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Q06418

- TYRO3_HUMAN

UniProt

Q06418 - TYRO3_HUMAN

Protein

Tyrosine-protein kinase receptor TYRO3

Gene

TYRO3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TULP1 or GAS6. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with PIK3R1 and thereby enhances PI3-kinase activity. Activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays a role in various processes such as neuron protection from excitotoxic injury, platelet aggregation and cytoskeleton reorganization. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3.2 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei550 – 5501ATPPROSITE-ProRule annotation
    Active sitei655 – 6551Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi524 – 5329ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphatidylinositol 3-kinase binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein tyrosine kinase activity Source: UniProtKB
    5. receptor signaling protein tyrosine kinase activity Source: UniProtKB
    6. transmembrane receptor protein tyrosine kinase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic cell clearance Source: UniProtKB
    2. cell adhesion Source: UniProtKB
    3. forebrain cell migration Source: UniProtKB
    4. natural killer cell differentiation Source: Ensembl
    5. negative regulation of inflammatory response Source: UniProtKB
    6. negative regulation of innate immune response Source: UniProtKB
    7. negative regulation of lymphocyte activation Source: Ensembl
    8. negative regulation of neuron apoptotic process Source: UniProtKB
    9. negative regulation of toll-like receptor signaling pathway Source: UniProtKB
    10. neuron cellular homeostasis Source: UniProtKB
    11. ovulation cycle Source: UniProtKB
    12. peptidyl-tyrosine phosphorylation Source: GOC
    13. phosphatidylinositol 3-kinase signaling Source: UniProtKB
    14. platelet activation Source: UniProtKB
    15. platelet aggregation Source: UniProtKB
    16. protein autophosphorylation Source: UniProtKB
    17. protein kinase B signaling Source: UniProtKB
    18. secretion by cell Source: UniProtKB
    19. signal transduction Source: UniProtKB
    20. signal transduction by phosphorylation Source: GOC
    21. spermatogenesis Source: UniProtKB
    22. substrate adhesion-dependent cell spreading Source: UniProtKB
    23. vagina development Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    SignaLinkiQ06418.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase receptor TYRO3 (EC:2.7.10.1)
    Alternative name(s):
    Tyrosine-protein kinase BYK
    Tyrosine-protein kinase DTK
    Tyrosine-protein kinase RSE
    Tyrosine-protein kinase SKY
    Tyrosine-protein kinase TIF
    Gene namesi
    Name:TYRO3
    Synonyms:BYK, DTK, RSE, SKY, TIF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:12446. TYRO3.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB
    2. integral component of plasma membrane Source: UniProtKB
    3. nuclear envelope Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi99 – 991I → R: Abolishes dimerization. 1 Publication

    Organism-specific databases

    PharmGKBiPA37097.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4040Sequence AnalysisAdd
    BLAST
    Chaini41 – 890850Tyrosine-protein kinase receptor TYRO3PRO_0000024478Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi64 ↔ 1171 PublicationPROSITE-ProRule annotation
    Disulfide bondi160 ↔ 2031 PublicationPROSITE-ProRule annotation
    Glycosylationi191 – 1911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi293 – 2931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi366 – 3661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis
    Modified residuei681 – 6811Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei685 – 6851Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei686 – 6861Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei804 – 8041Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylated.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ06418.
    PRIDEiQ06418.

    PTM databases

    PhosphoSiteiQ06418.

    Expressioni

    Tissue specificityi

    Abundant in the brain and lower levels in other tissues.

    Gene expression databases

    ArrayExpressiQ06418.
    BgeeiQ06418.
    CleanExiHS_TYRO3.
    GenevestigatoriQ06418.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Interacts (via N-terminus) with extracellular ligands TULP1 and GAS6 By similarity. Interacts with PIK3R1; this interaction increases PI3-kinase activity By similarity.By similarity

    Protein-protein interaction databases

    BioGridi113152. 12 interactions.
    IntActiQ06418. 6 interactions.
    STRINGi9606.ENSP00000263798.

    Structurei

    Secondary structure

    1
    890
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi50 – 556
    Beta strandi60 – 689
    Beta strandi74 – 785
    Beta strandi85 – 9410
    Beta strandi97 – 10610
    Helixi109 – 1113
    Beta strandi113 – 1219
    Beta strandi131 – 1366
    Beta strandi140 – 1434
    Beta strandi148 – 1503
    Beta strandi156 – 1638
    Beta strandi165 – 1673
    Beta strandi170 – 1756
    Beta strandi183 – 19210
    Beta strandi199 – 2079
    Beta strandi210 – 2134
    Beta strandi217 – 2215

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RHFX-ray1.96A/B41-222[»]
    ProteinModelPortaliQ06418.
    SMRiQ06418. Positions 47-410, 509-792.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ06418.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini41 – 429389ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini451 – 890440CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei430 – 45021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 12888Ig-like C2-type 1Add
    BLAST
    Domaini139 – 22082Ig-like C2-type 2Add
    BLAST
    Domaini227 – 32094Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini325 – 41692Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini518 – 790273Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily.PROSITE-ProRule annotation
    Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG006346.
    InParanoidiQ06418.
    KOiK05116.
    OMAiDQVYIPV.
    PhylomeDBiQ06418.
    TreeFamiTF317402.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF00041. fn3. 2 hits.
    PF07679. I-set. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00060. FN3. 2 hits.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50853. FN3. 2 hits.
    PS50835. IG_LIKE. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q06418-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALRRSMGRP GLPPLPLPPP PRLGLLLAAL ASLLLPESAA AGLKLMGAPV    50
    KLTVSQGQPV KLNCSVEGME EPDIQWVKDG AVVQNLDQLY IPVSEQHWIG 100
    FLSLKSVERS DAGRYWCQVE DGGETEISQP VWLTVEGVPF FTVEPKDLAV 150
    PPNAPFQLSC EAVGPPEPVT IVWWRGTTKI GGPAPSPSVL NVTGVTQSTM 200
    FSCEAHNLKG LASSRTATVH LQALPAAPFN ITVTKLSSSN ASVAWMPGAD 250
    GRALLQSCTV QVTQAPGGWE VLAVVVPVPP FTCLLRDLVP ATNYSLRVRC 300
    ANALGPSPYA DWVPFQTKGL APASAPQNLH AIRTDSGLIL EWEEVIPEAP 350
    LEGPLGPYKL SWVQDNGTQD ELTVEGTRAN LTGWDPQKDL IVRVCVSNAV 400
    GCGPWSQPLV VSSHDRAGQQ GPPHSRTSWV PVVLGVLTAL VTAAALALIL 450
    LRKRRKETRF GQAFDSVMAR GEPAVHFRAA RSFNRERPER IEATLDSLGI 500
    SDELKEKLED VLIPEQQFTL GRMLGKGEFG SVREAQLKQE DGSFVKVAVK 550
    MLKADIIASS DIEEFLREAA CMKEFDHPHV AKLVGVSLRS RAKGRLPIPM 600
    VILPFMKHGD LHAFLLASRI GENPFNLPLQ TLIRFMVDIA CGMEYLSSRN 650
    FIHRDLAARN CMLAEDMTVC VADFGLSRKI YSGDYYRQGC ASKLPVKWLA 700
    LESLADNLYT VQSDVWAFGV TMWEIMTRGQ TPYAGIENAE IYNYLIGGNR 750
    LKQPPECMED VYDLMYQCWS ADPKQRPSFT CLRMELENIL GQLSVLSASQ 800
    DPLYINIERA EEPTAGGSLE LPGRDQPYSG AGDGSGMGAV GGTPSDCRYI 850
    LTPGGLAEQP GQAEHQPESP LNETQRLLLL QQGLLPHSSC 890
    Length:890
    Mass (Da):96,905
    Last modified:October 1, 1996 - v1
    Checksum:iF9EC675077C4E8F1
    GO

    Sequence cautioni

    The sequence BAA21781.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 368Missing in AAC50070. (PubMed:7857658)Curated
    Sequence conflicti285 – 2851L → F in BAA21781. (PubMed:9175267)Curated
    Sequence conflicti293 – 2931N → I in BAA21781. (PubMed:9175267)Curated
    Sequence conflicti341 – 3411E → V in BAA21781. (PubMed:9175267)Curated
    Sequence conflicti812 – 8121E → D in BAA21781. (PubMed:9175267)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211P → L.1 Publication
    Corresponds to variant rs17854578 [ dbSNP | Ensembl ].
    VAR_045886
    Natural varianti346 – 3461I → N.
    Corresponds to variant rs12148316 [ dbSNP | Ensembl ].
    VAR_045887
    Natural varianti542 – 5421G → S.1 Publication
    Corresponds to variant rs17857363 [ dbSNP | Ensembl ].
    VAR_045888
    Natural varianti815 – 8151A → V.1 Publication
    Corresponds to variant rs1042057 [ dbSNP | Ensembl ].
    VAR_045889
    Natural varianti819 – 8191L → M.1 Publication
    Corresponds to variant rs17854579 [ dbSNP | Ensembl ].
    VAR_045890
    Natural varianti824 – 8241R → G.1 Publication
    Corresponds to variant rs17857364 [ dbSNP | Ensembl ].
    VAR_045891
    Natural varianti831 – 8311A → T.1 Publication
    VAR_041876

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05682 mRNA. Translation: AAA19236.1.
    D17517 mRNA. Translation: BAA04467.1.
    U18934 mRNA. Translation: AAC50070.1.
    D50479 mRNA. Translation: BAA21781.1. Different initiation.
    BC049368 mRNA. Translation: AAH49368.1.
    BC051756 mRNA. Translation: AAH51756.1.
    X72886 mRNA. Translation: CAA51396.1.
    CCDSiCCDS10080.1.
    PIRiA53743.
    I38912.
    RefSeqiNP_006284.2. NM_006293.3.
    UniGeneiHs.381282.

    Genome annotation databases

    EnsembliENST00000263798; ENSP00000263798; ENSG00000092445.
    GeneIDi7301.
    KEGGihsa:7301.
    UCSCiuc001zof.2. human.

    Polymorphism databases

    DMDMi1717829.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U05682 mRNA. Translation: AAA19236.1 .
    D17517 mRNA. Translation: BAA04467.1 .
    U18934 mRNA. Translation: AAC50070.1 .
    D50479 mRNA. Translation: BAA21781.1 . Different initiation.
    BC049368 mRNA. Translation: AAH49368.1 .
    BC051756 mRNA. Translation: AAH51756.1 .
    X72886 mRNA. Translation: CAA51396.1 .
    CCDSi CCDS10080.1.
    PIRi A53743.
    I38912.
    RefSeqi NP_006284.2. NM_006293.3.
    UniGenei Hs.381282.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RHF X-ray 1.96 A/B 41-222 [» ]
    ProteinModelPortali Q06418.
    SMRi Q06418. Positions 47-410, 509-792.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113152. 12 interactions.
    IntActi Q06418. 6 interactions.
    STRINGi 9606.ENSP00000263798.

    Chemistry

    BindingDBi Q06418.
    ChEMBLi CHEMBL5314.
    GuidetoPHARMACOLOGYi 1836.

    PTM databases

    PhosphoSitei Q06418.

    Polymorphism databases

    DMDMi 1717829.

    Proteomic databases

    PaxDbi Q06418.
    PRIDEi Q06418.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263798 ; ENSP00000263798 ; ENSG00000092445 .
    GeneIDi 7301.
    KEGGi hsa:7301.
    UCSCi uc001zof.2. human.

    Organism-specific databases

    CTDi 7301.
    GeneCardsi GC15P041851.
    HGNCi HGNC:12446. TYRO3.
    MIMi 600341. gene.
    neXtProti NX_Q06418.
    PharmGKBi PA37097.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG006346.
    InParanoidi Q06418.
    KOi K05116.
    OMAi DQVYIPV.
    PhylomeDBi Q06418.
    TreeFami TF317402.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    SignaLinki Q06418.

    Miscellaneous databases

    EvolutionaryTracei Q06418.
    GeneWikii TYRO3.
    GenomeRNAii 7301.
    NextBioi 28553.
    PROi Q06418.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q06418.
    Bgeei Q06418.
    CleanExi HS_TYRO3.
    Genevestigatori Q06418.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF00041. fn3. 2 hits.
    PF07679. I-set. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00060. FN3. 2 hits.
    SM00409. IG. 1 hit.
    SM00408. IGc2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50853. FN3. 2 hits.
    PS50835. IG_LIKE. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RSE, a novel receptor-type tyrosine kinase with homology to Axl/Ufo, is expressed at high levels in the brain."
      Mark M.R., Scadden D.T., Wang Z., Gu Q., Goddard A., Godowski P.J.
      J. Biol. Chem. 269:10720-10728(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning of the cDNA for a novel receptor tyrosine kinase, Sky, predominantly expressed in brain."
      Ohashi K., Mizuno K., Kuma K., Miyata T., Nakamura T.
      Oncogene 9:699-705(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Isolation and characterization of the human DTK receptor tyrosine kinase."
      Crosier K.E., Hall L.R., Lewis P.M., Morris C.M., Wood C.R., Morris J.C., Crosier P.S.
      Growth Factors 11:137-144(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-815.
      Tissue: Brain.
    4. "A tyrosine kinase-like molecule is localized in the nuclear membrane of neurons: hippocampal behavior under stress."
      Kajii Y., Ninomiya D., Kato M., Mizuguchi M., Saji M., Katsumoto T., Ohno K., Takashima S., Onodera K.
      Biol. Cell 88:45-54(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    5. "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], VARIANTS LEU-21; SER-542; MET-819 AND GLY-824.
      Tissue: Skin and Testis.
    6. "The human TYRO3 gene and pseudogene are located in chromosome 15q14-q25."
      Polvi A., Armstrong E., Lai C., Lemke G., Huebner K., Spritz R.A., Giuda L.C., Nicholls R.D., Alitalo K.
      Gene 134:289-293(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 519-720.
    7. "Autophosphorylation activity and association with Src family kinase of Sky receptor tyrosine kinase."
      Toshima J., Ohashi K., Iwashita S., Mizuno K.
      Biochem. Biophys. Res. Commun. 209:656-663(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOPHOSPHORYLATION.
    8. "Reevaluation of the roles of protein S and Gas6 as ligands for the receptor tyrosine kinase Rse/Tyro 3."
      Godowski P.J., Mark M.R., Chen J., Sadick M.D., Raab H., Hammonds R.G.
      Cell 82:355-358(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAS6.
    9. "Signalling and functional diversity within the Axl subfamily of receptor tyrosine kinases."
      Hafizi S., Dahlback B.
      Cytokine Growth Factor Rev. 17:295-304(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    10. Cited for: FUNCTION AS CELL ENTRY FACTOR IN FILOVIRUS INFECTION.
    11. Cited for: REVIEW ON FUNCTION.
    12. "Potentiating role of Gas6 and Tyro3, Axl and Mer (TAM) receptors in human and murine platelet activation and thrombus stabilization."
      Cosemans J.M., Van Kruchten R., Olieslagers S., Schurgers L.J., Verheyen F.K., Munnix I.C., Waltenberger J., Angelillo-Scherrer A., Hoylaerts M.F., Carmeliet P., Heemskerk J.W.
      J. Thromb. Haemost. 8:1797-1808(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PLATELET ACTIVATION.
    13. "Ligand recognition and homophilic interactions in Tyro3: structural insights into the Axl/Tyro3 receptor tyrosine kinase family."
      Heiring C., Dahlbaeck B., Muller Y.A.
      J. Biol. Chem. 279:6952-6958(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 41-222, SUBUNIT, INTERACTION WITH GAS6, MUTAGENESIS OF ILE-99, DISULFIDE BONDS.
    14. "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: VARIANT [LARGE SCALE ANALYSIS] THR-831.

    Entry informationi

    Entry nameiTYRO3_HUMAN
    AccessioniPrimary (citable) accession number: Q06418
    Secondary accession number(s): O14953, Q86VR3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 151 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3