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P54754

- EPHB3_MOUSE

UniProt

P54754 - EPHB3_MOUSE

Protein

Ephrin type-B receptor 3

Gene

Ephb3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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.6 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 sitei660 – 6601ATPPROSITE-ProRule annotation
    Active sitei753 – 7531Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi634 – 6429ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    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: MGI
    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: MGI
    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. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-B receptor 3 (EC:2.7.10.1)
    Alternative name(s):
    Developmental kinase 5
    Short name:
    mDK-5
    Tyrosine-protein kinase receptor SEK-4
    Gene namesi
    Name:Ephb3
    Synonyms:Etk2, Mdk5, Sek4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:104770. Ephb3.

    Subcellular locationi

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

    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

    Disruption phenotypei

    Mice are viable and fertile and show no obvious abnormal behavior. The corpus callosum, the main axon tract connecting the left and right cerebral hemispheres, is not formed in a significant fraction of newborns. This is associated with defects in guidance of callosal axons across the midline.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 993964Ephrin type-B receptor 3PRO_0000016832Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi73 ↔ 191By similarity
    Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
    Modified residuei609 – 6091Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Phosphorylated. Autophosphorylates upon ligand-binding. Autophosphorylation on Tyr-609 is required for interaction with SH2 domain-containing proteins By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP54754.
    PaxDbiP54754.
    PRIDEiP54754.

    PTM databases

    PhosphoSiteiP54754.

    Expressioni

    Tissue specificityi

    Expressed in cells of the retinal ganglion cell layer during retinal axon guidance to the optic disk. Expressed by Paneth and progenitor cells in the crypts of the intestinal epithelium (at protein level).2 Publications

    Developmental stagei

    Expressed during development in yolk sacs and by embryonic endothelial cells. Expressed in the developing intestinal epithelium at the bottom of the intervillus pockets where undifferentiated cells are allocated (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiP54754.
    BgeeiP54754.
    CleanExiMM_EPHB3.
    GenevestigatoriP54754.

    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

    BioGridi199477. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP54754.
    SMRiP54754. Positions 29-537, 543-899, 917-987.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 554525ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini576 – 993418CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei555 – 57521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 209179Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini331 – 446116Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini447 – 54094Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini628 – 891264Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini920 – 98465SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi991 – 9933PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi191 – 328138Cys-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.
    GeneTreeiENSGT00740000115081.
    HOGENOMiHOG000233856.
    HOVERGENiHBG062180.
    InParanoidiQ91YS9.
    KOiK05112.
    OMAiNLRPKFA.
    OrthoDBiEOG7VTDM6.
    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.

    P54754-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGARPPPGL LPLLAPLLLP LLLPAGCWAL EETLMDTKWV TSELAWTSHP    50
    ESGWEEVSGY DEAMNPIRTY QVCNVRESSQ NNWLRTGFIW RREVQRVYVE 100
    LKFTVRDCNS IPNIPGSCKE TFNLFYYEAD SDVASASSPF WMENPYVKVD 150
    TIAPDESFSR LDAGRVNTKV RSFGPLSKAG FYLAFQDQGA CMSLISVRAF 200
    YKKCASTTAG FALFPETLTG AEPTSLVIAP GTCIANAVEV SVPLKLYCNG 250
    DGEWMVPVGA CTCATGHEPA AKESQCRACP PGSYKAKQGE GPCLPCPPNS 300
    RTTSPAASIC TCHNNFYRAD SDSADSACTT VPSPPRGVIS NVNETSLILE 350
    WSEPRDLGGR DDLLYNVICK KCRGSSGAGG PATCSRCDDN VEFVPRQLGL 400
    TERRVHISHL LAHTRYTFEV QAVNGVSGKS PLPPRYAAVN ITTNQAAPSE 450
    VPTLHLHSSS GSSLTLSWAP PERPNGVILD YEMKYFEKSK GIASTVTSQK 500
    NSVQLDGLQP DARYVVQVRA RTVAGYGQYS HPAEFETTSE RGSGAQQLQE 550
    QLPLIVGSTV AGFVFMVVVV VIALVCLRKQ RHGPDAEYTE KLQQYIAPGM 600
    KVYIDPFTYE DPNEAVREFA KEIDVSCVKI EEVIGAGEFG EVCRGRLKLP 650
    GRREVFVAIK TLKVGYTERQ RRDFLSEASI MGQFDHPNII RLEGVVTKSR 700
    PVMILTEFME NCALDSFLRL NDGQFTVIQL VGMLRGIAAG MKYLSEMNYV 750
    HRDLAARNIL VNSNLVCKVS DFGLSRFLED DPSDPTYTSS LGGKIPIRWT 800
    APEAIAYRKF TSASDVWSYG IVMWEVMSYG ERPYWDMSNQ DVINAVEQDY 850
    RLPPPMDCPT ALHQLMLDCW VRDRNLRPKF SQIVNTLDKL IRNAASLKVT 900
    ASAPSGMSQP LLDRTVPDYT TFTTVGDWLD AIKMGRYKES FVGAGFASFD 950
    LVAQMTAEDL LRIGVTLAGH QKKILCSIQD MRLQMNQTLP VQV 993
    Length:993
    Mass (Da):109,662
    Last modified:July 27, 2011 - v2
    Checksum:i07C6EF2AC98AE1B4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti200 – 2012FY → GD in CAA88910. (PubMed:7478528)Curated
    Sequence conflicti331 – 3311V → E in CAA88910. (PubMed:7478528)Curated
    Sequence conflicti567 – 5671V → M in CAA88910. (PubMed:7478528)Curated
    Sequence conflicti719 – 7191R → Q in CAA53599. (PubMed:7947319)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49086 mRNA. Translation: CAA88910.1.
    BC014822 mRNA. Translation: AAH14822.1.
    BC053085 mRNA. Translation: AAH53085.1.
    X76012 mRNA. Translation: CAA53599.1.
    CCDSiCCDS28060.1.
    PIRiI48653.
    I48761.
    RefSeqiNP_034273.1. NM_010143.1.
    UniGeneiMm.6972.

    Genome annotation databases

    EnsembliENSMUST00000006112; ENSMUSP00000006112; ENSMUSG00000005958.
    GeneIDi13845.
    KEGGimmu:13845.
    UCSCiuc007yrg.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49086 mRNA. Translation: CAA88910.1 .
    BC014822 mRNA. Translation: AAH14822.1 .
    BC053085 mRNA. Translation: AAH53085.1 .
    X76012 mRNA. Translation: CAA53599.1 .
    CCDSi CCDS28060.1.
    PIRi I48653.
    I48761.
    RefSeqi NP_034273.1. NM_010143.1.
    UniGenei Mm.6972.

    3D structure databases

    ProteinModelPortali P54754.
    SMRi P54754. Positions 29-537, 543-899, 917-987.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199477. 1 interaction.

    PTM databases

    PhosphoSitei P54754.

    Proteomic databases

    MaxQBi P54754.
    PaxDbi P54754.
    PRIDEi P54754.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000006112 ; ENSMUSP00000006112 ; ENSMUSG00000005958 .
    GeneIDi 13845.
    KEGGi mmu:13845.
    UCSCi uc007yrg.1. mouse.

    Organism-specific databases

    CTDi 2049.
    MGIi MGI:104770. Ephb3.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115081.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi Q91YS9.
    KOi K05112.
    OMAi NLRPKFA.
    OrthoDBi EOG7VTDM6.
    TreeFami TF315608.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.

    Miscellaneous databases

    NextBioi 284688.
    PROi P54754.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54754.
    Bgeei P54754.
    CleanExi MM_EPHB3.
    Genevestigatori P54754.

    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. "Cloning, characterization, and differential expression of MDK2 and MDK5, two novel receptor tyrosine kinases of the eck/eph family."
      Ciossek T., Lerch M.M., Ullrich A.
      Oncogene 11:2085-2095(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      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].
      Strain: C57BL/6 and FVB/N.
      Tissue: Brain and Mammary tumor.
    3. "Several receptor tyrosine kinase genes of the Eph family are segmentally expressed in the developing hindbrain."
      Becker N., Seitanidou T., Murphy P., Mattei M.-G., Topilko P., Nieto A., Wilkinson D.G., Charnay P., Gilardi P.
      Mech. Dev. 47:3-17(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 719-993.
      Strain: BALB/c.
      Tissue: Brain.
    4. "Sek4 and Nuk receptors cooperate in guidance of commissural axons and in palate formation."
      Orioli D., Henkemeyer M., Lemke G., Klein R., Pawson T.
      EMBO J. 15:6035-6049(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN AXON GUIDANCE, FUNCTION IN PALATE DEVELOPMENT.
    5. "Roles of ephrinB ligands and EphB receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis."
      Adams R.H., Wilkinson G.A., Weiss C., Diella F., Gale N.W., Deutsch U., Risau W., Klein R.
      Genes Dev. 13:295-306(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS, DEVELOPMENTAL STAGE.
    6. "Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons."
      Imondi R., Wideman C., Kaprielian Z.
      Development 127:1397-1410(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Beta-catenin and TCF mediate cell positioning in the intestinal epithelium by controlling the expression of EphB/ephrinB."
      Batlle E., Henderson J.T., Beghtel H., van den Born M.M., Sancho E., Huls G., Meeldijk J., Robertson J., van de Wetering M., Pawson T., Clevers H.
      Cell 111:251-263(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN INTESTINAL EPITHELIUM DIFFERENTIATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    8. "Multiple EphB receptor tyrosine kinases shape dendritic spines in the hippocampus."
      Henkemeyer M., Itkis O.S., Ngo M., Hickmott P.W., Ethell I.M.
      J. Cell Biol. 163:1313-1326(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DENDRITIC SPINE DEVELOPMENT, FUNCTION IN EXCITATORY SYNAPSE FORMATION, SUBCELLULAR LOCATION.
    9. "Bidirectional signaling mediated by ephrin-B2 and EphB2 controls urorectal development."
      Dravis C., Yokoyama N., Chumley M.J., Cowan C.A., Silvany R.E., Shay J., Baker L.A., Henkemeyer M.
      Dev. Biol. 271:272-290(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN URORECTAL DEVELOPMENT.
    10. "On the role of Eph signalling in thymus histogenesis; EphB2/B3 and the organizing of the thymic epithelial network."
      Garcia-Ceca J., Jimenez E., Alfaro D., Cejalvo T., Chumley M.J., Henkemeyer M., Munoz J.J., Zapata A.G.
      Int. J. Dev. Biol. 53:971-982(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THYMUS DEVELOPMENT.

    Entry informationi

    Entry nameiEPHB3_MOUSE
    AccessioniPrimary (citable) accession number: P54754
    Secondary accession number(s): Q62214, Q91YS9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3