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O97799

- KIT_CANFA

UniProt

O97799 - KIT_CANFA

Protein

Mast/stem cell growth factor receptor Kit

Gene

KIT

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (05 Sep 2006)
      Previous versions | rss
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    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 By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi571 – 5711MagnesiumBy similarity
    Sitei571 – 5711Interaction with SH2B2/APSBy similarity
    Binding sitei626 – 6261ATPPROSITE-ProRule annotation
    Active sitei795 – 7951Proton acceptorPROSITE-ProRule annotation
    Binding sitei799 – 7991ATPPROSITE-ProRule annotation
    Metal bindingi800 – 8001MagnesiumBy similarity
    Metal bindingi813 – 8131MagnesiumBy similarity
    Sitei939 – 9391Important for interaction with phosphotyrosine-binding proteinsBy similarity
    Sitei939 – 9391Interaction with SH2B2/APSBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi599 – 6068ATPPROSITE-ProRule annotation
    Nucleotide bindingi674 – 6807ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cytokine binding Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. receptor signaling protein tyrosine kinase activity Source: InterPro
    5. stem cell factor receptor activity Source: Ensembl
    6. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. activation of MAPK activity Source: UniProtKB
    3. cell chemotaxis Source: UniProtKB
    4. cellular response to thyroid hormone stimulus Source: Ensembl
    5. cytokine-mediated signaling pathway Source: UniProtKB
    6. dendritic cell cytokine production Source: UniProtKB
    7. detection of mechanical stimulus involved in sensory perception of sound Source: UniProtKB
    8. digestive tract development Source: UniProtKB
    9. ectopic germ cell programmed cell death Source: Ensembl
    10. embryonic hemopoiesis Source: UniProtKB
    11. erythrocyte differentiation Source: UniProtKB
    12. erythropoietin-mediated signaling pathway Source: UniProtKB
    13. Fc receptor signaling pathway Source: UniProtKB
    14. glycosphingolipid metabolic process Source: Ensembl
    15. immature B cell differentiation Source: UniProtKB
    16. inflammatory response Source: UniProtKB
    17. Kit signaling pathway Source: UniProtKB
    18. lamellipodium assembly Source: UniProtKB
    19. lymphoid progenitor cell differentiation Source: Ensembl
    20. male gonad development Source: Ensembl
    21. mast cell chemotaxis Source: Ensembl
    22. mast cell cytokine production Source: UniProtKB
    23. mast cell degranulation Source: UniProtKB
    24. mast cell differentiation Source: UniProtKB
    25. megakaryocyte development Source: UniProtKB
    26. melanocyte adhesion Source: UniProtKB
    27. melanocyte differentiation Source: UniProtKB
    28. melanocyte migration Source: UniProtKB
    29. myeloid progenitor cell differentiation Source: Ensembl
    30. negative regulation of programmed cell death Source: Ensembl
    31. ovarian follicle development Source: UniProtKB
    32. peptidyl-tyrosine phosphorylation Source: UniProtKB
    33. pigmentation Source: UniProtKB
    34. positive regulation of cell proliferation Source: Ensembl
    35. positive regulation of gene expression Source: Ensembl
    36. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    37. positive regulation of tyrosine phosphorylation of Stat1 protein Source: Ensembl
    38. positive regulation of tyrosine phosphorylation of Stat3 protein Source: Ensembl
    39. positive regulation of tyrosine phosphorylation of Stat5 protein Source: Ensembl
    40. protein autophosphorylation Source: Ensembl
    41. regulation of cell shape Source: UniProtKB
    42. regulation of developmental pigmentation Source: Ensembl
    43. response to radiation Source: Ensembl
    44. spermatid development Source: Ensembl
    45. spermatogenesis Source: UniProtKB
    46. stem cell differentiation Source: UniProtKB
    47. T cell differentiation Source: UniProtKB

    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. 1154.
    ReactomeiREACT_174426. Signaling by SCF-KIT.
    REACT_175504. Regulation of KIT signaling.
    REACT_226965. Constitutive PI3K/AKT Signaling in Cancer.

    Protein family/group databases

    MEROPSiI43.001.

    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
    OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
    Taxonomic identifieri9615 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
    ProteomesiUP000002254: Chromosome 13

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: Ensembl
    2. extracellular space Source: Ensembl
    3. integral component of membrane Source: UniProtKB-KW
    4. mast cell granule Source: GOC
    5. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 979952Mast/stem cell growth factor receptor KitPRO_0000016751Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi60 ↔ 99PROSITE-ProRule annotation
    Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi138 ↔ 188PROSITE-ProRule annotation
    Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi153 ↔ 185PROSITE-ProRule annotation
    Disulfide bondi235 ↔ 293PROSITE-ProRule annotation
    Glycosylationi286 – 2861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi403 – 4031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi431 ↔ 494PROSITE-ProRule annotation
    Glycosylationi466 – 4661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi489 – 4891N-linked (GlcNAc...)Sequence Analysis
    Modified residuei550 – 5501Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei556 – 5561Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei571 – 5711Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei573 – 5731Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei706 – 7061Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei724 – 7241Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei733 – 7331Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei744 – 7441Phosphoserine; by PKC/PRKCABy similarity
    Modified residuei749 – 7491Phosphoserine; by PKC/PRKCABy similarity
    Modified residuei824 – 8241PhosphoserineBy similarity
    Modified residuei826 – 8261Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei894 – 8941PhosphoserineBy similarity
    Modified residuei903 – 9031Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei939 – 9391Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei962 – 9621PhosphoserineBy similarity

    Post-translational modificationi

    Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation.By similarity
    Autophosphorylated on tyrosine residues. KITLG/SCF binding promotes autophosphorylation. Phosphorylated tyrosine residues are important for interaction with specific binding partners By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    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 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 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO97799.
    SMRiO97799. Positions 35-510, 550-930.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini28 – 527500ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini549 – 979431CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei528 – 54821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 11486Ig-like C2-type 1Add
    BLAST
    Domaini123 – 20785Ig-like C2-type 2Add
    BLAST
    Domaini214 – 31198Ig-like C2-type 3Add
    BLAST
    Domaini320 – 41394Ig-like C2-type 4Add
    BLAST
    Domaini416 – 51095Ig-like C2-type 5Add
    BLAST
    Domaini592 – 940349Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni571 – 5733Important for interaction with phosphotyrosine-binding proteinsBy similarity

    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

    eggNOGiCOG0515.
    GeneTreeiENSGT00720000108490.
    HOGENOMiHOG000112008.
    HOVERGENiHBG004335.
    InParanoidiO97799.
    KOiK05091.
    OMAiYFCPGTE.
    OrthoDBiEOG7S7SCZ.
    TreeFamiTF325768.

    Family and domain databases

    Gene3Di2.60.40.10. 5 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    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]
    PfamiPF07679. I-set. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500951. SCGF_recepter. 1 hit.
    PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTiSM00409. IG. 3 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS50835. IG_LIKE. 2 hits.
    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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O97799-1) [UniParc]FASTAAdd to Basket

    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

    MRGARGAWDF LCVLLLLLLL GVQTGSSQPS VSPGEPSLPS IHPAKSELIV    50
    SVGDELRLSC TDPGFVKWTF ETLGQLNENT HNEWITEKAE AGHTGNYTCT 100
    NRDGLSRSIY VFVRDPAKLF LVDLPLYGKE GNDTLVRCPL TDPEVTNYSL 150
    RGCEGKPLPK DLTFVADPKA GITIRNVKRE YHRLCLHCSA DQKGRTVLSK 200
    KFTLKVRAAI RAVPVVSVSK TSSLLKEGEA FSVMCFIKDV SSFVDSMWIK 250
    ENSQQTNAQT QSNSWHHGDF NFERQEKLII SSARVNDSGV FMCYANNTFG 300
    SANVTTTLEV VDKGFINIFP MMSTTIFVND GENVDLIVEY EAYPKPEHQQ 350
    WIYMNRTFTD KWEDYPKSDN ESNIRYVSEL HLTRLKGNEG GTYTFQVSNS 400
    DVNSSVTFNV YVNTKPEILT HESLTNGMLQ CVVAGFPEPA VDWYFCPGAE 450
    QRCSVPIGPM DVQMQNSSLS PSGKLVVQSS IDYSAFKHNG TVECRAYNNV 500
    GRSSAFFNFA FKGNSKEQIH PHTLFTPLLI GFVIAAGMMC IIVMILTYKY 550
    LQKPMYEVQW KVVEEINGNN YVYIDPTQLP YDHKWEFPRN RLSFGKTLGA 600
    GAFGKVVEAT AYGLIKSDAA MTVAVKMLKP SAHLTEREAL MSELKVLSYL 650
    GNHMNIVNLL GACTVGGPTL VITEYCCYGD LLNFLRRKRD SFICSKQEDH 700
    GEVALYKNLL HSKESSCSDS TNEYMDMKPG VSYVVPTKAD KRRSARIGSY 750
    IERDVTPAIM EDDELALDLE DLLSFSYQVA KGMAFLASKN CIHRDLAARN 800
    ILLTHGRITK ICDFGLARDI KNDSNYVVKG NARLPVKWMA PESIFNCVYT 850
    FESDVWSYGI FLWELFSLGS SPYPGMPVDS KFYKMIKEGF RMLSPEHAPA 900
    EMYDIMKTCW DADPLKRPTF KQIVQLIEKQ ISDSTNHIYS NLANCSPNPE 950
    RPVVDHSVRI NSVGSSASST QPLLVHEDV 979
    Length:979
    Mass (Da):109,753
    Last modified:September 5, 2006 - v2
    Checksum:i46C30D5DEB8E33D3
    GO
    Isoform 2 (identifier: O97799-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:975
    Mass (Da):109,367
    Checksum:iD845FADB06231FD9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231Q → R in AAD02327. (PubMed:9989791)Curated
    Sequence conflicti332 – 3321E → Q in AAD02327. (PubMed:9989791)Curated
    Sequence conflicti442 – 4421D → G in AAD02327. (PubMed:9989791)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei512 – 5154Missing in isoform 2. 2 PublicationsVSP_020224

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF044249 mRNA. Translation: AAD02327.1.
    AF448148 mRNA. Translation: AAL40833.1.
    AY296484 mRNA. Translation: AAP51178.1.
    AY313776 mRNA. Translation: AAP76390.1.
    RefSeqiNP_001003181.1. NM_001003181.1.
    XP_005628025.1. XM_005627968.1. [O97799-1]
    UniGeneiCfa.184.

    Genome annotation databases

    EnsembliENSCAFT00000049830; ENSCAFP00000039467; ENSCAFG00000002065. [O97799-2]
    GeneIDi403811.
    KEGGicfa:403811.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF044249 mRNA. Translation: AAD02327.1 .
    AF448148 mRNA. Translation: AAL40833.1 .
    AY296484 mRNA. Translation: AAP51178.1 .
    AY313776 mRNA. Translation: AAP76390.1 .
    RefSeqi NP_001003181.1. NM_001003181.1.
    XP_005628025.1. XM_005627968.1. [O97799-1 ]
    UniGenei Cfa.184.

    3D structure databases

    ProteinModelPortali O97799.
    SMRi O97799. Positions 35-510, 550-930.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi I43.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSCAFT00000049830 ; ENSCAFP00000039467 ; ENSCAFG00000002065 . [O97799-2 ]
    GeneIDi 403811.
    KEGGi cfa:403811.

    Organism-specific databases

    CTDi 3815.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00720000108490.
    HOGENOMi HOG000112008.
    HOVERGENi HBG004335.
    InParanoidi O97799.
    KOi K05091.
    OMAi YFCPGTE.
    OrthoDBi EOG7S7SCZ.
    TreeFami TF325768.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 1154.
    Reactomei REACT_174426. Signaling by SCF-KIT.
    REACT_175504. Regulation of KIT signaling.
    REACT_226965. Constitutive PI3K/AKT Signaling in Cancer.

    Miscellaneous databases

    NextBioi 20817307.

    Family and domain databases

    Gene3Di 2.60.40.10. 5 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    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 ]
    Pfami PF07679. I-set. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500951. SCGF_recepter. 1 hit.
    PIRSF000615. TyrPK_CSF1-R. 1 hit.
    SMARTi SM00409. IG. 3 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS50835. IG_LIKE. 2 hits.
    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 ]
    ProtoNeti Search...

    Publicationsi

    1. "Clustering of activating mutations in c-KIT's juxtamembrane coding region in canine mast cell neoplasms."
      Ma Y., Longley B.J., Wang X., Blount J.L., Langley K., Caughey G.H.
      J. Invest. Dermatol. 112:165-170(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. Zemke D., Yuzbasiyan-Gurkan V.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Characterization of an isoform and RH mapping of canine c-kit."
      Tsai K.L., Guyon R., Murphy K.E.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).

    Entry informationi

    Entry nameiKIT_CANFA
    AccessioniPrimary (citable) accession number: O97799
    Secondary accession number(s): Q7YRV7, Q8WN23
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 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.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3