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P28693 (EPHB2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ephrin type-B receptor 2

EC=2.7.10.1
Alternative name(s):
EPH-like kinase 5
Short name=EK5
Short name=cEK5
Gene names
Name:EPHB2
Synonyms:CEK5
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length1004 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. Functions in axon guidance during development. Beside axon guidance, also regulates dendritic spines development and maturation and stimulates the formation of excitatory synapses 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 By similarity.

Subcellular location

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

Tissue specificity

Wide tissue distribution throughout development and sustained expression in adult brain. The longer form (CEK5+) is specifically expressed in the central nervous system.

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.

Sequence caution

The sequence AAA48667.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processNeurogenesis
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete 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

axonal fasciculation

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of synapse assembly

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

integral to 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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P28693-1)

Also known as: CEK5+;

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.
Isoform Short (identifier: P28693-2)

The sequence of this isoform differs from the canonical sequence as follows:
     591-606: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 1004985Ephrin type-B receptor 2
PRO_0000016829

Regions

Topological domain20 – 544525Extracellular Potential
Transmembrane545 – 56521Helical; Potential
Topological domain566 – 1004439Cytoplasmic Potential
Domain21 – 203183Eph LBD
Domain326 – 427102Fibronectin type-III 1
Domain433 – 52896Fibronectin type-III 2
Domain639 – 902264Protein kinase
Domain931 – 99565SAM
Nucleotide binding645 – 6539ATP By similarity
Motif1002 – 10043PDZ-binding Potential
Compositional bias20 – 321302Cys-rich

Sites

Active site7641Proton acceptor By similarity
Binding site6711ATP By similarity

Amino acid modifications

Glycosylation2661N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation4291N-linked (GlcNAc...) Potential
Glycosylation4781N-linked (GlcNAc...) Potential
Glycosylation4831N-linked (GlcNAc...) Potential
Disulfide bond63 ↔ 185 By similarity
Disulfide bond98 ↔ 108 By similarity

Natural variations

Alternative sequence591 – 60616Missing in isoform Short.
VSP_003018

Secondary structure

............ 1004
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long (CEK5+) [UniParc].

Last modified December 1, 2000. Version 3.
Checksum: 8D26213970ECC6E0

FASTA1,004111,963
        10         20         30         40         50         60 
MGPLWFCCLP LALLPLLAAV EETLMDSTTA TAELGWMVHP PSGWEEVSGY DENMNTIRTY 

        70         80         90        100        110        120 
QVCNVFESSQ NNWLRTKYIR RRGAHRIHVE MKFSVRDCSS IPNVPGSCKE TFNLYYYESD 

       130        140        150        160        170        180 
FDSATKTFPN WMENPWMKVD TIAADESFSQ VDLGGRVMKI NTEVRSFGPV SKNGFYLAFQ 

       190        200        210        220        230        240 
DYGGCMSLIA VRVFYRKCPR VIQNGAVFQE TLSGAESTSL VAARGTCISN AEEVDVPIKL 

       250        260        270        280        290        300 
YCNGDGEWLV PIGRCMCRPG YESVENGTVC RGCPSGTFKA SQGDEGCVHC PINSRTTSEG 

       310        320        330        340        350        360 
ATNCVCRNGY YRADADPVDM PCTTIPSAPQ AVISSVNETS LMLEWTPPRD SGGREDLVYN 

       370        380        390        400        410        420 
IICKSCGSGR GACTRCGDNV QFAPRQLGLT EPRIYISDLL AHTQYTFEIQ AVNGVTDQSP 

       430        440        450        460        470        480 
FSPQFASVNI TTNQAAPSAV SIMHQVSRTV DSITLSWSQP DQPNGVILDY ELQYYEKNLS 

       490        500        510        520        530        540 
ELNSTAVKSP TNTVTVQNLK AGTIYVFQVR ARTVAGYGRY SGKMYFQTMT EAEYQTSVQE 

       550        560        570        580        590        600 
KLPLIIGSSA AGLVFLIAVV VIIIVCNRRR GFERADSEYT DKLQHYTSGH STYRGPPPGL 

       610        620        630        640        650        660 
GVRLFVMTPG MKIYIDPFTY EDPNEAVREF AKEIDISCVK IEQVIGAGEF GEVCSGHLKL 

       670        680        690        700        710        720 
PGKREIFVAI KTLKSGYTEK QRRDFLSEAS IMGQFDHPNV IHLEGVVTKS SPVMIITEFM 

       730        740        750        760        770        780 
ENGSLDSFLR QNDGQFTVIQ LVGMLRGIAA GMKYLADMNY VHRDLAARNI LVNSNLVCKV 

       790        800        810        820        830        840 
SDFGLSRFLE DDTSDPTYTS ALGGKIPIRW TAPEAIQYRK FTSASDVWSY GIVMWEVMSY 

       850        860        870        880        890        900 
GERPYWDMTN QDVINAIEQD YRLPPPMDCP NALHQLMLDC WQKDRNHRPK FGQIVNTLDK 

       910        920        930        940        950        960 
MIRNPNSLKA MAPLSSGVNL PLLDRTIPDY TSFNTVDEWL DAIKMSQYKE SFASAGFTTF 

       970        980        990       1000 
DIVSQMTVED ILRVGVTLAG HQKKILNSIQ VMRAQMNQIQ SVEV 

« Hide

Isoform Short [UniParc].

Checksum: 510AD71D1DB1EE81
Show »

FASTA988110,265

References

[1]"Identification of chicken embryo kinase 5, a developmentally regulated receptor-type tyrosine kinase of the Eph family."
Pasquale E.B.
Cell Regul. 2:523-534(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Tissue: Embryo.
[2]"Five novel avian Eph-related tyrosine kinases are differentially expressed."
Sajjadi F.G., Pasquale E.B.
Oncogene 8:1807-1813(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62325 mRNA. Translation: AAA48667.1. Different initiation.
IPIIPI00589125.
IPI00602477.
PIRA56599.
RefSeqNP_996834.1. NM_206951.2.
UniGeneGga.3405.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SGGNMR-A924-998[»]
ProteinModelPortalP28693.
SMRP28693. Positions 20-200, 440-532, 612-910, 930-996.
ModBaseSearch...

Protein-protein interaction databases

STRING9031.ENSGALP00000007541.

Proteomic databases

PaxDbP28693.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000007555; ENSGALP00000007543; ENSGALG00000004741.
GeneID396513.
KEGGgga:396513.

Organism-specific databases

CTD2048.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00700000104274.
HOGENOMHOG000233856.
HOVERGENHBG062180.
InParanoidP28693.
KOK05111.
OrthoDBEOG4W9J35.

Enzyme and pathway databases

BRENDA2.7.10.1. 1306.
ReactomeREACT_115433. Developmental Biology.

Family and domain databases

Gene3D1.10.150.50. 1 hit.
2.60.40.10. 2 hits.
InterProIPR001090. Ephrin_rcpt_lig-bd_dom.
IPR003961. Fibronectin_type3.
IPR008979. Galactose-bd-like.
IPR009030. Growth_fac_rcpt.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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]
PfamPF01404. 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]
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]
SUPFAMSSF49265. FN_III-like. 2 hits.
SSF49785. Gal_bind_like. 1 hit.
SSF57184. Grow_fac_recept. 1 hit.
SSF56112. Kinase_like. 1 hit.
SSF47769. SAM_homology. 1 hit.
PROSITEPS01186. EGF_2. 1 hit. Uncertain.
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

EvolutionaryTraceP28693.
NextBio20816551.

Entry information

Entry nameEPHB2_CHICK
AccessionPrimary (citable) accession number: P28693
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 2000
Last modified: April 3, 2013
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families