TAF12_DROME
ID TAF12_DROME Reviewed; 196 AA.
AC P49905; A4V2Q1; Q26339; Q9VGK0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Transcription initiation factor TFIID subunit 12;
DE AltName: Full=TAFII30 alpha;
DE AltName: Full=Transcription initiation factor TFIID 28-alpha kDa/22 kDa subunits;
DE AltName: Full=p28-alpha/p22;
GN Name=Taf12; Synonyms=TAF30-ALPHA; ORFNames=CG17358;
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] (ISOFORMS 22 KDA AND 28 KDA), ALTERNATIVE
RP INITIATION, AND PROTEIN SEQUENCE OF 147-173.
RX PubMed=7545910; DOI=10.1038/367484a0;
RA Kokubo T., Gong D.-W., Wootton J.C., Horikoshi M., Roeder R.G.,
RA Nakatani Y.;
RT "Molecular cloning of Drosophila TFIID subunits.";
RL Nature 367:484-487(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 28 KDA), AND INTERACTION WITH TBP; TAF2
RP AND TAF4.
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 [3]
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 [4]
RP GENOME REANNOTATION, AND ALTERNATIVE INITIATION.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 28 KDA).
RC STRAIN=Berkeley; TISSUE=Embryo;
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).
CC -!- FUNCTION: TFIID is a multimeric protein complex that plays a central
CC role in mediating promoter responses to various activators and
CC repressors.
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, Taf2 and Taf4. {ECO:0000269|PubMed:8276241}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=28 kDa; Synonyms=A, B;
CC IsoId=P49905-1; Sequence=Displayed;
CC Name=22 kDa; Synonyms=D;
CC IsoId=P49905-2; Sequence=VSP_018890;
CC -!- SIMILARITY: Belongs to the TAF12 family. {ECO:0000305}.
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DR EMBL; U06450; AAC46479.1; -; mRNA.
DR EMBL; U06456; AAB19244.1; -; mRNA.
DR EMBL; S67741; AAB29540.1; -; mRNA.
DR EMBL; AE014297; AAF54677.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54678.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54679.2; -; Genomic_DNA.
DR EMBL; AY061435; AAL28983.1; -; mRNA.
DR PIR; A49453; A49453.
DR PIR; S42222; S42222.
DR RefSeq; NP_001262479.1; NM_001275550.1. [P49905-2]
DR RefSeq; NP_524320.1; NM_079596.3. [P49905-1]
DR RefSeq; NP_731616.1; NM_169420.2. [P49905-1]
DR RefSeq; NP_731617.2; NM_169421.3. [P49905-2]
DR AlphaFoldDB; P49905; -.
DR SMR; P49905; -.
DR BioGRID; 66532; 54.
DR DIP; DIP-779N; -.
DR IntAct; P49905; 7.
DR STRING; 7227.FBpp0081916; -.
DR PaxDb; P49905; -.
DR DNASU; 41406; -.
DR EnsemblMetazoa; FBtr0082440; FBpp0081916; FBgn0011290. [P49905-1]
DR EnsemblMetazoa; FBtr0082442; FBpp0081918; FBgn0011290. [P49905-1]
DR EnsemblMetazoa; FBtr0290205; FBpp0288644; FBgn0011290. [P49905-2]
DR EnsemblMetazoa; FBtr0335213; FBpp0307200; FBgn0011290. [P49905-2]
DR GeneID; 41406; -.
DR KEGG; dme:Dmel_CG17358; -.
DR CTD; 6883; -.
DR FlyBase; FBgn0011290; Taf12.
DR VEuPathDB; VectorBase:FBgn0011290; -.
DR eggNOG; KOG1142; Eukaryota.
DR GeneTree; ENSGT00390000002144; -.
DR InParanoid; P49905; -.
DR PhylomeDB; P49905; -.
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 SignaLink; P49905; -.
DR BioGRID-ORCS; 41406; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41406; -.
DR PRO; PR:P49905; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0011290; Expressed in brain and 24 other tissues.
DR ExpressionAtlas; P49905; baseline and differential.
DR Genevisible; P49905; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000124; C:SAGA complex; IDA:FlyBase.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IEA:InterPro.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:FlyBase.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:FlyBase.
DR CDD; cd07981; TAF12; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037794; TAF12.
DR InterPro; IPR003228; TFIID_TAF12_dom.
DR PANTHER; PTHR12264; PTHR12264; 1.
DR Pfam; PF03847; TFIID_20kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Direct protein sequencing; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..196
FT /note="Transcription initiation factor TFIID subunit 12"
FT /id="PRO_0000033584"
FT DOMAIN 93..160
FT /note="Histone-fold"
FT /evidence="ECO:0000255"
FT REGION 17..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 22 kDa)"
FT /evidence="ECO:0000303|PubMed:7545910"
FT /id="VSP_018890"
FT CONFLICT 15
FT /note="E -> R (in Ref. 2; AAB29540)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="E -> R (in Ref. 2; AAB29540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 196 AA; 21523 MW; 9D6AE98FB9AEC1EC CRC64;
MSDLFTTFDS NGVAEHHLHH NHNSTSSASG LLHDPPMASP SQHSPMTNNS NSSSQNGGPV
SGLGTGTGPI SGGSKSSNHT SSAAGSENTP MLTKPRLTEL VREVDTTTQL DEDVEELLLQ
IIDDFVEDTV KSTSAFAKHR KSNKIEVRDV QLHFERKYNM WIPGFGTDEL RPYKRAAVTE
AHKQRLALIR KTIKKY
