ID   REB1_YEAST              Reviewed;         810 AA.
AC   P21538; D6VQ49;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 2.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=DNA-binding protein REB1;
DE   AltName: Full=QBP;
GN   Name=REB1; Synonyms=GRF2; OrderedLocusNames=YBR049C; ORFNames=YBR0502;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=2204808; DOI=10.1128/mcb.10.10.5226-5234.1990;
RA   Ju Q., Morrow B.E., Warner J.R.;
RT   "REB1, a yeast DNA-binding protein with many targets, is essential for
RT   growth and bears some resemblance to the oncogene myb.";
RL   Mol. Cell. Biol. 10:5226-5234(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7597852; DOI=10.1002/yea.320110511;
RA   Aljinovic G., Pohl T.M.;
RT   "Sequence and analysis of 24 kb on chromosome II of Saccharomyces
RT   cerevisiae.";
RL   Yeast 11:475-479(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-807, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=EJY251-11b;
RX   PubMed=15542864; DOI=10.1074/mcp.m400154-mcp200;
RA   Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D.,
RA   Gygi S.P.;
RT   "A proteomic strategy for gaining insights into protein sumoylation in
RT   yeast.";
RL   Mol. Cell. Proteomics 4:246-254(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=11258704; DOI=10.1093/embo-reports/kve024;
RA   Fourel G., Boscheron C., Revardel E., Lebrun E., Hu Y.-F., Simmen K.C.,
RA   Mueller K., Li R., Mermod N., Gilson E.;
RT   "An activation-independent role of transcription factors in insulator
RT   function.";
RL   EMBO Rep. 2:124-132(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=12200417; DOI=10.1074/jbc.m202578200;
RA   Fourel G., Miyake T., Defossez P.-A., Li R., Gilson E.;
RT   "General regulatory factors (GRFs) as genome partitioners.";
RL   J. Biol. Chem. 277:41736-41743(2002).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: DNA-binding protein that recognizes sites within both the
CC       enhancer and the promoter of rRNA transcription, as well as upstream of
CC       many genes transcribed by RNA polymerase II. It is essential for cell
CC       growth. May stimulate or inhibit transcription. Specifically recognizes
CC       the sequence 5'-CCGGGTA-3' or 5'-CGGGTRR-3' (where R is any purine). A
CC       member of the general regulatory factors (GRFs) which act as genome
CC       partitioners. Acts as a chromatin insulator which are known as STARs
CC       (Subtelomeric anti-silencing region). STARs prevent negative or
CC       positive transcription influence by extending across chromatin to a
CC       promoter. {ECO:0000269|PubMed:11258704, ECO:0000269|PubMed:12200417}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 7510 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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; M58728; AAA34963.1; -; Genomic_DNA.
DR   EMBL; Z35918; CAA84992.1; -; Genomic_DNA.
DR   EMBL; Z46260; CAA86391.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07169.1; -; Genomic_DNA.
DR   PIR; S45907; S45907.
DR   RefSeq; NP_009605.1; NM_001178397.1.
DR   AlphaFoldDB; P21538; -.
DR   BioGRID; 32751; 639.
DR   DIP; DIP-6374N; -.
DR   IntAct; P21538; 33.
DR   MINT; P21538; -.
DR   STRING; 4932.YBR049C; -.
DR   iPTMnet; P21538; -.
DR   MaxQB; P21538; -.
DR   PaxDb; 4932-YBR049C; -.
DR   PeptideAtlas; P21538; -.
DR   EnsemblFungi; YBR049C_mRNA; YBR049C; YBR049C.
DR   GeneID; 852338; -.
DR   KEGG; sce:YBR049C; -.
DR   AGR; SGD:S000000253; -.
DR   SGD; S000000253; REB1.
DR   VEuPathDB; FungiDB:YBR049C; -.
DR   eggNOG; KOG0051; Eukaryota.
DR   GeneTree; ENSGT00940000176744; -.
DR   HOGENOM; CLU_016706_0_0_1; -.
DR   InParanoid; P21538; -.
DR   OMA; HVRRKYH; -.
DR   OrthoDB; 48176at2759; -.
DR   BioCyc; YEAST:G3O-29021-MONOMER; -.
DR   BioGRID-ORCS; 852338; 4 hits in 13 CRISPR screens.
DR   PRO; PR:P21538; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P21538; Protein.
DR   GO; GO:0000785; C:chromatin; IC:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006363; P:termination of RNA polymerase I transcription; TAS:SGD.
DR   GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:SGD.
DR   GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; IDA:SGD.
DR   CDD; cd00167; SANT; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR049260; REB1_MybAD.
DR   InterPro; IPR001005; SANT/Myb.
DR   PANTHER; PTHR46380; CYCLIN-D-BINDING MYB-LIKE TRANSCRIPTION FACTOR 1; 1.
DR   PANTHER; PTHR46380:SF2; CYCLIN-D-BINDING MYB-LIKE TRANSCRIPTION FACTOR 1; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   Pfam; PF21559; Reb1_MybAD; 1.
DR   SMART; SM00717; SANT; 4.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   PROSITE; PS51294; HTH_MYB; 1.
DR   PROSITE; PS50090; MYB_LIKE; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..810
FT                   /note="DNA-binding protein REB1"
FT                   /id="PRO_0000197089"
FT   DOMAIN          470..523
FT                   /note="HTH myb-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   DOMAIN          692..717
FT                   /note="Myb-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT   DNA_BIND        497..519
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..160
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..224
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..666
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         355
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950"
FT   CROSSLNK        807
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000269|PubMed:15542864"
FT   CONFLICT        56
FT                   /note="S -> N (in Ref. 1; AAA34963)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        592..618
FT                   /note="AAAAIQEQQQLLQQKQQDDDDAIAAAA -> RAVVFKNNNNFFNKSSKMMTM
FT                   LLRSC (in Ref. 1; AAA34963)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        627
FT                   /note="D -> E (in Ref. 1; AAA34963)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        636
FT                   /note="D -> E (in Ref. 1; AAA34963)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   810 AA;  91874 MW;  318EB17D20D004B6 CRC64;
     MPSGHNDKNA NQESVEEAVL KYVGVGLDHQ NHDPQLHTKD LENKHSKKQN IVESSSDVDV
     NNNDDSNRNE DNNDDSENIS ALNANESSSN VDHANSNEQH NAVMDWYLRQ TAHNQQDDED
     DENNNNTDNG NDSNNHFSQS DIVVDDDDDK NKKDAGVGVD DDHQSMAMAA VAAAYTLSKN
     NNNNNSIAND SNSRKRQHDN GNNHENSQKK RKNNNDDDDR QIGNVDPELT TLGDADDNDT
     NNDVIDRDQL VHKAIIDADS ITQHPDFQQY LNTAADTDDN EKLKHIKDHL MRTHGLNHQN
     KNHNDDTDDL SNSTKQYSEL QKDSMLDSSL NKSRNYMEVL PKVISQDTQP HQQKSPSHDN
     EAGSVDNSEI SQLLQSAATK ASSLVSLSSS SATPSTSRSN NSKAFDKAED AALERFINEY
     EAIERLTRQQ VCERIWSSDR PKDNFWNNIY KVLPYRSSSS IYKHMRRKYH IFEQRGKWTA
     EEEQELAKLC AEKEGQWAEI GKTLGRMPED CRDRWRNYVK CGTNRASNRW SVEEEELLKK
     VISDMLEEAQ QQQSQLHPNL LEEEQHLLQD DQNDHRNNDE DDDDTASAAA AAAAAIQEQQ
     QLLQQKQQDD DDAIAAAAAA ASSSLGDNKD EDKPHDSLGI QLDDNSQNSM VPAPSATSTH
     SKSLSNTIRR HNNKLRKSLM GNGKLDFKDI INWTIVSERM GGTRSRIQCR YKWNKLVKRE
     AIAKIQTVKD DDMLWIFEKL RDLGITEDSQ VDWDELAALK PGMKLNGLEL KLCYERMKKK
     VKGYKQKSIN EISKELVDYF SSNISMKTEN
//