Gene Ontology annotation through association of InterPro records with GO terms

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Gene Ontology annotation based on curation of immunofluorescence data

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

Identification of Tyr-703 and Tyr-936 as the primary association sites for Grb2 and Grb7 in the c-Kit/stem cell factor receptor.

The receptor protein tyrosine phosphatase, PTP-RO, is upregulated during megakaryocyte differentiation and Is associated with the c-Kit receptor.

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.

Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent phosphorylation site mediating interaction with c-Crk.

Inhibition of SH2 domain/phosphoprotein association by a nonhydrolyzable phosphonopeptide.

Tumor necrosis factor-alpha-converting enzyme controls surface expression of c-Kit and survival of embryonic stem cell-derived mast cells.

Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor.

Mutation of the KIT (mast/stem cell growth factor receptor) protooncogene in human piebaldism.

Activation of the human c-kit product by ligand-induced dimerization mediates circular actin reorganization and chemotaxis.

Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor.

Developmental changes in human fetal testicular cell numbers and messenger ribonucleic acid levels during the second trimester.

Induction of microRNA-221 by platelet-derived growth factor signaling is critical for modulation of vascular smooth muscle phenotype.

CD72 negatively regulates KIT-mediated responses in human mast cells.

Expression of a truncated form of KIT tyrosine kinase in human spermatozoa correlates with sperm DNA integrity.

Tumor-intrinsic and -extrinsic roles of c-Kit: mast cells as the primary off-target of tyrosine kinase inhibitors.

Mechanisms of STAT protein activation by oncogenic KIT mutants in neoplastic mast cells.

Mechanism of activation of human c-KIT kinase by internal tandem duplications of the juxtamembrane domain and point mutations at aspartic acid 816.

Enhanced prediction of Src homology 2 (SH2) domain binding potentials using a fluorescence polarization-derived c-Met, c-Kit, ErbB, and androgen receptor interactome.

Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.

Quantitative fragmentomics allow affinity mapping of interactomes.

The ubiquitously expressed Syp phosphatase interacts with c-kit and Grb2 in hematopoietic cells.

Formation of signal transfer complexes between stem cell and platelet-derived growth factor receptors and SH2 domain proteins in vitro.

Activating and dominant inactivating c-KIT catalytic domain mutations in distinct clinical forms of human mastocytosis.

Phosphorylation of JAK2

PTP-RO interacts with p-c-Kit complex

GRB2 is indirectly recruited to p-KIT through SHP2

JAK2 binds to p-KIT

Phosphorylation of GAB2 by SFKs

Recruitment of STATs

Activation of RAS by p-KIT bound SOS1

Phosphorylation of SHP2 by SFKs

Interaction of other adapter proteins with p-KIT

Phosphorylation of APS

PKC alpha interacts with and phosphorylates KIT

Synthesis of PIP3 from PIP2 by PI3K

Phosphorylation and activation of VAV1

Phosphorylation of STATs

Dimerization of STATs

Disassociation and translocation of STATs to the nucleus

Phosphorylation of p-KIT on Y900 by Src kinases

LNK binds to p-KIT and inhibit downstream signaling

Indirect recruitment of PI3K to KIT via p(Y)-GAB2

Dimerization of KIT upon SCF binding

Indirect recruitment of GAB2 to p-KIT

SHP2 interacts with p-KIT

Recruitment of CBL to KIT

Direct recruitment of PI3K to p-KIT

GRB2:SOS interacts with p-KIT

Autophosphorylation of KIT

Interaction of SHP1 and KIT

Interaction of APS and p-KIT

Interaction of KIT and sSCF

Interaction of other tyrosine kinases with p-KIT

PI3K phosphorylates PIP2 to PIP3

PI3K inhibitors block PI3K catalytic activity

RAS GEFs promote RAS nucleotide exchange

KIT gene expression is stimulated by TFAP2A,(TFAP2B) homodimers

KIT binds type II TKIs

Dasatinib-resistant KIT mutants do not bind dasatinib

Imatinib-resistant KIT mutants do not bind imatinib

Masitinib-resistant KIT mutants do not bind masitinib

Nilotinib-resistant KIT mutants do not bind nilotinib

Regorafenib-resistant KIT mutants do not bind regorafenib

Sorafenib-resistant KIT mutants do not bind sorafenib

Sunitinib-resistant KIT mutants do not bind sunitinib

Constitutive phosphorylation of kinase domain KIT mutants

KIT binds type I TKIs

KIT mutants bind type I TKIs

KIT mutants bind type II TKIs

Ligand-independent dimerization of KIT juxtamembrane domain mutants

Phosphorylation of juxtamembrane domain KIT mutants

Phosphorylation of STATs downstream of KIT mutants

JAK2 binds to p-KIT mutants

KIT mutants bind SFKs

Recruitment of STATs by KIT mutants

Dimerization of STATs downstream of KIT mutants

Phosphorylation of JAK2 downstream of KIT mutants

Disassociation and translocation of STATs to the nucleus downstream of KIT mutants

KIT mutants bind GRB2-SOS

Phosphorylated KIT mutants bind PI3K

KIT mutants:PI3K catalyze synthesis of PIP3

p-KIT mutants:GRB2:SOS catalyzes nucleotide exchange on RAS

Ligand-independent dimerization of KIT extracellular domain mutants

Phosphorylation of extracellular domain KIT mutants

KIT binds ripretinib

KIT mutants bind ripretinib