AstraPTM2
Post-Translational Modifications, Residue-by-Residue
Proteins are rarely just their sequence — they're phosphorylated, glycosylated, ubiquitinated and more. AstraPTM2 reads a sequence together with its predicted structure and flags where 39 different modification types are likely, one residue at a time.
The Broadest PTM Coverage in One Model
39 modification types — from the common regulatory marks to rare lipidations and processing events — scored at single-residue resolution across a full-length protein of any length, with no windowing or truncation.
Real Structure · Ubiquitin (PDB 1UBQ)
Modifications, mapped onto the fold
What It Predicts
39 Modification Types, One Model
From the common regulatory marks to rare lipidations and processing events — each scored per residue, so you know not just whether a protein is modified, but where.
Performance
Common Marks, Called Reliably
Coverage is broad — 39 types in a single pass — and the common regulatory marks, where public data is richest, are called most reliably.
Per-type F1, representative. Macro-F1 across all 39 types is 0.59 on held-out test — the common regulatory marks score above 0.7; rare modifications pull the average down. Full benchmarks are in the preprint.
In Context
Mapped Onto the Fold
Sites don't live in a vacuum. AstraPTM2's calls are shown against the structure and membrane topology, so a predicted glycosylation on an extracellular loop or a disulfide across a pocket reads at a glance.
How It Reads
Sequence and Structure, Together
Sequence Context
A protein language model captures the local and long-range context around every residue.
Structural Context
Predicted structure features — confidence, exposure, secondary structure — tell modification-likely surfaces apart.
Per-Residue Calls
Each residue gets a calibrated probability for every modification type, ready to overlay on the sequence.
Put Astra on Your Targets
Every Astra model runs inside the Orbion platform. Bring a sequence and get the full read-out — structure, function, modifications, binding, and stability.