Misplaced Pages

Zyxin

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
(Redirected from ZYX (gene))

Protein-coding gene in the species Homo sapiens
ZYX
Identifiers
AliasesZYX, ESP-2, HED-2, zyxin
External IDsOMIM: 602002; MGI: 103072; HomoloGene: 31164; GeneCards: ZYX; OMA:ZYX - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)
Chromosome 7 (human)Genomic location for ZYXGenomic location for ZYX
Band7q34Start143,381,295 bp
End143,391,111 bp
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)
Chromosome 6 (mouse)Genomic location for ZYXGenomic location for ZYX
Band6|6 B2.1Start42,326,564 bp
End42,337,147 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • body of uterus

  • myometrium

  • left uterine tube

  • granulocyte

  • blood

  • stromal cell of endometrium

  • thoracic aorta

  • right coronary artery

  • ascending aorta

  • smooth muscle tissue
Top expressed in
  • granulocyte

  • tail of embryo

  • ascending aorta

  • tibiofemoral joint

  • blood

  • aortic valve

  • tunica media of zone of aorta

  • internal carotid artery

  • external carotid artery

  • lip
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7791

22793

Ensembl

ENSG00000159840
ENSG00000285443

ENSMUSG00000029860

UniProt

Q15942

Q62523

RefSeq (mRNA)

NM_001010972
NM_003461
NM_001362783

NM_001289617
NM_001289618
NM_001289619
NM_011777

RefSeq (protein)

NP_001010972
NP_003452
NP_001349712

NP_001276546
NP_001276547
NP_001276548
NP_035907

Location (UCSC)Chr 7: 143.38 – 143.39 MbChr 6: 42.33 – 42.34 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Zyxin is a protein that in humans is encoded by the ZYX gene.

Function

Focal adhesions are actin-rich structures that enable cells to adhere to the extracellular matrix and at which protein complexes involved in signal transduction assemble. Zyxin is a zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three LIM domains in its C-terminal half. The proline-rich domain may interact with SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein binding. Zyxin may function as a messenger in the signal transduction pathway that mediates adhesion-stimulated changes in gene expression and may modulate the cytoskeletal organization of actin bundles. Alternative splicing results in multiple transcript variants that encode the same isoform.

Interactions

Zyxin has been shown to interact with:

References

  1. ^ ENSG00000285443 GRCh38: Ensembl release 89: ENSG00000159840, ENSG00000285443Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000029860Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Zumbrunn J, Trueb B (January 1997). "A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts". Eur J Biochem. 241 (2): 657–63. doi:10.1111/j.1432-1033.1996.00657.x. PMID 8917469.
  6. Macalma T, Otte J, Hensler ME, Bockholt SM, Louis HA, Kalff-Suske M, Grzeschik KH, von der Ahe D, Beckerle MC (January 1997). "Molecular characterization of human zyxin". J Biol Chem. 271 (49): 31470–8. doi:10.1074/jbc.271.49.31470. PMID 8940160.
  7. ^ "Entrez Gene: ZYX zyxin".
  8. Reinhard M, Zumbrunn J, Jaquemar D, Kuhn M, Walter U, Trueb B (May 1999). "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol. Chem. 274 (19): 13410–8. doi:10.1074/jbc.274.19.13410. PMID 10224105.
  9. Li B, Trueb B (September 2001). "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328–35. doi:10.1074/jbc.M100789200. PMID 11423549.
  10. Tani K, Sato S, Sukezane T, Kojima H, Hirose H, Hanafusa H, Shishido T (June 2003). "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase". J. Biol. Chem. 278 (24): 21685–92. doi:10.1074/jbc.M301447200. PMID 12672821.
  11. ^ Drees B, Friederich E, Fradelizi J, Louvard D, Beckerle MC, Golsteyn RM (July 2000). "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. 275 (29): 22503–11. doi:10.1074/jbc.M001698200. PMID 10801818.
  12. Li B, Zhuang L, Trueb B (May 2004). "Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1". J. Biol. Chem. 279 (19): 20401–10. doi:10.1074/jbc.M310304200. PMID 15004028.
  13. Hirota T, Morisaki T, Nishiyama Y, Marumoto T, Tada K, Hara T, Masuko N, Inagaki M, Hatakeyama K, Saya H (May 2000). "Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts/LATS1 tumor suppressor". J. Cell Biol. 149 (5): 1073–86. doi:10.1083/jcb.149.5.1073. PMC 2174824. PMID 10831611.
  14. Harbeck B, Hüttelmaier S, Schluter K, Jockusch BM, Illenberger S (October 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. PMID 10882740.

Further reading

External links

Categories: