TAF1
entrez
6872
canonical
uniprot
P21675
canonical
ensembl
ENSG00000147133
resolver
ensp
ENSP00000276072
resolver
ensp
ENSP00000362895
resolver
ensp
ENSP00000406549
resolver
ensp
ENSP00000506729
resolver
ensp
ENSP00000506996
resolver
ensp
ENSP00000507781
resolver
ensp
ENSP00000783326
resolver
enst
ENST00000683782
resolver
genesymbol
TAF1
resolver
genesymbol_syn
BA2R
resolver
genesymbol_syn
CCG1
resolver
genesymbol_syn
CCGS
resolver
genesymbol_syn
TAF2A
resolver
hgnc
HGNC:11535
resolver
uniprot
A0A804HIC2
resolver
uniprot
A5CVC8
resolver
uniprot
A5CVC9
resolver
uniprot
A5CVD0
resolver
uniprot
A5CVD1
resolver
uniprot
B1Q2X3
resolver
uniprot
Q59FZ3
resolver
uniprot
Q6IUZ1
resolver
uniprot
Q70Q86
resolver
uniprot
Q70Q87
resolver
uniprot
Q70T00
resolver
uniprot
Q70T01
resolver
uniprot
Q70T02
resolver
uniprot
Q70T03
resolver
uniprot_entry
A0A804HIC2_HUMAN
resolver
uniprot_entry
TAF1_HUMAN
resolver
uniprot_sec
A5CVC8
resolver
uniprot_sec
A5CVC9
resolver
uniprot_sec
A5CVD0
resolver
uniprot_sec
A5CVD1
resolver
uniprot_sec
B1Q2X3
resolver
uniprot_sec
Q59FZ3
resolver
uniprot_sec
Q6IUZ1
resolver
uniprot_sec
Q70Q86
resolver
uniprot_sec
Q70Q87
resolver
uniprot_sec
Q70T00
resolver
uniprot_sec
Q70T01
resolver
uniprot_sec
Q70T02
resolver
uniprot_sec
Q70T03
resolver
activity_regulation
ACTIVITY REGULATION: Autophosphorylates on Ser residues (PubMed:8625415). Inhibited by retinoblastoma tumor suppressor protein, RB1 (PubMed:9858607). Binding to TAF7 or CIITA inhibits the histone acetyltransferase activity (PubMed:11592977, PubMed:22711989). {ECO:0000269|PubMed:11592977, ECO:0000269|PubMed:22711989, ECO:0000269|PubMed:8625415, ECO:0000269|PubMed:9858607}.
uniprot
proteins
amino_acid_sequence
MGPGCDLLLRTAATITAAAIMSDTDSDEDSAGGGPFSLAGFLFGNINGAGQLEGESVLDDECKKHLAGLGALGLGSLITELTANEELTGTDGALVNDEGWVRSTEDAVDYSDINEVAEDESRRYQQTMGSLQPLCHSDYDEDDYDADCEDIDCKLMPPPPPPPGPMKKDKDQDSITGVSENGEGIILPSIIAPSSLASEKVDFSSSSDSESEMGPQEATQAESEDGKLTLPLAGIMQHDATKLLPSVTELFPEFRPGKVLRFLRLFGPGKNVPSVWRSARRKRKKKHRELIQEEQIQEVECSVESEVSQKSLWNYDYAPPPPPEQCLSDDEITMMAPVESKFSQSTGDIDKVTDTKPRVAEWRYGPARLWYDMLGVPEDGSGFDYGFKLRKTEHEPVIKSRMIEEFRKLEENNGTDLLADENFLMVTQLHWEDDIIWDGEDVKHKGTKPQRASLAGWLPSSMTRNAMAYNVQQGFAATLDDDKPWYSIFPIDNEDLVYGRWEDNIIWDAQAMPRLLEPPVLTLDPNDENLILEIPDEKEEATSNSPSKESKKESSLKKSRILLGKTGVIKEEPQQNMSQPEVKDPWNLSNDEYYYPKQQGLRGTFGGNIIQHSIPAVELRQPFFPTHMGPIKLRQFHRPPLKKYSFGALSQPGPHSVQPLLKHIKKKAKMREQERQASGGGEMFFMRTPQDLTGKDGDLILAEYSEENGPLMMQVGMATKIKNYYKRKPGKDPGAPDCKYGETVYCHTSPFLGSLHPGQLLQAFENNLFRAPIYLHKMPETDFLIIRTRQGYYIRELVDIFVVGQQCPLFEVPGPNSKRANTHIRDFLQVFIYRLFWKSKDRPRRIRMEDIKKAFPSHSESSIRKRLKLCADFKRTGMDSNWWVLKSDFRLPTEEEIRAMVSPEQCCAYYSMIAAEQRLKDAGYGEKSFFAPEEENEEDFQMKIDDEVRTAPWNTTRAFIAAMKGKCLLEVTGVADPTGCGEGFSYVKIPNKPTQQKDDKEPQPVKKTVTGTDADLRRLSLKNAKQLLRKFGVPEEEIKKLSRWEVIDVVRTMSTEQARSGEGPMSKFARGSRFSVAEHQERYKEECQRIFDLQNKVLSSTEVLSTDTDSSSAEDSDFEEMGKNIENMLQNKKTSSQLSREREEQERKELQRMLLAAGSAASGNNHRDDDTASVTSLNSSATGRCLKIYRTFRDEEGKEYVRCETVRKPAVIDAYVRIRTTKDEEFIRKFALFDEQHREEMRKERRRIQEQLRRLKRNQEKEKLKGPPEKKPKKMKERPDLKLKCGACGAIGHMRTNKFCPLYYQTNAPPSNPVAMTEEQEEELEKTVIHNDNEELIKVEGTKIVLGKQLIESADEVRRKSLVLKFPKQQLPPKKKRRVGTTVHCDYLNRPHKSIHRRRTDPMVTLSSILESIINDMRDLPNTYPFHTPVNAKVVKDYYKIITRPMDLQTLRENVRKRLYPSREEFREHLELIVKNSATYNGPKHSLTQISQSMLDLCDEKLKEKEDKLARLEKAINPLLDDDDQVAFSFILDNIVTQKMMAVPDSWPFHHPVNKKFVPDYYKVIVNPMDLETIRKNISKHKYQSRESFLDDVNLILANSVKYNGPESQYTKTAQEIVNVCYQTLTEYDEHLTQLEKDICTAKEAALEEAELESLDPMTPGPYTPQPPDLYDTNTSLSMSRDASVFQDESNMSVLDIPSATPEKQVTQEGEDGDGDLADEEEGTVQQPQASVLYEDLLMSEGEDDEEDAGSDEEGDNPFSAIQLSESGSDSDVGSGGIRPKQPRMLQENTRMDMENEESMMSYEGDGGEASHGLEDSNISYGSYEEPDPKSNTQDTSFSSIGGYEVSEEEEDEEEEEQRSGPSVLSQVHLSEDEEDSEDFHSIAGDSDLDSDE
uniprot
proteins
disease_involvement
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: Intellectual developmental disorder, X-linked, syndromic 33 (MRXS33) [MIM:300966]: A syndrome characterized by intellectual deficit, delayed psychomotor development, delayed speech and language, and characteristic facial features. {ECO:0000269|PubMed:26637982}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.1.48
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: 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). {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:33795473, ECO:0000269|PubMed:8450888, ECO:0000269|PubMed:8625415, ECO:0000269|PubMed:9660973, ECO:0000269|PubMed:9858607}.
uniprot
proteins
mass_dalton
214714
uniprot
proteins
mutagenesis
MUTAGEN 137; /note="S->A: No decrease in kinase activity."; /evidence="ECO:0000269|PubMed:9660973"; MUTAGEN 145; /note="D->A: Reduces kinase activity; when associated with A-147; A-149; A-150; A-152 and A-154."; /evidence="ECO:0000269|PubMed:9660973"; MUTAGEN 147; /note="D->A: Reduces kinase activity; when associated with A-145; A-149; A-150; A-152 and A-154."; /evidence="ECO:0000269|PubMed:9660973"; MUTAGEN 149; /note="E->A: Reduces kinase activity; when associated with A-145; A-147; A-150; A-152 and A-154."; /evidence="ECO:0000269|PubMed:9660973"; MUTAGEN 150; /note="D->A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-152 and A-154."; /evidence="ECO:0000269|PubMed:9660973"; MUTAGEN 152; /note="D->A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-154."; /evidence="ECO:0000269|PubMed:9660973"; MUTAGEN 154; /note="K->A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-152."; /evidence="ECO:0000269|PubMed:9660973"; MUTAGEN 326; /note="C->A: Reduces kinase activity; when associated with A-328; A-329; A-330 and A-331."; /evidence="ECO:0000269|PubMed:9660973"; MUTAGEN 328; /note="S->A: Reduces kinase activity; when associated with A-326; A-329; A-330 and A-331."; /evidence="ECO:0000269|PubMed:9660973"; MUTAGEN 329; /note="D->A: Reduces kinase activity; when associated with A-326; A-328; A-330 and A-331."; /evidence="ECO:0000269|PubMed:9660973"; MUTAGEN 330; /note="D->A: Reduces kinase activity; when associated with A-326; A-328; A-329 and A-331."; /evidence="ECO:0000269|PubMed:9660973"; MUTAGEN 331; /note="E->A: Reduces kinase activity; when associated with A-326; A-328; A-329 and A-330."; /evidence="ECO:0000269|PubMed:9660973"; MUTAGEN 742; /note="E->Q: 25% decrease in histone acetylation."; /evidence="ECO:0000269|PubMed:15870300"; MUTAGEN 848..850; /note="Missing: Dramatic decrease in histone acetylation."; /evidence="ECO:0000269|PubMed:15870300
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by casein kinase II in vitro. {ECO:0000269|PubMed:8625415}.
uniprot
proteins
protein_family
TAF1 family
uniprot
proteins
pubmed
10759893
uniprot
proteins
pubmed
10827952
uniprot
proteins
pubmed
11278496
uniprot
proteins
pubmed
11592977
uniprot
proteins
pubmed
12093919
uniprot
proteins
pubmed
12842904
uniprot
proteins
pubmed
12928496
uniprot
proteins
pubmed
15053879
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
15870300
uniprot
proteins
pubmed
15960975
uniprot
proteins
pubmed
17273961
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17952504
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
2038334
uniprot
proteins
pubmed
22464331
uniprot
proteins
pubmed
22711989
uniprot
proteins
pubmed
23184149
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25412659
uniprot
proteins
pubmed
25593309
uniprot
proteins
pubmed
25644381
uniprot
proteins
pubmed
26365797
uniprot
proteins
pubmed
26637982
uniprot
proteins
pubmed
27007846
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
3169001
uniprot
proteins
pubmed
33795473
uniprot
proteins
pubmed
7680771
uniprot
proteins
pubmed
8450888
uniprot
proteins
pubmed
8625415
uniprot
proteins
pubmed
8647434
uniprot
proteins
pubmed
8649420
uniprot
proteins
pubmed
9660973
uniprot
proteins
pubmed
9858607
uniprot
proteins
sequence_length
1893
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:2038334, ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:27007846}.
uniprot
proteins