Oops!
https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | This entry represents the N-terminal domain of dimerization/docking (D/D) domain of Calcium-binding tyrosine phosphorylation-regulated protein (CABYR), Sperm surface protein Sp17 (SP17) and similar animal proteins. This domain shows similarity to the D/D domain of the R subunit of cAMP-dependent protein kinase (PKA), which dimerises to form a four-helix bundle that serves as a docking site for A-kinase-anchoring proteins (AKAPs). This facilitates the localisation of PKA to specific sites in the cell. The D/D domain of CABYR and SP17 have been shown to bind to AKAP3, a protein that is also associated to the FS of mammalian spermatozoa [ ].CABYR and SP17 are naturally located in the human sperm fibrous sheath (FS). CABYR was originally isolated from spermatoza and was thought to be testis-specific, but has recently been observed in lung and brain tumours. It is a polymorphic calcium binding protein that is phosphorylated during capacitation [ , , ]. SP17 plays an important role in the interaction of sperm with the zona pellucida during fertilization. It also promotes cell-cell adhesion. SP17 is found in various human tumours of unrelated histological origin including metastatic squamous cell carcinoma, multiple myeloma, ovarian cancer, and primary nervous system tumours, among others [, , , , , , ]. | Name | CABYR/SP17, dimerization domain |
| Short Name | DD_CABYR_SP17 | Type | Domain |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
