Protein
Gene:
CABYR (official gene symbol)Other symbol:
CABYRCT family:
CT88CT identifier:
CT88Aliases from NCBI:
CBP86 , FSP-2 , MGC9117RefSeq :
NP_722454.1 | NP_722453.1 | NP_722452.1 | NP_619585.1 | NP_619584.1 | NP_036321.2
Protein Names (UNIPROT)
Calcium-binding tyrosine phosphorylation-regulated protein
Cellular localization
| Subcellular Localization | Cell type | Methodology | PMID |
|---|---|---|---|
| motile cilia | bronchus and fallopian tube cells | IHC | 18421703 |
| cytoplasm and nuclei | HeLA cell line | Indirect immunofluorescence | 15752768 |
| longitudinal columns and ribs of the fibrous sheath | sperm | Immunoelectron microscopy | 16139264 |
| principal piece of the flagellum | sperm | Indirect immunofluorescence | 16139264 |
| principal piece of the flagellum | sperm | Immunofluorescence | 11820818 |
| fibrous sheath | sperm | Immunoelectron microscopy | 11820818 |
| cytoplasm | spermatocytes within the seminiferous tubules | IHC | 18421703 |
Protein function and interaction
CABYR is a calcium-binding protein, that undergoes tyrosine (Naaby-Hansen et al., 2002 PMID: 11820818) and serine/threonine (Ficarro et al., 2003 PMID: 12509440) phosphorylation during sperm capacitation. Capacitation prepares the sperm to undergo the acrosome reaction and is also associated with changes in sperm motility. Kim et al, 2005 (PMID: 16139264) postulates that CABYR may have a role in calcium signaling pathways that regulate sperm motility during sperm capacitation.Immunoprecipitation studies demonstrated that CABYR binds FSCB (fibrous sheath CABYR binding) protein in mouse sperm (Li et al., 2007 PMID: 17855365). Two non-testis-specific variants of CABYR interact with glycogen synthase kinase 3 (GSK3b) in the yeast two-hybrid and GST pull down assay. GSK3b is able to phosphorylate these CABYR variants. The non-testis-specific variants exhibit aberrant expression in brain tumors, suggesting that these proteins may also be important in brain development and tumorigenesis (Hsu et al., 2005 PMID: 15752768). CABYR-a isoform was found to interact with α-enolase in vivo (Tseng et al., 2011 PMID: 21274509).
