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Protein

Transcription initiation factor TFIID subunit 4

Gene

Taf4

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. May function as a coactivator by serving as a site of protein-protein contact between activators like Sp1 (or btd) and TFIID complex.1 Publication

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • TFIIA-class transcription factor binding Source: FlyBase
  • transcription factor activity, sequence-specific DNA binding Source: InterPro
  • transcription factor binding Source: FlyBase

GO - Biological processi

  • dendrite morphogenesis Source: FlyBase
  • muscle organ development Source: FlyBase
  • neurogenesis Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • regulation of transcription, DNA-templated Source: UniProtKB
  • RNA polymerase II transcriptional preinitiation complex assembly Source: GOC
  • transcription from RNA polymerase II promoter Source: UniProtKB
  • transcription initiation from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

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 4
Alternative name(s):
110 kDa TBP-associated factor
Transcription initiation factor TFIID 110 kDa subunit
Short name:
TAFII-110
Short name:
p110
Gene namesi
Name:Taf4
Synonyms:TAF110
ORF Names:CG5444
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0010280. Taf4.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 921921Transcription initiation factor TFIID subunit 4PRO_0000118870Add
BLAST

Proteomic databases

PaxDbiP47825.
PRIDEiP47825.

Expressioni

Gene expression databases

BgeeiP47825.
ExpressionAtlasiP47825. differential.
GenevisibleiP47825. 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). Interacts with TFIIA-L when in complex with Tbp. Interacts with Taf1, Taf5, Taf11 and Taf12.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P032553EBI-277958,EBI-2603114From a different organism.

GO - Molecular functioni

  • TFIIA-class transcription factor binding Source: FlyBase
  • transcription factor binding Source: FlyBase

Protein-protein interaction databases

BioGridi65074. 20 interactions.
DIPiDIP-237N.
IntActiP47825. 6 interactions.
MINTiMINT-964448.
STRINGi7227.FBpp0113081.

Structurei

3D structure databases

ProteinModelPortaliP47825.
SMRiP47825. Positions 289-378, 711-758.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini290 – 38697TAFHPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi66 – 8217Poly-GlnAdd
BLAST
Compositional biasi108 – 1114Poly-Gln
Compositional biasi259 – 2657Poly-Gln

Sequence similaritiesi

Belongs to the TAF4 family.Curated
Contains 1 TAFH (NHR1) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2341. Eukaryota.
ENOG410XQS6. LUCA.
GeneTreeiENSGT00390000011620.
InParanoidiP47825.
KOiK03129.
OrthoDBiEOG7327N5.
PhylomeDBiP47825.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007900. TAF4.
IPR003894. TAFH_NHR1.
[Graphical view]
PfamiPF05236. TAF4. 1 hit.
PF07531. TAFH. 1 hit.
[Graphical view]
SMARTiSM00549. TAFH. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS51119. TAFH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P47825-1) [UniParc]FASTAAdd to basket

Also known as: B

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
MNTSQTAAGN RITFTSQPLP NGTISIAGNP GAVISTAQLP NTTTIKTIQA
60 70 80 90 100
GIGGQHQGLQ QVHHVQQQQQ SQQQQQQQQQ TQSAGQPLLN SMLPAGVVVG
110 120 130 140 150
MRQQAPSQQQ QKNVPTNPLS RVVINSHMAG VRPQSPSITL STLNTGQTPA
160 170 180 190 200
LLVKTDNGFQ LLRVGTTTGP PTVTQTITNT SNNSNTTSTT NHPTTTQIRL
210 220 230 240 250
QTVPAAASMT NTTATSNIIV NSVASSGYAN SSQPPHLTQL NAQAPQLPQI
260 270 280 290 300
TQIQTIPAQQ SQQQQVNNVS SAGGTATAVS STTAATTTQQ GNTKEKCRKF
310 320 330 340 350
LANLIELSTR EPKPVEKNVR TLIQELVNAN VEPEEFCDRL ERLLNASPQP
360 370 380 390 400
CLIGFLKKSL PLLRQALYTK ELVIEGIKPP PQHVLGLAGL SQQLPKIQAQ
410 420 430 440 450
IRPIGPSQTT TIGQTQVRMI TPNALGTPRP TIGHTTISKQ PPNIRLPTAP
460 470 480 490 500
RLVNTGGIRT QIPSLQVPGQ ANIVQIRGPQ HAQLQRTGSV QIRATTRPPN
510 520 530 540 550
SVPTANKLTA VKVGQTQIKA ITPSLHPPSL AAISGGPPPT PTLSVLSTLN
560 570 580 590 600
SASTTTLPIP SLPTVHLPPE ALRAREQMQN SLNHNSNHFD AKLVEIKAPS
610 620 630 640 650
LHPPHMERIN ASLTPIGAKT MARPPPAINK AIGKKKRDAM EMDAKLNTSS
660 670 680 690 700
GGAASAANSF FQQSSMSSMY GDDDINDVAA MGGVNLAEES QRILGCTENI
710 720 730 740 750
GTQIRSCKDE VFLNLPSLQA RIRAITSEAG LDEPSQDVAV LISHACQERL
760 770 780 790 800
KNIVEKLAVI AEHRIDVIKL DPRYEPAKDV RGQIKFLEEL DKAEQKRHEE
810 820 830 840 850
LEREMLLRAA KSRSRVEDPE QAKMKARAKE MQRAEMEELR QRDANLTALQ
860 870 880 890 900
AIGPRKKLKL DGETVSSGAG SSGGGVLSSS GSAPTTLRPR IKRVNLRDML
910 920
FYMEQEREFC RSSMLFKTYL K
Length:921
Mass (Da):99,338
Last modified:February 1, 1996 - v1
Checksum:i27E6852859872767
GO
Isoform C (identifier: P47825-2) [UniParc]FASTAAdd to basket

Also known as: D

The sequence of this isoform differs from the canonical sequence as follows:
     138-207: Missing.

Show »
Length:851
Mass (Da):92,061
Checksum:i9BEC6553E724D4A3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141V → M in AAL39952 (PubMed:12537569).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei138 – 20770Missing in isoform C. 2 PublicationsVSP_004441Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06861 mRNA. No translation available.
S63550 mRNA. Translation: AAB27433.1.
AE014296 Genomic DNA. Translation: AAF49535.1.
AE014296 Genomic DNA. Translation: AAO41248.1.
AY069807 mRNA. Translation: AAL39952.1.
BT025195 mRNA. Translation: ABF17886.2.
PIRiA48184.
RefSeqiNP_001163453.1. NM_001169982.2. [P47825-1]
NP_001287077.1. NM_001300148.1. [P47825-1]
NP_524102.1. NM_079378.4. [P47825-1]
NP_730109.1. NM_168651.3. [P47825-1]
NP_788511.1. NM_176333.3. [P47825-2]
NP_996101.1. NM_206379.3. [P47825-2]
UniGeneiDm.7812.

Genome annotation databases

EnsemblMetazoaiFBtr0075448; FBpp0075205; FBgn0010280. [P47825-1]
FBtr0075449; FBpp0075206; FBgn0010280. [P47825-1]
FBtr0301911; FBpp0291125; FBgn0010280. [P47825-1]
FBtr0345951; FBpp0311865; FBgn0010280. [P47825-1]
GeneIDi39765.
KEGGidme:Dmel_CG5444.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06861 mRNA. No translation available.
S63550 mRNA. Translation: AAB27433.1.
AE014296 Genomic DNA. Translation: AAF49535.1.
AE014296 Genomic DNA. Translation: AAO41248.1.
AY069807 mRNA. Translation: AAL39952.1.
BT025195 mRNA. Translation: ABF17886.2.
PIRiA48184.
RefSeqiNP_001163453.1. NM_001169982.2. [P47825-1]
NP_001287077.1. NM_001300148.1. [P47825-1]
NP_524102.1. NM_079378.4. [P47825-1]
NP_730109.1. NM_168651.3. [P47825-1]
NP_788511.1. NM_176333.3. [P47825-2]
NP_996101.1. NM_206379.3. [P47825-2]
UniGeneiDm.7812.

3D structure databases

ProteinModelPortaliP47825.
SMRiP47825. Positions 289-378, 711-758.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65074. 20 interactions.
DIPiDIP-237N.
IntActiP47825. 6 interactions.
MINTiMINT-964448.
STRINGi7227.FBpp0113081.

Proteomic databases

PaxDbiP47825.
PRIDEiP47825.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075448; FBpp0075205; FBgn0010280. [P47825-1]
FBtr0075449; FBpp0075206; FBgn0010280. [P47825-1]
FBtr0301911; FBpp0291125; FBgn0010280. [P47825-1]
FBtr0345951; FBpp0311865; FBgn0010280. [P47825-1]
GeneIDi39765.
KEGGidme:Dmel_CG5444.

Organism-specific databases

CTDi6874.
FlyBaseiFBgn0010280. Taf4.

Phylogenomic databases

eggNOGiKOG2341. Eukaryota.
ENOG410XQS6. LUCA.
GeneTreeiENSGT00390000011620.
InParanoidiP47825.
KOiK03129.
OrthoDBiEOG7327N5.
PhylomeDBiP47825.

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

ChiTaRSiTaf4. fly.
GenomeRNAii39765.
PROiP47825.

Gene expression databases

BgeeiP47825.
ExpressionAtlasiP47825. differential.
GenevisibleiP47825. DM.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007900. TAF4.
IPR003894. TAFH_NHR1.
[Graphical view]
PfamiPF05236. TAF4. 1 hit.
PF07531. TAFH. 1 hit.
[Graphical view]
SMARTiSM00549. TAFH. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS51119. TAFH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional analysis of Drosophila TAF110 reveal properties expected of coactivators."
    Hoey T., Weinzierl R.O.J., Gill G., Chen J.-L., Dynlacht B.D., Tjian R.
    Cell 72:247-260(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 519-540; 597-616 AND 857-874.
    Tissue: Embryo.
  2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 398-406; 520-540 AND 860-877, INTERACTION WITH TAF1.
    Tissue: Embryo.
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
    Strain: Berkeley.
    Tissue: Embryo.
  6. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
    Strain: Berkeley.
  7. "Drosophila TFIIA-L is processed into two subunits that are associated with the TBP/TAF complex."
    Yokomori K., Admon A., Goodrich J.A., Chen J.-L., Tjian R.
    Genes Dev. 7:2235-2245(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TFIIA-L.
    Tissue: Embryo.
  8. "Molecular cloning and characterization of dTAFII30 alpha and dTAFII30 beta: two small subunits of Drosophila TFIID."
    Yokomori K., Chen J.L., Admon A., Zhou S., Tjian R.
    Genes Dev. 7:2587-2597(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF11 AND TAF12.
  9. "Molecular cloning, expression, and characterization of the Drosophila 85-kilodalton TFIID subunit."
    Kokubo T., Gong D.-W., Yamashita S., Takada R., Roeder R.G., Horikoshi M., Nakatani Y.
    Mol. Cell. Biol. 13:7859-7863(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAF5.
    Tissue: Embryo.
  10. "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: INTERACTION WITH TAF1.

Entry informationi

Entry nameiTAF4_DROME
AccessioniPrimary (citable) accession number: P47825
Secondary accession number(s): P49845
, Q0E8E3, Q1LZ31, Q8T9E0, Q9VUY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 6, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.