Interval

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Interval (graph theory)

In graph theory, an interval I(h) in a directed graph is a maximal, single entry subgraph in which h is the only entry to I(h) and all closed paths in I(h) contain h. Intervals were described in 1976 by F. E. Allen and J. Cooke. Interval graphs are integral to some algorithms used in compilers, specifically data flow analyses.

The following algorithm finds all the intervals in a graph consisting of vertices N and the entry vertex n₀, and with the functions pred(n) and succ(n) which return the list of predecessors and successors of a given node n, respectively.

The algorithm effectively partitions the graph into its intervals.

Each interval can in turn be replaced with a single node, while all edges between nodes in different intervals in the original graph become edges between their corresponding nodes in the new graph. This new graph is called an interval derived graph. The process of creating derived graphs can be repeated until the resulting graph can't be reduced further. If the final graph consists of a single node, then the original graph is said to be reducible.

Partially ordered set

In mathematics, especially order theory, a partially ordered set (or poset) formalizes and generalizes the intuitive concept of an ordering, sequencing, or arrangement of the elements of a set. A poset consists of a set together with a binary relation that indicates that, for certain pairs of elements in the set, one of the elements precedes the other. Such a relation is called a partial order to reflect the fact that not every pair of elements need be related: for some pairs, it may be that neither element precedes the other in the poset. Thus, partial orders generalize the more familiar total orders, in which every pair is related. A finite poset can be visualized through its Hasse diagram, which depicts the ordering relation.

A familiar real-life example of a partially ordered set is a collection of people ordered by genealogical descendancy. Some pairs of people bear the descendant-ancestor relationship, but other pairs bear no such relationship.

Formal definition

SRC

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Proto-oncogene tyrosine-protein kinase Src

Proto-oncogene tyrosine-protein kinase Src, also known as proto-oncogene c-Src or simply c-Src , is a non-receptor tyrosine kinase protein that in humans is encoded by the SRC gene. This protein phosphorylates specific tyrosine residues in other proteins. An elevated level of activity of c-Src tyrosine kinase is suggested to be linked to cancer progression by promoting other signals. c-Src includes an SH2 domain, an SH3 domain, and a tyrosine kinase domain.

c-Src stands for "cellular Src kinase" and should not be confused with "C-terminal Src kinase" (CSK) which is an enzyme which phosphorylates c-Src at its C-terminus and provides negative regulation of Src's enzymatic activity. c-Src is a widely studied member of non-receptor tyrosine kinases which are not associated with a cell-surface receptor.

Src (pronounced "sarc" as it is short for sarcoma) is a proto-oncogene encoding a tyrosine kinase originally discovered by J. Michael Bishop and Harold E. Varmus, for which they were awarded the 1989 Nobel Prize in Physiology or Medicine. It belongs to a family of non-receptor tyrosine kinases called Src family kinases.

Nuclear receptor coactivator 2

The nuclear receptor coactivator 2 also known as NCoA-2 is a protein that in humans is encoded by the NCOA2 gene. NCoA-2 is also frequently called glucocorticoid receptor-interacting protein 1 (GRIP1), steroid receptor coactivator-2 (SRC-2), or transcriptional mediators/intermediary factor 2 (TIF2).

Function

NCoA-2 is a transcriptional coregulatory protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity. NCOA2 is recruited to DNA promotion sites by ligand-activated nuclear receptors. NCOA2 in turn acetylates histones, which makes downstream DNA more accessible to transcription. Hence, NCOA2 assists nuclear receptors in the upregulation of DNA expression.

GRIP1 is a transcriptional co-activator of the glucocorticoid receptor and interferon regulatory factor 1 (IRF1).

Interactions

Nuclear receptor coactivator 2 has been shown to interact with: