TAF5_HUMAN
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 03-AUG-2022, entry version 209.
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};
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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 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 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 AlphaFoldDB; Q15542; -.
DR SMR; Q15542; -.
DR BioGRID; 112740; 78.
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 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; Q15542; -.
DR PeptideAtlas; Q15542; -.
DR PRIDE; Q15542; -.
DR ProteomicsDB; 60623; -. [Q15542-1]
DR ProteomicsDB; 60624; -. [Q15542-2]
DR TopDownProteomics; Q15542-2; -. [Q15542-2]
DR Antibodypedia; 1798; 149 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 CTD; 6877; -.
DR DisGeNET; 6877; -.
DR GeneCards; TAF5; -.
DR HGNC; HGNC:11539; TAF5.
DR HPA; ENSG00000148835; Low tissue specificity.
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; 620721at2759; -.
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; 520 hits in 1097 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 170 other tissues.
DR Genevisible; Q15542; HS.
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:0043966; P:histone H3 acetylation; IDA:ComplexPortal.
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: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:0006282; P:regulation of DNA repair; IC: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 from RNA polymerase II promoter; IDA:UniProtKB.
DR CDD; cd08044; TAF5_NTD2; 1.
DR Gene3D; 1.25.40.500; -; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR037783; Taf5.
DR InterPro; IPR007582; TFIID_NTD2.
DR InterPro; IPR037264; TFIID_NTD2_sf.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19879; PTHR19879; 1.
DR Pfam; PF04494; TFIID_NTD2; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF160897; SSF160897; 1.
DR SUPFAM; SSF50978; SSF50978; 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.
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
