ID PDLI1_HUMAN Reviewed; 329 AA. AC O00151; B2RBS6; Q5VZH5; Q9BPZ9; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 210. DE RecName: Full=PDZ and LIM domain protein 1; DE AltName: Full=C-terminal LIM domain protein 1; DE AltName: Full=Elfin; DE AltName: Full=LIM domain protein CLP-36; GN Name=PDLIM1; Synonyms=CLIM1, CLP36; 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]. RC TISSUE=Heart; RX PubMed=10022510; RX DOI=10.1002/(sici)1097-4644(19990201)72:2<279::aid-jcb12>3.0.co;2-7; RA Kotaka M., Ngai S.M., Garcia-Barcelo M., Tsui S.K.W., Fung K.P., Lee C.Y., RA Waye M.M.Y.; RT "Characterization of the human 36-kDa carboxyl terminal LIM domain protein RT (hCLIM1)."; RL J. Cell. Biochem. 72:279-285(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ACTN1, AND SUBCELLULAR RP LOCATION. RX PubMed=11110697; RA Bauer K., Kratzer M., Otte M., Luber de Quintana K., Hagmann J., RA Arnold G.J., Eckerskorn C., Lottspeich F., Siess W.; RT "Human CLP-36, a PDZ-domain and LIM-domain protein, binds to alpha-actinin- RT 1 and associates with actin filaments and stress fibers in activated RT platelets and endothelial cells."; RL Blood 96:4236-4245(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-175. 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 [GENOMIC DNA], AND VARIANT SER-175. RG NIEHS SNPs program; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas, and Placenta; 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 [7] RP PROTEIN SEQUENCE OF 2-17. 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 [8] RP PROTEIN SEQUENCE OF 2-17; 23-32; 139-166; 212-238 AND 247-256, CLEAVAGE OF RP INITIATOR METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Platelet; RA Bienvenut W.V., Claeys D.; RL Submitted (NOV-2005) to UniProtKB. RN [9] RP FUNCTION, INTERACTION WITH ACTN2, AND SUBCELLULAR LOCATION. RX PubMed=10861853; RX DOI=10.1002/1097-4644(20000915)78:4<558::aid-jcb5>3.0.co;2-i; RA Kotaka M., Kostin S., Ngai S., Chan K., Lau Y., Lee S.M., Li H.Y., Ng E.K., RA Schaper J., Tsui S.K.W., Fung K.P., Lee C.Y., Waye M.M.Y.; RT "Interaction of hCLIM1, an enigma family protein, with alpha-actinin 2."; RL J. Cell. Biochem. 78:558-565(2000). RN [10] RP INTERACTION WITH ACTN1 AND ACTN4. RX PubMed=10753915; DOI=10.1074/jbc.275.15.11100; RA Vallenius T., Luukko K., Makela T.P.; RT "CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and RT alpha-actinin-4."; RL J. Biol. Chem. 275:11100-11105(2000). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-144, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND SER-130, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-130 AND THR-316, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP STRUCTURE BY NMR OF 250-315, AND ZINC-BINDING SITES. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the LIM domain of carboxyl terminal LIM domain RT protein 1."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- FUNCTION: Cytoskeletal protein that may act as an adapter that brings CC other proteins (like kinases) to the cytoskeleton (PubMed:10861853). CC Involved in assembly, disassembly and directioning of stress fibers in CC fibroblasts. Required for the localization of ACTN1 and PALLD to stress CC fibers. Required for cell migration and in maintaining cell polarity of CC fibroblasts (By similarity). {ECO:0000250|UniProtKB:P52944, CC ECO:0000269|PubMed:10861853}. CC -!- SUBUNIT: Interacts with ACTN1, ACTN2 and ACTN4 (PubMed:10861853, CC PubMed:10753915, PubMed:11110697). Interacts with PDLIM4 (By CC similarity). {ECO:0000250|UniProtKB:P52944, CC ECO:0000269|PubMed:10753915, ECO:0000269|PubMed:10861853, CC ECO:0000269|PubMed:11110697}. CC -!- INTERACTION: CC O00151; O43707: ACTN4; NbExp=3; IntAct=EBI-724897, EBI-351526; CC O00151; P14136: GFAP; NbExp=4; IntAct=EBI-724897, EBI-744302; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10861853, CC ECO:0000269|PubMed:11110697}. Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:10861853, ECO:0000269|PubMed:11110697}. Cytoplasm, CC myofibril, sarcomere, Z line {ECO:0000269|PubMed:10861853}. CC Note=Associates with actin stress fibers. CC {ECO:0000269|PubMed:11110697}. CC -!- TISSUE SPECIFICITY: Strongly expressed in the heart and skeletal CC muscle, moderately expressed in the spleen, small intestine, colon, CC placenta, and lung. A lower level expression is seen in liver, thymus, CC kidney, prostate and pancreas and is not found in the brain, testis, CC ovary, and peripheral blood leukocytes. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/pdlim1/"; 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; U90878; AAC05580.1; -; mRNA. DR EMBL; AJ310549; CAC32846.1; -; mRNA. DR EMBL; AK314792; BAG37323.1; -; mRNA. DR EMBL; AY923052; AAW82438.1; -; Genomic_DNA. DR EMBL; AL160288; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL157834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000915; AAH00915.1; -; mRNA. DR EMBL; BC018755; AAH18755.1; -; mRNA. DR CCDS; CCDS7441.1; -. DR RefSeq; NP_066272.1; NM_020992.3. DR PDB; 1X62; NMR; -; A=250-315. DR PDB; 2PKT; X-ray; 1.50 A; A=1-86. DR PDBsum; 1X62; -. DR PDBsum; 2PKT; -. DR AlphaFoldDB; O00151; -. DR BMRB; O00151; -. DR SMR; O00151; -. DR BioGRID; 114572; 117. DR CORUM; O00151; -. DR IntAct; O00151; 35. DR MINT; O00151; -. DR STRING; 9606.ENSP00000360305; -. DR GlyCosmos; O00151; 4 sites, 1 glycan. DR GlyGen; O00151; 10 sites, 2 O-linked glycans (9 sites). DR iPTMnet; O00151; -. DR MetOSite; O00151; -. DR PhosphoSitePlus; O00151; -. DR SwissPalm; O00151; -. DR BioMuta; PDLIM1; -. DR OGP; O00151; -. DR CPTAC; CPTAC-1441; -. DR CPTAC; CPTAC-1442; -. DR CPTAC; CPTAC-1443; -. DR CPTAC; CPTAC-1444; -. DR EPD; O00151; -. DR jPOST; O00151; -. DR MassIVE; O00151; -. DR PaxDb; 9606-ENSP00000360305; -. DR PeptideAtlas; O00151; -. DR ProteomicsDB; 47736; -. DR Pumba; O00151; -. DR Antibodypedia; 1897; 457 antibodies from 40 providers. DR CPTC; O00151; 3 antibodies. DR DNASU; 9124; -. DR Ensembl; ENST00000329399.7; ENSP00000360305.3; ENSG00000107438.9. DR GeneID; 9124; -. DR KEGG; hsa:9124; -. DR MANE-Select; ENST00000329399.7; ENSP00000360305.3; NM_020992.4; NP_066272.1. DR AGR; HGNC:2067; -. DR CTD; 9124; -. DR DisGeNET; 9124; -. DR GeneCards; PDLIM1; -. DR HGNC; HGNC:2067; PDLIM1. DR HPA; ENSG00000107438; Tissue enhanced (skeletal). DR MIM; 605900; gene. DR neXtProt; NX_O00151; -. DR OpenTargets; ENSG00000107438; -. DR PharmGKB; PA33158; -. DR VEuPathDB; HostDB:ENSG00000107438; -. DR eggNOG; KOG1703; Eukaryota. DR GeneTree; ENSGT00940000155525; -. DR HOGENOM; CLU_038114_1_1_1; -. DR InParanoid; O00151; -. DR OMA; QIYCETH; -. DR OrthoDB; 370973at2759; -. DR PhylomeDB; O00151; -. DR TreeFam; TF106408; -. DR PathwayCommons; O00151; -. DR SignaLink; O00151; -. DR BioGRID-ORCS; 9124; 11 hits in 1160 CRISPR screens. DR ChiTaRS; PDLIM1; human. DR EvolutionaryTrace; O00151; -. DR GeneWiki; PDLIM1; -. DR GenomeRNAi; 9124; -. DR Pharos; O00151; Tbio. DR PRO; PR:O00151; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; O00151; Protein. DR Bgee; ENSG00000107438; Expressed in lower lobe of lung and 199 other cell types or tissues. DR ExpressionAtlas; O00151; baseline and differential. DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB. DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB. DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl. DR GO; GO:0030018; C:Z disc; IDA:UniProtKB. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central. DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; ISS:UniProtKB. DR GO; GO:0010761; P:fibroblast migration; ISS:UniProtKB. DR GO; GO:0007507; P:heart development; IBA:GO_Central. DR GO; GO:0030011; P:maintenance of cell polarity; ISS:UniProtKB. DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc. DR GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB. DR CDD; cd09448; LIM_CLP36; 1. DR CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1. DR InterPro; IPR031847; PDLI1-4/Zasp-like_mid. DR InterPro; IPR028537; PDLIM1_LIM. DR InterPro; IPR001478; PDZ. DR InterPro; IPR036034; PDZ_sf. DR InterPro; IPR006643; Zasp-like_motif. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR24214:SF5; PDZ AND LIM DOMAIN PROTEIN 1; 1. DR PANTHER; PTHR24214; PDZ AND LIM DOMAIN PROTEIN ZASP; 1. DR Pfam; PF15936; DUF4749; 1. DR Pfam; PF00412; LIM; 1. DR Pfam; PF00595; PDZ; 1. DR SMART; SM00132; LIM; 1. DR SMART; SM00228; PDZ; 1. DR SMART; SM00735; ZM; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR PROSITE; PS00478; LIM_DOMAIN_1; 1. DR PROSITE; PS50023; LIM_DOMAIN_2; 1. DR PROSITE; PS50106; PDZ; 1. DR UCD-2DPAGE; O00151; -. DR Genevisible; O00151; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; LIM domain; Metal-binding; Phosphoprotein; KW Reference proteome; Zinc. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378" FT CHAIN 2..329 FT /note="PDZ and LIM domain protein 1" FT /id="PRO_0000075859" FT DOMAIN 3..85 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 258..317 FT /note="LIM zinc-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125" FT BINDING 260 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 263 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 280 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 283 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT BINDING 286 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 289 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 307 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT BINDING 310 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT MOD_RES 2 FT /note="N-acetylthreonine" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 90 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 130 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 144 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 316 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 321 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15144186" FT VARIANT 175 FT /note="N -> S (in dbSNP:rs2296961)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.4" FT /id="VAR_022271" FT CONFLICT 21 FT /note="G -> R (in Ref. 1; AAC05580)" FT /evidence="ECO:0000305" FT STRAND 2..12 FT /evidence="ECO:0007829|PDB:2PKT" FT STRAND 15..21 FT /evidence="ECO:0007829|PDB:2PKT" FT HELIX 22..24 FT /evidence="ECO:0007829|PDB:2PKT" FT STRAND 26..33 FT /evidence="ECO:0007829|PDB:2PKT" FT HELIX 38..41 FT /evidence="ECO:0007829|PDB:2PKT" FT STRAND 49..53 FT /evidence="ECO:0007829|PDB:2PKT" FT HELIX 63..71 FT /evidence="ECO:0007829|PDB:2PKT" FT STRAND 74..84 FT /evidence="ECO:0007829|PDB:2PKT" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:1X62" FT TURN 281..284 FT /evidence="ECO:0007829|PDB:1X62" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:1X62" FT HELIX 293..296 FT /evidence="ECO:0007829|PDB:1X62" FT STRAND 299..303 FT /evidence="ECO:0007829|PDB:1X62" FT HELIX 308..315 FT /evidence="ECO:0007829|PDB:1X62" SQ SEQUENCE 329 AA; 36072 MW; C85881A04D63D314 CRC64; MTTQQIDLQG PGPWGFRLVG GKDFEQPLAI SRVTPGSKAA LANLCIGDVI TAIDGENTSN MTHLEAQNRI KGCTDNLTLT VARSEHKVWS PLVTEEGKRH PYKMNLASEP QEVLHIGSAH NRSAMPFTAS PASSTTARVI TNQYNNPAGL YSSENISNFN NALESKTAAS GVEANSRPLD HAQPPSSLVI DKESEVYKML QEKQELNEPP KQSTSFLVLQ EILESEEKGD PNKPSGFRSV KAPVTKVAAS IGNAQKLPMC DKCGTGIVGV FVKLRDRHRH PECYVCTDCG TNLKQKGHFF VEDQIYCEKH ARERVTPPEG YEVVTVFPK //