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TAF3_SCHPO
ID   TAF3_SCHPO              Reviewed;         155 AA.
AC   Q9P6P0;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Transcription initiation factor TFIID subunit 3;
DE   AltName: Full=TBP-associated factor 3;
GN   Name=taf3; ORFNames=SPAC823.06;
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   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. Binding of TFIID to a promoter
CC       (with or without TATA element) is the initial step in pre-initiation
CC       complex (PIC) formation. TFIID plays a key role in the regulation of
CC       gene expression by RNA polymerase II through different activities such
CC       as transcription activator interaction, core promoter recognition and
CC       selectivity, TFIIA and TFIIB interaction, chromatin modification
CC       (histone acetylation by TAF1), facilitation of DNA opening and
CC       initiation of transcription (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the TAF3 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB90151.1; -; Genomic_DNA.
DR   RefSeq; NP_593833.1; NM_001019262.2.
DR   AlphaFoldDB; Q9P6P0; -.
DR   SMR; Q9P6P0; -.
DR   BioGRID; 280019; 2.
DR   STRING; 4896.SPAC823.06.1; -.
DR   iPTMnet; Q9P6P0; -.
DR   MaxQB; Q9P6P0; -.
DR   PaxDb; Q9P6P0; -.
DR   PRIDE; Q9P6P0; -.
DR   EnsemblFungi; SPAC823.06.1; SPAC823.06.1:pep; SPAC823.06.
DR   GeneID; 2543604; -.
DR   KEGG; spo:SPAC823.06; -.
DR   PomBase; SPAC823.06; taf3.
DR   VEuPathDB; FungiDB:SPAC823.06; -.
DR   eggNOG; ENOG502S96D; Eukaryota.
DR   HOGENOM; CLU_064111_0_0_1; -.
DR   InParanoid; Q9P6P0; -.
DR   OMA; TDIMIRY; -.
DR   PhylomeDB; Q9P6P0; -.
DR   PRO; PR:Q9P6P0; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; NAS:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005669; C:transcription factor TFIID complex; ISO:PomBase.
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:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:PomBase.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR006565; BTP.
DR   InterPro; IPR009072; Histone-fold.
DR   Pfam; PF07524; Bromo_TP; 1.
DR   SMART; SM00576; BTP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..155
FT                   /note="Transcription initiation factor TFIID subunit 3"
FT                   /id="PRO_0000343435"
SQ   SEQUENCE   155 AA;  17681 MW;  6D0B94AE8B57C309 CRC64;
     MEETQIDELY FSLMRIFCSQ TLRAAGIDRT KVSLLNSFTD ITIRYIRLLS ETAMAKAEVG
     RRSCCDLGDL RLAMEEIGLL NGSEEDVKTL VEWFNGPQVA ELRRVSGFVQ DSETQVKPKD
     WLTSLIQKQI RVSGPERFYE TVFSASNEEE DVKDS
 
 
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