., Munemitsu S., Dull T.J., Chen E., Schlessinger J., Francke U., Ullrich A. EMBO J. 6:3341-3351(1987) [PubMed: 2448137] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fetal brain and Term placenta.
[2]	"Organization and nucleotide sequence of the human KIT (mast/stem cell growth factor receptor) proto-oncogene." Giebel L.B., Strunk K.M., Holmes S.A., Spritz R.A. Oncogene 7:2207-2217(1992) [PubMed: 1279499] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence analysis of two genomic regions containing the KIT and the FMS receptor tyrosine kinase genes." Andre C., Hampe A., Lachaume P., Martin E., Wang X.P., Manus V., Hu W.X., Galibert F. Genomics 39:216-226(1997) [PubMed: 9027509] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Characterization of the promoter region of the human c-kit proto-oncogene." Yamamoto K., Tojo A., Aoki N., Shibuya M. Jpn. J. Cancer Res. 84:1136-1144(1993) [PubMed: 7506248] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[5]	"The receptor protein tyrosine phosphatase, PTP-RO, is upregulated during megakaryocyte differentiation and is associated with the c-Kit receptor." Taniguchi Y., London R., Schinkmann K., Jiang S., Avraham H. Blood 94:539-549(1999) [PubMed: 10397721] [Abstract] Cited for: INTERACTION WITH PTPRU.
[6]	"The direct association of the multiple PDZ domain containing proteins (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase activity." Mancini A., Koch A., Stefan M., Niemann H., Tamura T. FEBS Lett. 482:54-58(2000) [PubMed: 11018522] [Abstract] Cited for: INTERACTION WITH MPDZ, CHARACTERIZATION OF VARIANT VAL-816, MUTAGENESIS OF LYS-623.
[7]	"The adapter protein APS associates with the multifunctional docking sites Tyr-568 and Tyr-936 in c-Kit." Wollberg P., Lennartsson J., Gottfridsson E., Yoshimura A., Ronnstrand L. Biochem. J. 370:1033-1038(2003) [PubMed: 12444928] [Abstract] Cited for: INTERACTION WITH APS, MUTAGENESIS OF ILE-571 AND LEU-939.
[8]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130, MASS SPECTROMETRY. Tissue: Plasma.
[9]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-936, MASS SPECTROMETRY.
[10]	"Human piebald trait resulting from a dominant negative mutant allele of the c-kit membrane receptor gene." Fleischman R.A. J. Clin. Invest. 89:1713-1717(1992) [PubMed: 1376329] [Abstract] Cited for: VARIANT PIEBALDISM LYS-583.
[11]	"Dominant negative and loss of function mutations of the c-kit (mast/stem cell growth factor receptor) proto-oncogene in human piebaldism." Spritz R.A., Giebel L.B., Holmes S.A. Am. J. Hum. Genet. 50:261-269(1992) [PubMed: 1370874] [Abstract] Cited for: VARIANT PIEBALDISM LEU-584.
[12]	"Mutation of the KIT (mast/stem cell growth factor receptor) protooncogene in human piebaldism." Giebel L.B., Spritz R.A. Proc. Natl. Acad. Sci. U.S.A. 88:8696-8699(1991) [PubMed: 1717985] [Abstract] Cited for: VARIANT PIEBALDISM ARG-664.
[13]	"Identification of mutations in the coding sequence of the proto-oncogene c-kit in a human mast cell leukemia cell line causing ligand-independent activation of c-kit product." Furitsu T., Tsujimura T., Tono T., Ikeda H., Kitayama H., Koshimizu U., Sugahara H., Butterfield J.H., Ashman L.K., Kanayama Y., Matsuzawa Y., Kitamura Y., Kanakura Y. J. Clin. Invest. 92:1736-1744(1993) [PubMed: 7691885] [Abstract] Cited for: VARIANT MAST CELL LEUKEMIA VAL-816.
[14]	"Novel mutations of the KIT (mast/stem cell growth factor receptor) proto-oncogene in human piebaldism." Spritz R.A., Holmes S.A., Itin P., Kuester W. J. Invest. Dermatol. 101:22-25(1993) [PubMed: 7687267] [Abstract] Cited for: VARIANTS PIEBALDISM GLY-791 AND VAL-812.
[15]	"A 12-bp deletion (7818del12) in the c-kit protooncogene in a large Italian kindred with piebaldism." Riva P., Milani N., Gandolfi P., Larizza L. Hum. Mutat. 6:343-345(1995) [PubMed: 8680409] [Abstract] Cited for: VARIANT PIEBALDISM 893-GLU--PRO-896 DEL.
[16]	"A new c-kit mutation in a case of aggressive mast cell disease." Pignon J.-M., Giraudier S., Duquesnoy P., Jouault H., Imbert M., Vainchenker W., Vernant J.-P., Tulliez M. Br. J. Haematol. 96:374-376(1997) [PubMed: 9029028] [Abstract] Cited for: VARIANT MAST CELL DISEASE GLY-820.
[17]	"Piebaldism with deafness: molecular evidence for an expanded syndrome." Spritz R.A., Beighton P. Am. J. Med. Genet. 75:101-103(1998) [PubMed: 9450866] [Abstract] Cited for: VARIANT PIEBALDISM GLY-796.
[18]	"c-kit activating mutations and mast cell proliferation in human leukemia." Beghini A., Larizza L., Cairoli R., Morra E. Blood 92:701-702(1998) [PubMed: 9657776] [Abstract] Cited for: VARIANT ACUTE MYELOID LEUKEMIA TYR-816.
[19]	"A novel KIT gene missense mutation in a Japanese family with piebaldism." Nomura K., Hatayama I., Narita T., Kaneko T., Shiraishi M. J. Invest. Dermatol. 111:337-338(1998) [PubMed: 9699740] [Abstract] Cited for: VARIANT PIEBALDISM PRO-847.
[20]	"Familial gastrointestinal stromal tumours with germline mutation of the KIT gene." Nishida T., Hirota S., Taniguchi M., Hashimoto K., Isozaki K., Nakamura H., Kanakura Y., Tanaka T., Takabayashi A., Matsuda H., Kitamura Y. Nat. Genet. 19:323-324(1998) [PubMed: 9697690] [Abstract] Cited for: VARIANT GIST VAL-559 DEL.
[21]	"Gain-of-function mutations of c-kit in human gastrointestinal stromal tumors." 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. Science 279:577-580(1998) [PubMed: 9438854] [Abstract] Cited for: VARIANTS GIST ILE-550; 550-LYS--LYS-558 DEL; 551-PRO--VAL-555 DEL; ASP-559 AND 559-VAL-VAL-560 DEL.
[22]	"Activating c-kit gene mutations in human germ cell tumors." Tian Q., Frierson H.F. Jr., Krystal G.W., Moskaluk C.A. Am. J. Pathol. 154:1643-1647(1999) [PubMed: 10362788] [Abstract] Cited for: VARIANT GCT HIS-816, CHARACTERIZATION OF VARIANT GCT HIS-816.
[23]	"Activating and dominant inactivating c-KIT catalytic domain mutations in distinct clinical forms of human mastocytosis." Longley B.J. Jr., Metcalfe D.D., Tharp M., Wang X., Tyrrell L., Lu S.-Z., Heitjan D., Ma Y. Proc. Natl. Acad. Sci. U.S.A. 96:1609-1614(1999) [PubMed: 9990072] [Abstract] Cited for: VARIANTS MASTOCYTOSIS VAL-816; PHE-816; TYR-816 AND LYS-839, CHARACTERIZATION OF VARIANTS MASTOCYTOSIS VAL-816; PHE-816; TYR-816 AND LYS-839.
[24]	"Three novel mutations of the proto-oncogene KIT cause human piebaldism." Syrris P., Malik N.M., Murday V.A., Patton M.A., Carter N.D., Hughes H.E., Metcalfe K. Am. J. Med. Genet. 95:79-81(2000) [PubMed: 11074500] [Abstract] Cited for: VARIANTS PIEBALDISM CYS-584; ARG-601 AND PRO-656.
[25]	"Germline mutation in the juxtamembrane domain of the kit gene in a family with gastrointestinal stromal tumors and urticaria pigmentosa." Beghini A., Tibiletti M.G., Roversi G., Chiaravalli A.M., Serio G., Capella C., Larizza L. Cancer 92:657-662(2001) [PubMed: 11505412] [Abstract] Cited for: VARIANT GIST ALA-559.
[26]	"A mutation-created novel intra-exonic pre-mRNA splice site causes constitutive activation of KIT in human gastrointestinal stromal tumors." Chen L.L., Sabripour M., Wu E.F., Prieto V.G., Fuller G.N., Frazier M.L. Oncogene 24:4271-4280(2005) [PubMed: 15824741] [Abstract] Cited for: VARIANT GIST 550-LYS--LYS-558 DEL.
[27]	"Sequence analysis of the protein kinase gene family in human testicular germ-cell tumors of adolescents and adults." Bignell G., Smith R., Hunter C., Stephens P., Davies H., Greenman C., Teague J., Butler A., Edkins S., Stevens C., O'meara S., Parker A., Avis T., Barthorpe S., Brackenbury L., Buck G., Clements J., Cole J. , Dicks E., Edwards K., Forbes S., Gorton M., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jones D., Kosmidou V., Laman R., Lugg R., Menzies A., Perry J., Petty R., Raine K., Shepherd R., Small A., Solomon H., Stephens Y., Tofts C., Varian J., Webb A., West S., Widaa S., Yates A., Gillis A.J.M., Stoop H.J., van Gurp R.J.H.L.M., Oosterhuis J.W., Looijenga L.H.J., Futreal P.A., Wooster R., Stratton M.R. Genes Chromosomes Cancer 45:42-46(2006) [PubMed: 16175573] [Abstract] Cited for: VARIANTS TGCT TYR-816; LYS-822 AND PRO-829.
[28]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-532; LEU-541; SER-691; ASN-715; ASN-737; TRP-804; TYR-816; LYS-822 AND PRO-829.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Wikipedia

CD117 entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

X06182 mRNA. Translation: CAA29548.1.
X69301 , X69302, X69303, X69304, X69305, X69306, X69307, X69308, X69309, X69310, X69311, X69312, X69313, X69314, X69315, X69316 Genomic DNA. Translation: CAA49159.1.
U63834 Genomic DNA. Translation: AAC50968.1.
S67773 Genomic DNA. Translation: AAB29529.1.

IPI

IPI00022296.

PIR

TVHUKT. S01426.

RefSeq

NP_000213.1.
NP_001087241.1.

UniGene

Hs.479754

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PKG	X-ray	2.90	A/B	549-931	[»]
1QZJ	model	-	A	576-932	[»]
1QZK	model	-	A	576-932	[»]
1R01	model	-	A	576-932	[»]
1T45	X-ray	1.90	A	547-935	[»]
1T46	X-ray	1.60	A	565-935	[»]
2E9W	X-ray	3.50	A/B	26-514	[»]
2EC8	X-ray	3.00	A	1-519	[»]
2VIF	X-ray	1.45	P	564-574	[»]
3G0E	X-ray	1.60	A	544-935	[»]
3G0F	X-ray	2.60	A/B	544-935	[»]

ModBase

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Protein-protein interaction databases

DIP

DIP:1055N.

IntAct

P10721. 6 interactions.

PTM databases

PhosphoSite

P10721.

Proteomic databases

PRIDE

P10721.

Genome annotation databases

Ensembl

ENSG00000157404. Homo sapiens. [Contig view]

GeneID

3815.

KEGG

hsa:3815.

Organism-specific databases

GeneCards

GC04P055218.
GC04P055219.
GC04P055220.

H-InvDB

HIX0031398.

HGNC

HGNC:6342. KIT.

HPA

CAB003288.
HPA004471.

MIM

164920. gene.
172800. phenotype.
273300. phenotype.
606764. phenotype.

Orphanet

44890. Gastrointestinal stromal tumor.
98851. Mast cell leukemia.
98292. Mastocytosis.
98850. Mastocytosis, aggressive systemic.
98848. Mastocytosis, indolent systemic.
2467. Mastocytosis, systemic.
98849. Mastocytosis, systemic, with an associated clonal hematologic non-mast cell c lineage disease.
2884. Piebaldism.

PharmGKB

PA30128.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P10721.

HOVERGEN

P10721.

OMA

P10721. THGRITK.

Enzyme and pathway databases

BRENDA

2.7.10.1. 247.

Pathway_Interaction_DB

kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).

Gene expression databases

ArrayExpress

P10721.

Bgee

P10721.

CleanEx

HS_KIT.

GermOnline

ENSG00000157404. Homo sapiens.

Family and domain databases

InterPro

IPR013151. Ig.
IPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR001824. Recept_tyr_kinase-III_CS.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
IPR016243. TyrPK_CSF1-R.
[Graphical view]

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 1 hit.

Pfam

PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PIRSF

PIRSF000615. TyrPK_CSF1-R. 1 hit.

ProDom

PD000001. Prot_kinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

PROSITE

PS50835. IG_LIKE. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS00240. RECEPTOR_TYR_KIN_III. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

DrugBank

DB01254. Dasatinib.
DB00619. Imatinib.
DB00398. Sorafenib.
DB01268. Sunitinib.

NextBio

14995.

SOURCE

Search...

Entry information

Entry name

KIT_HUMAN

Accession

Primary (citable) accession number: P10721
Secondary accession number(s): Q9UM99

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	June 16, 2009
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)