Full text data of PDLIM1
PDLIM1
(CLIM1, CLP36)
[Confidence: low (only semi-automatic identification from reviews)]
PDZ and LIM domain protein 1 (C-terminal LIM domain protein 1; Elfin; LIM domain protein CLP-36)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
PDZ and LIM domain protein 1 (C-terminal LIM domain protein 1; Elfin; LIM domain protein CLP-36)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O00151
ID PDLI1_HUMAN Reviewed; 329 AA.
AC O00151; B2RBS6; Q5VZH5; Q9BPZ9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 134.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Lee C.Y., Waye M.M.Y.;
RT "Characterization of the human 36-kDa carboxyl terminal LIM domain
RT protein (hCLIM1).";
RL J. Cell. Biochem. 72:279-285(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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-
RT actinin-1 and associates with actin filaments and stress fibers in
RT activated 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [9]
RP INTERACTION WITH ALPHA-ACTININ-2.
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.,
RA Ng E.K., 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
RT 2.";
RL J. Cell. Biochem. 78:558-565(2000).
RN [10]
RP INTERACTION WITH ALPHA-ACTININ-1 AND ALPHA-ACTININ-4.
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 MASS
RP SPECTROMETRY.
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
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-144, AND MASS
RP SPECTROMETRY.
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of 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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
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
CC brings other proteins (like kinases) to the cytoskeleton.
CC -!- SUBUNIT: Interacts with alpha-actinins 1, 2 and 4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC cytoskeleton (By similarity). Note=Associates with the actin
CC stress fibers (By similarity).
CC -!- TISSUE SPECIFICITY: Strongly expressed in the heart and skeletal
CC muscle, moderately expressed in the spleen, small intestine,
CC colon, placenta, and lung. A lower level expression is seen in
CC liver, thymus, kidney, prostate and pancreas and is not found in
CC the brain, testis, ovary, and peripheral blood leukocytes.
CC -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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; CAH70720.1; -; Genomic_DNA.
DR EMBL; AL157834; CAH70720.1; JOINED; Genomic_DNA.
DR EMBL; AL157834; CAH72341.1; -; Genomic_DNA.
DR EMBL; AL160288; CAH72341.1; JOINED; Genomic_DNA.
DR EMBL; BC000915; AAH00915.1; -; mRNA.
DR EMBL; BC018755; AAH18755.1; -; mRNA.
DR RefSeq; NP_066272.1; NM_020992.3.
DR UniGene; Hs.368525; -.
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 ProteinModelPortal; O00151; -.
DR SMR; O00151; 1-87, 251-318.
DR IntAct; O00151; 11.
DR MINT; MINT-5005794; -.
DR STRING; 9606.ENSP00000360305; -.
DR PhosphoSite; O00151; -.
DR OGP; O00151; -.
DR UCD-2DPAGE; O00151; -.
DR PaxDb; O00151; -.
DR PeptideAtlas; O00151; -.
DR PRIDE; O00151; -.
DR DNASU; 9124; -.
DR Ensembl; ENST00000329399; ENSP00000360305; ENSG00000107438.
DR GeneID; 9124; -.
DR KEGG; hsa:9124; -.
DR UCSC; uc001kkh.4; human.
DR CTD; 9124; -.
DR GeneCards; GC10M096997; -.
DR HGNC; HGNC:2067; PDLIM1.
DR HPA; HPA017010; -.
DR MIM; 605900; gene.
DR neXtProt; NX_O00151; -.
DR PharmGKB; PA33158; -.
DR eggNOG; NOG250485; -.
DR HOGENOM; HOG000290704; -.
DR HOVERGEN; HBG061371; -.
DR InParanoid; O00151; -.
DR OMA; NLCIGDI; -.
DR OrthoDB; EOG77DJ69; -.
DR PhylomeDB; O00151; -.
DR ChiTaRS; PDLIM1; human.
DR EvolutionaryTrace; O00151; -.
DR GeneWiki; PDLIM1; -.
DR GenomeRNAi; 9124; -.
DR NextBio; 34201; -.
DR PRO; PR:O00151; -.
DR Bgee; O00151; -.
DR CleanEx; HS_PDLIM1; -.
DR Genevestigator; O00151; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
DR Gene3D; 2.10.110.10; -; 1.
DR InterPro; IPR028537; PDLIM1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR006643; ZASP.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24214:SF11; PTHR24214:SF11; 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; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; LIM domain; Metal-binding; Phosphoprotein;
KW Polymorphism; Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 329 PDZ and LIM domain protein 1.
FT /FTId=PRO_0000075859.
FT DOMAIN 3 85 PDZ.
FT DOMAIN 258 317 LIM zinc-binding.
FT METAL 260 260 Zinc 1.
FT METAL 263 263 Zinc 1.
FT METAL 280 280 Zinc 1.
FT METAL 283 283 Zinc 1.
FT METAL 286 286 Zinc 2.
FT METAL 289 289 Zinc 2.
FT METAL 307 307 Zinc 2.
FT METAL 310 310 Zinc 2.
FT MOD_RES 2 2 N-acetylthreonine.
FT MOD_RES 90 90 Phosphoserine.
FT MOD_RES 130 130 Phosphoserine.
FT MOD_RES 144 144 Phosphotyrosine.
FT MOD_RES 321 321 Phosphotyrosine.
FT VARIANT 175 175 N -> S (in dbSNP:rs2296961).
FT /FTId=VAR_022271.
FT CONFLICT 21 21 G -> R (in Ref. 1; AAC05580).
FT STRAND 2 12
FT STRAND 15 21
FT HELIX 22 24
FT STRAND 26 33
FT HELIX 38 41
FT STRAND 49 53
FT HELIX 63 71
FT STRAND 74 84
FT STRAND 261 263
FT TURN 281 284
FT STRAND 287 289
FT HELIX 293 296
FT STRAND 299 303
FT HELIX 308 315
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
//
ID PDLI1_HUMAN Reviewed; 329 AA.
AC O00151; B2RBS6; Q5VZH5; Q9BPZ9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 134.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Lee C.Y., Waye M.M.Y.;
RT "Characterization of the human 36-kDa carboxyl terminal LIM domain
RT protein (hCLIM1).";
RL J. Cell. Biochem. 72:279-285(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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-
RT actinin-1 and associates with actin filaments and stress fibers in
RT activated 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [9]
RP INTERACTION WITH ALPHA-ACTININ-2.
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.,
RA Ng E.K., 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
RT 2.";
RL J. Cell. Biochem. 78:558-565(2000).
RN [10]
RP INTERACTION WITH ALPHA-ACTININ-1 AND ALPHA-ACTININ-4.
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 MASS
RP SPECTROMETRY.
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
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-144, AND MASS
RP SPECTROMETRY.
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
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP SPECTROMETRY.
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of 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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
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
CC brings other proteins (like kinases) to the cytoskeleton.
CC -!- SUBUNIT: Interacts with alpha-actinins 1, 2 and 4.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC cytoskeleton (By similarity). Note=Associates with the actin
CC stress fibers (By similarity).
CC -!- TISSUE SPECIFICITY: Strongly expressed in the heart and skeletal
CC muscle, moderately expressed in the spleen, small intestine,
CC colon, placenta, and lung. A lower level expression is seen in
CC liver, thymus, kidney, prostate and pancreas and is not found in
CC the brain, testis, ovary, and peripheral blood leukocytes.
CC -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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; CAH70720.1; -; Genomic_DNA.
DR EMBL; AL157834; CAH70720.1; JOINED; Genomic_DNA.
DR EMBL; AL157834; CAH72341.1; -; Genomic_DNA.
DR EMBL; AL160288; CAH72341.1; JOINED; Genomic_DNA.
DR EMBL; BC000915; AAH00915.1; -; mRNA.
DR EMBL; BC018755; AAH18755.1; -; mRNA.
DR RefSeq; NP_066272.1; NM_020992.3.
DR UniGene; Hs.368525; -.
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 ProteinModelPortal; O00151; -.
DR SMR; O00151; 1-87, 251-318.
DR IntAct; O00151; 11.
DR MINT; MINT-5005794; -.
DR STRING; 9606.ENSP00000360305; -.
DR PhosphoSite; O00151; -.
DR OGP; O00151; -.
DR UCD-2DPAGE; O00151; -.
DR PaxDb; O00151; -.
DR PeptideAtlas; O00151; -.
DR PRIDE; O00151; -.
DR DNASU; 9124; -.
DR Ensembl; ENST00000329399; ENSP00000360305; ENSG00000107438.
DR GeneID; 9124; -.
DR KEGG; hsa:9124; -.
DR UCSC; uc001kkh.4; human.
DR CTD; 9124; -.
DR GeneCards; GC10M096997; -.
DR HGNC; HGNC:2067; PDLIM1.
DR HPA; HPA017010; -.
DR MIM; 605900; gene.
DR neXtProt; NX_O00151; -.
DR PharmGKB; PA33158; -.
DR eggNOG; NOG250485; -.
DR HOGENOM; HOG000290704; -.
DR HOVERGEN; HBG061371; -.
DR InParanoid; O00151; -.
DR OMA; NLCIGDI; -.
DR OrthoDB; EOG77DJ69; -.
DR PhylomeDB; O00151; -.
DR ChiTaRS; PDLIM1; human.
DR EvolutionaryTrace; O00151; -.
DR GeneWiki; PDLIM1; -.
DR GenomeRNAi; 9124; -.
DR NextBio; 34201; -.
DR PRO; PR:O00151; -.
DR Bgee; O00151; -.
DR CleanEx; HS_PDLIM1; -.
DR Genevestigator; O00151; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
DR Gene3D; 2.10.110.10; -; 1.
DR InterPro; IPR028537; PDLIM1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR006643; ZASP.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24214:SF11; PTHR24214:SF11; 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; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; LIM domain; Metal-binding; Phosphoprotein;
KW Polymorphism; Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 329 PDZ and LIM domain protein 1.
FT /FTId=PRO_0000075859.
FT DOMAIN 3 85 PDZ.
FT DOMAIN 258 317 LIM zinc-binding.
FT METAL 260 260 Zinc 1.
FT METAL 263 263 Zinc 1.
FT METAL 280 280 Zinc 1.
FT METAL 283 283 Zinc 1.
FT METAL 286 286 Zinc 2.
FT METAL 289 289 Zinc 2.
FT METAL 307 307 Zinc 2.
FT METAL 310 310 Zinc 2.
FT MOD_RES 2 2 N-acetylthreonine.
FT MOD_RES 90 90 Phosphoserine.
FT MOD_RES 130 130 Phosphoserine.
FT MOD_RES 144 144 Phosphotyrosine.
FT MOD_RES 321 321 Phosphotyrosine.
FT VARIANT 175 175 N -> S (in dbSNP:rs2296961).
FT /FTId=VAR_022271.
FT CONFLICT 21 21 G -> R (in Ref. 1; AAC05580).
FT STRAND 2 12
FT STRAND 15 21
FT HELIX 22 24
FT STRAND 26 33
FT HELIX 38 41
FT STRAND 49 53
FT HELIX 63 71
FT STRAND 74 84
FT STRAND 261 263
FT TURN 281 284
FT STRAND 287 289
FT HELIX 293 296
FT STRAND 299 303
FT HELIX 308 315
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
//
MIM
605900
*RECORD*
*FIELD* NO
605900
*FIELD* TI
*605900 PDZ AND LIM DOMAIN PROTEIN 1; PDLIM1
;;ELFIN;;
CLP36, RAT, HOMOLOG OF; CLP36;;
read moreC-TERMINAL LIM DOMAIN PROTEIN 1; CLIM1
*FIELD* TX
CLONING
Proteins of the Enigma family (see ENIGMA; 605903) possess a PDZ domain
at the N terminus and 1 to 3 LIM domains at the C terminus. Enigma PDZ
domains have a P/S-W-G-F motif in place of the G-L-G-F signature
sequence found in most PDZ domains. LIM domains are cysteine-rich double
zinc fingers that are involved in protein-protein interactions.
C-terminal LIM domain proteins are cytoplasmic and are associated with
the cytoskeleton, and some are involved in protein trafficking. By
partial sequencing of cDNA clones isolated from a cardiomyopathic heart
cDNA library, followed by searching sequence databases, Kotaka et al.
(1999) obtained a cDNA encoding PDLIM1, which they called CLIM1, the
human homolog of rat Clp36 (36-kD C-terminal LIM domain protein).
Sequence analysis predicted that the 329-amino acid PDLIM1 protein,
which is 88% homologous to the rat protein, shares 51 to 61% identity
with the PDZ domains of ENIGMA, ALP (605889), ENH (605904), and RIL
(603422). SDS-PAGE analysis showed that recombinant PDLIM1 was expressed
as a 36-kD protein. Northern blot analysis revealed expression of an
approximately 2.0-kb transcript that was most abundant in heart and
skeletal muscle, moderate in spleen, small intestine, colon, placenta,
and lung, low in liver, thymus, kidney, prostate, and pancreas, and not
detectable in brain, testis, ovary, and peripheral blood leukocytes.
GENE FUNCTION
By yeast 2-hybrid analysis, Kotaka et al. (2000) showed that the LIM
domain of PDLIM1 interacts with the C-terminal EF-hand region of
alpha-actinin-2 (ACTN2; 102573). Immunoprecipitation, Western blot
analysis, and immunofluorescence microscopy demonstrated that the 36-kD
PDLIM1 protein colocalizes with ACTN2 in the Z discs of myocardial
sarcomeres, particularly at intercalated discs, and with vinculin (VCL;
193065), which is localized in the fascia adherens of intercalated
discs.
Vallenius et al. (2000) demonstrated that CLP36 localizes to actin
stress fibers via its PDZ domain through its association with cellular
alpha-actinin-1 (ACTN1; 102575) and alpha-actinin-4 (ACTN4; 604638).
By yeast 2-hybrid analysis, Vallenius and Makela (2002) showed that
CLP36 interacts with CLIK1 (STK35; 609370) through the LIM domain.
Transfection experiments indicated that CLP36 acts as an adaptor,
recruiting the CLIK1 kinase to actin stress fibers in nonmuscle cells.
MAPPING
By FISH, radiation hybrid analysis, and somatic cell hybrid analysis,
Kotaka et al. (1999) mapped the PDLIM1 gene to 10q26.
*FIELD* RF
1. Kotaka, M.; Kostin, S.; Ngai, S.; Chan, K.; Lau, Y.; Lee, S. M.
Y.; Li, H.; Ng, E. K. O.; Schaper, J.; Tsui, S. K. W.; Fung, K.; Lee,
C.; Waye, M. M. Y.: Interaction of hCLIM1, an Enigma family protein,
with alpha-actinin 2. J. Cell. Biochem. 78: 558-565, 2000.
2. Kotaka, M.; Ngai, S.-M.; Garcia-Barcelo, M.; Tsui, S. K. W.; Fung,
K.-P.; Lee, C.-Y.; Waye, M. M. Y.: Characterization of the human
36-kDa carboxyl terminal LIM domain protein (hCLIM1). J. Cell. Biochem. 72:
279-285, 1999.
3. Vallenius, T.; Luukko, K.; Makela, T. P.: CLP-36 PDZ-LIM protein
associates with nonmuscle alpha-actinin-1 and alpha-actinin-4. J.
Biol. Chem. 275: 11100-11105, 2000.
4. Vallenius, T.; Makela, T. P.: Clik1: a novel kinase targeted to
actin stress fibers by the CLP-36 PDZ-LIM protein. J. Cell Sci. 115:
2067-2073, 2002.
*FIELD* CN
Carol A. Bocchini - updated: 6/3/2005
*FIELD* CD
Paul J. Converse: 5/3/2001
*FIELD* ED
terry: 07/30/2008
terry: 5/10/2006
carol: 6/3/2005
carol: 5/16/2005
terry: 3/11/2005
mgross: 5/3/2001
*RECORD*
*FIELD* NO
605900
*FIELD* TI
*605900 PDZ AND LIM DOMAIN PROTEIN 1; PDLIM1
;;ELFIN;;
CLP36, RAT, HOMOLOG OF; CLP36;;
read moreC-TERMINAL LIM DOMAIN PROTEIN 1; CLIM1
*FIELD* TX
CLONING
Proteins of the Enigma family (see ENIGMA; 605903) possess a PDZ domain
at the N terminus and 1 to 3 LIM domains at the C terminus. Enigma PDZ
domains have a P/S-W-G-F motif in place of the G-L-G-F signature
sequence found in most PDZ domains. LIM domains are cysteine-rich double
zinc fingers that are involved in protein-protein interactions.
C-terminal LIM domain proteins are cytoplasmic and are associated with
the cytoskeleton, and some are involved in protein trafficking. By
partial sequencing of cDNA clones isolated from a cardiomyopathic heart
cDNA library, followed by searching sequence databases, Kotaka et al.
(1999) obtained a cDNA encoding PDLIM1, which they called CLIM1, the
human homolog of rat Clp36 (36-kD C-terminal LIM domain protein).
Sequence analysis predicted that the 329-amino acid PDLIM1 protein,
which is 88% homologous to the rat protein, shares 51 to 61% identity
with the PDZ domains of ENIGMA, ALP (605889), ENH (605904), and RIL
(603422). SDS-PAGE analysis showed that recombinant PDLIM1 was expressed
as a 36-kD protein. Northern blot analysis revealed expression of an
approximately 2.0-kb transcript that was most abundant in heart and
skeletal muscle, moderate in spleen, small intestine, colon, placenta,
and lung, low in liver, thymus, kidney, prostate, and pancreas, and not
detectable in brain, testis, ovary, and peripheral blood leukocytes.
GENE FUNCTION
By yeast 2-hybrid analysis, Kotaka et al. (2000) showed that the LIM
domain of PDLIM1 interacts with the C-terminal EF-hand region of
alpha-actinin-2 (ACTN2; 102573). Immunoprecipitation, Western blot
analysis, and immunofluorescence microscopy demonstrated that the 36-kD
PDLIM1 protein colocalizes with ACTN2 in the Z discs of myocardial
sarcomeres, particularly at intercalated discs, and with vinculin (VCL;
193065), which is localized in the fascia adherens of intercalated
discs.
Vallenius et al. (2000) demonstrated that CLP36 localizes to actin
stress fibers via its PDZ domain through its association with cellular
alpha-actinin-1 (ACTN1; 102575) and alpha-actinin-4 (ACTN4; 604638).
By yeast 2-hybrid analysis, Vallenius and Makela (2002) showed that
CLP36 interacts with CLIK1 (STK35; 609370) through the LIM domain.
Transfection experiments indicated that CLP36 acts as an adaptor,
recruiting the CLIK1 kinase to actin stress fibers in nonmuscle cells.
MAPPING
By FISH, radiation hybrid analysis, and somatic cell hybrid analysis,
Kotaka et al. (1999) mapped the PDLIM1 gene to 10q26.
*FIELD* RF
1. Kotaka, M.; Kostin, S.; Ngai, S.; Chan, K.; Lau, Y.; Lee, S. M.
Y.; Li, H.; Ng, E. K. O.; Schaper, J.; Tsui, S. K. W.; Fung, K.; Lee,
C.; Waye, M. M. Y.: Interaction of hCLIM1, an Enigma family protein,
with alpha-actinin 2. J. Cell. Biochem. 78: 558-565, 2000.
2. Kotaka, M.; Ngai, S.-M.; Garcia-Barcelo, M.; Tsui, S. K. W.; Fung,
K.-P.; Lee, C.-Y.; Waye, M. M. Y.: Characterization of the human
36-kDa carboxyl terminal LIM domain protein (hCLIM1). J. Cell. Biochem. 72:
279-285, 1999.
3. Vallenius, T.; Luukko, K.; Makela, T. P.: CLP-36 PDZ-LIM protein
associates with nonmuscle alpha-actinin-1 and alpha-actinin-4. J.
Biol. Chem. 275: 11100-11105, 2000.
4. Vallenius, T.; Makela, T. P.: Clik1: a novel kinase targeted to
actin stress fibers by the CLP-36 PDZ-LIM protein. J. Cell Sci. 115:
2067-2073, 2002.
*FIELD* CN
Carol A. Bocchini - updated: 6/3/2005
*FIELD* CD
Paul J. Converse: 5/3/2001
*FIELD* ED
terry: 07/30/2008
terry: 5/10/2006
carol: 6/3/2005
carol: 5/16/2005
terry: 3/11/2005
mgross: 5/3/2001