Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P54753

- EPHB3_HUMAN

UniProt

P54753 - EPHB3_HUMAN

Protein

Ephrin type-B receptor 3

Gene

EPHB3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (27 Sep 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Generally has an overlapping and redundant function with EPHB2. Like EPHB2, functions in axon guidance during development regulating for instance the neurons forming the corpus callosum and the anterior commissure, 2 major interhemispheric connections between the temporal lobes of the cerebral cortex. In addition to its role in axon guidance plays also an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and the formation of excitatory synapses. Controls other aspects of development through regulation of cell migration and positioning. This includes angiogenesis, palate development and thymic epithelium development for instance. Forward and reverse signaling through the EFNB2/EPHB3 complex also regulate migration and adhesion of cells that tubularize the urethra and septate the cloaca. Finally, plays an important role in intestinal epithelium differentiation segregating progenitor from differentiated cells in the crypt.1 Publication

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei665 – 6651ATPPROSITE-ProRule annotation
    Active sitei758 – 7581Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi639 – 6479ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. axon guidance receptor activity Source: Ensembl
    3. ephrin receptor activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. axonal fasciculation Source: UniProtKB
    3. axon guidance Source: UniProtKB
    4. cell migration Source: UniProtKB
    5. central nervous system projection neuron axonogenesis Source: Ensembl
    6. corpus callosum development Source: UniProtKB
    7. dendritic spine development Source: UniProtKB
    8. dendritic spine morphogenesis Source: UniProtKB
    9. digestive tract morphogenesis Source: UniProtKB
    10. ephrin receptor signaling pathway Source: UniProtKB
    11. palate development Source: UniProtKB
    12. positive regulation of synapse assembly Source: UniProtKB
    13. protein autophosphorylation Source: UniProtKB
    14. regulation of axonogenesis Source: UniProtKB
    15. regulation of Cdc42 GTPase activity Source: UniProtKB
    16. regulation of cell-cell adhesion Source: UniProtKB
    17. regulation of Rac GTPase activity Source: UniProtKB
    18. retinal ganglion cell axon guidance Source: Ensembl
    19. substrate adhesion-dependent cell spreading Source: UniProtKB
    20. thymus development Source: UniProtKB
    21. urogenital system development Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Angiogenesis, Neurogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    SignaLinkiP54753.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-B receptor 3 (EC:2.7.10.1)
    Alternative name(s):
    EPH-like tyrosine kinase 2
    Short name:
    EPH-like kinase 2
    Embryonic kinase 2
    Short name:
    EK2
    Short name:
    hEK2
    Tyrosine-protein kinase TYRO6
    Gene namesi
    Name:EPHB3
    Synonyms:ETK2, HEK2, TYRO6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3394. EPHB3.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cell projectiondendrite By similarity

    GO - Cellular componenti

    1. dendrite Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi614 – 6141Y → F: Partial loss of phosphorylation and loss of interaction with SH2-containing proteins. 1 Publication
    Mutagenesisi665 – 6651K → R: Kinase-dead. Loss of autophosphorylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA27826.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 998965Ephrin type-B receptor 3PRO_0000016831Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi81 ↔ 1991 Publication
    Glycosylationi351 – 3511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi445 – 4451N-linked (GlcNAc...)Sequence Analysis
    Modified residuei614 – 6141Phosphotyrosine; by autocatalysis1 Publication

    Post-translational modificationi

    Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-614 is required for interaction with SH2 domain-containing proteins.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP54753.
    PaxDbiP54753.
    PRIDEiP54753.

    PTM databases

    PhosphoSiteiP54753.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP54753.
    BgeeiP54753.
    CleanExiHS_EPHB3.
    GenevestigatoriP54753.

    Organism-specific databases

    HPAiHPA007698.
    HPA008184.

    Interactioni

    Subunit structurei

    Heterotetramer upon binding of the ligand. The heterotetramer is composed of an ephrin dimer and a receptor dimer. Oligomerization is probably required to induce biological responses By similarity.By similarity

    Protein-protein interaction databases

    BioGridi108363. 10 interactions.
    IntActiP54753. 4 interactions.
    MINTiMINT-1538099.
    STRINGi9606.ENSP00000332118.

    Structurei

    Secondary structure

    1
    998
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi39 – 446
    Helixi45 – 473
    Beta strandi55 – 584
    Beta strandi63 – 686
    Beta strandi74 – 807
    Beta strandi85 – 873
    Beta strandi90 – 934
    Beta strandi103 – 11412
    Helixi116 – 1183
    Beta strandi130 – 13910
    Beta strandi155 – 1606
    Beta strandi175 – 1817
    Beta strandi186 – 19813
    Beta strandi200 – 21011
    Beta strandi633 – 6353
    Beta strandi648 – 6525
    Beta strandi660 – 6656
    Helixi673 – 68614
    Beta strandi697 – 7015
    Beta strandi703 – 7064
    Beta strandi708 – 7125
    Helixi719 – 7257
    Turni726 – 7283
    Helixi732 – 75120
    Helixi761 – 7633
    Beta strandi764 – 7663
    Beta strandi772 – 7743
    Helixi802 – 8043
    Helixi807 – 8126
    Helixi817 – 83216
    Turni838 – 8414
    Helixi844 – 8529
    Helixi865 – 87410
    Helixi879 – 8813
    Helixi885 – 89713
    Helixi899 – 9035

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3P1IX-ray2.10A/B/C39-211[»]
    3ZFYX-ray2.20A/B616-910[»]
    ProteinModelPortaliP54753.
    SMRiP54753. Positions 37-905, 922-992.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54753.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini34 – 559526ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini581 – 998418CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei560 – 58021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 217179Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini339 – 451113Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini452 – 54594Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini633 – 896264Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini925 – 98965SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi996 – 9983PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi199 – 336138Cys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.PROSITE-ProRule annotation
    Contains 1 Eph LBD (Eph ligand-binding) domain.PROSITE-ProRule annotation
    Contains 2 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233856.
    HOVERGENiHBG062180.
    InParanoidiP54753.
    KOiK05112.
    OMAiNLRPKFA.
    OrthoDBiEOG7VTDM6.
    PhylomeDBiP54753.
    TreeFamiTF315608.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.10. 2 hits.
    InterProiIPR027936. Eph_TM.
    IPR001090. Ephrin_rcpt_lig-bd_dom.
    IPR003961. Fibronectin_type3.
    IPR008979. Galactose-bd-like.
    IPR013783. Ig-like_fold.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016257. Tyr_kinase_ephrin_rcpt.
    IPR001426. Tyr_kinase_rcpt_V_CS.
    [Graphical view]
    PfamiPF14575. EphA2_TM. 1 hit.
    PF01404. Ephrin_lbd. 1 hit.
    PF00041. fn3. 2 hits.
    PF07699. GCC2_GCC3. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00536. SAM_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00615. EPH_lbd. 1 hit.
    SM00060. FN3. 2 hits.
    SM00454. SAM. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF49265. SSF49265. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51550. EPH_LBD. 1 hit.
    PS50853. FN3. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
    PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
    PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P54753-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARARPPPPP SPPPGLLPLL PPLLLLPLLL LPAGCRALEE TLMDTKWVTS    50
    ELAWTSHPES GWEEVSGYDE AMNPIRTYQV CNVRESSQNN WLRTGFIWRR 100
    DVQRVYVELK FTVRDCNSIP NIPGSCKETF NLFYYEADSD VASASSPFWM 150
    ENPYVKVDTI APDESFSRLD AGRVNTKVRS FGPLSKAGFY LAFQDQGACM 200
    SLISVRAFYK KCASTTAGFA LFPETLTGAE PTSLVIAPGT CIPNAVEVSV 250
    PLKLYCNGDG EWMVPVGACT CATGHEPAAK ESQCRPCPPG SYKAKQGEGP 300
    CLPCPPNSRT TSPAASICTC HNNFYRADSD SADSACTTVP SPPRGVISNV 350
    NETSLILEWS EPRDLGGRDD LLYNVICKKC HGAGGASACS RCDDNVEFVP 400
    RQLGLTERRV HISHLLAHTR YTFEVQAVNG VSGKSPLPPR YAAVNITTNQ 450
    AAPSEVPTLR LHSSSGSSLT LSWAPPERPN GVILDYEMKY FEKSEGIAST 500
    VTSQMNSVQL DGLRPDARYV VQVRARTVAG YGQYSRPAEF ETTSERGSGA 550
    QQLQEQLPLI VGSATAGLVF VVAVVVIAIV CLRKQRHGSD SEYTEKLQQY 600
    IAPGMKVYID PFTYEDPNEA VREFAKEIDV SCVKIEEVIG AGEFGEVCRG 650
    RLKQPGRREV FVAIKTLKVG YTERQRRDFL SEASIMGQFD HPNIIRLEGV 700
    VTKSRPVMIL TEFMENCALD SFLRLNDGQF TVIQLVGMLR GIAAGMKYLS 750
    EMNYVHRDLA ARNILVNSNL VCKVSDFGLS RFLEDDPSDP TYTSSLGGKI 800
    PIRWTAPEAI AYRKFTSASD VWSYGIVMWE VMSYGERPYW DMSNQDVINA 850
    VEQDYRLPPP MDCPTALHQL MLDCWVRDRN LRPKFSQIVN TLDKLIRNAA 900
    SLKVIASAQS GMSQPLLDRT VPDYTTFTTV GDWLDAIKMG RYKESFVSAG 950
    FASFDLVAQM TAEDLLRIGV TLAGHQKKIL SSIQDMRLQM NQTLPVQV 998
    Length:998
    Mass (Da):110,330
    Last modified:September 27, 2005 - v2
    Checksum:i9B65A4EF58B27407
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti367 – 3671G → V in CAA53021. (PubMed:8397371)Curated
    Sequence conflicti406 – 4083TER → SEP in CAA53021. (PubMed:8397371)Curated
    Sequence conflicti412 – 4121I → T in CAA53021. (PubMed:8397371)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti168 – 1681R → L in a lung small cell carcinoma sample; somatic mutation. 1 Publication
    VAR_042176
    Natural varianti440 – 4401R → C.1 Publication
    Corresponds to variant rs56029711 [ dbSNP | Ensembl ].
    VAR_042177
    Natural varianti579 – 5791I → V.1 Publication
    Corresponds to variant rs56103851 [ dbSNP | Ensembl ].
    VAR_042178
    Natural varianti601 – 6011I → L.1 Publication
    Corresponds to variant rs56129875 [ dbSNP | Ensembl ].
    VAR_042179
    Natural varianti724 – 7241R → W in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
    VAR_042180

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75208 mRNA. Translation: CAA53021.1.
    BC052968 mRNA. Translation: AAH52968.1.
    CCDSiCCDS3268.1.
    PIRiS37627.
    RefSeqiNP_004434.2. NM_004443.3.
    UniGeneiHs.2913.

    Genome annotation databases

    EnsembliENST00000330394; ENSP00000332118; ENSG00000182580.
    GeneIDi2049.
    KEGGihsa:2049.
    UCSCiuc003foz.3. human.

    Polymorphism databases

    DMDMi76803655.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75208 mRNA. Translation: CAA53021.1 .
    BC052968 mRNA. Translation: AAH52968.1 .
    CCDSi CCDS3268.1.
    PIRi S37627.
    RefSeqi NP_004434.2. NM_004443.3.
    UniGenei Hs.2913.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3P1I X-ray 2.10 A/B/C 39-211 [» ]
    3ZFY X-ray 2.20 A/B 616-910 [» ]
    ProteinModelPortali P54753.
    SMRi P54753. Positions 37-905, 922-992.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108363. 10 interactions.
    IntActi P54753. 4 interactions.
    MINTi MINT-1538099.
    STRINGi 9606.ENSP00000332118.

    Chemistry

    BindingDBi P54753.
    ChEMBLi CHEMBL2363043.
    GuidetoPHARMACOLOGYi 1832.

    PTM databases

    PhosphoSitei P54753.

    Polymorphism databases

    DMDMi 76803655.

    Proteomic databases

    MaxQBi P54753.
    PaxDbi P54753.
    PRIDEi P54753.

    Protocols and materials databases

    DNASUi 2049.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330394 ; ENSP00000332118 ; ENSG00000182580 .
    GeneIDi 2049.
    KEGGi hsa:2049.
    UCSCi uc003foz.3. human.

    Organism-specific databases

    CTDi 2049.
    GeneCardsi GC03P184279.
    HGNCi HGNC:3394. EPHB3.
    HPAi HPA007698.
    HPA008184.
    MIMi 601839. gene.
    neXtProti NX_P54753.
    PharmGKBi PA27826.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi P54753.
    KOi K05112.
    OMAi NLRPKFA.
    OrthoDBi EOG7VTDM6.
    PhylomeDBi P54753.
    TreeFami TF315608.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    SignaLinki P54753.

    Miscellaneous databases

    EvolutionaryTracei P54753.
    GeneWikii EPHB3.
    GenomeRNAii 2049.
    NextBioi 8331.
    PROi P54753.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54753.
    Bgeei P54753.
    CleanExi HS_EPHB3.
    Genevestigatori P54753.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    2.60.120.260. 1 hit.
    2.60.40.10. 2 hits.
    InterProi IPR027936. Eph_TM.
    IPR001090. Ephrin_rcpt_lig-bd_dom.
    IPR003961. Fibronectin_type3.
    IPR008979. Galactose-bd-like.
    IPR013783. Ig-like_fold.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR011641. Tyr-kin_ephrin_A/B_rcpt-like.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR016257. Tyr_kinase_ephrin_rcpt.
    IPR001426. Tyr_kinase_rcpt_V_CS.
    [Graphical view ]
    Pfami PF14575. EphA2_TM. 1 hit.
    PF01404. Ephrin_lbd. 1 hit.
    PF00041. fn3. 2 hits.
    PF07699. GCC2_GCC3. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00536. SAM_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000666. TyrPK_ephrin_receptor. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00615. EPH_lbd. 1 hit.
    SM00060. FN3. 2 hits.
    SM00454. SAM. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF49265. SSF49265. 1 hit.
    SSF49785. SSF49785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS51550. EPH_LBD. 1 hit.
    PS50853. FN3. 2 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS00790. RECEPTOR_TYR_KIN_V_1. 1 hit.
    PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
    PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PCR mediated detection of a new human receptor-tyrosine-kinase, HEK 2."
      Boehme B., Holtrich U., Wolf G., Luzius H., Grzeschik K.-H., Strebhardt K., Ruebsamen-Waigmann H.
      Oncogene 8:2857-2862(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION OF EFNB1 AND EFNB2 AS LIGANDS, AUTOPHOSPHORYLATION.
      Tissue: Embryo.
    2. "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].
      Tissue: Uterus.
    3. "Unified nomenclature for Eph family receptors and their ligands, the ephrins."
      Eph nomenclature committee
      Cell 90:403-404(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    4. "Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions."
      Hock B., Boehme B., Karn T., Feller S., Ruebsamen-Waigmann H., Strebhardt K.
      Oncogene 17:255-260(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-614, MUTAGENESIS OF TYR-614 AND LYS-665.
    5. "Inhibition of integrin-mediated cell adhesion but not directional cell migration requires catalytic activity of EphB3 receptor tyrosine kinase. Role of Rho family small GTPases."
      Miao H., Strebhardt K., Pasquale E.B., Shen T.L., Guan J.L., Wang B.
      J. Biol. Chem. 280:923-932(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOPHOSPHORYLATION, FUNCTION IN CELL ADHESION, FUNCTION IN CELL MIGRATION, SUBCELLULAR LOCATION.
    6. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Ligand binding domain of human EPHB3."
      Structural genomics consortium (SGC)
      Submitted (JAN-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 39-211, DISULFIDE BOND.
    8. "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] LEU-168; CYS-440; VAL-579; LEU-601 AND TRP-724.

    Entry informationi

    Entry nameiEPHB3_HUMAN
    AccessioniPrimary (citable) accession number: P54753
    Secondary accession number(s): Q7Z740
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: September 27, 2005
    Last modified: October 1, 2014
    This is version 150 of the entry and version 2 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 3
      Human chromosome 3: 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