serw-MX  [xml]  

 DeCS Categories

G02 Chemical Phenomena .
G02.111 Biochemical Phenomena .
G02.111.570 Molecular Structure .
G02.111.570.820 Molecular Conformation .
G02.111.570.820.709 Protein Conformation .
G02.111.570.820.709.275 Protein Structural Elements .
G02.111.570.820.709.275.500 Amino Acid Motifs .
G02.111.570.820.709.275.500.898 Sterile Alpha Motif .
G02.111.570.820.709.275.750 Protein Domains .
G02.111.570.820.709.275.750.477 PR-SET Domains .
G02.111.570.820.709.275.750.500 Protein Interaction Domains and Motifs .
G02.111.570.820.709.275.750.500.813 Sterile Alpha Motif .
H01 Natural Science Disciplines .
H01.770 Science .
SH1 Health Sciences, Technology and Innovation Management .
SH1.010 Policies and Cooperation in Science, Technology and Innovation .
SH1.010.020 International Cooperation .
SH1.010.020.060 Science and Technology Information Networks .
SH1. International Network of Information and Knowledge Sources for Sciences, Technology and Innovation Management .
SH1.020 Scientific and Technical Activities .
SH1.020.020 Scientific Domains .
SP4 Environmental Health .
SP4.011 Science .
 Synonyms & Historicals
Scientific Domains .
Domains, Scientific .
Domains of the Sciences .
Science Domains .
Scientific Activities .
Scientific Disciplines .
Scientific knowledge areas. .
Science .
Sciences .
The study of natural phenomena by observation, measurement, and experimentation. .
PR-SET Domains .
PR Domain .
SET Domain .
Domain, PR .
Domain, PR-SET .
Domain, SET .
Domains, PR .
Domains, PR-SET .
Domains, SET .
PR Domains .
PR SET Domains .
PR-SET Domain .
SET Domains .
Highly conserved protein domains of approximately 130 to 140 amino acids. The SET domain was first identified in the Drosophila proteins (S)u(var)3-9, (E)nhancer-of-zeste and (T)rithorax and occurs in other proteins with a variety of functions, including histone-lysine N-methyltransferases. Structurally, it consists of BETA-SHEETS interspersed among loops and turns that result in an "L" shape. The most conserved motifs are a stretch at the C-terminal that contains a strictly conserved tyrosine residue and an adjacent loop that the C-terminal segment passes through to form a "knot". These motifs and especially the tyrosine residue are essential for S-ADENOSYLMETHIONINE binding and catalysis. The PR domain has high homology to the catalytic region of the SET domain and occurs at the N-terminal of PRDM proteins such as PRDM1 PROTEIN. .
Sterile Alpha Motif .
SAM Domain .
Sterile Alpha Motif Domain .
Motif, Sterile Alpha .
Motifs, Sterile Alpha .
SAM Domains .
Sterile Alpha Motifs .
A putative protein interaction module, approximately 70 amino acids long, that forms a small five-helix bundle with two large interfaces which may homo- and hetero-oligomerize, or bind non-sterile-alpha motif targets. The sterile alpha motif is present in a wide variety of eukaryotic proteins that function in diverse biological processes. .
International Network of Information and Knowledge Sources for Sciences, Technology and Innovation Management .
ScienTI .
International Network of Information and Knowledge Sources for Sciences, Technology and Information Management .
ScienTI is a public network of sources of information and knowledge that aims to contribute to the management of scientific, technological and innovation activities. The network provides a public and cooperative space for stakeholders of national science, technology and innovation (ST & I) systems and communities of the member-countries to interact. The sources of information include résumés (CVs), research groups, institutions and projects. All sources are standardized using international references in order to assure interoperability in the Internet. The network is designed to have an updated identification of skilled human resources, institutions and research projects for development and assessment of national policies and capacities in ST&I, as well as to promote international cooperation programs. The network is the expression of international cooperation among the National Science and Technology Organizations (ONCYTs), International Science and Technology Cooperation Organizations (OICYTs), Groups of Research and Development in Information and Knowledge Systems (GDIs) and Sponsoring Institutions (SIs) ( .