PST2_SCHPO
ID PST2_SCHPO Reviewed; 1075 AA.
AC O13919;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Paired amphipathic helix protein pst2;
DE AltName: Full=SIN3 homolog 2;
GN Name=pst2; ORFNames=SPAC23C11.15;
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 [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 GENE NAME.
RX PubMed=10022921; DOI=10.1128/mcb.19.3.2351;
RA Dang V.D., Benedik M.J., Ekwall K., Choi J., Allshire R.C., Levin H.L.;
RT "A new member of the Sin3 family of corepressors is essential for cell
RT viability and required for retroelement propagation in fission yeast.";
RL Mol. Cell. Biol. 19:2351-2365(1999).
RN [3]
RP PROTEIN SEQUENCE OF 87-104; 280-291; 386-395; 424-446; 608-637; 678-709;
RP 780-788; 819-834; 869-883; 925-937 AND 1055-1075, FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12773392; DOI=10.1093/emboj/cdg248;
RA Nakayama J., Xiao G., Noma K., Malikzay A., Bjerling P., Ekwall K.,
RA Kobayashi R., Grewal S.I.S.;
RT "Alp13, an MRG family protein, is a component of fission yeast Clr6 histone
RT deacetylase required for genomic integrity.";
RL EMBO J. 22:2776-2787(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND SER-643, 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).
CC -!- FUNCTION: Has a role in chromatin assembly and chromosome segregation.
CC Involved in the deacetylation of histones.
CC {ECO:0000269|PubMed:12773392}.
CC -!- SUBUNIT: Heterotetramer of alp13, clr6, prw1 and pst2.
CC {ECO:0000269|PubMed:12773392}.
CC -!- INTERACTION:
CC O13919; O13953: alp13; NbExp=4; IntAct=EBI-904686, EBI-904711;
CC O13919; O59702: clr6; NbExp=7; IntAct=EBI-904686, EBI-904651;
CC O13919; O14021: prw1; NbExp=3; IntAct=EBI-904686, EBI-904698;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810,
CC ECO:0000269|PubMed:12773392}.
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DR EMBL; CU329670; CAB11171.1; -; Genomic_DNA.
DR PIR; T38253; T38253.
DR RefSeq; NP_593646.1; NM_001019077.2.
DR AlphaFoldDB; O13919; -.
DR SMR; O13919; -.
DR BioGRID; 278120; 252.
DR DIP; DIP-29341N; -.
DR IntAct; O13919; 6.
DR STRING; 4896.SPAC23C11.15.1; -.
DR iPTMnet; O13919; -.
DR MaxQB; O13919; -.
DR PaxDb; O13919; -.
DR PRIDE; O13919; -.
DR EnsemblFungi; SPAC23C11.15.1; SPAC23C11.15.1:pep; SPAC23C11.15.
DR GeneID; 2541624; -.
DR KEGG; spo:SPAC23C11.15; -.
DR PomBase; SPAC23C11.15; pst2.
DR VEuPathDB; FungiDB:SPAC23C11.15; -.
DR eggNOG; KOG4204; Eukaryota.
DR HOGENOM; CLU_001360_2_2_1; -.
DR InParanoid; O13919; -.
DR OMA; KQVHHIV; -.
DR PhylomeDB; O13919; -.
DR PRO; PR:O13919; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0032221; C:Rpd3S/Clr6-CII complex; IDA:PomBase.
DR GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IC:PomBase.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.20.1160.11; -; 3.
DR InterPro; IPR013194; HDAC_interact_dom.
DR InterPro; IPR003822; PAH.
DR InterPro; IPR036600; PAH_sf.
DR InterPro; IPR039774; Sin3-like.
DR InterPro; IPR031693; Sin3_C.
DR PANTHER; PTHR12346; PTHR12346; 1.
DR Pfam; PF08295; Sin3_corepress; 1.
DR Pfam; PF16879; Sin3a_C; 1.
DR SMART; SM00761; HDAC_interact; 1.
DR SUPFAM; SSF47762; SSF47762; 3.
DR PROSITE; PS51477; PAH; 3.
PE 1: Evidence at protein level;
KW Chromatin regulator; Direct protein sequencing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1075
FT /note="Paired amphipathic helix protein pst2"
FT /id="PRO_0000121542"
FT DOMAIN 28..102
FT /note="PAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 138..208
FT /note="PAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 243..319
FT /note="PAH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT REGION 647..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1075 AA; 124849 MW; 1AD301DB4EB1AFFB CRC64;
MEQTLAILKN DNSTLVAEMQ NQLVHDFSPN GTALPELDIK AFVQKLGQRL CHRPYVYSAF
MDVVKALHNE IVDFPGFIER ISVILRDYPD LLEYLNIFLP SSYKYLLSNS GANFTLQFTT
PSGPVSTPST YVATYNDLPC TYHRAIGFVS RVRRALLSNP EQFFKLQDSL RKFKNSECSL
SELQTIVTSL LAEHPSLAHE FHNFLPSSIF FGSKPPLGSF PLRGIQSSQF TLSNISDLLS
QSRPDNLSPF SHLSNESSDF FKNVKNVLTD VETYHEFLKL LNLYVQGIID RNILVSRGFG
FLKSNSGLWR SFLSLTSLSP EEFLSVYNSA CSDFPECGPS YRLLPVEERN ISCSGRDDFA
WGILNDDWVS HPTWASEESG FIVQRKTPYE EAMTKLEEER YEFDRHIEAT SWTIKSLKKI
QNRINELPEE ERETYTLEEG LGLPSKSIYK KTIKLVYTSE HAEEMFKALE RMPCLTLPLV
ISRLEEKNEE WKSVKRSLQP GWRSIEFKNY DKSLDSQCVY FKARDKKNVS SKFLLAEADI
LRSQAKLHFP LRSRSAFEFS FVYDNEIVLF DTCYMVCTYI VCNSPSGLKK VEHFFKNILP
LHFGLEKDKF SIFLDQVFRG PDYDVNAPNI VGNKPVRRKR SNSITQLTEF VKQPKINGQR
ESRSAAAARK KEESGNKSQS NSQNSLSDES GNVTPVSKKQ LSQPAAAIKA SLKYPSHPDS
LLEHQDHAGD TENEMHDDVD KEQFGYSSMY VFFRLFNLLY ERLYELQRLE DQVSIIQQRI
IPNPVSQKQK IWRDRWNDLS DVPDEKTHYE NTYVMILRLI YGIVDQSAFE DYLRFYYGNK
AYKIYTIDKL VWSAAKQVHH IVSDGKYKFV TSLVEQNSSA SPKKNYDDFL YRLEIEKLLN
PDEILFRFCW INKFKSFGIK IMKRANLIVD QSLDTQRRVW KKYVQNYRIQ KLTEEISYKN
YRCPFLCRNI EKERTVEQLV SRLQTKLLRS AELVSGLQAK LCLDSFKLLY LPRTEDSYID
ASYLRLRDTD FLDCQNKRKQ RWRNRWESLL KSVRGTSDNT AEVNFDADIN ALFIP
