EPHA7_MOUSE - dbPTM
EPHA7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
233PhosphorylationSLVEVRGTCVSSAEE
HCEEEECEECCCHHH
10.1223984901
236PhosphorylationEVRGTCVSSAEEEAE
EEECEECCCHHHHHH
26.4423984901
237PhosphorylationVRGTCVSSAEEEAEN
EECEECCCHHHHHHH
21.2123984901
251PhosphorylationNSPRMHCSAEGEWLV
HCCCCEECCCCCEEE
18.0623984901
343N-linked_GlycosylationQNLIFNINQTTVSLE
CCEEEEECCCEEEEE
33.96-
410N-linked_GlycosylationMDLLAHANYTFEVEA
HHHHHHCCEEEEEEE
26.89-
435PhosphorylationQRLFAAVSITTGQAA
HHHEEEEEEECCCCC
14.97-
437PhosphorylationLFAAVSITTGQAAPS
HEEEEEEECCCCCHH
19.84-
438PhosphorylationFAAVSITTGQAAPSQ
EEEEEEECCCCCHHH
26.15-
444PhosphorylationTTGQAAPSQVSGVMK
ECCCCCHHHCCHHHH
38.1928059163
447PhosphorylationQAAPSQVSGVMKERV
CCCHHHCCHHHHHHH
20.3128059163
607PhosphorylationFKFPGTKTYIDPETY
EECCCCCCEECHHHC
26.0824759943
608PhosphorylationKFPGTKTYIDPETYE
ECCCCCCEECHHHCC
12.60-
614PhosphorylationTYIDPETYEDPNRAV
CEECHHHCCCCCHHH
19.37-
653AcetylationEVCSGRLKLPGKRDV
CCCCCCCCCCCCHHH
51.807626461
780PhosphorylationKVSDFGLSRVIEDDP
EECHHCCCEEECCCC
25.5322817900
791PhosphorylationEDDPEAVYTTTGGKI
CCCCCCEEECCCCCC
12.8626824392
810PhosphorylationTAPEAIQYRKFTSAS
ECCHHHHCCCCCCHH
15.0610572014
940PhosphorylationQAIKMERYKDNFTAA
HHHHHHHCCCCCCHH
14.91-
951PhosphorylationFTAAGYNSLESVARM
CCHHCCCCHHHHHCC
25.6525521595

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPHA7_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of EPHA7_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPHA7_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP