| UniProt ID | EFNB3_MOUSE | |
|---|---|---|
| UniProt AC | O35393 | |
| Protein Name | Ephrin-B3 | |
| Gene Name | Efnb3 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 340 | |
| Subcellular Localization |
Membrane Single-pass type I membrane protein. |
|
| Protein Description | Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors 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 pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons.. | |
| Protein Sequence | MGAPHFGPGGVQVGALLLLGFAGLVSGLSLEPVYWNSANKRFQAEGGYVLYPQIGDRLDLLCPRARPPGPHSSPSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEYSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVGQSPRGGAVPRKPVSEMPMERDRGAAHSAEPGRDTIPGDPSSNATSRGAEGPLPPPSMPAVAGAAGGMALLLLGVAGAGGAMCWRRRRAKPSESRHPGPGSFGRGGSLGLGGGGGMGPREAEPGELGIALRGGGTADPPFCPHYEKVSGDYGHPVYIVQDGPPQSPPNIYYKV | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 75 | Phosphorylation | PGPHSSPSYEFYKLY CCCCCCCCCEEEEEE | 38.96 | 25338131 | |
| 210 | N-linked_Glycosylation | IPGDPSSNATSRGAE CCCCCCCCCCCCCCC | 52.13 | 19349973 | |
| 271 | Methylation | PGPGSFGRGGSLGLG CCCCCCCCCCCCCCC | 44.27 | 24129315 | |
| 274 | Phosphorylation | GSFGRGGSLGLGGGG CCCCCCCCCCCCCCC | 23.30 | 22324799 | |
| 308 | S-palmitoylation | GTADPPFCPHYEKVS CCCCCCCCCCCEECC | 2.21 | 28680068 | |
| 311 | Phosphorylation | DPPFCPHYEKVSGDY CCCCCCCCEECCCCC | 11.55 | - | |
| 315 | Phosphorylation | CPHYEKVSGDYGHPV CCCCEECCCCCCCCE | 36.69 | - | |
| 318 | Phosphorylation | YEKVSGDYGHPVYIV CEECCCCCCCCEEEE | 22.36 | 11983165 | |
| 323 | Phosphorylation | GDYGHPVYIVQDGPP CCCCCCEEEEECCCC | 10.38 | - | |
| 332 | Phosphorylation | VQDGPPQSPPNIYYK EECCCCCCCCCCEEE | 48.36 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of EFNB3_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EFNB3_MOUSE !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of EFNB3_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of EFNB3_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-210, AND MASSSPECTROMETRY. | |
