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P54762

- EPHB1_HUMAN

UniProt

P54762 - EPHB1_HUMAN

Protein

Ephrin type-B receptor 1

Gene

EPHB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      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.5 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 – 6511ATPCurated
    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: Ensembl
    3. protein binding Source: UniProtKB
    4. transmembrane-ephrin receptor activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Cell adhesion, Neurogenesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    SignaLinkiP54762.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ephrin type-B receptor 1 (EC:2.7.10.1)
    Alternative name(s):
    ELK
    EPH tyrosine kinase 2
    EPH-like kinase 6
    Short name:
    EK6
    Short name:
    hEK6
    Neuronally-expressed EPH-related tyrosine kinase
    Short name:
    NET
    Tyrosine-protein kinase receptor EPH-2
    Gene namesi
    Name:EPHB1
    Synonyms:ELK, EPHT2, HEK6, NET
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3392. EPHB1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. dendrite Source: UniProtKB-SubCell
    3. early endosome membrane Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. integral component of plasma membrane Source: UniProtKB
    6. membrane raft Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi594 – 5941Y → F: Loss of interaction with NCK1. 1 Publication
    Mutagenesisi600 – 6001Y → F: Loss of interaction with SHC1 and SRC. 1 Publication
    Mutagenesisi651 – 6511K → R: Kinase-dead mutant. Unable to autophosphorylate, to interact with SH2 domain-containing interactors, to activate the MAPK/ERK and JUN signaling cascades. Not ubiquitinated by CBL. 2 Publications
    Mutagenesisi778 – 7781Y → F: Loss of interaction with SHC1. 1 Publication
    Mutagenesisi928 – 9281Y → F: Disrupts binding with the GRB10 SH2 domain, providing evidence for phosphorylation. Disrupts interaction with GRB7 and ACP1. 3 Publications

    Organism-specific databases

    PharmGKBiPA27824.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17171 PublicationAdd
    BLAST
    Chaini18 – 984967Ephrin type-B receptor 1PRO_0000016824Add
    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.3 Publications
    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

    MaxQBiP54762.
    PaxDbiP54762.
    PRIDEiP54762.

    PTM databases

    PhosphoSiteiP54762.

    Miscellaneous databases

    PMAP-CutDBP54762.

    Expressioni

    Tissue specificityi

    Preferentially expressed in brain.

    Gene expression databases

    ArrayExpressiP54762.
    BgeeiP54762.
    CleanExiHS_EPHB1.
    GenevestigatoriP54762.

    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. Interacts with PICK1 By similarity. Interacts (through Tyr-594) with NCK1 (via SH2 domain); activates the JUN cascade to regulate cell adhesion By similarity. 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 similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GRB10Q133222EBI-80252,EBI-80275
    GRB2P629932EBI-80252,EBI-401755
    GRB7Q144514EBI-80252,EBI-970191

    Protein-protein interaction databases

    BioGridi108361. 12 interactions.
    IntActiP54762. 8 interactions.
    MINTiMINT-1519362.
    STRINGi9606.ENSP00000381097.

    Structurei

    Secondary structure

    1
    984
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi441 – 4455
    Beta strandi447 – 4537
    Beta strandi464 – 47310
    Beta strandi482 – 49514
    Beta strandi501 – 51212
    Beta strandi514 – 5174
    Beta strandi521 – 5244
    Helixi616 – 6183
    Beta strandi619 – 6268
    Beta strandi633 – 6386
    Beta strandi646 – 6527
    Helixi659 – 67214
    Beta strandi683 – 6875
    Beta strandi689 – 6924
    Beta strandi694 – 6985
    Helixi705 – 7106
    Turni711 – 7144
    Helixi718 – 73720
    Helixi747 – 7493
    Beta strandi750 – 7523
    Beta strandi758 – 7603
    Helixi793 – 7986
    Helixi803 – 81816
    Turni824 – 8274
    Helixi830 – 8389
    Helixi851 – 86010
    Helixi865 – 8673
    Helixi871 – 88313
    Helixi885 – 8884
    Beta strandi889 – 8913
    Helixi916 – 9216
    Turni922 – 9243
    Helixi926 – 9283
    Helixi929 – 9357
    Helixi940 – 9434
    Helixi948 – 9547
    Helixi959 – 97517

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DJSNMR-A434-528[»]
    2EAONMR-A899-984[»]
    3ZFXX-ray2.50A/B/C/D/E/F/G/H/I602-896[»]
    ProteinModelPortaliP54762.
    SMRiP54762. Positions 17-528, 592-984.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54762.

    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.
    HOGENOMiHOG000233856.
    HOVERGENiHBG062180.
    InParanoidiP54762.
    KOiK05110.
    OMAiTLMDTRT.
    OrthoDBiEOG7VTDM6.
    PhylomeDBiP54762.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P54762-1) [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

    MALDYLLLLL 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 SRSPAEASPI 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 KEAVYSDKLQ HYSTGRGSPG MKIYIDPFTY 600
    EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI 650
    KTLKAGYSEK QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM 700
    ENGALDSFLR QNDGQFTVIQ LVGMLRGIAA GMKYLAEMNY 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
    LLRIGITLAG HQKKILNSIH SMRVQISQSP TAMA 984
    Length:984
    Mass (Da):109,885
    Last modified:October 1, 1996 - v1
    Checksum:i8044160E24E93A92
    GO
    Isoform 2 (identifier: P54762-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-439: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:545
    Mass (Da):61,401
    Checksum:i2BC8548F9403B5C2
    GO
    Isoform 3 (identifier: P54762-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         158-242: VNTEVRSFGP...DVPIKLYCNG → LALQGHSRPA...LQGRQVGGMM
         243-984: Missing.

    Show »
    Length:242
    Mass (Da):26,906
    Checksum:iF89C739C1AB3F92E
    GO

    Sequence cautioni

    The sequence AAB94627.1 differs from that shown. Reason: wrong intron-exon boundaries.
    The sequence AAB94628.1 differs from that shown. Reason: wrong intron-exon boundaries.
    The sequence AAD02031.1 differs from that shown. Reason: Chimeric cDNA.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121A → E in AAD02030. (PubMed:9430661)Curated
    Sequence conflicti12 – 121A → E in AAB94627. (PubMed:9430661)Curated
    Sequence conflicti12 – 121A → E in AAB94628. (PubMed:9430661)Curated
    Sequence conflicti185 – 1851S → I in AAD02030. (PubMed:9430661)Curated
    Sequence conflicti185 – 1851S → I in AAD02031. (PubMed:9430661)Curated
    Sequence conflicti185 – 1851S → I in AAB94627. (PubMed:9430661)Curated
    Sequence conflicti185 – 1851S → I in AAB94628. (PubMed:9430661)Curated
    Sequence conflicti274 – 2741T → R in AAD02030. (PubMed:9430661)Curated
    Sequence conflicti274 – 2741T → R in AAD02031. (PubMed:9430661)Curated
    Sequence conflicti274 – 2741T → R in AAB94627. (PubMed:9430661)Curated
    Sequence conflicti274 – 2741T → R in AAB94628. (PubMed:9430661)Curated
    Sequence conflicti336 – 3361T → S in AAD02030. (PubMed:9430661)Curated
    Sequence conflicti336 – 3361T → S in AAD02031. (PubMed:9430661)Curated
    Sequence conflicti336 – 3361T → S in AAB94627. (PubMed:9430661)Curated
    Sequence conflicti336 – 3361T → S in AAB94628. (PubMed:9430661)Curated
    Sequence conflicti752 – 7521V → L in AAI11745. (PubMed:15489334)Curated
    Sequence conflicti813 – 8131V → H in AAD02030. (PubMed:9430661)Curated
    Sequence conflicti813 – 8131V → H in AAB94627. (PubMed:9430661)Curated
    Sequence conflicti819 – 8191S → Y in AAD02030. (PubMed:9430661)Curated
    Sequence conflicti819 – 8191S → Y in AAB94627. (PubMed:9430661)Curated
    Sequence conflicti881 – 8811M → I in BAF83897. (PubMed:14702039)Curated
    Sequence conflicti903 – 9031L → H in BAF83897. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181M → V.1 Publication
    Corresponds to variant rs55650774 [ dbSNP | Ensembl ].
    VAR_042165
    Natural varianti87 – 871T → S.
    Corresponds to variant rs1042794 [ dbSNP | Ensembl ].
    VAR_011801
    Natural varianti152 – 1521G → R.
    Corresponds to variant rs1042793 [ dbSNP | Ensembl ].
    VAR_011802
    Natural varianti367 – 3671R → G.
    Corresponds to variant rs1042789 [ dbSNP | Ensembl ].
    VAR_011803
    Natural varianti387 – 3871T → M.1 Publication
    Corresponds to variant rs56396912 [ dbSNP | Ensembl ].
    VAR_042166
    Natural varianti485 – 4851R → S.
    Corresponds to variant rs1042788 [ dbSNP | Ensembl ].
    VAR_011804
    Natural varianti707 – 7071S → T in an ovarian undifferentiated carcinoma sample; somatic mutation. 1 Publication
    VAR_042167
    Natural varianti719 – 7191I → V in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042168
    Natural varianti743 – 7431R → Q in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_042169
    Natural varianti847 – 8471M → T.
    Corresponds to variant rs1042785 [ dbSNP | Ensembl ].
    VAR_011805
    Natural varianti912 – 9121A → T.1 Publication
    Corresponds to variant rs56345346 [ dbSNP | Ensembl ].
    VAR_042170
    Natural varianti973 – 9731R → W.1 Publication
    Corresponds to variant rs1042784 [ dbSNP | Ensembl ].
    VAR_058479
    Natural varianti981 – 9811T → M.1 Publication
    Corresponds to variant rs56186270 [ dbSNP | Ensembl ].
    VAR_042171

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 439439Missing in isoform 2. 1 PublicationVSP_056017Add
    BLAST
    Alternative sequencei158 – 24285VNTEV…LYCNG → LALQGHSRPARKLKAAPTAP PTAAPLQRRLPSAPVGPVIT ERTLTLQKWHALASHQVPAM LSPSSMRRPSFWSGTLQGRQ VGGMM in isoform 3. 1 PublicationVSP_056018Add
    BLAST
    Alternative sequencei243 – 984742Missing in isoform 3. 1 PublicationVSP_056019Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L40636 mRNA. Translation: AAB08520.1.
    AF037331 mRNA. Translation: AAD02030.1.
    AF037332 mRNA. Translation: AAD02031.1. Sequence problems.
    AF037333 mRNA. Translation: AAB94627.1. Sequence problems.
    AF037334 mRNA. Translation: AAB94628.1. Sequence problems.
    EU826607 mRNA. Translation: ACF47643.1.
    AK095305 mRNA. Translation: BAG53024.1.
    AK291208 mRNA. Translation: BAF83897.1.
    AC016931 Genomic DNA. No translation available.
    AC016951 Genomic DNA. No translation available.
    AC063918 Genomic DNA. No translation available.
    AC073244 Genomic DNA. No translation available.
    AC092969 Genomic DNA. No translation available.
    BC111744 mRNA. Translation: AAI11745.1.
    CCDSiCCDS46921.1.
    RefSeqiNP_004432.1. NM_004441.4.
    UniGeneiHs.116092.

    Genome annotation databases

    EnsembliENST00000398015; ENSP00000381097; ENSG00000154928.
    ENST00000493838; ENSP00000419574; ENSG00000154928.
    GeneIDi2047.
    KEGGihsa:2047.
    UCSCiuc003eqt.3. human.

    Polymorphism databases

    DMDMi1706663.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L40636 mRNA. Translation: AAB08520.1 .
    AF037331 mRNA. Translation: AAD02030.1 .
    AF037332 mRNA. Translation: AAD02031.1 . Sequence problems.
    AF037333 mRNA. Translation: AAB94627.1 . Sequence problems.
    AF037334 mRNA. Translation: AAB94628.1 . Sequence problems.
    EU826607 mRNA. Translation: ACF47643.1 .
    AK095305 mRNA. Translation: BAG53024.1 .
    AK291208 mRNA. Translation: BAF83897.1 .
    AC016931 Genomic DNA. No translation available.
    AC016951 Genomic DNA. No translation available.
    AC063918 Genomic DNA. No translation available.
    AC073244 Genomic DNA. No translation available.
    AC092969 Genomic DNA. No translation available.
    BC111744 mRNA. Translation: AAI11745.1 .
    CCDSi CCDS46921.1.
    RefSeqi NP_004432.1. NM_004441.4.
    UniGenei Hs.116092.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DJS NMR - A 434-528 [» ]
    2EAO NMR - A 899-984 [» ]
    3ZFX X-ray 2.50 A/B/C/D/E/F/G/H/I 602-896 [» ]
    ProteinModelPortali P54762.
    SMRi P54762. Positions 17-528, 592-984.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108361. 12 interactions.
    IntActi P54762. 8 interactions.
    MINTi MINT-1519362.
    STRINGi 9606.ENSP00000381097.

    Chemistry

    BindingDBi P54762.
    ChEMBLi CHEMBL2363043.
    GuidetoPHARMACOLOGYi 1830.

    PTM databases

    PhosphoSitei P54762.

    Polymorphism databases

    DMDMi 1706663.

    Proteomic databases

    MaxQBi P54762.
    PaxDbi P54762.
    PRIDEi P54762.

    Protocols and materials databases

    DNASUi 2047.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000398015 ; ENSP00000381097 ; ENSG00000154928 .
    ENST00000493838 ; ENSP00000419574 ; ENSG00000154928 .
    GeneIDi 2047.
    KEGGi hsa:2047.
    UCSCi uc003eqt.3. human.

    Organism-specific databases

    CTDi 2047.
    GeneCardsi GC03P134316.
    HGNCi HGNC:3392. EPHB1.
    MIMi 600600. gene.
    neXtProti NX_P54762.
    PharmGKBi PA27824.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233856.
    HOVERGENi HBG062180.
    InParanoidi P54762.
    KOi K05110.
    OMAi TLMDTRT.
    OrthoDBi EOG7VTDM6.
    PhylomeDBi P54762.
    TreeFami TF315608.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 2681.
    SignaLinki P54762.

    Miscellaneous databases

    EvolutionaryTracei P54762.
    GeneWikii EPH_receptor_B1.
    GenomeRNAii 2047.
    NextBioi 8321.
    PMAP-CutDB P54762.
    PROi P54762.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54762.
    Bgeei P54762.
    CleanExi HS_EPHB1.
    Genevestigatori P54762.

    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. "cDNA cloning, molecular characterization, and chromosomal localization of NET(EPHT2), a human EPH-related receptor protein-tyrosine kinase gene preferentially expressed in brain."
      Tang X.X., Biegel J.A., Nycum L.M., Yoshioka A., Brodeur G.M., Pleasure D.E., Ikegaki N.
      Genomics 29:426-437(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN CELL ADHESION, FUNCTION IN JUN CASCADE ACTIVATION, INTERACTION WITH NCK1, MUTAGENESIS OF TYR-594 AND LYS-651, VARIANT TRP-973.
      Tissue: Kidney.
    3. "Novel splice variants derived from the receptor tyrosine kinase superfamily are potential therapeutics for rheumatoid arthritis."
      Jin P., Zhang J., Sumariwalla P.F., Ni I., Jorgensen B., Crawford D., Phillips S., Feldmann M., Shepard H.M., Paleolog E.M.
      Arthritis Res. Ther. 10:R73-R73(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Tongue.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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).
    7. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-32.
    8. "Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells."
      Stein E., Cerretti D.P., Daniel T.O.
      J. Biol. Chem. 271:23588-23593(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB2 AND GRB10, MUTAGENESIS OF TYR-928, PHOSPHORYLATION AT TYR-928.
    9. "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.
    10. "Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses."
      Stein E., Lane A.A., Cerretti D.P., Schoecklmann H.O., Schroff A.D., Van Etten R.L., Daniel T.O.
      Genes Dev. 12:667-678(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS, FUNCTION IN CELL ADHESION, INTERACTION WITH ACP1, MUTAGENESIS OF TYR-928.
    11. "The kinase-null EphB6 receptor undergoes transphosphorylation in a complex with EphB1."
      Freywald A., Sharfe N., Roifman C.M.
      J. Biol. Chem. 277:3823-3828(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPHB6.
    12. "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, FUNCTION, PHOSPHORYLATION AT TYR-928, MUTAGENESIS OF TYR-928.
    13. "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: FUNCTION IN CELL MIGRATION, FUNCTION IN ERK CASCADE ACTIVATION, INTERACTION WITH GRB2; SHC1 AND SRC, MUTAGENESIS OF TYR-600 AND TYR-778.
    14. "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: FUNCTION IN ERK CASCADE ACTIVATION, UBIQUITINATION BY CBL, INTERACTION WITH CBL, MUTAGENESIS OF LYS-651, AUTOPHOSPHORYLATION, IDENTIFICATION OF EFNB1 AS LIGAND, SUBCELLULAR LOCATION.
    15. "Solution structure of the C-terminal SAM-domain of mouse ephrin type-B receptor 1 precursor (EC 2.7.1.112)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 899-984.
    16. "Solution structures of the FN3 domain of human ephrin type-B receptor 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 434-528.
    17. "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] VAL-18; MET-387; THR-707; VAL-719; GLN-743; THR-912 AND MET-981.

    Entry informationi

    Entry nameiEPHB1_HUMAN
    AccessioniPrimary (citable) accession number: P54762
    Secondary accession number(s): A8K593
    , B3KTB2, B5A969, O43569, O95142, O95143, Q0VG87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 157 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, Direct protein sequencing, 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