Biophysical Proteome Atlas

Human herpesvirus 4

Epstein–Barr virus, strain B95-8

Sequence-based biophysical predictions for the human herpesvirus 4 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

80

Entries here

80

Genes

1

Chromosomes

80

Reviewed in UniProt

Browse all entries

Last updated 5 minutes 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.

80 reviewed · 87.0% 12 unreviewed · 13.0% 92 in the proteome
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 5 Dec 2025. Retrieved 19 Aug 2026 (3 days, 2 hours ago) and cached for a week.


Most viewed human herpesvirus 4 proteins

What visitors are reading in this proteome — 4 entry views in total.

  1. 1 P03185 · NEC2 NEC2_EBVB9 Chromosome Segment 4 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.