TAF1 Antibody – Rabbit Polyclonal

Function: Largest component and core scaffold of the TFIID basal transcription factor complex. Contains novel N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. Phosphorylates TP53 on 'Thr-55' which leads to MDM2-mediated degradation of TP53. Phosphorylates GTF2A1 and GTF2F1 on Ser residues. Possesses DNA-binding activity. Essential for progression of the G1 phase of the cell cycle. Ref.1 Ref.8 Ref.9 Ref.11 Ref.12 Ref.14 Ref.17

Catalytic activity: ATP + a protein = ADP + a phosphoprotein.

Cofactor: Magnesium.

Enzyme regulation: Autophosphorylates on Ser residues. Inhibited by retinoblastoma tumor suppressor protein, RB1.

Subunit structure: TAF1 is the largest component of transcription factor TFIID that is composed of TBP and a variety of TBP-associated factors. TAF1, when part of the TFIID complex, interacts with C-terminus of TP53. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. RB1 interacts with the N-terminal domain of TAF1. Interacts with ASF1A and ASF1B. Interacts with SV40 Large T antigen. Interacts (via bromo domains) with acetylated lysine residues on the N-terminus of histone H1.4, H2A, H2B, H3 and H4 (in vitro). Ref.3 Ref.10 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.24

Subcellular location: Nucleus Ref.1.

Post-translational modification: Phosphorylated by casein kinase II in vitro. Ref.9

Involvement in disease: Dystonia 3, torsion, X-linked (DYT3) [MIM:314250]: A X-linked dystonia-parkinsonism disorder. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. DYT3 is characterized by severe progressive torsion dystonia followed by parkinsonism. It has a well-defined pathology of extensive neuronal loss and mosaic gliosis in the striatum (caudate nucleus and putamen) which appears to resemble that in Huntington disease.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.23

Sequence similarities: Belongs to the TAF1 family.Contains 2 bromo domains.Contains 1 HMG box DNA-binding domain.Contains 2 protein kinase domains.