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P09759 (EPHB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin type-B receptor 1

EC=2.7.10.1
Alternative name(s):
ELK
Tyrosine-protein kinase receptor EPH-2
Gene names
Name:Ephb1
Synonyms:Elk, Epth2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length984 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Beside 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 By similarity.

Catalytic activity

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

Subunit structure

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. Interacts with EPHB6; transphosphorylates EPHB6 to form an active signaling complex. 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 similarity.

Subcellular location

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

Tissue specificity

Restricted to brain and testes. Ref.1

Post-translational modification

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. Ref.1

Ubiquitinated; (EFNB1)ligand-induced poly- and/or multi-ubiquitination by CBL is regulated by SRC and leads to lysosomal degradation By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Ephrin receptor subfamily.

Contains 1 Eph LBD (Eph ligand-binding) domain.

Contains 2 fibronectin type-III domains.

Contains 1 protein kinase domain.

Contains 1 SAM (sterile alpha motif) domain.

Ontologies

Keywords
   Biological processCell adhesion
Neurogenesis
   Cellular componentCell membrane
Cell projection
Endosome
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

axon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

cell-substrate adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

central nervous system projection neuron axonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine development

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

detection of temperature stimulus involved in sensory perception of pain

Inferred from sequence or structural similarity. Source: UniProtKB

ephrin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of cell polarity

Inferred from sequence or structural similarity. Source: UniProtKB

neural precursor cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

optic nerve morphogenesis

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.1. Source: GOC

positive regulation of synapse assembly

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.1. Source: RGD

regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of JNK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

retinal ganglion cell axon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: UniProtKB-SubCell

early endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

axon guidance receptor activity

Inferred from electronic annotation. Source: Ensembl

protein tyrosine kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

transmembrane-ephrin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 984967Ephrin type-B receptor 1
PRO_0000016825

Regions

Topological domain18 – 540523Extracellular Potential
Transmembrane541 – 56323Helical; Potential
Topological domain564 – 984421Cytoplasmic Potential
Domain19 – 201183Eph LBD
Domain322 – 432111Fibronectin type-III 1
Domain433 – 52896Fibronectin type-III 2
Domain619 – 882264Protein kinase
Domain911 – 97565SAM
Nucleotide binding625 – 6339ATP By similarity
Motif982 – 9843PDZ-binding Potential
Compositional bias183 – 319137Cys-rich

Sites

Active site7441Proton acceptor By similarity
Binding site6511ATP By similarity

Amino acid modifications

Modified residue9281Phosphotyrosine; by autocatalysis By similarity
Glycosylation3341N-linked (GlcNAc...) Potential
Glycosylation4261N-linked (GlcNAc...) Potential
Glycosylation4801N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P09759 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: 521EAC240D8FB91A

FASTA984109,883
        10         20         30         40         50         60 
MALDCLLLFL LASAVAAMEE TLMDTRTATA ELGWTANPAS GWEEVSGYDE NLNTIRTYQV 

        70         80         90        100        110        120 
CNVFEPNQNN WLLTTFINRR GAHRIYTEMR FTVRDCSSLP NVPGSCKETF NLYYYETDSV 

       130        140        150        160        170        180 
IATKKSAFWS EAPYLKVDTI AADESFSQVD FGGRLMKVNT EVRSFGPLTR NGFYLAFQDY 

       190        200        210        220        230        240 
GACMSLLSVR VFFKKCPSIV QNFAVFPETM TGAESTSLVI ARGTCIPNAE EVDVPIKLYC 

       250        260        270        280        290        300 
NGDGEWMVPI GRCTCKAGYE PENSVACKAC PAGTFKASQE AEGCSHCPSN SRSPSEASPI 

       310        320        330        340        350        360 
CTCRTGYYRA DFDPPEVACT SVPSGPRNVI SIVNETSIIL EWHPPRETGG RDDVTYNIIC 

       370        380        390        400        410        420 
KKCRADRRSC SRCDDNVEFV PRQLGLTECR VSISSLWAHT PYTFDIQAIN GVSSKSPFPP 

       430        440        450        460        470        480 
QHVSVNITTN QAAPSTVPIM HQVSATMRSI TLSWPQPEQP NGIILDYEIR YYEKEHNEFN 

       490        500        510        520        530        540 
SSMARSQTNT ARIDGLRPGM VYVVQVRART VAGYGKFSGK MCFQTLTDDD YKSELREQLP 

       550        560        570        580        590        600 
LIAGSAAAGV VFVVSLVAIS IVCSRKRAYS KEAVYSDKLQ HYSTGRGSPG MKIYIDPFTY 

       610        620        630        640        650        660 
EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI KTLKAGYSEK 

       670        680        690        700        710        720 
QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM ENGALDSFLR QNDGQFTVIQ 

       730        740        750        760        770        780 
LVGMLRGIAA GMKYLSEMNY VHRDLAARNI LVNSNLVCKV SDFGLSRYLQ DDTSDPTYTS 

       790        800        810        820        830        840 
SLGGKIPVRW TAPEAIAYRK FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD 

       850        860        870        880        890        900 
YRLPPPMDCP AALHQLMLDC WQKDRNSRPR FAEIVNTLDK MIRNPASLKT VATITAVPSQ 

       910        920        930        940        950        960 
PLLDRSIPDF TAFTTVDDWL SAIKMVQYRD SFLTAGFTSL QLVTQMTSED LLRIGVTLAG 

       970        980 
HQKKILSSIH SMRVQMNQSP SVMA 

« Hide

References

[1]"Characterization of elk, a brain-specific receptor tyrosine kinase."
Lhotak V., Greer P., Letwin K., Pawson T.
Mol. Cell. Biol. 11:2496-2502(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
Strain: Wistar.
Tissue: Brain.
[2]"Novel protein-tyrosine kinase cDNAs related to fps/fes and eph cloned using anti-phosphotyrosine antibody."
Letwin K., Yee S.P., Pawson T.
Oncogene 3:621-627(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 605-984.
Strain: Wistar.
Tissue: Brain.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59814 mRNA. No translation available.
X13411 mRNA. Translation: CAA31777.1.
PIRA39753.
RefSeqNP_001097998.1. NM_001104528.1.
UniGeneRn.46606.

3D structure databases

ProteinModelPortalP09759.
SMRP09759. Positions 18-197, 436-528, 592-889, 900-984.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid246515. 2 interactions.
DIPDIP-138N.
MINTMINT-1519436.
STRING10116.ENSRNOP00000010634.

PTM databases

PhosphoSiteP09759.

Proteomic databases

PaxDbP09759.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24338.
KEGGrno:24338.
UCSCRGD:2556. rat.

Organism-specific databases

CTD2047.
RGD2556. Ephb1.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidP09759.
KOK05110.
OrthoDBEOG7VTDM6.
PhylomeDBP09759.
TreeFamTF315608.

Enzyme and pathway databases

BRENDA2.7.10.1. 5301.

Gene expression databases

GenevestigatorP09759.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.120.260. 1 hit.
2.60.40.10. 2 hits.
InterProIPR027936. 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]
PfamPF14575. 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]
PIRSFPIRSF000666. TyrPK_ephrin_receptor. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00615. EPH_lbd. 1 hit.
SM00060. FN3. 2 hits.
SM00454. SAM. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF47769. SSF47769. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEPS01186. 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]
ProtoNetSearch...

Other

NextBio603035.

Entry information

Entry nameEPHB1_RAT
AccessionPrimary (citable) accession number: P09759
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families