Proteomic and Phosphoproteomic Data on Endometrial Decidualization

Modified supplementary tables and figures from a published Human Reproduction article. The data includes label-free quantification intensities for proteins and normalized intensities for phosphopeptides from endometrial stromal cells in proliferative and secretory phases. The dataset was created by Darja Lavõgina and is associated with an Open Access (green) license.

Use Cases

• Identify differentially abundant proteins between proliferative and secretory endometrial phases based on label-free quantification intensities.
• Analyze phosphosite abundance changes linked to the Rho kinase – cofilin axis during decidualization.
• Perform functional enrichment analysis using Gene Ontology terms for proteins corresponding to identified phosphosites.
• Investigate correlations between protein fold-change values and phosphosite abundances from the combined proteomic and phosphoproteomic tables.

Strengths

• Data is formally published in a peer-reviewed Human Reproduction article, providing a level of validation.
• Includes both a full list and a short-list of proteins and phosphosites, with filtering criteria like RMSD between experiments specified.
• Phosphoproteomic data is linked to corresponding protein log2 fold-change values from proteomic data.

Limitations

• Row count and dataset size are unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred from the description after download.
• Last update date is unknown; freshness unverified.

Provenance

Source

Human Reproduction article (https://doi.org/10.1093/humrep/deab161)

Collection Method

Experimental proteomic and phosphoproteomic analysis of in vitro and in vivo endometrial stromal cell samples.