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Reviewed, UniProtKB/Swiss-Prot P52800 (EFNB2_MOUSE)

Last modified May 5, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ephrin-B2
Alternative name(s):
    EPH-related receptor tyrosine kinase ligand 5
      Short name=LERK-5
      Short name=HTK ligand
      Short name=HTK-L
    ELF-2
Gene names
Name: Efnb2
Synonyms: Elf2, Epl5, Eplg5, Htkl, Lerk5
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Binds to the receptor tyrosine kinases EPHB2 and EPHB4. May play a role in constraining the orientation of longitudinally projecting axons. Ref.5

Subunit structure

Interacts with PDZRN3 By similarity. Binds to the receptor tyrosine kinase EPHB4.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Expressed on lateral floor plate cells, specifically on commissural axon segments that have passed through the floor plate. Expressed in cells of the retinal ganglion cell layer during retinal axon guidance to the optic disk.

Developmental stage

Expressed in the floor plate throughout the period of commissural axon pathfinding.

Post-translational modification

Inducible phosphorylation of tyrosine residues in the cytoplasmic domain By similarity.

Sequence similarities

Belongs to the ephrin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Epha4Q031371EBI-1032676,EBI-1539152

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 336308Ephrin-B2
PRO_0000008393

Regions

Topological domain29 – 232204Extracellular Potential
Transmembrane233 – 25321 Potential
Topological domain254 – 33683Cytoplasmic Potential
Motif334 – 3363PDZ-binding Potential

Amino acid modifications

Modified residue3071Phosphotyrosine Ref.6
Modified residue3281Phosphoserine By similarity
Modified residue3331Phosphotyrosine By similarity
Glycosylation391N-linked (GlcNAc...)
Glycosylation1421N-linked (GlcNAc...) Potential
Disulfide bond65 ↔ 104
Disulfide bond92 ↔ 156

Experimental info

Sequence conflict3 – 42Missing Ref.3
Sequence conflict1771A → T in AAA99708. Ref.1

Secondary structure

........................ 336
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52800-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D08894996E399554

FASTA33637,202
        10         20         30         40         50         60 
MAMARSRRDS VWKYCWGLLM VLCRTAISRS IVLEPIYWNS SNSKFLPGQG LVLYPQIGDK 

        70         80         90        100        110        120 
LDIICPKVDS KTVGQYEYYK VYMVDKDQAD RCTIKKENTP LLNCARPDQD VKFTIKFQEF 

       130        140        150        160        170        180 
SPNLWGLEFQ KNKDYYIIST SNGSLEGLDN QEGGVCQTRA MKILMKVGQD ASSAGSARNH 

       190        200        210        220        230        240 
GPTRRPELEA GTNGRSSTTS PFVKPNPGSS TDGNSAGHSG NNLLGSEVAL FAGIASGCII 

       250        260        270        280        290        300 
FIVIIITLVV LLLKYRRRHR KHSPQHTTTL SLSTLATPKR GGNNNGSEPS DVIIPLRTAD 

       310        320        330 
SVFCPHYEKV SGDYGHPVYI VQEMPPQSPA NIYYKV 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases."
Cerretti D.P., Vanden Bos T., Nelson N., Kozlosky C.J., Reddy P., Maraskovsky E., Park L.S., Lyman S.D., Copeland N.G., Gilbert D.J., Jenkins N.A., Fletcher R.A.
Mol. Immunol. 32:1197-1205(1995) [PubMed: 8559144] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning of a ligand for the EPH-related receptor protein-tyrosine kinase Htk."
Bennett B.D., Zeigler F.C., Gu Q., Fendly B., Goddard A.D., Gillett N., Matthews W.
Proc. Natl. Acad. Sci. U.S.A. 92:1866-1870(1995) [PubMed: 7534404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CB57BL/6J X SJL/J.
[3]"ELF-2, a new member of the Eph ligand family, is segmentally expressed in mouse embryos in the region of the hindbrain and newly forming somites."
Bergemann A.D., Cheng H.J., Brambilla R., Klein R., Flanagan J.G.
Mol. Cell. Biol. 15:4921-4929(1995) [PubMed: 7651410] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ICR.
Tissue: Brain.
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[5]"Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons."
Imondi R., Wideman C., Kaprielian Z.
Development 127:1397-1410(2000) [PubMed: 10704386] [Abstract]
Cited for: FUNCTION.
[6]"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks."
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-307, MASS SPECTROMETRY.
[7]"Crystal structure of an ephrin ectodomain."
Toth J., Cutforth T., Gelinas A.D., Bethoney K.A., Bard J., Harrison C.J.
Dev. Cell 1:83-92(2001) [PubMed: 11703926] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 30-170.
[8]"Crystal structure of an Eph receptor-ephrin complex."
Himanen J.-P., Rajashankar K.R., Lackmann M., Cowan C.A., Henkemeyer M., Nikolov D.B.
Nature 414:933-938(2001) [PubMed: 11780069] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 31-168 IN COMPLEX WITH EPHB2.
+Additional computationally mapped references.

Cross-references

Sequence databases

U16819 mRNA. Translation: AAA99708.1.
L38847 mRNA. Translation: AAC42052.1.
U30244 mRNA. Translation: AAA82934.1.
BC057009 mRNA. Translation: AAH57009.1.
IPIIPI00762720.
PIRI49766.
RefSeqNP_034241.2.
UniGeneMm.209813

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1IKOX-ray1.92P30-207[»]
1KGYX-ray2.70E/F/G/H31-168[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:29208N.
IntActP52800. 2 interactions.

PTM databases

PhosphoSiteP52800.

Proteomic databases

PRIDEP52800.

Genome annotation databases

EnsemblENSMUSG00000001300. Mus musculus. [Contig view]
GeneID13642.
KEGGmmu:13642.

Organism-specific databases

MGIMGI:105097. Efnb2.

Phylogenomic databases

HOVERGENP52800.

Gene expression databases

ArrayExpressP52800.
BgeeP52800.
CleanExMM_EFNB2.
MM_ELF2.
GermOnlineENSMUSG00000001300. Mus musculus.

Family and domain databases

InterProIPR008972. Cupredoxin.
IPR001799. Ephrin.
IPR019765. Ephrin_CS.
[Graphical view]
Gene3DG3DSA:2.60.40.420. Cupredoxin. 1 hit.
PANTHERPTHR11304. Ephrin. 1 hit.
PfamPF00812. Ephrin. 1 hit.
[Graphical view]
PRINTSPR01347. EPHRIN.
ProDomPD002533. Ephrin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS01299. EPHRIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio284346.
SOURCESearch...

Entry information

Entry nameEFNB2_MOUSE
AccessionPrimary (citable) accession number: P52800
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 5, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents