ID LIMS1_HUMAN Reviewed; 325 AA. AC P48059; B2RAJ4; B7Z483; B7Z7R3; B7Z907; Q53TE0; Q9BS44; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 222. DE RecName: Full=LIM and senescent cell antigen-like-containing domain protein 1; DE AltName: Full=Particularly interesting new Cys-His protein 1; DE Short=PINCH-1; DE AltName: Full=Renal carcinoma antigen NY-REN-48; GN Name=LIMS1; Synonyms=PINCH, PINCH1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal liver; RX PubMed=7517666; DOI=10.1006/bbrc.1994.1822; RA Rearden A.; RT "A new LIM protein containing an autoepitope homologous to 'senescent cell RT antigen'."; RL Biochem. Biophys. Res. Commun. 201:1124-1131(1994). RN [2] RP SEQUENCE REVISION TO C-TERMINUS. RA Rearden A.; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 5). RC TISSUE=Testis, Tongue, and Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 2-12, AND ACETYLATION AT ALA-2. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP INTERACTION WITH NCK2. RX PubMed=9843575; DOI=10.1091/mbc.9.12.3367; RA Tu Y., Li F., Wu C.; RT "Nck-2, a novel Src homology2/3-containing adaptor protein that interacts RT with the LIM-only protein PINCH and components of growth factor receptor RT kinase-signaling pathways."; RL Mol. Biol. Cell 9:3367-3382(1998). RN [8] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX PubMed=10508479; RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal-cell RT carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [9] RP INTERACTION WITH ILK AND NCK2, AND SUBCELLULAR LOCATION. RX PubMed=10022929; DOI=10.1128/mcb.19.3.2425; RA Tu Y., Li F., Goicoechea S., Wu C.; RT "The LIM-only protein PINCH directly interacts with integrin-linked kinase RT and is recruited to integrin-rich sites in spreading cells."; RL Mol. Cell. Biol. 19:2425-2434(1999). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP STRUCTURE BY NMR OF 1-70. RX PubMed=11078733; DOI=10.1074/jbc.m007632200; RA Velyvis A., Yang Y., Wu C., Qin J.; RT "Solution structure of the focal adhesion adaptor PINCH LIM1 domain and RT characterization of its interaction with the integrin-linked kinase ankyrin RT repeat domain."; RL J. Biol. Chem. 276:4932-4939(2001). RN [12] RP STRUCTURE BY NMR OF 188-251. RX PubMed=12794636; DOI=10.1038/nsb938; RA Velyvis A., Vaynberg J., Yang Y., Vinogradova O., Zhang Y., Wu C., Qin J.; RT "Structural and functional insights into PINCH LIM4 domain-mediated RT integrin signaling."; RL Nat. Struct. Biol. 10:558-564(2003). RN [13] RP STRUCTURE BY NMR OF 71-190. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the second and third LIM domain of particularly RT interesting new Cys-His protein (PINCH)."; RL Submitted (JUN-2006) to the PDB data bank. RN [14] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 6-68 IN COMPLEX WITH ILK, AND RP MUTAGENESIS OF PHE-42; HIS-61; ASP-62 AND LEU-66. RX PubMed=19074270; DOI=10.1073/pnas.0811415106; RA Chiswell B.P., Zhang R., Murphy J.W., Boggon T.J., Calderwood D.A.; RT "The structural basis of integrin-linked kinase-PINCH interactions."; RL Proc. Natl. Acad. Sci. U.S.A. 105:20677-20682(2008). RN [15] RP STRUCTURE BY NMR OF 1-70 IN COMPLEX WITH ILK, MUTAGENESIS OF PHE-42 AND RP ARG-56, AND SUBCELLULAR LOCATION. RX PubMed=19117955; DOI=10.1074/jbc.m805319200; RA Yang Y., Wang X., Hawkins C.A., Chen K., Vaynberg J., Mao X., Tu Y., RA Zuo X., Wang J., Wang Y.-X., Wu C., Tjandra N., Qin J.; RT "Structural basis of focal adhesion localization of LIM-only adaptor PINCH RT by integrin-linked kinase."; RL J. Biol. Chem. 284:5836-5844(2009). CC -!- FUNCTION: Adapter protein in a cytoplasmic complex linking beta- CC integrins to the actin cytoskeleton, bridges the complex to cell CC surface receptor tyrosine kinases and growth factor receptors. Involved CC in the regulation of cell survival, cell proliferation and cell CC differentiation. CC -!- SUBUNIT: Interacts (via LIM zinc-binding 5) with TGFB1I1 (By CC similarity). Interacts with integrin-linked protein kinase 1 (ILK) via CC the first LIM domain, and in competition with LIMS2. Part of the CC heterotrimeric IPP complex composed of integrin-linked kinase (ILK), CC LIMS1 or LIMS2, and PARVA. Interacts with SH3/SH2 adapter NCK2, thereby CC linking the complex to cell surface receptors. {ECO:0000250, CC ECO:0000269|PubMed:10022929, ECO:0000269|PubMed:19074270, CC ECO:0000269|PubMed:19117955, ECO:0000269|PubMed:9843575}. CC -!- INTERACTION: CC P48059; Q13418: ILK; NbExp=14; IntAct=EBI-306928, EBI-747644; CC P48059; O43639: NCK2; NbExp=2; IntAct=EBI-306928, EBI-713635; CC P48059; Q15404: RSU1; NbExp=6; IntAct=EBI-306928, EBI-1057132; CC P48059; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-306928, EBI-3957603; CC P48059; O55222: Ilk; Xeno; NbExp=4; IntAct=EBI-306928, EBI-6690138; CC P48059-3; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-12864460, EBI-744545; CC P48059-3; P27658: COL8A1; NbExp=3; IntAct=EBI-12864460, EBI-747133; CC P48059-3; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-12864460, EBI-5453285; CC P48059-3; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-12864460, EBI-6658203; CC P48059-3; P55040: GEM; NbExp=3; IntAct=EBI-12864460, EBI-744104; CC P48059-3; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-12864460, EBI-14103818; CC P48059-3; Q13418: ILK; NbExp=3; IntAct=EBI-12864460, EBI-747644; CC P48059-3; Q9C086: INO80B; NbExp=3; IntAct=EBI-12864460, EBI-715611; CC P48059-3; Q5T749: KPRP; NbExp=3; IntAct=EBI-12864460, EBI-10981970; CC P48059-3; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-12864460, EBI-11742507; CC P48059-3; O75771: RAD51D; NbExp=3; IntAct=EBI-12864460, EBI-1055693; CC P48059-3; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-12864460, EBI-748391; CC P48059-3; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-12864460, EBI-8787464; CC P48059-3; Q15560: TCEA2; NbExp=3; IntAct=EBI-12864460, EBI-710310; CC P48059-3; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-12864460, EBI-11962760; CC P48059-3; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-12864460, EBI-11741890; CC P48059-3; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-12864460, EBI-740727; CC P48059-3; Q8TBZ8: ZNF564; NbExp=3; IntAct=EBI-12864460, EBI-10273713; CC P48059-3; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-12864460, EBI-6427977; CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell membrane; CC Peripheral membrane protein; Cytoplasmic side. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P48059-1; Sequence=Displayed; CC Name=2; CC IsoId=P48059-2; Sequence=VSP_042672; CC Name=3; CC IsoId=P48059-3; Sequence=VSP_043210; CC Name=4; CC IsoId=P48059-4; Sequence=VSP_043211; CC Name=5; CC IsoId=P48059-5; Sequence=VSP_043212; CC -!- TISSUE SPECIFICITY: Expressed in most tissues except in the brain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U09284; AAA20086.2; -; mRNA. DR EMBL; AK296992; BAH12469.1; -; mRNA. DR EMBL; AK302411; BAH13699.1; -; mRNA. DR EMBL; AK304260; BAH14143.1; -; mRNA. DR EMBL; AK314217; BAG36891.1; -; mRNA. DR EMBL; AC010095; AAY14983.1; -; Genomic_DNA. DR EMBL; AC012487; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005341; AAH05341.1; -; mRNA. DR CCDS; CCDS2078.1; -. [P48059-1] DR CCDS; CCDS54382.1; -. [P48059-2] DR CCDS; CCDS54383.1; -. [P48059-4] DR CCDS; CCDS54384.1; -. [P48059-5] DR CCDS; CCDS54385.1; -. [P48059-3] DR PIR; JC2324; JC2324. DR RefSeq; NP_001180411.1; NM_001193482.1. [P48059-4] DR RefSeq; NP_001180412.1; NM_001193483.2. [P48059-2] DR RefSeq; NP_001180413.1; NM_001193484.1. [P48059-5] DR RefSeq; NP_001180414.1; NM_001193485.2. [P48059-3] DR RefSeq; NP_001180417.1; NM_001193488.1. [P48059-1] DR RefSeq; NP_004978.2; NM_004987.5. [P48059-1] DR PDB; 1G47; NMR; -; A=1-70. DR PDB; 1NYP; NMR; -; A=188-251. DR PDB; 1U5S; NMR; -; B=188-251. DR PDB; 2COR; NMR; -; A=125-190. DR PDB; 2D8X; NMR; -; A=71-127. DR PDB; 2KBX; NMR; -; B=1-70. DR PDB; 3F6Q; X-ray; 1.60 A; B=6-68. DR PDB; 4HI8; X-ray; 1.20 A; B=6-68. DR PDB; 4HI9; X-ray; 1.20 A; B=6-68. DR PDB; 6MIF; NMR; -; A=249-325. DR PDB; 7D2S; X-ray; 1.65 A; B=249-325. DR PDB; 7D2T; X-ray; 2.20 A; B/D=188-325. DR PDB; 7D2U; X-ray; 3.15 A; B=188-325. DR PDB; 7LT9; X-ray; 3.05 A; B=189-325. DR PDBsum; 1G47; -. DR PDBsum; 1NYP; -. DR PDBsum; 1U5S; -. DR PDBsum; 2COR; -. DR PDBsum; 2D8X; -. DR PDBsum; 2KBX; -. DR PDBsum; 3F6Q; -. DR PDBsum; 4HI8; -. DR PDBsum; 4HI9; -. DR PDBsum; 6MIF; -. DR PDBsum; 7D2S; -. DR PDBsum; 7D2T; -. DR PDBsum; 7D2U; -. DR PDBsum; 7LT9; -. DR AlphaFoldDB; P48059; -. DR SMR; P48059; -. DR BioGRID; 110175; 94. DR CORUM; P48059; -. DR DIP; DIP-40671N; -. DR IntAct; P48059; 67. DR MINT; P48059; -. DR STRING; 9606.ENSP00000337598; -. DR GlyGen; P48059; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P48059; -. DR PhosphoSitePlus; P48059; -. DR SwissPalm; P48059; -. DR BioMuta; LIMS1; -. DR DMDM; 18266876; -. DR OGP; P48059; -. DR EPD; P48059; -. DR jPOST; P48059; -. DR MassIVE; P48059; -. DR MaxQB; P48059; -. DR PaxDb; 9606-ENSP00000446121; -. DR PeptideAtlas; P48059; -. DR ProteomicsDB; 55846; -. [P48059-1] DR ProteomicsDB; 55847; -. [P48059-2] DR ProteomicsDB; 55848; -. [P48059-3] DR ProteomicsDB; 55849; -. [P48059-4] DR ProteomicsDB; 55850; -. [P48059-5] DR Pumba; P48059; -. DR Antibodypedia; 33091; 319 antibodies from 33 providers. DR DNASU; 3987; -. DR Ensembl; ENST00000332345.10; ENSP00000331775.6; ENSG00000169756.17. [P48059-1] DR Ensembl; ENST00000338045.7; ENSP00000337598.4; ENSG00000169756.17. [P48059-3] DR Ensembl; ENST00000393310.5; ENSP00000376987.1; ENSG00000169756.17. [P48059-1] DR Ensembl; ENST00000409441.5; ENSP00000387264.1; ENSG00000169756.17. [P48059-5] DR Ensembl; ENST00000410093.5; ENSP00000386926.1; ENSG00000169756.17. [P48059-4] DR Ensembl; ENST00000544547.6; ENSP00000437912.1; ENSG00000169756.17. [P48059-2] DR Ensembl; ENST00000695518.1; ENSP00000511981.1; ENSG00000169756.17. [P48059-1] DR Ensembl; ENST00000695521.1; ENSP00000511984.1; ENSG00000169756.17. [P48059-1] DR GeneID; 3987; -. DR KEGG; hsa:3987; -. DR MANE-Select; ENST00000544547.6; ENSP00000437912.1; NM_001193483.3; NP_001180412.1. [P48059-2] DR UCSC; uc002teg.4; human. [P48059-1] DR AGR; HGNC:6616; -. DR CTD; 3987; -. DR DisGeNET; 3987; -. DR GeneCards; LIMS1; -. DR HGNC; HGNC:6616; LIMS1. DR HPA; ENSG00000169756; Low tissue specificity. DR MIM; 602567; gene. DR neXtProt; NX_P48059; -. DR OpenTargets; ENSG00000169756; -. DR PharmGKB; PA30389; -. DR VEuPathDB; HostDB:ENSG00000169756; -. DR eggNOG; KOG2272; Eukaryota. DR GeneTree; ENSGT00940000153518; -. DR HOGENOM; CLU_001357_0_0_1; -. DR InParanoid; P48059; -. DR OMA; CHEPLGD; -. DR OrthoDB; 370973at2759; -. DR PhylomeDB; P48059; -. DR TreeFam; TF314113; -. DR PathwayCommons; P48059; -. DR Reactome; R-HSA-446353; Cell-extracellular matrix interactions. DR Reactome; R-HSA-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components. DR SignaLink; P48059; -. DR SIGNOR; P48059; -. DR BioGRID-ORCS; 3987; 250 hits in 1151 CRISPR screens. DR ChiTaRS; LIMS1; human. DR EvolutionaryTrace; P48059; -. DR GeneWiki; LIMS1; -. DR GenomeRNAi; 3987; -. DR Pharos; P48059; Tbio. DR PRO; PR:P48059; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P48059; Protein. DR Bgee; ENSG00000169756; Expressed in monocyte and 183 other cell types or tissues. DR ExpressionAtlas; P48059; baseline and differential. DR GO; GO:0005911; C:cell-cell junction; IMP:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0045216; P:cell-cell junction organization; IBA:GO_Central. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB. DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IMP:CAFA. DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:UniProtKB. DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB. DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB. DR GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IBA:GO_Central. DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB. DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:CAFA. DR CDD; cd09331; LIM1_PINCH; 1. DR CDD; cd09332; LIM2_PINCH; 1. DR CDD; cd09333; LIM3_PINCH; 1. DR CDD; cd09334; LIM4_PINCH; 1. DR CDD; cd09335; LIM5_PINCH; 1. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 5. DR InterPro; IPR047944; LIMS1/2-like_LIM1. DR InterPro; IPR047946; PINCH-1/2-like. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR24210:SF11; LIM AND SENESCENT CELL ANTIGEN-LIKE-CONTAINING DOMAIN PROTEIN 1; 1. DR PANTHER; PTHR24210; LIM DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00412; LIM; 5. DR PIRSF; PIRSF038003; PINCH; 1. DR SMART; SM00132; LIM; 5. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 6. DR PROSITE; PS00478; LIM_DOMAIN_1; 4. DR PROSITE; PS50023; LIM_DOMAIN_2; 5. DR Genevisible; P48059; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell junction; KW Cell membrane; Direct protein sequencing; LIM domain; Membrane; KW Metal-binding; Reference proteome; Repeat; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801" FT CHAIN 2..325 FT /note="LIM and senescent cell antigen-like-containing FT domain protein 1" FT /id="PRO_0000075888" FT DOMAIN 10..62 FT /note="LIM zinc-binding 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 71..121 FT /note="LIM zinc-binding 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 135..184 FT /note="LIM zinc-binding 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 193..243 FT /note="LIM zinc-binding 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT DOMAIN 252..303 FT /note="LIM zinc-binding 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:12665801" FT VAR_SEQ 1 FT /note="M -> MLGVAAGMTHSNM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042672" FT VAR_SEQ 1 FT /note="M -> MAFSGRARPCIIPENEEIPRAALNTVHEANGTEDERAVSKLQRRHSD FT VKVYKEFCDFYAKFNM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043210" FT VAR_SEQ 1 FT /note="M -> MTCNM (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_043211" FT VAR_SEQ 1 FT /note="M -> MTALQLKELSHSGLYRRRRDRPDSLRVNGLPEEELSNM (in FT isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043212" FT MUTAGEN 42 FT /note="F->A: Loss of interaction with ILK and loss of FT localization to focal adhesion." FT /evidence="ECO:0000269|PubMed:19074270, FT ECO:0000269|PubMed:19117955" FT MUTAGEN 56 FT /note="R->A: Alters interaction with ILK." FT /evidence="ECO:0000269|PubMed:19117955" FT MUTAGEN 61 FT /note="H->D: Alters interaction with ILK." FT /evidence="ECO:0000269|PubMed:19074270" FT MUTAGEN 62 FT /note="D->A: Alters interaction with ILK." FT /evidence="ECO:0000269|PubMed:19074270" FT MUTAGEN 66 FT /note="L->D: Alters interaction with ILK." FT /evidence="ECO:0000269|PubMed:19074270" FT CONFLICT 78 FT /note="I -> T (in Ref. 5; AAH05341)" FT /evidence="ECO:0000305" FT CONFLICT 262 FT /note="D -> G (in Ref. 5; AAH05341)" FT /evidence="ECO:0000305" FT TURN 11..13 FT /evidence="ECO:0007829|PDB:4HI8" FT STRAND 22..26 FT /evidence="ECO:0007829|PDB:4HI8" FT STRAND 29..32 FT /evidence="ECO:0007829|PDB:4HI8" FT TURN 33..35 FT /evidence="ECO:0007829|PDB:4HI8" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:4HI8" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:4HI8" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:4HI8" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:4HI8" FT HELIX 60..66 FT /evidence="ECO:0007829|PDB:4HI8" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:2D8X" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:2D8X" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:2D8X" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:2D8X" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:2D8X" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:2D8X" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:2D8X" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:2D8X" FT HELIX 119..126 FT /evidence="ECO:0007829|PDB:2D8X" FT TURN 136..138 FT /evidence="ECO:0007829|PDB:2COR" FT STRAND 150..152 FT /evidence="ECO:0007829|PDB:2COR" FT TURN 156..158 FT /evidence="ECO:0007829|PDB:2COR" FT STRAND 162..164 FT /evidence="ECO:0007829|PDB:2COR" FT STRAND 173..175 FT /evidence="ECO:0007829|PDB:2COR" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:2COR" FT HELIX 182..186 FT /evidence="ECO:0007829|PDB:2COR" FT TURN 194..196 FT /evidence="ECO:0007829|PDB:7D2T" FT STRAND 204..207 FT /evidence="ECO:0007829|PDB:7D2T" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:7D2T" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:7D2T" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:7D2T" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:1NYP" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:7D2T" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:7D2T" FT HELIX 241..248 FT /evidence="ECO:0007829|PDB:7D2T" FT TURN 253..255 FT /evidence="ECO:0007829|PDB:7D2S" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:6MIF" FT STRAND 263..266 FT /evidence="ECO:0007829|PDB:7D2S" FT STRAND 269..272 FT /evidence="ECO:0007829|PDB:7D2S" FT TURN 273..275 FT /evidence="ECO:0007829|PDB:7D2S" FT TURN 279..281 FT /evidence="ECO:0007829|PDB:7D2S" FT STRAND 291..294 FT /evidence="ECO:0007829|PDB:7D2S" FT STRAND 297..300 FT /evidence="ECO:0007829|PDB:7D2S" FT HELIX 301..305 FT /evidence="ECO:0007829|PDB:7D2S" FT HELIX 309..317 FT /evidence="ECO:0007829|PDB:7D2S" SQ SEQUENCE 325 AA; 37251 MW; E665FEB11D849CAE CRC64; MANALASATC ERCKGGFAPA EKIVNSNGEL YHEQCFVCAQ CFQQFPEGLF YEFEGRKYCE HDFQMLFAPC CHQCGEFIIG RVIKAMNNSW HPECFRCDLC QEVLADIGFV KNAGRHLCRP CHNREKARGL GKYICQKCHA IIDEQPLIFK NDPYHPDHFN CANCGKELTA DARELKGELY CLPCHDKMGV PICGACRRPI EGRVVNAMGK QWHVEHFVCA KCEKPFLGHR HYERKGLAYC ETHYNQLFGD VCFHCNRVIE GDVVSALNKA WCVNCFACST CNTKLTLKNK FVEFDMKPVC KKCYEKFPLE LKKRLKKLAE TLGRK //