UniProt ID | EPHA7_MOUSE | |
---|---|---|
UniProt AC | Q61772 | |
Protein Name | Ephrin type-A receptor 7 | |
Gene Name | Epha7 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 998 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein . |
|
Protein Description | Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A 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. Among GPI-anchored ephrin-A ligands, EFNA5 is a cognate/functional ligand for EPHA7 and their interaction regulates brain development modulating cell-cell adhesion and repulsion. Has a repellent activity on axons and is for instance involved in the guidance of corticothalamic axons and in the proper topographic mapping of retinal axons to the colliculus. May also regulate brain development through a caspase(CASP3)-dependent proapoptotic activity. Forward signaling may result in activation of components of the ERK signaling pathway including MAP2K1, MAP2K2, MAPK1 AND MAPK3 which are phosphorylated upon activation of EPHA7. Isoform 4 which lacks the kinase domain may regulate isoform 1 adhesive properties.. | |
Protein Sequence | MVVQTRFPSWIILCYIWLLGFAHTGEAQAAKEVLLLDSKAQQTELEWISSPPSGWEEISGLDENYTPIRTYQVCQVMEPNQNNWLRTNWISKGNAQRIFVELKFTLRDCNSLPGVLGTCKETFNLYYYETDYDTGRNIRENLYVKIDTIAADESFTQGDLGERKMKLNTEVREIGPLSKKGFYLAFQDVGACIALVSVKVYYKKCWSIVENLAVFPDTVTGSEFSSLVEVRGTCVSSAEEEAENSPRMHCSAEGEWLVPIGKCICKAGYQQKGDTCEPCGRRFYKSSSQDLQCSRCPTHSFSDREGSSRCECEDGYYRAPSDPPYVACTRPPSAPQNLIFNINQTTVSLEWSPPADNGGRNDVTYRILCKRCSWEQGECVPCGSNIGYMPQQTGLEDNYVTVMDLLAHANYTFEVEAVNGVSDLSRSQRLFAAVSITTGQAAPSQVSGVMKERVLQRSVQLSWQEPEHPNGVITEYEIKYYEKDQRERTYSTLKTKSTSASINNLKPGTVYVFQIRAVTAAGYGNYSPRLDVATLEEASGKMFEATAVSSEQNPVIIIAVVAVAGTIILVFMVFGFIIGRRHCGYSKADQEGDEELYFHFKFPGTKTYIDPETYEDPNRAVHQFAKELDASCIKIERVIGAGEFGEVCSGRLKLPGKRDVAVAIKTLKVGYTEKQRRDFLCEASIMGQFDHPNVVHLEGVVTRGKPVMIVIEFMENGALDAFLRKHDGQFTVIQLVGMLRGIAAGMRYLADMGYVHRDLAARNILVNSNLVCKVSDFGLSRVIEDDPEAVYTTTGGKIPVRWTAPEAIQYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVIKAIEEGYRLPAPMDCPAGLHQLMLDCWQKDRAERPKFEQIVGILDKMIRNPSSLKTPLGTCSRPLSPLLDQSTPDFTAFCSVGEWLQAIKMERYKDNFTAAGYNSLESVARMTIDDVMSLGITLVGHQKKIMSSIQTMRAQMLHLHGTGIQV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
233 | Phosphorylation | SLVEVRGTCVSSAEE HCEEEECEECCCHHH | 10.12 | 23984901 | |
236 | Phosphorylation | EVRGTCVSSAEEEAE EEECEECCCHHHHHH | 26.44 | 23984901 | |
237 | Phosphorylation | VRGTCVSSAEEEAEN EECEECCCHHHHHHH | 21.21 | 23984901 | |
251 | Phosphorylation | NSPRMHCSAEGEWLV HCCCCEECCCCCEEE | 18.06 | 23984901 | |
343 | N-linked_Glycosylation | QNLIFNINQTTVSLE CCEEEEECCCEEEEE | 33.96 | - | |
410 | N-linked_Glycosylation | MDLLAHANYTFEVEA HHHHHHCCEEEEEEE | 26.89 | - | |
435 | Phosphorylation | QRLFAAVSITTGQAA HHHEEEEEEECCCCC | 14.97 | - | |
437 | Phosphorylation | LFAAVSITTGQAAPS HEEEEEEECCCCCHH | 19.84 | - | |
438 | Phosphorylation | FAAVSITTGQAAPSQ EEEEEEECCCCCHHH | 26.15 | - | |
444 | Phosphorylation | TTGQAAPSQVSGVMK ECCCCCHHHCCHHHH | 38.19 | 28059163 | |
447 | Phosphorylation | QAAPSQVSGVMKERV CCCHHHCCHHHHHHH | 20.31 | 28059163 | |
607 | Phosphorylation | FKFPGTKTYIDPETY EECCCCCCEECHHHC | 26.08 | 24759943 | |
608 | Phosphorylation | KFPGTKTYIDPETYE ECCCCCCEECHHHCC | 12.60 | - | |
614 | Phosphorylation | TYIDPETYEDPNRAV CEECHHHCCCCCHHH | 19.37 | - | |
653 | Acetylation | EVCSGRLKLPGKRDV CCCCCCCCCCCCHHH | 51.80 | 7626461 | |
780 | Phosphorylation | KVSDFGLSRVIEDDP EECHHCCCEEECCCC | 25.53 | 22817900 | |
791 | Phosphorylation | EDDPEAVYTTTGGKI CCCCCCEEECCCCCC | 12.86 | 26824392 | |
810 | Phosphorylation | TAPEAIQYRKFTSAS ECCHHHHCCCCCCHH | 15.06 | 10572014 | |
940 | Phosphorylation | QAIKMERYKDNFTAA HHHHHHHCCCCCCHH | 14.91 | - | |
951 | Phosphorylation | FTAAGYNSLESVARM CCHHCCCCHHHHHCC | 25.65 | 25521595 |
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 EPHA7_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of EPHA7_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 EPHA7_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of EPHA7_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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