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Protein

Transcription initiation factor TFIID subunit 1

Gene

TAF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).10 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.
Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Cofactori

Enzyme regulationi

Autophosphorylates on Ser residues. Inhibited by retinoblastoma tumor suppressor protein, RB1. Binding to TAF1 or CIITA inhibits the histone acetyltransferase activity.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi1195 – 1273HMG boxAdd BLAST79

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • histone acetyltransferase activity Source: UniProtKB
  • kinase activity Source: ParkinsonsUK-UCL
  • lysine-acetylated histone binding Source: BHF-UCL
  • p53 binding Source: BHF-UCL
  • protein heterodimerization activity Source: ParkinsonsUK-UCL
  • protein serine/threonine kinase activity Source: UniProtKB
  • RNA polymerase II core promoter sequence-specific DNA binding Source: ParkinsonsUK-UCL
  • RNA polymerase II transcription factor activity, TBP-class protein binding, involved in preinitiation complex assembly Source: GO_Central
  • sequence-specific DNA binding Source: BHF-UCL
  • TBP-class protein binding Source: BHF-UCL
  • transcription coactivator activity Source: BHF-UCL
  • transcription factor binding Source: BHF-UCL
  • ubiquitin conjugating enzyme activity Source: ParkinsonsUK-UCL

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cellular response to ATP Source: ParkinsonsUK-UCL
  • cellular response to DNA damage stimulus Source: ParkinsonsUK-UCL
  • cellular response to UV Source: ParkinsonsUK-UCL
  • DNA-templated transcription, initiation Source: BHF-UCL
  • midbrain development Source: ParkinsonsUK-UCL
  • negative regulation of gene expression Source: ParkinsonsUK-UCL
  • negative regulation of protein autoubiquitination Source: ParkinsonsUK-UCL
  • negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
  • negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding Source: ParkinsonsUK-UCL
  • peptidyl-serine phosphorylation Source: BHF-UCL
  • peptidyl-threonine phosphorylation Source: BHF-UCL
  • positive regulation of androgen receptor activity Source: ParkinsonsUK-UCL
  • positive regulation of cell proliferation Source: ParkinsonsUK-UCL
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: BHF-UCL
  • positive regulation of protein binding Source: ParkinsonsUK-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase I promoter Source: ParkinsonsUK-UCL
  • positive regulation of transcription initiation from RNA polymerase II promoter Source: BHF-UCL
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: ParkinsonsUK-UCL
  • protein polyubiquitination Source: ParkinsonsUK-UCL
  • protein stabilization Source: ParkinsonsUK-UCL
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
  • regulation of cell cycle G1/S phase transition Source: ParkinsonsUK-UCL
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage Source: ParkinsonsUK-UCL
  • regulation of transcription initiation from RNA polymerase II promoter Source: ParkinsonsUK-UCL
  • RNA polymerase II transcriptional preinitiation complex assembly Source: BHF-UCL
  • transcription elongation from RNA polymerase II promoter Source: Reactome
  • transcription factor catabolic process Source: ParkinsonsUK-UCL
  • transcription from RNA polymerase II promoter Source: Reactome
  • transcription initiation from RNA polymerase II promoter Source: Reactome
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000147133-MONOMER.
ReactomeiR-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
SIGNORiP21675.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor TFIID subunit 1 (EC:2.3.1.48, EC:2.7.11.1)
Alternative name(s):
Cell cycle gene 1 protein
TBP-associated factor 250 kDa
Short name:
p250
Transcription initiation factor TFIID 250 kDa subunit
Short name:
TAF(II)250
Short name:
TAFII-250
Short name:
TAFII250
Gene namesi
Name:TAF1
Synonyms:BA2R, CCG1, CCGS, TAF2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:11535. TAF1.

Subcellular locationi

GO - Cellular componenti

  • MLL1 complex Source: UniProtKB
  • nuclear chromatin Source: ParkinsonsUK-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: ParkinsonsUK-UCL
  • transcription factor complex Source: ParkinsonsUK-UCL
  • transcription factor TFIID complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Dystonia 3, torsion, X-linked (DYT3)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:314250
Mental retardation, X-linked, syndromic, 33 (MRXS33)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:300966
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076394575P → S in MRXS33. 1 Publication1
Natural variantiVAR_076395786C → R in MRXS33. 1 Publication1
Natural variantiVAR_076396955D → H in MRXS33. 1 Publication1
Natural variantiVAR_0763971225R → W in MRXS33. 1 Publication1
Natural variantiVAR_0763981316I → T in MRXS33. 1 Publication1
Natural variantiVAR_0763991431R → H in MRXS33; unknown pathological significance. 1 Publication1
Natural variantiVAR_0764001496N → H in MRXS33; unknown pathological significance. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi137S → A: No decrease in kinase activity. 1 Publication1
Mutagenesisi145D → A: Reduces kinase activity; when associated with A-147; A-149; A-150; A-152 and A-154. 1 Publication1
Mutagenesisi147D → A: Reduces kinase activity; when associated with A-145; A-149; A-150; A-152 and A-154. 1 Publication1
Mutagenesisi149E → A: Reduces kinase activity; when associated with A-145; A-147; A-150; A-152 and A-154. 1 Publication1
Mutagenesisi150D → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-152 and A-154. 1 Publication1
Mutagenesisi152D → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-154. 1 Publication1
Mutagenesisi154K → A: Reduces kinase activity; when associated with A-145; A-147; A-149; A-150 and A-152. 1 Publication1
Mutagenesisi305C → A: Reduces kinase activity; when associated with A-307; A-308; A-309 and A-310. 1 Publication1
Mutagenesisi307S → A: Reduces kinase activity; when associated with A-305; A-308; A-309 and A-310. 1 Publication1
Mutagenesisi308D → A: Reduces kinase activity; when associated with A-305; A-307; A-309 and A-310. 1 Publication1
Mutagenesisi309D → A: Reduces kinase activity; when associated with A-305; A-307; A-308 and A-310. 1 Publication1
Mutagenesisi310E → A: Reduces kinase activity; when associated with A-305; A-307; A-308 and A-309. 1 Publication1
Mutagenesisi721E → Q: 25% decrease in histone acetylation. 1 Publication1
Mutagenesisi827 – 829Missing : Dramatic decrease in histone acetylation. 1 Publication3

Keywords - Diseasei

Disease mutation, Dystonia, Mental retardation, Parkinsonism

Organism-specific databases

DisGeNETi6872.
MalaCardsiTAF1.
MIMi300966. phenotype.
314250. phenotype.
OpenTargetsiENSG00000147133.
Orphaneti53351. X-linked dystonia-parkinsonism.
PharmGKBiPA36310.

Chemistry databases

ChEMBLiCHEMBL3217390.

Polymorphism and mutation databases

BioMutaiTAF1.
DMDMi115942.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002112151 – 1872Transcription initiation factor TFIID subunit 1Add BLAST1872

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei137Phosphoserine; by autocatalysis1 Publication1
Modified residuei307Phosphoserine; by autocatalysisCombined sources1 Publication1
Modified residuei544N6-acetyllysineBy similarity1
Modified residuei1669PhosphoserineBy similarity1
Modified residuei1672PhosphoserineBy similarity1
Modified residuei1778PhosphoserineBy similarity1
Modified residuei1781PhosphoserineBy similarity1
Modified residuei1799PhosphoserineBy similarity1
Modified residuei1826PhosphoserineCombined sources1
Isoform 3 (identifier: P21675-3)
Modified residuei1697PhosphoserineCombined sources1
Isoform 4 (identifier: P21675-4)
Modified residuei1700PhosphoserineCombined sources1
Isoform 2a (identifier: P21675-5)
Modified residuei1700PhosphoserineCombined sources1
Isoform 2g (identifier: P21675-9)
Modified residuei1702PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by casein kinase II in vitro.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP21675.
MaxQBiP21675.
PaxDbiP21675.
PeptideAtlasiP21675.
PRIDEiP21675.

PTM databases

iPTMnetiP21675.
PhosphoSitePlusiP21675.

Expressioni

Gene expression databases

BgeeiENSG00000147133.
ExpressionAtlasiP21675. baseline and differential.
GenevisibleiP21675. HS.

Organism-specific databases

HPAiCAB016283.
HPA001075.

Interactioni

Subunit structurei

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). Interacts with SV40 Large T antigen (PubMed:8647434). Interacts with herpes simplex virus 1 ICP4 (PubMed:8649420).12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P032553EBI-491289,EBI-2603114From a different organism.
GTF2F1P352693EBI-491289,EBI-457886
TBPP202265EBI-491289,EBI-355371

GO - Molecular functioni

  • lysine-acetylated histone binding Source: BHF-UCL
  • p53 binding Source: BHF-UCL
  • protein heterodimerization activity Source: ParkinsonsUK-UCL
  • TBP-class protein binding Source: BHF-UCL
  • transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi112735. 72 interactors.
DIPiDIP-147N.
IntActiP21675. 34 interactors.
MINTiMINT-1211825.
STRINGi9606.ENSP00000276072.

Chemistry databases

BindingDBiP21675.

Structurei

Secondary structure

11872
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi593 – 596Combined sources4
Turni600 – 602Combined sources3
Helixi609 – 613Combined sources5
Turni614 – 616Combined sources3
Beta strandi624 – 626Combined sources3
Helixi627 – 629Combined sources3
Beta strandi630 – 632Combined sources3
Beta strandi634 – 638Combined sources5
Helixi640 – 655Combined sources16
Turni656 – 658Combined sources3
Helixi668 – 671Combined sources4
Beta strandi675 – 685Combined sources11
Beta strandi697 – 704Combined sources8
Beta strandi708 – 710Combined sources3
Beta strandi718 – 724Combined sources7
Beta strandi729 – 732Combined sources4
Beta strandi739 – 756Combined sources18
Beta strandi761 – 767Combined sources7
Beta strandi770 – 774Combined sources5
Beta strandi778 – 782Combined sources5
Helixi797 – 817Combined sources21
Beta strandi820 – 822Combined sources3
Beta strandi824 – 826Combined sources3
Helixi827 – 833Combined sources7
Helixi839 – 847Combined sources9
Beta strandi850 – 853Combined sources4
Beta strandi856 – 858Combined sources3
Beta strandi861 – 864Combined sources4
Helixi873 – 879Combined sources7
Helixi882 – 900Combined sources19
Helixi905 – 907Combined sources3
Helixi925 – 928Combined sources4
Helixi931 – 942Combined sources12
Beta strandi947 – 952Combined sources6
Beta strandi958 – 962Combined sources5
Beta strandi964 – 968Combined sources5
Helixi1055 – 1078Combined sources24
Helixi1381 – 1397Combined sources17
Helixi1403 – 1405Combined sources3
Beta strandi1406 – 1408Combined sources3
Turni1411 – 1413Combined sources3
Helixi1417 – 1420Combined sources4
Helixi1427 – 1435Combined sources9
Helixi1442 – 1460Combined sources19
Beta strandi1462 – 1464Combined sources3
Helixi1465 – 1483Combined sources19
Helixi1485 – 1495Combined sources11
Turni1497 – 1500Combined sources4
Helixi1502 – 1517Combined sources16
Turni1518 – 1521Combined sources4
Helixi1526 – 1528Combined sources3
Turni1534 – 1536Combined sources3
Helixi1540 – 1543Combined sources4
Helixi1550 – 1558Combined sources9
Helixi1565 – 1583Combined sources19
Helixi1588 – 1606Combined sources19
Helixi1608 – 1634Combined sources27

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EQFX-ray2.10A1359-1638[»]
3AADX-ray3.30A1342-1629[»]
3UV4X-ray1.89A/B1501-1635[»]
3UV5X-ray2.03A1373-1635[»]
4RGWX-ray2.30A579-1215[»]
4YYMX-ray1.50A/B1497-1638[»]
4YYNX-ray1.85A/B1497-1638[»]
5FURelectron microscopy8.50G1-1872[»]
5I1QX-ray1.50A1497-1638[»]
5I29X-ray1.21A1497-1638[»]
ProteinModelPortaliP21675.
SMRiP21675.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21675.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 414Protein kinase 1Add BLAST414
Domaini1397 – 1467Bromo 1PROSITE-ProRule annotationAdd BLAST71
Domaini1425 – 1872Protein kinase 2Add BLAST448
Domaini1520 – 1590Bromo 2PROSITE-ProRule annotationAdd BLAST71

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni517 – 976Histone acetyltransferase (HAT)Add BLAST460
Regioni1342 – 1629Interaction with ASF1A and ASF1B1 PublicationAdd BLAST288

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1351 – 1358Nuclear localization signalSequence analysis8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi157 – 165Pro-rich9
Compositional biasi1627 – 1872Asp/Glu-rich (acidic tail)Add BLAST246

Sequence similaritiesi

Belongs to the TAF1 family.Curated
Contains 2 bromo domains.PROSITE-ProRule annotation
Contains 1 HMG box DNA-binding domain.Curated
Contains 2 protein kinase domains.Curated

Keywords - Domaini

Bromodomain, Repeat

Phylogenomic databases

eggNOGiKOG0008. Eukaryota.
COG5076. LUCA.
COG5179. LUCA.
GeneTreeiENSGT00390000012659.
HOGENOMiHOG000020066.
HOVERGENiHBG050223.
InParanoidiP21675.
KOiK03125.
OMAiFYYPKQQ.
OrthoDBiEOG091G00MO.
PhylomeDBiP21675.
TreeFamiTF313573.

Family and domain databases

Gene3Di1.10.1100.10. 1 hit.
1.20.920.10. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR011177. TAF1_animal.
IPR009067. TAF_II_230-bd.
IPR022591. TFIID_sub1_DUF3591.
[Graphical view]
PfamiPF00439. Bromodomain. 2 hits.
PF12157. DUF3591. 1 hit.
PF09247. TBP-binding. 1 hit.
[Graphical view]
PIRSFiPIRSF003047. TAF1_animal. 1 hit.
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 2 hits.
[Graphical view]
SUPFAMiSSF47055. SSF47055. 1 hit.
SSF47370. SSF47370. 2 hits.
PROSITEiPS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
[Graphical view]

Sequences (12)i

Sequence statusi: Complete.

This entry describes 12 isoformsi produced by alternative splicing. AlignAdd to basket

Note: the TAF1/DYT3 multiple transcript system is composed of 38 evolutionary conserved exons plus 5 downstream exons referred to as exons d1-d5 that are primate-specific. Multiple highly polymorphic variants can be generated by splicing exons d3 and d4 to various combinations of exons 1-37.
Isoform 1 (identifier: P21675-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGPGCDLLLR TAATITAAAI MSDTDSDEDS AGGGPFSLAG FLFGNINGAG
60 70 80 90 100
QLEGESVLDD ECKKHLAGLG ALGLGSLITE LTANEELTGT DGALVNDEGW
110 120 130 140 150
VRSTEDAVDY SDINEVAEDE SRRYQQTMGS LQPLCHSDYD EDDYDADCED
160 170 180 190 200
IDCKLMPPPP PPPGPMKKDK DQDSITGEKV DFSSSSDSES EMGPQEATQA
210 220 230 240 250
ESEDGKLTLP LAGIMQHDAT KLLPSVTELF PEFRPGKVLR FLRLFGPGKN
260 270 280 290 300
VPSVWRSARR KRKKKHRELI QEEQIQEVEC SVESEVSQKS LWNYDYAPPP
310 320 330 340 350
PPEQCLSDDE ITMMAPVESK FSQSTGDIDK VTDTKPRVAE WRYGPARLWY
360 370 380 390 400
DMLGVPEDGS GFDYGFKLRK TEHEPVIKSR MIEEFRKLEE NNGTDLLADE
410 420 430 440 450
NFLMVTQLHW EDDIIWDGED VKHKGTKPQR ASLAGWLPSS MTRNAMAYNV
460 470 480 490 500
QQGFAATLDD DKPWYSIFPI DNEDLVYGRW EDNIIWDAQA MPRLLEPPVL
510 520 530 540 550
TLDPNDENLI LEIPDEKEEA TSNSPSKESK KESSLKKSRI LLGKTGVIKE
560 570 580 590 600
EPQQNMSQPE VKDPWNLSND EYYYPKQQGL RGTFGGNIIQ HSIPAVELRQ
610 620 630 640 650
PFFPTHMGPI KLRQFHRPPL KKYSFGALSQ PGPHSVQPLL KHIKKKAKMR
660 670 680 690 700
EQERQASGGG EMFFMRTPQD LTGKDGDLIL AEYSEENGPL MMQVGMATKI
710 720 730 740 750
KNYYKRKPGK DPGAPDCKYG ETVYCHTSPF LGSLHPGQLL QAFENNLFRA
760 770 780 790 800
PIYLHKMPET DFLIIRTRQG YYIRELVDIF VVGQQCPLFE VPGPNSKRAN
810 820 830 840 850
THIRDFLQVF IYRLFWKSKD RPRRIRMEDI KKAFPSHSES SIRKRLKLCA
860 870 880 890 900
DFKRTGMDSN WWVLKSDFRL PTEEEIRAMV SPEQCCAYYS MIAAEQRLKD
910 920 930 940 950
AGYGEKSFFA PEEENEEDFQ MKIDDEVRTA PWNTTRAFIA AMKGKCLLEV
960 970 980 990 1000
TGVADPTGCG EGFSYVKIPN KPTQQKDDKE PQPVKKTVTG TDADLRRLSL
1010 1020 1030 1040 1050
KNAKQLLRKF GVPEEEIKKL SRWEVIDVVR TMSTEQARSG EGPMSKFARG
1060 1070 1080 1090 1100
SRFSVAEHQE RYKEECQRIF DLQNKVLSST EVLSTDTDSS SAEDSDFEEM
1110 1120 1130 1140 1150
GKNIENMLQN KKTSSQLSRE REEQERKELQ RMLLAAGSAA SGNNHRDDDT
1160 1170 1180 1190 1200
ASVTSLNSSA TGRCLKIYRT FRDEEGKEYV RCETVRKPAV IDAYVRIRTT
1210 1220 1230 1240 1250
KDEEFIRKFA LFDEQHREEM RKERRRIQEQ LRRLKRNQEK EKLKGPPEKK
1260 1270 1280 1290 1300
PKKMKERPDL KLKCGACGAI GHMRTNKFCP LYYQTNAPPS NPVAMTEEQE
1310 1320 1330 1340 1350
EELEKTVIHN DNEELIKVEG TKIVLGKQLI ESADEVRRKS LVLKFPKQQL
1360 1370 1380 1390 1400
PPKKKRRVGT TVHCDYLNRP HKSIHRRRTD PMVTLSSILE SIINDMRDLP
1410 1420 1430 1440 1450
NTYPFHTPVN AKVVKDYYKI ITRPMDLQTL RENVRKRLYP SREEFREHLE
1460 1470 1480 1490 1500
LIVKNSATYN GPKHSLTQIS QSMLDLCDEK LKEKEDKLAR LEKAINPLLD
1510 1520 1530 1540 1550
DDDQVAFSFI LDNIVTQKMM AVPDSWPFHH PVNKKFVPDY YKVIVNPMDL
1560 1570 1580 1590 1600
ETIRKNISKH KYQSRESFLD DVNLILANSV KYNGPESQYT KTAQEIVNVC
1610 1620 1630 1640 1650
YQTLTEYDEH LTQLEKDICT AKEAALEEAE LESLDPMTPG PYTPQPPDLY
1660 1670 1680 1690 1700
DTNTSLSMSR DASVFQDESN MSVLDIPSAT PEKQVTQEGE DGDGDLADEE
1710 1720 1730 1740 1750
EGTVQQPQAS VLYEDLLMSE GEDDEEDAGS DEEGDNPFSA IQLSESGSDS
1760 1770 1780 1790 1800
DVGSGGIRPK QPRMLQENTR MDMENEESMM SYEGDGGEAS HGLEDSNISY
1810 1820 1830 1840 1850
GSYEEPDPKS NTQDTSFSSI GGYEVSEEEE DEEEEEQRSG PSVLSQVHLS
1860 1870
EDEEDSEDFH SIAGDSDLDS DE
Length:1,872
Mass (Da):212,677
Last modified:May 1, 1992 - v2
Checksum:i93BE3D181A72ABEB
GO
Isoform 2 (identifier: P21675-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     177-177: G → GVSENGEGIILPSIIAPSSLAS

Show »
Length:1,893
Mass (Da):214,714
Checksum:iAE148C222B418BB4
GO
Isoform 3 (identifier: P21675-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1684-1686: Missing.
     1687-1687: Q → QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP
     1799-1872: SYGSYEEPDP...AGDSDLDSDE → RYQ

Show »
Length:1,832
Mass (Da):208,364
Checksum:i6C51A0F5885FF667
GO
Isoform 4 (identifier: P21675-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1687-1687: Q → QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP

Show »
Length:1,906
Mass (Da):216,451
Checksum:i8880885A3D444515
GO
Isoform 2a (identifier: P21675-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1687-1687: Q → QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP
     1799-1872: SYGSYEEPDP...AGDSDLDSDE → RYQ

Show »
Length:1,835
Mass (Da):208,693
Checksum:i4EF338B27B304C13
GO
Isoform 2c (identifier: P21675-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1799-1872: SYGSYEEPDP...AGDSDLDSDE → RYQ

Show »
Length:1,801
Mass (Da):204,919
Checksum:i245D4080FB804D6D
GO
Isoform 2d (identifier: P21675-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1645-1645: Q → QAK
     1799-1872: SYGSYEEPDP...AGDSDLDSDE → RYQ

Show »
Length:1,803
Mass (Da):205,118
Checksum:i1B90B7A234BDB92C
GO
Isoform 2e (identifier: P21675-8) [UniParc]FASTAAdd to basket
Also known as: 2F

The sequence of this isoform differs from the canonical sequence as follows:
     1585-1592: PESQYTKT → YMCTTCRT
     1593-1872: Missing.

Show »
Length:1,592
Mass (Da):182,054
Checksum:i72C8271DD47EE24D
GO
Isoform 2g (identifier: P21675-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1645-1645: Q → QAK
     1687-1687: Q → QMRQGRGRLGEEDSDVDIEGYDDEEEDGKPKTPAP
     1799-1872: SYGSYEEPDP...AGDSDLDSDE → RYQ

Show »
Length:1,837
Mass (Da):208,892
Checksum:i5165FAF620722AD3
GO
Isoform 2h (identifier: P21675-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1525-1528: SWPF → IITK
     1529-1872: Missing.

Show »
Length:1,528
Mass (Da):174,433
Checksum:i75267CFDD8211DD6
GO
Isoform 2i (identifier: P21675-11) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1525-1540: SWPFHHPVNKKFVPDY → VSCLCAKYFLAISSPS
     1541-1872: Missing.

Show »
Length:1,540
Mass (Da):175,648
Checksum:i4DC37D3B71D7AA10
GO
Isoform N-TAF1 (identifier: P21675-12) [UniParc]FASTAAdd to basket
Also known as: TA14-391

The sequence of this isoform differs from the canonical sequence as follows:
     177-177: G → GVSENGEGIILPSIIAPSSLAS
     1645-1645: Q → QAK

Note: Only detected in brain, highest expression in the caudate nucleus.
Show »
Length:1,895
Mass (Da):214,913
Checksum:i68B48D4582D8A090
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_020678269L → V.2 PublicationsCorresponds to variant rs28382158dbSNPEnsembl.1
Natural variantiVAR_041930297A → G.1 PublicationCorresponds to variant rs35317750dbSNPEnsembl.1
Natural variantiVAR_041931453G → D in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_076394575P → S in MRXS33. 1 Publication1
Natural variantiVAR_041932651E → K in a metastatic melanoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_041933691M → I in a lung bronchoalveolar carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_076395786C → R in MRXS33. 1 Publication1
Natural variantiVAR_076396955D → H in MRXS33. 1 Publication1
Natural variantiVAR_0763971225R → W in MRXS33. 1 Publication1
Natural variantiVAR_0763981316I → T in MRXS33. 1 Publication1
Natural variantiVAR_0484331383V → I.Corresponds to variant rs7050748dbSNPEnsembl.1
Natural variantiVAR_0763991431R → H in MRXS33; unknown pathological significance. 1 Publication1
Natural variantiVAR_0764001496N → H in MRXS33; unknown pathological significance. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_012362177G → GVSENGEGIILPSIIAPSSL AS in isoform 2 and isoform N-TAF1. 1 Publication1
Alternative sequenceiVSP_0533761525 – 1540SWPFH…FVPDY → VSCLCAKYFLAISSPS in isoform 2i. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_0533751525 – 1528SWPF → IITK in isoform 2h. 1 Publication4
Alternative sequenceiVSP_0533771529 – 1872Missing in isoform 2h. 1 PublicationAdd BLAST344
Alternative sequenceiVSP_0533781541 – 1872Missing in isoform 2i. 1 PublicationAdd BLAST332
Alternative sequenceiVSP_0533791585 – 1592PESQYTKT → YMCTTCRT in isoform 2e. 2 Publications8
Alternative sequenceiVSP_0533801593 – 1872Missing in isoform 2e. 2 PublicationsAdd BLAST280
Alternative sequenceiVSP_0533811645Q → QAK in isoform 2d, isoform 2g and isoform N-TAF1. 3 Publications1
Alternative sequenceiVSP_0533821684 – 1686Missing in isoform 3. 1 Publication3
Alternative sequenceiVSP_0533831687Q → QMRQGRGRLGEEDSDVDIEG YDDEEEDGKPKTPAP in isoform 2g, isoform 2a, isoform 3 and isoform 4. 3 Publications1
Alternative sequenceiVSP_0533841799 – 1872SYGSY…LDSDE → RYQ in isoform 2g, isoform 2a, isoform 2c, isoform 2d and isoform 3. 2 PublicationsAdd BLAST74

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90359 mRNA. Translation: BAA14374.1.
X07024 mRNA. Translation: CAA30073.1. Sequence problems.
AB300418 mRNA. Translation: BAG15901.1.
AY623109 Genomic DNA. Translation: AAT38105.1.
AL590762 Genomic DNA. No translation available.
AL590763 Genomic DNA. No translation available.
AB209316 mRNA. Translation: BAD92553.1.
AJ549247 mRNA. Translation: CAD70490.1.
AJ549248 mRNA. Translation: CAD70491.3.
AJ549249 mRNA. Translation: CAD70492.2.
AJ549250 mRNA. Translation: CAD70493.3.
AJ555148 mRNA. Translation: CAD87527.2.
AJ555149 mRNA. Translation: CAD87528.2.
AM711892 mRNA. Translation: CAM98555.1.
AM711893 mRNA. Translation: CAM98556.1.
AM711894 mRNA. Translation: CAM98557.1.
AM711895 mRNA. Translation: CAM98558.1.
CCDSiCCDS14412.1. [P21675-2]
CCDS35325.1. [P21675-1]
CCDS69783.1. [P21675-12]
PIRiA40262.
RefSeqiNP_001273003.1. NM_001286074.1. [P21675-12]
NP_004597.2. NM_004606.4. [P21675-2]
NP_620278.1. NM_138923.3. [P21675-1]
XP_005262354.1. XM_005262297.4. [P21675-4]
UniGeneiHs.158560.

Genome annotation databases

EnsembliENST00000276072; ENSP00000276072; ENSG00000147133. [P21675-2]
ENST00000373790; ENSP00000362895; ENSG00000147133. [P21675-1]
ENST00000423759; ENSP00000406549; ENSG00000147133. [P21675-12]
GeneIDi6872.
KEGGihsa:6872.
UCSCiuc004dzt.6. human. [P21675-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90359 mRNA. Translation: BAA14374.1.
X07024 mRNA. Translation: CAA30073.1. Sequence problems.
AB300418 mRNA. Translation: BAG15901.1.
AY623109 Genomic DNA. Translation: AAT38105.1.
AL590762 Genomic DNA. No translation available.
AL590763 Genomic DNA. No translation available.
AB209316 mRNA. Translation: BAD92553.1.
AJ549247 mRNA. Translation: CAD70490.1.
AJ549248 mRNA. Translation: CAD70491.3.
AJ549249 mRNA. Translation: CAD70492.2.
AJ549250 mRNA. Translation: CAD70493.3.
AJ555148 mRNA. Translation: CAD87527.2.
AJ555149 mRNA. Translation: CAD87528.2.
AM711892 mRNA. Translation: CAM98555.1.
AM711893 mRNA. Translation: CAM98556.1.
AM711894 mRNA. Translation: CAM98557.1.
AM711895 mRNA. Translation: CAM98558.1.
CCDSiCCDS14412.1. [P21675-2]
CCDS35325.1. [P21675-1]
CCDS69783.1. [P21675-12]
PIRiA40262.
RefSeqiNP_001273003.1. NM_001286074.1. [P21675-12]
NP_004597.2. NM_004606.4. [P21675-2]
NP_620278.1. NM_138923.3. [P21675-1]
XP_005262354.1. XM_005262297.4. [P21675-4]
UniGeneiHs.158560.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EQFX-ray2.10A1359-1638[»]
3AADX-ray3.30A1342-1629[»]
3UV4X-ray1.89A/B1501-1635[»]
3UV5X-ray2.03A1373-1635[»]
4RGWX-ray2.30A579-1215[»]
4YYMX-ray1.50A/B1497-1638[»]
4YYNX-ray1.85A/B1497-1638[»]
5FURelectron microscopy8.50G1-1872[»]
5I1QX-ray1.50A1497-1638[»]
5I29X-ray1.21A1497-1638[»]
ProteinModelPortaliP21675.
SMRiP21675.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112735. 72 interactors.
DIPiDIP-147N.
IntActiP21675. 34 interactors.
MINTiMINT-1211825.
STRINGi9606.ENSP00000276072.

Chemistry databases

BindingDBiP21675.
ChEMBLiCHEMBL3217390.

PTM databases

iPTMnetiP21675.
PhosphoSitePlusiP21675.

Polymorphism and mutation databases

BioMutaiTAF1.
DMDMi115942.

Proteomic databases

EPDiP21675.
MaxQBiP21675.
PaxDbiP21675.
PeptideAtlasiP21675.
PRIDEiP21675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000276072; ENSP00000276072; ENSG00000147133. [P21675-2]
ENST00000373790; ENSP00000362895; ENSG00000147133. [P21675-1]
ENST00000423759; ENSP00000406549; ENSG00000147133. [P21675-12]
GeneIDi6872.
KEGGihsa:6872.
UCSCiuc004dzt.6. human. [P21675-1]

Organism-specific databases

CTDi6872.
DisGeNETi6872.
GeneCardsiTAF1.
GeneReviewsiTAF1.
HGNCiHGNC:11535. TAF1.
HPAiCAB016283.
HPA001075.
MalaCardsiTAF1.
MIMi300966. phenotype.
313650. gene.
314250. phenotype.
neXtProtiNX_P21675.
OpenTargetsiENSG00000147133.
Orphaneti53351. X-linked dystonia-parkinsonism.
PharmGKBiPA36310.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0008. Eukaryota.
COG5076. LUCA.
COG5179. LUCA.
GeneTreeiENSGT00390000012659.
HOGENOMiHOG000020066.
HOVERGENiHBG050223.
InParanoidiP21675.
KOiK03125.
OMAiFYYPKQQ.
OrthoDBiEOG091G00MO.
PhylomeDBiP21675.
TreeFamiTF313573.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000147133-MONOMER.
ReactomeiR-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
SIGNORiP21675.

Miscellaneous databases

EvolutionaryTraceiP21675.
GeneWikiiTAF1.
GenomeRNAii6872.
PROiP21675.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000147133.
ExpressionAtlasiP21675. baseline and differential.
GenevisibleiP21675. HS.

Family and domain databases

Gene3Di1.10.1100.10. 1 hit.
1.20.920.10. 2 hits.
InterProiIPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR011177. TAF1_animal.
IPR009067. TAF_II_230-bd.
IPR022591. TFIID_sub1_DUF3591.
[Graphical view]
PfamiPF00439. Bromodomain. 2 hits.
PF12157. DUF3591. 1 hit.
PF09247. TBP-binding. 1 hit.
[Graphical view]
PIRSFiPIRSF003047. TAF1_animal. 1 hit.
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 2 hits.
[Graphical view]
SUPFAMiSSF47055. SSF47055. 1 hit.
SSF47370. SSF47370. 2 hits.
PROSITEiPS00633. BROMODOMAIN_1. 2 hits.
PS50014. BROMODOMAIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTAF1_HUMAN
AccessioniPrimary (citable) accession number: P21675
Secondary accession number(s): A5CVC8
, A5CVC9, A5CVD0, A5CVD1, B1Q2X3, Q59FZ3, Q6IUZ1, Q70Q86, Q70Q87, Q70T00, Q70T01, Q70T02, Q70T03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1992
Last modified: November 30, 2016
This is version 191 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.