TAF9_HUMAN
ID TAF9_HUMAN Reviewed; 264 AA.
AC Q16594; D3DWA3; Q5U0D1; Q9BTS1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Transcription initiation factor TFIID subunit 9;
DE AltName: Full=RNA polymerase II TBP-associated factor subunit G;
DE AltName: Full=STAF31/32;
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, TAFII31;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH VP16 AND TFIIB.
RX PubMed=7761466; DOI=10.1073/pnas.92.11.5154;
RA Lu H., Levine A.J.;
RT "Human TAFII31 protein is a transcriptional coactivator of the p53
RT protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5154-5158(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TAF6.
RX PubMed=7597030; DOI=10.1073/pnas.92.13.5788;
RA Klemm R.D., Goodrich J.A., Zhou S., Tjian R.;
RT "Molecular cloning and expression of the 32-kDa subunit of human TFIID
RT reveals interactions with VP16 and TFIIB that mediate transcriptional
RT activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5788-5792(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7667268; DOI=10.1073/pnas.92.18.8195;
RA Hisatake K., Ohta T., Takada R., Guermah M., Horikoshi M., Nakatani Y.,
RA Roeder R.G.;
RT "Evolutionary conservation of human TATA-binding-polypeptide-associated
RT factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and
RT with general transcription factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8195-8199(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-6.
RG NIEHS SNPs program;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Testis;
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 [8]
RP PROTEIN SEQUENCE OF 25-55; 79-89; 176-200 AND 223-246, SUBUNIT, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=9674425; DOI=10.1016/s0092-8674(00)81219-2;
RA Ogryzko V.V., Kotani T., Zhang X., Schiltz R.L., Howard T., Yang X.-J.,
RA Howard B.H., Qin J., Nakatani Y.;
RT "Histone-like TAFs within the PCAF histone acetylase complex.";
RL Cell 94:35-44(1998).
RN [9]
RP SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H;
RP GCN5L2; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10 AND TAF12, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11564863; DOI=10.1128/mcb.21.20.6782-6795.2001;
RA Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
RA Kundu T.K., Chait B.T., Roeder R.G.;
RT "Human STAGA complex is a chromatin-acetylating transcription coactivator
RT that interacts with pre-mRNA splicing and DNA damage-binding factors in
RT vivo.";
RL Mol. Cell. Biol. 21:6782-6795(2001).
RN [10]
RP IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L; TAF5L; SUPT3H;
RP TAF6L; TAF10; TAF12 AND TRRAP.
RX PubMed=9885574; DOI=10.1016/s1097-2765(00)80301-9;
RA Vassilev A., Yamauchi J., Kotani T., Prives C., Avantaggiati M.L., Qin J.,
RA Nakatani Y.;
RT "The 400 kDa subunit of the PCAF histone acetylase complex belongs to the
RT ATM superfamily.";
RL Mol. Cell 2:869-875(1998).
RN [11]
RP IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [12]
RP IDENTIFICATION.
RX PubMed=16079131; DOI=10.1074/jbc.m501982200;
RA Santama N., Ogg S.C., Malekkou A., Zographos S.E., Weis K., Lamond A.I.;
RT "Characterization of hCINAP, a novel coilin-interacting protein encoded by
RT a transcript from the transcription factor TAFIID32 locus.";
RL J. Biol. Chem. 280:36429-36441(2005).
RN [13]
RP INTERACTION WITH TAF6 IN A COMPLEX WITH TAF6; TAF9; TAF12 AND TAF4B, AND
RP DNA-BINDING.
RX PubMed=15601843; DOI=10.1128/mcb.25.1.206-219.2005;
RA Shao H., Revach M., Moshonov S., Tzuman Y., Gazit K., Albeck S., Unger T.,
RA Dikstein R.;
RT "Core promoter binding by histone-like TAF complexes.";
RL Mol. Cell. Biol. 25:206-219(2005).
RN [14]
RP FUNCTION, SUBUNIT, INDUCTION, AND INTERACTION WITH TAF5 AND TAF6.
RX PubMed=15899866; DOI=10.1128/mcb.25.11.4638-4649.2005;
RA Frontini M., Soutoglou E., Argentini M., Bole-Feysot C., Jost B.,
RA Scheer E., Tora L.;
RT "TAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping
RT roles with TAF9.";
RL Mol. Cell. Biol. 25:4638-4649(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161; THR-178 AND SER-181, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-158 AND THR-159, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND THR-178, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; THR-178 AND
RP SER-196, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20] {ECO:0007744|PDB:7EDX, ECO:0007744|PDB:7EG7, ECO:0007744|PDB:7EG8, ECO:0007744|PDB:7EG9, ECO:0007744|PDB:7EGA, ECO:0007744|PDB:7EGB, ECO:0007744|PDB:7EGC, ECO:0007744|PDB:7EGD, ECO:0007744|PDB:7EGE, ECO:0007744|PDB:7EGF}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.77 ANGSTROMS), FUNCTION, IDENTIFICATION
RP IN THE TFIID COMPLEX, AND SUBUNIT.
RX PubMed=33795473; DOI=10.1126/science.aba8490;
RA Chen X., Qi Y., Wu Z., Wang X., Li J., Zhao D., Hou H., Li Y., Yu Z.,
RA Liu W., Wang M., Ren Y., Li Z., Yang H., Xu Y.;
RT "Structural insights into preinitiation complex assembly on core
RT promoters.";
RL Science 372:0-0(2021).
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 (PubMed:33795473). TFIID recognizes and binds promoters
CC with or without a TATA box via its subunit TBP, a TATA-box-binding
CC protein, and promotes assembly of the pre-initiation complex (PIC)
CC (PubMed:33795473). The TFIID complex consists of TBP and TBP-associated
CC factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7,
CC TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 (PubMed:33795473). TAF9 is
CC also a component of the TBP-free TAFII complex (TFTC), the PCAF histone
CC acetylase complex and the STAGA transcription coactivator-HAT complex
CC (PubMed:15899866). TAF9 and its paralog TAF9B are involved in
CC transcriptional activation as well as repression of distinct but
CC overlapping sets of genes (PubMed:15899866). Essential for cell
CC viability (PubMed:15899866). May have a role in gene regulation
CC associated with apoptosis (PubMed:15899866).
CC {ECO:0000269|PubMed:15899866, ECO:0000269|PubMed:33795473}.
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
CC (PubMed:33795473). Component of the TATA-binding protein-free TAF
CC complex (TFTC), the PCAF histone acetylase complex and the STAGA
CC transcription coactivator-HAT complex (PubMed:11564863,
CC PubMed:9885574). The PCAF complex consists at least of TADA2L/ADA2,
CC SUPT3H/SPT3, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-alpha,
CC TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP (PubMed:9885574,
CC PubMed:9674425). The STAGA transcription coactivator-HAT complex
CC consists at least of SUPT3H, GCN5L2, SUPT7L, TAF5L, TAF6L, TADA3L,
CC TAD1L, TAF10, TAF12, TRRAP and TAF9 (PubMed:11564863). Binds N-terminal
CC domain of p53/TP53 which is essential for transcription
CC (PubMed:7761466). Component of some MLL1/MLL complex, at least composed
CC of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5,
CC as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C,
CC KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10 (PubMed:15960975). Binds TFIIB and the Herpes simplex virus
CC activator VP16 (PubMed:7761466). Forms a heterodimer with TAF6 in a
CC complex with the TAF4B-TAF12 heterodimer (PubMed:7597030,
CC PubMed:15601843). Also interacts with TAF5 (PubMed:15899866). Binds
CC directly DNA (PubMed:15601843). Increased DNA binding when complexed
CC with TAF6 (PubMed:15601843). {ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:15601843, ECO:0000269|PubMed:15899866,
CC ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:33795473,
CC ECO:0000269|PubMed:7597030, ECO:0000269|PubMed:7761466,
CC ECO:0000269|PubMed:9674425, ECO:0000269|PubMed:9885574}.
CC -!- INTERACTION:
CC Q16594; Q14919: DRAP1; NbExp=9; IntAct=EBI-712521, EBI-712941;
CC Q16594; Q92831: KAT2B; NbExp=3; IntAct=EBI-712521, EBI-477430;
CC Q16594; P52294: KPNA1; NbExp=4; IntAct=EBI-712521, EBI-358383;
CC Q16594; O60684: KPNA6; NbExp=4; IntAct=EBI-712521, EBI-359923;
CC Q16594; Q9Y6J9: TAF6L; NbExp=9; IntAct=EBI-712521, EBI-743984;
CC Q16594; P46099: Klf1; Xeno; NbExp=3; IntAct=EBI-712521, EBI-15761537;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:9674425}.
CC -!- INDUCTION: 6 to 8-fold by apoptotic signals.
CC {ECO:0000269|PubMed:15899866}.
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 -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/taf9/";
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DR EMBL; U25112; AAA91318.1; -; mRNA.
DR EMBL; U21858; AAC50153.1; -; mRNA.
DR EMBL; U30504; AAA84389.1; -; mRNA.
DR EMBL; BT019652; AAV38458.1; -; mRNA.
DR EMBL; AY189986; AAN84793.1; -; Genomic_DNA.
DR EMBL; CH471137; EAW51295.1; -; Genomic_DNA.
DR EMBL; CH471137; EAW51296.1; -; Genomic_DNA.
DR EMBL; BC003400; AAH03400.1; -; mRNA.
DR EMBL; BC033320; AAH33320.1; -; mRNA.
DR CCDS; CCDS4002.1; -.
DR PIR; I39141; I39141.
DR RefSeq; NP_001015892.1; NM_001015892.1.
DR RefSeq; NP_003178.1; NM_003187.4.
DR PDB; 6F3T; X-ray; 2.50 A; F/H/J/L=5-120.
DR PDB; 6MZC; EM; 4.50 A; M=1-264.
DR PDB; 6MZD; EM; 9.80 A; L=1-264.
DR PDB; 6MZL; EM; 23.00 A; L/M=1-264.
DR PDB; 6MZM; EM; 7.50 A; L=1-264.
DR PDB; 7EDX; EM; 4.50 A; I/i=1-264.
DR PDB; 7EG7; EM; 6.20 A; I/i=1-264.
DR PDB; 7EG8; EM; 7.40 A; I/i=1-264.
DR PDB; 7EG9; EM; 3.70 A; I/i=1-264.
DR PDB; 7EGA; EM; 4.10 A; I/i=1-264.
DR PDB; 7EGB; EM; 3.30 A; I/i=1-264.
DR PDB; 7EGC; EM; 3.90 A; I/i=1-264.
DR PDB; 7EGD; EM; 6.75 A; I/i=1-264.
DR PDB; 7EGE; EM; 9.00 A; I/i=1-264.
DR PDB; 7EGF; EM; 3.16 A; i=1-264.
DR PDB; 7EGG; EM; 2.77 A; I=1-264.
DR PDB; 7EGI; EM; 9.82 A; I/i=1-264.
DR PDB; 7EGJ; EM; 8.64 A; I/i=1-264.
DR PDB; 7ENA; EM; 4.07 A; DI/Di=1-264.
DR PDB; 7ENC; EM; 4.13 A; DI/Di=1-264.
DR PDBsum; 6F3T; -.
DR PDBsum; 6MZC; -.
DR PDBsum; 6MZD; -.
DR PDBsum; 6MZL; -.
DR PDBsum; 6MZM; -.
DR PDBsum; 7EDX; -.
DR PDBsum; 7EG7; -.
DR PDBsum; 7EG8; -.
DR PDBsum; 7EG9; -.
DR PDBsum; 7EGA; -.
DR PDBsum; 7EGB; -.
DR PDBsum; 7EGC; -.
DR PDBsum; 7EGD; -.
DR PDBsum; 7EGE; -.
DR PDBsum; 7EGF; -.
DR PDBsum; 7EGG; -.
DR PDBsum; 7EGI; -.
DR PDBsum; 7EGJ; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR AlphaFoldDB; Q16594; -.
DR SMR; Q16594; -.
DR BioGRID; 112743; 158.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR ComplexPortal; CPX-903; TFTC histone acetylation complex.
DR ComplexPortal; CPX-915; General transcription factor complex TFIID.
DR ComplexPortal; CPX-930; General transcription factor complex TFIID, TAF4B variant.
DR ComplexPortal; CPX-989; PCAF histone acetylase complex.
DR CORUM; Q16594; -.
DR DIP; DIP-435N; -.
DR IntAct; Q16594; 70.
DR MINT; Q16594; -.
DR STRING; 9606.ENSP00000370193; -.
DR GlyGen; Q16594; 6 sites, 2 O-linked glycans (6 sites).
DR iPTMnet; Q16594; -.
DR MetOSite; Q16594; -.
DR PhosphoSitePlus; Q16594; -.
DR BioMuta; TAF9; -.
DR DMDM; 2498981; -.
DR EPD; Q16594; -.
DR jPOST; Q16594; -.
DR MassIVE; Q16594; -.
DR MaxQB; Q16594; -.
DR PaxDb; Q16594; -.
DR PeptideAtlas; Q16594; -.
DR PRIDE; Q16594; -.
DR ProteomicsDB; 60938; -.
DR Antibodypedia; 74350; 136 antibodies from 23 providers.
DR DNASU; 6880; -.
DR Ensembl; ENST00000217893.10; ENSP00000217893.7; ENSG00000273841.6.
DR Ensembl; ENST00000328663.8; ENSP00000370193.1; ENSG00000273841.6.
DR Ensembl; ENST00000503245.6; ENSP00000425944.4; ENSG00000273841.6.
DR Ensembl; ENST00000504109.6; ENSP00000426283.2; ENSG00000273841.6.
DR Ensembl; ENST00000506736.2; ENSP00000421873.1; ENSG00000273841.6.
DR Ensembl; ENST00000508954.4; ENSP00000427617.4; ENSG00000273841.6.
DR Ensembl; ENST00000509462.6; ENSP00000427343.4; ENSG00000273841.6.
DR Ensembl; ENST00000512152.6; ENSP00000425798.4; ENSG00000273841.6.
DR Ensembl; ENST00000615404.1; ENSP00000478935.1; ENSG00000276463.4.
DR Ensembl; ENST00000616867.1; ENSP00000477750.1; ENSG00000276463.4.
DR Ensembl; ENST00000617893.4; ENSP00000477611.1; ENSG00000276463.4.
DR Ensembl; ENST00000687836.1; ENSP00000509753.1; ENSG00000273841.6.
DR Ensembl; ENST00000688968.1; ENSP00000510364.1; ENSG00000273841.6.
DR Ensembl; ENST00000689249.1; ENSP00000508645.1; ENSG00000273841.6.
DR Ensembl; ENST00000690749.1; ENSP00000510605.1; ENSG00000273841.6.
DR Ensembl; ENST00000691076.1; ENSP00000509913.1; ENSG00000273841.6.
DR Ensembl; ENST00000691515.1; ENSP00000509452.1; ENSG00000273841.6.
DR Ensembl; ENST00000691555.1; ENSP00000510101.1; ENSG00000273841.6.
DR Ensembl; ENST00000693414.1; ENSP00000509848.1; ENSG00000273841.6.
DR GeneID; 6880; -.
DR KEGG; hsa:6880; -.
DR MANE-Select; ENST00000217893.10; ENSP00000217893.7; NM_003187.5; NP_003178.1.
DR UCSC; uc003jwc.2; human.
DR CTD; 6880; -.
DR DisGeNET; 6880; -.
DR GeneCards; TAF9; -.
DR HGNC; HGNC:11542; TAF9.
DR HPA; ENSG00000273841; Low tissue specificity.
DR MIM; 600822; gene.
DR neXtProt; NX_Q16594; -.
DR OpenTargets; ENSG00000273841; -.
DR PharmGKB; PA36317; -.
DR VEuPathDB; HostDB:ENSG00000273841; -.
DR eggNOG; KOG3334; Eukaryota.
DR GeneTree; ENSGT00940000155097; -.
DR InParanoid; Q16594; -.
DR OMA; PRDFLME; -.
DR OrthoDB; 1429345at2759; -.
DR PhylomeDB; Q16594; -.
DR TreeFam; TF351417; -.
DR PathwayCommons; Q16594; -.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR SignaLink; Q16594; -.
DR SIGNOR; Q16594; -.
DR BioGRID-ORCS; 6880; 20 hits in 1045 CRISPR screens.
DR GeneWiki; TAF9; -.
DR GenomeRNAi; 6880; -.
DR Pharos; Q16594; Tbio.
DR PRO; PR:Q16594; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q16594; protein.
DR Bgee; ENSG00000273841; Expressed in left testis and 97 other tissues.
DR ExpressionAtlas; Q16594; baseline and differential.
DR Genevisible; Q16594; HS.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070761; C:pre-snoRNP complex; IDA:BHF-UCL.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:ARUK-UCL.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IC:BHF-UCL.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IC:BHF-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR GO; GO:0060760; P:positive regulation of response to cytokine stimulus; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
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; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0070555; P:response to interleukin-1; IMP:BHF-UCL.
DR GO; GO:1902065; P:response to L-glutamate; IEA:Ensembl.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IPI:ComplexPortal.
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 3D-structure; Acetylation; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..264
FT /note="Transcription initiation factor TFIID subunit 9"
FT /id="PRO_0000118888"
FT DNA_BIND 120..137
FT REGION 149..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI33"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI33"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 6
FT /note="T -> M (in dbSNP:rs4252233)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_016279"
FT VARIANT 210
FT /note="Q -> H (in dbSNP:rs11542580)"
FT /id="VAR_052260"
FT CONFLICT 46
FT /note="Y -> V (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="L -> F (in Ref. 7; AAH03400)"
FT /evidence="ECO:0000305"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:6F3T"
FT HELIX 34..60
FT /evidence="ECO:0007829|PDB:6F3T"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:6F3T"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:6F3T"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:7EGG"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:7EGG"
SQ SEQUENCE 264 AA; 28974 MW; 1925AEC65D6C84C7 CRC64;
MESGKTASPK SMPKDAQMMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH
AKKATVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQRN QTPLPLIKPY SGPRLPPDRY
CLTAPNYRLK SLQKKASTSA GRITVPRLSV GSVTSRPSTP TLGTPTPQTM SVSTKVGTPM
SLTGQRFTVQ MPTSQSPAVK ASIPATSAVQ NVLINPSLIG SKNILITTNM MSSQNTANES
SNALKRKRED DDDDDDDDDD YDNL
