Alternative titles; symbols
HGNC Approved Gene Symbol: NCKIPSD
Cytogenetic location: 3p21.31 Genomic coordinates (GRCh38) : 3:48,673,844-48,685,915 (from NCBI)
Sano et al. (2000) identified the NCKIPSD gene, which they called AF3p21, as a novel fusion partner of the MLL gene (159555) in a 23-year-old patient who developed therapy-related leukemia (AML, FAB M5b) with t(3;11)(p21;q23). Hayakawa et al. (2001) further characterized the AF3p21 gene. AF3p21 encodes a nuclear protein consisting of 722 amino acids with an SH3 domain, a proline-rich domain, and a bipartite nuclear localization signal. The protein's SH3 domain has high homology with that of FYN (137025). Dot blot RNA analysis showed that the AF3p21 gene was expressed in all adult and embryonic human tissues examined, including bone marrow, brain, liver, thymus, lung, and skeletal muscle. Northern blot analysis of HeLa cell RNA detected a 3.5-kb transcript. The protein had an apparent molecular mass of 80 kD and localized exclusively in the cell nucleus.
Using a yeast 2-hybrid screen of a human bone marrow cDNA expression library with FHOD1 (606881) as bait, Westendorf and Koka (2004) obtained a putative splice variant of WISH that they called WISH-B. The deduced 663-amino acid WISH-B protein lacks the C-terminal domain of full-length WISH.
Hayakawa et al. (2001) determined that the NCKIPSD gene spans 19 kb and contains 13 exons.
Sano et al. (2000) mapped the NCKIPSD gene to chromosome 3p21.
Using protein pull-down and immunoprecipitation analysis, Rahimi et al. (2012) found that the SH3 domain of SPIN90 interacted with the proline-rich C terminus of IGPR1 (TMIGD2; 614715). Overexpression or knockdown of either protein increased or reduced, respectively, tube formation by mouse or human endothelial cells in 3-dimensional culture. Rahimi et al. (2012) hypothesized that interaction between IGPR1 and SPIN90 regulates angiogenesis.
Using a yeast 2-hybrid screen with a human bone marrow cDNA expression library, Westendorf and Koka (2004) found that FHOD1 interacted with PRKCBP1 (ZMYND8; 615713), cyclophilin B (PPIB; 123841), and WISH-B. Coimmunoprecipitation analysis confirmed the interaction between FHOD1 and WISH-B. Domain analysis revealed that the N-terminal SH3 and PST domains of WISH-B interacted predominantly with the FH1 domain of FHOD1. The N-terminal domains of WISH-B, but not full-length WISH-B, inhibited FHOD1-induced stress fiber formation in transfected HEK293T cells. However, full-length WISH-B altered the solubility of FHOD1, suggesting that WISH-B may influence the subcellular localization of FHOD1 or recruit it to larger protein complexes.
Sano et al. (2000) identified the AF3p21 gene as a novel fusion partner of the MLL gene (159555) in a 23-year-old patient who developed therapy-related leukemia (AML, FAB M5b) with t(3;11)(p21;q23). Hayakawa et al. (2001) found that in DNA from the patient's leukemic cells, intron 6 of the MLL gene was fused at a point upstream of exon 1 in the AF3p21 gene, and that the der(11) chromosome formed an MLL-AF3p21 fusion transcript in leukemic cells, whereas the der(3) chromosome did not form any fusion transcript.
Hayakawa, A., Matsuda, Y., Daibata, M., Nakamura, H., Sano, K. Genomic organization, tissue expression, and cellular localization of AF3p21, a fusion partner of MLL in therapy-related leukemia. Genes Chromosomes Cancer 30: 364-374, 2001. [PubMed: 11241789] [Full Text: https://doi.org/10.1002/gcc.1102]
Rahimi, N., Rezazadeh, K., Mahoney, J. E., Hartsough, E., Meyer, R. D. Identification of IGPR-1 as a novel adhesion molecule involved in angiogenesis. Molec. Biol. Cell 23: 1646-1656, 2012. [PubMed: 22419821] [Full Text: https://doi.org/10.1091/mbc.E11-11-0934]
Sano, K., Hayakawa, A., Piao, J.-H., Kosaka, Y., Nakamura, H. Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed lineage leukemia protein in a therapy-related leukemia with t(3;11)(p21;q23). Blood 95: 1066-1068, 2000. [PubMed: 10648423]
Westendorf, J. J., Koka, S. Identification of FHOD1-binding proteins and mechanisms of FHOD1-regulated actin dynamics. J. Cell. Biochem. 92: 29-41, 2004. [PubMed: 15095401] [Full Text: https://doi.org/10.1002/jcb.20031]