| IED ID | IndEnz0002015883 |
| Enzyme Type ID | protease015883 |
| Protein Name |
Mast/stem cell growth factor receptor Kit SCFR EC 2.7.10.1 Piebald trait protein 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 Name | KIT SCFR |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MRGARGAWDFLCVLLLLLRVQTGSSQPSVSPGEPSPPSIHPGKSDLIVRVGDEIRLLCTDPGFVKWTFEILDETNENKQNEWITEKAEATNTGKYTCTNKHGLSNSIYVFVRDPAKLFLVDRSLYGKEDNDTLVRCPLTDPEVTNYSLKGCQGKPLPKDLRFIPDPKAGIMIKSVKRAYHRLCLHCSVDQEGKSVLSEKFILKVRPAFKAVPVVSVSKASYLLREGEEFTVTCTIKDVSSSVYSTWKRENSQTKLQEKYNSWHHGDFNYERQATLTISSARVNDSGVFMCYANNTFGSANVTTTLEVVDKGFINIFPMINTTVFVNDGENVDLIVEYEAFPKPEHQQWIYMNRTFTDKWEDYPKSENESNIRYVSELHLTRLKGTEGGTYTFLVSNSDVNAAIAFNVYVNTKPEILTYDRLVNGMLQCVAAGFPEPTIDWYFCPGTEQRCSASVLPVDVQTLNSSGPPFGKLVVQSSIDSSAFKHNGTVECKAYNDVGKTSAYFNFAFKGNNKEQIHPHTLFTPLLIGFVIVAGMMCIIVMILTYKYLQKPMYEVQWKVVEEINGNNYVYIDPTQLPYDHKWEFPRNRLSFGKTLGAGAFGKVVEATAYGLIKSDAAMTVAVKMLKPSAHLTEREALMSELKVLSYLGNHMNIVNLLGACTIGGPTLVITEYCCYGDLLNFLRRKRDSFICSKQEDHAEAALYKNLLHSKESSCSDSTNEYMDMKPGVSYVVPTKADKRRSVRIGSYIERDVTPAIMEDDELALDLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIKNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGIFLWELFSLGSSPYPGMPVDSKFYKMIKEGFRMLSPEHAPAEMYDIMKTCWDADPLKRPTFKQIVQLIEKQISESTNHIYSNLANCSPNRQKPVVDHSVRINSVGSTASSSQPLLVHDDV |
| Enzyme Length | 976 |
| Uniprot Accession Number | P10721 |
| Absorption | |
| Active Site | ACT_SITE 792; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028" |
| Activity Regulation | ACTIVITY 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. {ECO:0000269|PubMed:15123710, ECO:0000269|PubMed:19164557, ECO:0000269|PubMed:21640708, ECO:0000269|PubMed:7520444, ECO:0000269|PubMed:7539802}. |
| Binding Site | BINDING 623; /note=ATP; BINDING 796; /note=ATP |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:17662946, ECO:0000269|PubMed:19164557, ECO:0000269|PubMed:21640708, ECO:0000269|PubMed:2448137}; |
| DNA Binding | |
| EC Number | 2.7.10.1 |
| Enzyme Function | 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. {ECO:0000269|PubMed:10397721, ECO:0000269|PubMed:12444928, ECO:0000269|PubMed:12511554, ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:17904548, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:21640708, ECO:0000269|PubMed:7520444, ECO:0000269|PubMed:9528781}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 596..603; /note=ATP; NP_BIND 671..677; /note=ATP |
| Features | Active site (1); Alternative sequence (2); Beta strand (61); Binding site (2); Chain (1); Disulfide bond (5); Domain (6); Glycosylation (10); Helix (23); Metal binding (3); Modified residue (15); Mutagenesis (8); Natural variant (37); Nucleotide binding (2); Region (1); Sequence caution (1); Sequence conflict (2); Signal peptide (1); Site (1); Topological domain (2); Transmembrane (1); Turn (7) |
| Keywords | 3D-structure;ATP-binding;Alternative splicing;Cell membrane;Cytoplasm;Direct protein sequencing;Disease variant;Disulfide bond;Glycoprotein;Immunoglobulin domain;Kinase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Phosphoprotein;Proto-oncogene;Receptor;Reference proteome;Repeat;Signal;Transferase;Transmembrane;Transmembrane helix;Tyrosine-protein kinase;Ubl conjugation |
| Interact With | P00519; P42684; O75815; P51451; Q8WV28; P46108; P07332; P09769; O75791; P62993; Q14451; P08631; Q96JZ2; P21583; P06239; P07948; P16333; O43639; P27986; O00459; Q92569; P19174; P16885; Q13882; Q06124; Q92729; P20936; Q9UQQ2; O14796; Q9NP31; Q8N5H7; P78314; Q15464; P29353; P98077; Q92529; Q9H6Q3; O14508; O14543; O14544; P12931; Q9ULZ2; Q9HBL0; Q63HR2; Q68CZ2; P42681; P07947; P43403; Q8VBX6; P35235 |
| Induction | INDUCTION: Up-regulated by cis-retinoic acid in neuroblastoma cell lines. {ECO:0000269|PubMed:20658618}. |
| Subcellular Location | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:20601678}. Note=Detected in the cytoplasm of spermatozoa, especially in the equatorial and subacrosomal region of the sperm head. {ECO:0000269|PubMed:20601678}. |
| Modified Residue | MOD_RES 547; /note="Phosphotyrosine; by autocatalysis"; /evidence="ECO:0000305|PubMed:20147452"; MOD_RES 553; /note="Phosphotyrosine; by autocatalysis"; /evidence="ECO:0000305|PubMed:20147452"; MOD_RES 568; /note="Phosphotyrosine; by autocatalysis"; /evidence="ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:21030588, ECO:0000269|PubMed:9038210"; MOD_RES 570; /note="Phosphotyrosine; by autocatalysis"; /evidence="ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:9038210"; MOD_RES 703; /note="Phosphotyrosine; by autocatalysis"; /evidence="ECO:0000269|PubMed:10377264, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:20147452"; MOD_RES 721; /note="Phosphotyrosine; by autocatalysis"; /evidence="ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:20147452, ECO:0000269|PubMed:9038210"; MOD_RES 730; /note="Phosphotyrosine; by autocatalysis"; /evidence="ECO:0000305|PubMed:20147452"; MOD_RES 741; /note="Phosphoserine; by PKC/PRKCA"; /evidence="ECO:0000269|PubMed:7539802"; MOD_RES 746; /note="Phosphoserine; by PKC/PRKCA"; /evidence="ECO:0000269|PubMed:7539802"; MOD_RES 821; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:7539802"; MOD_RES 823; /note="Phosphotyrosine; by autocatalysis"; /evidence="ECO:0000269|PubMed:20147452"; MOD_RES 891; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:12878163"; MOD_RES 900; /note="Phosphotyrosine; by autocatalysis"; /evidence="ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:20147452"; MOD_RES 936; /note="Phosphotyrosine; by autocatalysis"; /evidence="ECO:0000269|PubMed:10377264, ECO:0000269|PubMed:19265199"; MOD_RES 959; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:7539802, ECO:0007744|PubMed:19369195" |
| Post Translational Modification | PTM: Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation. {ECO:0000269|PubMed:17904548, ECO:0000269|PubMed:19265199}.; PTM: 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. {ECO:0000269|PubMed:10377264, ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:20147452, ECO:0000269|PubMed:21030588, ECO:0000269|PubMed:9038210}. |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | X-ray crystallography (26) |
| Cross Reference PDB | 1PKG; 1T45; 1T46; 2E9W; 2EC8; 2IUH; 2VIF; 3G0E; 3G0F; 4HVS; 4K94; 4K9E; 4PGZ; 4U0I; 6GQJ; 6GQK; 6GQL; 6GQM; 6HH1; 6ITT; 6ITV; 6KLA; 6MOB; 6XV9; 6XVA; 6XVB; |
| Mapped Pubmed ID | 10022833; 10224103; 10358045; 10374881; 10523831; 10523834; 10679268; 10884405; 11369651; 11395417; 11435302; 11494148; 11520784; 11642722; 11707405; 11786393; 11809791; 11861291; 11919394; 11994499; 12008077; 12041664; 12072198; 12091362; 12111653; 12134042; 12172985; 12181401; 12192036; 12204004; 12379771; 12393703; 12429808; 12457234; 12475982; 12481435; 12485499; 12522257; 12584564; 12592353; 12598308; 12614164; 12660731; 12666065; 12697809; 12701114; 12711118; 12759497; 12824871; 12824925; 12918066; 1371879; 1375232; 1381360; 1382595; 14625290; 14634801; 14647465; 14654075; 14657715; 14669790; 14677065; 14695343; 14707129; 14724587; 14745431; 14871970; 14994370; 15007386; 15010069; 15018431; 15024050; 15033665; 15044924; 15062876; 15073597; 15073598; 15112348; 15143187; 15154005; 15161681; 15167915; 15194144; 15217946; 15224284; 15234225; 15308671; 15315962; 15326474; 15337769; 15339674; 15342366; 15363456; 15363457; 15370139; 15471556; 15502806; 15507672; 15507676; 15512818; 15583854; 15617841; 15618474; 15618926; 15621809; 15623596; 15650049; 15671569; 15685537; 15688149; 15780567; 15790786; 15791568; 15791570; 15795882; 15834429; 15869870; 15897742; 15972446; 15991300; 16015387; 16029447; 16076867; 16081693; 16082245; 16135486; 16143141; 16188233; 16189265; 16213582; 16220461; 16235251; 16242000; 16271084; 16320053; 16352739; 16357008; 16365291; 16373716; 16373964; 16397263; 16426921; 16445822; 16460801; 16483568; 16533529; 16551858; 16570044; 16597595; 16623778; 16647110; 16685437; 16697720; 16707477; 16737840; 16740725; 16741248; 16751810; 16760463; 16773696; 16780420; 16783341; 16784237; 16785193; 16786129; 16830365; 16840725; 16842246; 16873377; 16905672; 16908864; 16928224; 17018686; 17024483; 17060458; 17065430; 17072721; 17119051; 17156394; 17193819; 17193822; 17213284; 1721591; 17255936; 17289809; 17298867; 17337216; 17363509; 17367465; 17372901; 17438095; 17448763; 17452978; 17487504; 17487541; 17495964; 17519280; 17525721; 17526803; 17532173; 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| Motif | |
| Gene Encoded By | |
| Mass | 109,865 |
| Kinetics | |
| Metal Binding | METAL 568; /note=Magnesium; METAL 797; /note=Magnesium; METAL 810; /note=Magnesium |
| Rhea ID | RHEA:10596 |
| Cross Reference Brenda | 2.7.10.1; |