PaperBLAST – Find papers about a protein or its homologs

 

PaperBLAST

PaperBLAST Hits for AZOBR_RS07475 (67 a.a., MADTYKVGGM...)

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 46 similar proteins in the literature:

A3LVL5 Copper-transporting ATPase (Cu(2+)-ATPase) from Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)
40% identity, 5% coverage

PSPPH_4641 YccA from Pseudomonas syringae pv. phaseolicola 1448A
40% identity, 87% coverage

SMU_427 copper chaperone CopZ from Streptococcus mutans UA159
33% identity, 99% coverage

NCgl2860 heavy-metal-associated domain-containing protein from Corynebacterium glutamicum ATCC 13032
49% identity, 74% coverage

W6QTN1 Heavy metal transport/detoxification protein from Ectopseudomonas oleovorans (strain CECT 5344)
40% identity, 90% coverage

EP10_000121 copper chaperone CopZ from Geobacillus icigianus
43% identity, 93% coverage

WP_058616432 heavy-metal-associated domain-containing protein from Tepidimonas taiwanensis
36% identity, 91% coverage

T303_08745 copper chaperone CopZ from Streptococcus thermophilus ASCC 1275
35% identity, 99% coverage

GY20_RS0110545 heavy-metal-associated domain-containing protein from Corynebacterium glutamicum
49% identity, 53% coverage

H16_A3669 copper chaperone, heavy metal ion binding from Ralstonia eutropha H16
H16_A3669 heavy-metal-associated domain-containing protein from Cupriavidus necator H16
37% identity, 85% coverage

FRAAL0988 putative regulator from Frankia alni ACN14a
44% identity, 85% coverage

G8E09_12835 heavy-metal-associated domain-containing protein from Acinetobacter pittii
44% identity, 82% coverage

PFLU0660 putative substrate-binding periplasmic protein from Pseudomonas fluorescens SBW25
42% identity, 85% coverage

BDGL_000478 putative copper chaperone from Acinetobacter pittii PHEA-2
42% identity, 82% coverage

Q1LHH9 Copper chaperone, heavy metal ion binding (Modular protein) from Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
35% identity, 43% coverage

IYO_003325 heavy-metal-associated domain-containing protein from Pseudomonas syringae pv. actinidiae ICMP 18884
44% identity, 72% coverage

Aave_0033 Heavy metal transport/detoxification protein from Acidovorax avenae subsp. citrulli AAC00-1
38% identity, 91% coverage

ABUW_2708, ABUW_RS13140 heavy-metal-associated domain-containing protein from Acinetobacter baumannii
44% identity, 82% coverage

PSPTO0752 copZ protein, putative from Pseudomonas syringae pv. tomato str. DC3000
40% identity, 75% coverage

BAB1_0960 Heavy metal transport/detoxification protein:Heavy metal binding from Brucella melitensis biovar Abortus 2308
47% identity, 85% coverage

BP1727 putative exported protein from Bordetella pertussis Tohama I
43% identity, 91% coverage

JJQ59_18480 heavy-metal-associated domain-containing protein from Cupriavidus necator
37% identity, 85% coverage

A7J09_03980, DP111_07130 heavy metal translocating P-type ATPase from Streptococcus suis
38% identity, 7% coverage

SSUST1_0574 heavy metal translocating P-type ATPase from Streptococcus suis ST1
38% identity, 7% coverage

SPy1714 putative copper chaperone - copper transport operon from Streptococcus pyogenes M1 GAS
35% identity, 94% coverage

BC351_38480 copper ion binding protein from Paenibacillus ferrarius
45% identity, 88% coverage

PF0740 heavy-metal transporting cpx-type atpase from Pyrococcus furiosus DSM 3638
Q8TH11 Heavy-metal transporting cpx-type atpase from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
37% identity, 8% coverage

TL13_0615 heavy metal translocating P-type ATPase from Streptococcus suis TL13
38% identity, 7% coverage

ID09_03115 heavy metal translocating P-type ATPase from Streptococcus suis 6407
38% identity, 7% coverage

A6M16_02880, BFP66_02780 heavy metal translocating P-type ATPase from Streptococcus suis
38% identity, 7% coverage

Q6BIS6 DEHA2G07986p from Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968)
40% identity, 5% coverage

PP0588, PP_0588 copper-binding protein, putative from Pseudomonas putida KT2440
36% identity, 87% coverage

T1E_3759 heavy-metal-associated domain-containing protein from Pseudomonas putida DOT-T1E
36% identity, 87% coverage

IS492_27185 heavy-metal-associated domain-containing protein from Pseudomonas aeruginosa
40% identity, 85% coverage

PA14_18070 putative periplasmic metal-binding protein from Pseudomonas aeruginosa UCBPP-PA14
40% identity, 85% coverage

CWI26_08525 heavy metal translocating P-type ATPase from Streptococcus suis
40% identity, 7% coverage

DP112_07660 heavy metal translocating P-type ATPase from Streptococcus suis
36% identity, 7% coverage

FAY30_11165 copper chaperone CopZ from Bacillus sp. S3
39% identity, 87% coverage

Q9WYF3 P-type Cu+ transporter (EC 7.2.2.8) from Thermotoga maritima (see paper)
TC 3.A.3.5.33 / Q9WYF3 Ca2+ from Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
TM0317 cation-transporting ATPase, P-type from Thermotoga maritima MSB8
38% identity, 8% coverage

JK_RS07345 heavy-metal-associated domain-containing protein from Corynebacterium jeikeium K411
47% identity, 53% coverage

cg3402 copper chaperone from Corynebacterium glutamicum ATCC 13032
41% identity, 88% coverage

cg3282 cation transport ATPase from Corynebacterium glutamicum ATCC 13032
47% identity, 78% coverage

APL_1264 putative cation transport ATPase from Actinobacillus pleuropneumoniae L20
37% identity, 93% coverage

Francci3_0489 Heavy metal transport/detoxification protein from Frankia sp. CcI3
41% identity, 82% coverage

GSU1338 heavy-metal-associated domain protein from Geobacter sulfurreducens PCA
44% identity, 42% 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