# ProteoformDB: an integrative database for functional roles of proteoforms

**Authors:** Hanwen Luo, Sichao Qiu, Maozu Guo, Beibei Xin, Jun Wang, Guoxian Yu

PMC · DOI: 10.1093/database/baag005 · Database: The Journal of Biological Databases and Curation · 2026-02-09

## TL;DR

ProteoformDB is a new database that integrates functional annotations of proteoforms to help researchers study their roles in biology and disease.

## Contribution

ProteoformDB introduces an integrative platform with analytical tools for proteoform functional annotation and regulatory mechanisms.

## Key findings

- ProteoformDB includes transcript-level annotations for 214 animal and 28 plant species.
- The database supports analysis of functional differences through sequences, domains, and post-translational modifications.
- It provides tools for function prediction, differential analysis, and data download.

## Abstract

Proteoforms translated from alternatively spliced transcripts contribute to the functional repertoire of the cell by performing diverse biological functions, contributing to the functional diversity of genomics and proteomics. However, the lack of existing databases that integrate functional annotations of proteoforms, and analyse the drivers of their functional differences significantly hinders in-depth research into proteoform functions. We introduce ProteoformDB, a new web resource with integrated in-platform analytical capabilities, organizes transcript-level functional annotations of proteoforms across multiple species, and provides services for prediction of proteoform functions and analysis of functional regulatory mechanisms. ProteoformDB develops user-friendly interfaces for information search, visualization, function supplement, differential analysis, and data download services. Particularly, it enables users to investigate the impact of molecular events on the function of proteoforms at multiple levels, including sequences, domains, and post-translational modifications, among others, thereby uncovering the functional differences between protein variants. The current version includes processed data (154.83 GB) for 214 animal and 28 plant species, and will become a valuable and expandable proteoform functional resource for studying genome and transcriptome functions, disease mechanisms, and other related research.

## Full-text entities

- **Genes:** Srsf2 (serine and arginine-rich splicing factor 2) [NCBI Gene 20382] {aka D11Wsu175e, MRF-1, Pr264, SC35, Sfrs10, Sfrs2}, indole-3-glycerol-phosphate lyase [NCBI Gene 100856952], LOC100272792 (beta-glucosidase) [NCBI Gene 100272792] {aka GRMZM2G031628, GRMZM2G031660}, HSD17B6 (hydroxysteroid 17-beta dehydrogenase 6) [NCBI Gene 8630] {aka HSE, RODH, SDR9C6}, Bcl2l1 (BCL2-like 1) [NCBI Gene 12048] {aka Bcl(X)L, Bcl-XL, Bcl2l, BclX, bcl-x, bcl2-L-1}, Tnni3 (troponin I, cardiac 3) [NCBI Gene 21954] {aka Tn1, cTnI}
- **Diseases:** AS (MESH:C536589), lung, breast, and ovarian cancer (MESH:D061325), haematopoietic diseases (MESH:D004194), DDI (MESH:C563663), Alzheimer's disease (MESH:D000544), cancer (MESH:D009369), myocardial injury (MESH:D009202), neurofibrillary tangles (MESH:D055956)
- **Chemicals:** oxygen (MESH:D010100), indole-3-glycerol phosphate (MESH:C008117), water (MESH:D014867), indole (MESH:C030374), L-tryptophan (MESH:D014364)
- **Species:** Arabidopsis thaliana (mouse-ear cress, species) [taxon 3702], Danio rerio (leopard danio, species) [taxon 7955], Phaseolus vulgaris (common bean, species) [taxon 3885], Homo sapiens (human, species) [taxon 9606], Astatotilapia calliptera (eastern happy, species) [taxon 8154], Oryza meridionalis (Australian wild rice, species) [taxon 40149], Mus musculus (house mouse, species) [taxon 10090], Bos taurus (bovine, species) [taxon 9913], Pan troglodytes (chimpanzee, species) [taxon 9598]

## Full text

_Full body text omitted from this summary view._ Fetch the complete paper as Markdown: https://tomesphere.com/paper/PMC12883993/full.md

## Figures

3 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12883993/full.md

## References

42 references — full list in the complete paper: https://tomesphere.com/paper/PMC12883993/full.md

---
Source: https://tomesphere.com/paper/PMC12883993