TAF1

Initiation of transcription by RNA polymerase II requires the activities of more than 70 polypeptides. The protein that coordinates these activities is the basal transcription factor TFIID, which binds to the core promoter to position the polymerase properly, serves as the scaffold for assembly of the remainder of the transcription complex, and acts as a channel for regulatory signals. TFIID is composed of the TATA-binding protein (TBP) and a group of evolutionarily conserved proteins known as TBP-associated factors or TAFs. TAFs may participate in basal transcription, serve as coactivators, function in promoter recognition or modify general transcription factors (GTFs) to facilitate complex assembly and transcription initiation. This gene encodes the largest subunit of TFIID. This subunit binds to core promoter sequences encompassing the transcription start site. It also binds to activators and other transcriptional regulators, and these interactions affect the rate of transcription initiation. This subunit contains two independent protein kinase domains at the N- and C-terminals, but also possesses acetyltransferase activity and can act as a ubiquitin-activating/conjugating enzyme. Mutations in this gene result in Dystonia 3, torsion, X-linked, a dystonia-parkinsonism disorder. Alternative splicing of this gene results in multiple transcript variants. This gene is part of a complex transcription unit (TAF1/DYT3), wherein some transcript variants share exons with TAF1 as well as additional downstream DYT3 exons. [provided by RefSeq, Oct 2013]

TAF1 Gene(Protein Coding) TATA-Box Binding Protein Associated Factor 1

The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (PubMed:33795473).
TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (PubMed:33795473).
The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473).
TAF1 is the largest component and core scaffold of the TFIID complex, involved in nucleating complex assembly (PubMed:25412659, PubMed:27007846, PubMed:33795473).
TAF1 forms a promoter DNA binding subcomplex of TFIID, together with TAF7 and TAF2 (PubMed:33795473).
Contains novel N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors (PubMed:25412659, PubMed:8625415).
Phosphorylates TP53 on 'Thr-55' which leads to MDM2-mediated degradation of TP53 (PubMed:25412659).
Phosphorylates GTF2A1 and GTF2F1 on Ser residues (PubMed:25412659).
Possesses DNA-binding activity (PubMed:25412659).
Essential for progression of the G1 phase of the cell cycle (PubMed:11278496, PubMed:15053879, PubMed:2038334, PubMed:8450888, PubMed:8625415, PubMed:9660973, PubMed:9858607).
Exhibits histone acetyltransferase activity towards histones H3 and H4 (PubMed:15870300).

Biological Process cell cycleIEA:UniProtKB-KW
Biological Process cellular response to ATPIDA:ParkinsonsUK-UCL1 Publication
Biological Process cellular response to DNA damage stimulusIDA:ParkinsonsUK-UCL1 Publication
Biological Process cellular response to UVIDA:ParkinsonsUK-UCL1 Publication
Biological Process midbrain developmentIGI:ParkinsonsUK-UCL1 Publication
Biological Process mRNA transcription by RNA polymerase IIIDA:ComplexPortal1 Publication
Biological Process negative regulation of DNA-binding transcription factor activityIDA:ARUK-UCL1 Publication
Biological Process negative regulation of gene expressionIMP:ParkinsonsUK-UCL1 Publication
Biological Process negative regulation of protein autoubiquitinationIDA:ParkinsonsUK-UCL1 Publication
Biological Process negative regulation of RNA polymerase II regulatory region sequence-specific DNA bindingIDA:ParkinsonsUK-UCL1 Publication
Biological Process negative regulation of transcription by RNA polymerase IIIMP:ParkinsonsUK-UCL1 Publication
Biological Process negative regulation of ubiquitin-dependent protein catabolic processIMP:ParkinsonsUK-UCL1 Publication
Biological Process peptidyl-serine phosphorylationIDA:BHF-UCL1 Publication
Biological Process peptidyl-threonine phosphorylationIDA:BHF-UCL2 Publications
Biological Process positive regulation of androgen receptor activityIDA:ParkinsonsUK-UCL1 Publication
Biological Process positive regulation of proteasomal ubiquitin-dependent protein catabolic processIDA:BHF-UCL1 Publication
Biological Process positive regulation of protein bindingIDA:ParkinsonsUK-UCL1 Publication
Biological Process positive regulation of transcription initiation by RNA polymerase IIIDA:ComplexPortal1 Publication
Biological Process protein autophosphorylationIDA:ParkinsonsUK-UCL3 Publications
Biological Process protein phosphorylationIDA:ParkinsonsUK-UCL1 Publication
Biological Process protein polyubiquitinationIDA:ParkinsonsUK-UCL1 Publication
Biological Process protein stabilizationIDA:ParkinsonsUK-UCL1 Publication
Biological Process regulation of cell cycle G1/S phase transitionTAS:ParkinsonsUK-UCL1 Publication
Biological Process regulation of signal transduction by p53 class mediatorTAS:Reactome
Biological Process RNA polymerase II preinitiation complex assemblyIPI:ComplexPortal1 Publication
Biological Process transcription by RNA polymerase IIIGI:BHF-UCL1 Publication
Biological Process transcription factor catabolic processIDA:ParkinsonsUK-UCL1 Publication
Biological Process transcription initiation at RNA polymerase I promoterIGI:ParkinsonsUK-UCL1 Publication
Biological Process transcription initiation at RNA polymerase II promoterIDA:BHF-UCL1 Publication
Biological Process ubiquitin-dependent protein catabolic processIDA:ParkinsonsUK-UCL1 Publication

Nucleus

Dystonia 3, torsion, X-linked (DYT3):
An 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.
Intellectual developmental disorder, X-linked, syndromic 33 (MRXS33):
A syndrome characterized by intellectual deficit, delayed psychomotor development, delayed speech and language, and characteristic facial features.

Phosphorylated by casein kinase II in vitro.