Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Zyxin  

UniProtKB / Swiss-Prot ID :  ZYX_MOUSE

Gene Name (Synonyms) : 
Zyx  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm (By similarity). Cytoplasm, cytoskeleton (By similarity). Cell junction, focal adhesion (By similarity). Nucleus (By similarity). Note=Associates with the actin cytoskeleton near the adhesion plaques. Enters the nucleus in the presence of HESX1 

Protein 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). 

Protein Sequence MAAPRPPPAISVSVSAPAFYAPQKKFAPVVAPKPKVNPFRPGDSEPPVAAGAQRAQMGRVGEIPPPPPED...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
144PhosphoserineEKVCSIDLE
CCCCCCCCC
23.33PhosphoELM
Link-
144Phosphoserine.EKVCSIDLE
CCCCCCCCC
23.33UniProtKB
Link-
160PhosphothreonineLDDMTKNDP
CCCCCCCCC
33.42PhosphoELM
Link-
160Phosphothreonine.LDDMTKNDP
CCCCCCCCC
33.42UniProtKB
Link-
336PhosphoserineNQVRSPGGP
CCCCCCCCC
29.10PhosphoELM
Link-
336PhosphoserineNQVRSPGGP
CCCCCCCCC
29.10SysPTM
Link-
336Phosphoserine.NQVRSPGGP
CCCCCCCCC
29.10UniProtKB
Link-
376S-nitrosocysteineVNESCGKCN
CCCCCCCCC
5.01dbSNO
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 AND SER-336, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures