LIMS1

Protein-coding gene in the species Homo sapiens

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; OMA:LIMS1 - orthologs

Gene location (Human)

Chr.	Chromosome 2 (human)^[1]

Band	2q12.3	Start	108,534,355 bp^[1]
Band	2q12.3	End	108,687,246 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 10 (mouse)^[2]

Band	10 B4\|10 29.31 cM	Start	58,159,288 bp^[2]
Band	10 B4\|10 29.31 cM	End	58,260,513 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

monocyte

stromal cell of endometrium

gastrocnemius muscle

ascending aorta

muscle of thigh

decidua

tail of epididymis

Descending thoracic aorta

epithelium of colon

Skeletal muscle tissue of biceps brachii

Top expressed in

granulocyte

left lung lobe

genital tubercle

cardiac muscle tissue of left ventricle

sciatic nerve

soleus muscle

atrioventricular valve

corneal stroma

atrium

tail of embryo

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

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

LIM and senescent cell antigen-like-containing domain protein 1 is a protein that in humans is encoded by the LIMS1 gene.^[5]^[6]^[7]

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.^[7]

Interactions

LIMS1 has been shown to interact with Integrin-linked kinase^[6]^[8] and NCK2.^[6]^[9]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000169756 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000019920 – 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.
^ Rearden A (Aug 1994). "A new LIM protein containing an autoepitope homologous to "senescent cell antigen"". Biochem. Biophys. Res. Commun. 201 (3): 1124–31. doi:10.1006/bbrc.1994.1822. PMID 7517666.
^ ^a ^b ^c Tu Y, Li F, Goicoechea S, Wu C (Mar 1999). "The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells". Mol. Cell. Biol. 19 (3): 2425–34. doi:10.1128/mcb.19.3.2425. PMC 84035. PMID 10022929.
^ ^a ^b "Entrez Gene: LIMS1 LIM and senescent cell antigen-like domains 1".
^ Zhang Y, Chen K, Guo L, Wu C (Oct 2002). "Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration". J. Biol. Chem. 277 (41): 38328–38. doi:10.1074/jbc.M205576200. PMID 12167643.
^ Tu Y, Li F, Wu C (Dec 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.

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.

PDB gallery

1g47: 1ST LIM DOMAIN OF PINCH PROTEIN
1nyp: 4th LIM domain of PINCH protein
1u5s: NMR structure of the complex between Nck-2 SH3 domain and PINCH-1 LIM4 domain
2cor: Solution structure of the third LIM domain of particularly interesting new Cys-His protein
2d8x: Solution structure of the second LIM domain of particularly interesting new Cys-His protein (PINCH)