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{{Infobox_gene}}
{{PBB_Controls
'''LIM and SH3 domain protein 1''' is a [[protein]] that in humans is encoded by the ''LASP1'' [[gene]].<ref name="pmid7490069">{{cite journal |vauthors=Tomasetto C, Regnier C, Moog-Lutz C, Mattei MG, Chenard MP, Lidereau R, Basset P, Rio MC | title = Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17 | journal = Genomics | volume = 28 | issue = 3 | pages = 367–76 |date=Jan 1996 | pmid = 7490069 | pmc =  | doi = 10.1006/geno.1995.1163 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: LASP1 LIM and SH3 protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3927| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_LASP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1zfo.
| PDB = {{PDB2|1zfo}}
| Name = LIM and SH3 protein 1
| HGNCid = 6513
| Symbol = LASP1
| AltSymbols =; Lasp-1; MLN50
| OMIM = 602920
| ECnumber = 
| Homologene = 4480
| MGIid = 109656
| GeneAtlas_image1 = PBB_GE_LASP1_200618_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005070 |text = SH3/SH2 adaptor activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0015075 |text = ion transmembrane transporter activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0030864 |text = cortical actin cytoskeleton}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0030865 |text = cortical cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3927
    | Hs_Ensembl = ENSG00000002834
    | Hs_RefseqProtein = NP_006139
    | Hs_RefseqmRNA = NM_006148
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 34279894
    | Hs_GenLoc_end = 34331541
    | Hs_Uniprot = Q14847
    | Mm_EntrezGene = 16796
    | Mm_Ensembl = ENSMUSG00000038366
    | Mm_RefseqmRNA = NM_010688
    | Mm_RefseqProtein = NP_034818
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 97615762
    | Mm_GenLoc_end = 97654854
    | Mm_Uniprot = Q543N3
  }}
}}
'''LIM and SH3 protein 1''', also known as '''LASP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LASP1 LIM and SH3 protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3927| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: LASP1 LIM and SH3 protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3927| accessdate = }}</ref>
| summary_text = 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.<ref name="entrez"/>
}}
}}
==Interactions==
LASP1 has been shown to [[Protein-protein interaction|interact]] with [[Zyxin]].<ref name=pmid15004028>{{cite journal |last=Li |first=Bo |authorlink= |author2=Zhuang Lei |author3=Trueb Beat  |date=May 2004 |title=Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1 |journal=J. Biol. Chem. |volume=279 |issue=19 |pages=20401–10 |publisher= |location = United States| issn = 0021-9258| pmid = 15004028 |doi = 10.1074/jbc.M310304200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Tomasetto C, Régnier C, Moog-Lutz C, ''et al.'' |title=Identification of four novel human genes amplified and overexpressed in breast carcinoma and localized to the q11-q21.3 region of chromosome 17. |journal=Genomics |volume=28 |issue= 3 |pages= 367-76 |year= 1996 |pmid= 7490069 |doi= 10.1006/geno.1995.1163 }}
*{{cite journal   |vauthors=Tomasetto C, Moog-Lutz C, Régnier CH, etal |title=Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by the association of LIM and SH3 domains. |journal=FEBS Lett. |volume=373 |issue= 3 |pages= 245–9 |year= 1995 |pmid= 7589475 |doi=10.1016/0014-5793(95)01040-L }}
*{{cite journal  | author=Tomasetto C, Moog-Lutz C, Régnier CH, ''et al.'' |title=Lasp-1 (MLN 50) defines a new LIM protein subfamily characterized by the association of LIM and SH3 domains. |journal=FEBS Lett. |volume=373 |issue= 3 |pages= 245-9 |year= 1995 |pmid= 7589475 |doi=  }}
*{{cite journal   |vauthors=Chew CS, Parente JA, Zhou C, etal |title=Lasp-1 is a regulated phosphoprotein within the cAMP signaling pathway in the gastric parietal cell. |journal=Am. J. Physiol. |volume=275 |issue= 1 Pt 1 |pages= C56–67 |year= 1998 |pmid= 9688835 |doi=  }}
*{{cite journal | author=Chew CS, Parente JA, Zhou C, ''et al.'' |title=Lasp-1 is a regulated phosphoprotein within the cAMP signaling pathway in the gastric parietal cell. |journal=Am. J. Physiol. |volume=275 |issue= 1 Pt 1 |pages= C56-67 |year= 1998 |pmid= 9688835 |doi=  }}
*{{cite journal   |vauthors=Schreiber V, Moog-Lutz C, Régnier CH, etal |title=Lasp-1, a novel type of actin-binding protein accumulating in cell membrane extensions. |journal=Mol. Med. |volume=4 |issue= 10 |pages= 675–87 |year= 1999 |pmid= 9848085 |doi= | pmc=2230251 }}
*{{cite journal | author=Schreiber V, Moog-Lutz C, Régnier CH, ''et al.'' |title=Lasp-1, a novel type of actin-binding protein accumulating in cell membrane extensions. |journal=Mol. Med. |volume=4 |issue= 10 |pages= 675-87 |year= 1999 |pmid= 9848085 |doi=  }}
*{{cite journal   |vauthors=Chew CS, Chen X, Parente JA, etal |title=Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo. |journal=J. Cell Sci. |volume=115 |issue= Pt 24 |pages= 4787–99 |year= 2003 |pmid= 12432067 |doi=10.1242/jcs.00174 }}
*{{cite journal | author=Chew CS, Chen X, Parente JA, ''et al.'' |title=Lasp-1 binds to non-muscle F-actin in vitro and is localized within multiple sites of dynamic actin assembly in vivo. |journal=J. Cell. Sci. |volume=115 |issue= Pt 24 |pages= 4787-99 |year= 2003 |pmid= 12432067 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Butt E, Gambaryan S, Göttfert N, etal |title=Actin binding of human LIM and SH3 protein is regulated by cGMP- and cAMP-dependent protein kinase phosphorylation on serine 146. |journal=J. Biol. Chem. |volume=278 |issue= 18 |pages= 15601–7 |year= 2003 |pmid= 12571245 |doi= 10.1074/jbc.M209009200 }}
*{{cite journal | author=Butt E, Gambaryan S, Göttfert N, ''et al.'' |title=Actin binding of human LIM and SH3 protein is regulated by cGMP- and cAMP-dependent protein kinase phosphorylation on serine 146. |journal=J. Biol. Chem. |volume=278 |issue= 18 |pages= 15601-7 |year= 2003 |pmid= 12571245 |doi= 10.1074/jbc.M209009200 }}
*{{cite journal   |vauthors=Gevaert K, Goethals M, Martens L, etal |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566–9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Li B, Zhuang L, Trueb B |title=Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1. |journal=J. Biol. Chem. |volume=279 |issue= 19 |pages= 20401–10 |year= 2004 |pmid= 15004028 |doi= 10.1074/jbc.M310304200 }}
*{{cite journal  | author=Li B, Zhuang L, Trueb B |title=Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1. |journal=J. Biol. Chem. |volume=279 |issue= 19 |pages= 20401-10 |year= 2004 |pmid= 15004028 |doi= 10.1074/jbc.M310304200 }}
*{{cite journal   |vauthors=Keicher C, Gambaryan S, Schulze E, etal |title=Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase. |journal=Biochem. Biophys. Res. Commun. |volume=324 |issue= 1 |pages= 308–16 |year= 2004 |pmid= 15465019 |doi= 10.1016/j.bbrc.2004.08.235 }}
*{{cite journal | author=Keicher C, Gambaryan S, Schulze E, ''et al.'' |title=Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-dependent protein kinase. |journal=Biochem. Biophys. Res. Commun. |volume=324 |issue= 1 |pages= 308-16 |year= 2004 |pmid= 15465019 |doi= 10.1016/j.bbrc.2004.08.235 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Tao WA, Wollscheid B, O'Brien R, etal |title=Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. |journal=Nat. Methods |volume=2 |issue= 8 |pages= 591–8 |year= 2005 |pmid= 16094384 |doi= 10.1038/nmeth776 }}
*{{cite journal | author=Tao WA, Wollscheid B, O'Brien R, ''et al.'' |title=Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. |journal=Nat. Methods |volume=2 |issue= 8 |pages= 591-8 |year= 2005 |pmid= 16094384 |doi= 10.1038/nmeth776 }}
*{{cite journal   |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 |bibcode=2005Natur.437.1173R }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal   |vauthors=Grunewald TG, Kammerer U, Schulze E, etal |title=Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells. |journal=Exp. Cell Res. |volume=312 |issue= 7 |pages= 974–82 |year= 2006 |pmid= 16430883 |doi= 10.1016/j.yexcr.2005.12.016 }}
*{{cite journal | author=Grunewald TG, Kammerer U, Schulze E, ''et al.'' |title=Silencing of LASP-1 influences zyxin localization, inhibits proliferation and reduces migration in breast cancer cells. |journal=Exp. Cell Res. |volume=312 |issue= 7 |pages= 974-82 |year= 2006 |pmid= 16430883 |doi= 10.1016/j.yexcr.2005.12.016 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=3927}}
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Latest revision as of 18:33, 24 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

LIM and SH3 domain protein 1 is a protein that in humans is encoded by the LASP1 gene.[1][2]

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.[2]

Interactions

LASP1 has been shown to interact with Zyxin.[3]

References

  1. ↑ 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. doi:10.1006/geno.1995.1163. PMID 7490069.
  2. ↑ 2.0 2.1 "Entrez Gene: LASP1 LIM and SH3 protein 1".
  3. ↑ 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. doi:10.1074/jbc.M310304200. ISSN 0021-9258. PMID 15004028.

Further reading



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