ZYX_HUMAN
ID ZYX_HUMAN Reviewed; 572 AA.
AC Q15942; A4D2G6; B4DQX7; Q6I9S4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Zyxin;
DE AltName: Full=Zyxin-2;
GN Name=ZYX;
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).
RC TISSUE=Umbilical vein;
RX PubMed=8940160; DOI=10.1074/jbc.271.49.31470;
RA Macalma T., Otte J., Hensler M.E., Bockholt S.M., Louis H.A.,
RA Kalff-Suske M., Grzeschik K.H., von der Ahe D., Beckerle M.C.;
RT "Molecular characterization of human zyxin.";
RL J. Biol. Chem. 271:31470-31478(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=8917469; DOI=10.1111/j.1432-1033.1996.00657.x;
RA Zumbrunn J., Trueb B.;
RT "A zyxin-related protein whose synthesis is reduced in virally transformed
RT fibroblasts.";
RL Eur. J. Biochem. 241:657-663(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, Skin, and Uterus;
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 [9]
RP PROTEIN SEQUENCE OF 2-25; 36-54; 168-184; 280-320 AND 325-375, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F.;
RL Submitted (FEB-2008) to UniProtKB.
RN [10]
RP INTERACTION WITH ENAH AND VASP, AND MUTAGENESIS OF PHE-71; PHE-93; PHE-104
RP AND PHE-114.
RX PubMed=10801818; DOI=10.1074/jbc.m001698200;
RA Drees B., Friederich E., Fradelizi J., Louvard D., Beckerle M.C.,
RA Golsteyn R.M.;
RT "Characterization of the interaction between zyxin and members of the
RT Ena/vasodilator-stimulated phosphoprotein family of proteins.";
RL J. Biol. Chem. 275:22503-22511(2000).
RN [11]
RP INTERACTION WITH HPV6 E6 (MICROBIAL INFECTION).
RX PubMed=11689660; DOI=10.1128/jvi.75.23.11791-11802.2001;
RA Degenhardt Y.Y., Silverstein S.;
RT "Interaction of zyxin, a focal adhesion protein, with the E6 protein from
RT human papillomavirus type 6 results in its nuclear translocation.";
RL J. Virol. 75:11791-11802(2001).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TES.
RX PubMed=12695497; DOI=10.1083/jcb.200211015;
RA Garvalov B.K., Higgins T.E., Sutherland J.D., Zettl M., Scaplehorn N.,
RA Koecher T., Piddini E., Griffiths G., Way M.;
RT "The conformational state of Tes regulates its zyxin-dependent recruitment
RT to focal adhesions.";
RL J. Cell Biol. 161:33-39(2003).
RN [13]
RP INTERACTION WITH SYNPO2.
RX PubMed=16885336; DOI=10.1158/0008-5472.can-06-0227;
RA Yu Y.P., Luo J.H.;
RT "Myopodin-mediated suppression of prostate cancer cell migration involves
RT interaction with zyxin.";
RL Cancer Res. 66:7414-7419(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-281, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [16]
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 [17]
RP INTERACTION WITH EVL; VASP AND ENAH.
RX PubMed=18158903; DOI=10.1016/j.molcel.2007.10.033;
RA Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J.,
RA McDonald N.Q., Way M.;
RT "Tes, a specific Mena interacting partner, breaks the rules for EVH1
RT binding.";
RL Mol. Cell 28:1071-1082(2007).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=18297730; DOI=10.1002/dvdy.21471;
RA Martynova N.Y., Eroshkin F.M., Ermolina L.V., Ermakova G.V.,
RA Korotaeva A.L., Smurova K.M., Gyoeva F.K., Zaraisky A.G.;
RT "The LIM-domain protein zyxin binds the homeodomain factor Xanf1/Hesx1 and
RT modulates its activity in the anterior neural plate of Xenopus laevis
RT embryo.";
RL Dev. Dyn. 237:736-749(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; SER-281 AND SER-344, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-259; SER-267;
RP THR-270; THR-274; SER-281; SER-288; SER-308 AND SER-344, AND IDENTIFICATION
RP 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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
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 [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-279, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-179; SER-259;
RP THR-274; SER-281; SER-308 AND SER-344, AND IDENTIFICATION BY MASS
RP 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 [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; THR-270; SER-281 AND
RP SER-344, AND 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 [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-170; SER-259;
RP SER-267; THR-270; SER-281; SER-308 AND SER-344, 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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-142; SER-259;
RP SER-267; SER-281 AND SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Adhesion plaque protein. Binds alpha-actinin and the CRP
CC protein. Important for targeting TES and ENA/VASP family members to
CC focal adhesions and for the formation of actin-rich structures. May be
CC a component of a signal transduction pathway that mediates adhesion-
CC stimulated changes in gene expression (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HPV type 6 protein E6. Does not interact
CC significantly with E6 proteins from HPV types 11, 16, or 18. Interacts,
CC via the Pro-rich regions, with the EVH1 domains of ENAH, EVL and VASP.
CC Interacts with the first LIM domain of TES. Interacts with NEBL
CC (isoform 2). Interacts with SYNPO2. {ECO:0000269|PubMed:10801818,
CC ECO:0000269|PubMed:12695497, ECO:0000269|PubMed:16885336,
CC ECO:0000269|PubMed:18158903}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus type
CC 6/HPV6 protein E6. Does not interact significantly with E6 proteins
CC from HPV types 11, 16, or 18. {ECO:0000269|PubMed:11689660}.
CC -!- INTERACTION:
CC Q15942; Q9NQ75-2: CASS4; NbExp=4; IntAct=EBI-444225, EBI-12270182;
CC Q15942; Q9UI08-2: EVL; NbExp=5; IntAct=EBI-444225, EBI-6448852;
CC Q15942; Q9NV31: IMP3; NbExp=8; IntAct=EBI-444225, EBI-747481;
CC Q15942; P28838: LAP3; NbExp=3; IntAct=EBI-444225, EBI-2339312;
CC Q15942; O95835: LATS1; NbExp=10; IntAct=EBI-444225, EBI-444209;
CC Q15942; O14910: LIN7A; NbExp=3; IntAct=EBI-444225, EBI-2513988;
CC Q15942; A0A0S2Z4M0: NME5; NbExp=4; IntAct=EBI-444225, EBI-16430544;
CC Q15942; P35372: OPRM1; NbExp=2; IntAct=EBI-444225, EBI-2624570;
CC Q15942; Q96HC4: PDLIM5; NbExp=3; IntAct=EBI-444225, EBI-751267;
CC Q15942; Q96BD5: PHF21A; NbExp=6; IntAct=EBI-444225, EBI-745085;
CC Q15942; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-444225, EBI-2798044;
CC Q15942; Q8WWV3: RTN4IP1; NbExp=5; IntAct=EBI-444225, EBI-743502;
CC Q15942; P50552: VASP; NbExp=4; IntAct=EBI-444225, EBI-748201;
CC Q15942; Q96KM6: ZNF512B; NbExp=3; IntAct=EBI-444225, EBI-1049952;
CC Q15942; B2R9Y1; NbExp=3; IntAct=EBI-444225, EBI-10175746;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Nucleus. Cell
CC junction, focal adhesion. Note=Associates with the actin cytoskeleton
CC near the adhesion plaques. Enters the nucleus in the presence of HESX1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15942-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15942-2; Sequence=VSP_057288;
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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DR EMBL; X94991; CAA64447.1; -; mRNA.
DR EMBL; X95735; CAA65050.1; -; mRNA.
DR EMBL; AK299005; BAG61089.1; -; mRNA.
DR EMBL; AK316227; BAH14598.1; -; mRNA.
DR EMBL; CR457431; CAG33712.1; -; mRNA.
DR EMBL; AC092214; AAS07459.1; -; Genomic_DNA.
DR EMBL; CH236959; EAL23788.1; -; Genomic_DNA.
DR EMBL; CH471198; EAW51848.1; -; Genomic_DNA.
DR EMBL; BC008743; AAH08743.1; -; mRNA.
DR EMBL; BC009360; AAH09360.1; -; mRNA.
DR EMBL; BC010031; AAH10031.1; -; mRNA.
DR CCDS; CCDS5883.1; -. [Q15942-1]
DR PIR; G02845; G02845.
DR RefSeq; NP_001010972.1; NM_001010972.1. [Q15942-1]
DR RefSeq; NP_003452.1; NM_003461.4. [Q15942-1]
DR AlphaFoldDB; Q15942; -.
DR SMR; Q15942; -.
DR BioGRID; 113569; 293.
DR CORUM; Q15942; -.
DR IntAct; Q15942; 92.
DR MINT; Q15942; -.
DR STRING; 9606.ENSP00000324422; -.
DR ChEMBL; CHEMBL4295832; -.
DR DrugBank; DB11638; Artenimol.
DR GlyGen; Q15942; 18 sites, 3 O-linked glycans (18 sites).
DR iPTMnet; Q15942; -.
DR MetOSite; Q15942; -.
DR PhosphoSitePlus; Q15942; -.
DR SwissPalm; Q15942; -.
DR BioMuta; ZYX; -.
DR DMDM; 2497677; -.
DR OGP; Q15942; -.
DR CPTAC; CPTAC-1022; -.
DR CPTAC; CPTAC-452; -.
DR CPTAC; CPTAC-453; -.
DR EPD; Q15942; -.
DR jPOST; Q15942; -.
DR MassIVE; Q15942; -.
DR MaxQB; Q15942; -.
DR PaxDb; Q15942; -.
DR PeptideAtlas; Q15942; -.
DR PRIDE; Q15942; -.
DR ProteomicsDB; 4911; -.
DR ProteomicsDB; 60823; -. [Q15942-1]
DR Antibodypedia; 1394; 397 antibodies from 43 providers.
DR DNASU; 7791; -.
DR Ensembl; ENST00000322764.10; ENSP00000324422.5; ENSG00000159840.16. [Q15942-1]
DR Ensembl; ENST00000392910.6; ENSP00000376642.2; ENSG00000159840.16. [Q15942-2]
DR Ensembl; ENST00000645637.1; ENSP00000495629.1; ENSG00000285443.2. [Q15942-2]
DR Ensembl; ENST00000646695.2; ENSP00000494798.1; ENSG00000285443.2. [Q15942-1]
DR GeneID; 7791; -.
DR KEGG; hsa:7791; -.
DR MANE-Select; ENST00000322764.10; ENSP00000324422.5; NM_003461.5; NP_003452.1.
DR UCSC; uc003wcx.5; human. [Q15942-1]
DR CTD; 7791; -.
DR DisGeNET; 7791; -.
DR GeneCards; ZYX; -.
DR HGNC; HGNC:13200; ZYX.
DR HPA; ENSG00000159840; Tissue enhanced (endometrium).
DR MIM; 602002; gene.
DR neXtProt; NX_Q15942; -.
DR OpenTargets; ENSG00000159840; -.
DR PharmGKB; PA37765; -.
DR VEuPathDB; HostDB:ENSG00000159840; -.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000154273; -.
DR HOGENOM; CLU_001357_10_2_1; -.
DR InParanoid; Q15942; -.
DR OMA; NKPFMVT; -.
DR OrthoDB; 642235at2759; -.
DR PhylomeDB; Q15942; -.
DR TreeFam; TF320310; -.
DR PathwayCommons; Q15942; -.
DR SignaLink; Q15942; -.
DR SIGNOR; Q15942; -.
DR BioGRID-ORCS; 7791; 24 hits in 1083 CRISPR screens.
DR ChiTaRS; ZYX; human.
DR GeneWiki; Zyxin; -.
DR GenomeRNAi; 7791; -.
DR Pharos; Q15942; Tbio.
DR PRO; PR:Q15942; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q15942; protein.
DR Bgee; ENSG00000159840; Expressed in body of uterus and 96 other tissues.
DR ExpressionAtlas; Q15942; baseline and differential.
DR Genevisible; Q15942; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0007160; P:cell-matrix adhesion; IC:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell adhesion; Cell junction; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Host-virus interaction;
KW LIM domain; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330"
FT CHAIN 2..572
FT /note="Zyxin"
FT /id="PRO_0000075913"
FT DOMAIN 384..443
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 444..503
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 504..570
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 23..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..139
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..269
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62523"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 179
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 253
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q62523"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 265
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q62523"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 270
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q62523"
FT MOD_RES 274
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 279
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..157
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057288"
FT VARIANT 223
FT /note="H -> L (in dbSNP:rs11978404)"
FT /id="VAR_034081"
FT MUTAGEN 71
FT /note="F->A: Reduced interaction with ENAH and VASP."
FT /evidence="ECO:0000269|PubMed:10801818"
FT MUTAGEN 93
FT /note="F->A: Reduced interaction with ENAH and VASP."
FT /evidence="ECO:0000269|PubMed:10801818"
FT MUTAGEN 104
FT /note="F->A: Greatly reduced interaction with ENAH and
FT VASP; when associated with A-71 or with A-71 and A-93."
FT /evidence="ECO:0000269|PubMed:10801818"
FT MUTAGEN 114
FT /note="F->A: No targeting to focal adhesions and reduced
FT actin-rich structures; when associated with A-71; A-93 and
FT A-104."
FT /evidence="ECO:0000269|PubMed:10801818"
SQ SEQUENCE 572 AA; 61277 MW; 2833B1EFA260B762 CRC64;
MAAPRPSPAI SVSVSAPAFY APQKKFGPVV APKPKVNPFR PGDSEPPPAP GAQRAQMGRV
GEIPPPPPED FPLPPPPLAG DGDDAEGALG GAFPPPPPPI EESFPPAPLE EEIFPSPPPP
PEEEGGPEAP IPPPPQPREK VSSIDLEIDS LSSLLDDMTK NDPFKARVSS GYVPPPVATP
FSSKSSTKPA AGGTAPLPPW KSPSSSQPLP QVPAPAQSQT QFHVQPQPQP KPQVQLHVQS
QTQPVSLANT QPRGPPASSP APAPKFSPVT PKFTPVASKF SPGAPGGSGS QPNQKLGHPE
ALSAGTGSPQ PPSFTYAQQR EKPRVQEKQH PVPPPAQNQN QVRSPGAPGP LTLKEVEELE
QLTQQLMQDM EHPQRQNVAV NELCGRCHQP LARAQPAVRA LGQLFHIACF TCHQCAQQLQ
GQQFYSLEGA PYCEGCYTDT LEKCNTCGEP ITDRMLRATG KAYHPHCFTC VVCARPLEGT
SFIVDQANRP HCVPDYHKQY APRCSVCSEP IMPEPGRDET VRVVALDKNF HMKCYKCEDC
GKPLSIEADD NGCFPLDGHV LCRKCHTARA QT
