PST1_SCHPO
ID PST1_SCHPO Reviewed; 1522 AA.
AC Q09750;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Paired amphipathic helix protein pst1;
DE AltName: Full=SIN3 homolog 1;
GN Name=pst1; ORFNames=SPBC12C2.10c, SPBC21D10.01c;
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], AND CHARACTERIZATION.
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 [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 PROTEIN SEQUENCE OF 133-155; 179-193; 489-500; 655-664; 772-781; 901-915;
RP 933-946; 1364-1373 AND 1454-1468.
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-442; THR-446 AND SER-1443,
RP 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).
CC -!- FUNCTION: Has a role in modulating the nuclear import of TF1 virus-like
CC particles. Essential for viability.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; AF280407; AAF90180.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA20757.1; -; Genomic_DNA.
DR PIR; T39371; T39371.
DR RefSeq; NP_596012.2; NM_001021920.2.
DR AlphaFoldDB; Q09750; -.
DR SMR; Q09750; -.
DR BioGRID; 276562; 7.
DR DIP; DIP-29340N; -.
DR IntAct; Q09750; 4.
DR STRING; 4896.SPBC12C2.10c.1; -.
DR iPTMnet; Q09750; -.
DR MaxQB; Q09750; -.
DR PaxDb; Q09750; -.
DR PRIDE; Q09750; -.
DR EnsemblFungi; SPBC12C2.10c.1; SPBC12C2.10c.1:pep; SPBC12C2.10c.
DR GeneID; 2540018; -.
DR KEGG; spo:SPBC12C2.10c; -.
DR PomBase; SPBC12C2.10c; pst1.
DR VEuPathDB; FungiDB:SPBC12C2.10c; -.
DR eggNOG; KOG4204; Eukaryota.
DR HOGENOM; CLU_001360_2_4_1; -.
DR InParanoid; Q09750; -.
DR OMA; HKNEISY; -.
DR PhylomeDB; Q09750; -.
DR PRO; PR:Q09750; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:1990483; C:Clr6 histone deacetylase complex I''; IPI:PomBase.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0033698; C:Rpd3L 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:PomBase.
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; PF02671; PAH; 3.
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 Activator; Cell cycle; Cell division; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..1522
FT /note="Paired amphipathic helix protein pst1"
FT /id="PRO_0000121541"
FT DOMAIN 178..248
FT /note="PAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 345..415
FT /note="PAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT DOMAIN 504..576
FT /note="PAH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00810"
FT REGION 139..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1522
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 1443
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1522 AA; 171456 MW; 38433F99E153DDD2 CRC64;
MAKDWQDARL GQCHRLEDYS NVAINYTGPY LTPSGTMAYH PGNAPLFTQA PPHTNPQGPP
PFPLFNSISP VYDPATGRLL YRNVNTQVSH TAIPNPANGY AAVYGGPPSQ LPPPPQPQSH
PNVTVISASP ARAIEQQPTI LSSTDSNIPR PGTVKSSASP FVPNQNPSAP PPPPQEYRQL
NVTDALSYLD LVKLQFHQEP EIYNEFLDIM KEFKSQAIET PEVITRVSKL FAGYPNLIQG
FNTFLPPGYS IEISSADPGS LAGIHITTPQ GPLMINDLGK TTAPPPPHGS TTPLPAAASY
TSMNMKQSSA SHPVLQPPAP STLQFNPSPS PAAPSYPPVD ASVKQAADLD QAINFVNNVK
NRFSHKPEAY NSFLDILKSY QHDQRPIQLV YFQVSQLFAE APDLLEEFKR FLPDVSVNAP
AETQDKSTVV PQESATATPK RSPSATPTSA LPPIGKFAPP TTAKAQPAPE KRRGEPAVQT
RNHSKRTRTA TSSVEETTPR AFNVPIAQNK NPSELEFLEH ARQYLANESK YNEFIKLLEL
YSQEVFDKNA LVERCYVFFG SNEHLMNWLK DLVKYNPANP IPVPRPRVDL TQCKSCGPSY
RLLPKIELLL PCSGRDDLCW TILNDAWVSF PTLASEDSGF IAHRKNQFEE NLHKLEEERY
EYDRHIGANM RFIELLQIHA DKMLKMSEVE KANWTLPSNL GGKSVSIYHK VIKKVYGKEH
AQQIIENLQK NPSVTIPIVL ERLKKKDREW RSLQNHWNEL WHDIEEKNFY RSLDHQGVSF
KSVDKKSTTP KFLISELRNL AQQQKVELSE GKVTPSHQFL FSYKDPNIIT DIARLFGVFL
IHGSTHSAED NEKMSNFLRS FLSLFFDVPY DSFIPYLPTH FNEEESDIDS LSSSLIEKPR
ASSSPIHHAN NNGLRLLKDV LKKTYRGARE NRSSVKEDYV SESTERTPDA SEIDEHISEH
EENDDESSSV FSTGEVWVNC KFTDTDGSLL DDGTKLSDRS VYNLFGNMSL YCFFRLFHTL
YSRLEEIKNL EQMAYSKQHD VKSNPVAVEL GLVRHPSERL GFALPTADTV YEQAIQLCER
LMEGEIDQNG FEDALRCLYG IHAFRLYTVE KLVTSIIKQL HSVTTNRRLA QVFMYYEKDR
VQRRTSPRQQ IMYRIQTETA FGPDENLCCI DWNSQTRQSA IRLMGREDLT MGTLKSDAEK
WCYYIGSYIM SSPTEGILPE HVRIPFLRKC LPSDEGNEDD ESSSVVKSAN AIITSFLESG
LALTIPINTV KIRYENGTED VFARNSEQVY NGPYDKIRDY RQSKWREWLN SDEGWTQGLS
KDKVRRIKPC TIESLFNEST LRSGKAERFS ENAGVESIGK KGKNLLNESG NGKKLDKGLP
PKVNGKSSVT RGNKTNLKAR NGRNNDDSSN KINLSEKEKE KESIEDEEKN REGSMSPVAK
HASDVEDDHD VAKSTAPDFE TSSHRPERSS EKKSPSPVFT SVKQTAENDA DNEDDKTDMD
DQTEETLDAD NTMEEEPSKD DL
