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REBASE

Database of information about restriction enzymes and related proteins containing published and unpublished references, recognition and cleavage sites, isoschizomers, commercial availability, methylation sensitivity, crystal, genome, and sequence data. DNA methyltransferases, homing endonucleases, nicking enzymes, specificity subunits and control proteins are also included. Several tools are available including REBsites, BLAST against REBASE, NEBcutter and REBpredictor. Putative DNA methyltransferases and restriction enzymes, as predicted from analysis of genomic sequences, are also listed. REBASE is updated daily and is constantly expanding. Users may submit new enzyme and/or sequence information, recommend references, or send them corrections to existing data. The contents of REBASE may be browsed from the web and selected compilations can be downloaded by ftp (ftp.neb.com). Additionally, monthly updates can be requested via email.

URL: http://rebase.neb.com/rebase/

Resource ID: nif-0000-03391     Resource Type: Resource     Version: Latest Version

Keywords

endonuclease, enzyme, genome, archaeal, bacterial, cleavage, crystal, dna, individual protein family databases, isochizomer, methylation, methyltransferase, modification, protein, recognition, restriction, restriction enzyme, sensitivity, sequence, site, methylase, cleavage site, restriction-modification, blast

Additional Resource Types

Database, Data Repository, Data Analysis Service

Alternate URLs

http://rebase.neb.com

Species

microorganism

Abbreviation

REBASE

Synonyms

Restriction Enzyme Database, The Restriction Enzyme Database

Parent Organization

Funding Information

New England Biolabs Inc., NLM, LM04971

Availability

Public, Acknowledgement requested, The community can contribute to this resource

Old URLs

http://www.neb.com/rebase

Supercategory

Resource

Original Submitter

Anonymous

Version Status

Curated

Submitted On

12:00am July 16, 2011

Originated From

SciCrunch

Changes from Previous Version

  • Description was changed
  • Additional Resource Types was changed

Version 2

Created 2 weeks ago by Christie Wang

Version 1

Created 4 years ago by Anonymous

REBASE--enzymes and genes for DNA restriction and modification.

  • Roberts RJ
  • Nucleic Acids Res.
  • 2007 4

REBASE is a comprehensive database of information about restriction enzymes, DNA methyltransferases and related proteins involved in the biological process of restriction-modification. It contains fully referenced information about recognition and cleavage sites, isoschizomers, neoschizomers, commercial availability, methylation sensitivity, crystal and sequence data. Experimentally characterized homing endonucleases are also included. All newly sequenced genomes are analyzed for the presence of putative restriction systems and these data are included within the REBASE. The contents or REBASE may be browsed from the web (http://rebase.neb.com/rebase/rebase.ftp.html) and selected compilations can be downloaded by ftp (ftp.neb.com). Additionally, monthly updates can be requested via email.

REBASE--a database for DNA restriction and modification: enzymes, genes and genomes.

  • Roberts RJ
  • Nucleic Acids Res.
  • 2010 22

REBASE is a comprehensive database of information about restriction enzymes, DNA methyltransferases and related proteins involved in the biological process of restriction-modification (R-M). It contains fully referenced information about recognition and cleavage sites, isoschizomers, neoschizomers, commercial availability, methylation sensitivity, crystal and sequence data. Experimentally characterized homing endonucleases are also included. The fastest growing segment of REBASE contains the putative R-M systems found in the sequence databases. Comprehensive descriptions of the R-M content of all fully sequenced genomes are available including summary schematics. The contents of REBASE may be browsed from the web (http://rebase.neb.com) and selected compilations can be downloaded by ftp (ftp.neb.com). Additionally, monthly updates can be requested via email.