Skip Navigation

University of Nebraska–Lincoln


Home of the farrp allergen protein database

Latest News:

New Version
Version # 18B
Peer Reviewed Sequences 2089
taxonomic-protein groups 831
Released On March 23, 2018
Download: V18B.pdf

Welcome to

AllergenOnline provides access to a peer reviewed allergen list and sequence searchable database intended for the identification of proteins that may present a potential risk of allergenic cross-reactivity. This website was designed to help in assessing the safety of proteins that may be introduced into foods through genetic engineering or through food processing methods. The objective is to identify proteins that may require additional tests, such as serum IgE binding, basophil histamine release or in vivo challenge to evaluate potential cross-reactivity.

The database is updated annually. Version 4 was released on a public website in 2004. The database is freely accessible with the intent of providing a simple and useful tool that may be useful in food safety evaluations.

Features and Tools Available.

Sequence search routines for food safety

  • We continue provide simple amino acid search routines to allow you to compare a protein sequence with the sequences in the current AllergenOnline database, which is updated on an annual basis. This is intended primarily for evaluating new proteins in Genetically Modified crops or in Novel Foods.
  • Search for full-length alignments by FASTA: The most predictive search is the overall FASTA alignment (see FASTA Help Page), with identity matches greater than 50% indicating possible cross-reactivity (Aalberse, 2000).
  • Search for 80 amino acid alignments by FASTA: A precautionary search using a sliding window of 80 amino acid segments of each protein to find identities greater than 35% (according to CODEX Alimentarius guidelines, 2003).
  • Search for 8 amino acid exact match: An 8-amino acid short-sequence identity search is provided since some regulatory authorities demand results of this extremely precautionary search. Our scientific opinion is that there is no evidence that an 8 amino acid match will identify a protein that is likely to be cross-reactive and could be missed by the conservative 80 amino acid match (35%). In our experience, isolated identity matches of 8 contiguous amino acids occur by chance alone at some modest rate, matches of 7 and 6 occur more commonly.  Experience (published and unpublished) demonstrates that two proteins sharing only a single short identity match of from 6 to 8 contiguous amino acids do not share IgE binding in the absence of more extensive identity alignments (at least >35% identity over 80 or more amino acids).  And that sequences sharing less than 50% identity over their full-lengths are rarely cross-reactive.  Thus we recommend not using these short identity matches as there is no scientific evidence that they predict IgE cross-reactivity and they do not predict shared clinical activities.

Browse the database

  • Allergen Source: Sequences of allergens are compiled in a table under "species", shown in the left-hand column (scientific name: genus and species).  The common name of the source is listed.
  • Each sequence is listed separately:  And there can be multiple different isoforms or partial sequences for a single type of allergen (e.g. Actinidia deliciosa Act d 1)
  • WHO/IUIS  Allergen Nomenclature: (World Health Organization/International Union of Immunological Societies) designation or name is shown if known abbreviated as IUIS.
  • Type of allergen is shown:  (e.g. Aero plant, food animal, venom or salivary)
  • Allergen Groups: A group name includes the genus and protein type or IUIS designation.  Multiple isoforms or close homologues of proteins contained in the database were clustered into related groups based on taxonomy of the source organism and sequence identity of the proteins. Evidence of allergenicity is assembled and evaluated for the collective sequences within one group, for review by the expert panel and for presentation of references related to the sequences.  The allergen “group” is linked to more information including the published references describing the information used to classify the protein as an allergen, as well as the individual sequences clustered into the group.  The GI# in the table of allergens is linked to the NCBI entries to show the complete NCBI entry. For groups with multiple sequence entries, the list of all entries and GI#’s are shown.  The publication references are also listed.  The references may apply to a single sequence, or to one or more sequences in the group.  In some cases they provide information of the allergenicity of the source.
  • References: The group name links to "Group References" describing the evidence of allergenicity for the group and a list of "Group Sequences" included in this version of the database.
  • Length:  The number of amino acids included in that single allergen entry
  • GI#:  The NCBI record number is shown for the single entry and it is linked directly to NCBI for viewing.
  • Version:  The database version that the specific allergen was entered is included (e.g. 7, 9, 11)

New Celiac disease protein Database Risk Assessment Tool

FARRP has added a new bioinformatics tool as a separate linked database with exact peptide and FASTA search algorithms to evaluate whether a novel protein derived from wheat, or near-relatives of wheat (members of the Pooideae subfamily of Poaceae) is sufficiently similar to glutens that it might elicit symptoms in those with celiac disease. See Celiac-Disease link (left) for explanation and access to the database.

Who We Are

Allergen Online Team

This database was developed and is maintained by the Food Allergy Research and Resource Program (FARRP) in the Department of Food Science and Technology at the University of Nebraska in Lincoln. John Wise wrote the code and maintained the database through version 14. Sreedevi Lalithambika joined the database in 2014 and is now responsible for maintaining the system and helping identify new candidate allergens. Richard Goodman manages the database and leads the peer review team.

Peer Reviewers

A panel of scientists and clinicians are actively involved in reviewing data for inclusion of proteins in the database by comparing peer reviewed publications supporting the classification of the proteins as allergens or putative allergens following predetermined guidelines. The affiliations of the experts are listed below. However, the experts participate as independent consultants. There is no claim that the opinions of the experts or the information provided in this allergen website, has been endorsed by any of the institutions.

  • Joe Baumert, Ph.D.,
    University of Nebraska, Lincoln, NE, USA
  • Barbara Bohle, Ph.D.,
    Medical University of Vienna, Vienna, Austria
  • Motohiro Ebisawa, M.D.,
    National Sagamihara Hospital, Sagamihara, Japan
  • Fatima Ferreira, Ph.D.,
    University of Salzburg, Salzburg, Austria
  • Richard E. Goodman, Ph.D.,
    University of Nebraska, Lincoln, NE, USA
  • Joerg Kleine-Tebbe, MD, FAAAAI., (member since 2016)
    Allergie- & Asthma-Zentrum Berlin Westend, OPD Hanf, Ackermann & Kleine-Tebbe, Berlin, Germany
  • Steve L. Taylor, Ph.D.,
    University of Nebraska, Lincoln, NE, USA
  • Ronald van Ree, Ph.D.,
    Academic Medical Center, Amsterdam, The Netherlands
Former members:
  • Sue L. Hefle, Ph.D., (2005-2006)
    University of Nebraska, Lincoln, NE, USA
  • Stefan Vieths, Ph.D., (2005-2012)
    Paul-Ehrlich-Institut, Langen, Germany
  • Hugh A. Sampson, M.D., (2005-2016)
    Mount Sinai Medical Center, New York, NY, USA

Financial Support

Financial support for this database has been provided by grants from corporate subscribers and by FARRP (the Food Allergy Research and Resource Program, Department of Food Science & Technology at the University of Nebraska-Lincoln) and faculty.

A majority of the scientific information is collected and evaluated by Rick Goodman, then verified by the review team. The database is updated annually. The database construction was performed by John Wise.

Sponsors (2004 - 2015):
  • BASF Plant Science, LP
  • Bayer CropScience, AG
  • Dow AgroSciences, LLC
  • Monsanto Company
  • Pioneer Hi-Bred International, Inc., DuPont
  • Syngenta Crop Protection, LLC
  • Vilmorin & Cie
Subscribers (2016 - 2017):
  • BASF Plant Science, LP
  • Pioneer Hi-Bred International, Inc., DuPont
  • J.R. Simplot Company
  • Nuseed
  • Unilever
  • <

Subscribers 2018:

  • Nuseed
  • Unilever

    Liability statement

    The content of the database is the sole responsibility of researchers at the University of Nebraska-Lincoln, with the advice and collaboration of additional independent academic and medical consultants. This work is co-sponsored by the aforementioned corporate subscribers and the Food Allergy Research and Resource Program at the University of Nebraska-Lincoln. Corporate subscribers have the right to provide scientific input. However, all decisions regarding content are the responsibility of the FARRP expert panel. The subscribers and the University of Nebraska, make no representations or warranties of any kind, express or implied, concerning the content of the database, including, without limitation, warranties of merchantability, fitness for a particular purpose, non-infringement, validity of any intellectual property rights or claims, whether issued or pending, and the absence of latent or other defects, whether or not discoverable.

    Bioinformatic Allergen Assessment Reports

  • Siruguri V, Bharatraj DK, Vankudavath RN, Rao Mendu VV, Gupta V, Goodman RE. Evaluation of Bar, Barnase, and Barstar recombinant proteins expressed in genetically engineered Brassica juncea (Indian mustard) for potential risks of food allergy using bioinformatics and literature searches. Food Chem Toxicol. 2015 Jun 14;83:93-102. doi: 10.1016/j.fct.2015.06.003. [Epub ahead of print] PubMed PMID: 26079618.

  • Jin Y, Goodman RE, Tetteh AO, Lu M, Tripathi L. Bioinformatics analysis to assess potential risks of allergenicity and toxicity of HRAP and PFLP proteins in genetically modified bananas resistant to Xanthomonas wilt disease. Food Chem Toxicol. 2017; 109:81-89. (Open Access, PMID: 28830835).
  • Jin Y, He X, Ando-Kumi K, Fraser RZ, Lu M, Goodman RE. Evaluating potential risks of food allergy and toxicity of soy leghemoglobin expressed in Pichia pastoris. Mol Nutr Food Res. 2017 Sept. 18; doi: 10.1002/mnfr.201700297 [Epub ahead of print](Open Access, PMID: 28921896).