LIMS1_HUMAN
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 03-AUG-2022, entry version 213.
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.
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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; 82.
DR CORUM; P48059; -.
DR DIP; DIP-40671N; -.
DR IntAct; P48059; 67.
DR MINT; P48059; -.
DR STRING; 9606.ENSP00000446121; -.
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; P48059; -.
DR PeptideAtlas; P48059; -.
DR PRIDE; 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 Antibodypedia; 33091; 288 antibodies from 33 providers.
DR DNASU; 3987; -.
DR Ensembl; ENST00000332345.10; ENSP00000331775.6; ENSG00000169756.16. [P48059-1]
DR Ensembl; ENST00000338045.7; ENSP00000337598.4; ENSG00000169756.16. [P48059-3]
DR Ensembl; ENST00000393310.5; ENSP00000376987.1; ENSG00000169756.16. [P48059-1]
DR Ensembl; ENST00000409441.5; ENSP00000387264.1; ENSG00000169756.16. [P48059-5]
DR Ensembl; ENST00000410093.5; ENSP00000386926.1; ENSG00000169756.16. [P48059-4]
DR Ensembl; ENST00000544547.5; ENSP00000437912.1; ENSG00000169756.16. [P48059-2]
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 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; VCAQCFE; -.
DR OrthoDB; 1593918at2759; -.
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; 232 hits in 1074 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 181 other tissues.
DR ExpressionAtlas; P48059; baseline and differential.
DR Genevisible; P48059; HS.
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 transcription, DNA-templated; IDA:UniProtKB.
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:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:CAFA.
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 InterPro; IPR017351; PINCH_1-like.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24210; PTHR24210; 1.
DR Pfam; PF00412; LIM; 5.
DR PIRSF; PIRSF038003; PINCH; 1.
DR SMART; SM00132; LIM; 5.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 5.
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
