TBP
entrez
6908
canonical
uniprot
P20226
canonical
ensembl
ENSG00000112592
resolver
ensp
ENSP00000375942
resolver
ensp
ENSP00000442132
resolver
genesymbol
TBP
resolver
genesymbol_syn
GTF2D1
resolver
genesymbol_syn
TF2D
resolver
genesymbol_syn
TFIID
resolver
hgnc
HGNC:11588
resolver
uniprot
B4E3B3
resolver
uniprot
F5H869
resolver
uniprot
Q16845
resolver
uniprot
Q32MN7
resolver
uniprot
Q6IBM6
resolver
uniprot
Q9UC02
resolver
uniprot_entry
Q32MN7_HUMAN
resolver
uniprot_entry
TBP_HUMAN
resolver
uniprot_sec
B4E3B3
resolver
uniprot_sec
F5H869
resolver
uniprot_sec
Q16845
resolver
uniprot_sec
Q6IBM6
resolver
uniprot_sec
Q9UC02
resolver
amino_acid_sequence
MDQNNSLPPYAQGLASPQGAMTPGIPIFSPMMPYGTGLTPQPIQNTNSLSILEEQQRQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQAVAAAAVQQSTSQQATQGTSGQAPQLFHSQTLTTAPLPGTTPLYPSPMTPMTPITPATPASESSGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEEQSRLAARKYARVVQKLGFPAKFLDFKIQNMVGSCDVKFPIRLEGLVLTHQQFSSYEPELFPGLIYRMIKPRIVLLIFVSGKVVLTGAKVRAEIYEAFENIYPILKGFRKTT
uniprot
proteins
disease_involvement
DISEASE: Spinocerebellar ataxia 17 (SCA17) [MIM:607136]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA17 is an autosomal dominant cerebellar ataxia (ADCA) characterized by widespread cerebral and cerebellar atrophy, dementia and extrapyramidal signs. The molecular defect in SCA17 is the expansion of a CAG repeat in the coding region of TBP. Longer expansions result in earlier onset and more severe clinical manifestations of the disease. {ECO:0000269|PubMed:11313753, ECO:0000269|PubMed:11448935, ECO:0000269|PubMed:11939898}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:2194289, PubMed:2363050, PubMed:2374612, PubMed:27193682, 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:27007846, PubMed:33795473). The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (PubMed:33795473). TBP forms the TFIID-A module together with TAF3 and TAF5 (PubMed:33795473). TBP is a general transcription factor that functions at the core of the TFIID complex (PubMed:2194289, PubMed:2363050, PubMed:2374612, PubMed:27193682, PubMed:33795473, PubMed:9836642). During assembly of the core PIC on the promoter, as part of TFIID, TBP binds to and also bends promoter DNA, irrespective of whether the promoter contains a TATA box (PubMed:33795473). Component of a BRF2-containing transcription factor complex that regulates transcription mediated by RNA polymerase III (PubMed:26638071). Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC during RNA polymerase I-dependent transcription (PubMed:15970593). The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter (PubMed:15970593). SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA (PubMed:15970593). {ECO:0000269|PubMed:15970593, ECO:0000269|PubMed:2194289, ECO:0000269|PubMed:2363050, ECO:0000269|PubMed:2374612, ECO:0000269|PubMed:26638071, ECO:0000269|PubMed:27007846, ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:33795473, ECO:0000269|PubMed:9836642}.
uniprot
proteins
mass_dalton
37698
uniprot
proteins
protein_family
TBP family
uniprot
proteins
pubmed
10196196
uniprot
proteins
pubmed
10197586
uniprot
proteins
pubmed
10391676
uniprot
proteins
pubmed
10484774
uniprot
proteins
pubmed
10567404
uniprot
proteins
pubmed
10619841
uniprot
proteins
pubmed
11005381
uniprot
proteins
pubmed
11313753
uniprot
proteins
pubmed
11438666
uniprot
proteins
pubmed
11448935
uniprot
proteins
pubmed
11461703
uniprot
proteins
pubmed
11564744
uniprot
proteins
pubmed
11939898
uniprot
proteins
pubmed
12217962
uniprot
proteins
pubmed
12621023
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15280358
uniprot
proteins
pubmed
15719058
uniprot
proteins
pubmed
15970593
uniprot
proteins
pubmed
17570761
uniprot
proteins
pubmed
19106100
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
2194289
uniprot
proteins
pubmed
2363050
uniprot
proteins
pubmed
2374612
uniprot
proteins
pubmed
26638071
uniprot
proteins
pubmed
27007846
uniprot
proteins
pubmed
27193682
uniprot
proteins
pubmed
30619292
uniprot
proteins
pubmed
33795473
uniprot
proteins
pubmed
7608968
uniprot
proteins
pubmed
7801123
uniprot
proteins
pubmed
7982918
uniprot
proteins
pubmed
8121496
uniprot
proteins
pubmed
8146144
uniprot
proteins
pubmed
8392607
uniprot
proteins
pubmed
8504927
uniprot
proteins
pubmed
8643494
uniprot
proteins
pubmed
8757291
uniprot
proteins
pubmed
9748258
uniprot
proteins
pubmed
9836642
uniprot
proteins
sequence_length
339
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27007846}.
uniprot
proteins