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RXT3_SCHPO
ID   RXT3_SCHPO              Reviewed;         351 AA.
AC   O94707;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Transcriptional regulatory protein rxt3;
GN   Name=rxt3; ORFNames=SPCC1259.07;
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   IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=19040720; DOI=10.1186/gb-2008-9-11-r167;
RA   Shevchenko A., Roguev A., Schaft D., Buchanan L., Habermann B., Sakalar C.,
RA   Thomas H., Krogan N.J., Shevchenko A., Stewart A.F.;
RT   "Chromatin Central: towards the comparative proteome by accurate mapping of
RT   the yeast proteomic environment.";
RL   Genome Biol. 9:R167.1-R167.22(2008).
CC   -!- FUNCTION: Component of the RPD3C(L) histone deacetylase complex (HDAC)
CC       responsible for the deacetylation of lysine residues on the N-terminal
CC       part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation
CC       gives a tag for epigenetic repression and plays an important role in
CC       transcriptional regulation, cell cycle progression and developmental
CC       events (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of the RPD3C(L) complex.
CC       {ECO:0000269|PubMed:19040720}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RXT3 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA22545.1; -; Genomic_DNA.
DR   PIR; T40896; T40896.
DR   RefSeq; NP_588063.1; NM_001023055.2.
DR   AlphaFoldDB; O94707; -.
DR   BioGRID; 275940; 3.
DR   STRING; 4896.SPCC1259.07.1; -.
DR   iPTMnet; O94707; -.
DR   MaxQB; O94707; -.
DR   PaxDb; O94707; -.
DR   PRIDE; O94707; -.
DR   EnsemblFungi; SPCC1259.07.1; SPCC1259.07.1:pep; SPCC1259.07.
DR   GeneID; 2539374; -.
DR   KEGG; spo:SPCC1259.07; -.
DR   PomBase; SPCC1259.07; rxt3.
DR   VEuPathDB; FungiDB:SPCC1259.07; -.
DR   eggNOG; KOG4843; Eukaryota.
DR   HOGENOM; CLU_774233_0_0_1; -.
DR   InParanoid; O94707; -.
DR   PRO; PR:O94707; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:1990483; C:Clr6 histone deacetylase complex I''; IPI:PomBase.
DR   GO; GO:0033698; C:Rpd3L complex; IDA:PomBase.
DR   GO; GO:0070210; C:Rpd3L-Expanded complex; IDA:PomBase.
DR   GO; GO:0006338; P:chromatin remodeling; IC:PomBase.
DR   GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:PomBase.
DR   Gene3D; 2.170.130.20; -; 1.
DR   InterPro; IPR036609; LCCL_sf.
DR   InterPro; IPR013951; Rxt3.
DR   Pfam; PF08642; Rxt3; 1.
DR   SUPFAM; SSF69848; SSF69848; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..351
FT                   /note="Transcriptional regulatory protein rxt3"
FT                   /id="PRO_0000374009"
FT   REGION          1..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   351 AA;  39421 MW;  73F799CAFD7A7241 CRC64;
     MEEKTPENEQ SKKTFDPKDS MKIEETSTNG SSQPSQPSNI KLSIGSILES SNDNGDPEYS
     ENGMGNMNMN TLPMATSTPM SYTKQPSEAK YPNSVWERKG VSDQEENTSS VKRQKTLPTQ
     SSGEEEAKYS HPGAPTATSA DSISMESRPS NLSTSLSKTT SYPQFQVRQF VSPIISIDNS
     ALEPFLNRYP ASESLFPVTE YEYTPWLEFP LLYSSIGKFV RVTIDIKWLN AAINPRLCRR
     EIWGTDVYTD DSDIATILAH CGCFSLLKPV RKIAVVDLYI LPPLVHYKGT RKNQIESRSW
     SSRQDGISLK IKEVTWKPAC ASIFENSIHT LTLEERLQAR LELSRSSTFK I
 
 
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