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Protein

Mast/stem cell growth factor receptor Kit

Gene

Kit

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 SHC1.7 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation1 Publication

Enzyme regulationi

Present in an inactive conformation in the absence of bound ligand. KITLG/SCF binding leads to dimerization and activation by autophosphorylation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi571MagnesiumBy similarity1
Binding sitei626ATPPROSITE-ProRule annotation1
Active sitei794Proton acceptorPROSITE-ProRule annotation1
Binding sitei798ATPPROSITE-ProRule annotation1
Metal bindingi799MagnesiumBy similarity1
Metal bindingi812MagnesiumBy similarity1
Sitei938Important for interaction with phosphotyrosine-binding proteinsBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi599 – 606ATPPROSITE-ProRule annotation8
Nucleotide bindingi674 – 680ATPPROSITE-ProRule annotation7

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • activation of MAPK activity Source: MGI
  • cell chemotaxis Source: UniProtKB
  • cell differentiation Source: MGI
  • cellular response to thyroid hormone stimulus Source: UniProtKB
  • chemotaxis Source: MGI
  • cytokine-mediated signaling pathway Source: MGI
  • dendritic cell cytokine production Source: UniProtKB
  • detection of mechanical stimulus involved in sensory perception of sound Source: UniProtKB
  • developmental pigmentation Source: MGI
  • digestive tract development Source: UniProtKB
  • ectopic germ cell programmed cell death Source: MGI
  • embryonic hemopoiesis Source: UniProtKB
  • epithelial cell proliferation Source: Ensembl
  • erythrocyte differentiation Source: UniProtKB
  • erythropoietin-mediated signaling pathway Source: UniProtKB
  • Fc receptor signaling pathway Source: UniProtKB
  • germ cell development Source: MGI
  • germ cell migration Source: Ensembl
  • glycosphingolipid metabolic process Source: MGI
  • hematopoietic stem cell migration Source: MGI
  • hemopoiesis Source: MGI
  • immature B cell differentiation Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • intracellular signal transduction Source: MGI
  • Kit signaling pathway Source: MGI
  • lamellipodium assembly Source: UniProtKB
  • lymphoid progenitor cell differentiation Source: MGI
  • male gonad development Source: Ensembl
  • mast cell chemotaxis Source: MGI
  • mast cell cytokine production Source: UniProtKB
  • mast cell degranulation Source: UniProtKB
  • mast cell differentiation Source: UniProtKB
  • megakaryocyte development Source: UniProtKB
  • melanocyte adhesion Source: UniProtKB
  • melanocyte differentiation Source: UniProtKB
  • melanocyte migration Source: UniProtKB
  • myeloid leukocyte differentiation Source: MGI
  • myeloid progenitor cell differentiation Source: MGI
  • negative regulation of programmed cell death Source: MGI
  • ovarian follicle development Source: UniProtKB
  • peptidyl-tyrosine phosphorylation Source: MGI
  • pigmentation Source: UniProtKB
  • positive regulation of cell migration Source: Ensembl
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of gene expression Source: MGI
  • positive regulation of JAK-STAT cascade Source: MGI
  • positive regulation of long-term neuronal synaptic plasticity Source: Ensembl
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of MAP kinase activity Source: MGI
  • positive regulation of Notch signaling pathway Source: Ensembl
  • positive regulation of pseudopodium assembly Source: Ensembl
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  • positive regulation of tyrosine phosphorylation of Stat1 protein Source: MGI
  • positive regulation of tyrosine phosphorylation of Stat3 protein Source: MGI
  • positive regulation of tyrosine phosphorylation of Stat5 protein Source: MGI
  • positive regulation of vascular smooth muscle cell differentiation Source: MGI
  • protein autophosphorylation Source: MGI
  • protein phosphorylation Source: MGI
  • regulation of cell shape Source: UniProtKB
  • regulation of developmental pigmentation Source: MGI
  • response to radiation Source: MGI
  • somatic stem cell division Source: Ensembl
  • somatic stem cell population maintenance Source: Ensembl
  • spermatid development Source: MGI
  • spermatogenesis Source: UniProtKB
  • stem cell differentiation Source: UniProtKB
  • T cell differentiation Source: UniProtKB
  • visual learning Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiR-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1433559. Regulation of KIT signaling.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Mast/stem cell growth factor receptor Kit (EC:2.7.10.1)
Short name:
SCFR
Alternative name(s):
Proto-oncogene c-Kit
Tyrosine-protein kinase Kit
CD_antigen: CD117
Gene namesi
Name:Kit
Synonyms:Sl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:96677. Kit.

Subcellular locationi

Isoform 3 :
  • Cytoplasm

  • Note: Detected in the cytoplasm of spermatozoa, especially in the equatorial and subacrosomal region of the sperm head.By similarity

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 527ExtracellularSequence analysisAdd BLAST503
Transmembranei528 – 548HelicalSequence analysisAdd BLAST21
Topological domaini549 – 979CytoplasmicSequence analysisAdd BLAST431

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi571Y → F: Abolishes interaction with PTPN11/SHP-2. 1 Publication1
Mutagenesisi573Y → F: Abolishes interaction with PTPN6/SHP-1. 1 Publication1
Mutagenesisi573Missing : Abolishes interaction with PTPN6/SHP-1. 1 Publication1
Mutagenesisi723Y → F: Abolishes interaction with PIK3R1. 1 Publication1
Mutagenesisi860F → S: Mice display white fur, hearing loss, anemia and mast cell deficiency, plus sterility in both males and females. 1 Publication1

Keywords - Diseasei

Disease mutation, Proto-oncogene

Chemistry databases

ChEMBLiCHEMBL2034798.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000001675525 – 979Mast/stem cell growth factor receptor KitAdd BLAST955

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi58 ↔ 98PROSITE-ProRule annotation1 Publication
Disulfide bondi137 ↔ 187PROSITE-ProRule annotation1 Publication
Glycosylationi146N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi152 ↔ 184PROSITE-ProRule annotation1 Publication
Disulfide bondi234 ↔ 293PROSITE-ProRule annotation1 Publication
Glycosylationi296N-linked (GlcNAc...)1 Publication1
Glycosylationi303N-linked (GlcNAc...)1 Publication1
Glycosylationi323N-linked (GlcNAc...)Sequence analysis1
Glycosylationi355N-linked (GlcNAc...)Sequence analysis1
Glycosylationi370N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi431 ↔ 494PROSITE-ProRule annotation
Glycosylationi466N-linked (GlcNAc...)Sequence analysis1
Glycosylationi489N-linked (GlcNAc...)Sequence analysis1
Modified residuei550Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei556Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei571PhosphotyrosineCombined sources1
Modified residuei573PhosphotyrosineCombined sources1
Modified residuei706PhosphotyrosineCombined sources1
Modified residuei720PhosphoserineCombined sources1
Modified residuei723Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei732Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei743Phosphoserine; by PKC/PRKCABy similarity1
Modified residuei748Phosphoserine; by PKC/PRKCABy similarity1
Modified residuei823PhosphoserineBy similarity1
Modified residuei825Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei893PhosphoserineBy similarity1
Modified residuei902Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei938PhosphotyrosineCombined sources1
Modified residuei962PhosphoserineBy similarity1

Post-translational modificationi

Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation (By similarity).By similarity
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.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP05532.
PaxDbiP05532.
PRIDEiP05532.

PTM databases

iPTMnetiP05532.
PhosphoSitePlusiP05532.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiENSMUSG00000005672.
CleanExiMM_KIT.
ExpressionAtlasiP05532. baseline and differential.
GenevisibleiP05532. MM.

Interactioni

Subunit structurei

Monomer in the absence of bound KITLG/SCF. Homodimer in the presence of bound KITLG/SCF, forming a heterotetramer with two KITLG/SCF molecules. Interacts (via phosphorylated tyrosine residues) with the adapter proteins GRB2 and GRB7 (via SH2 domain), and SH2B2/APS. Interacts (via C-terminus) with MPDZ (via the tenth PDZ domain). Interacts (via phosphorylated tyrosine residues) with the protein phosphatases PTPN6/SHP-1 (via SH2 domain), PTPN11/SHP-2 (via SH2 domain) and PTPRU. Interacts with DOK1 and TEC (By similarity). Interacts with the protein kinase FES/FPS. Interacts with PLCG1. Interacts (via phosphorylated tyrosine residues) with PIK3R1 and PIK3 catalytic subunit. Interacts (KITLG/SCF-bound) with IL1RL1. Interacts with IL1RAP (independent of stimulation with KITLG/SCF). A mast cell-specific KITLG/SCF-induced interleukin-33 signaling complex contains IL1RL1, IL1RAP, KIT and MYD88.By similarity8 Publications

GO - Molecular functioni

  • cytokine binding Source: UniProtKB
  • protease binding Source: BHF-UCL
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi200957. 18 interactors.
DIPiDIP-59622N.
IntActiP05532. 3 interactors.
STRINGi10090.ENSMUSP00000005815.

Chemistry databases

BindingDBiP05532.

Structurei

Secondary structure

1979
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 41Combined sources4
Beta strandi43 – 49Combined sources7
Beta strandi54 – 59Combined sources6
Beta strandi63 – 69Combined sources7
Beta strandi71 – 73Combined sources3
Beta strandi75 – 78Combined sources4
Beta strandi80 – 85Combined sources6
Helixi90 – 92Combined sources3
Beta strandi94 – 103Combined sources10
Beta strandi105 – 113Combined sources9
Beta strandi125 – 128Combined sources4
Beta strandi133 – 135Combined sources3
Beta strandi145 – 151Combined sources7
Beta strandi162 – 166Combined sources5
Turni167 – 169Combined sources3
Beta strandi170 – 175Combined sources6
Helixi178 – 180Combined sources3
Beta strandi184 – 191Combined sources8
Beta strandi194 – 197Combined sources4
Beta strandi201 – 206Combined sources6
Beta strandi214 – 216Combined sources3
Beta strandi230 – 240Combined sources11
Beta strandi244 – 256Combined sources13
Beta strandi264 – 268Combined sources5
Beta strandi271 – 282Combined sources12
Beta strandi285 – 287Combined sources3
Beta strandi289 – 296Combined sources8
Beta strandi301 – 308Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O26X-ray2.50U/W/X/Y25-314[»]
ProteinModelPortaliP05532.
SMRiP05532.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05532.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 117Ig-like C2-type 1Add BLAST87
Domaini126 – 210Ig-like C2-type 2Add BLAST85
Domaini217 – 315Ig-like C2-type 3Add BLAST99
Domaini324 – 417Ig-like C2-type 4Add BLAST94
Domaini420 – 514Ig-like C2-type 5Add BLAST95
Domaini592 – 939Protein kinasePROSITE-ProRule annotationAdd BLAST348

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni571 – 573Important for interaction with phosphotyrosine-binding proteinsBy similarity3

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSF-1/PDGF receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000112008.
HOVERGENiHBG004335.
InParanoidiP05532.
KOiK05091.
OMAiYFCPGTE.
TreeFamiTF325768.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
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]
PfamiPF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500951. SCGF_recepter. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. 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]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P05532-1) [UniParc]FASTAAdd to basket
Also known as: GNNK(+), KitA(+)

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.

« Hide

        10         20         30         40         50
MRGARGAWDL LCVLLVLLRG QTATSQPSAS PGEPSPPSIH PAQSELIVEA
60 70 80 90 100
GDTLSLTCID PDFVRWTFKT YFNEMVENKK NEWIQEKAEA TRTGTYTCSN
110 120 130 140 150
SNGLTSSIYV FVRDPAKLFL VGLPLFGKED SDALVRCPLT DPQVSNYSLI
160 170 180 190 200
ECDGKSLPTD LTFVPNPKAG ITIKNVKRAY HRLCVRCAAQ RDGTWLHSDK
210 220 230 240 250
FTLKVRAAIK AIPVVSVPET SHLLKKGDTF TVVCTIKDVS TSVNSMWLKM
260 270 280 290 300
NPQPQHIAQV KHNSWHRGDF NYERQETLTI SSARVDDSGV FMCYANNTFG
310 320 330 340 350
SANVTTTLKV VEKGFINISP VKNTTVFVTD GENVDLVVEY EAYPKPEHQQ
360 370 380 390 400
WIYMNRTSAN KGKDYVKSDN KSNIRYVNQL RLTRLKGTEG GTYTFLVSNS
410 420 430 440 450
DASASVTFNV YVNTKPEILT YDRLINGMLQ CVAEGFPEPT IDWYFCTGAE
460 470 480 490 500
QRCTTPVSPV DVQVQNVSVS PFGKLVVQSS IDSSVFRHNG TVECKASNDV
510 520 530 540 550
GKSSAFFNFA FKGNNKEQIQ AHTLFTPLLI GFVVAAGAMG IIVMVLTYKY
560 570 580 590 600
LQKPMYEVQW KVVEEINGNN YVYIDPTQLP YDHKWEFPRN RLSFGKTLGA
610 620 630 640 650
GAFGKVVEAT AYGLIKSDAA MTVAVKMLKP SAHLTEREAL MSELKVLSYL
660 670 680 690 700
GNHMNIVNLL GACTVGGPTL VITEYCCYGD LLNFLRRKRD SFIFSKQEEQ
710 720 730 740 750
AEAALYKNLL HSTEPSCDSS NEYMDMKPGV SYVVPTKTDK RRSARIDSYI
760 770 780 790 800
ERDVTPAIME DDELALDLDD LLSFSYQVAK GMAFLASKNC IHRDLAARNI
810 820 830 840 850
LLTHGRITKI CDFGLARDIR NDSNYVVKGN ARLPVKWMAP ESIFSCVYTF
860 870 880 890 900
ESDVWSYGIF LWELFSLGSS PYPGMPVDSK FYKMIKEGFR MVSPEHAPAE
910 920 930 940 950
MYDVMKTCWD ADPLKRPTFK QVVQLIEKQI SDSTKHIYSN LANCNPNPEN
960 970
PVVVDHSVRV NSVGSSASST QPLLVHEDA
Length:979
Mass (Da):109,343
Last modified:October 19, 2011 - v3
Checksum:i03FB4D672248585E
GO
Isoform 2 (identifier: P05532-2) [UniParc]FASTAAdd to basket
Also known as: GNNK(-), Kit(+)

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

Show »
Length:975
Mass (Da):108,929
Checksum:i57BFE10AE456C145
GO
Isoform 3 (identifier: P05532-3) [UniParc]FASTAAdd to basket
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.

Show »
Length:202
Mass (Da):22,814
Checksum:i38323E3690025842
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti551L → F in AAH52457 (PubMed:15489334).Curated1
Sequence conflicti781G → A in CAA68772 (PubMed:2456920).Curated1
Sequence conflicti781G → A in CAA46799 (PubMed:1709486).Curated1
Sequence conflicti860F → S in AAS45607 (PubMed:15731517).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti207A → E Loss-of-function mutation abolishing ligand binding. 2 Publications1
Natural varianti586E → K in W37 spotting; impaired protein stability and loss of kinase activity. 2 Publications1
Natural varianti664T → M in Wv spotting. 1 Publication1
Natural varianti794D → N in W42 spotting; loss of kinase activity and impaired internalization after exposure to KITLG/SCF. 2 Publications1
Natural varianti835V → M in W41 spotting; decreased kinase activity. 2 Publications1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0418681 – 12MRGAR…WDLLC → MAVAVFPFLPQQ in isoform 3. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_04186913 – 789Missing in isoform 3. 1 PublicationAdd BLAST777
Alternative sequenceiVSP_041870512 – 515Missing in isoform 2. 3 Publications4

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS51525.1. [P05532-1]
CCDS80302.1. [P05532-2]
PIRiA44876.
S00474. TVMSKT.
S24667.
S34435.
RefSeqiNP_001116205.1. NM_001122733.1. [P05532-1]
NP_066922.2. NM_021099.3. [P05532-2]
UniGeneiMm.247073.

Genome annotation databases

EnsembliENSMUST00000005815; ENSMUSP00000005815; ENSMUSG00000005672. [P05532-1]
ENSMUST00000144270; ENSMUSP00000116465; ENSMUSG00000005672. [P05532-2]
GeneIDi16590.
KEGGimmu:16590.
UCSCiuc008xug.2. mouse. [P05532-1]
uc012dxj.1. mouse. [P05532-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS51525.1. [P05532-1]
CCDS80302.1. [P05532-2]
PIRiA44876.
S00474. TVMSKT.
S24667.
S34435.
RefSeqiNP_001116205.1. NM_001122733.1. [P05532-1]
NP_066922.2. NM_021099.3. [P05532-2]
UniGeneiMm.247073.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2O26X-ray2.50U/W/X/Y25-314[»]
ProteinModelPortaliP05532.
SMRiP05532.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200957. 18 interactors.
DIPiDIP-59622N.
IntActiP05532. 3 interactors.
STRINGi10090.ENSMUSP00000005815.

Chemistry databases

BindingDBiP05532.
ChEMBLiCHEMBL2034798.

PTM databases

iPTMnetiP05532.
PhosphoSitePlusiP05532.

Proteomic databases

MaxQBiP05532.
PaxDbiP05532.
PRIDEiP05532.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000005815; ENSMUSP00000005815; ENSMUSG00000005672. [P05532-1]
ENSMUST00000144270; ENSMUSP00000116465; ENSMUSG00000005672. [P05532-2]
GeneIDi16590.
KEGGimmu:16590.
UCSCiuc008xug.2. mouse. [P05532-1]
uc012dxj.1. mouse. [P05532-2]

Organism-specific databases

CTDi3815.
MGIiMGI:96677. Kit.

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000112008.
HOVERGENiHBG004335.
InParanoidiP05532.
KOiK05091.
OMAiYFCPGTE.
TreeFamiTF325768.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiR-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1433557. Signaling by SCF-KIT.
R-MMU-1433559. Regulation of KIT signaling.
R-MMU-5673001. RAF/MAP kinase cascade.
R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.

Miscellaneous databases

ChiTaRSiKit. mouse.
EvolutionaryTraceiP05532.
PROiP05532.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000005672.
CleanExiMM_KIT.
ExpressionAtlasiP05532. baseline and differential.
GenevisibleiP05532. MM.

Family and domain databases

Gene3Di2.60.40.10. 5 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
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]
PfamiPF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF500951. SCGF_recepter. 1 hit.
PIRSF000615. TyrPK_CSF1-R. 1 hit.
SMARTiSM00409. IG. 4 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 4 hits.
SSF56112. SSF56112. 2 hits.
PROSITEiPS50835. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiKIT_MOUSE
AccessioniPrimary (citable) accession number: P05532
Secondary accession number(s): Q61415
, Q61416, Q61417, Q6LEE9, Q6QJB7, Q6QJB8, Q7TS86, Q8C8K9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 19, 2011
Last modified: November 2, 2016
This is version 186 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.