REB1_YEAST
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 03-AUG-2022, entry version 192.
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}.
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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; 633.
DR DIP; DIP-6374N; -.
DR IntAct; P21538; 33.
DR MINT; P21538; -.
DR STRING; 4932.YBR049C; -.
DR iPTMnet; P21538; -.
DR MaxQB; P21538; -.
DR PaxDb; P21538; -.
DR PRIDE; P21538; -.
DR EnsemblFungi; YBR049C_mRNA; YBR049C; YBR049C.
DR GeneID; 852338; -.
DR KEGG; sce:YBR049C; -.
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 BioCyc; YEAST:G3O-29021-MON; -.
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:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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 InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR SMART; SM00717; SANT; 4.
DR SUPFAM; SSF46689; SSF46689; 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
