Q15942 (ZYX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Zyxin

Alternative name(s):
Zyxin-2

Gene names

Name:

ZYX

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	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). Ref.8 Ref.9 Ref.10 Ref.14
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. Ref.10 Ref.15
Sequence similarities	Belongs to the zyxin/ajuba family. Contains 3 LIM zinc-binding domains.

Ontologies

Keywords
Biological process	Cell adhesion Host-virus interaction
Cellular component	Cell junction Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Polymorphism
Domain	LIM domain Repeat
Ligand	Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Traceable author statement Ref.1. Source: ProtInc cell-cell signaling Traceable author statement Ref.1. Source: ProtInc signal transduction Traceable author statement Ref.1. Source: ProtInc virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell-cell adherens junction Inferred from direct assay Ref.1. Source: MGI cytoplasm Inferred from direct assay. Source: HPA focal adhesion Inferred from direct assay Ref.15. Source: UniProtKB integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell stress fiber Inferred from direct assay Ref.15. Source: UniProtKB
Molecular_function	zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LATS1	O95835	10	EBI-444225,EBI-444209

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 572	571	Zyxin		PRO_0000075913
Regions
	Domain	384 – 443	60	LIM zinc-binding 1
	Domain	444 – 503	60	LIM zinc-binding 2
	Domain	504 – 570	67	LIM zinc-binding 3
	Compositional bias	64 – 77	14	Pro-rich
	Compositional bias	94 – 108	15	Pro-rich
	Compositional bias	115 – 121	7	Pro-rich
	Compositional bias	127 – 137	11	Pro-rich
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7
	Modified residue	143	1	Phosphoserine By similarity
	Modified residue	159	1	Phosphothreonine By similarity
	Modified residue	169	1	Phosphoserine Ref.18 Ref.21
	Modified residue	179	1	Phosphothreonine Ref.21
	Modified residue	259	1	Phosphoserine Ref.12 Ref.18 Ref.21
	Modified residue	267	1	Phosphoserine Ref.17 Ref.18 Ref.23
	Modified residue	270	1	Phosphothreonine Ref.18 Ref.23
	Modified residue	274	1	Phosphothreonine Ref.18 Ref.21
	Modified residue	279	1	N6-acetyllysine Ref.20
	Modified residue	281	1	Phosphoserine Ref.12 Ref.17 Ref.18 Ref.21 Ref.23
	Modified residue	288	1	Phosphoserine Ref.18
	Modified residue	308	1	Phosphoserine Ref.18 Ref.21
	Modified residue	344	1	Phosphoserine Ref.11 Ref.17 Ref.18 Ref.21 Ref.23
Natural variations
	Natural variant	223	1	H → L. Corresponds to variant rs11978404 [ dbSNP | Ensembl ].		VAR_034081
Experimental info
	Mutagenesis	71	1	F → A: Reduced interaction with ENAH and VASP. Ref.8
	Mutagenesis	93	1	F → A: Reduced interaction with ENAH and VASP. Ref.8
	Mutagenesis	104	1	F → A: Greatly reduced interaction with ENAH and VASP; when associated with A-71 or with A-71 and A-93. Ref.8
	Mutagenesis	114	1	F → A: No targeting to focal adhesions and reduced actin-rich structures; when associated with A-71; A-93 and A-104. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Q15942 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 2833B1EFA260B762	FASTA	572	61,277
	10 20 30 40 50 60 MAAPRPSPAI SVSVSAPAFY APQKKFGPVV APKPKVNPFR PGDSEPPPAP GAQRAQMGRV 70 80 90 100 110 120 GEIPPPPPED FPLPPPPLAG DGDDAEGALG GAFPPPPPPI EESFPPAPLE EEIFPSPPPP 130 140 150 160 170 180 PEEEGGPEAP IPPPPQPREK VSSIDLEIDS LSSLLDDMTK NDPFKARVSS GYVPPPVATP 190 200 210 220 230 240 FSSKSSTKPA AGGTAPLPPW KSPSSSQPLP QVPAPAQSQT QFHVQPQPQP KPQVQLHVQS 250 260 270 280 290 300 QTQPVSLANT QPRGPPASSP APAPKFSPVT PKFTPVASKF SPGAPGGSGS QPNQKLGHPE 310 320 330 340 350 360 ALSAGTGSPQ PPSFTYAQQR EKPRVQEKQH PVPPPAQNQN QVRSPGAPGP LTLKEVEELE 370 380 390 400 410 420 QLTQQLMQDM EHPQRQNVAV NELCGRCHQP LARAQPAVRA LGQLFHIACF TCHQCAQQLQ 430 440 450 460 470 480 GQQFYSLEGA PYCEGCYTDT LEKCNTCGEP ITDRMLRATG KAYHPHCFTC VVCARPLEGT 490 500 510 520 530 540 SFIVDQANRP HCVPDYHKQY APRCSVCSEP IMPEPGRDET VRVVALDKNF HMKCYKCEDC 550 560 570 GKPLSIEADD NGCFPLDGHV LCRKCHTARA QT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of human zyxin." 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. J. Biol. Chem. 271:31470-31478(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Umbilical vein.
[2]	"A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts." Zumbrunn J., Trueb B. Eur. J. Biochem. 241:657-663(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence of human chromosome 7." 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. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Human chromosome 7: DNA sequence and biology." 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. Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney, Skin and Uterus.
[7]	Bienvenut W.V., Calvo F. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-25; 36-54; 168-184; 280-320 AND 325-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins." Drees B., Friederich E., Fradelizi J., Louvard D., Beckerle M.C., Golsteyn R.M. J. Biol. Chem. 275:22503-22511(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ENAH AND VASP, MUTAGENESIS OF PHE-71; PHE-93; PHE-104 AND PHE-114.
[9]	"Interaction of zyxin, a focal adhesion protein, with the E6 protein from human papillomavirus type 6 results in its nuclear translocation." Degenhardt Y.Y., Silverstein S. J. Virol. 75:11791-11802(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HPV6 E6.
[10]	"The conformational state of Tes regulates its zyxin-dependent recruitment to focal adhesions." Garvalov B.K., Higgins T.E., Sutherland J.D., Zettl M., Scaplehorn N., Koecher T., Piddini E., Griffiths G., Way M. J. Cell Biol. 161:33-39(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TES.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-281, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding." Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J., McDonald N.Q., Way M. Mol. Cell 28:1071-1082(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EVL; VASP AND ENAH.
[15]	"The LIM-domain protein zyxin binds the homeodomain factor Xanf1/Hesx1 and modulates its activity in the anterior neural plate of Xenopus laevis embryo." Martynova N.Y., Eroshkin F.M., Ermolina L.V., Ermakova G.V., Korotaeva A.L., Smurova K.M., Gyoeva F.K., Zaraisky A.G. Dev. Dyn. 237:736-749(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[16]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[17]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; SER-281 AND SER-344, MASS SPECTROMETRY. Tissue: Platelet.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-259; SER-267; THR-270; THR-274; SER-281; SER-288; SER-308 AND SER-344, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[20]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-279, MASS SPECTROMETRY.
[21]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-179; SER-259; THR-274; SER-281; SER-308 AND SER-344, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267; THR-270; SER-281 AND SER-344, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X94991 mRNA. Translation: CAA64447.1. X95735 mRNA. Translation: CAA65050.1. CR457431 mRNA. Translation: CAG33712.1. AC092214 Genomic DNA. Translation: AAS07459.1. CH236959 Genomic DNA. Translation: EAL23788.1. BC008743 mRNA. Translation: AAH08743.1. BC009360 mRNA. Translation: AAH09360.1. BC010031 mRNA. Translation: AAH10031.1.
IPI	IPI00926625.
PIR	G02845.
RefSeq	NP_001010972.1. NM_001010972.1. NP_003452.1. NM_003461.4.
UniGene	Hs.490415.
3D structure databases
ProteinModelPortal	Q15942.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15942. 34 interactions.
MINT	MINT-220515.
STRING	9606.ENSP00000324422.
PTM databases
PhosphoSite	Q15942.
Polymorphism databases
DMDM	2497677.
2D gel databases
OGP	Q15942.
Proteomic databases
PaxDb	Q15942.
PRIDE	Q15942.
Protocols and materials databases
DNASU	7791.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000322764; ENSP00000324422; ENSG00000159840.
GeneID	7791.
KEGG	hsa:7791.
UCSC	uc003wcw.3. human.
Organism-specific databases
CTD	7791.
GeneCards	GC07P143078.
HGNC	HGNC:13200. ZYX.
HPA	CAB009321. HPA004835.
MIM	602002. gene.
neXtProt	NX_Q15942.
PharmGKB	PA37765.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG279196.
HOGENOM	HOG000220910.
HOVERGEN	HBG093602.
InParanoid	Q15942.
KO	K06273.
OMA	DNGCFPL.
OrthoDB	EOG4MSCZN.
Gene expression databases
ArrayExpress	Q15942.
Bgee	Q15942.
CleanEx	HS_ZYX.
Genevestigator	Q15942.
GermOnline	ENSG00000159840. Homo sapiens.
Family and domain databases
Gene3D	2.10.110.10. 3 hits.
InterPro	IPR001781. Znf_LIM. [Graphical view]
Pfam	PF00412. LIM. 3 hits. [Graphical view]
SMART	SM00132. LIM. 3 hits. [Graphical view]
PROSITE	PS00478. LIM_DOMAIN_1. 2 hits. PS50023. LIM_DOMAIN_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ZYX. human.
GenomeRNAi	7791.
NextBio	30155.
PMAP-CutDB	Q15942.
SOURCE	Search...

Entry information

Entry name

ZYX_HUMAN

Accession

Primary (citable) accession number: Q15942
Secondary accession number(s): A4D2G6, Q6I9S4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 130 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.