Single protein view
Ask MIP to show you a protein’s features:- “Show me the protein features for BRCA1”
- “Visualize the domains and PTMs of UniProt P04637”
- “What are the annotated features of TNFRSF25?”
Protein header
Displays the gene name, UniProt accession (linked to uniprot.org), organism, protein name, length, and function summary.Feature tracks
A horizontal SVG overview of the full protein length with color-coded tracks grouped by category:| Track | What it shows | Visual |
|---|---|---|
| Domains | Named structural/functional domains (e.g., BRCT, Death domain) | Colored bars cycling through blue, purple, indigo, teal, cyan, sky |
| Repeats | Repeat regions like cysteine-rich domains (CRDs) | Amber bars |
| Signal peptide | N-terminal signal sequences | Emerald bars |
| Transmembrane | Membrane-spanning regions | Rose bars |
| Coiled coil | Coiled-coil regions | Lime bars |
| PTMs | Phosphorylation, glycosylation, lipidation, disulfide bonds | Colored circles (orange, pink, yellow, violet) |
| Active/binding sites | Catalytic residues and ligand-binding positions | Colored circles (red, sky) |
Sequence viewer
The full amino acid sequence displayed in monospace, 60 characters per line, grouped in blocks of 10. Each character is color-coded based on the annotations that overlap it:- Domain regions get a colored background matching the feature tracks
- PTM positions are marked with
*above the character - Active site positions are marked with
^below the character - Position numbers appear on the left of each line
Legend
A color key mapping each annotation type to its visual representation.Protein comparison
Ask MIP to compare two proteins:- “Compare DR3 and DcR3 proteins”
- “Show me the differences between UniProt Q93038 and O95407”
- “Compare the domain structure of TNFRSF25 vs TNFRSF6B”
Comparison header
The two gene names, overall sequence identity percentage, aligned length, and gap count.Domain comparisons table
A table showing identity percentages for each matching domain pair. Domains are matched by normalized name across both proteins (e.g., “TNFR-Cys 1” in protein 1 aligns with “TNFR-Cys 1” in protein 2). Domains unique to one protein are listed as “only in protein 1/2.”Individual protein views
Both proteins are rendered with their full feature tracks, sequence viewers, and annotations — identical to the single protein view. You can scroll through each independently.How the data is fetched
- MIP calls the UniProt REST API with the protein accession, requesting sequence, domains, PTMs, active sites, and all feature annotations.
- Domain and feature sequences are extracted from the full protein sequence using UniProt’s 1-indexed positions.
- For comparisons, a Needleman-Wunsch global alignment is computed in pure TypeScript with affine gap penalties — no external service is involved.
- All data is packaged as JSON and stored in the artifact. Subsequent opens read from the database — no re-fetch from UniProt.
All identity percentages and domain sequences are computed deterministically from tool output. MIP never estimates or approximates protein data — if a number appears in the viewer, it was calculated from real sequences.
Available actions
The protein viewer toolbar includes:- Copy FASTA — Copies the protein sequence in FASTA format to your clipboard
- Download JSON — Downloads the full protein data (sequence, annotations, alignment results) as a JSON file
What you can learn from the viewer
Domain architecture
Domain architecture
See which functional domains a protein contains, their exact boundaries, and how they are arranged along the sequence. Useful for understanding protein function and predicting the impact of variants in specific regions.
Post-translational modifications
Post-translational modifications
Identify phosphorylation, glycosylation, lipidation, and disulfide bond sites. Relevant for understanding regulation, signaling, and the functional consequences of missense variants near modification sites.
Structural features
Structural features
Locate signal peptides, transmembrane regions, and coiled-coil domains. Critical for understanding protein localization and whether a variant might disrupt membrane anchoring or secretion.
Evolutionary comparison
Evolutionary comparison
Compare paralog or ortholog sequences to understand conservation. High identity in a domain suggests functional importance; divergence may explain different biological roles.