Alternative titles; symbols
HGNC Approved Gene Symbol: AFAP1
Cytogenetic location: 4p16.1 Genomic coordinates (GRCh38) : 4:7,758,713-7,939,861 (from NCBI)
AFAP is an adaptor protein that binds Src (190090) family proteins and interacts with actin filaments directly (review by Baisden et al., 2001).
The chicken Afap protein, or pp110, was first identified as an SH2- and SH3-binding partner for the nonreceptor tyrosine kinase Src (Reynolds et al., 1989; Kanner et al., 1991). Flynn et al. (1993) cloned Afap, which they called Afap110, from a chick embryo cDNA library. The deduced protein contains 635 amino acids. Immunolocalization of Afap in chick embryo fibroblasts showed that it is associated with the cytoskeleton.
In a review, Baisden et al. (2001) stated that the 729-amino acid human AFAP protein shares 87% identity with the chick protein. The human AFAP protein contains a unique N terminus, followed by an SH3-binding motif, a WW-binding motif, an SH2-binding motif, a pleckstrin (173570) homology (PH) domain, a serine/threonine kinase phosphorylation domain, a PH domain, an SH2-binding motif, a leucine zipper motif, and a C-terminal actin-binding domain.
Flynn et al. (1993) presented evidence that chicken Afap can interact with the SH2 and SH3 domains of Src and other nonreceptor tyrosine kinases. They suggested that Afap may facilitate interactions between SH2 and SH3 domain-containing proteins and the cytoskeleton.
Baisden et al. (2001) reviewed the structure and function of AFAP, as well as potential binding partners and effectors of AFAP's ability to alter actin filament integrity.
Baisden et al. (2001) stated that the AFAP gene maps to chromosome 4p16.1.
Baisden, J. M., Qian, Y., Zot, H. M., Flynn, D. C. The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity. Oncogene 20: 6435-6447, 2001. [PubMed: 11607843] [Full Text: https://doi.org/10.1038/sj.onc.1204784]
Flynn, D. C., Leu, T. H., Reynolds, A. B., Parsons, J. T. Identification and sequence analysis of cDNAs encoding a 110-kilodalton actin filament-associated pp60src substrate. Molec. Cell Biol. 13: 7892-7900, 1993. [PubMed: 8247004] [Full Text: https://doi.org/10.1128/mcb.13.12.7892-7900.1993]
Kanner, S. B., Reynolds, A. B., Wang, H.-C. R., Vines, R. R., Parsons, J. T. The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110. EMBO J. 10: 1689-1698, 1991. [PubMed: 1710979] [Full Text: https://doi.org/10.1002/j.1460-2075.1991.tb07693.x]
Reynolds, A. B., Kanner, S. B., Wang, H.-C. R., Parsons, J. T. Stable association of activated pp60src with two tyrosine-phosphorylated cellular proteins. Molec. Cell Biol. 9: 3951-3958, 1989. [PubMed: 2476666] [Full Text: https://doi.org/10.1128/mcb.9.9.3951-3958.1989]