background:
Largest component and core scaffold of the TFIID basal transcription factor complex. Contains novel N- and SLCterminal 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.
Function:
Largest component and core scaffold of the TFIID basal transcription factor complex. Contains novel N- and SLCterminal 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.
Subunit:
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 SLCterminus of TP53. Component of some MLL1/MLL complex, at least composed of the core components MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components C17orf49, 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.
Subcellular Location:
Nucleus.
Post-translational modifications:
Phosphorylated by casein kinase II in vitro.
DISEASE:
Defects in TAF1 are the cause of dystonia type 3 (DYT3) [MIM:314250]; also called X-linked dystonia-parkinsonism (XDP). DYT3 is 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. Its prevalence is high in the Philippines. DYT3 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.
Similarity:
Belongs to the TAF1 family.
Contains 2 bromo domains.
Contains 1 HMG box DNA-binding domain.
Contains 2 protein kinase domains.
Database links:
Entrez Gene: 6872 Human
Entrez Gene: 270627 Mouse
Entrez Gene: 317256 Rat
Omim: 313650 Human
SwissProt: P21675 Human
SwissProt: Q80UV9 Mouse
Unigene: 158560 Human
Unigene: 722619 Human
Unigene: 261750 Mouse
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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