TAF2_DROME
ID TAF2_DROME Reviewed; 1221 AA.
AC Q24325; Q8SZR7; Q9VT64;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Transcription initiation factor TFIID subunit 2;
DE AltName: Full=Transcription initiation factor TFIID 150 kDa subunit;
DE Short=TAF(II)150;
DE Short=TAFII-150;
DE Short=TAFII150;
GN Name=Taf2; Synonyms=TAF150; ORFNames=CG6711;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
RP INTERACTION WITH TBP AND TAF1.
RC TISSUE=Embryo;
RX PubMed=8178153; DOI=10.1126/science.8178153;
RA Verrijzer C.P., Yokomori K., Chen J.-L., Tjian R.;
RT "Drosophila TAFII150: similarity to yeast gene TSM-1 and specific binding
RT to core promoter DNA.";
RL Science 264:933-941(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP INTERACTION WITH TAF11 AND TAF12.
RX PubMed=8276241; DOI=10.1101/gad.7.12b.2587;
RA Yokomori K., Chen J.L., Admon A., Zhou S., Tjian R.;
RT "Molecular cloning and characterization of dTAFII30 alpha and dTAFII30
RT beta: two small subunits of Drosophila TFIID.";
RL Genes Dev. 7:2587-2597(1993).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1135 AND SER-1136, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: TFIID is a multimeric protein complex that plays a central
CC role in mediating promoter responses to various activators and
CC repressors. An essential subunit binds to core promoter DNA.
CC {ECO:0000269|PubMed:8178153}.
CC -!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA binding
CC protein (Tbp) and a number of TBP-associated factors (TAFs). Interacts
CC with Tbp, Taf1, Taf11 and Taf12. {ECO:0000269|PubMed:8178153,
CC ECO:0000269|PubMed:8276241}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TAF2 family. {ECO:0000305}.
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DR EMBL; X79243; CAA55830.1; -; mRNA.
DR EMBL; AE014296; AAF50190.2; -; Genomic_DNA.
DR EMBL; AY070564; AAL48035.1; -; mRNA.
DR PIR; A54063; A54063.
DR RefSeq; NP_001261668.1; NM_001274739.1.
DR RefSeq; NP_729571.1; NM_168387.3.
DR AlphaFoldDB; Q24325; -.
DR SMR; Q24325; -.
DR BioGRID; 64551; 8.
DR DIP; DIP-255N; -.
DR IntAct; Q24325; 10.
DR STRING; 7227.FBpp0076090; -.
DR MEROPS; M01.972; -.
DR iPTMnet; Q24325; -.
DR PaxDb; Q24325; -.
DR PRIDE; Q24325; -.
DR EnsemblMetazoa; FBtr0076361; FBpp0076090; FBgn0011836.
DR EnsemblMetazoa; FBtr0332688; FBpp0304934; FBgn0011836.
DR GeneID; 39164; -.
DR KEGG; dme:Dmel_CG6711; -.
DR CTD; 6873; -.
DR FlyBase; FBgn0011836; Taf2.
DR VEuPathDB; VectorBase:FBgn0011836; -.
DR eggNOG; KOG1932; Eukaryota.
DR GeneTree; ENSGT00390000000420; -.
DR HOGENOM; CLU_002317_0_0_1; -.
DR InParanoid; Q24325; -.
DR OMA; GQESYEW; -.
DR OrthoDB; 142542at2759; -.
DR PhylomeDB; Q24325; -.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-DME-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-DME-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR BioGRID-ORCS; 39164; 1 hit in 1 CRISPR screen.
DR ChiTaRS; Taf2; fly.
DR GenomeRNAi; 39164; -.
DR PRO; PR:Q24325; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0011836; Expressed in eye disc (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q24325; baseline and differential.
DR Genevisible; Q24325; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0140296; F:general transcription initiation factor binding; IPI:FlyBase.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0017025; F:TBP-class protein binding; IPI:FlyBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:BHF-UCL.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:BHF-UCL.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:BHF-UCL.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR037813; TAF2.
DR PANTHER; PTHR15137; PTHR15137; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF63737; SSF63737; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..1221
FT /note="Transcription initiation factor TFIID subunit 2"
FT /id="PRO_0000118866"
FT REGION 845..1213
FT /note="Binds to Tbp and Taf1"
FT REGION 1011..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1111..1221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1183
FT /note="Highly charged"
FT COMPBIAS 1011..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1171
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1135
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1136
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 53
FT /note="R -> S (in Ref. 1; CAA55830)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="H -> P (in Ref. 1; CAA55830)"
FT /evidence="ECO:0000305"
FT CONFLICT 1175..1221
FT /note="DKDKERKDKDKRDPHISRLQARETATPDTLSSEDSSNSNSLPPMNLN -> E
FT RKDKDKRDPHISRLQAARQPLRTLSARRTVATAIACRP (in Ref. 1; AA
FT sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1221 AA; 139499 MW; C2DC066826B1AF6E CRC64;
METQPEVPEV PLRPFKLAHQ VVSLTGISFE RRSIIGVVEL TIVPNSENLR LIRLNAKQLR
IYSVVLNDVC QADFTYFDPF QNICYKEHKS RALEVYSKHH LTAAQYTDPD VNNGELLIQV
PPEGYSMIQE GQGLRIRIEF SLENPKCGVH FVIPPASTDE ETQMNSSHMF TNCYENSSRL
WFPCVDSFAD PCTWRLEFTV DKNMTAVSCG ELLEVIMTPD LRKKTFHYSV STPVCAPNIA
LAVGQFEIYV DPHMHEVTHF CLPGLLPLLK NTVRYLHEAF EFYEETLSTR YPFSCYKQVF
VDELDTDISA YATMSIASVN LLHSIAIIDQ TYISRTFMSR AVAEQFFGCF ITSHHWSDTW
LAKGIAEYLC GLYSRKCFGN NEYRAWVQSE LARVVRYEEQ YGGIILDCSQ PPAPLPVSGT
NQSAASSKQQ EIVHYFPIKS LHTVSPKYVE AMRRKAHFVI RMLENRIGQE LLIQVFNKQL
ALASSAATTK IGAGLWSQLL ISTNIFIKAI FTVTGKDMSV FMDQWVRTGG HAKFSLTSVF
NRKRNTIELE IRQDYVNQRG IRKYNGPLMV QLQELDGTFK HTLQIESTLV KSDITCHSKS
RRNKKKKIPL CTGEEVDMDL SAMDDSPVLW IRLDPEMILL RDLIIEQPDF QWQYQLRHER
DVTAQFQAIQ ALQKYPTNAT RLALTDTIES ERCFYQVRCE AAHSLTKVAN QMVASWSGPP
AMLNIFRKFF GSFSAPHIIK LNNFSNFQLY FLQKAIPVAM AGLRTSHGIC PPEVMRFLFD
LFKYNENSRN HYTDAYYRAA LVEALGETLT PVVSVAIHGT QITTDSLSTD AKLVLDEVTR
LLNMEKHLPS YKYMVSVSCL KVIRKLQKFG HLPSLPHIYR SYAEYGIYLD LRIAAMECLV
DFVKVDGRSE DLEHLITLLE TDPDPAARHA LAQLLIDNPP FTRESRSRLD KPNLVDRLWF
SINRLPYDTK LRCDIVDLYY ALYGTKRPNC LQAGENQSFY KDLMKDNNSS VGSVTGSFKK
TSDSKSHLPT PTNTLDNEPQ ERQKPAMVTI KRTATEAFEV GDEIIKLERS EEITVLDEPV
NVQAYDSETK VNALQADEEA RDTHQAAKRL KNEMYAEDDN SSTMLDVGDS TRYESSHEEG
KLKSGDGGLK KKKKKEKKKH KHKHKHRHSK DKDKDKDKER KDKDKRDPHI SRLQARETAT
PDTLSSEDSS NSNSLPPMNL N
