RSC58_SCHPO
ID RSC58_SCHPO Reviewed; 403 AA.
AC Q10412;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Chromatin structure-remodeling complex subunit rsc58;
DE AltName: Full=RSC complex subunit rsc58;
GN Name=rsc58; ORFNames=SPAC1F3.07c;
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-384, AND IDENTIFICATION BY
RP 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 RSC COMPLEX, FUNCTION OF THE RSC 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 chromatin structure remodeling complex
CC (RSC), which is involved in transcription regulation and nucleosome
CC positioning. Controls particularly membrane and organelle development
CC genes. {ECO:0000269|PubMed:18622392}.
CC -!- SUBUNIT: Component of the RSC complex composed of at least arp9, arp42,
CC rsc1, rsc4, rsc7, rsc9, rsc58, sfh1, snf21, ssr1, ssr2, ssr3 and ssr4.
CC The complex interacts with histone and histone variant components of
CC centromeric chromatin (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329670; CAA94625.1; -; Genomic_DNA.
DR PIR; T38078; T38078.
DR RefSeq; NP_593010.1; NM_001018409.2.
DR AlphaFoldDB; Q10412; -.
DR BioGRID; 277925; 10.
DR ComplexPortal; CPX-6363; RSC chromatin remodelling complex.
DR DIP; DIP-48392N; -.
DR IntAct; Q10412; 6.
DR STRING; 4896.SPAC1F3.07c.1; -.
DR iPTMnet; Q10412; -.
DR MaxQB; Q10412; -.
DR PaxDb; Q10412; -.
DR PRIDE; Q10412; -.
DR EnsemblFungi; SPAC1F3.07c.1; SPAC1F3.07c.1:pep; SPAC1F3.07c.
DR GeneID; 2541419; -.
DR KEGG; spo:SPAC1F3.07c; -.
DR PomBase; SPAC1F3.07c; rsc58.
DR VEuPathDB; FungiDB:SPAC1F3.07c; -.
DR eggNOG; ENOG502R7M9; Eukaryota.
DR HOGENOM; CLU_683628_0_0_1; -.
DR OMA; KSHALMM; -.
DR PRO; PR:Q10412; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016586; C:RSC-type complex; IDA:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..403
FT /note="Chromatin structure-remodeling complex subunit
FT rsc58"
FT /id="PRO_0000116597"
FT REGION 376..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 403 AA; 44621 MW; 3882059A78880CDE CRC64;
MNAESCSLIL SYISSAPAGN LVLNCTATTN KQTLEANLKS AVYQRYPEFL EDWTNVCVHI
IHSYFPKDAD YWNVDKLYTS VNRITTLEQS KVVGKEIKNG FTFDAENSTA SLENDLQPQF
RSHALFMVGS AGPLFSSTAR TSRLDSRLPD GGIIAKPVAL LPTPSVANSQ EYTLDKLSPP
STAKPPASVI EFNPSLAKLP TVKYLQSGPF SSIAPYKNSS SSVIPDSSFH SVACYRASSH
YKEAPVEKSI DIDIIQNNLS LLEEDSWTSV PIQGELVELN KLLQHLQLLQ NQRITSHNVL
SDEERQISVQ VQNLILKLAK DYDMSPEDFL MDDFTLSLTQ YGAFYRGTLP LSAQPLELPS
QQLLRSQSNA ALRSNSLSMN GSLSPSSTNV PLQSYRRTTK SRR
