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P30530

- UFO_HUMAN

UniProt

P30530 - UFO_HUMAN

Protein

Tyrosine-protein kinase receptor UFO

Gene

AXL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 3 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding growth factor GAS6 and which is thus regulating many physiological processes including cell survival, cell proliferation, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of AXL. Following activation by ligand, ALX binds and induces tyrosine phosphorylation of PI3-kinase subunits PIK3R1, PIK3R2 and PIK3R3; but also GRB2, PLCG1, LCK and PTPN11. Other downstream substrate candidates for AXL are CBL, NCK2, SOCS1 and TENC1. Recruitment of GRB2 and phosphatidylinositol 3 kinase regulatory subunits by AXL leads to the downstream activation of the AKT kinase. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. Plays also an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response. In case of filovirus infection, seems to function as a cell entry factor.9 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Activated by GAS6-binding and subsequent autophosphorylation.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei567 – 5671ATPPROSITE-ProRule annotation
    Active sitei672 – 6721Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi542 – 5509ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphatidylserine binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. transmembrane receptor protein tyrosine kinase activity Source: ProtInc

    GO - Biological processi

    1. apoptotic cell clearance Source: Ensembl
    2. blood vessel remodeling Source: Ensembl
    3. cell maturation Source: UniProtKB
    4. cellular response to extracellular stimulus Source: Ensembl
    5. cellular response to hydrogen peroxide Source: Ensembl
    6. cellular response to interferon-alpha Source: UniProtKB
    7. cellular response to lipopolysaccharide Source: UniProtKB
    8. dendritic cell differentiation Source: UniProtKB
    9. enzyme linked receptor protein signaling pathway Source: Ensembl
    10. erythrocyte homeostasis Source: Ensembl
    11. forebrain cell migration Source: Ensembl
    12. inflammatory response Source: Ensembl
    13. innate immune response Source: UniProtKB-KW
    14. natural killer cell differentiation Source: Ensembl
    15. negative regulation of dendritic cell apoptotic process Source: UniProtKB
    16. negative regulation of interferon-gamma production Source: UniProtKB
    17. negative regulation of lymphocyte activation Source: Ensembl
    18. negative regulation of neuron apoptotic process Source: Ensembl
    19. negative regulation of tumor necrosis factor production Source: Ensembl
    20. neuron migration Source: Ensembl
    21. organ regeneration Source: Ensembl
    22. ovulation cycle Source: Ensembl
    23. peptidyl-tyrosine phosphorylation Source: GOC
    24. phagocytosis Source: UniProtKB
    25. platelet activation Source: Ensembl
    26. positive regulation of cytokine-mediated signaling pathway Source: UniProtKB
    27. positive regulation of natural killer cell differentiation Source: UniProtKB
    28. positive regulation of protein kinase B signaling Source: Ensembl
    29. protein kinase B signaling Source: Ensembl
    30. secretion by cell Source: Ensembl
    31. signal transduction Source: ProtInc
    32. spermatogenesis Source: Ensembl
    33. substrate adhesion-dependent cell spreading Source: Ensembl
    34. vagina development Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Differentiation, Immunity, Innate immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    SignaLinkiP30530.

    Protein family/group databases

    MEROPSiI43.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase receptor UFO (EC:2.7.10.1)
    Alternative name(s):
    AXL oncogene
    Gene namesi
    Name:AXL
    Synonyms:UFO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:905. AXL.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. extracellular space Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. integral component of plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    AXL and its ligand GAS6 are highly expressed in thyroid carcinoma tissues, and might thus be involved in thyroid tumorigenesis. Overexpression of AXL and its ligand was also detected in many other cancers such as myeloproliferative disorders, prostatic carcinoma cells, or breast cancer.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi63 – 631E → R: Slightly reduced affinity for GAS6. 1 Publication
    Mutagenesisi66 – 661E → R: Reduced affinity for GAS6. 1 Publication
    Mutagenesisi84 – 841T → R: Reduced affinity for GAS6. 1 Publication

    Keywords - Diseasei

    Oncogene, Proto-oncogene

    Organism-specific databases

    PharmGKBiPA25197.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Sequence AnalysisAdd
    BLAST
    Chaini26 – 894869Tyrosine-protein kinase receptor UFOPRO_0000024481Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi43 – 431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi56 ↔ 117PROSITE-ProRule annotation
    Glycosylationi157 – 1571N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi160 ↔ 205PROSITE-ProRule annotation
    Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
    Modified residuei703 – 7031Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei779 – 7791Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei821 – 8211Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei866 – 8661Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei884 – 8841Phosphoserine1 Publication

    Post-translational modificationi

    Monoubiquitinated upon GAS6-binding. A very small proportion of the receptor could be subjected to polyubiquitination in a very transient fashion.1 Publication
    Phosphorylated at tyrosine residues by autocatalysis, which activates kinase activity.3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP30530.
    PaxDbiP30530.
    PRIDEiP30530.

    PTM databases

    PhosphoSiteiP30530.

    Expressioni

    Tissue specificityi

    Highly expressed in metastatic colon tumors. Expressed in primary colon tumors. Weakly expressed in normal colon tissue.1 Publication

    Gene expression databases

    ArrayExpressiP30530.
    BgeeiP30530.
    CleanExiHS_AXL.
    GenevestigatoriP30530.

    Organism-specific databases

    HPAiHPA037422.
    HPA037423.

    Interactioni

    Subunit structurei

    Heterodimer and heterotetramer with ligand GAS6. Interacts with CBL, GRB2, LCK, NCK2, PIK3R1, PIK3R2, PIK3R3, PLCG1, SOCS1 and TENC1. Part of a complex including AXL, TNK2 and GRB2, in which GRB2 promotes AXL recruitment by TNK2.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GAS6Q143938EBI-2850927,EBI-2802811
    GRB2P629933EBI-2850927,EBI-401755

    Protein-protein interaction databases

    BioGridi107036. 17 interactions.
    IntActiP30530. 7 interactions.
    MINTiMINT-2735752.
    STRINGi9606.ENSP00000301178.

    Structurei

    Secondary structure

    1
    894
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 394
    Beta strandi44 – 463
    Beta strandi52 – 6312
    Beta strandi68 – 714
    Beta strandi80 – 878
    Beta strandi89 – 913
    Beta strandi94 – 10613
    Beta strandi113 – 1219
    Beta strandi124 – 1274
    Beta strandi131 – 1355
    Beta strandi140 – 1434
    Beta strandi148 – 1503
    Beta strandi156 – 1638
    Beta strandi170 – 1778
    Beta strandi179 – 1835
    Beta strandi190 – 1945
    Beta strandi201 – 2099
    Beta strandi212 – 2154
    Beta strandi219 – 2235

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C5DX-ray3.30C/D33-227[»]
    ProteinModelPortaliP30530.
    SMRiP30530. Positions 34-224, 491-842.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30530.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 451426ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini473 – 894422CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei452 – 47221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 128102Ig-like C2-type 1Add
    BLAST
    Domaini139 – 22284Ig-like C2-type 2Add
    BLAST
    Domaini227 – 331105Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini336 – 42893Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini536 – 807272Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 9267Interaction with GAS6Add
    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.
    HOGENOMiHOG000231685.
    HOVERGENiHBG006346.
    InParanoidiP30530.
    KOiK05115.
    OMAiQVQGEPP.
    OrthoDBiEOG77DJ5C.
    PhylomeDBiP30530.
    TreeFamiTF317402.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    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.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00060. FN3. 2 hits.
    SM00409. IG. 2 hits.
    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]

    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 Long (identifier: P30530-1) [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

    MAWRCPRMGR VPLAWCLALC GWACMAPRGT QAEESPFVGN PGNITGARGL    50
    TGTLRCQLQV QGEPPEVHWL RDGQILELAD STQTQVPLGE DEQDDWIVVS 100
    QLRITSLQLS DTGQYQCLVF LGHQTFVSQP GYVGLEGLPY FLEEPEDRTV 150
    AANTPFNLSC QAQGPPEPVD LLWLQDAVPL ATAPGHGPQR SLHVPGLNKT 200
    SSFSCEAHNA KGVTTSRTAT ITVLPQQPRN LHLVSRQPTE LEVAWTPGLS 250
    GIYPLTHCTL QAVLSNDGMG IQAGEPDPPE EPLTSQASVP PHQLRLGSLH 300
    PHTPYHIRVA CTSSQGPSSW THWLPVETPE GVPLGPPENI SATRNGSQAF 350
    VHWQEPRAPL QGTLLGYRLA YQGQDTPEVL MDIGLRQEVT LELQGDGSVS 400
    NLTVCVAAYT AAGDGPWSLP VPLEAWRPGQ AQPVHQLVKE PSTPAFSWPW 450
    WYVLLGAVVA AACVLILALF LVHRRKKETR YGEVFEPTVE RGELVVRYRV 500
    RKSYSRRTTE ATLNSLGISE ELKEKLRDVM VDRHKVALGK TLGEGEFGAV 550
    MEGQLNQDDS ILKVAVKTMK IAICTRSELE DFLSEAVCMK EFDHPNVMRL 600
    IGVCFQGSER ESFPAPVVIL PFMKHGDLHS FLLYSRLGDQ PVYLPTQMLV 650
    KFMADIASGM EYLSTKRFIH RDLAARNCML NENMSVCVAD FGLSKKIYNG 700
    DYYRQGRIAK MPVKWIAIES LADRVYTSKS DVWSFGVTMW EIATRGQTPY 750
    PGVENSEIYD YLRQGNRLKQ PADCLDGLYA LMSRCWELNP QDRPSFTELR 800
    EDLENTLKAL PPAQEPDEIL YVNMDEGGGY PEPPGAAGGA DPPTQPDPKD 850
    SCSCLTAAEV HPAGRYVLCP STTPSPAQPA DRGSPAAPGQ EDGA 894
    Length:894
    Mass (Da):98,336
    Last modified:June 16, 2009 - v3
    Checksum:i2C2D3574EADA4116
    GO
    Isoform Short (identifier: P30530-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         429-437: Missing.

    Show »
    Length:885
    Mass (Da):97,377
    Checksum:iAFF0212BA8EAEAA1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti303 – 3031T → P in AAB20305. (PubMed:1834974)Curated
    Sequence conflicti303 – 3031T → P in CAA40338. (PubMed:1834974)Curated
    Sequence conflicti338 – 3381E → K in AAA61243. (PubMed:1656220)Curated
    Sequence conflicti430 – 4301Q → E in AAB20305. (PubMed:1834974)Curated
    Sequence conflicti430 – 4301Q → E in CAA40338. (PubMed:1834974)Curated
    Sequence conflicti639 – 6391D → G in AAB20305. (PubMed:1834974)Curated
    Sequence conflicti639 – 6391D → G in CAA40338. (PubMed:1834974)Curated
    Sequence conflicti696 – 6961K → I no nucleotide entry (PubMed:7896447)Curated
    Sequence conflicti764 – 7641Q → R in AAH32229. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121T → M.1 Publication
    Corresponds to variant rs35202236 [ dbSNP | Ensembl ].
    VAR_045596
    Natural varianti266 – 2661N → D.4 Publications
    Corresponds to variant rs7249222 [ dbSNP | Ensembl ].
    VAR_057990
    Natural varianti295 – 2951R → W in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
    VAR_045597
    Natural varianti499 – 4991R → C in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041877
    Natural varianti515 – 5151S → G.1 Publication
    VAR_041878

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei429 – 4379Missing in isoform Short. 1 PublicationVSP_005017

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76125 mRNA. Translation: AAA61243.1.
    S65125 mRNA. Translation: AAB20305.1.
    X57019 mRNA. Translation: CAA40338.1.
    AC011510 Genomic DNA. No translation available.
    BC032229 mRNA. Translation: AAH32229.1.
    CCDSiCCDS12574.1. [P30530-2]
    CCDS12575.1. [P30530-1]
    PIRiA41527.
    RefSeqiNP_001690.2. NM_001699.5.
    NP_068713.2. NM_021913.4.
    UniGeneiHs.590970.

    Genome annotation databases

    EnsembliENST00000301178; ENSP00000301178; ENSG00000167601. [P30530-1]
    ENST00000359092; ENSP00000351995; ENSG00000167601. [P30530-2]
    GeneIDi558.
    KEGGihsa:558.
    UCSCiuc010ehi.1. human. [P30530-1]
    uc010ehk.3. human. [P30530-2]

    Polymorphism databases

    DMDMi239938818.

    Keywords - Coding sequence diversityi

    Alternative splicing, 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
    M76125 mRNA. Translation: AAA61243.1 .
    S65125 mRNA. Translation: AAB20305.1 .
    X57019 mRNA. Translation: CAA40338.1 .
    AC011510 Genomic DNA. No translation available.
    BC032229 mRNA. Translation: AAH32229.1 .
    CCDSi CCDS12574.1. [P30530-2 ]
    CCDS12575.1. [P30530-1 ]
    PIRi A41527.
    RefSeqi NP_001690.2. NM_001699.5.
    NP_068713.2. NM_021913.4.
    UniGenei Hs.590970.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C5D X-ray 3.30 C/D 33-227 [» ]
    ProteinModelPortali P30530.
    SMRi P30530. Positions 34-224, 491-842.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107036. 17 interactions.
    IntActi P30530. 7 interactions.
    MINTi MINT-2735752.
    STRINGi 9606.ENSP00000301178.

    Chemistry

    BindingDBi P30530.
    ChEMBLi CHEMBL4895.
    GuidetoPHARMACOLOGYi 1835.

    Protein family/group databases

    MEROPSi I43.001.

    PTM databases

    PhosphoSitei P30530.

    Polymorphism databases

    DMDMi 239938818.

    Proteomic databases

    MaxQBi P30530.
    PaxDbi P30530.
    PRIDEi P30530.

    Protocols and materials databases

    DNASUi 558.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301178 ; ENSP00000301178 ; ENSG00000167601 . [P30530-1 ]
    ENST00000359092 ; ENSP00000351995 ; ENSG00000167601 . [P30530-2 ]
    GeneIDi 558.
    KEGGi hsa:558.
    UCSCi uc010ehi.1. human. [P30530-1 ]
    uc010ehk.3. human. [P30530-2 ]

    Organism-specific databases

    CTDi 558.
    GeneCardsi GC19P041725.
    HGNCi HGNC:905. AXL.
    HPAi HPA037422.
    HPA037423.
    MIMi 109135. gene.
    neXtProti NX_P30530.
    PharmGKBi PA25197.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000231685.
    HOVERGENi HBG006346.
    InParanoidi P30530.
    KOi K05115.
    OMAi QVQGEPP.
    OrthoDBi EOG77DJ5C.
    PhylomeDBi P30530.
    TreeFami TF317402.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    SignaLinki P30530.

    Miscellaneous databases

    ChiTaRSi AXL. human.
    EvolutionaryTracei P30530.
    GeneWikii AXL_receptor_tyrosine_kinase.
    GenomeRNAii 558.
    NextBioi 2293.
    PROi P30530.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30530.
    Bgeei P30530.
    CleanExi HS_AXL.
    Genevestigatori P30530.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    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.
    PF07714. Pkinase_Tyr. 1 hit.
    PF07686. V-set. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00060. FN3. 2 hits.
    SM00409. IG. 2 hits.
    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-266.
    2. "AXL, a transforming gene isolated from primary human myeloid leukemia cells, encodes a novel receptor tyrosine kinase."
      O'Bryan J.P., Frye R.A., Cogswell P.C., Neubauer A., Kitch B., Prokop C., Espinosa R., le Beau M.M., Earp H., Liu E.T.
      Mol. Cell. Biol. 11:5016-5031(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), VARIANT ASP-266, ROLE IN MYELOID LEUKEMIA.
      Tissue: Fibroblast.
    3. "A novel putative tyrosine kinase receptor with oncogenic potential."
      Janssen J.W.G., Schulz A.S., Steenvoorden A.C.M., Schmidberger M., Strehl S., Ambros P., Bartram C.R.
      Oncogene 6:2113-2120(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANT ASP-266.
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM LONG), VARIANT ASP-266.
    6. "A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes."
      Lee S.-T., Strunk K.M., Spritz R.A.
      Oncogene 8:3403-3410(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 674-730.
    7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 677-730, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Colon tumor.
    8. "Axl receptor tyrosine kinase stimulated by the vitamin K-dependent protein encoded by growth-arrest-specific gene 6."
      Varnum B.C., Young C., Elliott G., Garcia A., Bartley T.D., Fridell Y.W., Hunt R.W., Trail G., Clogston C., Toso R.J., Yanagihara D., Bennett L., Silber M., Merewether L.A., Tseng A., Escobar E., Liu E.T., Yamane H.K.
      Nature 373:623-626(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIGAND GAS6.
    9. "Characterization of Gas6, a member of the superfamily of G domain-containing proteins, as a ligand for Rse and Axl."
      Mark M.R., Chen J., Hammonds R.G., Sadick M., Godowski P.J.
      J. Biol. Chem. 271:9785-9789(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAS6, ENZYME REGULATION.
    10. "Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is mediated mainly by a multi-substrate docking-site."
      Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R., Ullrich A., Bartram C.R., Janssen J.W.
      Oncogene 14:2619-2631(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-779; TYR-821 AND TYR-866, INTERACTION WITH GRB2; LCK; PIK3R1; PIK3R2 AND PLCG1.
    11. "A receptor tyrosine kinase, UFO/Axl, and other genes isolated by a modified differential display PCR are overexpressed in metastatic prostatic carcinoma cell line DU145."
      Jacob A.N., Kalapurakal J., Davidson W.R., Kandpal G., Dunson N., Prashar Y., Kandpal R.P.
      Cancer Detect. Prev. 23:325-332(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN PROSTATIC CARCINOMA.
    12. "Estrogen dependent expression of the receptor tyrosine kinase axl in normal and malignant human breast."
      Berclaz G., Altermatt H.J., Rohrbach V., Kieffer I., Dreher E., Andres A.C.
      Ann. Oncol. 12:819-824(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN BREAST CANCER.
    13. "Interaction of Axl receptor tyrosine kinase with C1-TEN, a novel C1 domain-containing protein with homology to tensin."
      Hafizi S., Alindri F., Karlsson R., Dahlbaeck B.
      Biochem. Biophys. Res. Commun. 299:793-800(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCK2; PIK3R3; SOCS1 AND TENC1.
    14. "Acidification prevents endothelial cell apoptosis by Axl activation."
      D'Arcangelo D., Gaetano C., Capogrossi M.C.
      Circ. Res. 91:E4-12(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE GAS6/AXL SIGNALING PATHWAY.
    15. "Expression of receptor-type tyrosine kinase, Axl, and its ligand, Gas6, in pediatric thyroid carcinomas around Chernobyl."
      Ito M., Nakashima M., Nakayama T., Ohtsuru A., Nagayama Y., Takamura N., Demedchik E.P., Sekine I., Yamashita S.
      Thyroid 12:971-975(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN THYROID CARCINOMAS.
    16. "Effects of Gas6 and hydrogen peroxide in Axl ubiquitination and downregulation."
      Valverde P.
      Biochem. Biophys. Res. Commun. 333:180-185(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBL AND GAS6, UBIQUITINATION.
    17. "Inhibition of vascular endothelial growth factor receptor 2-mediated endothelial cell activation by Axl tyrosine kinase receptor."
      Gallicchio M., Mitola S., Valdembri D., Fantozzi R., Varnum B., Avanzi G.C., Bussolino F.
      Blood 105:1970-1976(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, FUNCTION.
    18. "Gas6 receptors Axl, Sky and Mer enhance platelet activation and regulate thrombotic responses."
      Gould W.R., Baxi S.M., Schroeder R., Peng Y.W., Leadley R.J., Peterson J.T., Perrin L.A.
      J. Thromb. Haemost. 3:733-741(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PLATELET ACTIVATION AND THROMBOTIC RESPONSE REGULATION.
    19. Cited for: FUNCTION AS CELL ENTRY FACTOR IN FILOVIRUS INFECTION.
    20. "In brain, Axl recruits Grb2 and the p85 regulatory subunit of PI3 kinase; in vitro mutagenesis defines the requisite binding sites for downstream Akt activation."
      Weinger J.G., Gohari P., Yan Y., Backer J.M., Varnum B., Shafit-Zagardo B.
      J. Neurochem. 106:134-146(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB2; PIK3R1 AND PIK3R2, PHOSPHORYLATION AT TYR-779; TYR-821 AND TYR-866.
    21. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-884, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. "The Axl/Gas6 pathway is required for optimal cytokine signaling during human natural killer cell development."
      Park I.K., Giovenzana C., Hughes T.L., Yu J., Trotta R., Caligiuri M.A.
      Blood 113:2470-2477(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE GAS6/AXL SIGNALING PATHWAY.
    23. "Cytoplasmic ACK1 interaction with multiple receptor tyrosine kinases is mediated by Grb2: an analysis of ACK1 effects on Axl signaling."
      Pao-Chun L., Chan P.M., Chan W., Manser E.
      J. Biol. Chem. 284:34954-34963(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB2 AND TNK2.
    24. Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 33-227 IN COMPLEX WITH GAS6, MUTAGENESIS OF GLU-63; GLU-66 AND THR-84, SUBUNIT.
    25. "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] MET-112; TRP-295; CYS-499 AND GLY-515.

    Entry informationi

    Entry nameiUFO_HUMAN
    AccessioniPrimary (citable) accession number: P30530
    Secondary accession number(s): Q8N5L2, Q9UD27
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 162 of the entry and version 3 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 19
      Human chromosome 19: 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