Biophysical Proteome Atlas

Western clawed frog

Xenopus tropicalis

Sequence-based biophysical predictions for the western clawed frog reference proteome from UniProt.

Traditionally, proteins are described in a single static state (a picture). It is now increasingly recognised that many proteins can adopt multiple states and move between these conformational states dynamically (a movie). Even more, not every protein has a well-defined three-dimensional structure, many are partly or fully disordered. These predictions describe backbone and side-chain dynamics, disorder, early folding events, beta-sheet aggregation and phase separation.


In this atlas

0

Entries here

0

Genes

1,714

Reviewed in UniProt

Browse all entries

This proteome is not organised by chromosome.

Last updated now.

About this proteome

Extracted from UniProtKB

No description is available for this proteome from UniProt.

What is included

This atlas covers the reviewed entries of this proteome — the manually curated Swiss-Prot section of UniProtKB. That is 4.6% of it. The other 35,950 entries are unreviewed (TrEMBL) and are not included, which is why the count above is smaller than the proteome. You can run the same predictions on any of them yourself in the online predictors.

1,714 reviewed · 4.6% 35,950 unreviewed · 95.4% 37,664 in the proteome
UniProt proteome
UP000008143
Taxonomy
8364 · XENTR
Proteome type
Reference proteome
Strain
Nigerian
Superkingdom
eukaryota
Genome assembly
GCF_000004195.4 · RefSeq
Completeness (BUSCO)
97% · 5138/5310

Source: UniProt proteome UP000008143, last modified 5 Dec 2025. Retrieved 19 Aug 2026 (2 days, 5 hours ago) and cached for a week.


What do we provide?

Sequence-based predictions that help explain the behaviour of the proteins in the western clawed frog proteome. Not all of these proteins, or regions of them, have a well-defined three-dimensional structure as available from the PDB; many are dynamic or ambiguous. These predictions give clues as to how such regions behave.

DynaMine
backbone and side-chain dynamics
DisoMine
disorder
EFoldMine
early folding
AgMata
beta-sheet aggregation
PSPer
phase separation

How do I proceed?

Open the entry list and click a UniProt accession. Each entry page carries:

  • Overview — every prediction on one plot.
  • Interpretation — disorder classified as order, transition or disorder.
  • Values and Statistics — the numbers behind the plots.
  • Sequence — residues coloured by prediction.
  • PSP — phase-separation propensity.
  • Visualization 1D-3D — a 3D model coloured by prediction.
  • Downloads — sequence, predictions and structures.

Prefer code? Everything is available through the REST API.