SSR2_SCHPO
ID SSR2_SCHPO Reviewed; 503 AA.
AC O14470; P78877;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=SWI/SNF and RSC complexes subunit ssr2;
GN Name=ssr2; ORFNames=SPAC23H3.10;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-503.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175 AND SER-306, 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 [5]
RP IDENTIFICATION IN THE SWI/SNF AND RSC COMPLEXES, FUNCTION OF THE SWI/SNF
RP AND RSC COMPLEXES, AND 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. Part 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 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). Component of the SWI/SNF global
CC transcription activator complex composed of at least arp9, arp42, snf5,
CC snf22, snf30, sbf59, sol1, ssr1, ssr2, ssr3, ssr4 and tfg3.
CC {ECO:0000250, ECO:0000269|PubMed:18622392}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00624}.
CC -!- SIMILARITY: Belongs to the SMARCC family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16236.1; -; Genomic_DNA.
DR EMBL; D89227; BAA13888.1; -; mRNA.
DR PIR; T38303; T38303.
DR PIR; T43061; T43061.
DR RefSeq; NP_593800.1; NM_001019229.2.
DR AlphaFoldDB; O14470; -.
DR SMR; O14470; -.
DR BioGRID; 278342; 13.
DR ComplexPortal; CPX-6362; SWI/SNF chromatin remodelling complex.
DR ComplexPortal; CPX-6363; RSC chromatin remodelling complex.
DR DIP; DIP-48383N; -.
DR IntAct; O14470; 10.
DR STRING; 4896.SPAC23H3.10.1; -.
DR iPTMnet; O14470; -.
DR MaxQB; O14470; -.
DR PaxDb; O14470; -.
DR PRIDE; O14470; -.
DR EnsemblFungi; SPAC23H3.10.1; SPAC23H3.10.1:pep; SPAC23H3.10.
DR GeneID; 2541851; -.
DR KEGG; spo:SPAC23H3.10; -.
DR PomBase; SPAC23H3.10; ssr2.
DR VEuPathDB; FungiDB:SPAC23H3.10; -.
DR eggNOG; KOG1279; Eukaryota.
DR HOGENOM; CLU_004447_3_2_1; -.
DR InParanoid; O14470; -.
DR OMA; EESPCTI; -.
DR PhylomeDB; O14470; -.
DR PRO; PR:O14470; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0016586; C:RSC-type complex; IDA:PomBase.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:PomBase.
DR GO; GO:0003677; F:DNA binding; ISM:PomBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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:1905168; P:positive regulation of double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IPI:PomBase.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02336; ZZ_RSC8; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR041984; Rsc8/Ssr1/Ssr2_ZZ.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR032451; SMARCC_C.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF16495; SWIRM-assoc_1; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..503
FT /note="SWI/SNF and RSC complexes subunit ssr2"
FT /id="PRO_0000197084"
FT DOMAIN 18..115
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT DOMAIN 245..296
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 188..242
FT /note="ZZ-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 465
FT /note="D -> A (in Ref. 2; BAA13888)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 503 AA; 57685 MW; 41FA0BEE2E372114 CRC64;
MTLDQVRIPF LVEQTYPIIV PSYAGWFDMS KIHDIERRSN PEFFNGKSPL KTPSIYKDYR
DFMINSYRLE PNEYLTVTAC RRNLVGDVCA IIRVHAFLEQ WGLINYQIDP ETRPAFRLPP
ISGHVQAISN TPIVTQEMLA QHPPPSTVGG SSSQEFVKLE EKHYSPSLNA MEQTSPKEED
EKSDKVPRVD KVCFTCGVNC SQTWYHNLKN KKYDICPNCY KQGRFSSSFN SSDFLCMDAI
DFNHDEEKPW SNQETLLLLE AIETYGDDWN QIALHVGSRT KEQCLIHFLQ IPIEDPYRQK
LQGDFSPFKK GFLPFDENEN PVLSTLTYLA SIVQQGMKER KQNESVKQGE TSFGNSEFKN
PLERVAYYAL KSAAQKAKLI AAFENRQLRR LVFSLIQAQL EKLQLKMKVL EQLEKMCSLE
LSELDLRGKN LLLSRLSTKK MLLAFNKKLE EAVNLGGEDG LKIIDDLMST EHAEALLTFE
MPTATTVSPL SKQYPDKFRT IAL
