Q62523

SS
Gene name
Zyx
Protein name
Zyxin
Names
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:22793
EC number
Protein Class

Descriptions

Zyxin is a LIM protein found prominently at sites of cell adhesion, faintly in leading lamellipodia, and transiently in cell nuclei. Zyxin displays an N-terminal proline-rich region and three C-terminal LIM domains that provide binding sites for several proteins associated with actin polymerization and intracellular signaling. The head-tail interaction of proline-rich region and LIM domains maintains zyxin in a closed conformation that limits access to binding partners.

Autoinhibitory domains (AIDs)

61-338 (Proline-rich region) SS

Target domain

376-562 (LIM domains)

Relief mechanism

PTM

Assay

376-562 (LIM domains) SS

Target domain

61-338 (Proline-rich region)

Relief mechanism

PTM

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q62523

Entry ID Method Resolution Chain Position Source
AF-Q62523-F1 Predicted AlphaFoldDB

17 variants for Q62523

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388821784 43 D>N No EVA
rs3388822255 50 A>T No EVA
rs3388812662 54 R>K No EVA
rs3388810063 70 D>V No EVA
rs3388827269 78 L>I No EVA
rs240964179 267 V>L No EVA
rs3388818805 284 N>I No EVA
rs223465370 297 S>G No EVA
rs3388824849 302 Q>E No EVA
rs3388805130 304 P>S No EVA
rs3388826067 350 E>K No EVA
rs3388805210 351 L>W No EVA
rs3388827586 376 C>Y No EVA
rs3388824770 394 G>* No EVA
rs3388810090 439 C>S No EVA
rs3388826050 467 C>Y No EVA
rs3388827349 508 G>R No EVA

No associated diseases with Q62523

3 regional properties for Q62523

Type Name Position InterPro Accession
domain Zinc finger, LIM-type 374 - 435 IPR001781-1
domain Zinc finger, LIM-type 435 - 493 IPR001781-2
domain Zinc finger, LIM-type 494 - 564 IPR001781-3

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • Cytoplasm, cytoskeleton
  • Cell junction, focal adhesion
  • Nucleus
  • Associates with the actin cytoskeleton near the adhesion plaques
  • Enters the nucleus in the presence of HESX1 (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 GO annotations of cellular component

Name Definition
adherens junction A cell-cell junction composed of the epithelial cadherin-catenin complex. The epithelial cadherins, or E-cadherins, of each interacting cell extend through the plasma membrane into the extracellular space and bind to each other. The E-cadherins bind to catenins on the cytoplasmic side of the membrane, where the E-cadherin-catenin complex binds to cytoskeletal components and regulatory and signaling molecules.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
focal adhesion A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ).
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
phagocytic vesicle A membrane-bounded intracellular vesicle that arises from the ingestion of particulate material by phagocytosis.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
stress fiber A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber.

1 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.

5 GO annotations of biological process

Name Definition
cell-matrix adhesion The binding of a cell to the extracellular matrix via adhesion molecules.
cellular response to type II interferon Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an interferon-gamma stimulus. Interferon gamma is the only member of the type II interferon found so far.
integrin-mediated signaling pathway The series of molecular signals initiated by an extracellular ligand binding to an integrin on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription.
stress fiber assembly The aggregation, arrangement and bonding together of a set of components to form a stress fiber. A stress fiber is a contractile actin filament bundle that consists of short actin filaments with alternating polarity.
transforming growth factor beta receptor signaling pathway The series of molecular signals initiated by an extracellular ligand binding to a transforming growth factor beta receptor on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q04584 ZYX Zyxin Gallus gallus (Chicken) EV
Q15942 ZYX Zyxin Homo sapiens (Human) EV
Q8BFW7 Lpp Lipoma-preferred partner homolog Mus musculus (Mouse) PR
Q5XI07 Lpp Lipoma-preferred partner homolog Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MAAPRPPPAI SVSVSAPAFY APQKKFAPVV APKPKVNPFR PGDSEPPVAA GAQRAQMGRV
70 80 90 100 110 120
GEIPPPPPED FPLPPPPLIG EGDDSEGALG GAFPPPPPPM IEEPFPPAPL EEDIFPSPPP
130 140 150 160 170 180
PLEEEGGPEA PTQLPPQPRE KVCSIDLEID SLSSLLDDMT KNDPFKARVS SGYVPPPVAT
190 200 210 220 230 240
PFVPKPSTKP APGGTAPLPP WKTPSSSQPP PQPQAKPQVQ LHVQPQAKPH VQPQPVSSAN
250 260 270 280 290 300
TQPRGPLSQA PTPAPKFAPV APKFTPVVSK FSPGAPSGPG PQPNQKMVPP DAPSSVSTGS
310 320 330 340 350 360
PQPPSFTYAQ QKEKPLVQEK QHPQPPPAQN QNQVRSPGGP GPLTLKEVEE LEQLTQQLMQ
370 380 390 400 410 420
DMEHPQRQSV AVNESCGKCN QPLARAQPAV RALGQLFHIT CFTCHQCQQQ LQGQQFYSLE
430 440 450 460 470 480
GAPYCEGCYT DTLEKCNTCG QPITDRMLRA TGKAYHPQCF TCVVCACPLE GTSFIVDQAN
490 500 510 520 530 540
QPHCVPDYHK QYAPRCSVCS EPIMPEPGRD ETVRVVALDK NFHMKCYKCE DCGKPLSIEA
550 560
DDNGCFPLDG HVLCRKCHSA RAQT