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Reviewed, UniProtKB/Swiss-Prot Q24325 (TAF2_DROME)

Last modified November 4, 2008. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Transcription initiation factor TFIID subunit 2
Alternative name(s):
    Transcription initiation factor TFIID 150 kDa subunit
      Short name=TAFII-150
      Short name=TAFII150
Gene names
Name: Taf2
Synonyms: TAF150
ORF Names: CG6711
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length1221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. An essential subunit binds to core promoter DNA.

Subunit structure

Belongs to the TFIID complex which is composed of TATA binding protein (Tbp) and a number of TBP-associated factors (TAFs). Interacts with Tbp, Taf1, Taf11 and Taf12.

Subcellular location

Nucleus.

Sequence similarities

Belongs to the TAF2 family.

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Ontologies

Keywords

   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing

Gene Ontology (GO)

   Biological processregulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12211221Transcription initiation factor TFIID subunit 2
PRO_0000118866

Regions

Region845 – 1213369Binds to Tbp and Taf1
Region1138 – 118346Highly charged

Amino acid modifications

Modified residue11351Phosphoserine
Modified residue11361Phosphoserine

Experimental info

Sequence conflict531R → S in CAA55830. Ref.1
Sequence conflict881H → P in CAA55830. Ref.1
Sequence conflict1175 – 122147DKDKE…PMNLN → ERKDKDKRDPHISRLQAARQ PLRTLSARRTVATAIACRP AA sequence Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q24325-1 [UniParc].

Last modified January 27, 2003. Version 2.
Checksum: C2DC066826B1AF6E

FASTA1,221139,499
        10         20         30         40         50         60 
METQPEVPEV PLRPFKLAHQ VVSLTGISFE RRSIIGVVEL TIVPNSENLR LIRLNAKQLR 

        70         80         90        100        110        120 
IYSVVLNDVC QADFTYFDPF QNICYKEHKS RALEVYSKHH LTAAQYTDPD VNNGELLIQV 

       130        140        150        160        170        180 
PPEGYSMIQE GQGLRIRIEF SLENPKCGVH FVIPPASTDE ETQMNSSHMF TNCYENSSRL 

       190        200        210        220        230        240 
WFPCVDSFAD PCTWRLEFTV DKNMTAVSCG ELLEVIMTPD LRKKTFHYSV STPVCAPNIA 

       250        260        270        280        290        300 
LAVGQFEIYV DPHMHEVTHF CLPGLLPLLK NTVRYLHEAF EFYEETLSTR YPFSCYKQVF 

       310        320        330        340        350        360 
VDELDTDISA YATMSIASVN LLHSIAIIDQ TYISRTFMSR AVAEQFFGCF ITSHHWSDTW 

       370        380        390        400        410        420 
LAKGIAEYLC GLYSRKCFGN NEYRAWVQSE LARVVRYEEQ YGGIILDCSQ PPAPLPVSGT 

       430        440        450        460        470        480 
NQSAASSKQQ EIVHYFPIKS LHTVSPKYVE AMRRKAHFVI RMLENRIGQE LLIQVFNKQL 

       490        500        510        520        530        540 
ALASSAATTK IGAGLWSQLL ISTNIFIKAI FTVTGKDMSV FMDQWVRTGG HAKFSLTSVF 

       550        560        570        580        590        600 
NRKRNTIELE IRQDYVNQRG IRKYNGPLMV QLQELDGTFK HTLQIESTLV KSDITCHSKS 

       610        620        630        640        650        660 
RRNKKKKIPL CTGEEVDMDL SAMDDSPVLW IRLDPEMILL RDLIIEQPDF QWQYQLRHER 

       670        680        690        700        710        720 
DVTAQFQAIQ ALQKYPTNAT RLALTDTIES ERCFYQVRCE AAHSLTKVAN QMVASWSGPP 

       730        740        750        760        770        780 
AMLNIFRKFF GSFSAPHIIK LNNFSNFQLY FLQKAIPVAM AGLRTSHGIC PPEVMRFLFD 

       790        800        810        820        830        840 
LFKYNENSRN HYTDAYYRAA LVEALGETLT PVVSVAIHGT QITTDSLSTD AKLVLDEVTR 

       850        860        870        880        890        900 
LLNMEKHLPS YKYMVSVSCL KVIRKLQKFG HLPSLPHIYR SYAEYGIYLD LRIAAMECLV 

       910        920        930        940        950        960 
DFVKVDGRSE DLEHLITLLE TDPDPAARHA LAQLLIDNPP FTRESRSRLD KPNLVDRLWF 

       970        980        990       1000       1010       1020 
SINRLPYDTK LRCDIVDLYY ALYGTKRPNC LQAGENQSFY KDLMKDNNSS VGSVTGSFKK 

      1030       1040       1050       1060       1070       1080 
TSDSKSHLPT PTNTLDNEPQ ERQKPAMVTI KRTATEAFEV GDEIIKLERS EEITVLDEPV 

      1090       1100       1110       1120       1130       1140 
NVQAYDSETK VNALQADEEA RDTHQAAKRL KNEMYAEDDN SSTMLDVGDS TRYESSHEEG 

      1150       1160       1170       1180       1190       1200 
KLKSGDGGLK KKKKKEKKKH KHKHKHRHSK DKDKDKDKER KDKDKRDPHI SRLQARETAT 

      1210       1220 
PDTLSSEDSS NSNSLPPMNL N

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References

« Hide 'large scale' references
[1]"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: 8178153] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH TBP AND TAF1.
Tissue: Embryo.
[2]"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. expand/collapse author list , 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: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[4]"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: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[5]"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: 8276241] [Abstract]
Cited for: INTERACTION WITH TAF11 AND TAF12.
[6]"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: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1135 AND SER-1136, MASS SPECTROMETRY.
Tissue: Embryo.

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Cross-references

Sequence databases

X79243 mRNA. Translation: CAA55830.1.
AE014296 Genomic DNA. Translation: AAF50190.2.
AY070564 mRNA. Translation: AAL48035.1.
PIRA54063.
RefSeqNP_729571.1.
UniGeneDm.6380

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:255N.
IntActQ24325.

Genome annotation databases

EnsemblCG6711. Drosophila melanogaster. [Contig view]
GeneID39164.
KEGGdme:Dmel_CG6711.
NMPDRfig|7227.3.peg.9180.

Organism-specific databases

FlyBaseFBgn0011836. Taf2.

Phylogenomic databases

HOGENOMQ24325.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-016070-MON.

Gene expression databases

ArrayExpressQ24325.
GermOnlineCG6711. Drosophila melanogaster.

Family and domain databases

InterProIPR014782. Peptidase_M1_N.
[Graphical view]
PfamPF01433. Peptidase_M1. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio812285.

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Entry information

Entry nameTAF2_DROME
AccessionPrimary (citable) accession number: Q24325
Secondary accession number(s): Q8SZR7, Q9VT64
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 27, 2003
Last modified: November 4, 2008
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents