TAFAB_DROME
ID TAFAB_DROME Reviewed; 146 AA.
AC Q9XZT7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transcription initiation factor TFIID subunit 10b;
DE AltName: Full=Transcription initiation factor TFIID 16 kDa subunit;
DE Short=TAFII-16;
DE Short=TAFII16;
DE AltName: Full=dTAF(II)16;
GN Name=Taf10b {ECO:0000312|EMBL:AAF51211.1, ECO:0000312|FlyBase:FBgn0026324};
GN Synonyms=Taf16 {ECO:0000312|EMBL:AAL48842.1}; ORFNames=CG3069;
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] {ECO:0000305, ECO:0000312|EMBL:CAB55761.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:10669741};
RX PubMed=10669741; DOI=10.1128/mcb.20.5.1639-1648.2000;
RA Georgieva S., Kirschner D.B., Jagla T., Nabirochkina E., Hanke S.,
RA Schenkel H., de Lorenzo C., Sinha P., Jagla K., Mechler B., Tora L.;
RT "Two novel Drosophila TAFIIs have homology with human TAFII30 and are
RT differentially regulated during development.";
RL Mol. Cell. Biol. 20:1639-1648(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAB40838.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TAF8, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11134347; DOI=10.1128/mcb.21.2.614-623.2001;
RA Hernandez-Hernandez A., Ferrus A.;
RT "Prodos is a conserved transcriptional regulator that interacts with
RT dTAF(II)16 in Drosophila melanogaster.";
RL Mol. Cell. Biol. 21:614-623(2001).
RN [3] {ECO:0000312|EMBL:AAF51211.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF51211.1}
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 [5] {ECO:0000312|EMBL:AAL48842.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48842.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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. {ECO:0000269|PubMed:10669741, ECO:0000269|PubMed:11134347}.
CC -!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA binding
CC protein (Tbp) and a number of TBP-associated factors (TAFs). The N-
CC terminus interacts with the histone fold of Taf8.
CC {ECO:0000269|PubMed:10669741, ECO:0000269|PubMed:11134347}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10669741}. Nucleus
CC {ECO:0000269|PubMed:10669741, ECO:0000269|PubMed:11134347}.
CC -!- TISSUE SPECIFICITY: At embryonic stage 9, expression is seen in the
CC mesodermal layer and midgut primordia. The mesoderm-specific expression
CC persists in later stages of development and at its highest level is
CC detected in midgut, hindgut, and differentiating somatic muscle fibers.
CC Coexpressed with Taf10 in the lateral epidermis and anal plate.
CC {ECO:0000269|PubMed:10669741}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout development. {ECO:0000269|PubMed:10669741,
CC ECO:0000269|PubMed:11134347}.
CC -!- SIMILARITY: Belongs to the TAF10 family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ243837; CAB55761.1; -; mRNA.
DR EMBL; AJ237968; CAB40838.1; -; mRNA.
DR EMBL; AE014134; AAF51211.1; -; Genomic_DNA.
DR EMBL; AY071220; AAL48842.1; -; mRNA.
DR RefSeq; NP_477418.1; NM_058070.6.
DR AlphaFoldDB; Q9XZT7; -.
DR SMR; Q9XZT7; -.
DR BioGRID; 59691; 28.
DR DIP; DIP-19377N; -.
DR IntAct; Q9XZT7; 9.
DR STRING; 7227.FBpp0077415; -.
DR PaxDb; Q9XZT7; -.
DR EnsemblMetazoa; FBtr0077735; FBpp0077415; FBgn0026324.
DR GeneID; 33468; -.
DR KEGG; dme:Dmel_CG3069; -.
DR CTD; 33468; -.
DR FlyBase; FBgn0026324; Taf10b.
DR VEuPathDB; VectorBase:FBgn0026324; -.
DR eggNOG; KOG3423; Eukaryota.
DR GeneTree; ENSGT00390000009368; -.
DR HOGENOM; CLU_064104_4_1_1; -.
DR InParanoid; Q9XZT7; -.
DR OMA; RTHMQNS; -.
DR OrthoDB; 1478962at2759; -.
DR PhylomeDB; Q9XZT7; -.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
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; 33468; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33468; -.
DR PRO; PR:Q9XZT7; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0026324; Expressed in antenna and 24 other tissues.
DR Genevisible; Q9XZT7; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0000124; C:SAGA complex; IDA:FlyBase.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:FlyBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:UniProtKB.
DR CDD; cd07982; TAF10; 1.
DR InterPro; IPR003923; TFIID_30kDa.
DR PANTHER; PTHR21242; PTHR21242; 1.
DR Pfam; PF03540; TFIID_30kDa; 1.
DR PIRSF; PIRSF017246; TFIID_TAF10; 1.
DR PRINTS; PR01443; TFIID30KDSUB.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..146
FT /note="Transcription initiation factor TFIID subunit 10b"
FT /id="PRO_0000118900"
FT REGION 16..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 146 AA; 15784 MW; 882984D4A6517991 CRC64;
MVGSNFGIIY HNSAGGASSH GQSSGGGGGG DRDRTTPSSH LSDFMSQLED YTPLIPDAVT
SHYLNMGGFQ SDDKRIVRLI SLAAQKYMSD IIDDALQHSK ARTHMQTTNT PGGSKAKDRK
FTLTMEDLQP ALADYGINVR KVDYSQ
