From left to right: i) The number of proteins in the reference proteome of Mus musculus, ii) the number of unique protein sequences for which at least one model is available, iii) the total number of models and iv) a coverage bar plot is shown.
The bar plot shows the coverage for every protein in the reference proteome of Mus musculus for which there is at least one model. Different colours (dark green to red boxes) represent the coverage of the targets. Targets with high coverage are represented in dark green (more than 80% of the target's length is covered by models), whereas low coverage is shown in red. The size of each box is proportional to the number of target sequences with a given coverage.

For information on the latest proteome for Mus musculus, please visit UniProtKB.

You can easily download the latest protein sequences for Mus musculus proteome here. Please note this download is for the current UniProtKB release, which may be different to release 2024_02 that was used for the most up to date SWISS-MODEL Repository.

Detailed coverage numbers are obtained by hovering the mouse over one of the boxes.

The plot shows the evolution over years (x-axis) of the fraction of Mus musculus reference proteome residues (y-axis) for which structural information is available. Different colors (light blue to dark blue) in the plot represent the quality of the sequence alignment between the reference proteome sequences (targets) and the sequences of the proteins in the structure database (templates). Alignments with low sequence identity are displayed in light blue, whereas alignments with high sequence identity are depicted in dark blue. The SWISS-MODEL Template Library is used as database of templates. Only target-template alignments found by HHblits and only residues with atom coordinates are considered.

This chart shows the percentage of residues in the Mus musculus proteome which are covered by experimental structures and the enhancement of coverage by homology modelling by the SWISS-MODEL pipeline. Experimental residue coverage is determined using SIFTS mapping. For residues which are not covered by experimental structures (including where there are no atom records in SIFTS mapping) the model coverage bars are coloured by QMEANDisCo local quality score.

Many proteins form oligomeric structures either by self-assembly (homo-oligomeric) or by assembly with other proteins (hetero-oligomeric) to accomplish their function. In SWISS-MODEL Repository, the quaternary structure annotation of the template is used to model the target sequence in its oligomeric form. Currently our method is limited to the modelling of homo-oligomeric assemblies. The oligomeric state of the template is only considered if the interface is conserved.

Metadata for homology models and experimental structures mapping to proteome (7.7 MB)

Coordinates for homology models (no experimental structures) mapping to proteome (3.9 GB)