TAF7_MOUSE
ID TAF7_MOUSE Reviewed; 341 AA.
AC Q9R1C0;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Transcription initiation factor TFIID subunit 7;
DE AltName: Full=RNA polymerase II TBP-associated factor subunit F;
DE AltName: Full=Transcription initiation factor TFIID 55 kDa subunit;
DE Short=TAF(II)55;
DE Short=TAFII-55;
DE Short=TAFII55 {ECO:0000303|PubMed:10438527};
GN Name=Taf7; Synonyms=Taf2f;
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], FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=10438527; DOI=10.1074/jbc.274.33.23480;
RA Wu S.Y., Thomas M.C., Hou S.Y., Likhite V., Chiang C.M.;
RT "Isolation of mouse TFIID and functional characterization of TBP and TFIID
RT in mediating estrogen receptor and chromatin transcription.";
RL J. Biol. Chem. 274:23480-23490(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Skin;
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].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171 AND SER-256, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. TFIID recognizes and binds promoters with or without a
CC TATA box via its subunit TBP, a TATA-box-binding protein, and promotes
CC assembly of the pre-initiation complex (PIC). The TFIID complex
CC consists of TBP and TBP-associated factors (TAFs), including TAF1,
CC TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and
CC TAF13. TAF7 forms a promoter DNA binding subcomplex of TFIID, together
CC with TAF1 and TAF2. Part of a TFIID complex containing TAF10 (TFIID
CC alpha) and a TFIID complex lacking TAF10 (TFIID beta).
CC {ECO:0000250|UniProtKB:Q15545, ECO:0000269|PubMed:10438527}.
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. Part of a TFIID-
CC containing RNA polymerase II pre-initiation complex that is composed of
CC TBP and at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2,
CC GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3,
CC TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13.
CC Interacts with TAF1; the interaction is direct (By similarity).
CC Interacts with TAF1, TAF5, TAF11, TAF12, and TAF13, but not with TAF10
CC or TBP (PubMed:10438527). Component of some MLL1/MLL complex, at least
CC composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and
CC RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70,
CC INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31,
CC RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9
CC and TEX10. Interacts with CIITA and TAF1 and inhibits their
CC acetyltransferase activity, and behaving as a repressor of CIITA- and
CC TAF1-regulated promoters (By similarity).
CC {ECO:0000250|UniProtKB:Q15545, ECO:0000269|PubMed:10438527}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10438527}.
CC -!- DOMAIN: The [KR]-[STA]-K motif is specifically recognized by the SETD7
CC methyltransferase. {ECO:0000250}.
CC -!- PTM: Phosphorylated by CIITA. Phosphorylation at Ser-256 by TAF1 in
CC early G1 phase disrupts binding to TAF1 (By similarity).
CC {ECO:0000250|UniProtKB:Q15545}.
CC -!- SIMILARITY: Belongs to the TAF7 family. {ECO:0000305}.
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DR EMBL; AF144562; AAD46767.1; -; mRNA.
DR EMBL; AK029380; BAC26429.1; -; mRNA.
DR EMBL; AK076362; BAC36313.1; -; mRNA.
DR EMBL; BC029673; AAH29673.1; -; mRNA.
DR CCDS; CCDS29189.1; -.
DR RefSeq; NP_786964.1; NM_175770.4.
DR AlphaFoldDB; Q9R1C0; -.
DR SMR; Q9R1C0; -.
DR BioGRID; 204884; 1.
DR ComplexPortal; CPX-916; TFTC histone acetylation complex.
DR ComplexPortal; CPX-932; General transcription factor complex TFIID.
DR ComplexPortal; CPX-959; General transcription factor complex TFIID, Taf4b variant.
DR CORUM; Q9R1C0; -.
DR IntAct; Q9R1C0; 1.
DR STRING; 10090.ENSMUSP00000065645; -.
DR iPTMnet; Q9R1C0; -.
DR PhosphoSitePlus; Q9R1C0; -.
DR EPD; Q9R1C0; -.
DR jPOST; Q9R1C0; -.
DR MaxQB; Q9R1C0; -.
DR PaxDb; Q9R1C0; -.
DR PeptideAtlas; Q9R1C0; -.
DR PRIDE; Q9R1C0; -.
DR ProteomicsDB; 262925; -.
DR Antibodypedia; 1826; 181 antibodies from 27 providers.
DR DNASU; 24074; -.
DR Ensembl; ENSMUST00000066272; ENSMUSP00000065645; ENSMUSG00000051316.
DR GeneID; 24074; -.
DR KEGG; mmu:24074; -.
DR UCSC; uc008eqi.2; mouse.
DR CTD; 6879; -.
DR MGI; MGI:1346348; Taf7.
DR VEuPathDB; HostDB:ENSMUSG00000051316; -.
DR eggNOG; KOG4011; Eukaryota.
DR GeneTree; ENSGT00940000160861; -.
DR HOGENOM; CLU_037860_0_1_1; -.
DR InParanoid; Q9R1C0; -.
DR OMA; KTLQYPH; -.
DR OrthoDB; 1348389at2759; -.
DR PhylomeDB; Q9R1C0; -.
DR TreeFam; TF313044; -.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR BioGRID-ORCS; 24074; 13 hits in 77 CRISPR screens.
DR ChiTaRS; Taf7; mouse.
DR PRO; PR:Q9R1C0; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9R1C0; protein.
DR Bgee; ENSMUSG00000051316; Expressed in animal zygote and 220 other tissues.
DR Genevisible; Q9R1C0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:MGI.
DR GO; GO:0033276; C:transcription factor TFTC complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0061628; F:H3K27me3 modified histone binding; ISO:MGI.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:MGI.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; ISO:MGI.
DR GO; GO:0106140; F:P-TEFb complex binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:MGI.
DR GO; GO:0001097; F:TFIIH-class transcription factor complex binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; ISO:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:MGI.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:MGI.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0035067; P:negative regulation of histone acetylation; ISO:MGI.
DR GO; GO:0090241; P:negative regulation of histone H4 acetylation; ISO:MGI.
DR GO; GO:0045344; P:negative regulation of MHC class I biosynthetic process; ISO:MGI.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; ISO:MGI.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; ISO:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR CDD; cd08047; TAF7; 1.
DR InterPro; IPR037817; TAF7.
DR InterPro; IPR006751; TAFII55_prot_cons_reg.
DR PANTHER; PTHR12228; PTHR12228; 1.
DR Pfam; PF04658; TAFII55_N; 1.
DR SMART; SM01370; TAFII55_N; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..341
FT /note="Transcription initiation factor TFIID subunit 7"
FT /id="PRO_0000118882"
FT REGION 187..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 236..341
FT /evidence="ECO:0000255"
FT MOTIF 3..5
FT /note="[KR]-[STA]-K motif"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15545"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15545"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15545"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 341 AA; 39126 MW; 5C4A95DFD68D685F CRC64;
MSKNKDDAPH ELESQFILRL PPEYAATVRR AVQSGHVNLK DKLSIELHPD GRHGIVRVDR
VPLAAKLVDL PCVTESLKTI DKKTFYKTAD ISQMLVATVD GDLYPPVEEA AATADPKANK
KKDKDKEKKF VWNHGITLPL KNVRKRRFRK TAKKKYIESP DVEKEVKRLL STDAEAVSTR
WEIIAEDETK ETENQGLDIS SPGMSGHRQG HDSLEHDELR EIFNDLSSSS EDEEDVNILD
TEEDLERQLQ DKLNESDEQH QENEGTNQLV MGIQKQIDNM KGKLQETQDR AKRQEDLIMK
VENLALKNRF QAVLDELKQK EDREKEQLSS LQEELESLLE K
