P05532 (KIT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mast/stem cell growth factor receptor Kit
Short name=SCFR
EC=2.7.10.1

Alternative name(s):
Proto-oncogene c-Kit
Tyrosine-protein kinase Kit
CD_antigen=CD117

Gene names

Name:	Kit
Synonyms:	Sl

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	979 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	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. Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.17 Ref.19
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.11
Enzyme regulation	Present in an inactive conformation in the absence of bound ligand. KITLG/SCF binding leads to dimerization and activation by autophosphorylation.
Subunit structure	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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.15
Subcellular location	Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.11. Isoform 2: Cell membrane; Single-pass type I membrane protein Ref.11. Isoform 3: Cytoplasm. Note: Detected in the cytoplasm of spermatozoa, especially in the equatorial and subacrosomal region of the sperm head By similarity. Ref.11
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. Ref.3 Ref.11 Ref.18
Post-translational modification	Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation By similarity. Ref.11 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. Ref.9 Ref.11
Involvement in disease	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. Ref.9 Ref.10 Ref.11 Ref.13 Ref.15 Ref.21 Ref.22 Ref.23
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.
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	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Proto-oncogene
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Fc receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB T cell differentiation Inferred from mutant phenotype PubMed 12354381. Source: UniProtKB actin cytoskeleton reorganization Inferred from sequence or structural similarity. Source: UniProtKB activation of MAPK activity Inferred from electronic annotation. Source: Compara cell chemotaxis Inferred from sequence or structural similarity. Source: UniProtKB cellular response to thyroid hormone stimulus Inferred from direct assay PubMed 19375645. Source: UniProtKB dendritic cell cytokine production Inferred from mutant phenotype PubMed 18454155. Source: UniProtKB detection of mechanical stimulus involved in sensory perception of sound Inferred from mutant phenotype Ref.4. Source: UniProtKB digestive tract development Inferred from mutant phenotype PubMed 15067126. Source: UniProtKB embryonic hemopoiesis Inferred from mutant phenotype PubMed 20536544. Source: UniProtKB erythrocyte differentiation Inferred from mutant phenotype PubMed 12354381. Source: UniProtKB erythropoietin-mediated signaling pathway Inferred from mutant phenotype PubMed 18538998. Source: UniProtKB germ cell programmed cell death Inferred from genetic interaction PubMed 14660547. Source: MGI glycosphingolipid metabolic process Inferred from mutant phenotype PubMed 18308723. Source: MGI immature B cell differentiation Inferred from mutant phenotype PubMed 15067126. Source: UniProtKB inflammatory response Inferred from mutant phenotype PubMed 18454155. Source: UniProtKB intracellular protein kinase cascade Inferred from direct assay PubMed 10872802. Source: MGI lamellipodium assembly Inferred from direct assay PubMed 10982396. Source: UniProtKB lymphoid progenitor cell differentiation Inferred from genetic interaction PubMed 7621074. Source: MGI male gonad development Inferred from electronic annotation. Source: Compara mast cell chemotaxis Inferred from electronic annotation. Source: Compara mast cell cytokine production Inferred from sequence or structural similarity. Source: UniProtKB mast cell degranulation Inferred from sequence or structural similarity. Source: UniProtKB mast cell differentiation Inferred from mutant phenotype PubMed 15067126PubMed 16127161. Source: UniProtKB megakaryocyte development Inferred from mutant phenotype PubMed 15067126. Source: UniProtKB melanocyte adhesion Inferred from direct assay PubMed 22637532. Source: UniProtKB melanocyte differentiation Inferred from mutant phenotype PubMed 15768389. Source: UniProtKB melanocyte migration Inferred from mutant phenotype PubMed 15067126. Source: UniProtKB myeloid progenitor cell differentiation Inferred from genetic interaction PubMed 7621074. Source: MGI negative regulation of programmed cell death Inferred from mutant phenotype PubMed 18308723. Source: MGI ovarian follicle development Inferred from mutant phenotype PubMed 20536544. Source: UniProtKB peptidyl-tyrosine phosphorylation Inferred from direct assay PubMed 10872802. Source: MGI positive regulation of MAP kinase activity Inferred from genetic interaction PubMed 10620616. Source: MGI positive regulation of cell proliferation Inferred from genetic interaction PubMed 10620616. Source: MGI positive regulation of gene expression Inferred from mutant phenotype PubMed 18308723. Source: MGI positive regulation of sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara positive regulation of tyrosine phosphorylation of Stat1 protein Inferred from electronic annotation. Source: Compara positive regulation of tyrosine phosphorylation of Stat3 protein Inferred from electronic annotation. Source: Compara positive regulation of tyrosine phosphorylation of Stat5 protein Inferred from electronic annotation. Source: Compara protein autophosphorylation Traceable author statement PubMed 12140361. Source: MGI regulation of cell shape Inferred from direct assay PubMed 10982396. Source: UniProtKB regulation of developmental pigmentation Inferred from mutant phenotype PubMed 18454205. Source: MGI response to radiation Inferred from mutant phenotype PubMed 12833143. Source: MGI signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC spermatid development Inferred from mutant phenotype PubMed 18308723. Source: MGI stem cell differentiation Inferred from mutant phenotype PubMed 18258857. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell external side of plasma membrane Inferred from direct assay PubMed 10943842PubMed 12714518PubMed 12714519PubMed 12900455PubMed 14990792PubMed 15909309PubMed 15947484PubMed 16287714PubMed 16455951PubMed 18958875PubMed 18971422PubMed 19934022PubMed 21708977. Source: MGI extracellular space Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cytokine binding Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor signaling protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro stem cell factor receptor activity Inferred from direct assay PubMed 10872802. Source: MGI
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P05532-1)

Also known as: GNNK(+); Kit(+);

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

Isoform 2 (identifier: P05532-2)

Also known as: GNNK(-); KitA(+);

The sequence of this isoform differs from the canonical sequence as follows:
     512-515: Missing.

Isoform 3 (identifier: P05532-3)

Also known as: Tr-kit; Truncated;

The sequence of this isoform differs from the canonical sequence as follows:
     1-12: MRGARGAWDLLC → MAVAVFPFLPQQ
     13-789: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Potential

Chain

25 – 979

955

Mast/stem cell growth factor receptor Kit

PRO_0000016755

Regions

Topological domain

25 – 527

503

Extracellular Potential

Transmembrane

528 – 548

21

Helical; Potential

Topological domain

549 – 979

431

Cytoplasmic Potential

Domain

31 – 117

87

Ig-like C2-type 1

Domain

126 – 210

85

Ig-like C2-type 2

Domain

217 – 315

99

Ig-like C2-type 3

Domain

324 – 417

94

Ig-like C2-type 4

Domain

420 – 514

95

Ig-like C2-type 5

Domain

592 – 939

348

Protein kinase

Nucleotide binding

599 – 606

8

ATP By similarity

Nucleotide binding

674 – 680

7

ATP By similarity

Region

571 – 573

3

Important for interaction with phosphotyrosine-binding proteins By similarity

Sites

Active site

794

1

Proton acceptor By similarity

Metal binding

571

1

Magnesium By similarity

Metal binding

799

1

Magnesium By similarity

Metal binding

812

1

Magnesium By similarity

Binding site

626

1

ATP By similarity

Binding site

798

1

ATP By similarity

Site

938

1

Important for interaction with phosphotyrosine-binding proteins By similarity

Amino acid modifications

Modified residue

550

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

556

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

571

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

573

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

706

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

723

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

732

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

743

1

Phosphoserine; by PKC/PRKCA By similarity

Modified residue

748

1

Phosphoserine; by PKC/PRKCA By similarity

Modified residue

823

1

Phosphoserine By similarity

Modified residue

825

1

Phosphotyrosine; by autocatalysis

Modified residue

893

1

Phosphoserine By similarity

Modified residue

902

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

938

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

962

1

Phosphoserine By similarity

Glycosylation

146

1

N-linked (GlcNAc...) Potential

Glycosylation

296

1

N-linked (GlcNAc...) Ref.21

Glycosylation

303

1

N-linked (GlcNAc...) Ref.21

Glycosylation

323

1

N-linked (GlcNAc...) Potential

Glycosylation

355

1

N-linked (GlcNAc...) Potential

Glycosylation

370

1

N-linked (GlcNAc...) Potential

Glycosylation

466

1

N-linked (GlcNAc...) Potential

Glycosylation

489

1

N-linked (GlcNAc...) Potential

Disulfide bond

58 ↔ 98

Ref.21

Disulfide bond

137 ↔ 187

Ref.21

Disulfide bond

152 ↔ 184

Ref.21

Disulfide bond

234 ↔ 293

Ref.21

Disulfide bond

431 ↔ 494

By similarity

Natural variations

Alternative sequence

1 – 12

12

MRGAR…WDLLC → MAVAVFPFLPQQ in isoform 3.

VSP_041868

Alternative sequence

13 – 789

777

Missing in isoform 3.

VSP_041869

Alternative sequence

512 – 515

4

Missing in isoform 2.

VSP_041870

Natural variant

207

1

A → E Loss-of-function mutation abolishing ligand binding. Ref.1 Ref.20

Natural variant

586

1

E → K in W37 spotting; impaired protein stability and loss of kinase activity. Ref.9 Ref.23

Natural variant

664

1

T → M in Wv spotting. Ref.23

Natural variant

794

1

D → N in W42 spotting; loss of kinase activity and impaired internalization after exposure to KITLG/SCF. Ref.11 Ref.22

Natural variant

835

1

V → M in W41 spotting; decreased kinase activity. Ref.9 Ref.23

Experimental info

Mutagenesis

571

1

Y → F: Abolishes interaction with PTPN11/SHP-2. Ref.13

Mutagenesis

573

1

Y → F: Abolishes interaction with PTPN6/SHP-1. Ref.13

Mutagenesis

573

1

Missing: Abolishes interaction with PTPN6/SHP-1. Ref.13

Mutagenesis

723

1

Y → F: Abolishes interaction with PIK3R1. Ref.11

Mutagenesis

860

1

F → S: Mice display white fur, hearing loss, anemia and mast cell deficiency, plus sterility in both males and females. Ref.4

Sequence conflict

551

1

L → F in AAH52457. Ref.6

Sequence conflict

781

1

G → A in CAA68772. Ref.1

Sequence conflict

781

1

G → A in CAA46799. Ref.2

Sequence conflict

860

1

F → S in AAS45607. Ref.4

Secondary structure

1

.

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979

Helix Strand Turn

Details...

Beta strand

38 – 41

4

Beta strand

43 – 49

7

Beta strand

54 – 59

6

Beta strand

63 – 69

7

Beta strand

71 – 73

3

Beta strand

75 – 78

4

Beta strand

80 – 85

6

Helix

90 – 92

3

Beta strand

94 – 103

10

Beta strand

105 – 113

9

Beta strand

125 – 128

4

Beta strand

133 – 135

3

Beta strand

145 – 151

7

Beta strand

162 – 166

5

Turn

167 – 169

3

Beta strand

170 – 175

6

Helix

178 – 180

3

Beta strand

184 – 191

8

Beta strand

194 – 197

4

Beta strand

201 – 206

6

Beta strand

214 – 216

3

Beta strand

230 – 240

11

Beta strand

244 – 256

13

Beta strand

264 – 268

5

Beta strand

271 – 282

12

Beta strand

285 – 287

3

Beta strand

289 – 296

8

Beta strand

301 – 308

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (GNNK(+)) (Kit(+)) [UniParc]. Last modified October 19, 2011. Version 3. Checksum: 03FB4D672248585E	FASTA	979	109,343
	10 20 30 40 50 60 MRGARGAWDL LCVLLVLLRG QTATSQPSAS PGEPSPPSIH PAQSELIVEA GDTLSLTCID 70 80 90 100 110 120 PDFVRWTFKT YFNEMVENKK NEWIQEKAEA TRTGTYTCSN SNGLTSSIYV FVRDPAKLFL 130 140 150 160 170 180 VGLPLFGKED SDALVRCPLT DPQVSNYSLI ECDGKSLPTD LTFVPNPKAG ITIKNVKRAY 190 200 210 220 230 240 HRLCVRCAAQ RDGTWLHSDK FTLKVRAAIK AIPVVSVPET SHLLKKGDTF TVVCTIKDVS 250 260 270 280 290 300 TSVNSMWLKM NPQPQHIAQV KHNSWHRGDF NYERQETLTI SSARVDDSGV FMCYANNTFG 310 320 330 340 350 360 SANVTTTLKV VEKGFINISP VKNTTVFVTD GENVDLVVEY EAYPKPEHQQ WIYMNRTSAN 370 380 390 400 410 420 KGKDYVKSDN KSNIRYVNQL RLTRLKGTEG GTYTFLVSNS DASASVTFNV YVNTKPEILT 430 440 450 460 470 480 YDRLINGMLQ CVAEGFPEPT IDWYFCTGAE QRCTTPVSPV DVQVQNVSVS PFGKLVVQSS 490 500 510 520 530 540 IDSSVFRHNG TVECKASNDV GKSSAFFNFA FKGNNKEQIQ AHTLFTPLLI GFVVAAGAMG 550 560 570 580 590 600 IIVMVLTYKY LQKPMYEVQW KVVEEINGNN YVYIDPTQLP YDHKWEFPRN RLSFGKTLGA 610 620 630 640 650 660 GAFGKVVEAT AYGLIKSDAA MTVAVKMLKP SAHLTEREAL MSELKVLSYL GNHMNIVNLL 670 680 690 700 710 720 GACTVGGPTL VITEYCCYGD LLNFLRRKRD SFIFSKQEEQ AEAALYKNLL HSTEPSCDSS 730 740 750 760 770 780 NEYMDMKPGV SYVVPTKTDK RRSARIDSYI ERDVTPAIME DDELALDLDD LLSFSYQVAK 790 800 810 820 830 840 GMAFLASKNC IHRDLAARNI LLTHGRITKI CDFGLARDIR NDSNYVVKGN ARLPVKWMAP 850 860 870 880 890 900 ESIFSCVYTF ESDVWSYGIF LWELFSLGSS PYPGMPVDSK FYKMIKEGFR MVSPEHAPAE 910 920 930 940 950 960 MYDVMKTCWD ADPLKRPTFK QVVQLIEKQI SDSTKHIYSN LANCNPNPEN PVVVDHSVRV 970 NSVGSSASST QPLLVHEDA
	Isoform 2 (GNNK(-)) (KitA(+)) [UniParc]. Checksum: 57BFE10AE456C145	FASTA	975	108,929
	10 20 30 40 50 60 MRGARGAWDL LCVLLVLLRG QTATSQPSAS PGEPSPPSIH PAQSELIVEA GDTLSLTCID 70 80 90 100 110 120 PDFVRWTFKT YFNEMVENKK NEWIQEKAEA TRTGTYTCSN SNGLTSSIYV FVRDPAKLFL 130 140 150 160 170 180 VGLPLFGKED SDALVRCPLT DPQVSNYSLI ECDGKSLPTD LTFVPNPKAG ITIKNVKRAY 190 200 210 220 230 240 HRLCVRCAAQ RDGTWLHSDK FTLKVRAAIK AIPVVSVPET SHLLKKGDTF TVVCTIKDVS 250 260 270 280 290 300 TSVNSMWLKM NPQPQHIAQV KHNSWHRGDF NYERQETLTI SSARVDDSGV FMCYANNTFG 310 320 330 340 350 360 SANVTTTLKV VEKGFINISP VKNTTVFVTD GENVDLVVEY EAYPKPEHQQ WIYMNRTSAN 370 380 390 400 410 420 KGKDYVKSDN KSNIRYVNQL RLTRLKGTEG GTYTFLVSNS DASASVTFNV YVNTKPEILT 430 440 450 460 470 480 YDRLINGMLQ CVAEGFPEPT IDWYFCTGAE QRCTTPVSPV DVQVQNVSVS PFGKLVVQSS 490 500 510 520 530 540 IDSSVFRHNG TVECKASNDV GKSSAFFNFA FKEQIQAHTL FTPLLIGFVV AAGAMGIIVM 550 560 570 580 590 600 VLTYKYLQKP MYEVQWKVVE EINGNNYVYI DPTQLPYDHK WEFPRNRLSF GKTLGAGAFG 610 620 630 640 650 660 KVVEATAYGL IKSDAAMTVA VKMLKPSAHL TEREALMSEL KVLSYLGNHM NIVNLLGACT 670 680 690 700 710 720 VGGPTLVITE YCCYGDLLNF LRRKRDSFIF SKQEEQAEAA LYKNLLHSTE PSCDSSNEYM 730 740 750 760 770 780 DMKPGVSYVV PTKTDKRRSA RIDSYIERDV TPAIMEDDEL ALDLDDLLSF SYQVAKGMAF 790 800 810 820 830 840 LASKNCIHRD LAARNILLTH GRITKICDFG LARDIRNDSN YVVKGNARLP VKWMAPESIF 850 860 870 880 890 900 SCVYTFESDV WSYGIFLWEL FSLGSSPYPG MPVDSKFYKM IKEGFRMVSP EHAPAEMYDV 910 920 930 940 950 960 MKTCWDADPL KRPTFKQVVQ LIEKQISDST KHIYSNLANC NPNPENPVVV DHSVRVNSVG 970 SSASSTQPLL VHEDA
	Isoform 3 (Tr-kit) (Truncated) [UniParc]. Checksum: 38323E3690025842	FASTA	202	22,814
	10 20 30 40 50 60 MAVAVFPFLP QQCIHRDLAA RNILLTHGRI TKICDFGLAR DIRNDSNYVV KGNARLPVKW 70 80 90 100 110 120 MAPESIFSCV YTFESDVWSY GIFLWELFSL GSSPYPGMPV DSKFYKMIKE GFRMVSPEHA 130 140 150 160 170 180 PAEMYDVMKT CWDADPLKRP TFKQVVQLIE KQISDSTKHI YSNLANCNPN PENPVVVDHS 190 200 VRVNSVGSSA SSTQPLLVHE DA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Qiu F., Ray P., Brown K., Barker P.E., Jhanwar S., Ruddle F.H., Besmer P. EMBO J. 7:1003-1011(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLU-207. Strain: BALB/c. Tissue: Brain.
[2]	"Exon skipping by mutation of an authentic splice site of c-kit gene in W/W mouse." Hayashi S., Kunisada T., Ogawa M., Yamaguchi K., Nishikawa S. Nucleic Acids Res. 19:1267-1271(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Medulla oblongata.
[3]	"A novel c-kit transcript, potentially encoding a truncated receptor, originates within a kit gene intron in mouse spermatids." Rossi P., Marziali G., Albanesi C., Charlesworth A., Geremia R., Sorrentino V. Dev. Biol. 152:203-207(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3), TISSUE SPECIFICITY. Strain: ICR.
[4]	"Identification of a novel point mutation of mouse proto-oncogene c-kit through N-ethyl-N-nitrosourea mutagenesis." Ruan H.B., Zhang N., Gao X. Genetics 169:819-831(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), MUTAGENESIS OF PHE-860. Strain: C57BL/6J.
[5]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6 and FVB/N. Tissue: Brain and Mammary tumor.
[7]	"Cloning and functional analysis of the mouse c-kit promoter." Yasuda H., Galli S.J., Geissler E.N. Biochem. Biophys. Res. Commun. 191:893-901(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. Strain: BALB/c.
[8]	"Candidate ligand for the c-kit transmembrane kinase receptor: KL, a fibroblast derived growth factor stimulates mast cells and erythroid progenitors." Tan J.C., Buck J., Levi E., Besmer P. EMBO J. 9:3287-3294(1990) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[9]	"Signal transduction by normal isoforms and W mutant variants of the Kit receptor tyrosine kinase." Reith A.D., Ellis C., Lyman S.D., Anderson D.M., Williams D.E., Bernstein A., Pawson T. EMBO J. 10:2451-2459(1991) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ACTIVATION OF PLCG1, INTERACTION WITH PLCG1, ALTERNATIVE SPLICING, PHOSPHORYLATION, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS W37 LYS-586 AND W41 MET-835.
[10]	"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." Serve H., Hsu Y.C., Besmer P. J. Biol. Chem. 269:6026-6030(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIK3R1, FUNCTION IN PHOSPHORYLATION OF PIK3R1.
[11]	"Mechanism of down-regulation of c-kit receptor. Roles of receptor tyrosine kinase, phosphatidylinositol 3'-kinase, and protein kinase C." Yee N.S., Hsiau C.W., Serve H., Vosseller K., Besmer P. J. Biol. Chem. 269:31991-31998(1994) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, INTERACTION WITH PIK3R1, CHARACTERIZATION OF VARIANT W42 ASN-794, MUTAGENESIS OF TYR-723, TISSUE SPECIFICITY.
[12]	"Involvement of phospholipase Cgamma1 in mouse egg activation induced by a truncated form of the C-kit tyrosine kinase present in spermatozoa." Sette C., Bevilacqua A., Geremia R., Rossi P. J. Cell Biol. 142:1063-1074(1998) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING, FUNCTION IN ACTIVATION OF PLCG1.
[13]	"SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain." Kozlowski M., Larose L., Lee F., Le D.M., Rottapel R., Siminovitch K.A. Mol. Cell. Biol. 18:2089-2099(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTPN6/SHP-1 AND PTPN11/SHP-2, FUNCTION IN PHOSPHORYLATION OF PTPN6/SHP-1, MUTAGENESIS OF TYR-571 AND TYR-573.
[14]	"Molecular mechanisms utilized by alternative c-kit gene products in the control of spermatogonial proliferation and sperm-mediated egg activation." Rossi P., Dolci S., Sette C., Geremia R. Andrologia 35:71-78(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN SPERMATOGENESIS AND FERTILITY.
[15]	"The tyrosine kinase FES is an essential effector of KITD816V proliferation signal." Voisset E., Lopez S., Dubreuil P., De Sepulveda P. Blood 110:2593-2599(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FES/FPS.
[16]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-571; TYR-573; TYR-706 AND TYR-938, MASS SPECTROMETRY. Tissue: Mast cell.
[17]	"Protein-tyrosine phosphatase alpha regulates stem cell factor-dependent c-Kit activation and migration of mast cells." Samayawardhena L.A., Pallen C.J. J. Biol. Chem. 283:29175-29185(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MAST CELL MIGRATION, IN SIGNALING VIA FYN.
[18]	"Murine hematopoietic stem cells and multipotent progenitors express truncated intracellular form of c-kit receptor." Zayas J., Spassov D.S., Nachtman R.G., Jurecic R. Stem Cells Dev. 17:343-353(2008) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[19]	"Nf1-/- Schwann cell-conditioned medium modulates mast cell degranulation by c-Kit-mediated hyperactivation of phosphatidylinositol 3-kinase." Chen S., Burgin S., McDaniel A., Li X., Yuan J., Chen M., Khalaf W., Clapp D.W., Yang F.C. Am. J. Pathol. 177:3125-3132(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MAST CELL DEGRANULATION.
[20]	Jawad-Alam J. Unpublished observations (APR-2010) Cited for: VARIANT GLU-207.
[21]	"Structural basis for stem cell factor-KIT signaling and activation of class III receptor tyrosine kinases." Liu H., Chen X., Focia P.J., He X. EMBO J. 26:891-901(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-314 IN COMPLEX WITH KITLG/SCF, DISULFIDE BONDS, GLYCOSYLATION AT ASN-296 AND ASN-303.
[22]	"The dominant W42 spotting phenotype results from a missense mutation in the c-kit receptor kinase." Tan J.C., Nocka K., Ray P., Traktman P., Besmer P. Science 247:209-212(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT W42 ASN-794.
[23]	"Molecular bases of dominant negative and loss of function mutations at the murine c-kit/white spotting locus: W37, Wv, W41 and W." Nocka K., Tan J.C., Chiu E., Chu T.Y., Ray P., Traktman P., Besmer P. EMBO J. 9:1805-1813(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS W37 LYS-586; WV MET-664 AND W41 MET-835.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00864 mRNA. Translation: CAA68772.1.
AK046795 mRNA. Translation: BAC32872.1.
X65997 mRNA. Translation: CAA46798.1.
X65998 Genomic DNA. Translation: CAA46799.1. Sequence problems.
X65998 Genomic DNA. Translation: CAA46800.1.
AY536430 mRNA. Translation: AAS45606.1.
AY536431 mRNA. Translation: AAS45607.1.
AC013622 Genomic DNA. No translation available.
AC115853 Genomic DNA. No translation available.
BC052457 mRNA. Translation: AAH52457.1.
BC075716 mRNA. Translation: AAH75716.1.
L11358 Genomic DNA. Translation: AAA37420.1.

IPI

IPI00120590.

PIR

A44876.
TVMSKT. S00474.
S24667.
S34435.

RefSeq

NP_001116205.1. NM_001122733.1.
NP_066922.2. NM_021099.3.

UniGene

Mm.247073.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2O26	X-ray	2.50	U/W/X/Y	25-314	[»]

ProteinModelPortal

P05532.

SMR

P05532. Positions 33-510, 550-696, 765-929.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59622N.

PTM databases

PhosphoSite

P05532.

Proteomic databases

PaxDb

P05532.

PRIDE

P05532.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000005815; ENSMUSP00000005815; ENSMUSG00000005672.

GeneID

16590.

KEGG

mmu:16590.

Organism-specific databases

CTD

3815.

MGI

MGI:96677. Kit.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00660000095142.

HOGENOM

HOG000112008.

HOVERGEN

HBG004335.

InParanoid

Q6QJB7.

KO

K05091.

Enzyme and pathway databases

BRENDA

2.7.10.1. 3474.

Reactome

REACT_115202. Signal Transduction.

Gene expression databases

ArrayExpress

P05532.

Bgee

P05532.

CleanEx

MM_KIT.

Genevestigator

P05532.

GermOnline

ENSMUSG00000005672. Mus musculus.

Family and domain databases

Gene3D

2.60.40.10. 5 hits.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR027263. SCGF_receptor.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016243. Tyr_kinase_CSF1/PDGF_rcpt.
IPR001824. Tyr_kinase_rcpt_3_CS.
[Graphical view]

Pfam

PF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PIRSF

PIRSF500951. SCGF_recepter. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.

SMART

SM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

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

Search...

Other

ChiTaRS

KIT. mouse.

EvolutionaryTrace

P05532.

NextBio

290137.

SOURCE

Search...

Entry information

Entry name

KIT_MOUSE

Accession

Primary (citable) accession number: P05532
Secondary accession number(s): Q61415 , Q61416, Q61417, Q6LEE9, Q6QJB7, Q6QJB8, Q7TS86, Q8C8K9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	October 19, 2011
Last modified:	May 1, 2013
This is version 151 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program