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 3 weeks, 5 days ago.
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 87.0% of it. The other 12 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
- UP000153037
- Taxonomy
- 10377 · EBVB9
- Proteome type
- Reference proteome
- Strain
- B95-8
- Superkingdom
- viruses
- Genome assembly
- GCA_002402265.1 · ENA/EMBL
Source: UniProt proteome UP000153037, last modified 22 Apr 2026. Retrieved 17 Sep 2026 (2 days, 22 hours ago) and cached for a week.
Most viewed human herpesvirus 4 proteins
What visitors are reading in this proteome — 512 entry views in total.
- 1 P03185 · NEC2 Chromosome Segment 23 views
- 2 P0CK51 · BBLF1 Chromosome Segment 14 views
- 3 P0C739 · BNLF2a Chromosome Segment 13 views
- 4 P03211 · EBNA1 Chromosome Segment 12 views
- 5 P03182 · BHRF1 Chromosome Segment 10 views
- 6 P03190 · RIR1 Chromosome Segment 10 views
- 7 P03196 · gN Chromosome Segment 10 views
- 8 P03212 · gL Chromosome Segment 10 views
- 9 P03217 · BGLF5 Chromosome Segment 10 views
- 10 P12978 · EBNA2 Chromosome Segment 10 views
What do we provide?
Sequence-based predictions that help explain the behaviour of the proteins in the human herpesvirus 4 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.