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Q91571 (EPB1A_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. 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-A

EC=2.7.10.1
Alternative name(s):
Tyrosine-protein kinase receptor XEK
Gene names
Name:ephb1-a
Synonyms:xek
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length985 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. May play a role in axon guidance during nervous system development. May also play an important redundant role with other ephrin-B receptors in development and maturation of dendritic spines and synapse formation. More generally, may play a role in targeted cell migration and adhesion. Upon activation by ephrin-B ligands activates the MAPK/ERK and the JNK signaling cascades to regulate cell migration and adhesion respectively. Ref.2

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 By similarity.

Subcellular location

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

Developmental stage

Maternally expressed, it decreases at mid blastula transition and reappears at late neurulation. Expressed at higher levels in the anterior and dorsal regions of embryonic stages 16, 24 and 37. In adult it appears to be ubiquitously expressed with higher expression in brain and ovary. Expression in the brain, brachial arches, trigeminal facial ganglion, and the retina of swimming tadpole stage of development.

Post-translational modification

Phosphorylated. Autophosphorylation is stimulated by ligands 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
Gene Ontology (GO)
   Biological_processaxon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

cell chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

cell-substrate adhesion

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

ephrin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of cell polarity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of synapse assembly

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

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

   Cellular_componentdendrite

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

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

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 – 1919 Potential
Chain20 – 985966Ephrin type-B receptor 1-A
PRO_0000016826

Regions

Topological domain20 – 542523Extracellular Potential
Transmembrane543 – 56321Helical; Potential
Topological domain564 – 985422Cytoplasmic Potential
Domain21 – 203183Eph LBD
Domain324 – 434111Fibronectin type-III 1
Domain435 – 53298Fibronectin type-III 2
Domain620 – 883264Protein kinase
Domain912 – 97665SAM
Nucleotide binding626 – 6349ATP By similarity
Motif983 – 9853PDZ-binding Potential
Compositional bias185 – 321137Cys-rich

Sites

Active site7451Proton acceptor By similarity
Binding site6521ATP By similarity

Amino acid modifications

Glycosylation3361N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential
Glycosylation4821N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q91571 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BE72CD1BFF51E623

FASTA985110,104
        10         20         30         40         50         60 
MELNVLLLLL CLSGGQVGAV EETLMDTRTA TAELGWTANP SSGWEEVSGY DENLNTIRTY 

        70         80         90        100        110        120 
QVCNVFGPKQ NNWLLTTFIP RRGAHRVYVE MRFTVRDCSS LPNVPGSCKE TFNLYYYETD 

       130        140        150        160        170        180 
SNIENKISTF WNESPYLKVD TIAADESFSQ VDFGGRLMKV NTEVRSFGPL TRSGFYLAFQ 

       190        200        210        220        230        240 
DYGACMSLLS VRVFFKEMPS VVQNLLVFPE TMTGAESTSL VIARGTCIPN AEEVDVPIKL 

       250        260        270        280        290        300 
YCNGDGEWMV PIGKCTCKAG YEPENHVVCK ACPAAMFKAN QGMGICAQCP ANSRSTSEAS 

       310        320        330        340        350        360 
PICICRNGYY RADFDTPEAP CTSVPSGPRN VISIVNETAI TLEWHPPRET GGRDDVDYNI 

       370        380        390        400        410        420 
VCKKCRADRR ACSRCDDNVD FVPRQLGLTD TRVFISNLWA HTPYTFETQA VNGVTNKSPF 

       430        440        450        460        470        480 
PPQHVSVNIT TNQAAPSSVP IMHQVKATMK SITLSWPQQE QPNGIILDYE IRYYEKDHHE 

       490        500        510        520        530        540 
FNSSLARSQT NTARRTGGRV WMFMSVQVRA RTVAGYGKFS SKCGFQTLTA EDYKSELREQ 

       550        560        570        580        590        600 
LPLTGSAAAG VVFIVSLVAI SIVCSRKRTY SKEAVYSDKL QHYSTGRGSP GMKIYIDPFT 

       610        620        630        640        650        660 
YEDPNEAVRE FAKEIDVSFV KIEEVIGAGE FGEVYKGRLK LPSKREISVA IKTLKAGYSE 

       670        680        690        700        710        720 
KQRRDFLSEA SIMGQFDHPN IIRLEGVVTK SRPVMIITEF MENGALDSFL RQNDGQFTVI 

       730        740        750        760        770        780 
QLVGMLRGIA AGMKYLSEMN YVHRDLAARN ILVNSNLVCK VSDFGLSRYL QDDTSDPTYT 

       790        800        810        820        830        840 
SSLGGKIPVR WTAQEAIAYR KFTSASDVWS YGIVMWEVMS YGERPYWTMS NQDVINAIEQ 

       850        860        870        880        890        900 
DYRLPPPMDC PAALHQLMLD CWQKDRNSRP RLAEIVNTLR PMIRNPASLK TVATIPAVPS 

       910        920        930        940        950        960 
QPLLDRSIPD ISAFTSVDDW LSAIKMGQYR DNFLSSGFTS LQLVAQMTSE DLLRIGITLA 

       970        980 
GHQKKILNSI QSMRVQITQS PTSIA 

« Hide

References

[1]"Expression of an amphibian homolog of the Eph family of receptor tyrosine kinases is developmentally regulated."
Jones T.L., Karavanova I., Maeno M., Ong R.C., Kung H.-F., Daar I.O.
Oncogene 10:1111-1117(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The EphA4 and EphB1 receptor tyrosine kinases and ephrin-B2 ligand regulate targeted migration of branchial neural crest cells."
Smith A., Robinson V., Patel K., Wilkinson D.G.
Curr. Biol. 7:561-570(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TARGETED CELL MIGRATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14164 mRNA. Translation: AAA74888.1.
PIRI51672.
RefSeqNP_001084070.1. NM_001090601.1.
UniGeneXl.1028.

3D structure databases

ProteinModelPortalQ91571.
SMRQ91571. Positions 20-199, 438-529, 593-890, 901-985.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID399288.
KEGGxla:399288.

Organism-specific databases

CTD2047.
XenbaseXB-GENE-865799. ephb1.

Phylogenomic databases

HOVERGENHBG062180.
KOK05110.

Enzyme and pathway databases

BRENDA2.7.10.1. 6726.

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.
IPR011510. SAM_2.
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.
PF07647. SAM_2. 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.
PS00791. RECEPTOR_TYR_KIN_V_2. 1 hit.
PS50105. SAM_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEPB1A_XENLA
AccessionPrimary (citable) accession number: Q91571
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 122 of the entry and version 1 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