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FBLIM1
Identifiers
Aliases	FBLIM1, CAL, FBLP-1, FBLP1, filamin binding LIM protein 1
External IDs	OMIM: 607747; MGI: 1921452; GeneCards: FBLIM1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2K9U, 2W0P, 4P3W
Gene location (Human)
Chr.	Chromosome 1 (human)
End	15,786,594 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	141,333,407 bp
RNA expression pattern
	Top expressed in
	right coronary artery; ; Descending thoracic aorta; ; ascending aorta; ; mucosa of ileum; ; popliteal artery; ; tibial arteries; ; cardiac muscle tissue of right atrium; ; saphenous vein; ; pancreatic ductal cell; ; left coronary artery;
	Top expressed in
	interventricular septum; ; ascending aorta; ; tunica media of zone of aorta; ; aortic valve; ; myocardium of ventricle; ; right ventricle; ; genital tubercle; ; cardiac muscles; ; epithelium of stomach; ; left colon;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	filamin binding; protein binding; metal ion binding;
Cellular component	cytoplasm; cytosol; cell cortex; cytoskeleton; stress fiber; focal adhesion; fibrillar center; cell junction;
Biological process	regulation of integrin activation; cell adhesion; cell junction assembly; regulation of cell shape; cell-cell adhesion;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	54751
	74202
	ENSG00000162458
	ENSMUSG00000006219
	Q8WUP2
	Q71FD7
	NM_001024215; NM_001024216; NM_017556; NM_001350151
	NM_001163256; NM_133754; NM_001378958; NM_001378959
	NP_001019386; NP_001019387; NP_060026; NP_001337080
NP_001156728; NP_598515; NP_001365887; NP_001365888; NP_001391569;
	NP_001391570; NP_001391571; NP_001391572; NP_001391573
	Wikidata
View/Edit Human	View/Edit Mouse

Filamin-binding LIM protein 1 is a protein that in humans is encoded by the FBLIM1 gene.^[5]^[6]^[7]

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 NKX2-5 transcription factor. Alternative splicing results in multiple transcript variants encoding different isoforms.^[7]

Interactions

FBLIM1 has been shown to interact with filamin,^[8] PLEKHC1^[5] and FLNB.^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000162458 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000006219 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b 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. S2CID 15051526.
^ 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.
^ ^a ^b "Entrez Gene: FBLIM1 filamin binding LIM protein 1".
^ Tu Y, 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. 113 (1). United States: 37–47. doi:10.1016/S0092-8674(03)00163-6. ISSN 0092-8674. PMID 12679033. S2CID 15051526.
^ Takafuta T, 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. 278 (14). United States: 12175–81. doi:10.1074/jbc.M209339200. ISSN 0021-9258. PMID 12496242.

Wu C (2005). "Migfilin and its binding partners: from cell biology to human diseases". J. Cell Sci. 118 (Pt 4): 659–64. doi:10.1242/jcs.01639. PMID 15701922. S2CID 14289176.
Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD (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.
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Akazawa H, Kudoh S, Mochizuki N, Takekoshi N, Takano H, Nagai T, Komuro I (2004). "A novel LIM protein Cal promotes cardiac differentiation by association with CSX/NKX2-5". J. Cell Biol. 164 (3): 395–405. doi:10.1083/jcb.200309159. PMC 2172236. PMID 14757752.
Brandenberger R, Wei H, Zhang S, Lei S, Murage J, Fisk GJ, Li Y, Xu C, Fang R (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R (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.
Gkretsi V, Zhang Y, Tu Y, Chen K, Stolz DB, Yang Y, Watkins SC, Wu C (2005). "Physical and functional association of migfilin with cell-cell adhesions". J. Cell Sci. 118 (Pt 4): 697–710. doi:10.1242/jcs.01638. PMID 15671069.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M (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.
Oh JH, Yang JO, Hahn Y, Kim MR, Byun SS, Jeon YJ, Kim JM, Song KS, Noh SM (2006). "Transcriptome analysis of human gastric cancer". Mamm. Genome. 16 (12): 942–54. doi:10.1007/s00335-005-0075-2. PMID 16341674. S2CID 69278.
Zhang Y, Tu Y, Gkretsi V, Wu C (2006). "Migfilin interacts with vasodilator-stimulated phosphoprotein (VASP) and regulates VASP localization to cell-matrix adhesions and migration". J. Biol. Chem. 281 (18): 12397–407. doi:10.1074/jbc.M512107200. PMID 16531412.
Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.
Papachristou DJ, Gkretsi V, Tu Y, Shi X, Chen K, Larjava H, Rao UN, Wu C (2007). "Increased cytoplasmic level of migfilin is associated with higher grades of human leiomyosarcoma". Histopathology. 51 (4): 499–508. doi:10.1111/j.1365-2559.2007.02791.x. PMC 2768333. PMID 17711449.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000162458 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000006219 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid12679033-5] 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. S2CID 15051526.

[pmid12496242-6] 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.

[entrez-7] "Entrez Gene: FBLIM1 filamin binding LIM protein 1".

[autogenerated2-8] Tu Y, 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. 113 (1). United States: 37–47. doi:10.1016/S0092-8674(03)00163-6. ISSN 0092-8674. PMID 12679033. S2CID 15051526.

[autogenerated1-9] Takafuta T, 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. 278 (14). United States: 12175–81. doi:10.1074/jbc.M209339200. ISSN 0021-9258. PMID 12496242.

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FBLIM1

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