UniProt functional annotation for P21675



	UniProt functional annotation for P21675

UniProt code: P21675.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Largest component and core scaffold of the TFIID basal transcription factor complex (PubMed:25412659, PubMed:27007846). 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 (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). {ECO:0000269|PubMed:11278496, ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15870300, ECO:0000269|PubMed:2038334, ECO:0000269|PubMed:25412659, ECO:0000269|PubMed:27007846, ECO:0000269|PubMed:8450888, ECO:0000269|PubMed:8625415, ECO:0000269|PubMed:9660973, ECO:0000269|PubMed:9858607}.

Catalytic activity: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;

Catalytic activity: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;

Catalytic activity: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:15870300};

Cofactor: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;

Activity regulation: Autophosphorylates on Ser residues. Inhibited by retinoblastoma tumor suppressor protein, RB1. Binding to TAF1 or CIITA inhibits the histone acetyltransferase activity. {ECO:0000269|PubMed:22711989}.

Subunit: TAF1 is the largest component of transcription factor TFIID that is composed of TBP and a variety of TBP-associated factors (PubMed:7680771). TAF1, when part of the TFIID complex, interacts with C-terminus of TP53 (PubMed:15053879). Part of a TFIID-containing RNA polymerase II pre-initiation complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:27007846). Interacts with TAF7; the interaction is direct (PubMed:25412659). 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 (PubMed:10759893, PubMed:12093919, PubMed:12842904). Interacts (via bromo domains) with acetylated lysine residues on the N- terminus of histone H1.4, H2A, H2B, H3 and H4 (in vitro) (PubMed:22464331). {ECO:0000269|PubMed:10759893, ECO:0000269|PubMed:12093919, ECO:0000269|PubMed:12842904, ECO:0000269|PubMed:15053879, ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:22464331, ECO:0000269|PubMed:25412659, ECO:0000269|PubMed:27007846, ECO:0000269|PubMed:7680771, ECO:0000269|PubMed:9858607}.

Subunit: (Microbial infection) Interacts with SV40 Large T antigen. {ECO:0000269|PubMed:8647434}.

Subunit: (Microbial infection) Interacts with herpes simplex virus 1 ICP4. {ECO:0000269|PubMed:8649420}.

Subcellular location: Nucleus {ECO:0000269|PubMed:2038334, ECO:0000269|PubMed:27007846}.

Domain: The Bromo domain mediates interaction with histones that have acetylated lysine residues at specific positions (PubMed:22464331). The second domain also recognizes and binds histones that are butyrylated and crotonylated (PubMed:26365797). {ECO:0000269|PubMed:22464331, ECO:0000269|PubMed:26365797}.

Ptm: Phosphorylated by casein kinase II in vitro. {ECO:0000269|PubMed:8625415}.

Disease: Dystonia 3, torsion, X-linked (DYT3) [MIM:314250]: 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. {ECO:0000269|PubMed:12928496, ECO:0000269|PubMed:17273961}. Note=The disease is caused by variants affecting the gene represented in this entry.

Disease: Mental retardation, X-linked, syndromic, 33 (MRXS33) [MIM:300966]: A mental retardation syndrome characterized by intellectual deficit, delayed psychomotor development, delayed speech and language, and characteristic facial features. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269|PubMed:26637982}. Note=The disease is caused by variants affecting the gene represented in this entry.

Miscellaneous: Isoforms including the downstream (d) exons are preferentially expressed in brain, and may play a role in the regulation of genes involved in dopamine processing and transport.

Miscellaneous: [Isoform N-TAF1]: Only detected in brain, highest expression in the caudate nucleus. {ECO:0000305}.

Similarity: Belongs to the TAF1 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Largest component and core scaffold of the TFIID basal transcription factor complex (PubMed:25412659, PubMed:27007846). 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 (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). {ECO:0000269\|PubMed:11278496, ECO:0000269\|PubMed:15053879, ECO:0000269\|PubMed:15870300, ECO:0000269\|PubMed:2038334, ECO:0000269\|PubMed:25412659, ECO:0000269\|PubMed:27007846, ECO:0000269\|PubMed:8450888, ECO:0000269\|PubMed:8625415, ECO:0000269\|PubMed:9660973, ECO:0000269\|PubMed:9858607}.


Catalytic activity:		Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
Catalytic activity:		Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
Catalytic activity:		Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269\|PubMed:15870300};
Cofactor:		Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Activity regulation:		Autophosphorylates on Ser residues. Inhibited by retinoblastoma tumor suppressor protein, RB1. Binding to TAF1 or CIITA inhibits the histone acetyltransferase activity. {ECO:0000269\|PubMed:22711989}.
Subunit:		TAF1 is the largest component of transcription factor TFIID that is composed of TBP and a variety of TBP-associated factors (PubMed:7680771). TAF1, when part of the TFIID complex, interacts with C-terminus of TP53 (PubMed:15053879). Part of a TFIID-containing RNA polymerase II pre-initiation complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:27007846). Interacts with TAF7; the interaction is direct (PubMed:25412659). 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 (PubMed:10759893, PubMed:12093919, PubMed:12842904). Interacts (via bromo domains) with acetylated lysine residues on the N- terminus of histone H1.4, H2A, H2B, H3 and H4 (in vitro) (PubMed:22464331). {ECO:0000269\|PubMed:10759893, ECO:0000269\|PubMed:12093919, ECO:0000269\|PubMed:12842904, ECO:0000269\|PubMed:15053879, ECO:0000269\|PubMed:15960975, ECO:0000269\|PubMed:22464331, ECO:0000269\|PubMed:25412659, ECO:0000269\|PubMed:27007846, ECO:0000269\|PubMed:7680771, ECO:0000269\|PubMed:9858607}.
Subunit:		(Microbial infection) Interacts with SV40 Large T antigen. {ECO:0000269\|PubMed:8647434}.
Subunit:		(Microbial infection) Interacts with herpes simplex virus 1 ICP4. {ECO:0000269\|PubMed:8649420}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:2038334, ECO:0000269\|PubMed:27007846}.
Domain:		The Bromo domain mediates interaction with histones that have acetylated lysine residues at specific positions (PubMed:22464331). The second domain also recognizes and binds histones that are butyrylated and crotonylated (PubMed:26365797). {ECO:0000269\|PubMed:22464331, ECO:0000269\|PubMed:26365797}.
Ptm:		Phosphorylated by casein kinase II in vitro. {ECO:0000269\|PubMed:8625415}.
Disease:		Dystonia 3, torsion, X-linked (DYT3) [MIM:314250]: 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. {ECO:0000269\|PubMed:12928496, ECO:0000269\|PubMed:17273961}. Note=The disease is caused by variants affecting the gene represented in this entry.
Disease:		Mental retardation, X-linked, syndromic, 33 (MRXS33) [MIM:300966]: A mental retardation syndrome characterized by intellectual deficit, delayed psychomotor development, delayed speech and language, and characteristic facial features. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. {ECO:0000269\|PubMed:26637982}. Note=The disease is caused by variants affecting the gene represented in this entry.
Miscellaneous:		Isoforms including the downstream (d) exons are preferentially expressed in brain, and may play a role in the regulation of genes involved in dopamine processing and transport.
Miscellaneous:		[Isoform N-TAF1]: Only detected in brain, highest expression in the caudate nucleus. {ECO:0000305}.
Similarity:		Belongs to the TAF1 family. {ECO:0000305}.