P10721 (KIT_HUMAN) 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):
Piebald trait protein
Short name=PBT
Proto-oncogene c-Kit
Tyrosine-protein kinase Kit
p145 c-kit
v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog
CD_antigen=CD117

Gene names

Name:	KIT
Synonyms:	SCFR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

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

General annotation (Comments)

Function	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.11 Ref.15 Ref.17 Ref.20 Ref.21 Ref.22 Ref.25 Ref.26 Ref.30 Ref.31
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.1 Ref.30 Ref.39 Ref.40
Enzyme regulation	Present in an inactive conformation in the absence of bound ligand. KITLG/SCF binding leads to dimerization and activation by autophosphorylation on tyrosine residues. Activity is down-regulated by PRKCA-mediated phosphorylation on serine residues. Inhibited by imatinib/STI-571 (Gleevec) and sunitinib; these compounds maintain the kinase in an inactive conformation. Ref.11 Ref.12 Ref.30 Ref.38 Ref.40
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 PIK3R1 and PIK3 catalytic subunit. Interacts (via phosphorylated tyrosine) with CRK (isoform Crk-II), FYN, SHC1 and MATK/CHK (via SH2 domain). Interacts with LYN and FES/FPS. Interacts (via phosphorylated tyrosine residues) with the protein phosphatases PTPN6/SHP-1 (via SH2 domain), PTPN11/SHP-2 (via SH2 domain) and PTPRU. Interacts with PLCG1. Interacts with DOK1 and TEC. Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.24 Ref.25 Ref.30 Ref.37 Ref.39
Subcellular location	Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.1 Ref.5 Ref.26 Ref.28. Isoform 2: Cell membrane; Single-pass type I membrane protein Ref.1 Ref.5 Ref.26 Ref.28. Isoform 3: Cytoplasm. Note: Detected in the cytoplasm of spermatozoa, especially in the equatorial and subacrosomal region of the sperm head. Ref.1 Ref.5 Ref.26 Ref.28
Tissue specificity	Isoform 1 and isoform 2 are detected in spermatogonia and Leydig cells. Isoform 3 is detected in round spermatids, elongating spermatids and spermatozoa (at protein level). Widely expressed. Detected in the hematopoietic system, the gastrointestinal system, in melanocytes and in germ cells. Ref.1 Ref.28
Induction	Up-regulated by cis-retinoic acid in neuroblastoma cell lines. Ref.5 Ref.11 Ref.12 Ref.30 Ref.38 Ref.40
Post-translational modification	Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation. Ref.25 Ref.26 Autophosphorylated on tyrosine residues. KITLG/SCF binding enhances autophosphorylation. Isoform 1 shows low levels of tyrosine phosphorylation in the absence of added KITLG/SCF (in vitro). Kinase activity is down-regulated by phosphorylation on serine residues by protein kinase C family members. Phosphorylation at Tyr-568 is required for interaction with PTPN11/SHP-2, CRK (isoform Crk-II) and members of the SRC tyrosine-protein kinase family. Phosphorylation at Tyr-570 is required for interaction with PTPN6/SHP-1. Phosphorylation at Tyr-703, Tyr-823 and Tyr-936 is important for interaction with GRB2. Phosphorylation at Tyr-721 is important for interaction with PIK3R1. Phosphorylation at Tyr-823 and Tyr-936 is important for interaction with GRB7. Ref.1 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.21 Ref.26 Ref.29 Ref.30 Ref.37 Ref.39 Ref.40 Ref.41
Involvement in disease	Piebald trait (PBT) [MIM:172800]: Autosomal dominant genetic developmental abnormality of pigmentation characterized by congenital patches of white skin and hair that lack melanocytes. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.42 Ref.43 Ref.44 Ref.46 Ref.47 Ref.48 Ref.49 Ref.51 Ref.56 Gastrointestinal stromal tumor (GIST) [MIM:606764]: Common mesenchymal neoplasms arising in the gastrointestinal tract, most often in the stomach. They are histologically, immunohistochemically, and genetically different from typical leiomyomas, leiomyosarcomas, and schwannomas. Most GISTs are composed of a fairly uniform population of spindle-shaped cells. Some tumors are dominated by epithelioid cells or contain a mixture of spindle and epithelioid morphologies. Primary GISTs in the gastrointestinal tract commonly metastasize in the omentum and mesenteries, often as multiple nodules. However, primary tumors may also occur outside of the gastrointestinal tract, in other intra-abdominal locations, especially in the omentum and mesentery. Note: The gene represented in this entry is involved in disease pathogenesis. Ref.48 Ref.52 Ref.53 Ref.57 Ref.58 Testicular germ cell tumor (TGCT) [MIM:273300]: A common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma. Note: The gene represented in this entry may be involved in disease pathogenesis. Ref.48 Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. Note: The gene represented in this entry is involved in disease pathogenesis. Somatic mutations that lead to constitutive activation of KIT are detected in AML patients. These mutations fall into two classes, the most common being in-frame internal tandem duplications of variable length in the juxtamembrane region that disrupt the normal regulation of the kinase activity. Likewise, point mutations in the kinase domain can result in a constitutively activated kinase. Ref.48
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 Polymorphism
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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Fc receptor signaling pathway Inferred from direct assay PubMed 20100931. Source: UniProtKB Kit signaling pathway Inferred from direct assay Ref.39. Source: UniProtKB T cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB actin cytoskeleton reorganization Inferred from direct assay PubMed 1721869. Source: UniProtKB activation of MAPK activity Inferred from direct assay Ref.30. Source: UniProtKB cellular response to thyroid hormone stimulus Inferred from electronic annotation. Source: Compara dendritic cell cytokine production Inferred from sequence or structural similarity. Source: UniProtKB detection of mechanical stimulus involved in sensory perception of sound Inferred from sequence or structural similarity. Source: UniProtKB digestive tract development Inferred from sequence or structural similarity. Source: UniProtKB embryonic hemopoiesis Inferred from sequence or structural similarity. Source: UniProtKB erythrocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB erythropoietin-mediated signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB germ cell programmed cell death Inferred from electronic annotation. Source: Compara glycosphingolipid metabolic process Inferred from electronic annotation. Source: Compara immature B cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB inflammatory response Inferred from sequence or structural similarity. Source: UniProtKB intracellular protein kinase cascade Inferred from electronic annotation. Source: Compara lamellipodium assembly Inferred from sequence or structural similarity. Source: UniProtKB lymphoid progenitor cell differentiation Inferred from electronic annotation. Source: Compara male gonad development Inferred from expression pattern PubMed 17848411. Source: UniProtKB mast cell chemotaxis Inferred from direct assay PubMed 20100931. Source: UniProtKB mast cell cytokine production Inferred from direct assay PubMed 20100931. Source: UniProtKB mast cell degranulation Inferred from mutant phenotype PubMed 20100931. Source: UniProtKB mast cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB mast cell proliferation Traceable author statement Ref.36. Source: UniProtKB megakaryocyte development Inferred from sequence or structural similarity. Source: UniProtKB melanocyte adhesion Inferred from sequence or structural similarity. Source: UniProtKB melanocyte differentiation Inferred from sequence or structural similarity. Source: UniProtKB melanocyte migration Inferred from sequence or structural similarity. Source: UniProtKB myeloid progenitor cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of programmed cell death Inferred from electronic annotation. Source: Compara ovarian follicle development Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.30. Source: UniProtKB positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of gene expression Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase activity Traceable author statement Ref.33. Source: UniProtKB positive regulation of phosphatidylinositol 3-kinase cascade Traceable author statement Ref.33. Source: UniProtKB positive regulation of phospholipase C activity Traceable author statement Ref.33. Source: UniProtKB positive regulation of sequence-specific DNA binding transcription factor activity Inferred from mutant phenotype Ref.31. Source: UniProtKB positive regulation of tyrosine phosphorylation of Stat1 protein Inferred from mutant phenotype Ref.31. Source: UniProtKB positive regulation of tyrosine phosphorylation of Stat3 protein Inferred from mutant phenotype Ref.31. Source: UniProtKB positive regulation of tyrosine phosphorylation of Stat5 protein Inferred from mutant phenotype Ref.31. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.30. Source: UniProtKB regulation of cell proliferation Traceable author statement Ref.33Ref.36. Source: UniProtKB regulation of cell shape Inferred from sequence or structural similarity. Source: UniProtKB regulation of developmental pigmentation Inferred from electronic annotation. Source: Compara response to radiation Inferred from electronic annotation. Source: Compara spermatid development Inferred from electronic annotation. Source: Compara spermatogenesis Inferred from sequence or structural similarity. Source: UniProtKB stem cell maintenance Traceable author statement Ref.36. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA external side of plasma membrane Inferred from electronic annotation. Source: Compara extracellular space Inferred from direct assay PubMed 14625290. Source: BHF-UCL integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay. Source: HPA plasma membrane Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cytokine binding Inferred from direct assay Ref.30. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW receptor signaling protein tyrosine kinase activity Traceable author statement Ref.53. Source: ProtInc stem cell factor receptor activity Inferred from electronic annotation. Source: Compara transmembrane receptor protein tyrosine kinase activity Inferred from direct assay Ref.30. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	2	EBI-1379503,EBI-401755
KITLG	P21583	2	EBI-1379503,EBI-1379527
Ptpn11	P35235	2	EBI-1379503,EBI-397236	From a different organism.

Alternative products

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

Isoform 1 (identifier: P10721-1)

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: P10721-2)

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

The sequence of this isoform differs from the canonical sequence as follows:
     510-513: Missing.

Isoform 3 (identifier: P10721-3)

Also known as: TR-KIT;

The sequence of this isoform differs from the canonical sequence as follows:
     412-413: KP → SL
     414-976: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential

Chain

26 – 976

951

Mast/stem cell growth factor receptor Kit

PRO_0000016754

Regions

Topological domain

26 – 524

499

Extracellular Potential

Transmembrane

525 – 545

21

Helical; Potential

Topological domain

546 – 976

431

Cytoplasmic Potential

Domain

27 – 112

86

Ig-like C2-type 1

Domain

121 – 205

85

Ig-like C2-type 2

Domain

212 – 308

97

Ig-like C2-type 3

Domain

317 – 410

94

Ig-like C2-type 4

Domain

413 – 507

95

Ig-like C2-type 5

Domain

589 – 937

349

Protein kinase

Nucleotide binding

596 – 603

8

ATP

Nucleotide binding

671 – 677

7

ATP

Region

568 – 570

3

Important for interaction with phosphotyrosine-binding proteins

Sites

Active site

792

1

Proton acceptor By similarity

Metal binding

568

1

Magnesium

Metal binding

797

1

Magnesium

Metal binding

810

1

Magnesium

Binding site

623

1

ATP

Binding site

796

1

ATP

Site

936

1

Important for interaction with phosphotyrosine-binding proteins

Amino acid modifications

Modified residue

547

1

Phosphotyrosine; by autocatalysis Probable

Modified residue

553

1

Phosphotyrosine; by autocatalysis Probable

Modified residue

568

1

Phosphotyrosine; by autocatalysis Ref.13 Ref.26 Ref.37 Ref.41

Modified residue

570

1

Phosphotyrosine; by autocatalysis Ref.13 Ref.37

Modified residue

703

1

Phosphotyrosine; by autocatalysis Ref.16 Ref.26 Ref.29

Modified residue

721

1

Phosphotyrosine; by autocatalysis Ref.13 Ref.26 Ref.29

Modified residue

730

1

Phosphotyrosine; by autocatalysis Probable

Modified residue

741

1

Phosphoserine; by PKC/PRKCA Ref.12

Modified residue

746

1

Phosphoserine; by PKC/PRKCA Ref.12

Modified residue

821

1

Phosphoserine Ref.12

Modified residue

823

1

Phosphotyrosine; by autocatalysis Ref.29

Modified residue

891

1

Phosphoserine Ref.21

Modified residue

900

1

Phosphotyrosine; by autocatalysis Ref.21 Ref.29

Modified residue

936

1

Phosphotyrosine; by autocatalysis Ref.16 Ref.26

Modified residue

959

1

Phosphoserine Ref.12 Ref.27

Glycosylation

130

1

N-linked (GlcNAc...) Ref.23 Ref.39

Glycosylation

145

1

N-linked (GlcNAc...) Potential

Glycosylation

283

1

N-linked (GlcNAc...) Ref.39

Glycosylation

293

1

N-linked (GlcNAc...) Ref.39

Glycosylation

300

1

N-linked (GlcNAc...) Ref.39

Glycosylation

320

1

N-linked (GlcNAc...) Ref.39

Glycosylation

352

1

N-linked (GlcNAc...) Ref.39

Glycosylation

367

1

N-linked (GlcNAc...) Ref.39

Glycosylation

463

1

N-linked (GlcNAc...) Potential

Glycosylation

486

1

N-linked (GlcNAc...) Potential

Disulfide bond

58 ↔ 97

Ref.39

Disulfide bond

136 ↔ 186

Ref.39

Disulfide bond

151 ↔ 183

Ref.39

Disulfide bond

233 ↔ 290

Ref.39

Disulfide bond

428 ↔ 491

Ref.39

Natural variations

Alternative sequence

412 – 413

2

KP → SL in isoform 3.

VSP_041866

Alternative sequence

414 – 976

563

Missing in isoform 3.

VSP_041867

Alternative sequence

510 – 513

4

Missing in isoform 2.

VSP_038385

Natural variant

532

1

V → I. Ref.60
Corresponds to variant rs55792975 [ dbSNP | Ensembl ].

VAR_042021

Natural variant

541

1

M → L. Ref.60
Corresponds to variant rs3822214 [ dbSNP | Ensembl ].

VAR_042022

Natural variant

541

1

M → V.
Corresponds to variant rs3822214 [ dbSNP | Ensembl ].

VAR_061289

Natural variant

550 – 558

9

Missing in GIST; somatic mutation.

VAR_033124

Natural variant

550

1

K → I in GIST; somatic mutation. Ref.53
Corresponds to variant rs28933968 [ dbSNP | Ensembl ].

VAR_033123

Natural variant

551 – 555

5

Missing in GIST; somatic mutation.

VAR_033125

Natural variant

559 – 560

2

Missing in GIST; somatic mutation. Ref.52

VAR_033128

Natural variant

559

1

V → A in GIST. Ref.57

VAR_033126

Natural variant

559

1

V → D in GIST; somatic mutation. Ref.53

VAR_033127

Natural variant

559

1

Missing in GIST. Ref.52

VAR_007965

Natural variant

583

1

E → K in PBT. Ref.42

VAR_004104

Natural variant

584

1

F → C in PBT. Ref.56
Corresponds to variant rs28933371 [ dbSNP | Ensembl ].

VAR_033129

Natural variant

584

1

F → L in PBT. Ref.43

VAR_004105

Natural variant

601

1

G → R in PBT. Ref.56

VAR_033130

Natural variant

656

1

L → P in PBT. Ref.56

VAR_033131

Natural variant

664

1

G → R in PBT. Ref.44

VAR_004106

Natural variant

691

1

C → S. Ref.60
Corresponds to variant rs35200131 [ dbSNP | Ensembl ].

VAR_042023

Natural variant

715

1

S → N. Ref.60
Corresponds to variant rs56094246 [ dbSNP | Ensembl ].

VAR_042024

Natural variant

737

1

D → N in a colorectal adenocarcinoma sample; somatic mutation. Ref.60

VAR_042025

Natural variant

791

1

R → G in PBT. Ref.46

VAR_004107

Natural variant

796

1

R → G in PBT; with sensorineural deafness. Ref.49

VAR_033132

Natural variant

804

1

R → W in a colorectal adenocarcinoma sample; somatic mutation. Ref.60

VAR_042026

Natural variant

812

1

G → V in PBT. Ref.46

VAR_004108

Natural variant

816

1

D → F in mastocytosis; requires 2 nucleotide substitutions; somatic mutation; constitutively activated and is much more rapidly autophosphorylated than wild type. Ref.55

VAR_033133

Natural variant

816

1

D → H in a testicular tumor; seminoma; somatic mutation; constitutively activated. Ref.29 Ref.40 Ref.54
Corresponds to variant rs28933969 [ dbSNP | Ensembl ].

VAR_033134

Natural variant

816

1

D → V in mast cell leukemia and mastocytosis; somatic mutation; constitutively activated; loss of interaction with MPDZ. Ref.18 Ref.24 Ref.26 Ref.30 Ref.40 Ref.45 Ref.55

VAR_004109

Natural variant

816

1

D → Y in acute myeloid leukemia, mastocytosis and a germ cell tumor of the testis; somatic mutation; constitutively activated. Ref.50 Ref.55 Ref.59 Ref.60

VAR_023828

Natural variant

820

1

D → G in mast cell disease; systemic. Ref.48

VAR_033135

Natural variant

822

1

N → K in a germ cell tumor of the testis; somatic mutation. Ref.59 Ref.60

VAR_023829

Natural variant

829

1

A → P in a germ cell tumor of the testis; somatic mutation. Ref.59 Ref.60

VAR_023830

Natural variant

839

1

E → K in mastocytosis; somatic mutation; dominant negative mutation; loss of autophosphorylation. Ref.55

VAR_033136

Natural variant

847

1

T → P in PBT. Ref.51

VAR_033137

Natural variant

893 – 896

4

Missing in PBT; severe.

VAR_004110

Experimental info

Mutagenesis

381

1

R → A: Reduces autophosphorylation in response to KITLG/SCF. Ref.39

Mutagenesis

386

1

E → A: Reduces autophosphorylation in response to KITLG/SCF. Ref.39

Mutagenesis

571

1

I → A: Reduction in SH2B2/APS binding. Abolishes SH2B2/APS binding; when associated with A-939. Ref.20

Mutagenesis

623

1

K → M: Stronger interaction with MPDZ. Ref.18

Mutagenesis

741

1

S → A: Abolishes down-regulation of kinase activity by PKC/PRKCA-mediated phosphorylation; when associated with A-746. Ref.12

Mutagenesis

746

1

S → A: Abolishes down-regulation of kinase activity by PKC/PRKCA-mediated phosphorylation; when associated with A-741. Ref.12

Mutagenesis

823

1

Y → F: No decrease in activity. Leads to autophosphorylation at Tyr-900. Ref.29

Mutagenesis

939

1

L → A: Reduction in SH2B2/APS binding. Abolishes SH2B2/APS binding; when associated with A-571. Ref.20

Sequence conflict

764

1

L → I in AAH71593. Ref.9

Sequence conflict

838

1

P → H in AAH71593. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

976

Helix Strand Turn

Details...

Beta strand

38 – 41

4

Beta strand

44 – 47

4

Beta strand

54 – 59

6

Beta strand

63 – 72

10

Beta strand

75 – 77

3

Beta strand

79 – 86

8

Helix

89 – 91

3

Beta strand

93 – 99

7

Beta strand

104 – 110

7

Beta strand

125 – 130

6

Beta strand

132 – 134

3

Beta strand

146 – 149

4

Beta strand

151 – 153

3

Beta strand

161 – 165

5

Turn

166 – 168

3

Beta strand

169 – 174

6

Helix

177 – 179

3

Beta strand

183 – 188

6

Beta strand

193 – 200

8

Beta strand

203 – 205

3

Beta strand

213 – 215

3

Beta strand

219 – 224

6

Beta strand

229 – 239

11

Beta strand

243 – 248

6

Beta strand

258 – 263

6

Beta strand

265 – 267

3

Beta strand

269 – 279

11

Turn

282 – 284

3

Beta strand

286 – 293

8

Beta strand

298 – 310

13

Beta strand

312 – 319

8

Beta strand

321 – 325

5

Beta strand

331 – 341

11

Beta strand

345 – 352

8

Beta strand

356 – 359

4

Beta strand

362 – 364

3

Beta strand

367 – 369

3

Beta strand

372 – 379

8

Helix

384 – 386

3

Beta strand

388 – 395

8

Beta strand

400 – 409

10

Beta strand

411 – 419

9

Beta strand

422 – 424

3

Beta strand

426 – 434

9

Beta strand

437 – 439

3

Beta strand

468 – 470

3

Beta strand

472 – 478

7

Beta strand

492 – 494

3

Beta strand

499 – 501

3

Beta strand

558 – 564

7

Beta strand

567 – 570

4

Turn

573 – 575

3

Helix

580 – 582

3

Helix

586 – 588

3

Beta strand

589 – 597

9

Beta strand

599 – 613

15

Beta strand

617 – 625

9

Helix

631 – 647

17

Beta strand

656 – 660

5

Beta strand

662 – 665

4

Beta strand

667 – 671

5

Helix

678 – 684

7

Turn

685 – 688

4

Helix

766 – 785

20

Beta strand

788 – 790

3

Helix

795 – 797

3

Beta strand

798 – 801

4

Turn

802 – 804

3

Beta strand

805 – 808

4

Helix

812 – 814

3

Helix

817 – 819

3

Beta strand

823 – 825

3

Beta strand

827 – 831

5

Helix

833 – 835

3

Helix

838 – 843

6

Helix

848 – 863

16

Turn

864 – 866

3

Helix

877 – 885

9

Helix

897 – 906

10

Helix

911 – 913

3

Helix

917 – 930

14

Turn

931 – 933

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (GNNK(+)) (Kit(+)) [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 81B0CD76817F3454	FASTA	976	109,865
	10 20 30 40 50 60 MRGARGAWDF LCVLLLLLRV QTGSSQPSVS PGEPSPPSIH PGKSDLIVRV GDEIRLLCTD 70 80 90 100 110 120 PGFVKWTFEI LDETNENKQN EWITEKAEAT NTGKYTCTNK HGLSNSIYVF VRDPAKLFLV 130 140 150 160 170 180 DRSLYGKEDN DTLVRCPLTD PEVTNYSLKG CQGKPLPKDL RFIPDPKAGI MIKSVKRAYH 190 200 210 220 230 240 RLCLHCSVDQ EGKSVLSEKF ILKVRPAFKA VPVVSVSKAS YLLREGEEFT VTCTIKDVSS 250 260 270 280 290 300 SVYSTWKREN SQTKLQEKYN SWHHGDFNYE RQATLTISSA RVNDSGVFMC YANNTFGSAN 310 320 330 340 350 360 VTTTLEVVDK GFINIFPMIN TTVFVNDGEN VDLIVEYEAF PKPEHQQWIY MNRTFTDKWE 370 380 390 400 410 420 DYPKSENESN IRYVSELHLT RLKGTEGGTY TFLVSNSDVN AAIAFNVYVN TKPEILTYDR 430 440 450 460 470 480 LVNGMLQCVA AGFPEPTIDW YFCPGTEQRC SASVLPVDVQ TLNSSGPPFG KLVVQSSIDS 490 500 510 520 530 540 SAFKHNGTVE CKAYNDVGKT SAYFNFAFKG NNKEQIHPHT LFTPLLIGFV IVAGMMCIIV 550 560 570 580 590 600 MILTYKYLQK PMYEVQWKVV EEINGNNYVY IDPTQLPYDH KWEFPRNRLS FGKTLGAGAF 610 620 630 640 650 660 GKVVEATAYG LIKSDAAMTV AVKMLKPSAH LTEREALMSE LKVLSYLGNH MNIVNLLGAC 670 680 690 700 710 720 TIGGPTLVIT EYCCYGDLLN FLRRKRDSFI CSKQEDHAEA ALYKNLLHSK ESSCSDSTNE 730 740 750 760 770 780 YMDMKPGVSY VVPTKADKRR SVRIGSYIER DVTPAIMEDD ELALDLEDLL SFSYQVAKGM 790 800 810 820 830 840 AFLASKNCIH RDLAARNILL THGRITKICD FGLARDIKND SNYVVKGNAR LPVKWMAPES 850 860 870 880 890 900 IFNCVYTFES DVWSYGIFLW ELFSLGSSPY PGMPVDSKFY KMIKEGFRML SPEHAPAEMY 910 920 930 940 950 960 DIMKTCWDAD PLKRPTFKQI VQLIEKQISE STNHIYSNLA NCSPNRQKPV VDHSVRINSV 970 GSTASSSQPL LVHDDV
	Isoform 2 (GNNK(-)) (KitA(+)) [UniParc]. Checksum: D59DEFE9AF761FDA	FASTA	972	109,451
	10 20 30 40 50 60 MRGARGAWDF LCVLLLLLRV QTGSSQPSVS PGEPSPPSIH PGKSDLIVRV GDEIRLLCTD 70 80 90 100 110 120 PGFVKWTFEI LDETNENKQN EWITEKAEAT NTGKYTCTNK HGLSNSIYVF VRDPAKLFLV 130 140 150 160 170 180 DRSLYGKEDN DTLVRCPLTD PEVTNYSLKG CQGKPLPKDL RFIPDPKAGI MIKSVKRAYH 190 200 210 220 230 240 RLCLHCSVDQ EGKSVLSEKF ILKVRPAFKA VPVVSVSKAS YLLREGEEFT VTCTIKDVSS 250 260 270 280 290 300 SVYSTWKREN SQTKLQEKYN SWHHGDFNYE RQATLTISSA RVNDSGVFMC YANNTFGSAN 310 320 330 340 350 360 VTTTLEVVDK GFINIFPMIN TTVFVNDGEN VDLIVEYEAF PKPEHQQWIY MNRTFTDKWE 370 380 390 400 410 420 DYPKSENESN IRYVSELHLT RLKGTEGGTY TFLVSNSDVN AAIAFNVYVN TKPEILTYDR 430 440 450 460 470 480 LVNGMLQCVA AGFPEPTIDW YFCPGTEQRC SASVLPVDVQ TLNSSGPPFG KLVVQSSIDS 490 500 510 520 530 540 SAFKHNGTVE CKAYNDVGKT SAYFNFAFKE QIHPHTLFTP LLIGFVIVAG MMCIIVMILT 550 560 570 580 590 600 YKYLQKPMYE VQWKVVEEIN GNNYVYIDPT QLPYDHKWEF PRNRLSFGKT LGAGAFGKVV 610 620 630 640 650 660 EATAYGLIKS DAAMTVAVKM LKPSAHLTER EALMSELKVL SYLGNHMNIV NLLGACTIGG 670 680 690 700 710 720 PTLVITEYCC YGDLLNFLRR KRDSFICSKQ EDHAEAALYK NLLHSKESSC SDSTNEYMDM 730 740 750 760 770 780 KPGVSYVVPT KADKRRSVRI GSYIERDVTP AIMEDDELAL DLEDLLSFSY QVAKGMAFLA 790 800 810 820 830 840 SKNCIHRDLA ARNILLTHGR ITKICDFGLA RDIKNDSNYV VKGNARLPVK WMAPESIFNC 850 860 870 880 890 900 VYTFESDVWS YGIFLWELFS LGSSPYPGMP VDSKFYKMIK EGFRMLSPEH APAEMYDIMK 910 920 930 940 950 960 TCWDADPLKR PTFKQIVQLI EKQISESTNH IYSNLANCSP NRQKPVVDHS VRINSVGSTA 970 SSSQPLLVHD DV
	Isoform 3 (TR-KIT) [UniParc]. Checksum: 08B327362CEF1B7E	FASTA	413	46,658
	10 20 30 40 50 60 MRGARGAWDF LCVLLLLLRV QTGSSQPSVS PGEPSPPSIH PGKSDLIVRV GDEIRLLCTD 70 80 90 100 110 120 PGFVKWTFEI LDETNENKQN EWITEKAEAT NTGKYTCTNK HGLSNSIYVF VRDPAKLFLV 130 140 150 160 170 180 DRSLYGKEDN DTLVRCPLTD PEVTNYSLKG CQGKPLPKDL RFIPDPKAGI MIKSVKRAYH 190 200 210 220 230 240 RLCLHCSVDQ EGKSVLSEKF ILKVRPAFKA VPVVSVSKAS YLLREGEEFT VTCTIKDVSS 250 260 270 280 290 300 SVYSTWKREN SQTKLQEKYN SWHHGDFNYE RQATLTISSA RVNDSGVFMC YANNTFGSAN 310 320 330 340 350 360 VTTTLEVVDK GFINIFPMIN TTVFVNDGEN VDLIVEYEAF PKPEHQQWIY MNRTFTDKWE 370 380 390 400 410 DYPKSENESN IRYVSELHLT RLKGTEGGTY TFLVSNSDVN AAIAFNVYVN TSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human proto-oncogene c-kit: a new cell surface receptor tyrosine kinase for an unidentified ligand." Yarden Y., Kuang W.-J., Yang-Feng T., Coussens L., Munemitsu S., Dull T.J., Chen E., Schlessinger J., Francke U., Ullrich A. EMBO J. 6:3341-3351(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Fetal brain and Term placenta.
[2]	"Organization and nucleotide sequence of the human KIT (mast/stem cell growth factor receptor) proto-oncogene." Giebel L.B., Strunk K.M., Holmes S.A., Spritz R.A. Oncogene 7:2207-2217(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
[3]	"Sequence analysis of two genomic regions containing the KIT and the FMS receptor tyrosine kinase genes." Andre C., Hampe A., Lachaume P., Martin E., Wang X.P., Manus V., Hu W.X., Galibert F. Genomics 39:216-226(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis." Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M. Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[5]	"Retinoic acid enhances sensitivity of neuroblastoma cells for imatinib mesylate." Neumann I., Foell J.L., Bremer M., Volkmer I., Korholz D., Burdach S., Staege M.S. Pediatr. Blood Cancer 55:464-470(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, INDUCTION.
[6]	"Sequence of KIT mRNA from all-trans retinoic acid treated neuroblastoma cell lines." Staege M.S., Neumann I., Volkmer I. Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Trachea.
[8]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] (ISOFORM 1). Tissue: Brain.
[10]	"Characterization of the promoter region of the human c-kit proto-oncogene." Yamamoto K., Tojo A., Aoki N., Shibuya M. Jpn. J. Cancer Res. 84:1136-1144(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
[11]	"Modulation of Kit/stem cell factor receptor-induced signaling by protein kinase C." Blume-Jensen P., Ronnstrand L., Gout I., Waterfield M.D., Heldin C.H. J. Biol. Chem. 269:21793-21802(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF PIK3R1; RAF1 AND MAPK1, INTERACTION WITH GRB2; PIK3R1 AND PIK3 CATALYTIC SUBUNIT, ENZYME REGULATION, PHOSPHORYLATION.
[12]	"Identification of the major phosphorylation sites for protein kinase C in kit/stem cell factor receptor in vitro and in intact cells." Blume-Jensen P., Wernstedt C., Heldin C.H., Ronnstrand L. J. Biol. Chem. 270:14192-14200(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-741; SER-746; SER-821 AND SER-959, ENZYME REGULATION, PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF SER-741 AND SER-746.
[13]	"Direct association of Csk homologous kinase (CHK) with the diphosphorylated site Tyr568/570 of the activated c-KIT in megakaryocytes." Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H. J. Biol. Chem. 272:5915-5920(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIK3R1; MATK/CHK; FYN AND SHC1, PHOSPHORYLATION AT TYR-568; TYR-570 AND TYR-721.
[14]	"Lyn associates with the juxtamembrane region of c-Kit and is activated by stem cell factor in hematopoietic cell lines and normal progenitor cells." Linnekin D., DeBerry C.S., Mou S. J. Biol. Chem. 272:27450-27455(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LYN.
[15]	"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, AUTOPHOSPHORYLATION, FUNCTION IN PHOSPHORYLATION OF PTPN6.
[16]	"Identification of Tyr-703 and Tyr-936 as the primary association sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor." Thommes K., Lennartsson J., Carlberg M., Ronnstrand L. Biochem. J. 341:211-216(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB2 AND GRB7, PARTIAL PROTEIN SEQUENCE, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-703 AND TYR-936.
[17]	"The receptor protein tyrosine phosphatase, PTP-RO, is upregulated during megakaryocyte differentiation and is associated with the c-Kit receptor." Taniguchi Y., London R., Schinkmann K., Jiang S., Avraham H. Blood 94:539-549(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTPRU, FUNCTION IN PHOSPHORYLATION OF PTPRU.
[18]	"The direct association of the multiple PDZ domain containing proteins (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine kinase activity." Mancini A., Koch A., Stefan M., Niemann H., Tamura T. FEBS Lett. 482:54-58(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MPDZ, CHARACTERIZATION OF VARIANT VAL-816, MUTAGENESIS OF LYS-623.
[19]	"Phosphatidylinositol 3-kinase and Src family kinases are required for phosphorylation and membrane recruitment of Dok-1 in c-Kit signaling." Liang X., Wisniewski D., Strife A., Shivakrupa R., Clarkson B., Resh M.D. J. Biol. Chem. 277:13732-13738(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LYN; TEC AND DOK1.
[20]	"The adapter protein APS associates with the multifunctional docking sites Tyr-568 and Tyr-936 in c-Kit." Wollberg P., Lennartsson J., Gottfridsson E., Yoshimura A., Ronnstrand L. Biochem. J. 370:1033-1038(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SH2B2/APS, FUNCTION IN PHOSPHORYLATION OF SH2B2/APS, MUTAGENESIS OF ILE-571 AND LEU-939.
[21]	"Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent phosphorylation site mediating interaction with c-Crk." Lennartsson J., Wernstedt C., Engstrom U., Hellman U., Ronnstrand L. Exp. Cell Res. 288:110-118(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-891 AND TYR-900, PARTIAL PROTEIN SEQUENCE, INTERACTION WITH CRK AND PIK3R1, FUNCTION IN PHOSPHORYLATION OF CRK; AKT1 AND MAP KINASES, MASS SPECTROMETRY.
[22]	"Src family kinases are involved in the differential signaling from two splice forms of c-Kit." Voytyuk O., Lennartsson J., Mogi A., Caruana G., Courtneidge S., Ashman L.K., Ronnstrand L. J. Biol. Chem. 278:9159-9166(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ALTERNATIVE SPLICING.
[23]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130, MASS SPECTROMETRY. Tissue: Plasma.
[24]	"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, CHARACTERIZATION OF VARIANT VAL-816.
[25]	"Grb2 mediates negative regulation of stem cell factor receptor/c-Kit signaling by recruitment of Cbl." Sun J., Pedersen M., Bengtsson S., Ronnstrand L. Exp. Cell Res. 313:3935-3942(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GRB2 AND CBL, UBIQUITINATION, FUNCTION IN PHOSPHORYLATION OF CBL.
[26]	"The D816V mutation of c-Kit circumvents a requirement for Src family kinases in c-Kit signal transduction." Sun J., Pedersen M., Ronnstrand L. J. Biol. Chem. 284:11039-11047(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ACTIVATION OF SIGNALING PATHWAYS AND CELL SURVIVAL, FUNCTION IN PHOSPHORYLATION OF CBL, PHOSPHORYLATION AT TYR-568; TYR-703; TYR-721 AND TYR-936, UBIQUITINATION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT VAL-816.
[27]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-959, MASS SPECTROMETRY.
[28]	"Expression of a truncated form of KIT tyrosine kinase in human spermatozoa correlates with sperm DNA integrity." Muciaccia B., Sette C., Paronetto M.P., Barchi M., Pensini S., D'Agostino A., Gandini L., Geremia R., Stefanini M., Rossi P. Hum. Reprod. 25:2188-2202(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[29]	"Function of activation loop tyrosine phosphorylation in the mechanism of c-Kit auto-activation and its implication in sunitinib resistance." DiNitto J.P., Deshmukh G.D., Zhang Y., Jacques S.L., Coli R., Worrall J.W., Diehl W., English J.M., Wu J.C. J. Biochem. 147:601-609(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-547; TYR-553; TYR-703; TYR-721; TYR-730; TYR-823 AND TYR-900, MASS SPECTROMETRY, MUTAGENESIS OF TYR-823, CHARACTERIZATION OF VARIANT HIS-816.
[30]	"Mechanism of activation of human c-KIT kinase by internal tandem duplications of the juxtamembrane domain and point mutations at aspartic acid 816." Kim S.Y., Kang J.J., Lee H.H., Kang J.J., Kim B., Kim C.G., Park T.K., Kang H. Biochem. Biophys. Res. Commun. 410:224-228(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, SUBUNIT, CHARACTERIZATION OF VARIANT VAL-816.
[31]	"Mechanisms of STAT protein activation by oncogenic KIT mutants in neoplastic mast cells." Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P. J. Biol. Chem. 286:5956-5966(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ACTIVATION AND PHOSPHORYLATION OF STAT1; STAT3; STAT5A AND STAT5B.
[32]	"Signal transduction via the stem cell factor receptor/c-Kit." Ronnstrand L. Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[33]	"Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor." Roskoski R. Jr. Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON KIT SIGNALING.
[34]	"Normal and oncogenic forms of the receptor tyrosine kinase kit." Lennartsson J., Jelacic T., Linnekin D., Shivakrupa R. Stem Cells 23:16-43(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[35]	"Regulation of hematopoietic stem cells by the steel factor/KIT signaling pathway." Kent D., Copley M., Benz C., Dykstra B., Bowie M., Eaves C. Clin. Cancer Res. 14:1926-1930(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[36]	"Tumor-intrinsic and -extrinsic roles of c-Kit: mast cells as the primary off-target of tyrosine kinase inhibitors." Pittoni P., Piconese S., Tripodo C., Colombo M.P. Oncogene 30:757-769(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[37]	"Structure of a c-kit product complex reveals the basis for kinase transactivation." Mol C.D., Lim K.B., Sridhar V., Zou H., Chien E.Y., Sang B.C., Nowakowski J., Kassel D.B., Cronin C.N., McRee D.E. J. Biol. Chem. 278:31461-31464(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 549-931 IN COMPLEX WITH ADP AND MAGNESIUM IONS, SUBUNIT, AUTOPHOSPHORYLATION AT TYR-568 AND TYR-570, MASS SPECTROMETRY.
[38]	"Structural basis for the autoinhibition and STI-571 inhibition of c-Kit tyrosine kinase." Mol C.D., Dougan D.R., Schneider T.R., Skene R.J., Kraus M.L., Scheibe D.N., Snell G.P., Zou H., Sang B.C., Wilson K.P. J. Biol. Chem. 279:31655-31663(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 565-935 IN COMPLEXES WITH INHIBITOR IMATINIB AND PHOSPHATE, ENZYME REGULATION.
[39]	"Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor." Yuzawa S., Opatowsky Y., Zhang Z., Mandiyan V., Lax I., Schlessinger J. Cell 130:323-334(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-519 IN COMPLEX WITH KITLG/SCF, INTERACTION WITH KITLG/SCF, SUBUNIT, DISULFIDE BONDS, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF ARG-381 AND GLU-386, GLYCOSYLATION AT ASN-130; ASN-283; ASN-293; ASN-300; ASN-320; ASN-352 AND ASN-367.
[40]	"KIT kinase mutants show unique mechanisms of drug resistance to imatinib and sunitinib in gastrointestinal stromal tumor patients." Gajiwala K.S., Wu J.C., Christensen J., Deshmukh G.D., Diehl W., DiNitto J.P., English J.M., Greig M.J., He Y.A., Jacques S.L., Lunney E.A., McTigue M., Molina D., Quenzer T., Wells P.A., Yu X., Zhang Y., Zou A. , Emmett M.R., Marshall A.G., Zhang H.M., Demetri G.D. Proc. Natl. Acad. Sci. U.S.A. 106:1542-1547(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 544-935 IN COMPLEX WITH SUNITINIB, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, CHARACTERIZATION OF VARIANTS HIS-816 AND VAL-816, ENZYME REGULATION.
[41]	"Structural basis for c-KIT inhibition by the suppressor of cytokine signaling 6 (SOCS6) ubiquitin ligase." Zadjali F., Pike A.C., Vesterlund M., Sun J., Wu C., Li S.S., Ronnstrand L., Knapp S., Bullock A.N., Flores-Morales A. J. Biol. Chem. 286:480-490(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 564-574 IN COMPLEX WITH SOCS6, PHOSPHORYLATION AT TYR-568.
[42]	"Human piebald trait resulting from a dominant negative mutant allele of the c-kit membrane receptor gene." Fleischman R.A. J. Clin. Invest. 89:1713-1717(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PBT LYS-583.
[43]	"Dominant negative and loss of function mutations of the c-kit (mast/stem cell growth factor receptor) proto-oncogene in human piebaldism." Spritz R.A., Giebel L.B., Holmes S.A. Am. J. Hum. Genet. 50:261-269(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PBT LEU-584.
[44]	"Mutation of the KIT (mast/stem cell growth factor receptor) protooncogene in human piebaldism." Giebel L.B., Spritz R.A. Proc. Natl. Acad. Sci. U.S.A. 88:8696-8699(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PBT ARG-664.
[45]	"Identification of mutations in the coding sequence of the proto-oncogene c-kit in a human mast cell leukemia cell line causing ligand-independent activation of c-kit product." Furitsu T., Tsujimura T., Tono T., Ikeda H., Kitayama H., Koshimizu U., Sugahara H., Butterfield J.H., Ashman L.K., Kanayama Y., Matsuzawa Y., Kitamura Y., Kanakura Y. J. Clin. Invest. 92:1736-1744(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MAST CELL LEUKEMIA VAL-816.
[46]	"Novel mutations of the KIT (mast/stem cell growth factor receptor) proto-oncogene in human piebaldism." Spritz R.A., Holmes S.A., Itin P., Kuester W. J. Invest. Dermatol. 101:22-25(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PBT GLY-791 AND VAL-812.
[47]	"A 12-bp deletion (7818del12) in the c-kit protooncogene in a large Italian kindred with piebaldism." Riva P., Milani N., Gandolfi P., Larizza L. Hum. Mutat. 6:343-345(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PBT 893-GLU--PRO-896 DEL.
[48]	"A new c-kit mutation in a case of aggressive mast cell disease." Pignon J.-M., Giraudier S., Duquesnoy P., Jouault H., Imbert M., Vainchenker W., Vernant J.-P., Tulliez M. Br. J. Haematol. 96:374-376(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MAST CELL DISEASE GLY-820.
[49]	"Piebaldism with deafness: molecular evidence for an expanded syndrome." Spritz R.A., Beighton P. Am. J. Med. Genet. 75:101-103(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PBT GLY-796.
[50]	"c-kit activating mutations and mast cell proliferation in human leukemia." Beghini A., Larizza L., Cairoli R., Morra E. Blood 92:701-702(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ACUTE MYELOID LEUKEMIA TYR-816.
[51]	"A novel KIT gene missense mutation in a Japanese family with piebaldism." Nomura K., Hatayama I., Narita T., Kaneko T., Shiraishi M. J. Invest. Dermatol. 111:337-338(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PBT PRO-847.
[52]	"Familial gastrointestinal stromal tumours with germline mutation of the KIT gene." Nishida T., Hirota S., Taniguchi M., Hashimoto K., Isozaki K., Nakamura H., Kanakura Y., Tanaka T., Takabayashi A., Matsuda H., Kitamura Y. Nat. Genet. 19:323-324(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GIST VAL-559 DEL.
[53]	"Gain-of-function mutations of c-kit in human gastrointestinal stromal tumors." Hirota S., Isozaki K., Moriyama Y., Hashimoto K., Nishida T., Ishiguro S., Kawano K., Hanada M., Kurata A., Takeda M., Muhammad Tunio G., Matsuzawa Y., Kanakura Y., Shinomura Y., Kitamura Y. Science 279:577-580(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS GIST ILE-550; 550-LYS--LYS-558 DEL; 551-PRO--VAL-555 DEL; ASP-559 AND 559-VAL-VAL-560 DEL.
[54]	"Activating c-kit gene mutations in human germ cell tumors." Tian Q., Frierson H.F. Jr., Krystal G.W., Moskaluk C.A. Am. J. Pathol. 154:1643-1647(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HIS-816, CHARACTERIZATION OF VARIANT HIS-816.
[55]	"Activating and dominant inactivating c-KIT catalytic domain mutations in distinct clinical forms of human mastocytosis." Longley B.J. Jr., Metcalfe D.D., Tharp M., Wang X., Tyrrell L., Lu S.-Z., Heitjan D., Ma Y. Proc. Natl. Acad. Sci. U.S.A. 96:1609-1614(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MASTOCYTOSIS VAL-816; PHE-816; TYR-816 AND LYS-839, CHARACTERIZATION OF VARIANTS MASTOCYTOSIS VAL-816; PHE-816; TYR-816 AND LYS-839.
[56]	"Three novel mutations of the proto-oncogene KIT cause human piebaldism." Syrris P., Malik N.M., Murday V.A., Patton M.A., Carter N.D., Hughes H.E., Metcalfe K. Am. J. Med. Genet. 95:79-81(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PBT CYS-584; ARG-601 AND PRO-656.
[57]	"Germline mutation in the juxtamembrane domain of the kit gene in a family with gastrointestinal stromal tumors and urticaria pigmentosa." Beghini A., Tibiletti M.G., Roversi G., Chiaravalli A.M., Serio G., Capella C., Larizza L. Cancer 92:657-662(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GIST ALA-559.
[58]	"A mutation-created novel intra-exonic pre-mRNA splice site causes constitutive activation of KIT in human gastrointestinal stromal tumors." Chen L.L., Sabripour M., Wu E.F., Prieto V.G., Fuller G.N., Frazier M.L. Oncogene 24:4271-4280(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GIST 550-LYS--LYS-558 DEL.
[59]	"Sequence analysis of the protein kinase gene family in human testicular germ-cell tumors of adolescents and adults." Bignell G., Smith R., Hunter C., Stephens P., Davies H., Greenman C., Teague J., Butler A., Edkins S., Stevens C., O'meara S., Parker A., Avis T., Barthorpe S., Brackenbury L., Buck G., Clements J., Cole J. , Dicks E., Edwards K., Forbes S., Gorton M., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jones D., Kosmidou V., Laman R., Lugg R., Menzies A., Perry J., Petty R., Raine K., Shepherd R., Small A., Solomon H., Stephens Y., Tofts C., Varian J., Webb A., West S., Widaa S., Yates A., Gillis A.J.M., Stoop H.J., van Gurp R.J.H.L.M., Oosterhuis J.W., Looijenga L.H.J., Futreal P.A., Wooster R., Stratton M.R. Genes Chromosomes Cancer 45:42-46(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TYR-816; LYS-822 AND PRO-829.
[60]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-532; LEU-541; SER-691; ASN-715; ASN-737; TRP-804; TYR-816; LYS-822 AND PRO-829.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Wikipedia

CD117 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X06182 mRNA. Translation: CAA29548.1.
X69301 , X69302, X69303, X69304, X69305, X69306, X69307, X69308, X69309, X69310, X69311, X69312, X69313, X69314, X69315, X69316 Genomic DNA. Translation: CAA49159.1.
U63834 Genomic DNA. Translation: AAC50968.1.
U63834 Genomic DNA. Translation: AAC50969.1.
EU826594 mRNA. Translation: ACF47630.1.
GU983671 mRNA. Translation: ADF36702.1.
HM015525 mRNA. Translation: ADF50068.1.
HM015526 mRNA. Translation: ADF50069.1.
AK304031 mRNA. Translation: BAG64945.1.
AC006552 Genomic DNA. No translation available.
AC092545 Genomic DNA. No translation available.
BC071593 mRNA. Translation: AAH71593.1.
S67773 Genomic DNA. Translation: AAB29529.1.

IPI

IPI00022296.
IPI00848233.

PIR

TVHUKT. S01426.

RefSeq

NP_000213.1. NM_000222.2.
NP_001087241.1. NM_001093772.1.

UniGene

Hs.479754.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P10721.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1055N.

IntAct

P10721. 4 interactions.

STRING

9606.ENSP00000288135.

PTM databases

PhosphoSite

P10721.

Polymorphism databases

DMDM

125472.

Proteomic databases

PaxDb

P10721.

PRIDE

P10721.

Protocols and materials databases

DNASU

3815.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000288135; ENSP00000288135; ENSG00000157404.
ENST00000412167; ENSP00000390987; ENSG00000157404.

GeneID

3815.

KEGG

hsa:3815.

UCSC

uc010igr.3. human.

Organism-specific databases

CTD

3815.

GeneCards

GC04P055524.

HGNC

HGNC:6342. KIT.

HPA

CAB003288.
HPA004471.

MIM

164920. gene.
172800. phenotype.
273300. phenotype.
601626. phenotype.
606764. phenotype.

neXtProt

NX_P10721.

Orphanet

98850. Aggressive systemic mastocytosis.
79455. Cutaneous mastocytoma.
79456. Diffuse cutaneous mastocytosis.
44890. Gastrointestinal stromal tumor.
98848. Indolent systemic mastocytosis.
98851. Mast cell leukemia.
2884. Piebaldism.
98849. Systemic mastocytosis with an associated clonal hematologic non-mast cell lineage disease.
79457. Urticaria pigmentosa.

PharmGKB

PA30128.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000112008.

HOVERGEN

HBG104348.

InParanoid

P10721.

KO

K05091.

OMA

DSGVFMC.

OrthoDB

EOG4W0XCD.

PhylomeDB

P10721.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Pathway_Interaction_DB

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

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P10721.

Bgee

P10721.

CleanEx

HS_KIT.

Genevestigator

P10721.

GermOnline

ENSG00000157404. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 5 hits.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
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

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

PIRSF

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

SMART

SM00409. IG. 1 hit.
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

BindingDB

P10721.

ChEMBL

CHEMBL1936.

DrugBank

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

EvolutionaryTrace

P10721.

GenomeRNAi

3815.

NextBio

14995.

SOURCE

Search...

Entry information

Entry name

KIT_HUMAN

Accession

Primary (citable) accession number: P10721
Secondary accession number(s): B5A956 , D5LXN2, D5M931, F5H8F8, Q6IQ28, Q99662, Q9UM99

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	May 1, 2013
This is version 166 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.