LASP1

LASP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3I35
Identifiers
Aliases	LASP1, MLN50, LIM and SH3 protein 1, LASP-1
External IDs	OMIM: 602920 MGI: 109656 HomoloGene: 4480 GeneCards: LASP1
Gene location (Human) Chr. Chromosome 17 (human) Band 17q12 Start 38,869,859 bp End 38,921,770 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11 D|11 61.1 cM Start 97,689,826 bp End 97,729,590 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in lower lobe of lung jejunal mucosa lactiferous duct duodenum stromal cell of endometrium superficial temporal artery trabecular bone thymus pylorus blood Top expressed in retinal pigment epithelium conjunctival fornix external carotid artery ciliary body internal carotid artery epithelium of stomach otic placode saccule sexually immature organism iris More reference expression data BioGPS More reference expression data
Gene ontology Molecular function ion transmembrane transporter activity actin filament binding actin binding protein binding metal ion binding cadherin binding Cellular component cell cortex extracellular exosome cytoskeleton focal adhesion cortical actin cytoskeleton cytoplasm Biological process ion transmembrane transport ion transport positive regulation of signal transduction transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3927 16796 Ensembl ENSG00000002834 ENSMUSG00000038366 UniProt Q14847 Q61792 RefSeq (mRNA) NM_001271608 NM_006148 NM_010688 RefSeq (protein) NP_001258537 NP_006139 NP_034818 Location (UCSC) Chr 17: 38.87 – 38.92 Mb Chr 11: 97.69 – 97.73 Mb PubMed search
Wikidata
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LIM and SH3 domain protein 1 is a protein that in humans is encoded by the LASP1 gene.

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.

Interactions

LASP1 has been shown to interact with Zyxin.

Further reading

• 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. doi:10.1016/0014-5793(95)01040-L. PMID 7589475. S2CID 648563.
• 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. doi:10.1152/ajpcell.1998.275.1.C56. 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. doi:10.1007/BF03401929. PMC 2230251. 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. doi:10.1242/jcs.00174. PMID 12432067. S2CID 18385678.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. 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:10.1074/jbc.M209009200. 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:10.1038/nbt810. PMID 12665801. S2CID 23783563.
• 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:10.1038/ng1285. 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:10.1074/jbc.M310304200. 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:10.1016/j.bbrc.2004.08.235. 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:10.1101/gr.2596504. PMC 528928. 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:10.1038/nmeth776. PMID 16094384. S2CID 20475874.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• 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:10.1016/j.yexcr.2005.12.016. PMID 16430883.