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SOL1_SCHPO
ID   SOL1_SCHPO              Reviewed;         865 AA.
AC   O74365;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=SWI/SNF chromatin-remodeling complex subunit sol1;
DE   AltName: Full=SWI/SNF complex subunit sol1;
DE   AltName: Full=Switch one-like protein;
DE   AltName: Full=Transcription regulatory protein sol1;
GN   Name=sol1; ORFNames=SPBC30B4.04c;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852 AND SER-855, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
RN   [4]
RP   IDENTIFICATION IN THE SWI/SNF COMPLEX, FUNCTION OF THE SWI/SNF 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, required for the positive and negative regulation
CC       of gene expression of a large number of genes. It changes chromatin
CC       structure by altering DNA-histone contacts within a nucleosome, leading
CC       eventually to a change in nucleosome position, thus facilitating or
CC       repressing binding of gene-specific transcription factors.
CC       {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, sbf59,
CC       sol1, ssr1, ssr2, ssr3, ssr4 and tfg3. {ECO:0000269|PubMed:18622392}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC       ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the SWI1 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA20317.1; -; Genomic_DNA.
DR   PIR; T40170; T40170.
DR   RefSeq; NP_595529.1; NM_001021439.2.
DR   AlphaFoldDB; O74365; -.
DR   SMR; O74365; -.
DR   BioGRID; 276848; 64.
DR   ComplexPortal; CPX-6362; SWI/SNF chromatin remodelling complex.
DR   DIP; DIP-48378N; -.
DR   IntAct; O74365; 6.
DR   STRING; 4896.SPBC30B4.04c.1; -.
DR   iPTMnet; O74365; -.
DR   MaxQB; O74365; -.
DR   PaxDb; O74365; -.
DR   PRIDE; O74365; -.
DR   EnsemblFungi; SPBC30B4.04c.1; SPBC30B4.04c.1:pep; SPBC30B4.04c.
DR   GeneID; 2540318; -.
DR   KEGG; spo:SPBC30B4.04c; -.
DR   PomBase; SPBC30B4.04c; sol1.
DR   VEuPathDB; FungiDB:SPBC30B4.04c; -.
DR   eggNOG; KOG2744; Eukaryota.
DR   HOGENOM; CLU_326016_0_0_1; -.
DR   InParanoid; O74365; -.
DR   OMA; INLMMLY; -.
DR   PhylomeDB; O74365; -.
DR   Reactome; R-SPO-3214815; HDACs deacetylate histones.
DR   PRO; PR:O74365; -.
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:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
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; IDA:PomBase.
DR   Gene3D; 1.10.150.60; -; 1.
DR   InterPro; IPR001606; ARID_dom.
DR   InterPro; IPR036431; ARID_dom_sf.
DR   InterPro; IPR016024; ARM-type_fold.
DR   Pfam; PF01388; ARID; 1.
DR   SMART; SM00501; BRIGHT; 1.
DR   SUPFAM; SSF46774; SSF46774; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51011; ARID; 1.
PE   1: Evidence at protein level;
KW   Activator; Chromatin regulator; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..865
FT                   /note="SWI/SNF chromatin-remodeling complex subunit sol1"
FT                   /id="PRO_0000318141"
FT   DOMAIN          188..278
FT                   /note="ARID"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..357
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         852
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         855
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   865 AA;  96018 MW;  0DEF2AEC233425A8 CRC64;
     MNNQGFVPAS DYPTAVSYPT QGQSYNTQEE QPAYPQRFST SQGMYAAEYG NANMMNTSEN
     EPNNLAHSQP FRQSPSTQRN LPNQSFDFAS NGAWNGSGSV KYSSPMMPSS RIPFQQEKEA
     AMQQQQQQQQ QQQLYQRQMQ SREALLSQQI PPNQIGINAH PAVRQTPQPA PSPNTPSGNA
     NQLTPAYAAS FDKFMVSLIS FMEKRGTPIK SYPQINNTPI NLMMLYALVM RAGGSRQVSA
     HNFWPKISAS LGFPSPDAIS LLIQYYNSYL LPYEEAWLAA QQQQKSLQQA KANHSANVQS
     RPKNYPQKPV QTTPEAVHAN GSMHGSLHSK SPSPAFTANR FSPAAPTTVS SERNAPPYPS
     APTRPTPPTV QTSSSAAPVD SAEPVAYQPI KKPIDPMLGY PLNVAATYRL DESLLRLQMP
     SIVDLGTVNI QALCMSLQST LEKEITYAMN VLLILTNDQK WMFPLSECQD VVDALIDVAT
     QCLDNLLSVL PNEDLMEIAD KRPSYRQLLY NCCVEISQFS REDFSNSLSE NKTKDSINAI
     DVHNSEQNLL AVFVIFRNLS HFEANQNVLV QNPDFFPLLI RVVKSLNFHA TSLLRSSRNT
     LDLHKDVLIV LCQLSQNFIL PNVDVARHVL LFILSFSPFN RKKSKTILND TLPTSIPSYT
     PATHPYAGPA INAYAKLLAK DANNKTNFQA IFDNNPKFLD SLFLLLASVV PKFNRHCLKI
     CERRLPLLQQ SFFCLAATVS YVKQSEQAAN WCNIGEGFFV SMLRLLILLS GHPSLNPPSR
     VASQYPTTNP FRYVIQSGIS TVRRLLSLVE AGNISLSSFP KSETLLAVLL APTTETSFLK
     EISNLLDRTG DSDASLENTD DKSGI
 
 
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