TOPDOM: database of domains and motifs with conservative location in transmembrane proteins
- PMID: 18434342
- PMCID: PMC2427164
- DOI: 10.1093/bioinformatics/btn202
TOPDOM: database of domains and motifs with conservative location in transmembrane proteins
Abstract
The TOPDOM database is a collection of domains and sequence motifs located consistently on the same side of the membrane in alpha-helical transmembrane proteins. The database was created by scanning well-annotated transmembrane protein sequences in the UniProt database by specific domain or motif detecting algorithms. The identified domains or motifs were added to the database if they were uniformly annotated on the same side of the membrane of the various proteins in the UniProt database. The information about the location of the collected domains and motifs can be incorporated into constrained topology prediction algorithms, like HMMTOP, increasing the prediction accuracy.
Availability: The TOPDOM database and the constrained HMMTOP prediction server are available on the page http://topdom.enzim.hu
Contact: tusi@enzim.hu; lkalmar@enzim.hu.
Similar articles
-
TOPDOM: database of conservatively located domains and motifs in proteins.Bioinformatics. 2016 Sep 1;32(17):2725-6. doi: 10.1093/bioinformatics/btw193. Epub 2016 Apr 12. Bioinformatics. 2016. PMID: 27153630 Free PMC article.
-
The HMMTOP transmembrane topology prediction server.Bioinformatics. 2001 Sep;17(9):849-50. doi: 10.1093/bioinformatics/17.9.849. Bioinformatics. 2001. PMID: 11590105
-
gpDB: a database of GPCRs, G-proteins, effectors and their interactions.Bioinformatics. 2008 Jun 15;24(12):1471-2. doi: 10.1093/bioinformatics/btn206. Epub 2008 Apr 25. Bioinformatics. 2008. PMID: 18441001
-
Large-scale database searching using tandem mass spectra: looking up the answer in the back of the book.Nat Methods. 2004 Dec;1(3):195-202. doi: 10.1038/nmeth725. Nat Methods. 2004. PMID: 15789030 Review.
-
Pfam 10 years on: 10,000 families and still growing.Brief Bioinform. 2008 May;9(3):210-9. doi: 10.1093/bib/bbn010. Epub 2008 Mar 15. Brief Bioinform. 2008. PMID: 18344544 Review.
Cited by
-
The human transmembrane proteome.Biol Direct. 2015 May 28;10:31. doi: 10.1186/s13062-015-0061-x. Biol Direct. 2015. PMID: 26018427 Free PMC article.
-
MeMotif: a database of linear motifs in alpha-helical transmembrane proteins.Nucleic Acids Res. 2010 Jan;38(Database issue):D181-9. doi: 10.1093/nar/gkp1042. Epub 2009 Nov 12. Nucleic Acids Res. 2010. PMID: 19910368 Free PMC article.
-
Computational modeling of membrane proteins.Proteins. 2015 Jan;83(1):1-24. doi: 10.1002/prot.24703. Epub 2014 Nov 19. Proteins. 2015. PMID: 25355688 Free PMC article. Review.
-
UniTmp: unified resources for transmembrane proteins.Nucleic Acids Res. 2024 Jan 5;52(D1):D572-D578. doi: 10.1093/nar/gkad897. Nucleic Acids Res. 2024. PMID: 37870462 Free PMC article.
-
Structural fragment clustering reveals novel structural and functional motifs in alpha-helical transmembrane proteins.BMC Bioinformatics. 2010 Apr 26;11:204. doi: 10.1186/1471-2105-11-204. BMC Bioinformatics. 2010. PMID: 20420672 Free PMC article.
References
-
- Arora A, Tamm LK. Biophysical approaches to membrane protein structure determination. Curr. Opin. Struct. Biol. 2001;11:540–547. - PubMed