PaperBLAST – Find papers about a protein or its homologs

 

PaperBLAST

PaperBLAST Hits for sp|Q9HX17|3MGH_PSEAE Putative 3-methyladenine DNA glycosylase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=PA4010 PE=3 SV=1 (239 a.a., MSRDPILSLP...)

Other sequence analysis tools:

Find functional residues: SitesBLAST

Search for conserved domains

Find the best match in UniProt

Compare to protein structures

Predict transmenbrane helices: Phobius

Predict protein localization: PSORTb

Find homologs in fast.genomics

Fitness BLAST: loading...

Found 29 similar proteins in the literature:

PA4010 3-methyladenine DNA glycosylase from Pseudomonas aeruginosa PAO1
100% identity, 100% coverage

PA14_11970 methylpurine-DNA glycosylase family protein from Pseudomonas aeruginosa UCBPP-PA14
99% identity, 100% coverage

PputGB1_4865 3-methyladenine DNA glycosylase from Pseudomonas putida GB-1
76% identity, 90% coverage

PP_4812 DNA-3-methyladenine glycosylase, putative from Pseudomonas putida KT2440
76% identity, 90% coverage

NP_034952 DNA-3-methyladenine glycosylase from Mus musculus
32% identity, 55% coverage

Krad_3154 DNA-3-methyladenine glycosylase from Kineococcus radiotolerans SRS30216 = ATCC BAA-149
41% identity, 38% coverage

SCO1792 3-methyladenine DNA glycosylase from Streptomyces coelicolor A3(2)
33% identity, 61% coverage

AT3G12040 DNA-3-methyladenine glycosylase (MAG) from Arabidopsis thaliana
33% identity, 72% coverage

LOC102847768 uncharacterized protein LOC102847768 from Elephantulus edwardii
29% identity, 27% coverage

P23571 DNA-3-methyladenine glycosylase (Fragment) from Rattus norvegicus
33% identity, 46% coverage

FTL_0940 Methylpurine-DNA glycosylase family protein from Francisella tularensis subsp. holarctica
27% identity, 73% coverage

3MG_HUMAN / P29372 DNA-3-methyladenine glycosylase; 3-alkyladenine DNA glycosylase; 3-methyladenine DNA glycosidase; ADPG; N-methylpurine-DNA glycosylase; EC 3.2.2.21 from Homo sapiens (Human) (see paper)
32% identity, 46% coverage

Dgeo_1660 DNA-3-methyladenine glycosylase from Deinococcus geothermalis DSM 11300
31% identity, 80% coverage

NP_001015054 DNA-3-methyladenine glycosylase isoform c from Homo sapiens
30% identity, 56% coverage

A2IDA3 DNA-3-methyladenine glycosylase II (Fragment) from Homo sapiens
30% identity, 63% coverage

1f6oA / P29372 Crystal structure of the human aag DNA repair glycosylase complexed with DNA (see paper)
32% identity, 58% coverage

LMOf2365_0949 DNA-3-methyladenine glycosylase, putative from Listeria monocytogenes str. 4b F2365
Q721N6 Putative 3-methyladenine DNA glycosylase from Listeria monocytogenes serotype 4b (strain F2365)
29% identity, 77% coverage

lmo0928 similar to 3-methyladenine DNA glycosylase from Listeria monocytogenes EGD-e
27% identity, 87% coverage

CAB1_0249 DNA-3-methyladenine glycosylase from Chlamydia abortus LLG
29% identity, 79% coverage

B598_0269 DNA-3-methyladenine glycosylase from Chlamydia psittaci GR9
29% identity, 79% coverage

BRE_425 3-methyladenine DNA glycosylase from Borrelia recurrentis A1
31% identity, 62% coverage

SMb20709 putative 3-methyladenine DNA glycosylase protein from Sinorhizobium meliloti 1021
33% identity, 51% coverage

NP_391741 3-alkylated purines and hypoxanthine DNA glycosidase from Bacillus subtilis subsp. subtilis str. 168
27% identity, 80% coverage

CCA00239 DNA-3-methyladenine glycosylase from Chlamydophila caviae GPIC
27% identity, 79% coverage

3MG_ENCCU / Q8SQI1 Probable DNA-3-methyladenine glycosylase; 3-methyladenine DNA glycosidase; EC 3.2.2.21 from Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) (see paper)
ECU05_1590 3-METHYLADENINE DNA GLYCOSYLASE from Encephalitozoon cuniculi GB-M1
28% identity, 79% coverage

WD_1110 DNA-3-methyladenine glycosylase from Wolbachia endosymbiont of Drosophila melanogaster
36% identity, 31% coverage

SACE_5255 DNA-3-methyladenine glycosylase II from Saccharopolyspora erythraea NRRL 2338
35% identity, 36% coverage

EF_1978 DNA-3-methyladenine glycosylase from Enterococcus faecalis V583
26% identity, 79% coverage

EF1978 DNA-3-methyladenine glycosylase from Enterococcus faecalis V583
Q833H5 Putative 3-methyladenine DNA glycosylase from Enterococcus faecalis (strain ATCC 700802 / V583)
26% identity, 79% coverage

New Search

For advice on how to use these tools together, see Interactive tools for functional annotation of bacterial genomes.

Statistics

The PaperBLAST database links 793,807 different protein sequences to 1,259,118 scientific articles. Searches against EuropePMC were last performed on March 13 2025.

How It Works

PaperBLAST builds a database of protein sequences that are linked to scientific articles. These links come from automated text searches against the articles in EuropePMC and from manually-curated information from GeneRIF, UniProtKB/Swiss-Prot, BRENDA, CAZy (as made available by dbCAN), BioLiP, CharProtDB, MetaCyc, EcoCyc, TCDB, REBASE, the Fitness Browser, and a subset of the European Nucleotide Archive with the /experiment tag. Given this database and a protein sequence query, PaperBLAST uses protein-protein BLAST to find similar sequences with E < 0.001.

To build the database, we query EuropePMC with locus tags, with RefSeq protein identifiers, and with UniProt accessions. We obtain the locus tags from RefSeq or from MicrobesOnline. We use queries of the form "locus_tag AND genus_name" to try to ensure that the paper is actually discussing that gene. Because EuropePMC indexes most recent biomedical papers, even if they are not open access, some of the links may be to papers that you cannot read or that our computers cannot read. We query each of these identifiers that appears in the open access part of EuropePMC, as well as every locus tag that appears in the 500 most-referenced genomes, so that a gene may appear in the PaperBLAST results even though none of the papers that mention it are open access. We also incorporate text-mined links from EuropePMC that link open access articles to UniProt or RefSeq identifiers. (This yields some additional links because EuropePMC uses different heuristics for their text mining than we do.)

For every article that mentions a locus tag, a RefSeq protein identifier, or a UniProt accession, we try to select one or two snippets of text that refer to the protein. If we cannot get access to the full text, we try to select a snippet from the abstract, but unfortunately, unique identifiers such as locus tags are rarely provided in abstracts.

PaperBLAST also incorporates manually-curated protein functions:

Except for GeneRIF and ENA, the curated entries include a short curated description of the protein's function. For entries from BioLiP, the protein's function may not be known beyond binding to the ligand. Many of these entries also link to articles in PubMed.

For more information see the PaperBLAST paper (mSystems 2017) or the code. You can download PaperBLAST's database here.

Changes to PaperBLAST since the paper was written:

Many of these changes are described in Interactive tools for functional annotation of bacterial genomes.

Secrets

PaperBLAST cannot provide snippets for many of the papers that are published in non-open-access journals. This limitation applies even if the paper is marked as "free" on the publisher's web site and is available in PubmedCentral or EuropePMC. If a journal that you publish in is marked as "secret," please consider publishing elsewhere.

Omissions from the PaperBLAST Database

Many important articles are missing from PaperBLAST, either because the article's full text is not in EuropePMC (as for many older articles), or because the paper does not mention a protein identifier such as a locus tag, or because of PaperBLAST's heuristics. If you notice an article that characterizes a protein's function but is missing from PaperBLAST, please notify the curators at UniProt or add an entry to GeneRIF. Entries in either of these databases will eventually be incorporated into PaperBLAST. Note that to add an entry to UniProt, you will need to find the UniProt identifier for the protein. If the protein is not already in UniProt, you can ask them to create an entry. To add an entry to GeneRIF, you will need an NCBI Gene identifier, but unfortunately many prokaryotic proteins in RefSeq do not have corresponding Gene identifers.

References

PaperBLAST: Text-mining papers for information about homologs.
M. N. Price and A. P. Arkin (2017). mSystems, 10.1128/mSystems.00039-17.

Europe PMC in 2017.
M. Levchenko et al (2017). Nucleic Acids Research, 10.1093/nar/gkx1005.

Gene indexing: characterization and analysis of NLM's GeneRIFs.
J. A. Mitchell et al (2003). AMIA Annu Symp Proc 2003:460-464.

UniProt: the universal protein knowledgebase.
The UniProt Consortium (2016). Nucleic Acids Research, 10.1093/nar/gkw1099.

BRENDA in 2017: new perspectives and new tools in BRENDA.
S. Placzek et al (2017). Nucleic Acids Research, 10.1093/nar/gkw952.

The EcoCyc database: reflecting new knowledge about Escherichia coli K-12.
I. M. Keeseler et al (2016). Nucleic Acids Research, 10.1093/nar/gkw1003.

The MetaCyc database of metabolic pathways and enzymes.
R. Caspi et al (2018). Nucleic Acids Research, 10.1093/nar/gkx935.

CharProtDB: a database of experimentally characterized protein annotations.
R. Madupu et al (2012). Nucleic Acids Research, 10.1093/nar/gkr1133.

The carbohydrate-active enzymes database (CAZy) in 2013.
V. Lombard et al (2014). Nucleic Acids Research, 10.1093/nar/gkt1178.

The Transporter Classification Database (TCDB): recent advances
M. H. Saier, Jr. et al (2016). Nucleic Acids Research, 10.1093/nar/gkv1103.

REBASE - a database for DNA restriction and modification: enzymes, genes and genomes.
R. J. Roberts et al (2015). Nucleic Acids Research, 10.1093/nar/gku1046.

Deep annotation of protein function across diverse bacteria from mutant phenotypes.
M. N. Price et al (2016). bioRxiv, 10.1101/072470.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory