STE11_SCHPO
ID STE11_SCHPO Reviewed; 468 AA.
AC P36631; O59696; Q9UU71;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Transcription factor ste11;
GN Name=ste11; Synonyms=stex; ORFNames=SPBC32C12.02;
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=1657709; DOI=10.1101/gad.5.11.1990;
RA Sugimoto A., Iino Y., Maeda T., Watanabe Y., Yamamoto M.;
RT "Schizosaccharomyces pombe ste11+ encodes a transcription factor with an
RT HMG motif that is a critical regulator of sexual development.";
RL Genes Dev. 5:1990-1999(1991).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-101.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-173 AND SER-218, AND
RP MUTAGENESIS OF THR-173 AND SER-218.
RX PubMed=12697825; DOI=10.1128/mcb.23.9.3253-3264.2003;
RA Qin J., Kang W., Leung B., McLeod M.;
RT "Ste11p, a high-mobility-group box DNA-binding protein, undergoes
RT pheromone- and nutrient-regulated nuclear-cytoplasmic shuttling.";
RL Mol. Cell. Biol. 23:3253-3264(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND SER-211, 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: Key transcription factor for sexual development. Activates
CC the transcription of the matp, matm, mei2, mfm, ste6 and rgs1 genes.
CC Binds specifically to a DNA fragment carrying a 10-base motif 5'-
CC TTCTTTGTTY-3'.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:12697825}. Cytoplasm {ECO:0000269|PubMed:12697825}.
CC Note=Accumulates in the nucleus under conditions of nitrogen starvation
CC and in the presence of mating pheromones.
CC -!- INDUCTION: By nitrogen starvation.
CC -!- PTM: Phosphorylation results in inactivation.
CC {ECO:0000269|PubMed:12697825, ECO:0000269|PubMed:18257517}.
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DR EMBL; Z11156; CAA77507.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA18162.1; -; Genomic_DNA.
DR EMBL; AB027776; BAA87080.1; -; Genomic_DNA.
DR PIR; A41518; A41518.
DR PIR; T40223; T40223.
DR RefSeq; NP_596656.1; NM_001022578.2.
DR AlphaFoldDB; P36631; -.
DR SMR; P36631; -.
DR BioGRID; 276789; 31.
DR STRING; 4896.SPBC32C12.02.1; -.
DR iPTMnet; P36631; -.
DR MaxQB; P36631; -.
DR PaxDb; P36631; -.
DR PRIDE; P36631; -.
DR EnsemblFungi; SPBC32C12.02.1; SPBC32C12.02.1:pep; SPBC32C12.02.
DR GeneID; 2540258; -.
DR KEGG; spo:SPBC32C12.02; -.
DR PomBase; SPBC32C12.02; ste11.
DR VEuPathDB; FungiDB:SPBC32C12.02; -.
DR eggNOG; KOG0528; Eukaryota.
DR HOGENOM; CLU_577655_0_0_1; -.
DR InParanoid; P36631; -.
DR PhylomeDB; P36631; -.
DR PRO; PR:P36631; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:PomBase.
DR GO; GO:0034064; C:Tor2-Mei2-Ste11 complex; IDA:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:PomBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IMP:PomBase.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:PomBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0044377; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding, bending; IDA:PomBase.
DR GO; GO:0010514; P:induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:1900237; P:positive regulation of induction of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..468
FT /note="Transcription factor ste11"
FT /id="PRO_0000048579"
FT DNA_BIND 16..80
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:12697825"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12697825"
FT MUTAGEN 173
FT /note="T->A: 100% activity; nuclear accumulation."
FT /evidence="ECO:0000269|PubMed:12697825"
FT MUTAGEN 218
FT /note="S->A: 100% activity; nuclear accumulation."
FT /evidence="ECO:0000269|PubMed:12697825"
FT CONFLICT 92
FT /note="R -> P (in Ref. 1; CAA77507)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..101
FT /note="PSSG -> LLPD (in Ref. 3; BAA87080)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 468 AA; 51245 MW; 9EC98FE93219EA0E CRC64;
MSASLTAEQK DQKSSVKRPL NSFMLYRRDR QAEIPTSNHQ SISRIIGQLW RNESAQVKKY
YSDLSALERQ KHMLENPEYK YTPKKRSTVR RRHKKVSPSS GSFVASDYVV LQQIAQSSKT
LKQTEPEKPV NEEETLAALL APALSYPKSG KSNLIETSEL SCLSSSPMIR SHTIPSLSFT
DQVSTTISTL DKSEQAPSSL GIYYRSPSSG SPIGRTKSVC LANKARIVPK RSMSSDGCVD
KSYQMSKTPS LEANLPQNSS NCSARRVPKF DSKGTVSEQS NSDSPELSAD KVLSHCSPID
ARPSTPSCPN ASISPKTPNT GDHYGFDGAE YLGTPLSVGS TTAYLYGQET ELLSTPYCHT
SYPAMSRLNS SSGYTCVSSS SVTNSGHTEN NTWRSDEQSK GFVDINSFSQ SLFSNGNYEF
AAHSQELDDL FSQITDFTST DPIASSLKDA NSLGPSLLEP WLPNSNLF
