# ProtGO: A Transformer based Fusion Model for accurately predicting Gene Ontology (GO) Terms from full scale Protein Sequences

arXiv: https://arxiv.org/abs/2412.05776 · HTML: https://mlsanity.com/paper/2412.05776/

## Key facts

- Cited by 1 papers in the map (data through 14 Oct 2026).
- Builds on 3 of its 40 references that are in the map.
- First posted on arXiv 8 Dec 2024.

## Builds on (most cited first, 3 of 3)

- [HuggingFace's Transformers: State-of-the-art Natural Language Processing](https://mlsanity.com/paper/1910.03771/) (2019)
- [Pretrained Transformers as Universal Computation Engines](https://mlsanity.com/paper/2103.05247/) (2021)
- [Energy-based models for atomic-resolution protein conformations](https://mlsanity.com/paper/2004.13167/) (2020)

## Built on by (most cited first, 1 of 1)

- [A Systematic Review on the Generative AI Applications in Human Medical Genomics](https://mlsanity.com/paper/2508.20275/) (2025)

## Abstract (arXiv)

Recent developments in next generation sequencing technology have led to the creation of extensive, open-source protein databases consisting of hundreds of millions of sequences. To render these sequences applicable in biomedical applications, they must be meticulously annotated by wet lab testing or extracting them from existing literature. Over the last few years, researchers have developed numerous automatic annotation systems, particularly deep learning models based on machine learning and artificial intelligence, to address this issue. In this work, we propose a transformer-based fusion model capable of predicting Gene Ontology (GO) terms from full-scale protein sequences, achieving state-of-the-art accuracy compared to other contemporary machine learning annotation systems. The approach performs particularly well on clustered split datasets, which comprise training and testing samples originating from distinct distributions that are structurally diverse. This demonstrates that the model is able to understand both short and long term dependencies within the enzyme's structure and can precisely identify the motifs associated with the various GO terms. Furthermore, the technique is lightweight and less computationally expensive compared to the benchmark methods, while at the same time not unaffected by sequence length, rendering it appropriate for diverse applications with varying sequence lengths.