TAF8_HUMAN
ID TAF8_HUMAN Reviewed; 310 AA.
AC Q7Z7C8; Q5T0K1; Q8N4R9; Q96M52;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Transcription initiation factor TFIID subunit 8;
DE AltName: Full=Protein taube nuss;
DE AltName: Full=TBP-associated factor 43 kDa;
DE AltName: Full=TBP-associated factor 8;
DE AltName: Full=Transcription initiation factor TFIID 43 kDa subunit;
DE Short=TAFII-43;
DE Short=TAFII43;
DE Short=hTAFII43;
GN Name=TAF8; Synonyms=TAFII43, TBN;
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 1), PROTEIN SEQUENCE OF 134-157;
RP 162-178 AND 268-292, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP TBP; TAF1; TAF6; TAF10 AND TAF11.
RX PubMed=14580349; DOI=10.1016/s1097-2765(03)00396-4;
RA Guermah M., Ge K., Chiang C.-M., Roeder R.G.;
RT "The TBN protein, which is essential for early embryonic mouse development,
RT is an inducible TAFII implicated in adipogenesis.";
RL Mol. Cell 12:991-1001(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP INTERACTION WITH TAF10.
RX PubMed=15870280; DOI=10.1128/mcb.25.10.4092-4104.2005;
RA Soutoglou E., Demeny M.A., Scheer E., Fienga G., Sassone-Corsi P., Tora L.;
RT "The nuclear import of TAF10 is regulated by one of its three histone fold
RT domain-containing interaction partners.";
RL Mol. Cell. Biol. 25:4092-4104(2005).
RN [6]
RP INTERACTION IN A SMAT COMPLEX WITH TAF10 AND SUPT7L, AND INTERACTION IN A
RP TFIID COMPLEX WITH TAF1; TAF6; TAF11 AND TBP.
RX PubMed=17375202; DOI=10.1371/journal.pone.0000316;
RA Demeny M.A., Soutoglou E., Nagy Z., Scheer E., Janoshazi A., Richardot M.,
RA Argentini M., Kessler P., Tora L.;
RT "Identification of a small TAF complex and its role in the assembly of TAF-
RT containing complexes.";
RL PLoS ONE 2:E316-E316(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND IDENTIFICATION BY
RP 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, 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 [11] {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:7EGG}
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). The TFIID
CC complex structure can be divided into 3 modules TFIID-A, TFIID-B, and
CC TFIID-C (PubMed:33795473). TAF8 is involved in forming the TFIID-B
CC module, together with TAF5 (PubMed:33795473). Mediates both basal and
CC activator-dependent transcription (PubMed:14580349). Plays a role in
CC the differentiation of preadipocyte fibroblasts to adipocytes, however,
CC does not seem to play a role in differentiation of myoblasts
CC (PubMed:14580349). Required for the integration of TAF10 in the TAF
CC complex (PubMed:14580349). May be important for survival of cells of
CC the inner cell mass which constitute the pluripotent cell population of
CC the early embryo (By similarity). {ECO:0000250|UniProtKB:Q9EQH4,
CC ECO:0000269|PubMed:14580349, 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). Interacts with TBP, TAF1, TAF6, TAF10, TAF11 and
CC TAF13 (PubMed:14580349, PubMed:17375202, PubMed:15870280). Component
CC also of a small TAF complex (SMAT) containing TAF8, TAF10 and SUPT7L
CC (PubMed:17375202). Forms a heterodimer with TAF10 (PubMed:17375202).
CC Interaction with TAF10 is mediated mainly via its histone fold domain
CC while interaction with SUPT7L is via its C-terminal region
CC (PubMed:15870280). {ECO:0000269|PubMed:14580349,
CC ECO:0000269|PubMed:15870280, ECO:0000269|PubMed:17375202,
CC ECO:0000269|PubMed:33795473}.
CC -!- INTERACTION:
CC Q7Z7C8-2; P41091: EIF2S3; NbExp=3; IntAct=EBI-9089028, EBI-1054228;
CC Q7Z7C8-2; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-9089028, EBI-10226858;
CC Q7Z7C8-2; P54652: HSPA2; NbExp=3; IntAct=EBI-9089028, EBI-356991;
CC Q7Z7C8-2; P49591: SARS1; NbExp=3; IntAct=EBI-9089028, EBI-1053431;
CC Q7Z7C8-2; Q12962: TAF10; NbExp=6; IntAct=EBI-9089028, EBI-708376;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14580349}. Cytoplasm
CC {ECO:0000250}. Note=Localized in the cytoplasm and transported from the
CC cytoplasm to the nucleus in some cells, possibly depending on the
CC functional or developmental state of the cell. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z7C8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z7C8-2; Sequence=VSP_030549;
CC Name=3;
CC IsoId=Q7Z7C8-4; Sequence=VSP_030548;
CC -!- INDUCTION: Induced with triglyceride accumulation.
CC -!- DOMAIN: Ectopic expression of the histone fold domain acts as a
CC dominant-negative mutant resulting in differentiation inhibition.
CC -!- MISCELLANEOUS: 'Taube nuss' means 'empty nut' in German.
CC -!- SIMILARITY: Belongs to the TAF8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB71460.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF465841; AAP47094.1; -; mRNA.
DR EMBL; AK057383; BAB71460.1; ALT_FRAME; mRNA.
DR EMBL; AL513008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC119678; AAI19679.1; -; mRNA.
DR EMBL; BC119679; AAI19680.1; -; mRNA.
DR CCDS; CCDS43462.1; -. [Q7Z7C8-1]
DR RefSeq; NP_612639.2; NM_138572.2. [Q7Z7C8-1]
DR RefSeq; XP_011512598.1; XM_011514296.1. [Q7Z7C8-4]
DR PDB; 4WV4; X-ray; 1.91 A; B=25-120.
DR PDB; 4WV6; X-ray; 1.75 A; B/C=297-310.
DR PDB; 5FUR; EM; 8.50 A; L=1-310.
DR PDB; 6MZC; EM; 4.50 A; K=1-310.
DR PDB; 6MZL; EM; 23.00 A; K=1-310.
DR PDB; 6MZM; EM; 7.50 A; K=1-310.
DR PDB; 7EDX; EM; 4.50 A; H=1-310.
DR PDB; 7EG7; EM; 6.20 A; H=1-310.
DR PDB; 7EG8; EM; 7.40 A; H=1-310.
DR PDB; 7EG9; EM; 3.70 A; H=1-310.
DR PDB; 7EGA; EM; 4.10 A; H=1-310.
DR PDB; 7EGB; EM; 3.30 A; H=1-310.
DR PDB; 7EGC; EM; 3.90 A; H=1-310.
DR PDB; 7EGD; EM; 6.75 A; H=1-310.
DR PDB; 7EGE; EM; 9.00 A; H=1-310.
DR PDB; 7EGG; EM; 2.77 A; H=1-310.
DR PDB; 7EGH; EM; 3.04 A; H=1-310.
DR PDB; 7EGI; EM; 9.82 A; H=1-310.
DR PDB; 7EGJ; EM; 8.64 A; H=1-310.
DR PDB; 7ENA; EM; 4.07 A; DH=1-310.
DR PDB; 7ENC; EM; 4.13 A; DH=1-310.
DR PDBsum; 4WV4; -.
DR PDBsum; 4WV6; -.
DR PDBsum; 5FUR; -.
DR PDBsum; 6MZC; -.
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; 7EGG; -.
DR PDBsum; 7EGH; -.
DR PDBsum; 7EGI; -.
DR PDBsum; 7EGJ; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR AlphaFoldDB; Q7Z7C8; -.
DR SMR; Q7Z7C8; -.
DR BioGRID; 126205; 49.
DR ComplexPortal; CPX-915; General transcription factor complex TFIID.
DR ComplexPortal; CPX-930; General transcription factor complex TFIID, TAF4B variant.
DR DIP; DIP-60591N; -.
DR IntAct; Q7Z7C8; 32.
DR MINT; Q7Z7C8; -.
DR STRING; 9606.ENSP00000362068; -.
DR GlyGen; Q7Z7C8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q7Z7C8; -.
DR MetOSite; Q7Z7C8; -.
DR PhosphoSitePlus; Q7Z7C8; -.
DR BioMuta; TAF8; -.
DR DMDM; 74723384; -.
DR EPD; Q7Z7C8; -.
DR jPOST; Q7Z7C8; -.
DR MassIVE; Q7Z7C8; -.
DR MaxQB; Q7Z7C8; -.
DR PaxDb; Q7Z7C8; -.
DR PeptideAtlas; Q7Z7C8; -.
DR PRIDE; Q7Z7C8; -.
DR ProteomicsDB; 69515; -. [Q7Z7C8-1]
DR ProteomicsDB; 69516; -. [Q7Z7C8-2]
DR ProteomicsDB; 69517; -. [Q7Z7C8-4]
DR Antibodypedia; 30123; 147 antibodies from 21 providers.
DR DNASU; 129685; -.
DR Ensembl; ENST00000372977.8; ENSP00000362068.3; ENSG00000137413.17. [Q7Z7C8-1]
DR Ensembl; ENST00000372982.8; ENSP00000362073.4; ENSG00000137413.17. [Q7Z7C8-4]
DR Ensembl; ENST00000456846.6; ENSP00000411900.2; ENSG00000137413.17. [Q7Z7C8-2]
DR Ensembl; ENST00000494547.5; ENSP00000417867.1; ENSG00000137413.17. [Q7Z7C8-4]
DR GeneID; 129685; -.
DR KEGG; hsa:129685; -.
DR MANE-Select; ENST00000372977.8; ENSP00000362068.3; NM_138572.3; NP_612639.2.
DR UCSC; uc003ors.4; human. [Q7Z7C8-1]
DR CTD; 129685; -.
DR DisGeNET; 129685; -.
DR GeneCards; TAF8; -.
DR HGNC; HGNC:17300; TAF8.
DR HPA; ENSG00000137413; Low tissue specificity.
DR MalaCards; TAF8; -.
DR MIM; 609514; gene.
DR neXtProt; NX_Q7Z7C8; -.
DR OpenTargets; ENSG00000137413; -.
DR PharmGKB; PA162405144; -.
DR VEuPathDB; HostDB:ENSG00000137413; -.
DR eggNOG; KOG4336; Eukaryota.
DR GeneTree; ENSGT00390000017567; -.
DR InParanoid; Q7Z7C8; -.
DR OMA; SAHNYCE; -.
DR OrthoDB; 1290064at2759; -.
DR PhylomeDB; Q7Z7C8; -.
DR TreeFam; TF316311; -.
DR PathwayCommons; Q7Z7C8; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; Q7Z7C8; -.
DR SIGNOR; Q7Z7C8; -.
DR BioGRID-ORCS; 129685; 555 hits in 1092 CRISPR screens.
DR ChiTaRS; TAF8; human.
DR GeneWiki; TAF8; -.
DR GenomeRNAi; 129685; -.
DR Pharos; Q7Z7C8; Tbio.
DR PRO; PR:Q7Z7C8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q7Z7C8; protein.
DR Bgee; ENSG00000137413; Expressed in buccal mucosa cell and 145 other tissues.
DR ExpressionAtlas; Q7Z7C8; baseline and differential.
DR Genevisible; Q7Z7C8; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001112; P:DNA-templated transcription open complex formation; IDA:MGI.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IDA:HGNC-UCL.
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:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IDA:MGI.
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; IBA:GO_Central.
DR CDD; cd08049; TAF8; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037818; TAF8.
DR InterPro; IPR019473; TFIID_su8_C.
DR PANTHER; PTHR46469; PTHR46469; 1.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF10406; TAF8_C; 1.
DR SMART; SM00576; BTP; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Developmental protein; Differentiation; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..310
FT /note="Transcription initiation factor TFIID subunit 8"
FT /id="PRO_0000315396"
FT DOMAIN 35..102
FT /note="Histone-fold; involved in forming hexamer structure
FT in TFIID complex"
FT /evidence="ECO:0000269|PubMed:33795473"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 294..307
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 12..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 261..310
FT /note="EDSGAEKENTSVLQQNPSLSGSRNGEENIIDNPYLRPVKKPKIRRKKSLS
FT -> IESRSVTQAGVQWQDLGSLQPPPPGFKRFSSLSLLSSWNYRRILEPRRRTPLSCSR
FT TPPCRVAGMGRRTSSITLICGR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030548"
FT VAR_SEQ 308..310
FT /note="SLS -> PDTF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030549"
FT CONFLICT 139
FT /note="N -> D (in Ref. 2; BAB71460)"
FT /evidence="ECO:0000305"
FT HELIX 29..48
FT /evidence="ECO:0007829|PDB:4WV4"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:4WV4"
FT HELIX 55..80
FT /evidence="ECO:0007829|PDB:4WV4"
FT HELIX 90..99
FT /evidence="ECO:0007829|PDB:4WV4"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4WV4"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:4WV4"
FT HELIX 172..196
FT /evidence="ECO:0007829|PDB:7EGH"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:7EGH"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:7EGH"
SQ SEQUENCE 310 AA; 34262 MW; 0F955828FE9FC0EA CRC64;
MADAAATAGA GGSGTRSGSK QSTNPADNYH LARRRTLQVV VSSLLTEAGF ESAEKASVET
LTEMLQSYIS EIGRSAKSYC EHTARTQPTL SDIVVTLVEM GFNVDTLPAY AKRSQRMVIT
APPVTNQPVT PKALTAGQNR PHPPHIPSHF PEFPDPHTYI KTPTYREPVS DYQVLREKAA
SQRRDVERAL TRFMAKTGET QSLFKDDVST FPLIAARPFT IPYLTALLPS ELEMQQMEET
DSSEQDEQTD TENLALHISM EDSGAEKENT SVLQQNPSLS GSRNGEENII DNPYLRPVKK
PKIRRKKSLS
