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Zyxin (Zyxin-2)

 ZYX_HUMAN               Reviewed;         572 AA.
Q15942; A4D2G6; B4DQX7; Q6I9S4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
23-MAY-2018, entry version 179.
RecName: Full=Zyxin;
AltName: Full=Zyxin-2;
Name=ZYX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Umbilical vein;
PubMed=8940160; DOI=10.1074/jbc.271.49.31470;
Macalma T., Otte J., Hensler M.E., Bockholt S.M., Louis H.A.,
Kalff-Suske M., Grzeschik K.H., von der Ahe D., Beckerle M.C.;
"Molecular characterization of human zyxin.";
J. Biol. Chem. 271:31470-31478(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8917469; DOI=10.1111/j.1432-1033.1996.00657.x;
Zumbrunn J., Trueb B.;
"A zyxin-related protein whose synthesis is reduced in virally
transformed fibroblasts.";
Eur. J. Biochem. 241:657-663(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney, Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 2-25; 36-54; 168-184; 280-320 AND 325-375,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V., Calvo F.;
Submitted (FEB-2008) to UniProtKB.
[10]
INTERACTION WITH ENAH AND VASP, AND MUTAGENESIS OF PHE-71; PHE-93;
PHE-104 AND PHE-114.
PubMed=10801818; DOI=10.1074/jbc.M001698200;
Drees B., Friederich E., Fradelizi J., Louvard D., Beckerle M.C.,
Golsteyn R.M.;
"Characterization of the interaction between zyxin and members of the
Ena/vasodilator-stimulated phosphoprotein family of proteins.";
J. Biol. Chem. 275:22503-22511(2000).
[11]
INTERACTION WITH HPV6 E6.
PubMed=11689660; DOI=10.1128/JVI.75.23.11791-11802.2001;
Degenhardt Y.Y., Silverstein S.;
"Interaction of zyxin, a focal adhesion protein, with the E6 protein
from human papillomavirus type 6 results in its nuclear
translocation.";
J. Virol. 75:11791-11802(2001).
[12]
SUBCELLULAR LOCATION, AND INTERACTION WITH TES.
PubMed=12695497; DOI=10.1083/jcb.200211015;
Garvalov B.K., Higgins T.E., Sutherland J.D., Zettl M., Scaplehorn N.,
Koecher T., Piddini E., Griffiths G., Way M.;
"The conformational state of Tes regulates its zyxin-dependent
recruitment to focal adhesions.";
J. Cell Biol. 161:33-39(2003).
[13]
INTERACTION WITH SYNPO2.
PubMed=16885336; DOI=10.1158/0008-5472.CAN-06-0227;
Yu Y.P., Luo J.H.;
"Myopodin-mediated suppression of prostate cancer cell migration
involves interaction with zyxin.";
Cancer Res. 66:7414-7419(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-281, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[17]
INTERACTION WITH EVL; VASP AND ENAH.
PubMed=18158903; DOI=10.1016/j.molcel.2007.10.033;
Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J.,
McDonald N.Q., Way M.;
"Tes, a specific Mena interacting partner, breaks the rules for EVH1
binding.";
Mol. Cell 28:1071-1082(2007).
[18]
SUBCELLULAR LOCATION.
PubMed=18297730; DOI=10.1002/dvdy.21471;
Martynova N.Y., Eroshkin F.M., Ermolina L.V., Ermakova G.V.,
Korotaeva A.L., Smurova K.M., Gyoeva F.K., Zaraisky A.G.;
"The LIM-domain protein zyxin binds the homeodomain factor Xanf1/Hesx1
and modulates its activity in the anterior neural plate of Xenopus
laevis embryo.";
Dev. Dyn. 237:736-749(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; SER-281 AND
SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-259; SER-267;
THR-270; THR-274; SER-281; SER-288; SER-308 AND SER-344, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-279, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-179; SER-259;
THR-274; SER-281; SER-308 AND SER-344, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; THR-270; SER-281
AND SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-170; SER-259;
SER-267; THR-270; SER-281; SER-308 AND SER-344, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-142; SER-259;
SER-267; SER-281 AND SER-344, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[32]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Adhesion plaque protein. Binds alpha-actinin and the CRP
protein. Important for targeting TES and ENA/VASP family members
to focal adhesions and for the formation of actin-rich structures.
May be a component of a signal transduction pathway that mediates
adhesion-stimulated changes in gene expression (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts with HPV type 6 protein E6. Does not interact
significantly with E6 proteins from HPV types 11, 16, or 18.
Interacts, via the Pro-rich regions, with the EVH1 domains of
ENAH, EVL and VASP. Interacts with the first LIM domain of TES.
Interacts with NEBL (isoform 2). Interacts with SYNPO2.
{ECO:0000269|PubMed:10801818, ECO:0000269|PubMed:11689660,
ECO:0000269|PubMed:12695497, ECO:0000269|PubMed:16885336,
ECO:0000269|PubMed:18158903}.
-!- INTERACTION:
B2R9Y1:-; NbExp=3; IntAct=EBI-444225, EBI-10175746;
Q9UI08-2:EVL; NbExp=4; IntAct=EBI-444225, EBI-6448852;
Q9NV31:IMP3; NbExp=5; IntAct=EBI-444225, EBI-747481;
Q14847:LASP1; NbExp=5; IntAct=EBI-444225, EBI-742828;
O95835:LATS1; NbExp=10; IntAct=EBI-444225, EBI-444209;
O14910:LIN7A; NbExp=3; IntAct=EBI-444225, EBI-2513988;
A0A0S2Z4M0:NME5; NbExp=4; IntAct=EBI-444225, EBI-16430544;
P35372:OPRM1; NbExp=2; IntAct=EBI-444225, EBI-2624570;
Q96HC4:PDLIM5; NbExp=3; IntAct=EBI-444225, EBI-751267;
Q96BD5:PHF21A; NbExp=3; IntAct=EBI-444225, EBI-745085;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Nucleus.
Cell junction, focal adhesion. Note=Associates with the actin
cytoskeleton near the adhesion plaques. Enters the nucleus in the
presence of HESX1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15942-1; Sequence=Displayed;
Name=2;
IsoId=Q15942-2; Sequence=VSP_057288;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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EMBL; X94991; CAA64447.1; -; mRNA.
EMBL; X95735; CAA65050.1; -; mRNA.
EMBL; AK299005; BAG61089.1; -; mRNA.
EMBL; AK316227; BAH14598.1; -; mRNA.
EMBL; CR457431; CAG33712.1; -; mRNA.
EMBL; AC092214; AAS07459.1; -; Genomic_DNA.
EMBL; CH236959; EAL23788.1; -; Genomic_DNA.
EMBL; CH471198; EAW51848.1; -; Genomic_DNA.
EMBL; BC008743; AAH08743.1; -; mRNA.
EMBL; BC009360; AAH09360.1; -; mRNA.
EMBL; BC010031; AAH10031.1; -; mRNA.
CCDS; CCDS5883.1; -. [Q15942-1]
PIR; G02845; G02845.
RefSeq; NP_001010972.1; NM_001010972.1. [Q15942-1]
RefSeq; NP_003452.1; NM_003461.4. [Q15942-1]
UniGene; Hs.490415; -.
ProteinModelPortal; Q15942; -.
SMR; Q15942; -.
BioGrid; 113569; 113.
IntAct; Q15942; 68.
MINT; Q15942; -.
STRING; 9606.ENSP00000324422; -.
iPTMnet; Q15942; -.
PhosphoSitePlus; Q15942; -.
SwissPalm; Q15942; -.
BioMuta; ZYX; -.
DMDM; 2497677; -.
OGP; Q15942; -.
EPD; Q15942; -.
MaxQB; Q15942; -.
PaxDb; Q15942; -.
PeptideAtlas; Q15942; -.
PRIDE; Q15942; -.
DNASU; 7791; -.
Ensembl; ENST00000322764; ENSP00000324422; ENSG00000159840. [Q15942-1]
Ensembl; ENST00000392910; ENSP00000376642; ENSG00000159840. [Q15942-2]
GeneID; 7791; -.
KEGG; hsa:7791; -.
UCSC; uc003wcx.5; human. [Q15942-1]
CTD; 7791; -.
DisGeNET; 7791; -.
EuPathDB; HostDB:ENSG00000159840.15; -.
GeneCards; ZYX; -.
HGNC; HGNC:13200; ZYX.
HPA; CAB009321; -.
HPA; CAB075747; -.
HPA; HPA004835; -.
HPA; HPA073497; -.
MIM; 602002; gene.
neXtProt; NX_Q15942; -.
OpenTargets; ENSG00000159840; -.
PharmGKB; PA37765; -.
eggNOG; KOG1701; Eukaryota.
eggNOG; ENOG410Y3GP; LUCA.
GeneTree; ENSGT00760000119039; -.
HOGENOM; HOG000220910; -.
HOVERGEN; HBG093602; -.
InParanoid; Q15942; -.
KO; K06273; -.
OMA; EADENGC; -.
OrthoDB; EOG091G085F; -.
PhylomeDB; Q15942; -.
TreeFam; TF320310; -.
SIGNOR; Q15942; -.
ChiTaRS; ZYX; human.
GeneWiki; Zyxin; -.
GenomeRNAi; 7791; -.
PMAP-CutDB; Q15942; -.
PRO; PR:Q15942; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000159840; -.
CleanEx; HS_ZYX; -.
ExpressionAtlas; Q15942; baseline and differential.
Genevisible; Q15942; HS.
GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0007160; P:cell-matrix adhesion; IC:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0043149; P:stress fiber assembly; IMP:UniProtKB.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR001781; Znf_LIM.
Pfam; PF00412; LIM; 3.
SMART; SM00132; LIM; 3.
PROSITE; PS00478; LIM_DOMAIN_1; 2.
PROSITE; PS50023; LIM_DOMAIN_2; 3.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell adhesion; Cell junction;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
Host-virus interaction; LIM domain; Metal-binding; Methylation;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Zinc.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.9}.
CHAIN 2 572 Zyxin.
/FTId=PRO_0000075913.
DOMAIN 384 443 LIM zinc-binding 1. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 444 503 LIM zinc-binding 2. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
DOMAIN 504 570 LIM zinc-binding 3. {ECO:0000255|PROSITE-
ProRule:PRU00125}.
COMPBIAS 64 77 Pro-rich.
COMPBIAS 94 108 Pro-rich.
COMPBIAS 115 121 Pro-rich.
COMPBIAS 127 137 Pro-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.9}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 142 142 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000250|UniProtKB:Q62523}.
MOD_RES 169 169 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 179 179 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 253 253 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q62523}.
MOD_RES 259 259 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 265 265 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q62523}.
MOD_RES 267 267 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 270 270 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 272 272 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q62523}.
MOD_RES 274 274 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 279 279 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 281 281 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 288 288 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 308 308 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 157 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057288.
VARIANT 223 223 H -> L (in dbSNP:rs11978404).
/FTId=VAR_034081.
MUTAGEN 71 71 F->A: Reduced interaction with ENAH and
VASP. {ECO:0000269|PubMed:10801818}.
MUTAGEN 93 93 F->A: Reduced interaction with ENAH and
VASP. {ECO:0000269|PubMed:10801818}.
MUTAGEN 104 104 F->A: Greatly reduced interaction with
ENAH and VASP; when associated with A-71
or with A-71 and A-93.
{ECO:0000269|PubMed:10801818}.
MUTAGEN 114 114 F->A: No targeting to focal adhesions and
reduced actin-rich structures; when
associated with A-71; A-93 and A-104.
{ECO:0000269|PubMed:10801818}.
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


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