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{{Infobox_gene}}
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'''Filamin-binding LIM protein 1''' is a [[protein]] that in humans is encoded by the ''FBLIM1'' [[gene]].<ref name="pmid12679033">{{cite journal | vauthors = Tu Y, Wu S, Shi X, Chen K, Wu C | title = Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation | journal = Cell | volume = 113 | issue = 1 | pages = 37–47 |date=April 2003 | pmid = 12679033 | pmc =  | doi =10.1016/S0092-8674(03)00163-6 }}</ref><ref name="pmid12496242">{{cite journal | vauthors = Takafuta T, Saeki M, Fujimoto TT, Fujimura K, Shapiro SS | title = A new member of the LIM protein family binds to filamin B and localizes at stress fibers | journal = J Biol Chem | volume = 278 | issue = 14 | pages = 12175–81 |date=March 2003 | pmid = 12496242 | pmc =  | doi = 10.1074/jbc.M209339200 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: FBLIM1 filamin binding LIM protein 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54751| 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 =
| image_source =
| PDB =
| Name = Filamin binding LIM protein 1
| HGNCid = 24686
| Symbol = FBLIM1
| AltSymbols =; CAL; DKFZp434G171; FBLP-1; FBLP1; RP11-169K16.5
| OMIM = 607747
| ECnumber =
| Homologene = 56774
| MGIid = 1921452
  | GeneAtlas_image1 = PBB_GE_FBLIM1_gnf1h06896_at_tn.png
  | Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0008360 |text = regulation of cell shape}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 54751
    | Hs_Ensembl = ENSG00000162458
    | Hs_RefseqProtein = NP_001019386
    | Hs_RefseqmRNA = NM_001024215
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 15955741
    | Hs_GenLoc_end = 15985676
    | Hs_Uniprot = Q8WUP2
    | Mm_EntrezGene = 74202
    | Mm_Ensembl = ENSMUSG00000006219
    | Mm_RefseqmRNA = NM_133754
    | Mm_RefseqProtein = NP_598515
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 140848801
    | Mm_GenLoc_end = 140870300
    | Mm_Uniprot = Q3TDK3
  }}
}}
'''Filamin binding LIM protein 1''', also known as '''FBLIM1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FBLIM1 filamin binding LIM protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54751| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene encodes a protein with an N-terminal filamin-binding domain, a central proline-rich domain, and, multiple C-terminal LIM domains. This protein localizes at cell junctions and may link cell adhesion structures to the actin cytoskeleton. This protein may be involved in the assembly and stabilization of actin-filaments and likely plays a role in modulating cell adhesion, cell morphology and cell motility. This protein also localizes to the nucleus and may affect cardiomyocyte differentiation after binding with the CSX/NKX2-5 transcription factor. Alternative splicing results in multiple transcript variants encoding different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: FBLIM1 filamin binding LIM protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=54751| accessdate = }}</ref>
| summary_text = This gene encodes a protein with an N-terminal filamin-binding domain, a central proline-rich domain, and, multiple C-terminal LIM domains. This protein localizes at cell junctions and may link cell adhesion structures to the actin cytoskeleton. This protein may be involved in the assembly and stabilization of actin-filaments and likely plays a role in modulating cell adhesion, cell morphology and cell motility. This protein also localizes to the nucleus and may affect cardiomyocyte differentiation after binding with the CSX/NKX2-5 transcription factor. Alternative splicing results in multiple transcript variants encoding different isoforms.<ref name="entrez" />
}}
}}
==Interactions==
FBLIM1 has been shown to [[Protein-protein interaction|interact]] with [[Filamin]],<ref name=autogenerated2>{{cite journal |last=Tu |first=Yizeng |author2=Wu Shan |author3=Shi Xiaohua |author4=Chen Ka |author5=Wu Chuanyue  |date=April 2003  |title=Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation |journal=Cell |volume=113 |issue=1 |pages=37–47 |publisher= |location = United States| issn = 0092-8674| pmid = 12679033 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1016/S0092-8674(03)00163-6 }}</ref> [[PLEKHC1]]<ref name=pmid12679033/> and [[FLNB]].<ref name=autogenerated1>{{cite journal |last=Takafuta |first=Toshiro |author2=Saeki Mari |author3=Fujimoto Tetsuro-Takahiro |author4=Fujimura Kingo |author5=Shapiro Sandor S  |date=April 2003  |title=A new member of the LIM protein family binds to filamin B and localizes at stress fibers |journal=J. Biol. Chem. |volume=278 |issue=14 |pages=12175–81 |publisher= |location = United States| issn = 0021-9258| pmid = 12496242 |doi = 10.1074/jbc.M209339200 | 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=Wu C |title=Migfilin and its binding partners: from cell biology to human diseases. |journal=J. Cell. Sci. |volume=118 |issue= Pt 4 |pages= 659-64 |year= 2005 |pmid= 15701922 |doi= 10.1242/jcs.01639 }}
*{{cite journal  | author=Wu C |title=Migfilin and its binding partners: from cell biology to human diseases |journal=J. Cell Sci. |volume=118 |issue= Pt 4 |pages= 659–64 |year= 2005 |pmid= 15701922 |doi= 10.1242/jcs.01639 }}
*{{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  | author=Strausberg RL |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  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD |bibcode=2002PNAS...9916899M}}
*{{cite journal | author=Takafuta T, Saeki M, Fujimoto TT, ''et al.'' |title=A new member of the LIM protein family binds to filamin B and localizes at stress fibers. |journal=J. Biol. Chem. |volume=278 |issue= 14 |pages= 12175-81 |year= 2003 |pmid= 12496242 |doi= 10.1074/jbc.M209339200 }}
*{{cite journal  | author=Ota T |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 |name-list-format=vanc| author2=Suzuki Y  | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
*{{cite journal | author=Tu Y, Wu S, Shi X, ''et al.'' |title=Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. |journal=Cell |volume=113 |issue= 1 |pages= 37-47 |year= 2003 |pmid= 12679033 |doi= }}
*{{cite journal  | author=Akazawa H |title=A novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5 |journal=J. Cell Biol. |volume=164 |issue= 3 |pages= 395–405 |year= 2004 |pmid= 14757752 |doi= 10.1083/jcb.200309159 | pmc=2172236  |name-list-format=vanc| author2=Kudoh S  | author3=Mochizuki N  | display-authors=3  | last4=Takekoshi  | first4=N  | last5=Takano  | first5=H  | last6=Nagai  | first6=T  | last7=Komuro  | first7=I }}
*{{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  | author=Brandenberger R |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707–16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 |name-list-format=vanc| author2=Wei H  | author3=Zhang S  | display-authors=3  | last4=Lei  | first4=Shirley  | last5=Murage  | first5=Jaji  | last6=Fisk  | first6=Gregory J  | last7=Li  | first7=Yan  | last8=Xu  | first8=Chunhui  | last9=Fang  | first9=Rixun }}
*{{cite journal  | author=Akazawa H, Kudoh S, Mochizuki N, ''et al.'' |title=A novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5. |journal=J. Cell Biol. |volume=164 |issue= 3 |pages= 395-405 |year= 2004 |pmid= 14757752 |doi= 10.1083/jcb.200309159 }}
*{{cite journal  | author=Gerhard DS |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  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
*{{cite journal  | author=Brandenberger R, Wei H, Zhang S, ''et al.'' |title=Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. |journal=Nat. Biotechnol. |volume=22 |issue= 6 |pages= 707-16 |year= 2005 |pmid= 15146197 |doi= 10.1038/nbt971 }}
*{{cite journal  | author=Gkretsi V |title=Physical and functional association of migfilin with cell-cell adhesions |journal=J. Cell Sci. |volume=118 |issue= Pt 4 |pages= 697–710 |year= 2005 |pmid= 15671069 |doi= 10.1242/jcs.01638 |name-list-format=vanc| author2=Zhang Y  | author3=Tu Y  | display-authors=3  | last4=Chen  | first4=K  | last5=Stolz  | first5=DB  | last6=Yang  | first6=Y  | last7=Watkins  | first7=SC  | last8=Wu  | first8=C }}
*{{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  | author=Rual JF |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 |name-list-format=vanc| author2=Venkatesan K  | author3=Hao T  | display-authors=3  | last4=Hirozane-Kishikawa  | first4=Tomoko  | last5=Dricot  | first5=Amélie  | last6=Li  | first6=Ning  | last7=Berriz  | first7=Gabriel F.  | last8=Gibbons  | first8=Francis D.  | last9=Dreze  | first9=Matija |bibcode=2005Natur.437.1173R}}
*{{cite journal  | author=Gkretsi V, Zhang Y, Tu Y, ''et al.'' |title=Physical and functional association of migfilin with cell-cell adhesions. |journal=J. Cell. Sci. |volume=118 |issue= Pt 4 |pages= 697-710 |year= 2005 |pmid= 15671069 |doi= 10.1242/jcs.01638 }}
*{{cite journal  | author=Oh JH |title=Transcriptome analysis of human gastric cancer |journal=Mamm. Genome |volume=16 |issue= 12 |pages= 942–54 |year= 2006 |pmid= 16341674 |doi= 10.1007/s00335-005-0075-2 |name-list-format=vanc| author2=Yang JO  | author3=Hahn Y  | display-authors=3  | last4=Kim  | first4=Mi-Rang  | last5=Byun  | first5=Sang-Soon  | last6=Jeon  | first6=Yeo-Jin  | last7=Kim  | first7=Jeong-Min  | last8=Song  | first8=Kyu-Sang  | last9=Noh  | first9=Seung-Moo }}
*{{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=Zhang Y, Tu Y, Gkretsi V, Wu C |title=Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration |journal=J. Biol. Chem. |volume=281 |issue= 18 |pages= 12397–407 |year= 2006 |pmid= 16531412 |doi= 10.1074/jbc.M512107200 }}
*{{cite journal  | author=Oh JH, Yang JO, Hahn Y, ''et al.'' |title=Transcriptome analysis of human gastric cancer. |journal=Mamm. Genome |volume=16 |issue= 12 |pages= 942-54 |year= 2006 |pmid= 16341674 |doi= 10.1007/s00335-005-0075-2 }}
*{{cite journal  | author=Gregory SG |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |name-list-format=vanc| author2=Barlow KF  | author3=McLay KE  | display-authors=3  | last4=Kaul  | first4=R.  | last5=Swarbreck  | first5=D.  | last6=Dunham  | first6=A.  | last7=Scott  | first7=C. E.  | last8=Howe  | first8=K. L.  | last9=Woodfine  | first9=K. |bibcode=2006Natur.441..315G}}
*{{cite journal  | author=Zhang Y, Tu Y, Gkretsi V, Wu C |title=Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration. |journal=J. Biol. Chem. |volume=281 |issue= 18 |pages= 12397-407 |year= 2006 |pmid= 16531412 |doi= 10.1074/jbc.M512107200 }}
*{{cite journal  | author=Papachristou DJ |title=Increased cytoplasmic level of migfilin is associated with higher grades of human leiomyosarcoma |journal=Histopathology |volume=51 |issue= 4 |pages= 499–508 |year= 2007 |pmid= 17711449 |doi= 10.1111/j.1365-2559.2007.02791.x | pmc=2768333  |name-list-format=vanc| author2=Gkretsi V  | author3=Tu Y  | display-authors=3  | last4=Shi  | first4=X  | last5=Chen  | first5=K  | last6=Larjava  | first6=H  | last7=Rao  | first7=U N M  | last8=Wu  | first8=C }}
*{{cite journal  | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
*{{cite journal  | author=Papachristou DJ, Gkretsi V, Tu Y, ''et al.'' |title=Increased cytoplasmic level of migfilin is associated with higher grades of human leiomyosarcoma. |journal=Histopathology |volume=51 |issue= 4 |pages= 499-508 |year= 2007 |pmid= 17711449 |doi= 10.1111/j.1365-2559.2007.02791.x }}
}}
}}
{{refend}}
{{refend}}


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{{gene-1-stub}}

Latest revision as of 14:02, 23 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

Filamin-binding LIM protein 1 is a protein that in humans is encoded by the FBLIM1 gene.[1][2][3]

This gene encodes a protein with an N-terminal filamin-binding domain, a central proline-rich domain, and, multiple C-terminal LIM domains. This protein localizes at cell junctions and may link cell adhesion structures to the actin cytoskeleton. This protein may be involved in the assembly and stabilization of actin-filaments and likely plays a role in modulating cell adhesion, cell morphology and cell motility. This protein also localizes to the nucleus and may affect cardiomyocyte differentiation after binding with the CSX/NKX2-5 transcription factor. Alternative splicing results in multiple transcript variants encoding different isoforms.[3]

Interactions

FBLIM1 has been shown to interact with Filamin,[4] PLEKHC1[1] and FLNB.[5]

References

  1. ↑ 1.0 1.1 Tu Y, Wu S, Shi X, Chen K, Wu C (April 2003). "Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation". Cell. 113 (1): 37–47. doi:10.1016/S0092-8674(03)00163-6. PMID 12679033.
  2. ↑ Takafuta T, Saeki M, Fujimoto TT, Fujimura K, Shapiro SS (March 2003). "A new member of the LIM protein family binds to filamin B and localizes at stress fibers". J Biol Chem. 278 (14): 12175–81. doi:10.1074/jbc.M209339200. PMID 12496242.
  3. ↑ 3.0 3.1 "Entrez Gene: FBLIM1 filamin binding LIM protein 1".
  4. ↑ Tu, Yizeng; Wu Shan; Shi Xiaohua; Chen Ka; Wu Chuanyue (April 2003). "Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation". Cell. United States. 113 (1): 37–47. doi:10.1016/S0092-8674(03)00163-6. ISSN 0092-8674. PMID 12679033.
  5. ↑ Takafuta, Toshiro; Saeki Mari; Fujimoto Tetsuro-Takahiro; Fujimura Kingo; Shapiro Sandor S (April 2003). "A new member of the LIM protein family binds to filamin B and localizes at stress fibers". J. Biol. Chem. United States. 278 (14): 12175–81. doi:10.1074/jbc.M209339200. ISSN 0021-9258. PMID 12496242.

Further reading



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