ID TAF4_HUMAN Reviewed; 1085 AA. AC O00268; A6NGD9; Q5TBP6; Q99721; Q9BR40; Q9BX42; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 2. DT 27-MAR-2024, entry version 225. DE RecName: Full=Transcription initiation factor TFIID subunit 4; DE AltName: Full=RNA polymerase II TBP-associated factor subunit C; DE AltName: Full=TBP-associated factor 4; DE AltName: Full=Transcription initiation factor TFIID 130 kDa subunit; DE Short=TAF(II)130; DE Short=TAFII-130; DE Short=TAFII130; DE AltName: Full=Transcription initiation factor TFIID 135 kDa subunit; DE Short=TAF(II)135; DE Short=TAFII-135; DE Short=TAFII135; GN Name=TAF4; Synonyms=TAF2C, TAF2C1, TAF4A, TAFII130, TAFII135; 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 FUNCTION. RX PubMed=9192867; DOI=10.1101/gad.11.11.1381; RA Mengus G., May M., Carre L., Chambon P., Davidson I.; RT "Human TAF(II)135 potentiates transcriptional activation by the AF-2s of RT the retinoic acid, vitamin D3, and thyroid hormone receptors in mammalian RT cells."; RL Genes Dev. 11:1381-1395(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 105-1085, PARTIAL PROTEIN SEQUENCE, AND RP FUNCTION. RX PubMed=8942982; DOI=10.1073/pnas.93.24.13611; RA Tanese N., Saluja D., Vassallo M.F., Chen J.-L., Admon A.; RT "Molecular cloning and analysis of two subunits of the human TFIID complex: RT hTAFII130 and hTAFII100."; RL Proc. Natl. Acad. Sci. U.S.A. 93:13611-13616(1996). RN [6] RP INTERACTION WITH SV40 LARGE T ANTIGEN (MICROBIAL INFECTION). RX PubMed=8647434; DOI=10.1101/gad.10.11.1369; RA Damania B., Alwine J.C.; RT "TAF-like function of SV40 large T antigen."; RL Genes Dev. 10:1369-1381(1996). RN [7] RP IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H; RP TAF2; TAF5; TRRAP; TAF12; GCN5L2 AND TAF10. RX PubMed=10373431; DOI=10.1074/jbc.274.26.18285; RA Brand M., Yamamoto K., Staub A., Tora L.; RT "Identification of TATA-binding protein-free TAFII-containing complex RT subunits suggests a role in nucleosome acetylation and signal RT transduction."; RL J. Biol. Chem. 274:18285-18289(1999). RN [8] RP IDENTIFICATION IN THE TFTC-HAT COMPLEX, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=12601814; DOI=10.1002/pmic.200390030; RA Cavusoglu N., Brand M., Tora L., van Dorsselaer A.; RT "Novel subunits of the TATA binding protein free TAFII-containing RT transcription complex identified by matrix-assisted laser RT desorption/ionization-time of flight mass spectrometry following one- RT dimensional gel electrophoresis."; RL Proteomics 3:217-223(2003). RN [9] 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 [10] RP INTERACTION WITH ATF7. RX PubMed=15735663; DOI=10.1038/sj.onc.1208565; RA Hamard P.J., Dalbies-Tran R., Hauss C., Davidson I., Kedinger C., RA Chatton B.; RT "A functional interaction between ATF7 and TAF12 that is modulated by RT TAF4."; RL Oncogene 24:3472-3483(2005). RN [11] 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY RP 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 [13] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-424 AND ARG-435, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [14] RP INVOLVEMENT IN MRD73, AND VARIANT MRD73 949-GLN--LYS-1085 DEL. RX PubMed=33875846; DOI=10.1038/s41436-021-01159-0; RA Bertoli-Avella A.M., Kandaswamy K.K., Khan S., Ordonez-Herrera N., RA Tripolszki K., Beetz C., Rocha M.E., Urzi A., Hotakainen R., Leubauer A., RA Al-Ali R., Karageorgou V., Moldovan O., Dias P., Alhashem A., Tabarki B., RA Albalwi M.A., Alswaid A.F., Al-Hassnan Z.N., Alghamdi M.A., Hadipour Z., RA Hadipour F., Al Hashmi N., Al-Gazali L., Cheema H., Zaki M.S., Huening I., RA Alfares A., Eyaid W., Al Mutairi F., Alfadhel M., Alkuraya F.S., RA Al-Sannaa N.A., AlShamsi A.M., Ameziane N., Rolfs A., Bauer P.; RT "Combining exome/genome sequencing with data repository analysis reveals RT novel gene-disease associations for a wide range of genetic disorders."; RL Genet. Med. 23:1551-1568(2021). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 872-920 IN COMPLEX WITH TAF12, AND RP FUNCTION. RX PubMed=10594036; DOI=10.1128/mcb.20.1.340-351.2000; RA Gangloff Y.-G., Werten S., Romier C., Carre L., Poch O., Moras D., RA Davidson I.; RT "The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA RT components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs."; RL Mol. Cell. Biol. 20:340-351(2000). RN [16] {ECO:0007744|PDB:2P6V} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 575-688, AND METHYLATION AT RP LYS-594; LYS-595; LYS-597; LYS-605; LYS-611; LYS-621; LYS-631 AND LYS-658. RX PubMed=17483474; DOI=10.1073/pnas.0608570104; RA Wang X., Truckses D.M., Takada S., Matsumura T., Tanese N., Jacobson R.H.; RT "Conserved region I of human coactivator TAF4 binds to a short hydrophobic RT motif present in transcriptional regulators."; RL Proc. Natl. Acad. Sci. U.S.A. 104:7839-7844(2007). RN [17] {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). RN [18] RP VARIANTS MRD73 450-GLN--LYS-1085 DEL; 677-GLN--LYS-1085 DEL AND RP 729-GLN--LYS-1085 DEL. RX PubMed=35904126; DOI=10.1002/humu.24444; RA Janssen B.D.E., van den Boogaard M.H., Lichtenbelt K., Seaby E.G., RA Stals K., Ellard S., Newbury-Ecob R., Dixit A., Roht L., Pajusalu S., RA Ounap K., Firth H.V., Buckley M., Wilson M., Roscioli T., Tidwell T., RA Mao R., Ennis S., Holwerda S.J., van Gassen K., van Jaarsveld R.H.; RT "De novo putative loss-of-function variants in TAF4 are associated with a RT neuro-developmental disorder."; RL Hum. Mutat. 43:1844-1851(2022). 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, CC PubMed:10594036, PubMed:8942982). TAF4 may maintain an association CC between the TFIID and TFIIA complexes, while bound to the promoter, CC together with TBP, during PIC assembly (PubMed:33795473). Potentiates CC transcriptional activation by the AF-2S of the retinoic acid, vitamin CC D3 and thyroid hormone (PubMed:9192867). {ECO:0000269|PubMed:10594036, CC ECO:0000269|PubMed:33795473, ECO:0000269|PubMed:8942982, CC ECO:0000269|PubMed:9192867}. 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 (PubMed:33795473, CC PubMed:10594036). Component of the TFTC-HAT complex, at least composed CC of TAF5L, TAF6L, TADA3L, SUPT3H, TAF2, TAF4, TAF5, GCN5L2/GCN5, TAF10, CC TAF12 and TRRAP (PubMed:10373431, PubMed:12601814). Component of some CC MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, CC ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative CC components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, CC MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10 (PubMed:15960975). CC Interacts with ATF7; the interaction inhibits ATF7-mediated CC tranactivation (PubMed:15735663). {ECO:0000269|PubMed:10373431, CC ECO:0000269|PubMed:10594036, ECO:0000269|PubMed:12601814, CC ECO:0000269|PubMed:15735663, ECO:0000269|PubMed:15960975, CC ECO:0000269|PubMed:33795473}. CC -!- SUBUNIT: (Microbial infection) Interacts with SV40 Large T antigen. CC {ECO:0000269|PubMed:8647434}. CC -!- INTERACTION: CC O00268; O43889: CREB3; NbExp=2; IntAct=EBI-1034261, EBI-625002; CC O00268; Q9NS37: CREBZF; NbExp=2; IntAct=EBI-1034261, EBI-632965; CC O00268; Q16514-1: TAF12; NbExp=16; IntAct=EBI-1034261, EBI-1034253; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 73 CC (MRD73) [MIM:620450]: An autosomal dominant disorder characterized by CC intellectual disability ranging from mild to severe, developmental CC delay, speech delay, behavioral abnormalities, and non-specific CC dysmorphic facial features. {ECO:0000269|PubMed:33875846, CC ECO:0000269|PubMed:35904126}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the TAF4 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/taf4/"; 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; Y11354; CAA72189.1; -; mRNA. DR EMBL; AY623115; AAT38111.1; -; Genomic_DNA. DR EMBL; AL109911; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137077; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW75407.1; -; Genomic_DNA. DR EMBL; U75308; AAC50901.1; -; mRNA. DR CCDS; CCDS33500.1; -. DR RefSeq; NP_003176.2; NM_003185.3. DR PDB; 1H3O; X-ray; 2.30 A; A/C=872-945. DR PDB; 2P6V; X-ray; 2.00 A; A=575-688. DR PDB; 6MZC; EM; 4.50 A; E=1-1085. DR PDB; 6MZD; EM; 9.80 A; D=1-1085. DR PDB; 6MZL; EM; 23.00 A; D/E=1-1085. DR PDB; 6MZM; EM; 7.50 A; D=61-1085. DR PDB; 7EDX; EM; 4.50 A; D/d=1-1085. DR PDB; 7EG7; EM; 6.20 A; D/d=1-1085. DR PDB; 7EG8; EM; 7.40 A; D/d=1-1085. DR PDB; 7EG9; EM; 3.70 A; D/d=1-1085. DR PDB; 7EGA; EM; 4.10 A; D/d=1-1085. DR PDB; 7EGB; EM; 3.30 A; D/d=1-1085. DR PDB; 7EGC; EM; 3.90 A; D/d=1-1085. DR PDB; 7EGD; EM; 6.75 A; D/d=1-1085. DR PDB; 7EGE; EM; 9.00 A; D/d=1-1085. DR PDB; 7EGF; EM; 3.16 A; d=1-1085. DR PDB; 7EGG; EM; 2.77 A; D=1-1085. DR PDB; 7EGI; EM; 9.82 A; D/d=1-1085. DR PDB; 7EGJ; EM; 8.64 A; D/d=1-1085. DR PDB; 7ENA; EM; 4.07 A; DD/Dd=1-1085. DR PDB; 7ENC; EM; 4.13 A; DD/Dd=1-1085. DR PDB; 8GXQ; EM; 5.04 A; DD/Dd=1-1085. DR PDB; 8GXS; EM; 4.16 A; DD/Dd=1-1085. DR PDB; 8WAK; EM; 5.47 A; D/d=1-1085. DR PDB; 8WAL; EM; 8.52 A; D/d=1-1085. DR PDB; 8WAN; EM; 6.07 A; D/d=1-1085. DR PDB; 8WAO; EM; 6.40 A; D/d=1-1085. DR PDB; 8WAP; EM; 5.85 A; D/d=1-1085. DR PDB; 8WAQ; EM; 6.29 A; D/d=1-1085. DR PDB; 8WAR; EM; 7.20 A; D/d=1-1085. DR PDB; 8WAS; EM; 6.13 A; D/d=1-1085. DR PDBsum; 1H3O; -. DR PDBsum; 2P6V; -. 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 PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR PDBsum; 8WAK; -. DR PDBsum; 8WAL; -. DR PDBsum; 8WAN; -. DR PDBsum; 8WAO; -. DR PDBsum; 8WAP; -. DR PDBsum; 8WAQ; -. DR PDBsum; 8WAR; -. DR PDBsum; 8WAS; -. DR AlphaFoldDB; O00268; -. DR EMDB; EMD-31075; -. DR EMDB; EMD-31107; -. DR EMDB; EMD-31108; -. DR EMDB; EMD-31109; -. DR EMDB; EMD-31110; -. DR EMDB; EMD-31111; -. DR EMDB; EMD-31112; -. DR EMDB; EMD-31113; -. DR EMDB; EMD-31114; -. DR EMDB; EMD-31115; -. DR EMDB; EMD-31116; -. DR EMDB; EMD-31118; -. DR EMDB; EMD-31119; -. DR EMDB; EMD-31204; -. DR EMDB; EMD-31207; -. DR EMDB; EMD-34359; -. DR EMDB; EMD-34360; -. DR EMDB; EMD-9298; -. DR EMDB; EMD-9302; -. DR EMDB; EMD-9305; -. DR EMDB; EMD-9306; -. DR SMR; O00268; -. DR BioGRID; 112737; 135. DR ComplexPortal; CPX-903; TFTC histone acetylation complex. DR ComplexPortal; CPX-915; General transcription factor complex TFIID. DR CORUM; O00268; -. DR DIP; DIP-35350N; -. DR ELM; O00268; -. DR IntAct; O00268; 39. DR MINT; O00268; -. DR STRING; 9606.ENSP00000252996; -. DR GlyConnect; 2870; 1 O-GlcNAc glycan (1 site). DR GlyCosmos; O00268; 10 sites, 2 glycans. DR GlyGen; O00268; 17 sites, 2 O-linked glycans (17 sites). DR iPTMnet; O00268; -. DR PhosphoSitePlus; O00268; -. DR BioMuta; TAF4; -. DR EPD; O00268; -. DR jPOST; O00268; -. DR MassIVE; O00268; -. DR MaxQB; O00268; -. DR PaxDb; 9606-ENSP00000252996; -. DR PeptideAtlas; O00268; -. DR ProteomicsDB; 47818; -. DR Pumba; O00268; -. DR Antibodypedia; 1785; 106 antibodies from 24 providers. DR DNASU; 6874; -. DR Ensembl; ENST00000252996.9; ENSP00000252996.3; ENSG00000130699.20. DR GeneID; 6874; -. DR KEGG; hsa:6874; -. DR MANE-Select; ENST00000252996.9; ENSP00000252996.3; NM_003185.4; NP_003176.2. DR UCSC; uc002ybs.3; human. DR AGR; HGNC:11537; -. DR CTD; 6874; -. DR DisGeNET; 6874; -. DR GeneCards; TAF4; -. DR HGNC; HGNC:11537; TAF4. DR HPA; ENSG00000130699; Low tissue specificity. DR MalaCards; TAF4; -. DR MIM; 601796; gene. DR MIM; 620450; phenotype. DR neXtProt; NX_O00268; -. DR OpenTargets; ENSG00000130699; -. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR PharmGKB; PA36312; -. DR VEuPathDB; HostDB:ENSG00000130699; -. DR eggNOG; KOG2341; Eukaryota. DR GeneTree; ENSGT00390000011620; -. DR HOGENOM; CLU_010576_0_0_1; -. DR InParanoid; O00268; -. DR OMA; GQTMQGG; -. DR OrthoDB; 2910924at2759; -. DR PhylomeDB; O00268; -. DR TreeFam; TF316520; -. DR PathwayCommons; O00268; -. 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-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation. 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; O00268; -. DR SIGNOR; O00268; -. DR BioGRID-ORCS; 6874; 143 hits in 1170 CRISPR screens. DR ChiTaRS; TAF4; human. DR EvolutionaryTrace; O00268; -. DR GeneWiki; TAF4; -. DR GenomeRNAi; 6874; -. DR Pharos; O00268; Tbio. DR PRO; PR:O00268; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; O00268; Protein. DR Bgee; ENSG00000130699; Expressed in right testis and 101 other cell types or tissues. DR ExpressionAtlas; O00268; baseline and differential. DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl. DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; EXP:ComplexPortal. DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA. DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:MGI. DR GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB. DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:CAFA. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0006352; P:DNA-templated transcription initiation; IDA:UniProtKB. DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0006282; P:regulation of DNA repair; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IPI:ComplexPortal. DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:UniProtKB. DR CDD; cd08045; TAF4; 1. DR DisProt; DP01170; -. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR Gene3D; 1.20.120.1110; TAFH/NHR1 domain; 1. DR IDEAL; IID00231; -. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR045144; TAF4. DR InterPro; IPR007900; TAF4_C. DR InterPro; IPR037249; TAFH/NHR1_dom_sf. DR InterPro; IPR003894; TAFH_NHR1. DR PANTHER; PTHR15138; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 4; 1. DR PANTHER; PTHR15138:SF18; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 4; 1. DR Pfam; PF05236; TAF4; 1. DR Pfam; PF07531; TAFH; 1. DR SMART; SM00549; TAFH; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR SUPFAM; SSF158553; TAFH domain-like; 1. DR PROSITE; PS51119; TAFH; 1. DR Genevisible; O00268; HS. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disease variant; KW Host-virus interaction; Intellectual disability; Methylation; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..1085 FT /note="Transcription initiation factor TFIID subunit 4" FT /id="PRO_0000118869" FT DOMAIN 590..687 FT /note="TAFH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00440" FT REGION 66..204 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 243..341 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 383..425 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 479..499 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 566..586 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 870..913 FT /note="Minimal region required to interact with TAF12" FT /evidence="ECO:0000269|PubMed:10594036" FT REGION 1015..1049 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 82..128 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 173..189 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 245..298 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 384..398 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 408..425 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 109 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 424 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 435 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 594 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0007744|PDB:2P6V" FT MOD_RES 595 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0007744|PDB:2P6V" FT MOD_RES 597 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0007744|PDB:2P6V" FT MOD_RES 605 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0007744|PDB:2P6V" FT MOD_RES 611 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0007744|PDB:2P6V" FT MOD_RES 621 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0007744|PDB:2P6V" FT MOD_RES 631 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0007744|PDB:2P6V" FT MOD_RES 658 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0007744|PDB:2P6V" FT VARIANT 450..1085 FT /note="Missing (in MRD73; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:35904126" FT /id="VAR_088796" FT VARIANT 651 FT /note="P -> L (in dbSNP:rs6089604)" FT /id="VAR_052258" FT VARIANT 677..1085 FT /note="Missing (in MRD73; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:35904126" FT /id="VAR_088797" FT VARIANT 729..1085 FT /note="Missing (in MRD73; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:35904126" FT /id="VAR_088798" FT VARIANT 949..1085 FT /note="Missing (in MRD73; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:33875846" FT /id="VAR_088799" FT CONFLICT 105..117 FT /note="PGPPSPRRPLVPA -> GRGLLQQRGGRES (in Ref. 5; FT AAC50901)" FT /evidence="ECO:0000305" FT CONFLICT 136 FT /note="S -> A (in Ref. 1; CAA72189 and 5; AAC50901)" FT /evidence="ECO:0000305" FT CONFLICT 186..187 FT /note="Missing (in Ref. 1; CAA72189 and 5; AAC50901)" FT /evidence="ECO:0000305" FT CONFLICT 235..266 FT /note="Missing (in Ref. 5; AAC50901)" FT /evidence="ECO:0000305" FT CONFLICT 295 FT /note="P -> L (in Ref. 5; AAC50901)" FT /evidence="ECO:0000305" FT HELIX 585..593 FT /evidence="ECO:0007829|PDB:2P6V" FT HELIX 599..604 FT /evidence="ECO:0007829|PDB:2P6V" FT HELIX 614..620 FT /evidence="ECO:0007829|PDB:2P6V" FT HELIX 623..628 FT /evidence="ECO:0007829|PDB:2P6V" FT HELIX 634..644 FT /evidence="ECO:0007829|PDB:2P6V" FT HELIX 653..657 FT /evidence="ECO:0007829|PDB:2P6V" FT HELIX 661..666 FT /evidence="ECO:0007829|PDB:2P6V" FT HELIX 671..677 FT /evidence="ECO:0007829|PDB:2P6V" FT HELIX 843..856 FT /evidence="ECO:0007829|PDB:7EGG" FT HELIX 875..887 FT /evidence="ECO:0007829|PDB:1H3O" FT TURN 888..890 FT /evidence="ECO:0007829|PDB:1H3O" FT HELIX 898..918 FT /evidence="ECO:0007829|PDB:1H3O" FT HELIX 923..925 FT /evidence="ECO:0007829|PDB:7EGF" FT TURN 928..930 FT /evidence="ECO:0007829|PDB:7EGG" FT STRAND 932..936 FT /evidence="ECO:0007829|PDB:7EGG" FT HELIX 940..969 FT /evidence="ECO:0007829|PDB:7EGG" FT STRAND 1056..1058 FT /evidence="ECO:0007829|PDB:7EGG" FT HELIX 1060..1065 FT /evidence="ECO:0007829|PDB:7EGG" FT STRAND 1068..1071 FT /evidence="ECO:0007829|PDB:7EGG" FT STRAND 1074..1076 FT /evidence="ECO:0007829|PDB:7EGG" FT HELIX 1077..1082 FT /evidence="ECO:0007829|PDB:7EGG" SQ SEQUENCE 1085 AA; 110114 MW; BC2F5B5F143DB145 CRC64; MAAGSDLLDE VFFNSEVDEK VVSDLVGSLE SQLAASAAHH HHLAPRTPEV RAAAAGALGN HVVSGSPAGA AGAGPAAPAE GAPGAAPEPP PAGRARPGGG GPQRPGPPSP RRPLVPAGPA PPAAKLRPPP EGSAGSCAPV PAAAAVAAGP EPAPAGPAKP AGPAALAARA GPGPGPGPGP GPGPGPGKPA GPGAAQTLNG SAALLNSHHA AAPAVSLVNN GPAALLPLPK PAAPGTVIQT PPFVGAAAPP APAAPSPPAA PAPAAPAAAP PPPPPAPATL ARPPGHPAGP PTAAPAVPPP AAAQNGGSAG AAPAPAPAAG GPAGVSGQPG PGAAAAAPAP GVKAESPKRV VQAAPPAAQT LAASGPASTA ASMVIGPTMQ GALPSPAAVP PPAPGTPTGL PKGAAGAVTQ SLSRTPTATT SGIRATLTPT VLAPRLPQPP QNPTNIQNFQ LPPGMVLVRS ENGQLLMIPQ QALAQMQAQA HAQPQTTMAP RPATPTSAPP VQISTVQAPG TPIIARQVTP TTIIKQVSQA QTTVQPSATL QRSPGVQPQL VLGGAAQTAS LGTATAVQTG TPQRTVPGAT TTSSAATETM ENVKKCKNFL STLIKLASSG KQSTETAANV KELVQNLLDG KIEAEDFTSR LYRELNSSPQ PYLVPFLKRS LPALRQLTPD SAAFIQQSQQ QPPPPTSQAT TALTAVVLSS SVQRTAGKTA ATVTSALQPP VLSLTQPTQV GVGKQGQPTP LVIQQPPKPG ALIRPPQVTL TQTPMVALRQ PHNRIMLTTP QQIQLNPLQP VPVVKPAVLP GTKALSAVSA QAAAAQKNKL KEPGGGSFRD DDDINDVASM AGVNLSEESA RILATNSELV GTLTRSCKDE TFLLQAPLQR RILEIGKKHG ITELHPDVVS YVSHATQQRL QNLVEKISET AQQKNFSYKD DDRYEQASDV RAQLKFFEQL DQIEKQRKDE QEREILMRAA KSRSRQEDPE QLRLKQKAKE MQQQELAQMR QRDANLTALA AIGPRKKRKV DCPGPGSGAE GSGPGSVVPG SSGVGTPRQF TRQRITRVNL RDLIFCLENE RETSHSLLLY KAFLK //