PDLI5_HUMAN
ID PDLI5_HUMAN Reviewed; 596 AA.
AC Q96HC4; A8K6F9; D6RB78; E9PBF5; O60705; Q56VN4; Q5UW38; Q8WVK0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 5.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=PDZ and LIM domain protein 5 {ECO:0000305};
DE AltName: Full=Enigma homolog {ECO:0000303|PubMed:10429367};
DE AltName: Full=Enigma-like PDZ and LIM domains protein {ECO:0000303|PubMed:10429367};
GN Name=PDLIM5 {ECO:0000303|PubMed:15346770, ECO:0000312|HGNC:HGNC:17468};
GN Synonyms=ENH {ECO:0000303|PubMed:10429367}; ORFNames=L9;
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), TISSUE SPECIFICITY, AND VARIANTS
RP LEU-319; THR-345 AND ASN-492.
RX PubMed=10429367; DOI=10.1007/s100380050155;
RA Ueki N., Seki N., Yano K., Masuho Y., Saito T., Muramatsu M.;
RT "Isolation, tissue expression, and chromosomal assignment of a human LIM
RT protein gene, showing homology to rat enigma homologue (ENH).";
RL J. Hum. Genet. 44:256-260(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX PubMed=15346770; DOI=10.1080/10425170310001656756;
RA Wu M., Li Y., Ji C., Xu J., Zheng H., Zou X., Gu S., Lou Y., Xie Y.,
RA Mao Y.;
RT "Cloning and identification of a novel human gene PDLIM5, a homolog of AD-
RT associated neuronal thread protein (AD7c-NTP).";
RL DNA Seq. 15:144-147(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS LEU-319; THR-345 AND
RP ASN-492.
RX PubMed=15334068; DOI=10.1038/sj.onc.1207921;
RA Petroziello J., Yamane A., Westendorf L., Thompson M., McDonagh C.,
RA Cerveny C., Law C.-L., Wahl A., Carter P.;
RT "Suppression subtractive hybridization and expression profiling identifies
RT a unique set of genes overexpressed in non-small-cell lung cancer.";
RL Oncogene 23:7734-7745(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS THR-345;
RP ALA-381 AND ASN-492.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP PHE-136; THR-345 AND ASN-492.
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS THR-345;
RP ALA-381 AND ASN-492.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP THR-345; ALA-381 AND ASN-492.
RC TISSUE=Skin;
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 [11]
RP PROTEIN SEQUENCE OF 2-17 AND 84-97 (ISOFORMS 1/2), CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RA Bienvenut W.V., Claeys D.;
RL Submitted (NOV-2005) to UniProtKB.
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=16044170; DOI=10.1038/sj.mp.4001719;
RA Kato T., Iwayama Y., Kakiuchi C., Iwamoto K., Yamada K., Minabe Y.,
RA Nakamura K., Mori N., Fujii K., Nanko S., Yoshikawa T.;
RT "Gene expression and association analyses of LIM (PDLIM5) in bipolar
RT disorder and schizophrenia.";
RL Mol. Psychiatry 10:1045-1055(2005).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=16213469; DOI=10.1016/j.biopsych.2005.07.041;
RA Horiuchi Y., Arai M., Niizato K., Iritani S., Noguchi E., Ohtsuki T.,
RA Koga M., Kato T., Itokawa M., Arinami T.;
RT "A polymorphism in the PDLIM5 gene associated with gene expression and
RT schizophrenia.";
RL Biol. Psychiatry 59:434-439(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-313, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP IDENTIFICATION BY 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-137; SER-309 AND
RP SER-313, AND IDENTIFICATION BY 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-137; SER-309 AND
RP SER-313, AND 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-134; SER-137;
RP SER-260; SER-309; SER-313; SER-360 AND SER-362, AND IDENTIFICATION BY MASS
RP 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313 AND SER-360, AND
RP IDENTIFICATION BY 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 [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-89, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [25]
RP STRUCTURE BY NMR OF 400-476.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of first LIM domain of enigma-like PDZ and LIM domains
RT protein.";
RL Submitted (DEC-2006) to the PDB data bank.
RN [26]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-83.
RX PubMed=20120020; DOI=10.1002/pro.349;
RA Elkins J.M., Gileadi C., Shrestha L., Phillips C., Wang J., Muniz J.R.,
RA Doyle D.A.;
RT "Unusual binding interactions in PDZ domain crystal structures help explain
RT binding mechanisms.";
RL Protein Sci. 19:731-741(2010).
RN [27]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-492, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: May play an important role in the heart development by
CC scaffolding PKC to the Z-disk region. May play a role in the regulation
CC of cardiomyocyte expansion. Isoforms lacking the LIM domains may
CC negatively modulate the scaffolding activity of isoform 1.
CC Overexpression promotes the development of heart hypertrophy.
CC Contributes to the regulation of dendritic spine morphogenesis in
CC neurons. May be required to restrain postsynaptic growth of excitatory
CC synapses. Isoform 1, but not isoform 2, expression favors spine
CC thinning and elongation. {ECO:0000250|UniProtKB:Q62920}.
CC -!- SUBUNIT: Interacts with various PKC isoforms through the LIM domains.
CC Interacts with actin and alpha-actinin through the PDZ domain.
CC Interacts (via LIM domains) with SIPA1L1/SPAR; this interaction may
CC occur preferentially with isoform 1. {ECO:0000250|UniProtKB:Q62920}.
CC -!- INTERACTION:
CC Q96HC4; P54253: ATXN1; NbExp=6; IntAct=EBI-751267, EBI-930964;
CC Q96HC4; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-751267, EBI-10171416;
CC Q96HC4; P38432: COIL; NbExp=4; IntAct=EBI-751267, EBI-945751;
CC Q96HC4; P14136: GFAP; NbExp=3; IntAct=EBI-751267, EBI-744302;
CC Q96HC4; P42858: HTT; NbExp=9; IntAct=EBI-751267, EBI-466029;
CC Q96HC4; Q02363: ID2; NbExp=5; IntAct=EBI-751267, EBI-713450;
CC Q96HC4; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-751267, EBI-1055254;
CC Q96HC4; Q6A162: KRT40; NbExp=3; IntAct=EBI-751267, EBI-10171697;
CC Q96HC4; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-751267, EBI-10172290;
CC Q96HC4; Q15942: ZYX; NbExp=3; IntAct=EBI-751267, EBI-444225;
CC Q96HC4-3; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-25913059, EBI-618189;
CC Q96HC4-3; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-25913059, EBI-9088619;
CC Q96HC4-3; Q9NWZ8: GEMIN8; NbExp=3; IntAct=EBI-25913059, EBI-2626001;
CC Q96HC4-3; Q03403: TFF2; NbExp=3; IntAct=EBI-25913059, EBI-4314702;
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000250|UniProtKB:Q62920}. Presynapse
CC {ECO:0000250|UniProtKB:Q62920}. Postsynapse
CC {ECO:0000250|UniProtKB:Q62920}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q62920}. Note=Detected both at presynaptic and
CC postsynaptic sites, exclusively at excitatory synapses, but not
CC inhibitory synapses, in hippocampal neurons.
CC {ECO:0000250|UniProtKB:Q62920}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q96HC4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96HC4-2; Sequence=VSP_039075, VSP_039076, VSP_039077,
CC VSP_039078;
CC Name=3;
CC IsoId=Q96HC4-3; Sequence=VSP_039206, VSP_039207, VSP_039077,
CC VSP_039078;
CC Name=4;
CC IsoId=Q96HC4-4; Sequence=VSP_039075;
CC Name=5;
CC IsoId=Q96HC4-5; Sequence=VSP_045098, VSP_045099;
CC Name=6;
CC IsoId=Q96HC4-6; Sequence=VSP_039075, VSP_039076, VSP_053796;
CC Name=7;
CC IsoId=Q96HC4-7; Sequence=VSP_039075, VSP_039076, VSP_053797;
CC -!- TISSUE SPECIFICITY: Heart and skeletal muscle specific. Expression is
CC commonly increased in the brain of patients with bipolar disorder,
CC schizophrenia, and major depression. {ECO:0000269|PubMed:10429367,
CC ECO:0000269|PubMed:16044170, ECO:0000269|PubMed:16213469}.
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; AF061258; AAC15767.1; -; mRNA.
DR EMBL; AY345240; AAR09142.1; -; mRNA.
DR EMBL; AY598328; AAT06739.1; -; mRNA.
DR EMBL; BT007328; AAP35992.1; -; mRNA.
DR EMBL; AK291624; BAF84313.1; -; mRNA.
DR EMBL; AK291898; BAF84587.1; -; mRNA.
DR EMBL; CR610626; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL833438; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC093778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX06054.1; -; Genomic_DNA.
DR EMBL; BC017902; AAH17902.1; -; mRNA.
DR EMBL; BC008741; AAH08741.1; -; mRNA.
DR CCDS; CCDS3641.1; -. [Q96HC4-1]
DR CCDS; CCDS47102.1; -. [Q96HC4-4]
DR CCDS; CCDS47103.1; -. [Q96HC4-2]
DR CCDS; CCDS47104.1; -. [Q96HC4-3]
DR CCDS; CCDS58915.1; -. [Q96HC4-5]
DR CCDS; CCDS58916.1; -. [Q96HC4-6]
DR CCDS; CCDS58917.1; -. [Q96HC4-7]
DR RefSeq; NP_001011515.1; NM_001011515.2. [Q96HC4-2]
DR RefSeq; NP_001011516.1; NM_001011516.2. [Q96HC4-3]
DR RefSeq; NP_001243358.1; NM_001256429.1. [Q96HC4-5]
DR RefSeq; NP_006448.4; NM_006457.4. [Q96HC4-1]
DR PDB; 2DAR; NMR; -; A=400-476.
DR PDB; 2UZC; X-ray; 1.50 A; A/B/C/D/E=1-83.
DR PDBsum; 2DAR; -.
DR PDBsum; 2UZC; -.
DR AlphaFoldDB; Q96HC4; -.
DR SMR; Q96HC4; -.
DR BioGRID; 115857; 130.
DR DIP; DIP-34898N; -.
DR IntAct; Q96HC4; 54.
DR MINT; Q96HC4; -.
DR GlyGen; Q96HC4; 18 sites, 2 O-linked glycans (18 sites).
DR iPTMnet; Q96HC4; -.
DR MetOSite; Q96HC4; -.
DR PhosphoSitePlus; Q96HC4; -.
DR SwissPalm; Q96HC4; -.
DR BioMuta; PDLIM5; -.
DR DMDM; 317373590; -.
DR EPD; Q96HC4; -.
DR jPOST; Q96HC4; -.
DR MassIVE; Q96HC4; -.
DR MaxQB; Q96HC4; -.
DR PaxDb; Q96HC4; -.
DR PeptideAtlas; Q96HC4; -.
DR PRIDE; Q96HC4; -.
DR ProteomicsDB; 13553; -.
DR ProteomicsDB; 19211; -.
DR ProteomicsDB; 62593; -.
DR ProteomicsDB; 76730; -. [Q96HC4-1]
DR ProteomicsDB; 76731; -. [Q96HC4-2]
DR ProteomicsDB; 76732; -. [Q96HC4-3]
DR ProteomicsDB; 76733; -. [Q96HC4-4]
DR Antibodypedia; 4614; 417 antibodies from 30 providers.
DR DNASU; 10611; -.
DR Ensembl; ENST00000317968.9; ENSP00000321746.4; ENSG00000163110.15. [Q96HC4-1]
DR Ensembl; ENST00000318007.9; ENSP00000322021.5; ENSG00000163110.15. [Q96HC4-3]
DR Ensembl; ENST00000359265.8; ENSP00000352210.4; ENSG00000163110.15. [Q96HC4-5]
DR Ensembl; ENST00000380180.7; ENSP00000369527.3; ENSG00000163110.15. [Q96HC4-2]
DR Ensembl; ENST00000503974.5; ENSP00000424297.1; ENSG00000163110.15. [Q96HC4-7]
DR Ensembl; ENST00000508216.5; ENSP00000426804.1; ENSG00000163110.15. [Q96HC4-2]
DR Ensembl; ENST00000514743.5; ENSP00000424360.1; ENSG00000163110.15. [Q96HC4-6]
DR Ensembl; ENST00000542407.5; ENSP00000442187.2; ENSG00000163110.15. [Q96HC4-4]
DR Ensembl; ENST00000615540.4; ENSP00000480359.1; ENSG00000163110.15. [Q96HC4-6]
DR GeneID; 10611; -.
DR KEGG; hsa:10611; -.
DR MANE-Select; ENST00000317968.9; ENSP00000321746.4; NM_006457.5; NP_006448.5.
DR UCSC; uc003htf.5; human. [Q96HC4-1]
DR CTD; 10611; -.
DR DisGeNET; 10611; -.
DR GeneCards; PDLIM5; -.
DR HGNC; HGNC:17468; PDLIM5.
DR HPA; ENSG00000163110; Group enriched (heart muscle, skeletal muscle, tongue).
DR MIM; 605904; gene.
DR neXtProt; NX_Q96HC4; -.
DR OpenTargets; ENSG00000163110; -.
DR PharmGKB; PA134917248; -.
DR VEuPathDB; HostDB:ENSG00000163110; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000155292; -.
DR HOGENOM; CLU_038114_3_0_1; -.
DR InParanoid; Q96HC4; -.
DR OMA; QDTFVQR; -.
DR OrthoDB; 1013114at2759; -.
DR PhylomeDB; Q96HC4; -.
DR TreeFam; TF106408; -.
DR PathwayCommons; Q96HC4; -.
DR Reactome; R-HSA-6794361; Neurexins and neuroligins.
DR SignaLink; Q96HC4; -.
DR BioGRID-ORCS; 10611; 17 hits in 1088 CRISPR screens.
DR ChiTaRS; PDLIM5; human.
DR EvolutionaryTrace; Q96HC4; -.
DR GeneWiki; PDLIM5; -.
DR GenomeRNAi; 10611; -.
DR Pharos; Q96HC4; Tbio.
DR PRO; PR:Q96HC4; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q96HC4; protein.
DR Bgee; ENSG00000163110; Expressed in skeletal muscle tissue of biceps brachii and 207 other tissues.
DR ExpressionAtlas; Q96HC4; baseline and differential.
DR Genevisible; Q96HC4; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:LIFEdb.
DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0042805; F:actinin 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:0005080; F:protein kinase C binding; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISS:BHF-UCL.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0051963; P:regulation of synapse assembly; ISS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR031847; DUF4749.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF15936; DUF4749; 1.
DR Pfam; PF00412; LIM; 3.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Cytoplasm; Direct protein sequencing; Isopeptide bond; LIM domain;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Synapse;
KW Ubl conjugation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.11, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..596
FT /note="PDZ and LIM domain protein 5"
FT /id="PRO_0000075877"
FT DOMAIN 2..85
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 418..477
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 477..536
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 536..596
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 121..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.11, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62920"
FT MOD_RES 89
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CI51"
FT MOD_RES 89
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8CI51"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI51"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62920"
FT MOD_RES 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI51"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 33..136
FT /note="LKDGGKAAQANVRIGDVVLSIDGINAQGMTHLEAQNKIKGCTGSLNMTLQRA
FT SAAPKPEPVPVQKGEPKEVVKPVPITSPAVSKVTSTNNMAYNKAPRPFGSVS -> AGV
FT QWRNLGSPQPPSPEFKRFSCLSLPSSWDYRHVPPRLANFVFLVETKFPYVGQAGLELPT
FT SGDLPTSASQSAKITGVSHRAWPTLFYTLLFFATIYPEIILY (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15346770"
FT /id="VSP_045098"
FT VAR_SEQ 98..206
FT /note="Missing (in isoform 2, isoform 4, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.6"
FT /id="VSP_039075"
FT VAR_SEQ 98..117
FT /note="GEPKEVVKPVPITSPAVSKV -> KTQVTNNPGTVKIPPKRPPR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039206"
FT VAR_SEQ 118..240
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_039207"
FT VAR_SEQ 137..596
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15346770"
FT /id="VSP_045099"
FT VAR_SEQ 237
FT /note="G -> GKIPPKR (in isoform 2, isoform 6 and isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039076"
FT VAR_SEQ 307..337
FT /note="NNSQEPSPQLASSVASTRSMPESLDSPTSGR -> KEKIPLHVFSPKYTKLR
FT DWHHEVSARALNVQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_039077"
FT VAR_SEQ 307
FT /note="N -> KFDSALEDLPKSGPHPPATPQVLTIGSQVATLSKVATTYSSLSSSTG
FT NVEDSFEGFRNFSTFSSPARYSAAVLSSAAATVSAVIATKTRLYTPERYHSLLDALCIS
FT PVSKPLAFSYLQSSRKSTGSIHVKKTS (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_053796"
FT VAR_SEQ 338..596
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_039078"
FT VAR_SEQ 587..596
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_053797"
FT VARIANT 136
FT /note="S -> F (in dbSNP:rs2452600)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_023779"
FT VARIANT 319
FT /note="S -> L (in dbSNP:rs1064238)"
FT /evidence="ECO:0000269|PubMed:10429367,
FT ECO:0000269|PubMed:15334068"
FT /id="VAR_046662"
FT VARIANT 345
FT /note="A -> T (in dbSNP:rs966845)"
FT /evidence="ECO:0000269|PubMed:10429367,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15334068,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.9"
FT /id="VAR_046663"
FT VARIANT 381
FT /note="T -> A (in dbSNP:rs7690296)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.9"
FT /id="VAR_046664"
FT VARIANT 388
FT /note="P -> S (in dbSNP:rs7690464)"
FT /id="VAR_046665"
FT VARIANT 492
FT /note="S -> N (in dbSNP:rs13107595)"
FT /evidence="ECO:0000269|PubMed:10429367,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15334068,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.9, ECO:0007744|PubMed:21269460"
FT /id="VAR_046666"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:2UZC"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:2UZC"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:2UZC"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2UZC"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:2UZC"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:2UZC"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:2UZC"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:2UZC"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:2DAR"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:2DAR"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:2DAR"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:2DAR"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:2DAR"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:2DAR"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:2DAR"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:2DAR"
FT STRAND 458..463
FT /evidence="ECO:0007829|PDB:2DAR"
FT HELIX 468..474
FT /evidence="ECO:0007829|PDB:2DAR"
FT CONFLICT Q96HC4-2:221
FT /note="D -> G (in Ref. 6; AL833438)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 596 AA; 63945 MW; BBEAB9EDFA060736 CRC64;
MSNYSVSLVG PAPWGFRLQG GKDFNMPLTI SSLKDGGKAA QANVRIGDVV LSIDGINAQG
MTHLEAQNKI KGCTGSLNMT LQRASAAPKP EPVPVQKGEP KEVVKPVPIT SPAVSKVTST
NNMAYNKAPR PFGSVSSPKV TSIPSPSSAF TPAHATTSSH ASPSPVAAVT PPLFAASGLH
ANANLSADQS PSALSAGKTA VNVPRQPTVT SVCSETSQEL AEGQRRGSQG DSKQQNGPPR
KHIVERYTEF YHVPTHSDAS KKRLIEDTED WRPRTGTTQS RSFRILAQIT GTEHLKESEA
DNTKKANNSQ EPSPQLASSV ASTRSMPESL DSPTSGRPGV TSLTAAAAFK PVGSTGVIKS
PSWQRPNQGV PSTGRISNSA TYSGSVAPAN SALGQTQPSD QDTLVQRAEH IPAGKRTPMC
AHCNQVIRGP FLVALGKSWH PEEFNCAHCK NTMAYIGFVE EKGALYCELC YEKFFAPECG
RCQRKILGEV ISALKQTWHV SCFVCVACGK PIRNNVFHLE DGEPYCETDY YALFGTICHG
CEFPIEAGDM FLEALGYTWH DTCFVCSVCC ESLEGQTFFS KKDKPLCKKH AHSVNF
