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
Entries here
Genes
Chromosomes
Reviewed in UniProt
Last updated 2 days, 6 hours ago.
About this proteome
Extracted from UniProtKB
Sus scrofa, the domestic pig, is a member of the Artiodactyla (even-toed ungulates). First domesticated around 10,000 years ago, they are an important agricultural species worldwide. In addition, pigs are useful as a non-primate biomedical model organism, especially for the study of complex traits (e.g. obesity, cardiovascular disease, and arthritis) and for xenotransplantation experiments. The first draft genome was released in 2012 by the Swine Genome Sequencing Consortium, using sequence derived from a single Duroc sow (Duroc 2-14). Assembly 10.2 contains approximately 2.6 Gb of sequence and 21,000 protein-coding genes.
What is included
This atlas covers the reviewed entries of this proteome — the manually curated Swiss-Prot section of UniProtKB. That is 3.2% of it. The other 44,543 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.
- UniProt proteome
- UP000008227
- Taxonomy
- 9823 · PIG
- Proteome type
- Reference proteome
- Strain
- Duroc
- Superkingdom
- eukaryota
- Genome assembly
- GCA_000003025.6 · Ensembl
- Completeness (BUSCO)
- 97% · 12877/13335
Source: UniProt proteome UP000008227, 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 pig 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.