SFH1_SCHPO
ID SFH1_SCHPO Reviewed; 418 AA.
AC Q9USM3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Chromatin structure-remodeling complex subunit sfh1;
DE AltName: Full=RSC complex subunit sfh1;
DE AltName: Full=SNF5 homolog 1;
GN Name=sfh1; ORFNames=SPCC16A11.14;
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 INTERACTION WITH SAD1, AND SUBCELLULAR LOCATION.
RX PubMed=14655046; DOI=10.1007/s00438-003-0938-8;
RA Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.;
RT "Two-hybrid search for proteins that interact with Sad1 and Kms1, two
RT membrane-bound components of the spindle pole body in fission yeast.";
RL Mol. Genet. Genomics 270:449-461(2004).
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-269, 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 [5]
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). Interacts with sad1.
CC {ECO:0000250, ECO:0000269|PubMed:14655046,
CC ECO:0000269|PubMed:18622392}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14655046,
CC ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SNF5 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329672; CAB53086.1; -; Genomic_DNA.
DR PIR; T41087; T41087.
DR RefSeq; NP_588001.1; NM_001022992.2.
DR AlphaFoldDB; Q9USM3; -.
DR SMR; Q9USM3; -.
DR BioGRID; 275716; 19.
DR ComplexPortal; CPX-6363; RSC chromatin remodelling complex.
DR DIP; DIP-38847N; -.
DR IntAct; Q9USM3; 15.
DR MINT; Q9USM3; -.
DR STRING; 4896.SPCC16A11.14.1; -.
DR iPTMnet; Q9USM3; -.
DR MaxQB; Q9USM3; -.
DR PaxDb; Q9USM3; -.
DR EnsemblFungi; SPCC16A11.14.1; SPCC16A11.14.1:pep; SPCC16A11.14.
DR GeneID; 2539144; -.
DR KEGG; spo:SPCC16A11.14; -.
DR PomBase; SPCC16A11.14; sfh1.
DR VEuPathDB; FungiDB:SPCC16A11.14; -.
DR eggNOG; KOG1601; Eukaryota.
DR eggNOG; KOG1649; Eukaryota.
DR HOGENOM; CLU_014421_3_0_1; -.
DR InParanoid; Q9USM3; -.
DR OMA; MWNLNES; -.
DR PhylomeDB; Q9USM3; -.
DR PRO; PR:Q9USM3; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000228; C:nuclear chromosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0016586; C:RSC-type complex; IDA:PomBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003712; F:transcription coregulator activity; 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR006939; SNF5.
DR InterPro; IPR000679; Znf_GATA.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00320; GATA; 1.
DR Pfam; PF04855; SNF5; 2.
DR SMART; SM00401; ZnF_GATA; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..418
FT /note="Chromatin structure-remodeling complex subunit sfh1"
FT /id="PRO_0000205960"
FT REGION 57..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 418 AA; 46839 MW; 00CBDC92BE975D26 CRC64;
MAQACKTTYS SRLKTGNTCL IQKNVAVSTR SHSSYTGRNS LRNVPAVNYA AFEQGEDFET
PVETPEKEEE KFETDDRGLA VGRPTGNNIY PRFATKTRHI YVTDEQLKCA AEERDVYIPI
RLDIELPNNY RLKDTFLWNM NEQVMTPDVF AQILCADLDL STNVYGTQIS SSIRAQIEEY
APVAEVPMPK GQEMLVVFNI QVQLAQLSYN DQVEWNLTSP LTPEEFSVLT CNDLGLSGES
RPEIAYAIHE CLLKLKKNAC EGDLPDYDSD AVPGTKAGPR QDMDTLGALW QPVLETVSLE
DAKKNENNRE NLVKQWRREA SKFGGFAADV SAERWRAAAL GNLSQSETAN LPSASVSDAQ
TLLEQERPRW RCRWCNVLGT GTFCVRRGPE GNKSLCNACG VAYAKTGQLP YWRKSLYT
