NEXN_HUMAN
ID NEXN_HUMAN Reviewed; 675 AA.
AC Q0ZGT2; A0PJ84; B4DPZ7; Q0D2H2; Q14CC2; Q14CC3; Q16081; Q7Z2X0; Q96DL0;
AC Q9Y2V1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Nexilin;
DE AltName: Full=F-actin-binding protein;
DE AltName: Full=Nelin;
GN Name=NEXN {ECO:0000312|HGNC:HGNC:29557};
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), FUNCTION, TISSUE SPECIFICITY,
RP VARIANTS CMD1CC THR-611; GLY-650 DEL AND CYS-652, VARIANT ARG-245, AND
RP CHARACTERIZATION OF VARIANTS CMD1CC THR-611; GLY-650 DEL AND CYS-652.
RX PubMed=19881492; DOI=10.1038/nm.2037;
RA Hassel D., Dahme T., Erdmann J., Meder B., Huge A., Stoll M., Just S.,
RA Hess A., Ehlermann P., Weichenhan D., Grimmler M., Liptau H., Hetzer R.,
RA Regitz-Zagrosek V., Fischer C., Nurnberg P., Schunkert H., Katus H.A.,
RA Rottbauer W.;
RT "Nexilin mutations destabilize cardiac Z-disks and lead to dilated
RT cardiomyopathy.";
RL Nat. Med. 15:1281-1288(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAB71622.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 100-675 (ISOFORM 3).
RC TISSUE=Gastric mucosa {ECO:0000312|EMBL:BAB71622.1};
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAI14446.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 100-675 (ISOFORM 1), AND VARIANT ARG-245.
RC TISSUE=Skeletal muscle {ECO:0000312|EMBL:AAI11396.1};
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 [5] {ECO:0000305, ECO:0000312|EMBL:AAD29607.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 91-675 (ISOFORM 1), FUNCTION, TISSUE
RP SPECIFICITY, AND VARIANT ARG-245.
RC TISSUE=Heart {ECO:0000312|EMBL:AAD29607.1};
RX PubMed=12053183;
RA Zhao Y., Wei Y.-J., Cao H.-Q., Ding J.-F.;
RT "Molecular cloning of NELIN, a putative human cytoskeleton regulation
RT gene.";
RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 33:19-24(2001).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAB28815.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 108-454 (ISOFORM 1).
RX PubMed=8227983; DOI=10.1007/bf03348900;
RA Elisei R., Weightman D., Kendall-Taylor P., Vassart G., Ludgate M.;
RT "Muscle autoantigens in thyroid associated ophthalmopathy: the limits of
RT molecular genetics.";
RL J. Endocrinol. Invest. 16:533-540(1993).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH F-ACTIN, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15823560; DOI=10.1016/j.bbrc.2005.03.082;
RA Wang W., Zhang W., Han Y., Chen J., Wang Y., Zhang Z., Hui R.;
RT "NELIN, a new F-actin associated protein, stimulates HeLa cell migration
RT and adhesion.";
RL Biochem. Biophys. Res. Commun. 330:1127-1131(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-16 (ISOFORM 4), AND IDENTIFICATION BY MASS
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-370, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-357,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 (ISOFORM 4), AND
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-241; SER-357 AND
RP THR-370, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-365, AND
RP IDENTIFICATION BY 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-365, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND THR-370, 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 [16]
RP VARIANTS CMH20 GLU-131 AND CYS-279, AND CHARACTERIZATION OF VARIANTS CMH20
RP GLU-131 AND CYS-279.
RX PubMed=20970104; DOI=10.1016/j.ajhg.2010.10.002;
RA Wang H., Li Z., Wang J., Sun K., Cui Q., Song L., Zou Y., Wang X., Liu X.,
RA Hui R., Fan Y.;
RT "Mutations in NEXN, a Z-disc gene, are associated with hypertrophic
RT cardiomyopathy.";
RL Am. J. Hum. Genet. 87:687-693(2010).
CC -!- FUNCTION: Involved in regulating cell migration through association
CC with the actin cytoskeleton. Has an essential role in the maintenance
CC of Z line and sarcomere integrity. {ECO:0000269|PubMed:12053183,
CC ECO:0000269|PubMed:15823560, ECO:0000269|PubMed:19881492}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000269|PubMed:15823560}.
CC -!- INTERACTION:
CC Q0ZGT2-4; P51116: FXR2; NbExp=3; IntAct=EBI-10977819, EBI-740459;
CC Q0ZGT2-4; P15622-3: ZNF250; NbExp=6; IntAct=EBI-10977819, EBI-10177272;
CC Q0ZGT2-4; P10073: ZSCAN22; NbExp=3; IntAct=EBI-10977819, EBI-10178224;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9Z2J4}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q9Z2J4}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:Q9Z2J4}. Note=Localizes to the cell-matrix AJ.
CC Not found at the cell-cell AJ. {ECO:0000250|UniProtKB:Q9Z2J4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:8227983};
CC IsoId=Q0ZGT2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q0ZGT2-2; Sequence=VSP_052541, VSP_052543;
CC Name=3 {ECO:0000269|PubMed:14702039};
CC IsoId=Q0ZGT2-3; Sequence=VSP_052542;
CC Name=4;
CC IsoId=Q0ZGT2-4; Sequence=VSP_043439;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in heart and skeletal muscle,
CC and at lower levels in placenta, lung, liver and pancreas. Also
CC expressed in HeLaS3 and MOLT-4 cell lines.
CC {ECO:0000269|PubMed:12053183, ECO:0000269|PubMed:15823560,
CC ECO:0000269|PubMed:19881492}.
CC -!- DISEASE: Cardiomyopathy, dilated 1CC (CMD1CC) [MIM:613122]: A disorder
CC characterized by ventricular dilation and impaired systolic function,
CC resulting in congestive heart failure and arrhythmia. Patients are at
CC risk of premature death. {ECO:0000269|PubMed:19881492}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Cardiomyopathy, familial hypertrophic 20 (CMH20) [MIM:613876]:
CC A hereditary heart disorder characterized by ventricular hypertrophy,
CC which is usually asymmetric and often involves the interventricular
CC septum. The symptoms include dyspnea, syncope, collapse, palpitations,
CC and chest pain. They can be readily provoked by exercise. The disorder
CC has inter- and intrafamilial variability ranging from benign to
CC malignant forms with high risk of cardiac failure and sudden cardiac
CC death. {ECO:0000269|PubMed:20970104}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17827.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH55084.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH55084.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI11396.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI14445.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI14446.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB71622.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ464902; ABE97925.1; -; mRNA.
DR EMBL; AK057954; BAB71622.1; ALT_INIT; mRNA.
DR EMBL; AK298565; BAG60759.1; -; mRNA.
DR EMBL; AC096948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC055084; AAH55084.1; ALT_SEQ; mRNA.
DR EMBL; BC017827; AAH17827.1; ALT_SEQ; mRNA.
DR EMBL; BC111395; AAI11396.1; ALT_INIT; mRNA.
DR EMBL; BC114444; AAI14445.1; ALT_INIT; mRNA.
DR EMBL; BC114445; AAI14446.1; ALT_INIT; mRNA.
DR EMBL; AF114264; AAD29607.1; -; mRNA.
DR EMBL; S67069; AAB28815.1; -; mRNA.
DR CCDS; CCDS41351.1; -. [Q0ZGT2-1]
DR CCDS; CCDS53335.1; -. [Q0ZGT2-4]
DR RefSeq; NP_001165780.1; NM_001172309.1. [Q0ZGT2-4]
DR RefSeq; NP_653174.3; NM_144573.3. [Q0ZGT2-1]
DR RefSeq; XP_005271380.1; XM_005271323.3. [Q0ZGT2-2]
DR AlphaFoldDB; Q0ZGT2; -.
DR SMR; Q0ZGT2; -.
DR BioGRID; 124855; 88.
DR IntAct; Q0ZGT2; 62.
DR MINT; Q0ZGT2; -.
DR STRING; 9606.ENSP00000333938; -.
DR iPTMnet; Q0ZGT2; -.
DR MetOSite; Q0ZGT2; -.
DR PhosphoSitePlus; Q0ZGT2; -.
DR BioMuta; NEXN; -.
DR DMDM; 121945484; -.
DR EPD; Q0ZGT2; -.
DR jPOST; Q0ZGT2; -.
DR MassIVE; Q0ZGT2; -.
DR MaxQB; Q0ZGT2; -.
DR PaxDb; Q0ZGT2; -.
DR PeptideAtlas; Q0ZGT2; -.
DR PRIDE; Q0ZGT2; -.
DR ProteomicsDB; 58848; -. [Q0ZGT2-1]
DR ProteomicsDB; 58849; -. [Q0ZGT2-2]
DR ProteomicsDB; 58850; -. [Q0ZGT2-3]
DR ProteomicsDB; 58851; -. [Q0ZGT2-4]
DR TopDownProteomics; Q0ZGT2-4; -. [Q0ZGT2-4]
DR Antibodypedia; 2776; 75 antibodies from 16 providers.
DR DNASU; 91624; -.
DR Ensembl; ENST00000330010.12; ENSP00000327363.8; ENSG00000162614.19. [Q0ZGT2-4]
DR Ensembl; ENST00000334785.12; ENSP00000333938.7; ENSG00000162614.19. [Q0ZGT2-1]
DR GeneID; 91624; -.
DR KEGG; hsa:91624; -.
DR MANE-Select; ENST00000334785.12; ENSP00000333938.7; NM_144573.4; NP_653174.3.
DR UCSC; uc001dib.5; human. [Q0ZGT2-1]
DR CTD; 91624; -.
DR DisGeNET; 91624; -.
DR GeneCards; NEXN; -.
DR GeneReviews; NEXN; -.
DR HGNC; HGNC:29557; NEXN.
DR HPA; ENSG00000162614; Group enriched (heart muscle, skeletal muscle, tongue).
DR MalaCards; NEXN; -.
DR MIM; 613121; gene.
DR MIM; 613122; phenotype.
DR MIM; 613876; phenotype.
DR neXtProt; NX_Q0ZGT2; -.
DR OpenTargets; ENSG00000162614; -.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy.
DR PharmGKB; PA134974801; -.
DR VEuPathDB; HostDB:ENSG00000162614; -.
DR eggNOG; ENOG502QU7W; Eukaryota.
DR GeneTree; ENSGT00730000111176; -.
DR HOGENOM; CLU_023108_1_1_1; -.
DR InParanoid; Q0ZGT2; -.
DR OMA; MVRSESQ; -.
DR OrthoDB; 928616at2759; -.
DR PhylomeDB; Q0ZGT2; -.
DR TreeFam; TF328960; -.
DR PathwayCommons; Q0ZGT2; -.
DR SignaLink; Q0ZGT2; -.
DR BioGRID-ORCS; 91624; 12 hits in 1078 CRISPR screens.
DR ChiTaRS; NEXN; human.
DR GenomeRNAi; 91624; -.
DR Pharos; Q0ZGT2; Tbio.
DR PRO; PR:Q0ZGT2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q0ZGT2; protein.
DR Bgee; ENSG00000162614; Expressed in left ventricle myocardium and 157 other tissues.
DR ExpressionAtlas; Q0ZGT2; baseline and differential.
DR Genevisible; Q0ZGT2; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0008307; F:structural constituent of muscle; IMP:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IEP:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cardiomyopathy; Cell junction;
KW Cytoplasm; Cytoskeleton; Disease variant; Immunoglobulin domain;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..675
FT /note="Nexilin"
FT /id="PRO_0000302085"
FT DOMAIN 582..670
FT /note="Ig-like"
FT /evidence="ECO:0000255"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, 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 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 370
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TPW1"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2J4"
FT VAR_SEQ 9..72
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043439"
FT VAR_SEQ 150..163
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052541"
FT VAR_SEQ 237..298
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052542"
FT VAR_SEQ 673..675
FT /note="SKN -> TDDY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052543"
FT VARIANT 131
FT /note="Q -> E (in CMH20; affects interaction with ACTA1 and
FT F-actin; dbSNP:rs387907079)"
FT /evidence="ECO:0000269|PubMed:20970104"
FT /id="VAR_065477"
FT VARIANT 245
FT /note="G -> R (in dbSNP:rs1166698)"
FT /evidence="ECO:0000269|PubMed:12053183,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:19881492"
FT /id="VAR_049963"
FT VARIANT 279
FT /note="R -> C (in CMH20; the mutant protein accumulates in
FT the cytoplasm but binding to ACTA1 is not altered;
FT dbSNP:rs146245480)"
FT /evidence="ECO:0000269|PubMed:20970104"
FT /id="VAR_065478"
FT VARIANT 335
FT /note="R -> K (in dbSNP:rs9660322)"
FT /id="VAR_059414"
FT VARIANT 611
FT /note="P -> T (in CMD1CC; affects cardiac Z line integrity;
FT no effect on protein expression and stability;
FT dbSNP:rs137853198)"
FT /evidence="ECO:0000269|PubMed:19881492"
FT /id="VAR_063009"
FT VARIANT 650
FT /note="Missing (in CMD1CC; affects cardiac Z-disk
FT integrity; no effect on protein expression and stability)"
FT /evidence="ECO:0000269|PubMed:19881492"
FT /id="VAR_063010"
FT VARIANT 652
FT /note="Y -> C (in CMD1CC; affects cardiac Z line integrity;
FT no effect on protein expression and stability;
FT dbSNP:rs137853197)"
FT /evidence="ECO:0000269|PubMed:19881492"
FT /id="VAR_063011"
FT CONFLICT 94..101
FT /note="YVPKLTGT -> NLPFTVP (in Ref. 4; AAD29607)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="K -> E (in Ref. 5; AAI14446)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="R -> K (in Ref. 4; AAD29607)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="L -> Q (in Ref. 5; AAH17827)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="A -> T (in Ref. 2; BAB71622)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="Y -> H (in Ref. 2; BAB71622)"
FT /evidence="ECO:0000305"
FT MOD_RES Q0ZGT2-4:16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
SQ SEQUENCE 675 AA; 80658 MW; 18D6336E62503E7F CRC64;
MNDISQKAEI LLSSSKPVPK TYVPKLGKGD VKDKFEAMQR AREERNQRRS RDEKQRRKEQ
YIREREWNRR KQEIKEMLAS DDEEDVSSKV EKAYVPKLTG TVKGRFAEME KQRQEEQRKR
TEEERKRRIE QDMLEKRKIQ RELAKRAEQI EDINNTGTES ASEEGDDSLL ITVVPVKSYK
TSGKMKKNFE DLEKEREEKE RIKYEEDKRI RYEEQRPSLK EAKCLSLVMD DEIESEAKKE
SLSPGKLKLT FEELERQRQE NRKKQAEEEA RKRLEEEKRA FEEARRQMVN EDEENQDTAK
IFKGYRPGKL KLSFEEMERQ RREDEKRKAE EEARRRIEEE KKAFAEARRN MVVDDDSPEM
YKTISQEFLT PGKLEINFEE LLKQKMEEEK RRTEEERKHK LEMEKQEFEQ LRQEMGEEEE
ENETFGLSRE YEELIKLKRS GSIQAKNLKS KFEKIGQLSE KEIQKKIEEE RARRRAIDLE
IKEREAENFH EEDDVDVRPA RKSEAPFTHK VNMKARFEQM AKAREEEEQR RIEEQKLLRM
QFEQREIDAA LQKKREEEEE EEGSIMNGST AEDEEQTRSG APWFKKPLKN TSVVDSEPVR
FTVKVTGEPK PEITWWFEGE ILQDGEDYQY IERGETYCLY LPETFPEDGG EYMCKAVNNK
GSAASTCILT IESKN
