ID   TAF9B_MOUSE             Reviewed;         249 AA.
AC   Q6NZA9; A2AP80; Q3UXZ3; Q3V2M4; Q80WW6;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=Transcription initiation factor TFIID subunit 9B;
DE   AltName: Full=Transcription initiation factor TFIID subunit 9-like;
DE   AltName: Full=Transcription-associated factor TAFII31L;
GN   Name=Taf9b; Synonyms=Taf9l;
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] {ECO:0000312|EMBL:BAE22420.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE22420.1};
RC   TISSUE=Olfactory bulb {ECO:0000312|EMBL:BAE22420.1}, and Testis
RC   {ECO:0000312|EMBL:BAE20773.1};
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0000312|EMBL:AAH66223.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH51635.1,
RC   ECO:0000312|EMBL:AAH66223.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAH51635.1}, and Kidney
RC   {ECO:0000312|EMBL:AAH66223.1};
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Spleen, and 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: Essential for cell viability. TAF9 and TAF9B are involved in
CC       transcriptional activation as well as repression of distinct but
CC       overlapping sets of genes. May have a role in gene regulation
CC       associated with apoptosis. TAFs are components of the transcription
CC       factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF
CC       histone acetylase complex and the STAGA transcription coactivator-HAT
CC       complex. TFIID or TFTC are essential for the regulation of RNA
CC       polymerase II-mediated transcription (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds TAF5 and TAF6. Component of TFIID and the TATA-binding
CC       protein-free TAF complex (TFTC). TFIID is composed of TATA binding
CC       protein (TBP) and a number of TBP-associated factors (TAFs). Binds N-
CC       terminal domain of p53/TP53 which is essential for transcription (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TAF9 family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH51635.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE20773.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK131710; BAE20773.1; ALT_INIT; mRNA.
DR   EMBL; AK135097; BAE22420.1; -; mRNA.
DR   EMBL; AL833778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC051635; AAH51635.1; ALT_INIT; mRNA.
DR   EMBL; BC066223; AAH66223.1; -; mRNA.
DR   CCDS; CCDS30340.1; -.
DR   RefSeq; NP_001001176.2; NM_001001176.2.
DR   RefSeq; NP_001161460.1; NM_001167988.1.
DR   AlphaFoldDB; Q6NZA9; -.
DR   SMR; Q6NZA9; -.
DR   STRING; 10090.ENSMUSP00000109123; -.
DR   iPTMnet; Q6NZA9; -.
DR   PhosphoSitePlus; Q6NZA9; -.
DR   jPOST; Q6NZA9; -.
DR   MaxQB; Q6NZA9; -.
DR   PaxDb; 10090-ENSMUSP00000109123; -.
DR   ProteomicsDB; 263249; -.
DR   Antibodypedia; 28250; 150 antibodies from 24 providers.
DR   DNASU; 407786; -.
DR   Ensembl; ENSMUST00000055497.15; ENSMUSP00000059751.9; ENSMUSG00000047242.15.
DR   GeneID; 407786; -.
DR   KEGG; mmu:407786; -.
DR   UCSC; uc009ubq.2; mouse.
DR   AGR; MGI:3039562; -.
DR   CTD; 51616; -.
DR   MGI; MGI:3039562; Taf9b.
DR   VEuPathDB; HostDB:ENSMUSG00000047242; -.
DR   eggNOG; KOG3334; Eukaryota.
DR   GeneTree; ENSGT00940000161697; -.
DR   HOGENOM; CLU_068315_2_0_1; -.
DR   InParanoid; Q6NZA9; -.
DR   OMA; DDNDTMI; -.
DR   OrthoDB; 10695at2759; -.
DR   PhylomeDB; Q6NZA9; -.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
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-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; 407786; 4 hits in 76 CRISPR screens.
DR   PRO; PR:Q6NZA9; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q6NZA9; Protein.
DR   Bgee; ENSMUSG00000047242; Expressed in animal zygote and 216 other cell types or tissues.
DR   ExpressionAtlas; Q6NZA9; baseline and differential.
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:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR   GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:GOC.
DR   CDD; cd07979; TAF9; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR003162; TFIID-31.
DR   PANTHER; PTHR48068; TAF9 RNA POLYMERASE II, TATA BOX-BINDING PROTEIN (TBP)-ASSOCIATED FACTOR; 1.
DR   PANTHER; PTHR48068:SF5; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 9B; 1.
DR   Pfam; PF02291; TFIID-31kDa; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   Genevisible; Q6NZA9; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..249
FT                   /note="Transcription initiation factor TFIID subunit 9B"
FT                   /id="PRO_0000118892"
FT   REGION          148..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          224..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBM6"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBM6"
FT   MOD_RES         172
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBM6"
FT   MOD_RES         175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HBM6"
FT   CONFLICT        28
FT                   /note="I -> T (in Ref. 3; AAH66223)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        193
FT                   /note="A -> T (in Ref. 1; BAE22420)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   249 AA;  27172 MW;  5615C356885322FD CRC64;
     MEPAKMAPIK NAPRDALVMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH
     AKKPTVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQKN QTPLPLIKPY AGPRLPPDRY
     CLTAPNYRLK SLVKKGPNQG RLVPRLSAVS SRPTTPPVAP PQAVSGPNKA ATPVSVTSQR
     FAVQIPPSQS TPAKPAPAAT AVQNVLINPS MIGPKNILIT TSMVSSQNTA TDSNPLKRKH
     DDDDDNDTM
//