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Description |
HTATIP (HIV-1
Tat interacting protein TIP60, about 60kDa) belongs to the MYST
family of histone acetyl transferases (HATs) and was originally
isolated as an HIV-1 TAT-interactive protein. HATs play
important roles in regulating chromatin remodeling,
transcription and other nuclear processes by acetylating histone
and nonhistone proteins. The nucleosome, made up of four core
histone proteins (H2A, H2B, H3 and H4), is the primary building
block of chromatin. In addition to the growing number of
post-translational histone modifications regulating chromatin
structure, cells can also exchange canonical histones with
variant histones that can directly or indirectly modulate
chromatin structure. There are five major variants of histone
H2A: canonical H2A (most abundant), H2A.X, MacroH2A, H2ABbd and
H2A.Z. Histone H2A.Z, the most conserved variant across species,
functions as both a positive and negative regulator of
transcription and is important for chromosome stability. Several
homologous protein complexes, such as SWR-C, TIP60 and SRCAP
(mammals), have been shown to catalyze the ATP-dependent
exchange of H2A.Z for H2A in the nucleosome. This protein is a
histone acetylase that has a role in DNA repair and apoptosis
and is thought to play an important role in signal transduction. |
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Synonyms |
EC 2.3.1.48; EC 2.3.1.- ; ESA1; HTATIP;
HTATIP1; PLIP; TIP; TIP60; Tip60; cPLA2; 60 kDa Tat interactive
protein; HIV-1 Tat interactive protein; HIV-1 Tat interactive
protein, 60kDa; HIV-1 Tat interacting protein TIP60; K(lysine)
acetyltransferase 5; K-acetyltransferase 5; Tat interacting
protein, 60kDa; cPLA(2)-interacting protein; cPLA2 interacting
protein |
