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Q15942 (ZYX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zyxin
Alternative name(s):
Zyxin-2
Gene names
Name:ZYX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Cytoplasmcytoskeleton. Nucleus. Cell junctionfocal 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 processCell adhesion
Host-virus interaction
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityPolymorphism
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Traceable author statement Ref.1. Source: ProtInc

cell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell-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 component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement Ref.1. Source: ProtInc

stress fiber

Inferred from direct assay Ref.15. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10831611PubMed 22665060PubMed 23840749. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 572571Zyxin
PRO_0000075913

Regions

Domain384 – 44360LIM zinc-binding 1
Domain444 – 50360LIM zinc-binding 2
Domain504 – 57067LIM zinc-binding 3
Compositional bias64 – 7714Pro-rich
Compositional bias94 – 10815Pro-rich
Compositional bias115 – 1217Pro-rich
Compositional bias127 – 13711Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.19
Modified residue1431Phosphoserine By similarity
Modified residue1691Phosphoserine Ref.18 Ref.22
Modified residue1791Phosphothreonine Ref.22
Modified residue2591Phosphoserine Ref.12 Ref.18 Ref.22
Modified residue2651N6-acetyllysine By similarity
Modified residue2671Phosphoserine Ref.17 Ref.18 Ref.24
Modified residue2701Phosphothreonine Ref.18 Ref.24
Modified residue2721N6-acetyllysine By similarity
Modified residue2741Phosphothreonine Ref.18 Ref.22
Modified residue2791N6-acetyllysine Ref.21
Modified residue2811Phosphoserine Ref.12 Ref.17 Ref.18 Ref.22 Ref.24
Modified residue2881Phosphoserine Ref.18
Modified residue3081Phosphoserine Ref.18 Ref.22
Modified residue3441Phosphoserine Ref.11 Ref.17 Ref.18 Ref.22 Ref.24

Natural variations

Natural variant2231H → L.
Corresponds to variant rs11978404 [ dbSNP | Ensembl ].
VAR_034081

Experimental info

Mutagenesis711F → A: Reduced interaction with ENAH and VASP. Ref.8
Mutagenesis931F → A: Reduced interaction with ENAH and VASP. Ref.8
Mutagenesis1041F → A: Greatly reduced interaction with ENAH and VASP; when associated with A-71 or with A-71 and A-93. Ref.8
Mutagenesis1141F → 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 LengthMass (Da)Tools
Q15942 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 2833B1EFA260B762

FASTA57261,277
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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.
[21]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"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].
[24]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
CCDSCCDS5883.1.
PIRG02845.
RefSeqNP_001010972.1. NM_001010972.1.
NP_003452.1. NM_003461.4.
UniGeneHs.490415.

3D structure databases

ProteinModelPortalQ15942.
SMRQ15942. Positions 383-564.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113569. 62 interactions.
IntActQ15942. 40 interactions.
MINTMINT-220515.
STRING9606.ENSP00000324422.

PTM databases

PhosphoSiteQ15942.

Polymorphism databases

DMDM2497677.

2D gel databases

OGPQ15942.

Proteomic databases

MaxQBQ15942.
PaxDbQ15942.
PRIDEQ15942.

Protocols and materials databases

DNASU7791.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322764; ENSP00000324422; ENSG00000159840.
GeneID7791.
KEGGhsa:7791.
UCSCuc003wcw.3. human.

Organism-specific databases

CTD7791.
GeneCardsGC07P143078.
HGNCHGNC:13200. ZYX.
HPACAB009321.
HPA004835.
MIM602002. gene.
neXtProtNX_Q15942.
PharmGKBPA37765.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279196.
HOGENOMHOG000220910.
HOVERGENHBG093602.
InParanoidQ15942.
KOK06273.
OMAAPQKKFG.
OrthoDBEOG7992Q6.
PhylomeDBQ15942.
TreeFamTF320310.

Gene expression databases

ArrayExpressQ15942.
BgeeQ15942.
CleanExHS_ZYX.
GenevestigatorQ15942.

Family and domain databases

Gene3D2.10.110.10. 3 hits.
InterProIPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 3 hits.
[Graphical view]
SMARTSM00132. LIM. 3 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZYX. human.
GeneWikiZyxin.
GenomeRNAi7791.
NextBio30155.
PMAP-CutDBQ15942.
PROQ15942.
SOURCESearch...

Entry information

Entry nameZYX_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM