TAF10_SCHPO
ID TAF10_SCHPO Reviewed; 215 AA.
AC O60171;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Transcription initiation factor TFIID subunit 10;
DE AltName: Full=TBP-associated factor 10;
GN Name=taf10 {ECO:0000312|EMBL:CAA18862.1}; ORFNames=SPBC21H7.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAA18862.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Functions as a component of the DNA-binding general
CC transcription factor complex TFIID and the transcription regulatory
CC histone acetylation (HAT) complexes SAGA and SLIK. Binding of TFIID to
CC a promoter (with or without TATA element) is the initial step in
CC preinitiation complex (PIC) formation. TFIID plays a key role in the
CC regulation of gene expression by RNA polymerase II through different
CC activities such as transcription activator interaction, core promoter
CC recognition and selectivity, TFIIA and TFIIB interaction, chromatin
CC modification (histone acetylation), facilitation of DNA opening and
CC initiation of transcription. SAGA is involved in RNA polymerase II-
CC dependent transcriptional regulation. At the promoters, SAGA is
CC required for recruitment of the basal transcription machinery. It
CC influences RNA polymerase II transcriptional activity through different
CC activities such as TBP interaction and promoter selectivity,
CC interaction with transcription activators, and chromatin modification
CC through histone acetylation (gcn5) and deubiquitination (ubp8). SAGA
CC acetylates nucleosomal histone H3 to some extent (to form H3K9ac,
CC H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream
CC activating sequences (UASs). SLIK is proposed to have partly
CC overlapping functions with SAGA. It preferentially acetylates
CC methylated histone H3 (By similarity). {ECO:0000250|UniProtKB:Q12030}.
CC -!- SUBUNIT: Component of the TFIID, SAGA, and SLIK complexes.
CC {ECO:0000250|UniProtKB:Q12030}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the TAF10 family. {ECO:0000255}.
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DR EMBL; CU329671; CAA18862.1; -; Genomic_DNA.
DR PIR; T39928; T39928.
DR RefSeq; NP_595927.1; NM_001021835.2.
DR AlphaFoldDB; O60171; -.
DR SMR; O60171; -.
DR BioGRID; 277140; 9.
DR IntAct; O60171; 2.
DR MINT; O60171; -.
DR STRING; 4896.SPBC21H7.02.1; -.
DR iPTMnet; O60171; -.
DR MaxQB; O60171; -.
DR PaxDb; O60171; -.
DR PRIDE; O60171; -.
DR EnsemblFungi; SPBC21H7.02.1; SPBC21H7.02.1:pep; SPBC21H7.02.
DR GeneID; 2540614; -.
DR KEGG; spo:SPBC21H7.02; -.
DR PomBase; SPBC21H7.02; taf10.
DR VEuPathDB; FungiDB:SPBC21H7.02; -.
DR eggNOG; KOG3423; Eukaryota.
DR HOGENOM; CLU_064104_0_0_1; -.
DR InParanoid; O60171; -.
DR OMA; DAYQYSK; -.
DR PhylomeDB; O60171; -.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SPO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SPO-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SPO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR PRO; PR:O60171; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:PomBase.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IBA:GO_Central.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:PomBase.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:GOC.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:PomBase.
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 3: Inferred from homology;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..215
FT /note="Transcription initiation factor TFIID subunit 10"
FT /id="PRO_0000326090"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 215 AA; 23526 MW; E314301007678DA8 CRC64;
MSDINNNEPA ENIEQPKQEP EDGNNSMSVD EQPETSSTNL PTGDNLAPMS VESPAHLNNE
DSPKSDDSRE RHGSNYVIEP HLELRDMAKD KTLENFLAQM DDYSPLIPDV LLDYYLSLSG
FKCVDPRLKK LLGLTAQKFI SDVAQDAYQY SKIRTGSSNA SSTTFGAQNF GAGGASGIGS
SGRRGDRGKT VLTVDDLSAA LNEYGINLKR PDFFR
