ID   MBX1_SCHPO              Reviewed;         457 AA.
AC   O42954;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=MADS-box transcription factor 1;
GN   Name=mbx1; ORFNames=SPBC19G7.06;
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   FUNCTION, AND PHOSPHORYLATION.
RX   PubMed=15509866; DOI=10.1242/jcs.01473;
RA   Buck V., Ng S.S., Ruiz-Garcia A.B., Papadopoulou K., Bhatti S.,
RA   Samuel J.M., Anderson M., Millar J.B.A., McInerny C.J.;
RT   "Fkh2p and Sep1p regulate mitotic gene transcription in fission yeast.";
RL   J. Cell Sci. 117:5623-5632(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, 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).
CC   -!- FUNCTION: Acts as a transcriptional activator with a role in the
CC       regulation of mitosis. Regulates septation and the periodic
CC       transcription of cdc15. {ECO:0000269|PubMed:15509866}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
CC   -!- PTM: Phosphorylated. Occurs periodically during mitosis.
CC       {ECO:0000269|PubMed:15509866, ECO:0000269|PubMed:18257517}.
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DR   EMBL; CU329671; CAA17060.2; -; Genomic_DNA.
DR   PIR; T39837; T39837.
DR   RefSeq; NP_595972.2; NM_001021880.3.
DR   AlphaFoldDB; O42954; -.
DR   SMR; O42954; -.
DR   BioGRID; 277168; 56.
DR   STRING; 4896.SPBC19G7.06.1; -.
DR   iPTMnet; O42954; -.
DR   SwissPalm; O42954; -.
DR   MaxQB; O42954; -.
DR   PaxDb; O42954; -.
DR   PRIDE; O42954; -.
DR   EnsemblFungi; SPBC19G7.06.1; SPBC19G7.06.1:pep; SPBC19G7.06.
DR   PomBase; SPBC19G7.06; mbx1.
DR   VEuPathDB; FungiDB:SPBC19G7.06; -.
DR   eggNOG; KOG0014; Eukaryota.
DR   HOGENOM; CLU_598731_0_0_1; -.
DR   InParanoid; O42954; -.
DR   OMA; KNACHVY; -.
DR   PRO; PR:O42954; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0097221; C:M/G1 phase-specific MADS box-forkhead transcription factor 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; IDA:PomBase.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00266; MADS_SRF_like; 1.
DR   Gene3D; 3.40.1810.10; -; 1.
DR   InterPro; IPR033897; MADS_SRF-like.
DR   InterPro; IPR002100; TF_MADSbox.
DR   InterPro; IPR036879; TF_MADSbox_sf.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; SSF55455; 1.
DR   PROSITE; PS00350; MADS_BOX_1; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Cell cycle; Cell division; DNA-binding; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..457
FT                   /note="MADS-box transcription factor 1"
FT                   /id="PRO_0000199443"
FT   DOMAIN          11..71
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT   REGION          195..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          295..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         372
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   457 AA;  50907 MW;  23466BEE2DC2A3CC CRC64;
     MDINPPPSTA PSSPRRSIQR ISDAKNKALT FNRRRLGLIK KAHELSVLCD AKVVVMIFDS
     KNACHVYSSE EPEEQRDALL QKFLNKDFVT VDPLRNINPN IPSDESLHNW RPKDKRIASV
     TTYSAQPSNN CSSATDSEND FQSFTIKSST TYHTTPTTAS ENKKIESITI PDHASVYNDL
     PLSPTVKHSF VSPVSGDYSD SPLEPSSSSS FSVPPESLNP TLSFQHNDVP QTDNFIPFLT
     PKRQAYGQSS SRADRSSVRR SQSFKNRRNG KPRISRLHTS HASIDGLTDF IQSPSSGYLD
     PSSTPITPLD SAINQITPPF LPDNLGQENR GELYSHDNPT SMVYEHPKFD ELPNGFIDTH
     ELNILSRSFT ASPNQILRES NMVNQDSFTD NPVDATWDAL IGTTQIDLDL DYERSSIPSS
     TIPADQLKDG VPTNSVYRNN MVDHNLYPSL NIERNAP