Reviewed,
UniProtKB/Swiss-Prot P52800 (EFNB2_MOUSE)
Last modified
May 5, 2009.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
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| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 336 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Differentiation Neurogenesis |
| Cellular component | Membrane |
| Domain | Signal Transmembrane |
| Molecular function | Developmental protein |
| PTM | Disulfide bond Glycoprotein Phosphoprotein |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | Notch signaling pathway Inferred from direct assay. Source: UniProtKB cell differentiationInferred from electronic annotation. Source: UniProtKB-KW lymph vessel developmentInferred from mutant phenotype. Source: MGI nervous system developmentInferred from electronic annotation. Source: UniProtKB-KW organ morphogenesisInferred from mutant phenotype. Source: MGI |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from direct assay. Source: MGI |
| Molecular function | receptor binding Ref.8 Inferred from physical interaction. Source: MGI |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 28 | 28 | Potential | |||||||||||||||||||||||||||||
| Chain | 29 – 336 | 308 | Ephrin-B2 | PRO_0000008393 | ||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||
| Topological domain | 29 – 232 | 204 | Extracellular Potential | |||||||||||||||||||||||||||||
| Transmembrane | 233 – 253 | 21 | Potential | |||||||||||||||||||||||||||||
| Topological domain | 254 – 336 | 83 | Cytoplasmic Potential | |||||||||||||||||||||||||||||
| Motif | 334 – 336 | 3 | PDZ-binding Potential | |||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||
| Modified residue | 307 | 1 | Phosphotyrosine Ref.6 | |||||||||||||||||||||||||||||
| Modified residue | 328 | 1 | Phosphoserine By similarity | |||||||||||||||||||||||||||||
| Modified residue | 333 | 1 | Phosphotyrosine By similarity | |||||||||||||||||||||||||||||
| Glycosylation | 39 | 1 | N-linked (GlcNAc...) | |||||||||||||||||||||||||||||
| Glycosylation | 142 | 1 | N-linked (GlcNAc...) Potential | |||||||||||||||||||||||||||||
| Disulfide bond | 65 ↔ 104 | |||||||||||||||||||||||||||||||
| Disulfide bond | 92 ↔ 156 | |||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||
| Sequence conflict | 3 – 4 | 2 | Missing Ref.3 | |||||||||||||||||||||||||||||
| Sequence conflict | 177 | 1 | A → T in AAA99708. Ref.1 | |||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||
| Turn | 47 – 49 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 50 – 53 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 60 – 64 | 5 | ||||||||||||||||||||||||||||||
| Beta strand | 70 – 72 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 78 – 84 | 7 | ||||||||||||||||||||||||||||||
| Helix | 86 – 91 | 6 | ||||||||||||||||||||||||||||||
| Beta strand | 101 – 104 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 112 – 116 | 5 | ||||||||||||||||||||||||||||||
| Beta strand | 133 – 138 | 6 | ||||||||||||||||||||||||||||||
| Helix | 145 – 147 | 3 | ||||||||||||||||||||||||||||||
| Helix | 154 – 158 | 5 | ||||||||||||||||||||||||||||||
| Beta strand | 162 – 167 | 6 | ||||||||||||||||||||||||||||||
Sequences
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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. | |||||||||||||||||||
| IPI | IPI00762720. | ||||||||||||||||||
| PIR | I49766. | ||||||||||||||||||
| RefSeq | NP_034241.2. | ||||||||||||||||||
| UniGene | Mm.209813 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP:29208N. | ||||||||||||||||||
| IntAct | P52800. 2 interactions. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | P52800. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | P52800. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSMUSG00000001300. Mus musculus. [Contig view] | ||||||||||||||||||
| GeneID | 13642. | ||||||||||||||||||
| KEGG | mmu:13642. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| MGI | MGI:105097. Efnb2. | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOVERGEN | P52800. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | P52800. | ||||||||||||||||||
| Bgee | P52800. | ||||||||||||||||||
| CleanEx | MM_EFNB2. MM_ELF2. | ||||||||||||||||||
| GermOnline | ENSMUSG00000001300. Mus musculus. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR008972. Cupredoxin. IPR001799. Ephrin. IPR019765. Ephrin_CS. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:2.60.40.420. Cupredoxin. 1 hit. | ||||||||||||||||||
| PANTHER | PTHR11304. Ephrin. 1 hit. | ||||||||||||||||||
| Pfam | PF00812. Ephrin. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR01347. EPHRIN. | ||||||||||||||||||
| ProDom | PD002533. Ephrin. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||||||||
| PROSITE | PS01299. EPHRIN. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| NextBio | 284346. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | EFNB2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P52800 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (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 |

Clusters with


