TAF12_SCHPO
ID TAF12_SCHPO Reviewed; 450 AA.
AC O13722;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Transcription initiation factor TFIID subunit 12;
DE AltName: Full=TBP-associated factor 12;
GN Name=taf12 {ECO:0000312|EMBL:CAB10099.1}; ORFNames=SPAC15A10.02;
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:CAB10099.1}
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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, SALSA and SLIK. Binding of
CC TFIID to a promoter (with or without TATA element) is the initial step
CC in 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). SALSA, an altered form of SAGA, may be
CC involved in positive transcriptional regulation. SLIK is proposed to
CC have partly overlapping functions with SAGA. It preferentially
CC acetylates methylated histone H3 (By similarity).
CC {ECO:0000250|UniProtKB:Q03761}.
CC -!- SUBUNIT: Component of the TFIID, SAGA, SALSA and SLIK complexes.
CC {ECO:0000250|UniProtKB:Q03761}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the TAF12 family. {ECO:0000255}.
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DR EMBL; CU329670; CAB10099.1; -; Genomic_DNA.
DR PIR; T37702; T37702.
DR RefSeq; NP_594289.1; NM_001019712.2.
DR AlphaFoldDB; O13722; -.
DR SMR; O13722; -.
DR BioGRID; 279234; 11.
DR IntAct; O13722; 2.
DR MINT; O13722; -.
DR STRING; 4896.SPAC15A10.02.1; -.
DR iPTMnet; O13722; -.
DR MaxQB; O13722; -.
DR PaxDb; O13722; -.
DR PRIDE; O13722; -.
DR EnsemblFungi; SPAC15A10.02.1; SPAC15A10.02.1:pep; SPAC15A10.02.
DR GeneID; 2542785; -.
DR KEGG; spo:SPAC15A10.02; -.
DR PomBase; SPAC15A10.02; taf12.
DR VEuPathDB; FungiDB:SPAC15A10.02; -.
DR eggNOG; KOG1142; Eukaryota.
DR HOGENOM; CLU_645771_0_0_1; -.
DR InParanoid; O13722; -.
DR OMA; RAPHYEL; -.
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:O13722; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IC: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; IPI:PomBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; ISO:PomBase.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:GOC.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR CDD; cd07981; TAF12; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR037794; TAF12.
DR InterPro; IPR003228; TFIID_TAF12_dom.
DR PANTHER; PTHR12264; PTHR12264; 1.
DR Pfam; PF03847; TFIID_20kDa; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..450
FT /note="Transcription initiation factor TFIID subunit 12"
FT /id="PRO_0000326091"
FT DOMAIN 338..413
FT /note="Histone-fold"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 450 AA; 49196 MW; 4865CEE7D478B28B CRC64;
MNGQHSSPGT PVQRPSAGPV NQAQFSQQRT NQLTSLLHTM TMYQQLAQNV GLNTPQGQVY
LLQAQTIRRQ LQGHAQSGQL PNQQLLQQLQ SNGALQQGTP EPSNTRPRPQ LNAQEQTMLL
VRHRQLQTAQ NYLTEMKEAL GRIKNELSTN ERLDTSAREA LVKQESELTV KIAQFTAAIS
NGIRSIQQLQ NRQASSANGN NTGTSTPVNA STDTRKSTAS TPQLQQTQAQ ANAPQQRINP
ETSSVPETPV GVSAANVSNE STELATSATQ QSGLANNVEK SQTPSYMSAN HLPKVDSKSP
IPFSVPPSRA TLTGGYASGS IGLSTPGLSR APHYELDNGN RLLSKRKLHD LLQQIDSEEK
IEPEVEELLL EIADEFVESV TNFACRLAKH RKSDTLDVRD VQLHLERNWN IRLPGFASDD
IVKSARKTGP TPSYQQKQNA IGTAKSLNKD
