NCKIPSD
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NCK interacting protein with SH3 domain | |||||||||||||
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Identifiers | |||||||||||||
Symbols | NCKIPSD; AF3P21; DIP; DIP1; ORF1; SPIN90; WASLBP; WISH | ||||||||||||
External IDs | OMIM: 606671 MGI: 1931834 HomoloGene: 9514 GeneCards: NCKIPSD Gene | ||||||||||||
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Orthologs | |||||||||||||
Species | Human | Mouse | |||||||||||
Entrez | 51517 | 80987 | |||||||||||
Ensembl | ENSG00000213672 | ENSMUSG00000032598 | |||||||||||
UniProt | Q9NZQ3 | Q9ESJ4 | |||||||||||
RefSeq (mRNA) | NM_016453 | NM_030729 | |||||||||||
RefSeq (protein) | NP_057537 | NP_109654 | |||||||||||
Location (UCSC) | Chr 3: 48.7 – 48.72 Mb | Chr 9: 108.81 – 108.82 Mb | |||||||||||
PubMed search | |||||||||||||
NCK-interacting protein with SH3 domain is a protein that in humans is encoded by the NCKIPSD gene.[1][2][3]
The protein encoded by this gene is localized exclusively in the cell nucleus. It plays a role in signal transduction, and may function in the maintenance of sarcomeres and in the assembly of myofibrils into sarcomeres. It also plays an important role in stress fiber formation. The gene is involved in therapy-related leukemia by a chromosomal translocation t(3;11)(p21;q23) that involves this gene and the myeloid/lymphoid leukemia gene. Alternative splicing occurs in this locus and two transcript variants encoding distinct isoforms have been identified.[3]
Interactions
NCKIPSD has been shown to interact with Grb2[4][5] and NCK1.[6]
References
- ↑ Sano K, Hayakawa A, Piao JH, Kosaka Y, Nakamura H (Feb 2000). "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 (3): 1066–8. PMID 10648423.
- ↑ de Bernard M, Moschioni M, Napolitani G, Rappuoli R, Montecucco C (Feb 2000). "The VacA toxin of Helicobacter pylori identifies a new intermediate filament-interacting protein". EMBO J 19 (1): 48–56. doi:10.1093/emboj/19.1.48. PMC 1171776. PMID 10619843.
- ↑ 3.0 3.1 "Entrez Gene: NCKIPSD NCK interacting protein with SH3 domain".
- ↑ Satoh, S; Tominaga T (Oct 2001). "mDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation". J. Biol. Chem. (United States) 276 (42): 39290–4. doi:10.1074/jbc.M107026200. ISSN 0021-9258. PMID 11509578.
- ↑ Fukuoka, M; Suetsugu S, Miki H, Fukami K, Endo T, Takenawa T (Feb 2001). "A Novel Neural Wiskott-Aldrich Syndrome Protein (N-Wasp) Binding Protein, Wish, Induces Arp2/3 Complex Activation Independent of Cdc42". J. Cell Biol. (United States) 152 (3): 471–82. doi:10.1083/jcb.152.3.471. ISSN 0021-9525. PMC 2196001. PMID 11157975.
- ↑ Lim, C S; Park E S, Kim D J, Song Y H, Eom S H, Chun J S, Kim J H, Kim J K, Park D, Song W K (Apr 2001). "SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adaptor protein that is developmentally regulated during cardiac myocyte differentiation". J. Biol. Chem. (United States) 276 (16): 12871–8. doi:10.1074/jbc.M009411200. ISSN 0021-9258. PMID 11278500.
Further reading
- Fukuoka M, Suetsugu S, Miki H, et al. (2001). "A Novel Neural Wiskott-Aldrich Syndrome Protein (N-Wasp) Binding Protein, Wish, Induces Arp2/3 Complex Activation Independent of Cdc42". J. Cell Biol. 152 (3): 471–82. doi:10.1083/jcb.152.3.471. PMC 2196001. PMID 11157975.
- Hayakawa A, Matsuda Y, Daibata M, et al. (2001). "Genomic organization, tissue expression, and cellular localization of AF3p21, a fusion partner of MLL in therapy-related leukemia". Genes Chromosomes Cancer 30 (4): 364–74. doi:10.1002/gcc.1102. PMID 11241789.
- Lim CS, Park ES, Kim DJ, et al. (2001). "SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adaptor protein that is developmentally regulated during cardiac myocyte differentiation". J. Biol. Chem. 276 (16): 12871–8. doi:10.1074/jbc.M009411200. PMID 11278500.
- Satoh S, Tominaga T (2001). "mDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation". J. Biol. Chem. 276 (42): 39290–4. doi:10.1074/jbc.M107026200. PMID 11509578.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Lim CS, Kim SH, Jung JG, et al. (2004). "Regulation of SPIN90 phosphorylation and interaction with Nck by ERK and cell adhesion". J. Biol. Chem. 278 (52): 52116–23. doi:10.1074/jbc.M310974200. PMID 14559906.
- Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Kim DJ, Kim SH, Lim CS, et al. (2006). "Interaction of SPIN90 with the Arp2/3 complex mediates lamellipodia and actin comet tail formation". J. Biol. Chem. 281 (1): 617–25. doi:10.1074/jbc.M504450200. PMID 16253999.
- Eisenmann KM, Harris ES, Kitchen SM, et al. (2007). "Dia-interacting protein modulates formin-mediated actin assembly at the cell cortex". Curr. Biol. 17 (7): 579–91. doi:10.1016/j.cub.2007.03.024. PMID 17398099.
- Rönty M, Taivainen A, Heiska L, et al. (2007). "Palladin interacts with SH3 domains of SPIN90 and Src and is required for Src-induced cytoskeletal remodeling". Exp. Cell Res. 313 (12): 2575–85. doi:10.1016/j.yexcr.2007.04.030. PMC 2000818. PMID 17537434.
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