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P05532 (KIT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length979 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Proto-oncogene
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc 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: Ensembl

cell chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

cell differentiation

Traceable author statement PubMed 12140361. Source: MGI

cellular response to thyroid hormone stimulus

Inferred from direct assay PubMed 19375645. Source: UniProtKB

chemotaxis

Traceable author statement PubMed 12140361. Source: MGI

cytokine-mediated signaling pathway

Inferred from direct assay PubMed 10872802. Source: MGI

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

developmental pigmentation

Inferred from mutant phenotype PubMed 15322542. Source: MGI

digestive tract development

Inferred from mutant phenotype PubMed 15067126. Source: UniProtKB

ectopic germ cell programmed cell death

Inferred from genetic interaction PubMed 14660547. Source: MGI

embryonic hemopoiesis

Inferred from mutant phenotype PubMed 20536544. Source: UniProtKB

epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

erythrocyte differentiation

Inferred from mutant phenotype PubMed 12354381. Source: UniProtKB

erythropoietin-mediated signaling pathway

Inferred from mutant phenotype PubMed 18538998. Source: UniProtKB

germ cell development

Traceable author statement PubMed 12140361. Source: MGI

germ cell migration

Inferred from electronic annotation. Source: Ensembl

glycosphingolipid metabolic process

Inferred from mutant phenotype PubMed 18308723. Source: MGI

hemopoiesis

Inferred from mutant phenotype PubMed 11805142. 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 signal transduction

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: Ensembl

mast cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

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 leukocyte differentiation

Inferred from mutant phenotype PubMed 18258601. Source: MGI

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

pigmentation

Inferred from mutant phenotype PubMed 15067126. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from genetic interaction PubMed 10620616. Source: MGI

positive regulation of Notch signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

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 long-term neuronal synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

positive regulation of pseudopodium assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of tyrosine phosphorylation of Stat1 protein

Inferred from electronic annotation. Source: Ensembl

positive regulation of tyrosine phosphorylation of Stat3 protein

Inferred from electronic annotation. Source: Ensembl

positive regulation of tyrosine phosphorylation of Stat5 protein

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Traceable author statement PubMed 12140361. Source: MGI

protein phosphorylation

Inferred from direct assay PubMed 11805142. 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

somatic stem cell division

Inferred from electronic annotation. Source: Ensembl

somatic stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

spermatid development

Inferred from mutant phenotype PubMed 18308723. Source: MGI

spermatogenesis

Inferred from mutant phenotype PubMed 20536544. Source: UniProtKB

stem cell differentiation

Inferred from mutant phenotype PubMed 18258857. Source: UniProtKB

visual learning

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 9216738PubMed 9324354. Source: MGI

cell-cell junction

Inferred from direct assay PubMed 23284756. Source: MGI

cytoplasmic side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

mast cell granule

Inferred from sequence or structural similarity. Source: GOC

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP 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

protease binding

Inferred from physical interaction PubMed 12135759. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 10679268PubMed 10872802PubMed 11805142PubMed 12646235PubMed 16760463PubMed 1698557. Source: MGI

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

transmembrane receptor protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 979955Mast/stem cell growth factor receptor Kit
PRO_0000016755

Regions

Topological domain25 – 527503Extracellular Potential
Transmembrane528 – 54821Helical; Potential
Topological domain549 – 979431Cytoplasmic Potential
Domain31 – 11787Ig-like C2-type 1
Domain126 – 21085Ig-like C2-type 2
Domain217 – 31599Ig-like C2-type 3
Domain324 – 41794Ig-like C2-type 4
Domain420 – 51495Ig-like C2-type 5
Domain592 – 939348Protein kinase
Nucleotide binding599 – 6068ATP By similarity
Nucleotide binding674 – 6807ATP By similarity
Region571 – 5733Important for interaction with phosphotyrosine-binding proteins By similarity

Sites

Active site7941Proton acceptor By similarity
Metal binding5711Magnesium By similarity
Metal binding7991Magnesium By similarity
Metal binding8121Magnesium By similarity
Binding site6261ATP By similarity
Binding site7981ATP By similarity
Site9381Important for interaction with phosphotyrosine-binding proteins By similarity

Amino acid modifications

Modified residue5501Phosphotyrosine; by autocatalysis By similarity
Modified residue5561Phosphotyrosine; by autocatalysis By similarity
Modified residue5711Phosphotyrosine; alternate Ref.16
Modified residue5711Phosphotyrosine; by autocatalysis; alternate By similarity
Modified residue5731Phosphotyrosine; alternate Ref.16
Modified residue5731Phosphotyrosine; by autocatalysis; alternate By similarity
Modified residue7061Phosphotyrosine; alternate Ref.16
Modified residue7061Phosphotyrosine; by autocatalysis; alternate By similarity
Modified residue7231Phosphotyrosine; by autocatalysis By similarity
Modified residue7321Phosphotyrosine; by autocatalysis By similarity
Modified residue7431Phosphoserine; by PKC/PRKCA By similarity
Modified residue7481Phosphoserine; by PKC/PRKCA By similarity
Modified residue8231Phosphoserine By similarity
Modified residue8251Phosphotyrosine; by autocatalysis Ref.11
Modified residue8931Phosphoserine By similarity
Modified residue9021Phosphotyrosine; by autocatalysis By similarity
Modified residue9381Phosphotyrosine; alternate Ref.16
Modified residue9381Phosphotyrosine; by autocatalysis; alternate By similarity
Modified residue9621Phosphoserine By similarity
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Ref.21
Glycosylation3031N-linked (GlcNAc...) Ref.21
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation3551N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation4661N-linked (GlcNAc...) Potential
Glycosylation4891N-linked (GlcNAc...) Potential
Disulfide bond58 ↔ 98 Ref.21
Disulfide bond137 ↔ 187 Ref.21
Disulfide bond152 ↔ 184 Ref.21
Disulfide bond234 ↔ 293 Ref.21
Disulfide bond431 ↔ 494 By similarity

Natural variations

Alternative sequence1 – 1212MRGAR…WDLLC → MAVAVFPFLPQQ in isoform 3.
VSP_041868
Alternative sequence13 – 789777Missing in isoform 3.
VSP_041869
Alternative sequence512 – 5154Missing in isoform 2.
VSP_041870
Natural variant2071A → E Loss-of-function mutation abolishing ligand binding. Ref.1 Ref.20
Natural variant5861E → K in W37 spotting; impaired protein stability and loss of kinase activity. Ref.9 Ref.23
Natural variant6641T → M in Wv spotting. Ref.23
Natural variant7941D → N in W42 spotting; loss of kinase activity and impaired internalization after exposure to KITLG/SCF. Ref.11 Ref.22
Natural variant8351V → M in W41 spotting; decreased kinase activity. Ref.9 Ref.23

Experimental info

Mutagenesis5711Y → F: Abolishes interaction with PTPN11/SHP-2. Ref.13
Mutagenesis5731Y → F: Abolishes interaction with PTPN6/SHP-1. Ref.13
Mutagenesis5731Missing: Abolishes interaction with PTPN6/SHP-1. Ref.13
Mutagenesis7231Y → F: Abolishes interaction with PIK3R1. Ref.11
Mutagenesis8601F → S: Mice display white fur, hearing loss, anemia and mast cell deficiency, plus sterility in both males and females. Ref.4
Sequence conflict5511L → F in AAH52457. Ref.6
Sequence conflict7811G → A in CAA68772. Ref.1
Sequence conflict7811G → A in CAA46799. Ref.2
Sequence conflict8601F → S in AAS45607. Ref.4

Secondary structure

....................................................... 979
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (GNNK(+)) (Kit(+)) [UniParc].

Last modified October 19, 2011. Version 3.
Checksum: 03FB4D672248585E

FASTA979109,343
        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 

« Hide

Isoform 2 (GNNK(-)) (KitA(+)) [UniParc].

Checksum: 57BFE10AE456C145
Show »

FASTA975108,929
Isoform 3 (Tr-kit) (Truncated) [UniParc].

Checksum: 38323E3690025842
Show »

FASTA20222,814

References

« Hide '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. expand/collapse author list , 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, PHOSPHORYLATION AT TYR-825, 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
CCDSCCDS51525.1. [P05532-1]
PIRA44876.
TVMSKT. S00474.
S24667.
S34435.
RefSeqNP_001116205.1. NM_001122733.1. [P05532-1]
NP_066922.2. NM_021099.3. [P05532-2]
UniGeneMm.247073.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2O26X-ray2.50U/W/X/Y25-314[»]
ProteinModelPortalP05532.
SMRP05532. Positions 33-511, 550-933.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200957. 18 interactions.
DIPDIP-59622N.
IntActP05532. 3 interactions.

Chemistry

ChEMBLCHEMBL2034798.

PTM databases

PhosphoSiteP05532.

Proteomic databases

MaxQBP05532.
PaxDbP05532.
PRIDEP05532.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005815; ENSMUSP00000005815; ENSMUSG00000005672. [P05532-1]
GeneID16590.
KEGGmmu:16590.
UCSCuc008xug.2. mouse. [P05532-1]
uc012dxj.1. mouse. [P05532-2]

Organism-specific databases

CTD3815.
MGIMGI:96677. Kit.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00720000108490.
HOGENOMHOG000112008.
HOVERGENHBG004335.
InParanoidQ6QJB7.
KOK05091.
TreeFamTF325768.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.
ReactomeREACT_188257. Signal Transduction.

Gene expression databases

ArrayExpressP05532.
BgeeP05532.
CleanExMM_KIT.
GenevestigatorP05532.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_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]
PfamPF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF500951. SCGF_recepter. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTSM00409. IG. 2 hits.
SM00408. IGc2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 2 hits.
PROSITEPS50835. 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]
ProtoNetSearch...

Other

ChiTaRSKIT. mouse.
EvolutionaryTraceP05532.
NextBio290137.
PROP05532.
SOURCESearch...

Entry information

Entry nameKIT_MOUSE
AccessionPrimary (citable) accession number: P05532
Secondary accession number(s): Q61415 expand/collapse secondary AC list , 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: July 9, 2014
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot