LIMS1

LIM and senescent cell antigen-like-containing domain protein 1 is a protein that in humans is encoded by the LIMS1 gene.

LIMS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1G47, 1NYP, 1U5S, 2COR, 2D8X, 2KBX, 3F6Q, 4HI8, 4HI9
Identifiers
Aliases	LIMS1, PINCH, PINCH-1, PINCH1, LIM zinc finger domain containing 1
External IDs	OMIM: 602567 MGI: 1195263 HomoloGene: 68428 GeneCards: LIMS1
Gene location (Human) Chr. Chromosome 2 (human) Band 2q12.3 Start 108,534,355 bp End 108,687,246 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10 B4|10 29.31 cM Start 58,159,288 bp End 58,260,513 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte stromal cell of endometrium gastrocnemius muscle ascending aorta corpus epididymis gallbladder caput epididymis right coronary artery Achilles tendon islet of Langerhans Top expressed in left lung lobe sciatic nerve soleus muscle atrioventricular valve corneal stroma atrium renal corpuscle semi-lunar valve dermis masseter muscle More reference expression data BioGPS n/a
Gene ontology Molecular function metal ion binding protein binding protein kinase binding zinc ion binding Cellular component cytosol membrane cell-cell junction focal adhesion plasma membrane cell junction perinuclear region of cytoplasm protein-containing complex cytoplasm Biological process cellular response to transforming growth factor beta stimulus establishment of protein localization positive regulation of GTPase activity positive regulation of substrate adhesion-dependent cell spreading positive regulation of gene expression epithelial to mesenchymal transition positive regulation of focal adhesion assembly regulation of epithelial cell proliferation negative regulation of transcription, DNA-templated cell junction assembly positive regulation of cell-substrate adhesion tumor necrosis factor-mediated signaling pathway protein heterooligomerization positive regulation of NIK/NF-kappaB signaling cell-cell junction organization cell-cell adhesion positive regulation of integrin-mediated signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3987 110829 Ensembl ENSG00000169756 ENSMUSG00000019920 UniProt P48059 Q99JW4 RefSeq (mRNA) NM_001193482 NM_001193483 NM_001193484 NM_001193485 NM_001193488 NM_004987 NM_001193303 NM_026148 NM_201242 NM_001346676 NM_001359115 NM_001359116 RefSeq (protein) NP_001180411 NP_001180412 NP_001180413 NP_001180414 NP_001180417 NP_004978 NP_001358423 NP_001358424 NP_001358425 NP_001358426 NP_001358427 NP_001358428 NP_001358429 NP_001180232 NP_001333605 NP_080424 NP_957694 NP_001346044 NP_001346045 Location (UCSC) Chr 2: 108.53 – 108.69 Mb Chr 10: 58.16 – 58.26 Mb PubMed search
Wikidata
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Function

The protein encoded by this gene is an adaptor protein which contains five LIM domains, or double zinc fingers. The protein is likely involved in integrin signaling through its LIM domain-mediated interaction with integrin-linked kinase, found in focal adhesion plaques. It is also thought to act as a bridge linking integrin-linked kinase to NCK adaptor protein 2, which is involved in growth factor receptor kinase signaling pathways. Its localization to the periphery of spreading cells also suggests that this protein may play a role in integrin-mediated cell adhesion or spreading.

Interactions

LIMS1 has been shown to interact with Integrin-linked kinase and NCK2.

Further reading

• Tu Y, Li F, Wu C (1998). "Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways". Mol. Biol. Cell. 9 (12): 3367–82. doi:10.1091/mbc.9.12.3367. PMC 25640. PMID 9843575.
• Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jäger D, Jäger E, Knuth A, Chen YT, Old LJ (1999). "Antigens recognized by autologous antibody in patients with renal-cell carcinoma". Int. J. Cancer. 83 (4): 456–64. doi:10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5. PMID 10508479. S2CID 21839750.
• Velyvis A, Yang Y, Wu C, Qin J (2001). "Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain". J. Biol. Chem. 276 (7): 4932–9. doi:10.1074/jbc.M007632200. PMID 11078733.
• Tu Y, Huang Y, Zhang Y, Hua Y, Wu C (2001). "A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading". J. Cell Biol. 153 (3): 585–98. doi:10.1083/jcb.153.3.585. PMC 2190577. PMID 11331308.
• Zhang Y, Chen K, Tu Y, Velyvis A, Yang Y, Qin J, Wu C (2002). "Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites". J. Cell Sci. 115 (Pt 24): 4777–86. doi:10.1242/jcs.00166. PMID 12432066. S2CID 13630628.
• Campana WM, Myers RR, Rearden A (2003). "Identification of PINCH in Schwann cells and DRG neurons: shuttling and signaling after nerve injury". Glia. 41 (3): 213–23. doi:10.1002/glia.10138. PMID 12528177. S2CID 33508275.
• Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2003). "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.
• Velyvis A, Vaynberg J, Yang Y, Vinogradova O, Zhang Y, Wu C, Qin J (2003). "Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling". Nat. Struct. Biol. 10 (7): 558–64. doi:10.1038/nsb938. PMID 12794636. S2CID 175531.
• Fukuda T, Chen K, Shi X, Wu C (2003). "PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival". J. Biol. Chem. 278 (51): 51324–33. doi:10.1074/jbc.M309122200. PMID 14551191.
• Bock-Marquette I, Saxena A, White MD, Dimaio JM, Srivastava D (2004). "Thymosin beta4 activates integrin-linked kinase and promotes cardiac cell migration, survival and cardiac repair". Nature. 432 (7016): 466–72. Bibcode:2004Natur.432..466B. doi:10.1038/nature03000. PMID 15565145. S2CID 4420896.
• Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
• Dougherty GW, Chopp T, Qi SM, Cutler ML (2005). "The Ras suppressor Rsu-1 binds to the LIM 5 domain of the adaptor protein PINCH1 and participates in adhesion-related functions". Exp. Cell Res. 306 (1): 168–79. doi:10.1016/j.yexcr.2005.01.025. PMID 15878342.
• Xu Z, Fukuda T, Li Y, Zha X, Qin J, Wu C (2005). "Molecular dissection of PINCH-1 reveals a mechanism of coupling and uncoupling of cell shape modulation and survival". J. Biol. Chem. 280 (30): 27631–7. doi:10.1074/jbc.M504189200. PMID 15941716.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal 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.