RSC4_SCHPO
ID RSC4_SCHPO Reviewed; 542 AA.
AC Q09948;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Chromatin structure-remodeling complex subunit rsc4;
DE AltName: Full=Bromodomain-containing protein brd1;
DE AltName: Full=RSC complex subunit rsc4;
GN Name=rsc4; Synonyms=brd1; ORFNames=SPBC1734.15;
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 [GENOMIC DNA].
RX PubMed=7565614; DOI=10.1007/bf02191650;
RA Aves S.J., Hindley J., Phear G.A., Tongue N.;
RT "A fission yeast gene mapping close to suc1 encodes a protein containing
RT two bromodomains.";
RL Mol. Gen. Genet. 248:491-498(1995).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-271; SER-287 AND
RP SER-313, AND 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:0000305}.
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DR EMBL; X86764; CAA60444.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA21309.1; -; Genomic_DNA.
DR PIR; S58680; S54260.
DR RefSeq; NP_595432.1; NM_001021340.2.
DR AlphaFoldDB; Q09948; -.
DR SMR; Q09948; -.
DR BioGRID; 276543; 137.
DR ComplexPortal; CPX-6363; RSC chromatin remodelling complex.
DR DIP; DIP-48391N; -.
DR IntAct; Q09948; 6.
DR STRING; 4896.SPBC1734.15.1; -.
DR iPTMnet; Q09948; -.
DR MaxQB; Q09948; -.
DR PaxDb; Q09948; -.
DR PRIDE; Q09948; -.
DR EnsemblFungi; SPBC1734.15.1; SPBC1734.15.1:pep; SPBC1734.15.
DR GeneID; 2539999; -.
DR KEGG; spo:SPBC1734.15; -.
DR PomBase; SPBC1734.15; rsc4.
DR VEuPathDB; FungiDB:SPBC1734.15; -.
DR eggNOG; KOG1827; Eukaryota.
DR HOGENOM; CLU_506375_0_0_1; -.
DR InParanoid; Q09948; -.
DR OMA; YNEAGSF; -.
DR PRO; PR:Q09948; -.
DR Proteomes; UP000002485; Chromosome II.
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:0003682; F:chromatin binding; IBA:GO_Central.
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:0006366; P:transcription by RNA polymerase II; IC:PomBase.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR037382; Rsc/polybromo.
DR InterPro; IPR027180; RSC1/2/4.
DR PANTHER; PTHR16062; PTHR16062; 2.
DR PANTHER; PTHR16062:SF19; PTHR16062:SF19; 2.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Bromodomain; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..542
FT /note="Chromatin structure-remodeling complex subunit rsc4"
FT /id="PRO_0000211178"
FT DOMAIN 29..99
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 162..232
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 114..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 542 AA; 60667 MW; B900D1F77327C2A6 CRC64;
MVDDSHNAPF DKTKFDEVLE ALVGLKDNEG NPFDDIFEEL PSKRYFPDYY QIIQKPICYK
MMRNKAKTGK YLSMGDFYDD IRLMVSNAQT YNMPGSLVYE CSVLIANTAN SLESKDGTLN
EEENEEMESS INEEHKPGTN EIDVPKVIQN ILDALHEEKD EQGRFLIDIF IDLPSKRLYP
DYYEIIKSPM TIKMLEKRFK KGEYTTLESF VKDLNQMFIN AKTYNAPGSF VYEDAEKLSQ
LSSSLISSFS EQPKEHSPAT SKHEPEETPA SPTPSVSAST SRERSTSVAP SFITSDQAAT
PDVLKSEEAH VESFSKESEK DQTPIPEDVP SPMDTLSQAN YGAFALIKSF PSTPVPDFLN
FSHKSVMGRS TFNMPNFPEP KFFEDIPNTE RCILSAFICS PPQLPLPNPL RMYLPCPSLN
STEVSVITLA PQHSFLNIVI NLNPALALKS YTIITLLNGK RLGAGVSTPP STLYALEGIK
HTEEPIRTVY EAKLSVGLNC LEFVLGSTEP VEPPSIEPGL PASAYSRTVE RERFVLMAYV
QP
