Pith. sign in

REVIEW 1 cited by

MAP Format for Representing Chemical Modifications, Annotations, and Mutations in Protein Sequences: An Extension of the FASTA Format

Not yet reviewed by Pith; the record is open.

This paper has not been read by Pith yet. Machine review is queued; the pith claim, tier, and objections will appear here once it completes.

SPECIMEN: schema-true, not a live event

T0 review · schema-true

One-sentence machine reading of the paper's core claim.

pith:XXXXXXXX · record.json · timestamp

arxiv 2505.03403 v1 pith:QATMEKSP submitted 2025-05-06 q-bio.BM

classification q-bio.BM
keywords formatfastaproteinformatsmodificationsaminoannotationsincluding
verification ladder T0 review T1 audit T2 compute T3 formal
0 comments
read the original abstract

Several formats, including FASTA, PIR, GenBank, EMBL, and GCG, have been developed for representing protein sequences composed of natural amino acids. Among these, FASTA remains the most widely used due to its simplicity and human readability. However, FASTA lacks the capability to represent chemically modified or non-natural residues, as well as structural annotations and mutations in protein variants. To address some of these limitations, the PEFF format was recently introduced as an extension of FASTA. Additionally, formats such as HELM and BILN have been proposed to represent amino acids and their modifications at the atomic level. Despite their advancements, these formats have not achieved widespread adoption within the bioinformatics community due to their complexity. To complement existing formats and overcome current challenges, we propose a new format called MAP (Modification and Annotation in Proteins), which enables comprehensive annotation of protein sequences. MAP introduces meta tags in the header for protein-level annotations and inline tags within the sequence for residue-level modifications. In this format, standard one-letter amino acid codes are augmented with curly-brace tags to denote various modifications, including phosphorylation, acetylation, non-natural residues, cyclization, and other residue-specific features. The header metadata also captures information such as organism, function, and sequence variants. We describe the structure, objectives, and capabilities of the MAP format and demonstrate its application in bioinformatics, particularly in the domain of protein therapeutics. To facilitate community adoption, we are developing a comprehensive suite of MAP-format resources, including a detailed manual, annotated datasets, and conversion tools, available at http://webs.iiitd.edu.in/raghava/maprepo/.

Discussion (0). Continue with ORCID to comment.

Forward citations

Cited by 1 Pith paper

Reviewed papers in the Pith corpus that reference this work. Sorted by Pith novelty score. Full citation record

  1. TumorHoPe2: An updated database for Tumor Homing Peptides

    q-bio.BM 2025-05 conditional novelty 5.0 of 10

    TumorHoPe2 is an updated manually curated database of 1,847 entries (1,297 unique) experimentally validated tumor-homing peptides, with web tools and a REST API.

Pith tools