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 an hour ago.
About this proteome
Extracted from UniProtKB
Dictyostelium discoideum, commonly known as slime mold, is a species of soil-living amoeba. It has the remarkable ability to switch from a solitary to a multicellular form. Under certain conditions, such as starvation, individuals aggregate and differentiate to generate a spore-releasing fruiting body. Since it is relatively easy to cultivate and manipulate in the laboratory, D. discoideum is a popular eukaryote model organism for researchers studying basic cellular processes such as chemotaxis, phagocytosis, apoptosis, signal transduction and cell differentiation. The genome was sequenced in 2005, has a size of 34 Mb, and contains approximately 12,500 protein-coding genes. It has an unusually high repeat number and is also AT-rich (approximately 78%), making sequencing and assembly particularly challenging.
What is included
This atlas covers the reviewed entries of this proteome — the manually curated Swiss-Prot section of UniProtKB. That is 32.5% of it. The other 8,588 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
- UP000002195
- Taxonomy
- 44689 · DICDI
- Proteome type
- Reference proteome
- Strain
- AX4
- Superkingdom
- eukaryota
- Genome assembly
- GCA_000004695.1 · ENA/EMBL
- Completeness (BUSCO)
- 95% · 239/255
Source: UniProt proteome UP000002195, last modified 5 Dec 2025. Retrieved 24 Aug 2026 (an hour ago) and cached for a week.
What do we provide?
Sequence-based predictions that help explain the behaviour of the proteins in the social amoeba 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.