1B0X


Conserved Protein Domain Family
SAM_EPH-A4

?
cd09545: SAM_EPH-A4 
Click on image for an interactive view with Cn3D
SAM domain of EPH-A4 subfamily of tyrosine kinase receptors
SAM (sterile alpha motif) domain of EPH-A4 subfamily of receptor tyrosine kinases is a C-terminal potential protein-protein interaction domain. This domain is located in the cytoplasmic region of EPH-A4 receptors and appears to mediate cell-cell initiated signal transduction. SAM domains of EPH-A4 receptors can form homodimers. EPH-A4 receptors bind ligands such as erphirin A1, A4, A5. They are known to interact with a number of different proteins, including meltrin beta metalloprotease, Cdk5, and EFS2alpha, however SAM domain doesn't participate in these interactions. EPH-A4 receptors are involved in regulation of corticospinal tract formation, in pathway controlling voluntary movements, in formation of motor neurons, and in axon guidance (SAM domain is not required for axon guidance or for EPH-A4 kinase signaling). In Xenopus embryos EPH-A4 induces loss of cell adhesion, ventro-lateral protrusions, and severely expanded posterior structures. Mutations in SAM domain conserved tyrosine (Y928F) enhance the ability of EPH-A4 to induce these phenotypes, thus supporting the idea that the SAM domain may negatively regulate some aspects of EPH-A4 activity. EphA4 gene was found overexpressed in a number of different cancers including human gastric cancer, colorectal cancer, and pancreatic ductal adenocarcinoma. It is likely to be a promising molecular target for the cancer therapy.
Statistics
?
PSSM-Id: 188944
Aligned: 5 rows
Threshold Bit Score: 130.072
Created: 10-May-2010
Updated: 2-Oct-2020
Structure
?
Program:
Drawing:
Aligned Rows:
 
putativehomodimer
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:putative phosphorylation site [posttranslational modification site]
Evidence:
  • Comment:Highlighted tyrosine is a potential phosphoregulatory site and histidine is its bonding partner (phosphorylated upon activation by ephrin).
  • Citation:PMID 9886291

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
Feature 1                         #                                #                    
1B0X_A        24 SAVVSVGDWLQAIKMDRYKDNFTAAGYTTLEAVVHMSQDDLARIGITAITHQNKILSSVQAMRTQMQQMHG 94   house mouse
Q07496       911 SAVVSVSDWLQAIKMERYKDNFTAAGYTTLEAVVHMNQDDLARIGITAITHQNKILSSVQAMRSQMQQMHG 981  chicken
Q91694       910 SQVASVLDWLQASKWKRYKDNFTAAGYTSLEAVVHVNQDDLTRIGISSPSHQNKILSSVQGMRTQLQQMQG 980  African clawed frog
NP_001005919 911 STLGSVADWLQAINMERYRDNFTAAGYTTPEAVVHMTQEDMTRIGISTAAHQDKILNSAQGMLSQMQQMQD 981  zebrafish
XP_687698    913 PSLASVDDWLKLIGLEQYRENFNTAGYSSIESVIPMNHEDLAKMGISCSAHQRKILSSVEDLLSGMHHRQD 983  zebrafish

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap