LASP1

LASP1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
3I35

Identifiers

LASP1, Lasp-1, MLN50, LIM and SH3 protein 1

External IDs

MGI: 109656 HomoloGene: 4480 GeneCards: LASP1

Gene ontology
Molecular function	• ion transmembrane transporter activity • actin filament binding • actin binding • protein binding • metal ion binding • SH3/SH2 adaptor activity • 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

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse


3927


16796


ENSG00000002834


ENSMUSG00000038366


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: 97.8 – 97.84 Mb

PubMed search

^[1]

^[2]

View/Edit Human

View/Edit Mouse

LIM and SH3 domain protein 1 is a protein that in humans is encoded by the LASP1 gene.^[3]^[4]

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.^[4]

Interactions

LASP1 has been shown to interact with Zyxin.^[5]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Tomasetto C, Regnier C, Moog-Lutz C, Mattei MG, Chenard MP, Lidereau R, Basset P, Rio MC (Jan 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. PMID 7490069. doi:10.1006/geno.1995.1163.
1 2 "Entrez Gene: LASP1 LIM and SH3 protein 1".
↑ Li, Bo; Zhuang Lei; Trueb Beat (May 2004). "Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1". J. Biol. Chem. United States. 279 (19): 20401–10. ISSN 0021-9258. PMID 15004028. doi:10.1074/jbc.M310304200.

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. PMID 7589475. doi:10.1016/0014-5793(95)01040-L.
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. 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. PMID 12432067. doi:10.1242/jcs.00174.
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. PMC 139241 . PMID 12477932. doi:10.1073/pnas.242603899.
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. PMID 12571245. doi:10.1074/jbc.M209009200.
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. PMID 12665801. doi:10.1038/nbt810.
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. PMID 14702039. doi:10.1038/ng1285.
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. PMID 15004028. doi:10.1074/jbc.M310304200.
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. PMID 15465019. doi:10.1016/j.bbrc.2004.08.235.
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. PMC 528928 . PMID 15489334. doi:10.1101/gr.2596504.
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. PMID 16094384. doi:10.1038/nmeth776.
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. PMID 16189514. doi:10.1038/nature04209.
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. PMID 16430883. doi:10.1016/j.yexcr.2005.12.016.

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