ID TAF5_HUMAN Reviewed; 800 AA. AC Q15542; A8K5B4; B2RMR0; B7ZKJ6; Q53EM4; Q5SYD5; Q86UZ7; Q9Y4K5; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 3. DT 27-MAR-2024, entry version 218. DE RecName: Full=Transcription initiation factor TFIID subunit 5; DE AltName: Full=Transcription initiation factor TFIID 100 kDa subunit; DE Short=TAF(II)100; DE Short=TAFII-100; DE Short=TAFII100; GN Name=TAF5; Synonyms=TAF2D; 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] (ISOFORM LONG), FUNCTION, AND VARIANT ALA-130. RC TISSUE=Cervix carcinoma; RX PubMed=8758937; DOI=10.1002/j.1460-2075.1996.tb00740.x; RA Dubrovskaya V., Lavigne A.-C., Davidson I., Acker J., Staub A., Tora L.; RT "Distinct domains of hTAFII100 are required for functional interaction with RT transcription factor TFIIF beta (RAP30) and incorporation into the TFIID RT complex."; RL EMBO J. 15:3702-3712(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), PROTEIN SEQUENCE OF 109-117; RP 119-142; 151-174; 372-388; 611-621; 635-649 AND 737-742, AND ALTERNATIVE RP SPLICING. RC TISSUE=Cervix carcinoma; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), AND VARIANT ALA-130. RC TISSUE=Cervix carcinoma; RX PubMed=9045704; DOI=10.1074/jbc.272.10.6714; RA Tao Y., Guermah M., Martinez E., Oegelschlaeger T., Hasegawa S., Takada R., RA Yamamoto T., Horikoshi M., Roeder R.G.; RT "Specific interactions and potential functions of human TAFII100."; RL J. Biol. Chem. 272:6714-6721(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANT ALA-130. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT), AND RP VARIANT ALA-130. RC TISSUE=Prostate, 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 [9] 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 [10] RP IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H; RP TAF2; TAF4; TRRAP; 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 [11] 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 188-343, AND SUBUNIT. RX PubMed=17227857; DOI=10.1073/pnas.0610297104; RA Bhattacharya S., Takada S., Jacobson R.H.; RT "Structural analysis and dimerization potential of the human TAF5 subunit RT of TFIID."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1189-1194(2007). RN [14] {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} 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, CC PubMed:8758937, PubMed:8942982, PubMed:9045704). The TFIID complex CC structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C CC (PubMed:33795473). TAF5 is involved in two modules of TFIID, in TFIID-A CC together with TAF3 and TBP, and in TFIID-B with TAF8 (PubMed:33795473). CC Involved in contacts between TFIID and TFIIF in the PIC CC (PubMed:33795473). {ECO:0000269|PubMed:33795473, CC ECO:0000269|PubMed:8758937, ECO:0000269|PubMed:8942982, CC ECO:0000269|PubMed:9045704}. CC -!- SUBUNIT: Homodimer (PubMed:17227857). Component of the TFIID basal CC transcription factor complex, composed of TATA-box-binding protein TBP, CC and a number of TBP-associated factors (TAFs), including TAF1, TAF2, CC TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13 CC (PubMed:10373431, PubMed:33795473). The TFIID complex structure can be CC divided into 3 modules TFIID-A, TFIID-B, and TFIID-C (PubMed:33795473). CC TAF5 forms the TFIID-A module together with TAF3 and TBP, and in TFIID- CC B with TAF8 (PubMed:33795473). Component of the TFTC-HAT complex, at CC least composed of TAF5L, TAF6L, TADA3L, SUPT3H/SPT3, TAF2, TAF4, TAF5, CC GCN5L2/GCN5, TAF10 and TRRAP (PubMed:10373431, PubMed:12601814, CC PubMed:17227857). TBP is not part of the TFTC-HAT complex CC (PubMed:10373431, PubMed:12601814). Interacts strongly with the histone CC H4-related TAF6 and the histone H3-related TAF9, as well as a stable CC complex comprised of both TAF6 and TAF9 (PubMed:9045704). Apparently CC weaker interactions with TBP, TAF1, TAF11, and TAF12, but not TAF7, CC also have been observed (PubMed:8758937, PubMed:9045704). CC {ECO:0000269|PubMed:10373431, ECO:0000269|PubMed:12601814, CC ECO:0000269|PubMed:17227857, ECO:0000269|PubMed:33795473, CC ECO:0000269|PubMed:8758937, ECO:0000269|PubMed:9045704}. CC -!- SUBUNIT: (Microbial infection) Interacts with SV40 Large T antigen. CC {ECO:0000269|PubMed:8647434}. CC -!- INTERACTION: CC Q15542; Q15542: TAF5; NbExp=4; IntAct=EBI-1560145, EBI-1560145; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=Q15542-1; Sequence=Displayed; CC Name=Short; CC IsoId=Q15542-2; Sequence=VSP_006787; CC -!- DOMAIN: Distinct domains of TAF5/TAFII100 are required for functional CC interaction with transcription factor TFIIFB (RAP30) and incorporation CC into the TFIID complex. CC -!- SIMILARITY: Belongs to the WD repeat TAF5 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC50902.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAD97335.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; X95525; CAA64777.1; -; mRNA. DR EMBL; U75309; AAC50902.1; ALT_INIT; mRNA. DR EMBL; U80191; AAC51215.1; -; mRNA. DR EMBL; AK223615; BAD97335.1; ALT_INIT; mRNA. DR EMBL; AK291229; BAF83918.1; -; mRNA. DR EMBL; AL591408; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49645.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49646.1; -; Genomic_DNA. DR EMBL; BC052268; AAH52268.2; -; mRNA. DR EMBL; BC136340; AAI36341.1; -; mRNA. DR EMBL; BC136348; AAI36349.1; -; mRNA. DR CCDS; CCDS7547.1; -. [Q15542-1] DR CCDS; CCDS91341.1; -. [Q15542-2] DR RefSeq; NP_008882.2; NM_006951.4. [Q15542-1] DR RefSeq; NP_620640.1; NM_139052.2. [Q15542-2] DR PDB; 2NXP; X-ray; 2.17 A; A/B/C/D/E/F/G/H=188-343. DR PDB; 6F3T; X-ray; 2.50 A; A/B/C/D=194-800. DR PDB; 6MZC; EM; 4.50 A; G=1-800. DR PDB; 6MZD; EM; 9.80 A; F=1-800. DR PDB; 6MZL; EM; 23.00 A; F/G=1-800. DR PDB; 6MZM; EM; 7.50 A; G=1-800. DR PDB; 7EDX; EM; 4.50 A; E/e=1-800. DR PDB; 7EG7; EM; 6.20 A; E/e=1-800. DR PDB; 7EG8; EM; 7.40 A; E/e=1-800. DR PDB; 7EG9; EM; 3.70 A; E/e=1-800. DR PDB; 7EGA; EM; 4.10 A; E/e=1-800. DR PDB; 7EGB; EM; 3.30 A; E/e=1-800. DR PDB; 7EGC; EM; 3.90 A; E/e=1-800. DR PDB; 7EGD; EM; 6.75 A; E/e=1-800. DR PDB; 7EGE; EM; 9.00 A; E/e=1-800. DR PDB; 7EGF; EM; 3.16 A; e=1-800. DR PDB; 7EGG; EM; 2.77 A; E=1-800. DR PDB; 7EGI; EM; 9.82 A; E/e=1-800. DR PDB; 7EGJ; EM; 8.64 A; E/e=1-800. DR PDB; 7ENA; EM; 4.07 A; DE/De=1-800. DR PDB; 7ENC; EM; 4.13 A; DE/De=1-800. DR PDB; 8GXQ; EM; 5.04 A; DE/De=1-800. DR PDB; 8GXS; EM; 4.16 A; DE/De=1-800. DR PDB; 8WAK; EM; 5.47 A; E/e=1-800. DR PDB; 8WAL; EM; 8.52 A; E/e=1-800. DR PDB; 8WAN; EM; 6.07 A; E/e=1-800. DR PDB; 8WAO; EM; 6.40 A; E/e=1-800. DR PDB; 8WAP; EM; 5.85 A; E/e=1-800. DR PDB; 8WAQ; EM; 6.29 A; E/e=1-800. DR PDB; 8WAR; EM; 7.20 A; E/e=1-800. DR PDB; 8WAS; EM; 6.13 A; E/e=1-800. DR PDBsum; 2NXP; -. 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 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; Q15542; -. 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; Q15542; -. DR BioGRID; 112740; 86. 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 CORUM; Q15542; -. DR DIP; DIP-28150N; -. DR IntAct; Q15542; 41. DR MINT; Q15542; -. DR STRING; 9606.ENSP00000358854; -. DR GlyCosmos; Q15542; 1 site, 2 glycans. DR GlyGen; Q15542; 1 site, 2 O-linked glycans (1 site). DR iPTMnet; Q15542; -. DR PhosphoSitePlus; Q15542; -. DR BioMuta; TAF5; -. DR DMDM; 78103206; -. DR EPD; Q15542; -. DR jPOST; Q15542; -. DR MassIVE; Q15542; -. DR MaxQB; Q15542; -. DR PaxDb; 9606-ENSP00000358854; -. DR PeptideAtlas; Q15542; -. DR ProteomicsDB; 60623; -. [Q15542-1] DR ProteomicsDB; 60624; -. [Q15542-2] DR Pumba; Q15542; -. DR TopDownProteomics; Q15542-2; -. [Q15542-2] DR Antibodypedia; 1798; 166 antibodies from 23 providers. DR DNASU; 6877; -. DR Ensembl; ENST00000369839.4; ENSP00000358854.3; ENSG00000148835.12. [Q15542-1] DR Ensembl; ENST00000692195.1; ENSP00000510076.1; ENSG00000148835.12. [Q15542-2] DR GeneID; 6877; -. DR KEGG; hsa:6877; -. DR MANE-Select; ENST00000369839.4; ENSP00000358854.3; NM_006951.5; NP_008882.2. DR UCSC; uc001kwv.5; human. [Q15542-1] DR AGR; HGNC:11539; -. DR CTD; 6877; -. DR DisGeNET; 6877; -. DR GeneCards; TAF5; -. DR HGNC; HGNC:11539; TAF5. DR HPA; ENSG00000148835; Tissue enhanced (testis). DR MIM; 601787; gene. DR neXtProt; NX_Q15542; -. DR OpenTargets; ENSG00000148835; -. DR PharmGKB; PA36314; -. DR VEuPathDB; HostDB:ENSG00000148835; -. DR eggNOG; KOG0263; Eukaryota. DR GeneTree; ENSGT00940000153342; -. DR HOGENOM; CLU_005884_2_0_1; -. DR InParanoid; Q15542; -. DR OMA; RCAFAPE; -. DR OrthoDB; 3138699at2759; -. DR PhylomeDB; Q15542; -. DR TreeFam; TF300669; -. DR PathwayCommons; Q15542; -. 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-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; Q15542; -. DR SIGNOR; Q15542; -. DR BioGRID-ORCS; 6877; 550 hits in 1174 CRISPR screens. DR ChiTaRS; TAF5; human. DR EvolutionaryTrace; Q15542; -. DR GeneWiki; TAF5; -. DR GenomeRNAi; 6877; -. DR Pharos; Q15542; Tbio. DR PRO; PR:Q15542; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q15542; Protein. DR Bgee; ENSG00000148835; Expressed in secondary oocyte and 171 other cell types or tissues. DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA. DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; 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:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IMP:UniProtKB. 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: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:0006367; P:transcription initiation at RNA polymerase II promoter; IDA:UniProtKB. DR CDD; cd08044; TAF5_NTD2; 1. DR CDD; cd00200; WD40; 1. DR Gene3D; 1.25.40.500; TFIID subunit TAF5, NTD2 domain; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR006594; LisH. DR InterPro; IPR007582; TFIID_NTD2. DR InterPro; IPR037264; TFIID_NTD2_sf. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19879; TRANSCRIPTION INITIATION FACTOR TFIID; 1. DR PANTHER; PTHR19879:SF4; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 5; 1. DR Pfam; PF04494; TFIID_NTD2; 1. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF160897; Taf5 N-terminal domain-like; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50896; LISH; 1. DR PROSITE; PS00678; WD_REPEATS_1; 3. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. DR Genevisible; Q15542; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Host-virus interaction; Nucleus; Reference proteome; Repeat; Transcription; KW Transcription regulation; WD repeat. FT CHAIN 1..800 FT /note="Transcription initiation factor TFIID subunit 5" FT /id="PRO_0000051257" FT DOMAIN 92..124 FT /note="LisH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126" FT REPEAT 468..507 FT /note="WD 1" FT /evidence="ECO:0000255" FT REPEAT 541..580 FT /note="WD 2" FT /evidence="ECO:0000255" FT REPEAT 583..624 FT /note="WD 3" FT /evidence="ECO:0000255" FT REPEAT 625..666 FT /note="WD 4" FT /evidence="ECO:0000255" FT REPEAT 667..706 FT /note="WD 5" FT /evidence="ECO:0000255" FT REPEAT 709..748 FT /note="WD 6" FT /evidence="ECO:0000255" FT REGION 1..74 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 153..189 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 194..340 FT /note="NTD2; involved in homo-dimerization; also involved FT in TFIID-TFIIF contacts in the RNA Pol II pre-initiation FT complex (PIC)" FT /evidence="ECO:0000303|PubMed:33795473, FT ECO:0007744|PDB:2NXP" FT REGION 384..438 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 34..62 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 556..610 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_006787" FT VARIANT 130 FT /note="S -> A (in dbSNP:rs10883859)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:8758937, ECO:0000269|PubMed:9045704, FT ECO:0000269|Ref.5" FT /id="VAR_018462" FT CONFLICT 126 FT /note="A -> T (in Ref. 1; CAA64777 and 5; BAD97335)" FT /evidence="ECO:0000305" FT CONFLICT 300 FT /note="F -> L (in Ref. 1; CAA64777)" FT /evidence="ECO:0000305" FT CONFLICT 455 FT /note="P -> S (in Ref. 1; CAA64777)" FT /evidence="ECO:0000305" FT CONFLICT 469 FT /note="A -> V (in Ref. 1; CAA64777)" FT /evidence="ECO:0000305" FT CONFLICT 778 FT /note="Missing (in Ref. 1; CAA64777)" FT /evidence="ECO:0000305" FT CONFLICT 787 FT /note="R -> L (in Ref. 8; AAH52268)" FT /evidence="ECO:0000305" FT HELIX 198..202 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 203..205 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:6F3T" FT HELIX 214..226 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 230..236 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 237..239 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 240..253 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 257..267 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 273..275 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 276..283 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 288..291 FT /evidence="ECO:0007829|PDB:2NXP" FT TURN 292..294 FT /evidence="ECO:0007829|PDB:7EGG" FT HELIX 295..300 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:2NXP" FT STRAND 305..310 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 311..321 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 324..326 FT /evidence="ECO:0007829|PDB:6F3T" FT HELIX 328..335 FT /evidence="ECO:0007829|PDB:2NXP" FT STRAND 338..342 FT /evidence="ECO:0007829|PDB:2NXP" FT HELIX 349..355 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 359..362 FT /evidence="ECO:0007829|PDB:6F3T" FT HELIX 365..368 FT /evidence="ECO:0007829|PDB:6F3T" FT TURN 424..428 FT /evidence="ECO:0007829|PDB:7EGG" FT HELIX 434..447 FT /evidence="ECO:0007829|PDB:6F3T" FT TURN 454..456 FT /evidence="ECO:0007829|PDB:7EGG" FT STRAND 460..465 FT /evidence="ECO:0007829|PDB:6F3T" FT HELIX 466..469 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 473..478 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 484..489 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 494..498 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 500..505 FT /evidence="ECO:0007829|PDB:6F3T" FT HELIX 510..513 FT /evidence="ECO:0007829|PDB:6F3T" FT HELIX 514..517 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 518..520 FT /evidence="ECO:0007829|PDB:6F3T" FT HELIX 522..527 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 528..531 FT /evidence="ECO:0007829|PDB:7EGF" FT STRAND 534..539 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 546..551 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 555..562 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 565..571 FT /evidence="ECO:0007829|PDB:6F3T" FT TURN 572..574 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 576..582 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 588..593 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 597..604 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 607..613 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 620..624 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 630..635 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 639..646 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 649..655 FT /evidence="ECO:0007829|PDB:6F3T" FT TURN 656..658 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 661..666 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 672..677 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 681..688 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 693..697 FT /evidence="ECO:0007829|PDB:6F3T" FT TURN 698..701 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 702..707 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 714..719 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 723..730 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 733..739 FT /evidence="ECO:0007829|PDB:6F3T" FT HELIX 740..743 FT /evidence="ECO:0007829|PDB:6F3T" FT TURN 744..746 FT /evidence="ECO:0007829|PDB:6F3T" FT HELIX 765..768 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 769..774 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 780..785 FT /evidence="ECO:0007829|PDB:6F3T" FT STRAND 787..789 FT /evidence="ECO:0007829|PDB:7EGF" FT STRAND 790..795 FT /evidence="ECO:0007829|PDB:6F3T" SQ SEQUENCE 800 AA; 86830 MW; 87A178BFB7071992 CRC64; MAALAEEQTE VAVKLEPEGP PTLLPPQAGD GAGEGSGGTT NNGPNGGGGN VAASSSTGGD GGTPKPTVAV SAAAPAGAAP VPAAAPDAGA PHDRQTLLAV LQFLRQSKLR EAEEALRREA GLLEEAVAGS GAPGEVDSAG AEVTSALLSR VTASAPGPAA PDPPGTGASG ATVVSGSASG PAAPGKVGSV AVEDQPDVSA VLSAYNQQGD PTMYEEYYSG LKHFIECSLD CHRAELSQLF YPLFVHMYLE LVYNQHENEA KSFFEKFHGD QECYYQDDLR VLSSLTKKEH MKGNETMLDF RTSKFVLRIS RDSYQLLKRH LQEKQNNQIW NIVQEHLYID IFDGMPRSKQ QIDAMVGSLA GEAKREANKS KVFFGLLKEP EIEVPLDDED EEGENEEGKP KKKKPKKDSI GSKSKKQDPN APPQNRIPLP ELKDSDKLDK IMNMKETTKR VRLGPDCLPS ICFYTFLNAY QGLTAVDVTD DSSLIAGGFA DSTVRVWSVT PKKLRSVKQA SDLSLIDKES DDVLERIMDE KTASELKILY GHSGPVYGAS FSPDRNYLLS SSEDGTVRLW SLQTFTCLVG YKGHNYPVWD TQFSPYGYYF VSGGHDRVAR LWATDHYQPL RIFAGHLADV NCTRFHPNSN YVATGSADRT VRLWDVLNGN CVRIFTGHKG PIHSLTFSPN GRFLATGATD GRVLLWDIGH GLMVGELKGH TDTVCSLRFS RDGEILASGS MDNTVRLWDA IKAFEDLETD DFTTATGHIN LPENSQELLL GTYMTKSTPV VHLHFTRRNL VLAAGAYSPQ //