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P30530 (UFO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase receptor UFO

EC=2.7.10.1
Alternative name(s):
AXL oncogene
Gene names
Name:AXL
Synonyms:UFO
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length894 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17 Ref.18 Ref.19 Ref.22

Catalytic activity

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

Enzyme regulation

Activated by GAS6-binding and subsequent autophosphorylation. Ref.9 Ref.17

Subunit structure

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. Ref.8 Ref.9 Ref.10 Ref.13 Ref.16 Ref.20 Ref.23 Ref.24

Subcellular location

Cell membrane; Single-pass type I membrane protein Ref.7.

Tissue specificity

Highly expressed in metastatic colon tumors. Expressed in primary colon tumors. Weakly expressed in normal colon tissue. Ref.7

Post-translational modification

Monoubiquitinated upon GAS6-binding. A very small proportion of the receptor could be subjected to polyubiquitination in a very transient fashion.

Phosphorylated at tyrosine residues by autocatalysis, which activates kinase activity. Ref.10 Ref.20

Involvement in disease

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.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. AXL/UFO subfamily.

Contains 2 fibronectin type-III domains.

Contains 2 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processDifferentiation
Immunity
Innate immunity
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseOncogene
Proto-oncogene
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic cell clearance

Inferred from electronic annotation. Source: Ensembl

blood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

cell maturation

Inferred from expression pattern PubMed 19657094. Source: UniProtKB

cellular response to extracellular stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

cellular response to interferon-alpha

Inferred from direct assay PubMed 19657094. Source: UniProtKB

cellular response to lipopolysaccharide

Inferred from direct assay PubMed 19657094. Source: UniProtKB

dendritic cell differentiation

Inferred from expression pattern PubMed 19657094. Source: UniProtKB

enzyme linked receptor protein signaling pathway

Inferred from electronic annotation. Source: Ensembl

erythrocyte homeostasis

Inferred from electronic annotation. Source: Ensembl

forebrain cell migration

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

natural killer cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of dendritic cell apoptotic process

Inferred from direct assay PubMed 19657094. Source: UniProtKB

negative regulation of interferon-gamma production

Inferred from direct assay Ref.22. Source: UniProtKB

negative regulation of lymphocyte activation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

ovulation cycle

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Traceable author statement Ref.2. Source: GOC

phagocytosis

Inferred from direct assay PubMed 21501828. Source: UniProtKB

platelet activation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokine-mediated signaling pathway

Inferred from direct assay Ref.22. Source: UniProtKB

positive regulation of natural killer cell differentiation

Inferred from direct assay Ref.22. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

secretion by cell

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.2. Source: ProtInc

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

substrate adhesion-dependent cell spreading

Inferred from electronic annotation. Source: Ensembl

vagina development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from direct assay PubMed 19657094. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 20088931. Source: UniProtKB

integral component of plasma membrane

Traceable author statement Ref.2. Source: ProtInc

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylserine binding

Inferred from direct assay PubMed 21501828. Source: UniProtKB

transmembrane receptor protein tyrosine kinase activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P30530-1)

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.
Isoform Short (identifier: P30530-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 894869Tyrosine-protein kinase receptor UFO
PRO_0000024481

Regions

Topological domain26 – 451426Extracellular Potential
Transmembrane452 – 47221Helical; Potential
Topological domain473 – 894422Cytoplasmic Potential
Domain27 – 128102Ig-like C2-type 1
Domain139 – 22284Ig-like C2-type 2
Domain227 – 331105Fibronectin type-III 1
Domain336 – 42893Fibronectin type-III 2
Domain536 – 807272Protein kinase
Nucleotide binding542 – 5509ATP By similarity
Region26 – 9267Interaction with GAS6

Sites

Active site6721Proton acceptor By similarity
Binding site5671ATP By similarity

Amino acid modifications

Modified residue7031Phosphotyrosine; by autocatalysis By similarity
Modified residue7791Phosphotyrosine; by autocatalysis Ref.10 Ref.20
Modified residue8211Phosphotyrosine; by autocatalysis Ref.10 Ref.20
Modified residue8661Phosphotyrosine; by autocatalysis Ref.10 Ref.20
Modified residue8841Phosphoserine Ref.21
Glycosylation431N-linked (GlcNAc...) Potential
Glycosylation1571N-linked (GlcNAc...) Potential
Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation3391N-linked (GlcNAc...) Potential
Glycosylation3451N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential
Disulfide bond56 ↔ 117 By similarity
Disulfide bond160 ↔ 205 By similarity

Natural variations

Alternative sequence429 – 4379Missing in isoform Short.
VSP_005017
Natural variant1121T → M. Ref.25
Corresponds to variant rs35202236 [ dbSNP | Ensembl ].
VAR_045596
Natural variant2661N → D. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs7249222 [ dbSNP | Ensembl ].
VAR_057990
Natural variant2951R → W in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.25
VAR_045597
Natural variant4991R → C in a gastric adenocarcinoma sample; somatic mutation. Ref.25
VAR_041877
Natural variant5151S → G. Ref.25
VAR_041878

Experimental info

Mutagenesis631E → R: Slightly reduced affinity for GAS6. Ref.24
Mutagenesis661E → R: Reduced affinity for GAS6. Ref.24
Mutagenesis841T → R: Reduced affinity for GAS6. Ref.24
Sequence conflict3031T → P in AAB20305. Ref.3
Sequence conflict3031T → P in CAA40338. Ref.3
Sequence conflict3381E → K in AAA61243. Ref.2
Sequence conflict4301Q → E in AAB20305. Ref.3
Sequence conflict4301Q → E in CAA40338. Ref.3
Sequence conflict6391D → G in AAB20305. Ref.3
Sequence conflict6391D → G in CAA40338. Ref.3
Sequence conflict6961K → I Ref.7
Sequence conflict7641Q → R in AAH32229. Ref.5

Secondary structure

....................................... 894
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: 2C2D3574EADA4116

FASTA89498,336
        10         20         30         40         50         60 
MAWRCPRMGR VPLAWCLALC GWACMAPRGT QAEESPFVGN PGNITGARGL TGTLRCQLQV 

        70         80         90        100        110        120 
QGEPPEVHWL RDGQILELAD STQTQVPLGE DEQDDWIVVS QLRITSLQLS DTGQYQCLVF 

       130        140        150        160        170        180 
LGHQTFVSQP GYVGLEGLPY FLEEPEDRTV AANTPFNLSC QAQGPPEPVD LLWLQDAVPL 

       190        200        210        220        230        240 
ATAPGHGPQR SLHVPGLNKT SSFSCEAHNA KGVTTSRTAT ITVLPQQPRN LHLVSRQPTE 

       250        260        270        280        290        300 
LEVAWTPGLS GIYPLTHCTL QAVLSNDGMG IQAGEPDPPE EPLTSQASVP PHQLRLGSLH 

       310        320        330        340        350        360 
PHTPYHIRVA CTSSQGPSSW THWLPVETPE GVPLGPPENI SATRNGSQAF VHWQEPRAPL 

       370        380        390        400        410        420 
QGTLLGYRLA YQGQDTPEVL MDIGLRQEVT LELQGDGSVS NLTVCVAAYT AAGDGPWSLP 

       430        440        450        460        470        480 
VPLEAWRPGQ AQPVHQLVKE PSTPAFSWPW WYVLLGAVVA AACVLILALF LVHRRKKETR 

       490        500        510        520        530        540 
YGEVFEPTVE RGELVVRYRV RKSYSRRTTE ATLNSLGISE ELKEKLRDVM VDRHKVALGK 

       550        560        570        580        590        600 
TLGEGEFGAV MEGQLNQDDS ILKVAVKTMK IAICTRSELE DFLSEAVCMK EFDHPNVMRL 

       610        620        630        640        650        660 
IGVCFQGSER ESFPAPVVIL PFMKHGDLHS FLLYSRLGDQ PVYLPTQMLV KFMADIASGM 

       670        680        690        700        710        720 
EYLSTKRFIH RDLAARNCML NENMSVCVAD FGLSKKIYNG DYYRQGRIAK MPVKWIAIES 

       730        740        750        760        770        780 
LADRVYTSKS DVWSFGVTMW EIATRGQTPY PGVENSEIYD YLRQGNRLKQ PADCLDGLYA 

       790        800        810        820        830        840 
LMSRCWELNP QDRPSFTELR EDLENTLKAL PPAQEPDEIL YVNMDEGGGY PEPPGAAGGA 

       850        860        870        880        890 
DPPTQPDPKD SCSCLTAAEV HPAGRYVLCP STTPSPAQPA DRGSPAAPGQ EDGA 

« Hide

Isoform Short [UniParc].

Checksum: AFF0212BA8EAEAA1
Show »

FASTA88597,377

References

« Hide 'large scale' references
[1]"Putative tyrosine kinases expressed in K-562 human leukemia cells."
Partanen J., Maekelae T.P., Alitalo R., Lehvaeslaiho H., Alitalo K.
Proc. Natl. Acad. Sci. U.S.A. 87:8913-8917(1990) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Receptor tyrosine kinases expressed in metastatic colon cancer."
Craven R.J., Xu L.H., Weiner T.M., Fridell Y.-W., Dent G.A., Srivastava S., Varnum B., Liu E.T., Cance W.G.
Int. J. Cancer 60:791-797(1995) [PubMed] [Europe PMC] [Abstract]
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]"Tyro3 family-mediated cell entry of Ebola and Marburg viruses."
Shimojima M., Takada A., Ebihara H., Neumann G., Fujioka K., Irimura T., Jones S., Feldmann H., Kawaoka Y.
J. Virol. 80:10109-10116(2006) [PubMed] [Europe PMC] [Abstract]
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]"Structural basis for Gas6-Axl signalling."
Sasaki T., Knyazev P.G., Clout N.J., Cheburkin Y., Goehring W., Ullrich A., Timpl R., Hohenester E.
EMBO J. 25:80-87(2006) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA41527.
RefSeqNP_001690.2. NM_001699.5.
NP_068713.2. NM_021913.4.
UniGeneHs.590970.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C5DX-ray3.30C/D33-227[»]
ProteinModelPortalP30530.
SMRP30530. Positions 34-224, 491-842.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107036. 17 interactions.
IntActP30530. 7 interactions.
MINTMINT-2735752.
STRING9606.ENSP00000301178.

Chemistry

BindingDBP30530.
ChEMBLCHEMBL4895.
GuidetoPHARMACOLOGY1835.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteP30530.

Polymorphism databases

DMDM239938818.

Proteomic databases

PaxDbP30530.
PRIDEP30530.

Protocols and materials databases

DNASU558.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000301178; ENSP00000301178; ENSG00000167601. [P30530-1]
ENST00000359092; ENSP00000351995; ENSG00000167601. [P30530-2]
GeneID558.
KEGGhsa:558.
UCSCuc010ehi.1. human. [P30530-1]
uc010ehk.3. human. [P30530-2]

Organism-specific databases

CTD558.
GeneCardsGC19P041725.
HGNCHGNC:905. AXL.
HPAHPA037422.
HPA037423.
MIM109135. gene.
neXtProtNX_P30530.
PharmGKBPA25197.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000231685.
HOVERGENHBG006346.
InParanoidP30530.
KOK05115.
OMAQVQGEPP.
OrthoDBEOG77DJ5C.
PhylomeDBP30530.
TreeFamTF317402.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
SignaLinkP30530.

Gene expression databases

ArrayExpressP30530.
BgeeP30530.
CleanExHS_AXL.
GenevestigatorP30530.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR003961. 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]
PfamPF00041. fn3. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00060. FN3. 2 hits.
SM00409. IG. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50853. 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]
ProtoNetSearch...

Other

ChiTaRSAXL. human.
EvolutionaryTraceP30530.
GeneWikiAXL_receptor_tyrosine_kinase.
GenomeRNAi558.
NextBio2293.
PROP30530.
SOURCESearch...

Entry information

Entry nameUFO_HUMAN
AccessionPrimary (citable) accession number: P30530
Secondary accession number(s): Q8N5L2, Q9UD27
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: June 16, 2009
Last modified: April 16, 2014
This is version 157 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM