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P30530

- UFO_HUMAN

UniProt

P30530 - UFO_HUMAN

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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

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. 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
Complete GO annotation...

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.
ReactomeiREACT_228166. VEGFA-VEGFR2 Pathway.
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 451426ExtracellularSequence AnalysisAdd
BLAST
Transmembranei452 – 47221HelicalSequence AnalysisAdd
BLAST
Topological domaini473 – 894422CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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

BgeeiP30530.
CleanExiHS_AXL.
ExpressionAtlasiP30530. baseline and differential.
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 – 394Combined sources
Beta strandi44 – 463Combined sources
Beta strandi52 – 6312Combined sources
Beta strandi68 – 714Combined sources
Beta strandi80 – 878Combined sources
Beta strandi89 – 913Combined sources
Beta strandi94 – 10613Combined sources
Beta strandi113 – 1219Combined sources
Beta strandi124 – 1274Combined sources
Beta strandi131 – 1355Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi156 – 1638Combined sources
Beta strandi170 – 1778Combined sources
Beta strandi179 – 1835Combined sources
Beta strandi190 – 1945Combined sources
Beta strandi201 – 2099Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi219 – 2235Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C5DX-ray3.30C/D33-227[»]
4RA0X-ray3.07C/D33-227[»]
ProteinModelPortaliP30530.
SMRiP30530. Positions 34-329, 491-826.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30530.

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

        10         20         30         40         50
MAWRCPRMGR VPLAWCLALC GWACMAPRGT QAEESPFVGN PGNITGARGL
60 70 80 90 100
TGTLRCQLQV QGEPPEVHWL RDGQILELAD STQTQVPLGE DEQDDWIVVS
110 120 130 140 150
QLRITSLQLS DTGQYQCLVF LGHQTFVSQP GYVGLEGLPY FLEEPEDRTV
160 170 180 190 200
AANTPFNLSC QAQGPPEPVD LLWLQDAVPL ATAPGHGPQR SLHVPGLNKT
210 220 230 240 250
SSFSCEAHNA KGVTTSRTAT ITVLPQQPRN LHLVSRQPTE LEVAWTPGLS
260 270 280 290 300
GIYPLTHCTL QAVLSNDGMG IQAGEPDPPE EPLTSQASVP PHQLRLGSLH
310 320 330 340 350
PHTPYHIRVA CTSSQGPSSW THWLPVETPE GVPLGPPENI SATRNGSQAF
360 370 380 390 400
VHWQEPRAPL QGTLLGYRLA YQGQDTPEVL MDIGLRQEVT LELQGDGSVS
410 420 430 440 450
NLTVCVAAYT AAGDGPWSLP VPLEAWRPGQ AQPVHQLVKE PSTPAFSWPW
460 470 480 490 500
WYVLLGAVVA AACVLILALF LVHRRKKETR YGEVFEPTVE RGELVVRYRV
510 520 530 540 550
RKSYSRRTTE ATLNSLGISE ELKEKLRDVM VDRHKVALGK TLGEGEFGAV
560 570 580 590 600
MEGQLNQDDS ILKVAVKTMK IAICTRSELE DFLSEAVCMK EFDHPNVMRL
610 620 630 640 650
IGVCFQGSER ESFPAPVVIL PFMKHGDLHS FLLYSRLGDQ PVYLPTQMLV
660 670 680 690 700
KFMADIASGM EYLSTKRFIH RDLAARNCML NENMSVCVAD FGLSKKIYNG
710 720 730 740 750
DYYRQGRIAK MPVKWIAIES LADRVYTSKS DVWSFGVTMW EIATRGQTPY
760 770 780 790 800
PGVENSEIYD YLRQGNRLKQ PADCLDGLYA LMSRCWELNP QDRPSFTELR
810 820 830 840 850
EDLENTLKAL PPAQEPDEIL YVNMDEGGGY PEPPGAAGGA DPPTQPDPKD
860 870 880 890
SCSCLTAAEV HPAGRYVLCP STTPSPAQPA DRGSPAAPGQ EDGA
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000359092; ENSP00000351995; ENSG00000167601.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C5D X-ray 3.30 C/D 33-227 [» ]
4RA0 X-ray 3.07 C/D 33-227 [» ]
ProteinModelPortali P30530.
SMRi P30530. Positions 34-329, 491-826.
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 .
ENST00000359092 ; ENSP00000351995 ; ENSG00000167601 .
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.
Reactomei REACT_228166. VEGFA-VEGFR2 Pathway.
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

Bgeei P30530.
CleanExi HS_AXL.
ExpressionAtlasi P30530. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 164 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