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Q06418

- TYRO3_HUMAN

UniProt

Q06418 - TYRO3_HUMAN

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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

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 tyrosine kinase activity Source: UniProtKB
  4. receptor signaling protein tyrosine kinase activity Source: UniProtKB
  5. 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini41 – 429389ExtracellularSequence AnalysisAdd
BLAST
Transmembranei430 – 45021HelicalSequence AnalysisAdd
BLAST
Topological domaini451 – 890440CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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

MaxQBiQ06418.
PaxDbiQ06418.
PRIDEiQ06418.

PTM databases

PhosphoSiteiQ06418.

Expressioni

Tissue specificityi

Abundant in the brain and lower levels in other tissues.

Gene expression databases

BgeeiQ06418.
CleanExiHS_TYRO3.
ExpressionAtlasiQ06418. baseline and differential.
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. 14 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 – 556Combined sources
Beta strandi60 – 689Combined sources
Beta strandi74 – 785Combined sources
Beta strandi85 – 9410Combined sources
Beta strandi97 – 10610Combined sources
Helixi109 – 1113Combined sources
Beta strandi113 – 1219Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi140 – 1434Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi156 – 1638Combined sources
Beta strandi165 – 1673Combined sources
Beta strandi170 – 1756Combined sources
Beta strandi183 – 19210Combined sources
Beta strandi199 – 2079Combined sources
Beta strandi210 – 2134Combined sources
Beta strandi217 – 2215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RHFX-ray1.96A/B41-222[»]
ProteinModelPortaliQ06418.
SMRiQ06418. Positions 47-410, 468-792.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06418.

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.
GeneTreeiENSGT00770000120499.
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

        10         20         30         40         50
MALRRSMGRP GLPPLPLPPP PRLGLLLAAL ASLLLPESAA AGLKLMGAPV
60 70 80 90 100
KLTVSQGQPV KLNCSVEGME EPDIQWVKDG AVVQNLDQLY IPVSEQHWIG
110 120 130 140 150
FLSLKSVERS DAGRYWCQVE DGGETEISQP VWLTVEGVPF FTVEPKDLAV
160 170 180 190 200
PPNAPFQLSC EAVGPPEPVT IVWWRGTTKI GGPAPSPSVL NVTGVTQSTM
210 220 230 240 250
FSCEAHNLKG LASSRTATVH LQALPAAPFN ITVTKLSSSN ASVAWMPGAD
260 270 280 290 300
GRALLQSCTV QVTQAPGGWE VLAVVVPVPP FTCLLRDLVP ATNYSLRVRC
310 320 330 340 350
ANALGPSPYA DWVPFQTKGL APASAPQNLH AIRTDSGLIL EWEEVIPEAP
360 370 380 390 400
LEGPLGPYKL SWVQDNGTQD ELTVEGTRAN LTGWDPQKDL IVRVCVSNAV
410 420 430 440 450
GCGPWSQPLV VSSHDRAGQQ GPPHSRTSWV PVVLGVLTAL VTAAALALIL
460 470 480 490 500
LRKRRKETRF GQAFDSVMAR GEPAVHFRAA RSFNRERPER IEATLDSLGI
510 520 530 540 550
SDELKEKLED VLIPEQQFTL GRMLGKGEFG SVREAQLKQE DGSFVKVAVK
560 570 580 590 600
MLKADIIASS DIEEFLREAA CMKEFDHPHV AKLVGVSLRS RAKGRLPIPM
610 620 630 640 650
VILPFMKHGD LHAFLLASRI GENPFNLPLQ TLIRFMVDIA CGMEYLSSRN
660 670 680 690 700
FIHRDLAARN CMLAEDMTVC VADFGLSRKI YSGDYYRQGC ASKLPVKWLA
710 720 730 740 750
LESLADNLYT VQSDVWAFGV TMWEIMTRGQ TPYAGIENAE IYNYLIGGNR
760 770 780 790 800
LKQPPECMED VYDLMYQCWS ADPKQRPSFT CLRMELENIL GQLSVLSASQ
810 820 830 840 850
DPLYINIERA EEPTAGGSLE LPGRDQPYSG AGDGSGMGAV GGTPSDCRYI
860 870 880 890
LTPGGLAEQP GQAEHQPESP LNETQRLLLL QQGLLPHSSC
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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, 468-792.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113152. 14 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

MaxQBi Q06418.
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.
GeneTreei ENSGT00770000120499.
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

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

Gene expression databases

Bgeei Q06418.
CleanExi HS_TYRO3.
ExpressionAtlasi Q06418. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 153 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

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