LASP1
From Wikipedia, the free encyclopedia
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LIM and SH3 protein 1
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| PDB rendering based on 1zfo. | ||||||||||||||
| Available structures: 1zfo | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbol(s) | LASP1; Lasp-1; MLN50 | |||||||||||||
| External IDs | OMIM: 602920 MGI: 109656 HomoloGene: 4480 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 3927 | 16796 | ||||||||||||
| Ensembl | ENSG00000002834 | ENSMUSG00000038366 | ||||||||||||
| Uniprot | Q14847 | Q543N3 | ||||||||||||
| Refseq | NM_006148 (mRNA) NP_006139 (protein) |
NM_010688 (mRNA) NP_034818 (protein) |
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| Location | Chr 17: 34.28 - 34.33 Mb | Chr 11: 97.62 - 97.65 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
LIM and SH3 protein 1, also known as LASP1, is a human gene.[1]
This gene encodes a member of a LIM protein subfamily which is characterized by a LIM motif and a domain of Src homology region 3. This protein functions as an actin-binding protein and possibly in cytoskeletal organization.[1]
[edit] References
[edit] Further reading
- Tomasetto C, Régnier C, Moog-Lutz C, et al. (1996). "Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17.". Genomics 28 (3): 367-76. doi:. PMID 7490069.
- Tomasetto C, Moog-Lutz C, Régnier CH, et al. (1995). "Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by the association of LIM and SH3 domains.". FEBS Lett. 373 (3): 245-9. PMID 7589475.
- Chew CS, Parente JA, Zhou C, et al. (1998). "Lasp-1 is a regulated phosphoprotein within the cAMP signaling pathway in the gastric parietal cell.". Am. J. Physiol. 275 (1 Pt 1): C56-67. PMID 9688835.
- Schreiber V, Moog-Lutz C, Régnier CH, et al. (1999). "Lasp-1, a novel type of actin-binding protein accumulating in cell membrane extensions.". Mol. Med. 4 (10): 675-87. PMID 9848085.
- Chew CS, Chen X, Parente JA, et al. (2003). "Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo.". J. Cell. Sci. 115 (Pt 24): 4787-99. PMID 12432067.
- 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:. PMID 12477932.
- Butt E, Gambaryan S, Göttfert N, et al. (2003). "Actin binding of human LIM and SH3 protein is regulated by cGMP- and cAMP-dependent protein kinase phosphorylation on serine 146.". J. Biol. Chem. 278 (18): 15601-7. doi:. PMID 12571245.
- Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566-9. doi:. PMID 12665801.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:. PMID 14702039.
- Li B, Zhuang L, Trueb B (2004). "Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1.". J. Biol. Chem. 279 (19): 20401-10. doi:. PMID 15004028.
- Keicher C, Gambaryan S, Schulze E, et al. (2004). "Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase.". Biochem. Biophys. Res. Commun. 324 (1): 308-16. doi:. PMID 15465019.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:. PMID 15489334.
- Tao WA, Wollscheid B, O'Brien R, et al. (2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry.". Nat. Methods 2 (8): 591-8. doi:. PMID 16094384.
- 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:. PMID 16189514.
- Grunewald TG, Kammerer U, Schulze E, et al. (2006). "Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells.". Exp. Cell Res. 312 (7): 974-82. doi:. PMID 16430883.

