ID RSC1_SCHPO Reviewed; 803 AA.
AC O74964;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=Chromatin structure-remodeling complex subunit rsc1;
DE AltName: Full=RSC complex subunit rsc1;
DE AltName: Full=Remodel the structure of chromatin complex subunit 1;
GN Name=rsc1; ORFNames=SPBC4B4.03;
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-168; SER-331 AND SER-334, 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 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: Nucleus {ECO:0000269|PubMed:16823372}.
CC Note=Localizes to centromeric and flanking chromatin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RSC1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA19283.1; -; Genomic_DNA.
DR PIR; T40475; T40475.
DR RefSeq; NP_596420.1; NM_001022339.2.
DR AlphaFoldDB; O74964; -.
DR SMR; O74964; -.
DR BioGRID; 277271; 107.
DR ComplexPortal; CPX-6363; RSC chromatin remodelling complex.
DR DIP; DIP-48389N; -.
DR IntAct; O74964; 12.
DR STRING; 284812.O74964; -.
DR iPTMnet; O74964; -.
DR MaxQB; O74964; -.
DR PaxDb; 4896-SPBC4B4-03-1; -.
DR EnsemblFungi; SPBC4B4.03.1; SPBC4B4.03.1:pep; SPBC4B4.03.
DR GeneID; 2540749; -.
DR KEGG; spo:SPBC4B4.03; -.
DR PomBase; SPBC4B4.03; rsc1.
DR VEuPathDB; FungiDB:SPBC4B4.03; -.
DR eggNOG; KOG1827; Eukaryota.
DR HOGENOM; CLU_338353_0_0_1; -.
DR InParanoid; O74964; -.
DR OMA; YEMILFD; -.
DR PhylomeDB; O74964; -.
DR PRO; PR:O74964; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; NAS:ComplexPortal.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016586; C:RSC-type complex; IDA:PomBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:UniProt.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IC:PomBase.
DR CDD; cd04717; BAH_polybromo; 1.
DR CDD; cd05522; Bromo_Rsc1_2_II; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 2.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR037382; Rsc/polybromo.
DR InterPro; IPR048047; RSC1/2_bromodom.
DR PANTHER; PTHR16062:SF24; CHROMATIN STRUCTURE-REMODELING COMPLEX SUBUNIT RSC1; 1.
DR PANTHER; PTHR16062; SWI/SNF-RELATED; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; Bromodomain; 2.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Bromodomain; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..803
FT /note="Chromatin structure-remodeling complex subunit rsc1"
FT /id="PRO_0000211210"
FT DOMAIN 31..101
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 229..299
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 351..469
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REGION 128..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 803 AA; 90132 MW; 2C2706CB022510F7 CRC64;
MSSKIRPSAD DKKLQRVLYF FLERVRAAKD VSGQLLSPLI DNASVDTASV SPSSNGRPTT
LKSIQSKIDE FQYHDFSEFV SDLAYLFINV KALYEGTQTY SFVQALEEFC IQQLRTFQQQ
GYIPVITWPN TDSPSATTSS PISRNPEYSV SPPNGSKFVK NEDEAYDSDL YVEEEDSDVK
GRSMVGRDGR YKSEDLKRRK LQPSSKPLSS LEARAKVIMR QVRRYRDGSG RQLFAPFERL
PDPRMFPEYY QAIEQPMALE VIQKKLSKHR YETIEQFVDD FNLMFDNAKS FNDPSSQVYR
DADFLKNYLA DVLRLEAGKL DSEFFNYETD SRASPQLPKN DIQPAVSIDG TLLNVGDWVL
IRNPADSSKP IVSQIYRIWK SDDDINYVTV CWYLRPEQTV HRADAVFYEN EVFKTSLYRD
HPVSEIVGRC FVMYITRYIR GRPKGIRSTP VFVCESRYND DTKQFSKIKS WKACMPQEVS
GSEYEMILFD RPITLTKVAS PLLHLLASKS QGLPSPATTD SNTHMLPSQG SLLPPSSISE
TKSFSTKAST PLSTDDIATP LSSAPNPPSV MPTYARKTSS HSERSSHSSY HNSSHVPTAA
FNSPIMRTST KSTSPIPARP FYAQSGSLQS LNTTQHSHQI SGGHSGRMNV PYAKLSYTSH
NGRHGGSNGN ISGAKTPMTN YTINSMPSLP VFPPAFIVPG THQKLDESSP VPGIDDVTVI
NTETAKMLDK DEHQNVLWYT VPPLDPIPLE NRNGSLTHSV EYVLYKKSKG SQVITEKARS
NELSREAKFE NLVASLSDAL IPP
//
