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Q8CBF3

- EPHB1_MOUSE

UniProt

Q8CBF3 - EPHB1_MOUSE

Protein

Ephrin type-B receptor 1

Gene

Ephb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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. Cognate/functional ephrin ligands for this receptor include EFNB1, EFNB2 and EFNB3. During nervous system development, regulates retinal axon guidance redirecting ipsilaterally ventrotemporal retinal ganglion cells axons at the optic chiasm midline. This probably requires repulsive interaction with EFNB2. In the adult nervous system together with EFNB3, regulates chemotaxis, proliferation and polarity of the hippocampus neural progenitors. 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 synapse formation. May also regulate angiogenesis. More generally, may play a role in targeted cell migration and adhesion. Upon activation by EFNB1 and probably other ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively.4 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 sitei651 – 6511ATPPROSITE-ProRule annotation
    Active sitei744 – 7441Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi625 – 6339ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. axon guidance Source: MGI
    3. camera-type eye morphogenesis Source: MGI
    4. cell chemotaxis Source: UniProtKB
    5. cell-substrate adhesion Source: UniProtKB
    6. central nervous system projection neuron axonogenesis Source: MGI
    7. cranial nerve development Source: MGI
    8. dendritic spine development Source: UniProtKB
    9. dendritic spine morphogenesis Source: UniProtKB
    10. detection of temperature stimulus involved in sensory perception of pain Source: UniProtKB
    11. ephrin receptor signaling pathway Source: UniProtKB
    12. establishment of cell polarity Source: UniProtKB
    13. neural precursor cell proliferation Source: UniProtKB
    14. neurogenesis Source: UniProtKB
    15. optic nerve morphogenesis Source: MGI
    16. positive regulation of synapse assembly Source: UniProtKB
    17. protein autophosphorylation Source: UniProtKB
    18. regulation of ERK1 and ERK2 cascade Source: UniProtKB
    19. regulation of JNK cascade Source: UniProtKB
    20. retinal ganglion cell axon guidance Source: MGI

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell adhesion, Neurogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-B receptor 1 (EC:2.7.10.1)
    Gene namesi
    Name:Ephb1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1096337. Ephb1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. axon Source: MGI
    2. cytoplasm Source: MGI
    3. dendrite Source: UniProtKB-SubCell
    4. early endosome membrane Source: UniProtKB
    5. integral component of plasma membrane Source: UniProtKB
    6. membrane Source: MGI
    7. membrane raft Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Endosome, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice development is apparently normal. However, they display a dramatic reduction of ipsilateral retinal projection. Mice do not develop neuropathic algesia and physical dependence to morphine.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 984967Ephrin type-B receptor 1PRO_0000260317Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi426 – 4261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence Analysis
    Modified residuei928 – 9281Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Phosphorylated. Autophosphorylation is stimulated by the ligand EFNB1. Required for interaction with SH2 domain-containing interactors, for activation of the MAPK/ERK and JUN signaling cascades and for ubiquitination by CBL By similarity.By similarity
    Ubiquitinated; (EFNB1)ligand-induced poly- and/or multi-ubiquitination by CBL is regulated by SRC and leads to lysosomal degradation.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ8CBF3.
    PRIDEiQ8CBF3.

    PTM databases

    PhosphoSiteiQ8CBF3.

    Expressioni

    Tissue specificityi

    Expressed in neural stem and progenitor cells in the dentate gyrus.1 Publication

    Developmental stagei

    Expressed in growth cones of ventrotemporal (uncrossed) retinal ganglion cells that give rise to ipsilateral projections (at protein level).2 Publications

    Gene expression databases

    BgeeiQ8CBF3.
    CleanExiMM_EPHB1.
    GenevestigatoriQ8CBF3.

    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. Interacts with EPHB6; transphosphorylates EPHB6 to form an active signaling complex By similarity. Interacts with PICK1. Interacts (through Tyr-594) with NCK1 (via SH2 domain); activates the JUN cascade to regulate cell adhesion. The ligand-activated form interacts (through Tyr-928) with GRB7 and GRB10 (via SH2 domains). The ligand-activated form interacts (residues within the catalytic domain) with GRB2 (via SH2 domain). Interacts with GRB2, SHC1 and SRC; activates the MAPK/ERK cascade to regulate cell migration. Interacts with CBL; regulates receptor degradation through ubiquitination. Interacts with ACP1.By similarity5 Publications

    Protein-protein interaction databases

    BioGridi234781. 1 interaction.
    IntActiQ8CBF3. 1 interaction.
    STRINGi10090.ENSMUSP00000035129.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CBF3.
    SMRiQ8CBF3. Positions 17-528, 606-984.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini18 – 540523ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini564 – 984421CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei541 – 56323HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 201183Eph LBDPROSITE-ProRule annotationAdd
    BLAST
    Domaini322 – 432111Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini433 – 52896Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini619 – 882264Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini911 – 97565SAMPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi982 – 9843PDZ-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi183 – 319137Cys-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.
    InParanoidiQ8CBF3.
    KOiK05110.
    OMAiTLMDTRT.
    OrthoDBiEOG7VTDM6.
    PhylomeDBiQ8CBF3.
    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.
    IPR009030. Growth_fac_rcpt_N_dom.
    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.
    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.
    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.
    SSF57184. SSF57184. 2 hits.
    PROSITEiPS01186. EGF_2. 1 hit.
    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]

    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 1 (identifier: Q8CBF3-1) [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

    MALDCLLLFL LASAVAAMEE TLMDTRTATA ELGWTANPAS GWEEVSGYDE    50
    NLNTIRTYQV CNVFEPNQNN WLLTTFINRR GAHRIYTEMR FTVRDCSSLP 100
    NVPGSCKETF NLYYYETDSV IATKKSAFWS EAPYLKVDTI AADESFSQVD 150
    FGGRLMKVNT EVRSFGPLTR NGFYLAFQDY GACMSLLSVR VFFKKCPSIV 200
    QNFAVFPETM TGAESTSLVI ARGTCIPNAE EVDVPIKLYC NGDGEWMVPI 250
    GRCTCKPGYE PENSVACKAC PAGTFKASQE AEGCSHCPSN SRSPSEASPI 300
    CTCRTGYYRA DFDPPEVACT SVPSGPRNVI SIVNETSIIL EWHPPRETGG 350
    RDDVTYNIIC KKCRADRRSC SRCDDNVEFV PRQLGLTECR VSISSLWAHT 400
    PYTFDIQAIN GVSSKSPFPP QHVSVNITTN QAAPSTVPIM HQVSATMRSI 450
    TLSWPQPEQP NGIILDYEIR YYEKEHNEFN SSMARSQTNT ARIDGLRPGM 500
    VYVVQVRART VAGYGKFSGK MCFQTLTDDD YKSELREQLP LIAGSAAAGV 550
    VFVVSLVAIS IVCSRKRAYS KEAAYSDKLQ HYSTGRGSPG MKIYIDPFTY 600
    EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI 650
    KTLKAGYSEK QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM 700
    ENGALDSFLR QNDGQFTVIQ LVGMLRGIAA GMKYLSEMNY VHRDLAARNI 750
    LVNSNLVCKV SDFGLSRYLQ DDTSDPTYTS SLGGKIPVRW TAPEAIAYRK 800
    FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD YRLPPPMDCP 850
    AALHQLMLDC WQKDRNSRPR FAEIVNTLDK MIRNPASLKT VATITAVPSQ 900
    PLLDRSIPDF TAFTTVDDWL SAIKMVQYRD SFLTAGFTSL QLVTQMTSED 950
    LLRIGVTLAG HQKKILSSIH SMRVQMNQSP SVMA 984
    Length:984
    Mass (Da):109,881
    Last modified:March 1, 2003 - v1
    Checksum:iE967019C82AA400A
    GO
    Isoform 2 (identifier: Q8CBF3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         588-628: Missing.

    Show »
    Length:943
    Mass (Da):105,294
    Checksum:iEF28BF1D7FE097C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti72 – 721L → Q in BAE22386. (PubMed:16141072)Curated
    Sequence conflicti187 – 1871L → P in BAE22386. (PubMed:16141072)Curated
    Sequence conflicti194 – 1941K → I in AAH57301. (PubMed:15489334)Curated
    Sequence conflicti641 – 6411P → Q in BAC29348. (PubMed:16141072)Curated
    Sequence conflicti678 – 6781P → R in AAH57301. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei588 – 62841Missing in isoform 2. 1 PublicationVSP_021595Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK036148 mRNA. Translation: BAC29320.1.
    AK036211 mRNA. Translation: BAC29348.1.
    AK135018 mRNA. Translation: BAE22386.1.
    CT025594
    , AC109247, AC132684, AC156635 Genomic DNA. Translation: CAM23741.1.
    BC057301 mRNA. Translation: AAH57301.1.
    CCDSiCCDS40742.1. [Q8CBF3-1]
    CCDS52901.1. [Q8CBF3-2]
    RefSeqiNP_001161768.1. NM_001168296.1. [Q8CBF3-2]
    NP_775623.3. NM_173447.3. [Q8CBF3-1]
    UniGeneiMm.22897.

    Genome annotation databases

    EnsembliENSMUST00000035129; ENSMUSP00000035129; ENSMUSG00000032537. [Q8CBF3-1]
    ENSMUST00000085169; ENSMUSP00000082261; ENSMUSG00000032537. [Q8CBF3-2]
    GeneIDi270190.
    KEGGimmu:270190.
    UCSCiuc009rfn.2. mouse. [Q8CBF3-1]
    uc012gzg.1. mouse. [Q8CBF3-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK036148 mRNA. Translation: BAC29320.1 .
    AK036211 mRNA. Translation: BAC29348.1 .
    AK135018 mRNA. Translation: BAE22386.1 .
    CT025594
    , AC109247 , AC132684 , AC156635 Genomic DNA. Translation: CAM23741.1 .
    BC057301 mRNA. Translation: AAH57301.1 .
    CCDSi CCDS40742.1. [Q8CBF3-1 ]
    CCDS52901.1. [Q8CBF3-2 ]
    RefSeqi NP_001161768.1. NM_001168296.1. [Q8CBF3-2 ]
    NP_775623.3. NM_173447.3. [Q8CBF3-1 ]
    UniGenei Mm.22897.

    3D structure databases

    ProteinModelPortali Q8CBF3.
    SMRi Q8CBF3. Positions 17-528, 606-984.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 234781. 1 interaction.
    IntActi Q8CBF3. 1 interaction.
    STRINGi 10090.ENSMUSP00000035129.

    PTM databases

    PhosphoSitei Q8CBF3.

    Proteomic databases

    PaxDbi Q8CBF3.
    PRIDEi Q8CBF3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000035129 ; ENSMUSP00000035129 ; ENSMUSG00000032537 . [Q8CBF3-1 ]
    ENSMUST00000085169 ; ENSMUSP00000082261 ; ENSMUSG00000032537 . [Q8CBF3-2 ]
    GeneIDi 270190.
    KEGGi mmu:270190.
    UCSCi uc009rfn.2. mouse. [Q8CBF3-1 ]
    uc012gzg.1. mouse. [Q8CBF3-2 ]

    Organism-specific databases

    CTDi 2047.
    MGIi MGI:1096337. Ephb1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115081.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi Q8CBF3.
    KOi K05110.
    OMAi TLMDTRT.
    OrthoDBi EOG7VTDM6.
    PhylomeDBi Q8CBF3.
    TreeFami TF315608.

    Miscellaneous databases

    NextBioi 393293.
    PROi Q8CBF3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8CBF3.
    CleanExi MM_EPHB1.
    Genevestigatori Q8CBF3.

    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.
    IPR009030. Growth_fac_rcpt_N_dom.
    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.
    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.
    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.
    SSF57184. SSF57184. 2 hits.
    PROSITEi PS01186. EGF_2. 1 hit.
    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Cerebellum and Olfactory bulb.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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 1).
      Strain: C57BL/6.
      Tissue: Brain.
    4. "Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase."
      Stein E., Huynh-Do U., Lane A.A., Cerretti D.P., Daniel T.O.
      J. Biol. Chem. 273:1303-1308(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCK1.
      Tissue: Kidney.
    5. "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands."
      Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N., Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D.
      Neuron 21:1453-1463(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PICK1.
    6. "EphB1 associates with Grb7 and regulates cell migration."
      Han D.C., Shen T.L., Miao H., Wang B., Guan J.L.
      J. Biol. Chem. 277:45655-45661(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB7.
    7. "EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis."
      Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.
      J. Cell Biol. 162:661-671(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB2; SHC1 AND SRC.
    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. "Ephrin-B2 and EphB1 mediate retinal axon divergence at the optic chiasm."
      Williams S.E., Mann F., Erskine L., Sakurai T., Wei S., Rossi D.J., Gale N.W., Holt C.E., Mason C.A., Henkemeyer M.
      Neuron 39:919-935(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN RETINAL GLANGLION CELL AXON GUIDANCE, DEVELOPMENTAL STAGE.
    10. "EphB receptors regulate stem/progenitor cell proliferation, migration, and polarity during hippocampal neurogenesis."
      Chumley M.J., Catchpole T., Silvany R.E., Kernie S.G., Henkemeyer M.
      J. Neurosci. 27:13481-13490(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NEUROGENESIS, IDENTIFICATION OF EFNB3 AS LIGAND, TISSUE SPECIFICITY.
    11. "Zic2 regulates retinal ganglion cell axon avoidance of ephrinB2 through inducing expression of the guidance receptor EphB1."
      Lee R., Petros T.J., Mason C.A.
      J. Neurosci. 28:5910-5919(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DEVELOPMENTAL STAGE.
    12. "Targeted mutation of EphB1 receptor prevents development of neuropathic hyperalgesia and physical dependence on morphine in mice."
      Han Y., Song X.S., Liu W.T., Henkemeyer M., Song X.J.
      Mol. Pain 4:60-60(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    13. "Ligand binding induces Cbl-dependent EphB1 receptor degradation through the lysosomal pathway."
      Fasen K., Cerretti D.P., Huynh-Do U.
      Traffic 9:251-266(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY CBL, INTERACTION WITH CBL.

    Entry informationi

    Entry nameiEPHB1_MOUSE
    AccessioniPrimary (citable) accession number: Q8CBF3
    Secondary accession number(s): B1B1C2
    , Q3UY27, Q6PG23, Q8CBE2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 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