PDLI1_HUMAN
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 03-AUG-2022, entry version 201.
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/";
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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; 100.
DR CORUM; O00151; -.
DR IntAct; O00151; 31.
DR MINT; O00151; -.
DR STRING; 9606.ENSP00000360305; -.
DR GlyGen; O00151; 5 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; O00151; -.
DR MetOSite; O00151; -.
DR PhosphoSitePlus; O00151; -.
DR SwissPalm; O00151; -.
DR BioMuta; PDLIM1; -.
DR OGP; O00151; -.
DR UCD-2DPAGE; 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; O00151; -.
DR PeptideAtlas; O00151; -.
DR PRIDE; O00151; -.
DR ProteomicsDB; 47736; -.
DR Antibodypedia; 1897; 413 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 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; EPQEVKH; -.
DR OrthoDB; 840552at2759; -.
DR PhylomeDB; O00151; -.
DR TreeFam; TF106408; -.
DR PathwayCommons; O00151; -.
DR SignaLink; O00151; -.
DR BioGRID-ORCS; 9124; 10 hits in 1082 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 197 other tissues.
DR ExpressionAtlas; O00151; baseline and differential.
DR Genevisible; O00151; HS.
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 Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR031847; DUF4749.
DR InterPro; IPR028537; PDLIM1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR006643; Zasp-like_motif.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24214:SF5; PTHR24214:SF5; 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; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS50106; PDZ; 1.
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
