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SNF59_SCHPO
ID   SNF59_SCHPO             Reviewed;         515 AA.
AC   O74792;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=SWI/SNF global transcription activator complex subunit snf59;
GN   Name=snf59; ORFNames=SPBC26H8.09c;
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).
RN   [3]
RP   IDENTIFICATION IN THE SWI/SNF COMPLEX, FUNCTION OF THE 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).
CC   -!- FUNCTION: Component of the SWI/SNF complex, an ATP-dependent chromatin
CC       remodeling complex, which is required for the positive and negative
CC       regulation of gene expression of a large number of genes. It changes
CC       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. {ECO:0000269|PubMed:18622392}.
CC   -!- SUBUNIT: Component of the SWI/SNF global transcription activator
CC       complex composed of at least arp9, arp42, snf5, snf22, snf30, snf59,
CC       sol1, ssr1, ssr2, ssr3, ssr4 and tfg3. {ECO:0000269|PubMed:18622392}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the RSC7/SWP82 family. SWP82 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CU329671; CAA21101.1; -; Genomic_DNA.
DR   PIR; T40021; T40021.
DR   RefSeq; NP_596652.1; NM_001022574.2.
DR   AlphaFoldDB; O74792; -.
DR   BioGRID; 277002; 30.
DR   ComplexPortal; CPX-6362; SWI/SNF chromatin remodelling complex.
DR   DIP; DIP-48382N; -.
DR   IntAct; O74792; 11.
DR   STRING; 4896.SPBC26H8.09c.1; -.
DR   iPTMnet; O74792; -.
DR   MaxQB; O74792; -.
DR   PaxDb; O74792; -.
DR   PRIDE; O74792; -.
DR   EnsemblFungi; SPBC26H8.09c.1; SPBC26H8.09c.1:pep; SPBC26H8.09c.
DR   GeneID; 2540474; -.
DR   KEGG; spo:SPBC26H8.09c; -.
DR   PomBase; SPBC26H8.09c; snf59.
DR   VEuPathDB; FungiDB:SPBC26H8.09c; -.
DR   HOGENOM; CLU_529091_0_0_1; -.
DR   InParanoid; O74792; -.
DR   OMA; PHETTES; -.
DR   PhylomeDB; O74792; -.
DR   Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
DR   PRO; PR:O74792; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0016514; C:SWI/SNF complex; IDA:PomBase.
DR   GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
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   InterPro; IPR013933; CRC_Rsc7/Swp82.
DR   Pfam; PF08624; CRC_subunit; 1.
PE   1: Evidence at protein level;
KW   Activator; Chromatin regulator; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..515
FT                   /note="SWI/SNF global transcription activator complex
FT                   subunit snf59"
FT                   /id="PRO_0000373987"
FT   REGION          1..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..127
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  59039 MW;  41F6F294909739B6 CRC64;
     MEEEDITLEH SDDLNKEESG ESNRVNIEEP EHHDNSNKES TNLDDLNMLE EPKYHDNSNK
     ESTNLDDLNM LEEPEHHDNS KKESTNLDDS NMLEEPKHHD NSNKESTNLD DLNMSEEPKH
     HDSSNKESTN LDNSNMDESE NQKNFKIEEP KPSGDFRNEG PKQCDDSKIE KPELHVNSKI
     EEPIHRIDSE HNEPEYHTES KNEESEHNTK SIREEPIHHV DSKNEEPVYS KIPEKMGDEF
     SENSLSKSDS AVKQEGNLLI HPNNSLKDTA PSKCKEPPVD EALSKKEISD DIAQITSVTP
     ITEKIEDKDK YISEVIDTYG KLADGFEYRA KTFCLEGRGK VLYMLGTECS RLLGFKDSYF
     MFHKTPSLRK VLTTQSERDQ MVEMGLLASN FRFRQLSIVP ARQMFLAFGA RILMKGTIDP
     ESHKALIEKN ISWADDEYYH MDVMANGSTR SSSVKLELKS MDNQNSPSPF QGKDILTLAQ
     GASFYNSKVM RTRNLRKEAR LSYYTKLRGV NRSVS
 
 
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