TAF14_SCHPO
ID TAF14_SCHPO Reviewed; 241 AA.
AC O94436;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Transcription initiation factor TFIID subunit 14;
DE AltName: Full=SWI/SNF chromatin-remodeling complex subunit tfg3;
DE AltName: Full=SWI/SNF complex subunit tfg3;
DE AltName: Full=TBP-associated factor 14;
DE AltName: Full=TBP-associated factor 30 kDa;
DE AltName: Full=Transcription factor G 30 kDa subunit;
DE AltName: Full=Transcription initiation factor TFIIF 30 kDa subunit;
GN Name=tfg3; Synonyms=taf14; ORFNames=SPAC22H12.02;
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]
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]
RP FUNCTION, INTERACTION WITH TFIIF-ALPHA, TFIIF-BETA AND TBP, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15616156; DOI=10.1093/nar/gkh1000;
RA Kimura M., Ishihama A.;
RT "Tfg3, a subunit of the general transcription factor TFIIF in
RT Schizosaccharomyces pombe, functions under stress conditions.";
RL Nucleic Acids Res. 32:6706-6715(2004).
RN [3]
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 [4]
RP IDENTIFICATION IN THE SWI/SNF COMPLEX, FUNCTION OF THE SWI/SNF COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18622392; DOI=10.1038/nsmb.1452;
RA Monahan B.J., Villen J., Marguerat S., Baehler J., Gygi S.P., Winston F.;
RT "Fission yeast SWI/SNF and RSC complexes show compositional and functional
RT differences from budding yeast.";
RL Nat. Struct. Mol. Biol. 15:873-880(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MST2 COMPLEX,
RP AND FUNCTION.
RX PubMed=22184112; DOI=10.1074/jbc.m111.329417;
RA Wang Y., Kallgren S.P., Reddy B.D., Kuntz K., Lopez-Maury L., Thompson J.,
RA Watt S., Ma C., Hou H., Shi Y., Yates J.R. III, Bahler J., O'Connell M.J.,
RA Jia S.;
RT "Histone H3 lysine 14 acetylation is required for activation of a DNA
RT damage checkpoint in fission yeast.";
RL J. Biol. Chem. 287:4386-4393(2012).
CC -!- FUNCTION: Functions as a component of the DNA-binding general
CC transcription factor complex TFIID, and the RNA polymerase II
CC associated general transcription factor complex TFIIF. Binding of TFIID
CC to 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, facilitation
CC of DNA opening and initiation of transcription. TFIIF is essential for
CC the initiation of transcription by RNA polymerase II. TFIIF functions
CC include the recruitment of RNA polymerase II to the promoter bound DNA-
CC TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for
CC non-specific DNA, allowing for the subsequent recruitment of TFIIE and
CC TFIIH, and facilitating RNA polymerase II elongation. The TAF14 subunit
CC has stimulatory activity. Component of the SWI/SNF complex, an ATP-
CC dependent chromatin remodeling complex, required for the positive and
CC negative regulation of gene expression of a large number of genes. It
CC changes chromatin structure by altering DNA-histone contacts within a
CC nucleosome, leading eventually to a change in nucleosome position, thus
CC facilitating or repressing binding of gene-specific transcription
CC factors. Component of the mst2 complex which is a highly specific H3
CC lysine 14 (H3K14) acetyltransferase that functions together with gcn5
CC to regulate global levels of H3K14 acetylation (H3K14ac), critical for
CC DNA damage checkpoint activation. {ECO:0000269|PubMed:15616156,
CC ECO:0000269|PubMed:18622392, ECO:0000269|PubMed:22184112}.
CC -!- SUBUNIT: Component of the fcp1/TFIIF/polII complex via interaction of
CC tfg3 with both tfg1/TFIIF-alpha and tfg2/TFIIF-beta subunits. Component
CC of the SWI/SNF global transcription activator complex composed of at
CC least arp9, arp42, snf5, snf22, snf30, sbf59, sol1, ssr1, ssr2, ssr3,
CC ssr4 and tfg3. Interacts also with the TATA-binding protein (TBP).
CC Component of the mst2 complex composed of at least eaf6, mst2, nto1,
CC pdp3, ptf1, ptf2 and tfg3. {ECO:0000269|PubMed:15616156,
CC ECO:0000269|PubMed:18622392, ECO:0000269|PubMed:22184112}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15616156, ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the TAF14 family. {ECO:0000305}.
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DR EMBL; CU329670; CAA22554.1; -; Genomic_DNA.
DR PIR; T38217; T38217.
DR RefSeq; NP_593114.1; NM_001018511.2.
DR AlphaFoldDB; O94436; -.
DR SMR; O94436; -.
DR BioGRID; 278223; 23.
DR ComplexPortal; CPX-6362; SWI/SNF chromatin remodelling complex.
DR DIP; DIP-39996N; -.
DR IntAct; O94436; 7.
DR STRING; 4896.SPAC22H12.02.1; -.
DR iPTMnet; O94436; -.
DR MaxQB; O94436; -.
DR PaxDb; O94436; -.
DR PRIDE; O94436; -.
DR EnsemblFungi; SPAC22H12.02.1; SPAC22H12.02.1:pep; SPAC22H12.02.
DR GeneID; 2541729; -.
DR KEGG; spo:SPAC22H12.02; -.
DR PomBase; SPAC22H12.02; tfg3.
DR VEuPathDB; FungiDB:SPAC22H12.02; -.
DR eggNOG; KOG3149; Eukaryota.
DR HOGENOM; CLU_078004_0_0_1; -.
DR InParanoid; O94436; -.
DR OMA; GEFDMTI; -.
DR PhylomeDB; O94436; -.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:O94436; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0031011; C:Ino80 complex; IPI:PomBase.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:PomBase.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:PomBase.
DR GO; GO:0005674; C:transcription factor TFIIF complex; IDA:PomBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:PomBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IDA:PomBase.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IPI:PomBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:PomBase.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 2.60.40.1970; -; 1.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR InterPro; IPR016665; Sas5/TAF14.
DR InterPro; IPR038704; YEAST_sf.
DR InterPro; IPR005033; YEATS.
DR PANTHER; PTHR23195; PTHR23195; 1.
DR PANTHER; PTHR23195:SF2; PTHR23195:SF2; 1.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF03366; YEATS; 1.
DR PIRSF; PIRSF016551; SAS5/TFIID_14; 1.
DR PROSITE; PS51037; YEATS; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; DNA damage; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..241
FT /note="Transcription initiation factor TFIID subunit 14"
FT /id="PRO_0000238606"
FT DOMAIN 1..137
FT /note="YEATS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00376"
FT REGION 141..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 241 AA; 27638 MW; 278FAF8B67883D46 CRC64;
MTTVKRTVRL ITDQNVLPGG EAAVLNDQSF PVREWSIKLV CLNPQGEETD ASFVDRVTYK
LHPTFQNPTR TIRKPPFQIK EQGWGEFEME IIIYYADKGG EHRFLHYLHF QQEHYHEDIE
LNINATRPGL LKALTATGEV PGYSDEGEEA RKDKRKNESE VGAGKKKAKA KPVDMDKLAE
GLQKLQEDDL LQVVQMVNEN KTPDMYVRND IEGGEFHIDL YTLPDNLLLL LYSFCAKRVT
M
