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Protein

Transcription initiation factor TFIID subunit 1

Gene

Taf1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Largest component and core scaffold of the complex. Contains N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. Possesses DNA-binding activity. Essential for progression of the G1 phase of the cell cycle. Negative regulator of the TATA box-binding activity of Tbp.3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Autophosphorylates on Ser residues.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: FlyBase
  • histone acetyltransferase activity Source: FlyBase
  • protein kinase activity Source: FlyBase
  • protein serine/threonine kinase activity Source: FlyBase
  • RNA polymerase II transcription factor activity, TBP-class protein binding, involved in preinitiation complex assembly Source: FlyBase
  • sequence-specific DNA binding Source: FlyBase
  • transcription factor binding Source: FlyBase

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • DNA-templated transcription, initiation Source: BHF-UCL
  • histone acetylation Source: FlyBase
  • neurogenesis Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • positive regulation of transcription initiation from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of transcription of Notch receptor target Source: FlyBase
  • protein complex assembly Source: FlyBase
  • protein phosphorylation Source: FlyBase
  • regulation of cell cycle Source: FlyBase
  • regulation of JAK-STAT cascade Source: FlyBase
  • regulation of transcription, DNA-templated Source: FlyBase
  • RNA polymerase II transcriptional preinitiation complex assembly Source: BHF-UCL
  • transcription initiation from RNA polymerase II promoter Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-DME-674695. RNA Polymerase II Pre-transcription Events.
R-DME-73776. RNA Polymerase II Promoter Escape.
R-DME-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-DME-75953. RNA Polymerase II Transcription Initiation.
R-DME-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor TFIID subunit 1 (EC:2.7.11.1)
Alternative name(s):
TAFII250
TBP-associated factor 230 kDa
Short name:
p230
Transcription initiation factor TFIID 230 kDa subunit
Short name:
TAFII-230
Gene namesi
Name:Taf1
Synonyms:TAF250
ORF Names:CG17603
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0010355. Taf1.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: FlyBase
  • nucleoplasm Source: FlyBase
  • nucleus Source: FlyBase
  • transcription factor TFIID complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21292129Transcription initiation factor TFIID subunit 1PRO_0000211216Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei286 – 2861Phosphoserine1 Publication
Modified residuei288 – 2881Phosphoserine1 Publication
Modified residuei290 – 2901Phosphoserine1 Publication
Modified residuei315 – 3151Phosphoserine; by autocatalysisBy similarity
Modified residuei603 – 6031Phosphoserine1 Publication
Modified residuei1740 – 17401Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP51123.
PRIDEiP51123.

PTM databases

iPTMnetiP51123.

Expressioni

Gene expression databases

BgeeiP51123.
ExpressionAtlasiP51123. differential.
GenevisibleiP51123. DM.

Interactioni

Subunit structurei

Belongs to the TFIID complex which is composed of TATA binding protein (Tbp) and a number of TBP-associated factors (Tafs). Taf1 is the largest component of the TFIID complex. Interacts with Tbp, Taf2, Taf4 and Taf6.4 Publications

GO - Molecular functioni

  • transcription factor binding Source: FlyBase

Protein-protein interaction databases

BioGridi66011. 16 interactions.
DIPiDIP-228N.
IntActiP51123. 7 interactions.
MINTiMINT-788336.
STRINGi7227.FBpp0293442.

Structurei

Secondary structure

1
2129
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 264Combined sources
Turni30 – 323Combined sources
Beta strandi42 – 443Combined sources
Turni50 – 523Combined sources
Helixi53 – 564Combined sources
Turni60 – 623Combined sources
Helixi64 – 696Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TBANMR-A11-77[»]
DisProtiDP00081.
ProteinModelPortaliP51123.
SMRiP51123. Positions 11-77, 633-1024, 1098-1130.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51123.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 423423Protein kinase 1Add
BLAST
Domaini1487 – 155771Bromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini1515 – 2065551Protein kinase 2Add
BLAST
Domaini1609 – 167971Bromo 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1442 – 14487Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2056 – 212065Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the TAF1 family.Curated
Contains 2 bromo domains.PROSITE-ProRule annotation
Contains 2 protein kinase domains.Curated

Keywords - Domaini

Bromodomain, Repeat

Phylogenomic databases

eggNOGiKOG0008. Eukaryota.
COG5076. LUCA.
COG5179. LUCA.
GeneTreeiENSGT00390000012659.
InParanoidiP51123.
KOiK03125.
OrthoDBiEOG7QNVK2.
PhylomeDBiP51123.

Family and domain databases

Gene3Di1.10.1100.10. 1 hit.
1.20.920.10. 2 hits.
InterProiIPR017956. AT_hook_DNA-bd_motif.
IPR001487. 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.
SMARTiSM00384. AT_hook. 2 hits.
SM00297. 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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B (identifier: P51123-1) [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
MEMESDNSDD EGSIGNGLDL TGILFGNIDS EGRLLQDDDG EGRGGTGFDA
60 70 80 90 100
ELRENIGSLS KLGLDSMLLE VIDLKEAEPP SDDEEEEDAR PSAVSASEGM
110 120 130 140 150
SAFDALKAGV KREDGAVKAQ DDAIDYSDIT ELSEDCPRTP PEETSTYDDL
160 170 180 190 200
EDAIPASKVE AKLTKDDKEL MPPPSAPMRS GSGGGIEEPA KSNDASSPSD
210 220 230 240 250
DSKSTDSKDA DRKLDTPLAD ILPSKYQNVD VRELFPDFRP QKVLRFSRLF
260 270 280 290 300
GPGKPTSLPQ IWRHVRKRRR KRNQSRDQKT TNTGGSDSPS DTEEPRKRGF
310 320 330 340 350
SLHYAAEPTP AECMSDDEDK LLGDFNSEDV RPEGPDNGEN SDQKPKVADW
360 370 380 390 400
RFGPAQIWYD MLEVPDSGEG FNYGFKTKAA STSSQPQLKD ERRVKSPEDD
410 420 430 440 450
VEDPSIADDA FLMVSQLHWE DDVVWDGNDI KAKVLQKLNS KTNAAGWLPS
460 470 480 490 500
SGSRTAGAFS QPGKPSMPVG SGSSKQGSGA SSKKAQQNAQ AKPAEAPDDT
510 520 530 540 550
WYSLFPVENE ELIYYKWEDE VIWDAQQVSK VPKPKVLTLD PNDENIILGI
560 570 580 590 600
PDDIDPSKIN KSTGPPPKIK IPHPHVKKSK ILLGKAGVIN VLAEDTPPPP
610 620 630 640 650
PKSPDRDPFN ISNDTYYTPK TEPTLRLKVG GNLIQHSTPV VELRAPFVPT
660 670 680 690 700
HMGPMKLRAF HRPPLKKYSH GPMAQSIPHP VFPLLKTIAK KAKQREVERI
710 720 730 740 750
ASGGGDVFFM RNPEDLSGRD GDIVLAEFCE EHPPLINQVG MCSKIKNYYK
760 770 780 790 800
RKAEKDSGPQ DFVYGEVAFA HTSPFLGILH PGQCIQAIEN NMYRAPIYPH
810 820 830 840 850
KMAHNDFLVI RTRNNYWIRS VNSIYTVGQE CPLYEVPGPN SKRANNFTRD
860 870 880 890 900
FLQVFIYRLF WKSRDNPRRI RMDDIKQAFP AHSESSIRKR LKQCADFKRT
910 920 930 940 950
GMDSNWWVIK PEFRLPSEEE IRAMVSPEQC CAYFSMIAAE QRLKDAGYGE
960 970 980 990 1000
KFLFAPQEDD DEEAQLKLDD EVKVAPWNTT RAYIQAMRGK CLLQLSGPAD
1010 1020 1030 1040 1050
PTGCGEGFSY VRVPNKPTQT KEEQESQPKR SVTGTDADLR RLPLQRAKEL
1060 1070 1080 1090 1100
LRQFKVPEEE IKKLSRWEVI DVVRTLSTEK AKAGEEGMDK FSRGNRFSIA
1110 1120 1130 1140 1150
EHQERYKEEC QRIFDLQNRV LASSEVLSTD EAESSASEES DLEELGKNLE
1160 1170 1180 1190 1200
NMLSNKKTST QLSREREELE RQELLRQLDE EHGGPSGSGG AKGAKGKDDP
1210 1220 1230 1240 1250
GQQMLATNNQ GRILRITRTF RGNDGKEYTR VETVRRQPVI DAYIKIRTTK
1260 1270 1280 1290 1300
DEQFIKQFAT LDEQQKEEMK REKRRIQEQL RRIKRNQERE RLAQLAQNQK
1310 1320 1330 1340 1350
LQPGGMPTSL GDPKSSGGHS HKERDSGYKE VSPSRKKFKL KPDLKLKCGA
1360 1370 1380 1390 1400
CGQVGHMRTN KACPLYSGMQ SSLSQSNPSL ADDFDEQSEK EMTMDDDDLV
1410 1420 1430 1440 1450
NVDGTKVTLS SKILKRHGGD DGKRRSGSSS GFTLKVPRDA MGKKKRRVGG
1460 1470 1480 1490 1500
DLHCDYLQRH NKTANRRRTD PVVVLSSILE IIHNELRSMP DVSPFLFPVS
1510 1520 1530 1540 1550
AKKVPDYYRV VTKPMDLQTM REYIRQRRYT SREMFLEDLK QIVDNSLIYN
1560 1570 1580 1590 1600
GPQSAYTLAA QRMFSSCFEL LAEREDKLMR LEKAINPLLD DDDQVALSFI
1610 1620 1630 1640 1650
FDKLHSQIKQ LPESWPFLKP VNKKQVKDYY TVIKRPMDLE TIGKNIEAHR
1660 1670 1680 1690 1700
YHSRAEYLAD IELIATNCEQ YNGSDTRYTK FSKKILEYAQ TQLIEFSEHC
1710 1720 1730 1740 1750
GQLENNIAKT QERARENAPE FDEAWGNDDY NFDRGSRASS PGDDYIDVEG
1760 1770 1780 1790 1800
HGGHASSSNS IHRSMGAEAG SSHTAPAVRK PAPPGPGEVK RGRGRPRKQR
1810 1820 1830 1840 1850
DPVEEVKSQN PVKRGRGRPR KDSLASNMSH TQAYFLDEDL QCSTDDEDDD
1860 1870 1880 1890 1900
EEEDFQEVSE DENNAASILD QGERINAPAD AMDGMFDPKN IKTEIDLEAH
1910 1920 1930 1940 1950
QMAEEPIGED DSQQVAEAMV QLSGVGGYYA QQQQDESMDV DPNYDPSDFL
1960 1970 1980 1990 2000
AMHKQRQSLG EPSSLQGAFT NFLSHEQDDN GPYNPAEAST SAASGADLGM
2010 2020 2030 2040 2050
DASMAMQMAP EMPVNTMNNG MGIDDDLDIS ESDEEDDGSR VRIKKEVFDD
2060 2070 2080 2090 2100
GDYALQHQQM GQAASQSQIY MVDSSNEPTT LDYQQPPQLD FQQVQEMEQL
2110 2120
QHQVMPPMQS EQLQQQQTPQ GDNDYAWTF
Note: No experimental confirmation available.
Length:2,129
Mass (Da):239,315
Last modified:July 19, 2005 - v3
Checksum:i6BF505E5A3EFF160
GO
Isoform A (identifier: P51123-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1805-1837: Missing.
     1904-1934: Missing.

Show »
Length:2,065
Mass (Da):232,222
Checksum:i221BAAC465AB224A
GO
Isoform C (identifier: P51123-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1904-1934: Missing.

Note: No experimental confirmation available.
Show »
Length:2,098
Mass (Da):235,978
Checksum:i7656922A4291CA4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 981E → G in AAB26991 (PubMed:8504928).Curated
Sequence conflicti113 – 1131E → EERE AA sequence (PubMed:8504928).Curated
Sequence conflicti169 – 1691E → D in AAO47866 (PubMed:12537569).Curated
Sequence conflicti267 – 2682KR → QS in AAB26991 (PubMed:8504928).Curated
Sequence conflicti361 – 3611M → I in AAB26991 (PubMed:8504928).Curated
Sequence conflicti386 – 3861P → Q in AAB26991 (PubMed:8504928).Curated
Sequence conflicti656 – 6572KL → NV in AAB26991 (PubMed:8504928).Curated
Sequence conflicti670 – 6712HG → QR (PubMed:8464492).Curated
Sequence conflicti762 – 7621F → Y in AAB26991 (PubMed:8504928).Curated
Sequence conflicti932 – 9321A → G (PubMed:8464492).Curated
Sequence conflicti966 – 9661L → M (PubMed:8464492).Curated
Sequence conflicti1088 – 10881M → I in AAO47866 (PubMed:12537569).Curated
Sequence conflicti1420 – 14201D → G (PubMed:8464492).Curated
Sequence conflicti1437 – 14371P → G (PubMed:8464492).Curated
Sequence conflicti1462 – 14621K → E in AAO47866 (PubMed:12537569).Curated
Sequence conflicti1472 – 14721V → G (PubMed:8464492).Curated
Sequence conflicti1487 – 14871R → G (PubMed:8464492).Curated
Sequence conflicti1525 – 15262RQ → AKGGTRVARC (PubMed:8464492).Curated
Sequence conflicti1534 – 15341M → N (PubMed:8464492).Curated
Sequence conflicti1611 – 16111L → LG (PubMed:8464492).Curated
Sequence conflicti1680 – 16801K → E in AAO47866 (PubMed:12537569).Curated
Sequence conflicti1685 – 16851I → IRYTKFSKKI (PubMed:8464492).Curated
Sequence conflicti2072 – 20721V → G (PubMed:8464492).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti572 – 5721P → S.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1805 – 183733Missing in isoform A. 2 PublicationsVSP_014794Add
BLAST
Alternative sequencei1904 – 193431Missing in isoform A and isoform C. 2 PublicationsVSP_014795Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S61883 mRNA. Translation: AAB26991.2.
AE001572 Genomic DNA. Translation: AAD19815.1.
AE014297 Genomic DNA. Translation: AAF54102.3.
AE014297 Genomic DNA. Translation: AAS65116.1.
AE014297 Genomic DNA. Translation: AAS65117.1.
BT004888 mRNA. Translation: AAO47866.1.
PIRiA47371.
RefSeqiNP_476956.3. NM_057608.5. [P51123-2]
NP_996159.1. NM_206437.2. [P51123-3]
NP_996160.1. NM_206438.2. [P51123-1]
UniGeneiDm.7380.

Genome annotation databases

EnsemblMetazoaiFBtr0081685; FBpp0089369; FBgn0010355. [P51123-1]
GeneIDi40813.
KEGGidme:Dmel_CG17603.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S61883 mRNA. Translation: AAB26991.2.
AE001572 Genomic DNA. Translation: AAD19815.1.
AE014297 Genomic DNA. Translation: AAF54102.3.
AE014297 Genomic DNA. Translation: AAS65116.1.
AE014297 Genomic DNA. Translation: AAS65117.1.
BT004888 mRNA. Translation: AAO47866.1.
PIRiA47371.
RefSeqiNP_476956.3. NM_057608.5. [P51123-2]
NP_996159.1. NM_206437.2. [P51123-3]
NP_996160.1. NM_206438.2. [P51123-1]
UniGeneiDm.7380.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1TBANMR-A11-77[»]
DisProtiDP00081.
ProteinModelPortaliP51123.
SMRiP51123. Positions 11-77, 633-1024, 1098-1130.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66011. 16 interactions.
DIPiDIP-228N.
IntActiP51123. 7 interactions.
MINTiMINT-788336.
STRINGi7227.FBpp0293442.

PTM databases

iPTMnetiP51123.

Proteomic databases

PaxDbiP51123.
PRIDEiP51123.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0081685; FBpp0089369; FBgn0010355. [P51123-1]
GeneIDi40813.
KEGGidme:Dmel_CG17603.

Organism-specific databases

CTDi6872.
FlyBaseiFBgn0010355. Taf1.

Phylogenomic databases

eggNOGiKOG0008. Eukaryota.
COG5076. LUCA.
COG5179. LUCA.
GeneTreeiENSGT00390000012659.
InParanoidiP51123.
KOiK03125.
OrthoDBiEOG7QNVK2.
PhylomeDBiP51123.

Enzyme and pathway databases

ReactomeiR-DME-674695. RNA Polymerase II Pre-transcription Events.
R-DME-73776. RNA Polymerase II Promoter Escape.
R-DME-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-DME-75953. RNA Polymerase II Transcription Initiation.
R-DME-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Miscellaneous databases

EvolutionaryTraceiP51123.
GenomeRNAii40813.
PROiP51123.

Gene expression databases

BgeeiP51123.
ExpressionAtlasiP51123. differential.
GenevisibleiP51123. DM.

Family and domain databases

Gene3Di1.10.1100.10. 1 hit.
1.20.920.10. 2 hits.
InterProiIPR017956. AT_hook_DNA-bd_motif.
IPR001487. 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.
SMARTiSM00384. AT_hook. 2 hits.
SM00297. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Drosophila 230-kD TFIID subunit, a functional homolog of the human cell cycle gene product, negatively regulates DNA binding of the TATA box-binding subunit of TFIID."
    Kokubo T., Gong D.-W., Yamashita S., Horikoshi M., Roeder R.G., Nakatani Y.
    Genes Dev. 7:1033-1046(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 63-75 AND 540-546, FUNCTION.
  2. "Complete sequence of the Antennapedia complex of Drosophila."
    Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A., Palazzolo M.J.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Berkeley.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Largest subunit of Drosophila transcription factor IID directs assembly of a complex containing TBP and a coactivator."
    Weinzierl R.O., Dynlacht B.D., Tjian R.
    Nature 362:511-517(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 658-2129 (ISOFORM B), INTERACTION WITH TBP AND TAF4.
  7. "TAFII250 is a bipartite protein kinase that phosphorylates the base transcription factor RAP74."
    Dikstein R., Ruppert S., Tjian R.
    Cell 84:781-790(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOPHOSPHORYLATION, ATP-BINDING.
  8. "Cloning and expression of Drosophila TAFII60 and human TAFII70 reveal conserved interactions with other subunits of TFIID."
    Weinzierl R.O., Ruppert S., Dynlacht B.D., Tanese N., Tjian R.
    EMBO J. 12:5303-5309(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF6.
    Strain: Oregon-R.
  9. "The Drosophila 110-kDa transcription factor TFIID subunit directly interacts with the N-terminal region of the 230-kDa subunit."
    Kokubo T., Gong D.-W., Roeder R.G., Horikoshi M., Nakatani Y.
    Proc. Natl. Acad. Sci. U.S.A. 90:5896-5900(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF4.
    Tissue: Embryo.
  10. "Drosophila TAFII150: similarity to yeast gene TSM-1 and specific binding to core promoter DNA."
    Verrijzer C.P., Yokomori K., Chen J.-L., Tjian R.
    Science 264:933-941(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF2.
    Tissue: Embryo.
  11. "TAF1 activates transcription by phosphorylation of serine 33 in histone H2B."
    Maile T., Kwoczynski S., Katzenberger R.J., Wassarman D.A., Sauer F.
    Science 304:1010-1014(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CAUTION.
  12. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; SER-288; SER-290; SER-603 AND SER-1740, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  13. "Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP."
    Liu D., Ishima R., Tong K.I., Bagby S., Kokubo T., Muhandiram D.R., Kay L.E., Nakatani Y., Ikura M.
    Cell 94:573-583(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 11-77, FUNCTION.

Entry informationi

Entry nameiTAF1_DROME
AccessioniPrimary (citable) accession number: P51123
Secondary accession number(s): O97068
, Q7KSX6, Q7KSX7, Q86LF7, Q9TX96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 19, 2005
Last modified: June 8, 2016
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

The C-terminal Ser/Thr kinase domain was reported to phosphorylate histone H2B at 'Ser-33' (PubMed:15143281). However, the paper was retracted because some data, results and conclusions in the paper are not reliable.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.