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SDS3_SCHPO
ID   SDS3_SCHPO              Reviewed;         267 AA.
AC   Q9UTB6;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Transcriptional regulatory protein sds3;
DE   AltName: Full=Clr6 histone deacetylase complex I subunit Sds3;
GN   Name=sds3; ORFNames=SPAC25B8.02;
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   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE CLR6 COMPLEX I,
RP   AND FUNCTION OF THE CLR6 COMPLEX I.
RX   PubMed=17450151; DOI=10.1038/nsmb1239;
RA   Nicolas E., Yamada T., Cam H.P., Fitzgerald P.C., Kobayashi R.,
RA   Grewal S.I.S.;
RT   "Distinct roles of HDAC complexes in promoter silencing, antisense
RT   suppression and DNA damage protection.";
RL   Nat. Struct. Mol. Biol. 14:372-380(2007).
CC   -!- FUNCTION: Component of the clr6 histone deacetylase complex I
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. {ECO:0000269|PubMed:17450151}.
CC   -!- SUBUNIT: Component of the clr6 histone deacetylase complex I composed
CC       of at least clr6, png2, prw1, pst1 and sds3.
CC       {ECO:0000269|PubMed:17450151}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SDS3 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB61768.1; -; Genomic_DNA.
DR   PIR; T50189; T50189.
DR   RefSeq; NP_594462.1; NM_001019891.2.
DR   AlphaFoldDB; Q9UTB6; -.
DR   SMR; Q9UTB6; -.
DR   BioGRID; 278193; 7.
DR   DIP; DIP-29345N; -.
DR   IntAct; Q9UTB6; 5.
DR   STRING; 4896.SPAC25B8.02.1; -.
DR   iPTMnet; Q9UTB6; -.
DR   MaxQB; Q9UTB6; -.
DR   PaxDb; Q9UTB6; -.
DR   PRIDE; Q9UTB6; -.
DR   EnsemblFungi; SPAC25B8.02.1; SPAC25B8.02.1:pep; SPAC25B8.02.
DR   GeneID; 2541697; -.
DR   KEGG; spo:SPAC25B8.02; -.
DR   PomBase; SPAC25B8.02; sds3.
DR   VEuPathDB; FungiDB:SPAC25B8.02; -.
DR   eggNOG; KOG4466; Eukaryota.
DR   HOGENOM; CLU_1038836_0_0_1; -.
DR   InParanoid; Q9UTB6; -.
DR   OMA; TLNFFDD; -.
DR   PRO; PR:Q9UTB6; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:1990483; C:Clr6 histone deacetylase complex I''; IPI:PomBase.
DR   GO; GO:0033698; C:Rpd3L complex; IDA:PomBase.
DR   GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR   GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR   GO; GO:0006338; P:chromatin remodeling; NAS:PomBase.
DR   GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR013907; Sds3.
DR   PANTHER; PTHR21964; PTHR21964; 1.
DR   Pfam; PF08598; Sds3; 1.
DR   SMART; SM01401; Sds3; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..267
FT                   /note="Transcriptional regulatory protein sds3"
FT                   /id="PRO_0000352833"
FT   REGION          208..252
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   267 AA;  30753 MW;  AA0DE92BDCE75671 CRC64;
     MDVLSRVFDN EKEELDPLLN NPLTASEFRA KKAELEAELE SIRNGTCKTL LDLADELRRS
     RDEELEIAER WRTFLVNRAQ EEYEVEMKAA KEEYEYRCKT LKEMVLSHLN EKKRKIYEAK
     DMFDIGSESS TLLLHDASSQ FIDRRKLRHR RNAGNQQNTQ QLPSLNFFDD YLLFPTDETA
     VIPQSVKNAV RNSVNSVKPT SAEASLFSPL LSMANANPTN GRERDPRASE RAERDREKAV
     EKGLSGATEE DIQSDLQLLK KELAKKK
 
 
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