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TAF4_SCHPO
ID   TAF4_SCHPO              Reviewed;         365 AA.
AC   Q9P7S4;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Transcription initiation factor TFIID subunit 4;
DE   AltName: Full=TBP-associated factor 4;
GN   Name=taf4; ORFNames=SPAC23G3.09;
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   -!- SUBUNIT: The 1.2 MDa TFIID complex is composed of TATA binding protein
CC       (TBP) and the 14 TBP-associated factors. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the TAF4 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB72234.1; -; Genomic_DNA.
DR   PIR; T50183; T50183.
DR   RefSeq; NP_593109.1; NM_001018506.2.
DR   AlphaFoldDB; Q9P7S4; -.
DR   BioGRID; 278215; 17.
DR   STRING; 4896.SPAC23G3.09.1; -.
DR   iPTMnet; Q9P7S4; -.
DR   MaxQB; Q9P7S4; -.
DR   PaxDb; Q9P7S4; -.
DR   PRIDE; Q9P7S4; -.
DR   EnsemblFungi; SPAC23G3.09.1; SPAC23G3.09.1:pep; SPAC23G3.09.
DR   GeneID; 2541721; -.
DR   KEGG; spo:SPAC23G3.09; -.
DR   PomBase; SPAC23G3.09; taf4.
DR   VEuPathDB; FungiDB:SPAC23G3.09; -.
DR   eggNOG; KOG2341; Eukaryota.
DR   HOGENOM; CLU_759021_0_0_1; -.
DR   InParanoid; Q9P7S4; -.
DR   OMA; KYSWMAT; -.
DR   PhylomeDB; Q9P7S4; -.
DR   PRO; PR:Q9P7S4; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; NAS:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005669; C:transcription factor TFIID complex; EXP: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:0051123; P:RNA polymerase II preinitiation complex assembly; ISO:PomBase.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR   CDD; cd08045; TAF4; 1.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR045144; TAF4.
DR   InterPro; IPR007900; TAF4_C.
DR   PANTHER; PTHR15138; PTHR15138; 1.
DR   Pfam; PF05236; TAF4; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..365
FT                   /note="Transcription initiation factor TFIID subunit 4"
FT                   /id="PRO_0000343443"
FT   DOMAIN          164..227
FT                   /note="Histone-fold"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          202..236
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        7..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   365 AA;  40546 MW;  D024E4707701C731 CRC64;
     MDLNNPPSKR FGDDDDIPAN KRPKNEEYPE IPGYLGNRKP SYTQNPNSGP GKLHYASPRP
     NNVSSSVGVA SGGDRQEADQ LQDALISCGI QLKEEELNLS TSFYDPSSLN TFALTTEDRS
     RKSDFLNSFV LMQTVSNIVN LHRLKSMDSD IHALISMAVR DYLANLLQKM IVESHHRTSQ
     LHTDNYKQVD NVRQTLANFA YKEYESEERR RTVLNIRRAE HEARLAELNS ASTNEEGSSR
     RRKEQSSSAA AKNISEDAQN RMTNATASIM AGSALPSGGK KYSWMATDMT PMTPAVGGGF
     GIRKKDSNSL KPSSRDGVLP LQQEEKGIIT IRDALAVLEM DREGAGRIFG RGAKAMMRAY
     IRLKD
 
 
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