ID TAF8_MOUSE Reviewed; 308 AA.
AC Q9EQH4; Q3TSE4; Q6PES8; Q8C382; Q8C664; Q8C7L7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 154.
DE RecName: Full=Transcription initiation factor TFIID subunit 8;
DE AltName: Full=Protein taube nuss;
DE AltName: Full=TBP-associated factor 8;
GN Name=Taf8; Synonyms=Tbn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11076765; DOI=10.1242/dev.127.24.5449;
RA Voss A.K., Thomas T., Petrou P., Anastassiadis K., Schoeler H., Gruss P.;
RT "Taube nuss is a novel gene essential for the survival of pluripotent cells
RT of early mouse embryos.";
RL Development 127:5449-5461(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Egg, Head, and Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=129; TISSUE=Mammary tumor;
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 [4]
RP FUNCTION.
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).
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 (By similarity). 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) (By
CC similarity). 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 (By similarity). The TFIID
CC complex structure can be divided into 3 modules TFIID-A, TFIID-B, and
CC TFIID-C (By similarity). TAF8 is involved in forming the TFIID-B
CC module, together with TAF5 (By similarity). Mediates both basal and
CC activator-dependent transcription (By similarity). Plays a role in the
CC 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 (By similarity). May be important for survival of cells of the
CC inner cell mass which constitute the pluripotent cell population of the
CC early embryo (PubMed:11076765). {ECO:0000250|UniProtKB:Q7Z7C8,
CC ECO:0000269|PubMed:11076765, ECO:0000269|PubMed:14580349}.
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. Interacts with
CC TBP, TAF1, TAF6, TAF10, TAF11 and TAF13. Component also of a small TAF
CC complex (SMAT) containing TAF8, TAF10 and SUPT7L. Forms a heterodimer
CC with TAF10. Interaction with TAF10 is mediated mainly via its histone
CC fold domain while interaction with SUPT7L is via its C-terminal region.
CC {ECO:0000250|UniProtKB:Q7Z7C8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11076765}. Cytoplasm
CC {ECO:0000269|PubMed:11076765}. Note=Localized in the cytoplasm and
CC transported from the cytoplasm to the nucleus in some cells, possibly
CC depending on the functional or developmental state of the cell.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9EQH4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EQH4-2; Sequence=VSP_030555;
CC Name=3;
CC IsoId=Q9EQH4-3; Sequence=VSP_030553, VSP_030554;
CC Name=4;
CC IsoId=Q9EQH4-4; Sequence=VSP_030552;
CC Name=5;
CC IsoId=Q9EQH4-5; Sequence=VSP_030550, VSP_030551;
CC -!- TISSUE SPECIFICITY: Low level of expression throughout the brain with
CC slightly higher expression in the hippocampus.
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously at very low levels
CC throughout embryonic development. Higher levels of expression seen in
CC inner cell mass and heart. {ECO:0000269|PubMed:11076765}.
CC -!- DISRUPTION PHENOTYPE: Death during early embryonic development. The
CC inner cell mass cells of mutant embryos died of apoptosis.
CC {ECO:0000269|PubMed:11076765}.
CC -!- MISCELLANEOUS: 'Taube nuss' means 'empty nut' in German.
CC -!- SIMILARITY: Belongs to the TAF8 family. {ECO:0000305}.
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DR EMBL; AF222802; AAG01682.1; -; mRNA.
DR EMBL; AK045108; BAC32225.1; -; mRNA.
DR EMBL; AK049949; BAC34001.1; -; mRNA.
DR EMBL; AK076486; BAC36363.1; -; mRNA.
DR EMBL; AK086656; BAC39712.1; -; mRNA.
DR EMBL; AK162110; BAE36731.1; -; mRNA.
DR EMBL; BC057895; AAH57895.1; -; mRNA.
DR CCDS; CCDS37642.1; -. [Q9EQH4-1]
DR CCDS; CCDS89109.1; -. [Q9EQH4-3]
DR RefSeq; NP_071298.1; NM_022015.3. [Q9EQH4-1]
DR RefSeq; XP_006524827.1; XM_006524764.2.
DR RefSeq; XP_006524828.1; XM_006524765.3.
DR RefSeq; XP_006524830.1; XM_006524767.3.
DR AlphaFoldDB; Q9EQH4; -.
DR SMR; Q9EQH4; -.
DR ComplexPortal; CPX-932; General transcription factor complex TFIID.
DR ComplexPortal; CPX-959; General transcription factor complex TFIID, Taf4b variant.
DR CORUM; Q9EQH4; -.
DR STRING; 10090.ENSMUSP00000063201; -.
DR iPTMnet; Q9EQH4; -.
DR PhosphoSitePlus; Q9EQH4; -.
DR EPD; Q9EQH4; -.
DR MaxQB; Q9EQH4; -.
DR PaxDb; 10090-ENSMUSP00000063201; -.
DR PeptideAtlas; Q9EQH4; -.
DR ProteomicsDB; 263244; -. [Q9EQH4-1]
DR ProteomicsDB; 263245; -. [Q9EQH4-2]
DR ProteomicsDB; 263246; -. [Q9EQH4-3]
DR ProteomicsDB; 263247; -. [Q9EQH4-4]
DR ProteomicsDB; 263248; -. [Q9EQH4-5]
DR Pumba; Q9EQH4; -.
DR Antibodypedia; 30123; 154 antibodies from 21 providers.
DR DNASU; 63856; -.
DR Ensembl; ENSMUST00000067103.4; ENSMUSP00000063201.3; ENSMUSG00000023980.8. [Q9EQH4-1]
DR Ensembl; ENSMUST00000233121.2; ENSMUSP00000156629.2; ENSMUSG00000023980.8. [Q9EQH4-2]
DR Ensembl; ENSMUST00000233174.2; ENSMUSP00000156668.2; ENSMUSG00000023980.8. [Q9EQH4-3]
DR GeneID; 63856; -.
DR KEGG; mmu:63856; -.
DR UCSC; uc008cvh.1; mouse. [Q9EQH4-1]
DR UCSC; uc008cvj.1; mouse. [Q9EQH4-4]
DR AGR; MGI:1926879; -.
DR CTD; 129685; -.
DR MGI; MGI:1926879; Taf8.
DR VEuPathDB; HostDB:ENSMUSG00000023980; -.
DR eggNOG; KOG4336; Eukaryota.
DR GeneTree; ENSGT00390000017567; -.
DR HOGENOM; CLU_070829_0_0_1; -.
DR InParanoid; Q9EQH4; -.
DR OMA; SAHNYCE; -.
DR OrthoDB; 5483295at2759; -.
DR PhylomeDB; Q9EQH4; -.
DR TreeFam; TF316311; -.
DR Reactome; R-MMU-6807505; RNA polymerase II transcribes snRNA genes.
DR BioGRID-ORCS; 63856; 24 hits in 82 CRISPR screens.
DR ChiTaRS; Taf8; mouse.
DR PRO; PR:Q9EQH4; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9EQH4; Protein.
DR Bgee; ENSMUSG00000023980; Expressed in granulocyte and 248 other cell types or tissues.
DR Genevisible; Q9EQH4; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001112; P:DNA-templated transcription open complex formation; ISO:MGI.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; ISO:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0060261; P:positive regulation of transcription initiation by RNA polymerase II; ISO:MGI.
DR GO; GO:0045598; P:regulation of fat cell differentiation; ISO:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; ISO:MGI.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd08049; TAF8; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR006565; BTP.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037818; TAF8.
DR InterPro; IPR019473; TFIID_su8_C.
DR PANTHER; PTHR46469; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 8; 1.
DR PANTHER; PTHR46469:SF1; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 8; 1.
DR Pfam; PF07524; Bromo_TP; 1.
DR Pfam; PF10406; TAF8_C; 1.
DR SMART; SM00576; BTP; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7C8"
FT CHAIN 2..308
FT /note="Transcription initiation factor TFIID subunit 8"
FT /id="PRO_0000315398"
FT DOMAIN 35..102
FT /note="Histone-fold"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 292..305
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 13..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7C8"
FT MOD_RES 128
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7C8"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7C8"
FT VAR_SEQ 213..221
FT /note="AARPFTIPY -> SDQHLIKAP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030550"
FT VAR_SEQ 222..308
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030551"
FT VAR_SEQ 259..308
FT /note="DDSGAEKESASVLQQSSSLSGSRNGEESVIDNPYLRPVKKPKIRRKKSLS
FT -> VGPPLLPASQQSQNSLSHILPLPLGTEQGLPQVSGWLLQACMMGCVSSLHHETHLL
FT GSHTFSRW (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030552"
FT VAR_SEQ 259..265
FT /note="DDSGAEK -> GHPEASA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030553"
FT VAR_SEQ 266..308
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030554"
FT VAR_SEQ 306..308
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030555"
FT CONFLICT 127
FT /note="V -> L (in Ref. 2; BAC36363)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="D -> V (in Ref. 2; BAC34001)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="E -> G (in Ref. 2; BAC34001)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 33988 MW; FD527CD7905CC8D9 CRC64;
MADTAAGPGG SGTRPGSKQS TNPADNYHLA RRRTLQVVVS SLLTEAGFES AEKASVETLT
EMLQSYISEI GRSAKSYCEH TARTQPTLSD IVVTLVEMGF NVDTLPAYAK RSQRMVITAP
PVTNQPVTPK ALTAGQNRPH PPHIPSHFPE FPDPHTYIKT PTYREPVSDY QILREKAASQ
RRDVERALTR FMAKTGETQS LFKDDVSTFP LIAARPFTIP YLTALLPSEL EIQQMEETDS
SEQEEQTDTE NNALHISTDD SGAEKESASV LQQSSSLSGS RNGEESVIDN PYLRPVKKPK
IRRKKSLS
//
