TAF10_MOUSE
ID TAF10_MOUSE Reviewed; 218 AA.
AC Q8K0H5; Q8C8H2; Q9QYY5;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Transcription initiation factor TFIID subunit 10;
DE AltName: Full=Transcription initiation factor TFIID 30 kDa subunit;
DE Short=TAF(II)30;
DE Short=TAFII-30;
DE Short=TAFII30;
DE Short=mTAFII30;
GN Name=Taf10; Synonyms=Taf2h, Tafii30;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=10469660; DOI=10.1093/emboj/18.17.4823;
RA Metzger D., Scheer E., Soldatov A., Tora L.;
RT "Mammalian TAFII30 is required for cell cycle progression and specific
RT differentiation programmes.";
RL EMBO J. 18:4823-4834(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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=C57BL/6J; TISSUE=Brain, and 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 INTERACTION WITH TAF3.
RX PubMed=11438666; DOI=10.1128/mcb.21.15.5109-5121.2001;
RA Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C.,
RA Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.;
RT "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are
RT novel metazoan homologues of yeast TAFII47 containing a histone fold and a
RT PHD finger.";
RL Mol. Cell. Biol. 21:5109-5121(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, 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).
RN [6]
RP METHYLATION AT LYS-189.
RX PubMed=25959397; DOI=10.1016/j.molcel.2015.04.012;
RA Iturbide A., Pascual-Reguant L., Fargas L., Cebria J.P., Alsina B.,
RA Garcia de Herreros A., Peiro S.;
RT "LOXL2 oxidizes methylated TAF10 and controls TFIID-dependent genes during
RT neural progenitor differentiation.";
RL Mol. Cell 58:755-766(2015).
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. TAF10 is also component of the PCAF histone acetylase complex,
CC the TATA-binding protein-free TAF complex (TFTC) and the STAGA
CC transcription coactivator-HAT complex (By similarity). May regulate
CC cyclin E expression (PubMed:10469660). {ECO:0000250|UniProtKB:Q12962,
CC ECO:0000269|PubMed:10469660}.
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. Component of the
CC TATA-binding protein-free TAF complex (TFTC), the PCAF histone
CC acetylase complex and the STAGA transcription coactivator-HAT complex.
CC The PCAF complex consists at least of TADA2L/ADA2, TADA3L/ADA3, SUPT3H,
CC TAF5L TAF6L, TAF9, TAF10, TAF12 and TRRAP. The TFTC-HAT complex
CC consists at least of TAF5L, TAF6L, TADA3L, SUPT3H, TAF2, TAF4, TAF5,
CC GCN5L2/GCN5, TAF10 and TRRAP. The STAGA transcription coactivator-HAT
CC complex consists at least of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L,
CC TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. The STAGA core complex is
CC associated with a subcomplex required for histone deubiquitination
CC composed of ATXN7L3, ENY2 and USP22. Interacts with LOXL2. Interacts
CC with TAF12 isoform TAFII20; the interaction is direct (By similarity).
CC Interacts with TAF3 (PubMed:11438666). {ECO:0000250|UniProtKB:Q12962,
CC ECO:0000269|PubMed:11438666}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12962}.
CC -!- DOMAIN: The [KR]-[STA]-K motif is specifically recognized by the SETD7
CC methyltransferase. {ECO:0000250|UniProtKB:Q12962}.
CC -!- PTM: Monomethylated at Lys-189 by SETD7, leading to increased affinity
CC for RNA polymerase II. {ECO:0000250|UniProtKB:Q12962}.
CC -!- PTM: Lysine deamination at Lys-189 to form allysine is mediated by
CC LOXL2. Allysine formation by LOXL2 results in release of TAF10 from
CC promoters, leading to inhibition of TFIID-dependent transcription.
CC {ECO:0000250|UniProtKB:Q12962}.
CC -!- SIMILARITY: Belongs to the TAF10 family. {ECO:0000305}.
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DR EMBL; AK047115; BAC32964.1; -; mRNA.
DR EMBL; AJ249987; CAB59510.1; -; Genomic_DNA.
DR EMBL; BC031418; AAH31418.1; -; mRNA.
DR EMBL; BC080311; AAH80311.1; -; mRNA.
DR CCDS; CCDS21660.1; -.
DR RefSeq; NP_064408.2; NM_020024.3.
DR AlphaFoldDB; Q8K0H5; -.
DR SMR; Q8K0H5; -.
DR BioGRID; 204885; 4.
DR ComplexPortal; CPX-1024; PCAF histone acetylase complex.
DR ComplexPortal; CPX-6803; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-916; TFTC histone acetylation complex.
DR ComplexPortal; CPX-920; SAGA complex, KAT2A variant.
DR ComplexPortal; CPX-932; General transcription factor complex TFIID.
DR ComplexPortal; CPX-959; General transcription factor complex TFIID, Taf4b variant.
DR CORUM; Q8K0H5; -.
DR DIP; DIP-59890N; -.
DR IntAct; Q8K0H5; 5.
DR MINT; Q8K0H5; -.
DR STRING; 10090.ENSMUSP00000118105; -.
DR iPTMnet; Q8K0H5; -.
DR PhosphoSitePlus; Q8K0H5; -.
DR EPD; Q8K0H5; -.
DR MaxQB; Q8K0H5; -.
DR PaxDb; Q8K0H5; -.
DR PeptideAtlas; Q8K0H5; -.
DR PRIDE; Q8K0H5; -.
DR ProteomicsDB; 263242; -.
DR Antibodypedia; 1301; 151 antibodies from 27 providers.
DR DNASU; 24075; -.
DR Ensembl; ENSMUST00000141116; ENSMUSP00000118105; ENSMUSG00000043866.
DR GeneID; 24075; -.
DR KEGG; mmu:24075; -.
DR UCSC; uc009izf.1; mouse.
DR CTD; 6881; -.
DR MGI; MGI:1346320; Taf10.
DR VEuPathDB; HostDB:ENSMUSG00000043866; -.
DR eggNOG; KOG3423; Eukaryota.
DR GeneTree; ENSGT00390000009368; -.
DR HOGENOM; CLU_064104_1_0_1; -.
DR InParanoid; Q8K0H5; -.
DR OMA; TGPMSCS; -.
DR OrthoDB; 1478962at2759; -.
DR PhylomeDB; Q8K0H5; -.
DR TreeFam; TF313156; -.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
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; 24075; 20 hits in 81 CRISPR screens.
DR ChiTaRS; Taf10; mouse.
DR PRO; PR:Q8K0H5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8K0H5; protein.
DR Bgee; ENSMUSG00000043866; Expressed in yolk sac and 187 other tissues.
DR Genevisible; Q8K0H5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0000124; C:SAGA complex; ISO:MGI.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
DR GO; GO:0033276; C:transcription factor TFTC complex; ISO:MGI.
DR GO; GO:0097550; C:transcription preinitiation complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:MGI.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:MGI.
DR GO; GO:1905069; P:allantois development; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IMP:MGI.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; ISO:MGI.
DR GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0070365; P:hepatocyte differentiation; IMP:MGI.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0016578; P:histone deubiquitination; ISO:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0048371; P:lateral mesodermal cell differentiation; IMP:MGI.
DR GO; GO:0060173; P:limb development; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP: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:0035264; P:multicellular organism growth; IMP: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:0065003; P:protein-containing complex assembly; IMP:MGI.
DR GO; GO:0051101; P:regulation of DNA binding; IMP:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:MGI.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IMP:MGI.
DR GO; GO:0036285; P:SAGA complex assembly; IMP:MGI.
DR GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR CDD; cd07982; TAF10; 1.
DR InterPro; IPR003923; TFIID_30kDa.
DR PANTHER; PTHR21242; PTHR21242; 1.
DR Pfam; PF03540; TFIID_30kDa; 1.
DR PIRSF; PIRSF017246; TFIID_TAF10; 1.
DR PRINTS; PR01443; TFIID30KDSUB.
PE 1: Evidence at protein level;
KW Acetylation; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q12962"
FT CHAIN 2..218
FT /note="Transcription initiation factor TFIID subunit 10"
FT /id="PRO_0000118898"
FT REGION 27..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 187..189
FT /note="[KR]-[STA]-K motif"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q12962"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12962"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q12962"
FT MOD_RES 189
FT /note="Allysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q12962"
FT MOD_RES 189
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:25959397"
FT CONFLICT 2
FT /note="S -> G (in Ref. 2; BAC32964)"
FT /evidence="ECO:0000305"
FT CONFLICT 29..31
FT /note="APA -> GSP (in Ref. 1; CAB59510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 218 AA; 21841 MW; 4ACD72C59ACC367A CRC64;
MSCSGSGADP EAATACAASV AGPAPLVSAP AALPTSTAAE SKASPAGTAG GPVAGVATAG
TGPVAARAGE PAERRGPASV AAGGAAPPEG AMSNGVYALP SAANGEVKPV VSSTPLVDFL
MQLEDYTPTI PDAVTGYYLN RAGFEASDPR IIRLISLAAQ KFISDIANDA LQHCKMKGTA
SGSSRSKSKD RKYTLTMEDL TPALSEYGIN VKKPHYFT
