TAF9_MOUSE
ID TAF9_MOUSE Reviewed; 264 AA.
AC Q8VI33; Q32P09; Q80XS3; Q9CV61;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Transcription initiation factor TFIID subunit 9;
DE AltName: Full=RNA polymerase II TBP-associated factor subunit G;
DE AltName: Full=Transcription initiation factor TFIID 31 kDa subunit;
DE Short=TAFII-31;
DE Short=TAFII31;
DE AltName: Full=Transcription initiation factor TFIID 32 kDa subunit;
DE Short=TAFII-32;
DE Short=TAFII32;
GN Name=Taf9; Synonyms=Taf2g;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Ng K., Lee S., Tsui S.K.W., Fung K.-P., Lee C.-Y., Waye M.M.Y.;
RT "Molecular cloning of Mus musculus TATA box binding protein (TBP)-
RT associated factor, RNA polymerase II, G, (TAF2G).";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, Czech II, and FVB/N-3; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; THR-159; THR-161 AND
RP THR-164, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: The TFIID basal transcription factor complex plays a major
CC role in the initiation of RNA polymerase II (Pol II)-dependent
CC transcription. TFIID recognizes and binds promoters with or without a
CC TATA box via its subunit TBP, a TATA-box-binding protein, and promotes
CC assembly of the pre-initiation complex (PIC). The TFIID complex
CC consists of TBP and TBP-associated factors (TAFs), including TAF1,
CC TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and
CC TAF13. TAF9 is also a component of the TBP-free TAFII complex (TFTC),
CC the PCAF histone acetylase complex and the STAGA transcription
CC coactivator-HAT complex. TAF9 and its paralog TAF9B are involved in
CC transcriptional activation as well as repression of distinct but
CC overlapping sets of genes. Essential for cell viability. May have a
CC role in gene regulation associated with apoptosis.
CC {ECO:0000250|UniProtKB:Q16594}.
CC -!- SUBUNIT: Component of the TFIID basal transcription factor complex,
CC composed of TATA-box-binding protein TBP, and a number of TBP-
CC associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5,
CC TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. Component of the
CC TATA-binding protein-free TAF complex (TFTC), the PCAF histone
CC acetylase complex and the STAGA transcription coactivator-HAT complex.
CC The PCAF complex consists at least of TADA2L/ADA2, SUPT3H/SPT3,
CC TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-alpha, TAF10/TAFII30,
CC TAF12/TAFII20, TAF9/TAFII31 and TRRAP. The STAGA transcription
CC coactivator-HAT complex consists at least of SUPT3H, GCN5L2, SUPT7L,
CC TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. Binds N-
CC terminal domain of p53/TP53 which is essential for transcription.
CC Component of some MLL1/MLL complex, at least composed of the core
CC components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as
CC the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
CC LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10. Binds TFIIB and the Herpes simplex virus activator VP16. Forms a
CC heterodimer with TAF6 in a complex with the TAF4B-TAF12 heterodimer.
CC Also interacts with TAF5. Binds directly DNA. Increased DNA binding
CC when complexed with TAF6. {ECO:0000250|UniProtKB:Q16594}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TAF9 family. {ECO:0000305}.
CC -!- CAUTION: AK6 and TAF9 were initially considered as products of the same
CC gene since they share two exons. However, they are translated from
CC different initiation codons and reading frames and encode unrelated
CC proteins. This arrangement is conserved in some mammalian species.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB26216.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF305839; AAL47693.1; -; mRNA.
DR EMBL; AK009322; BAB26216.2; ALT_INIT; mRNA.
DR EMBL; BC042723; AAH42723.1; -; mRNA.
DR EMBL; BC043028; AAH43028.1; -; mRNA.
DR EMBL; BC108348; AAI08349.1; -; mRNA.
DR CCDS; CCDS26735.1; -.
DR RefSeq; NP_001015889.1; NM_001015889.2.
DR RefSeq; NP_081415.1; NM_027139.5.
DR AlphaFoldDB; Q8VI33; -.
DR SMR; Q8VI33; -.
DR BioGRID; 223860; 10.
DR ComplexPortal; CPX-1024; PCAF histone acetylase complex.
DR ComplexPortal; CPX-6803; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-916; TFTC histone acetylation complex.
DR ComplexPortal; CPX-920; SAGA complex, KAT2A variant.
DR ComplexPortal; CPX-932; General transcription factor complex TFIID.
DR ComplexPortal; CPX-959; General transcription factor complex TFIID, Taf4b variant.
DR CORUM; Q8VI33; -.
DR DIP; DIP-48737N; -.
DR IntAct; Q8VI33; 5.
DR MINT; Q8VI33; -.
DR STRING; 10090.ENSMUSP00000140244; -.
DR iPTMnet; Q8VI33; -.
DR PhosphoSitePlus; Q8VI33; -.
DR EPD; Q8VI33; -.
DR jPOST; Q8VI33; -.
DR MaxQB; Q8VI33; -.
DR PaxDb; Q8VI33; -.
DR PeptideAtlas; Q8VI33; -.
DR PRIDE; Q8VI33; -.
DR ProteomicsDB; 254647; -.
DR DNASU; 108143; -.
DR Ensembl; ENSMUST00000084721; ENSMUSP00000081772; ENSMUSG00000078941.
DR Ensembl; ENSMUST00000167256; ENSMUSP00000132143; ENSMUSG00000052293.
DR Ensembl; ENSMUST00000190594; ENSMUSP00000140244; ENSMUSG00000052293.
DR GeneID; 108143; -.
DR KEGG; mmu:108143; -.
DR UCSC; uc007rrf.2; mouse.
DR CTD; 6880; -.
DR MGI; MGI:1888697; Taf9.
DR VEuPathDB; HostDB:ENSMUSG00000052293; -.
DR VEuPathDB; HostDB:ENSMUSG00000078941; -.
DR eggNOG; KOG3334; Eukaryota.
DR GeneTree; ENSGT00940000155097; -.
DR HOGENOM; CLU_068315_2_0_1; -.
DR InParanoid; Q8VI33; -.
DR OMA; PRDFLME; -.
DR OrthoDB; 1429345at2759; -.
DR PhylomeDB; Q8VI33; -.
DR TreeFam; TF351417; -.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR BioGRID-ORCS; 108143; 11 hits in 61 CRISPR screens.
DR PRO; PR:Q8VI33; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8VI33; protein.
DR Bgee; ENSMUSG00000052293; Expressed in spermatid and 82 other tissues.
DR ExpressionAtlas; Q8VI33; baseline and differential.
DR Genevisible; Q8VI33; MM.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0070761; C:pre-snoRNP complex; ISO:MGI.
DR GO; GO:0000124; C:SAGA complex; ISO:MGI.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
DR GO; GO:0033276; C:transcription factor TFTC complex; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0000492; P:box C/D snoRNP assembly; ISO:MGI.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:MGI.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0060760; P:positive regulation of response to cytokine stimulus; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; ISO:MGI.
DR CDD; cd07979; TAF9; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR003162; TFIID-31.
DR Pfam; PF02291; TFIID-31kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..264
FT /note="Transcription initiation factor TFIID subunit 9"
FT /id="PRO_0000118889"
FT REGION 150..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..264
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16594"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16594"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16594"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16594"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16594"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16594"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16594"
FT CONFLICT 161
FT /note="T -> P (in Ref. 3; AAH43028)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 264 AA; 28979 MW; EFB2AE27AEFEE794 CRC64;
MESGKMASPK SMPKDAQMMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH
AKKATVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQRN QTPLPLIKPY SGPRLPPDRY
CLTAPNYRLK SLQKKAPAPA GRITVPRLSV GSVSSRPSTP TLGTPTPQTM SVSTKVGTPM
SLTGQRFTVQ MPASQSPAVK ASIPATSTVQ NVLINPSLIG SKNILITTNM VSQNTAESAN
ALKRKREDDD DDDDDDDDDD YDNM
