Systematic identification of novel protein domain families associated with nuclear functions.
By Tobias Doerks, Richard R. Copley, Jörg Schultz, Chris P. Ponting, Peer Bork. Genome Research, 2002
599 citations recorded by the source corpus.
A systematic computational analysis of protein sequences containing known nuclear domains led to the identification of 28 novel domain families. This represents a 26% increase in the starting set of 107 known nuclear domain families used for the analysis. Most of the novel domains are present in all major eukaryotic lineages, but 3 are species specific. For about 500 of the 1200 proteins that contain these new domains, nuclear localization could be inferred, and for 700, additional features could be predicted. For example, we identified a new domain, likely to have a role downstream of the unfolded protein response; a nematode-specific signalling domain; and a widespread domain, likely to be a noncatalytic homolog of ubiquitin-conjugating enzymes.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/807ce5fc7e7edbf1d709116ac00a79e8c25d7db7
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
- Xiaodong Cheng
- Herborg Hauksdóttir
- R. Blumenthal
- Andrew Troy
- J. Herschleb
- J. Callis
- H. Schubert
- Sophia L. Stone
Citations in the corpus
- Many paths to methyltransfer: a chronicle of convergence. (2003, background): “Amino-acid sequence comparison [34] suggests that there are hundreds of these proteins, and several have been shown to methylate lysines in the flexible tails of histones or in Rubisco (ribulose-1,5-bisphosphate carboxylase) [35].”
- Functional Analysis of the RING-Type Ubiquitin Ligase Family of Arabidopsis1[w] (2005, background): “The RWD domain is found in the mammalian E3 ligase AO7 (Lorick et al., 1999; Doerks et al., 2002).”