ID   BRE2_YEAST              Reviewed;         505 AA.
AC   P43132; D6VY17; E9PA88;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=COMPASS component BRE2 {ECO:0000303|PubMed:11742990};
DE   AltName: Full=Brefeldin-A sensitivity protein 2 {ECO:0000303|PubMed:11169758};
DE   AltName: Full=COMPASS protein 60 {ECO:0000303|PubMed:11687631};
DE   AltName: Full=Complex proteins associated with SET1 protein BRE2 {ECO:0000303|PubMed:11742990};
DE   AltName: Full=Set1C component BRE2 {ECO:0000303|PubMed:11742990};
GN   Name=BRE2 {ECO:0000303|PubMed:11169758};
GN   Synonyms=CPS60 {ECO:0000303|PubMed:11687631};
GN   OrderedLocusNames=YLR015W;
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;
RA   Saville S.P., Atkinson S., Jamieson L., Pocklington M.J., Orr E.;
RT   "A 7.8kb fragment from chromosome XII of Saccharomyces cerevisiae does not
RT   harbour PKC2.";
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-472.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7874498; DOI=10.1016/s0960-9822(00)00223-2;
RA   Levin D.E., Stevenson W.D., Watanabe M.;
RT   "Evidence against the existence of the purported Saccharomyces cerevisiae
RT   PKC2 gene.";
RL   Curr. Biol. 4:990-995(1994).
RN   [5]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=11742990; DOI=10.1093/emboj/20.24.7137;
RA   Roguev A., Schaft D., Shevchenko A., Pijnappel W.W.M.P., Wilm M.,
RA   Aasland R., Stewart A.F.;
RT   "The Saccharomyces cerevisiae Set1 complex includes an Ash2 homologue and
RT   methylates histone 3 lysine 4.";
RL   EMBO J. 20:7137-7148(2001).
RN   [6]
RP   SUBUNIT.
RX   PubMed=11687631; DOI=10.1073/pnas.231473398;
RA   Miller T., Krogan N.J., Dover J., Erdjument-Bromage H., Tempst P.,
RA   Johnston M., Greenblatt J.F., Shilatifard A.;
RT   "COMPASS: a complex of proteins associated with a trithorax-related SET
RT   domain protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12902-12907(2001).
RN   [7]
RP   IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11169758;
RX   DOI=10.1002/1097-0061(20010130)18:2<163::aid-yea659>3.0.co;2-#;
RA   Muren E., Oeyen M., Barmark G., Ronne H.;
RT   "Identification of yeast deletion strains that are hypersensitive to
RT   brefeldin A or monensin, two drugs that affect intracellular transport.";
RL   Yeast 18:163-172(2001).
RN   [8]
RP   FUNCTION.
RX   PubMed=11805083; DOI=10.1074/jbc.c200023200;
RA   Krogan N.J., Dover J., Khorrami S., Greenblatt J.F., Schneider J.,
RA   Johnston M., Shilatifard A.;
RT   "COMPASS, a histone H3 (Lysine 4) methyltransferase required for telomeric
RT   silencing of gene expression.";
RL   J. Biol. Chem. 277:10753-10755(2002).
RN   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION BY
RP   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 IN THE SET1C/COMPASS COMPLEX.
RX   PubMed=29071121; DOI=10.1038/celldisc.2017.40;
RA   Luciano P., Jeon J., El-Kaoutari A., Challal D., Bonnet A., Barucco M.,
RA   Candelli T., Jourquin F., Lesage P., Kim J., Libri D., Geli V.;
RT   "Binding to RNA regulates Set1 function.";
RL   Cell Discov. 3:17040-17040(2017).
RN   [12] {ECO:0007744|PDB:4RT4}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 476-505, AND INTERACTION WITH
RP   SDC1.
RX   PubMed=25542209; DOI=10.1007/s13238-014-0127-z;
RA   Zhang H., Li M., Gao Y., Jia C., Pan X., Cao P., Zhao X., Zhang J.,
RA   Chang W.;
RT   "Structural implications of Dpy30 oligomerization for MLL/SET1 COMPASS H3K4
RT   trimethylation.";
RL   Protein Cell 6:147-151(2015).
RN   [13] {ECO:0007744|PDB:6BX3}
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS) OF 87-503 WITHIN THE CORE
RP   COMPASS COMPLEX, AND SUBUNIT.
RX   PubMed=30100186; DOI=10.1016/j.cell.2018.07.020;
RA   Qu Q., Takahashi Y.H., Yang Y., Hu H., Zhang Y., Brunzelle J.S.,
RA   Couture J.F., Shilatifard A., Skiniotis G.;
RT   "Structure and conformational dynamics of a COMPASS histone H3K4
RT   methyltransferase complex.";
RL   Cell 174:1117-1126(2018).
RN   [14] {ECO:0007744|PDB:6VEN}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS) WITHIN THE CORE COMPASS
RP   H2B-UBIQUITIN NUCLEOSOME COMPLEX, DNA-BINDING, AND FUNCTION.
RX   PubMed=31922488; DOI=10.7554/elife.53199;
RA   Worden E.J., Zhang X., Wolberger C.;
RT   "Structural basis for COMPASS recognition of an H2B-ubiquitinated
RT   nucleosome.";
RL   Elife 9:e53199-e53199(2020).
CC   -!- FUNCTION: Component of the Set1C/COMPASS complex that specifically
CC       mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which
CC       subsequently plays a role in telomere length maintenance and
CC       transcription elongation regulation (PubMed:11742990, PubMed:11805083).
CC       COMPASS recognizes ubiquitinated H2B on one face of the nucleosome
CC       which stimulates the methylation of H3 on the opposing face
CC       (PubMed:31922488). {ECO:0000269|PubMed:11742990,
CC       ECO:0000269|PubMed:11805083, ECO:0000269|PubMed:31922488}.
CC   -!- SUBUNIT: Component of the Set1C/COMPASS complex which consists of
CC       SET1(2), BRE2(2), SPP1(2), SDC1(1), SHG1(1), SWD1(1), SWD2(1), and
CC       SWD3(1) (PubMed:11742990, PubMed:11687631, PubMed:30100186,
CC       PubMed:31922488, PubMed:29071121). Interacts directly with SDC1
CC       (PubMed:25542209). {ECO:0000269|PubMed:11687631,
CC       ECO:0000269|PubMed:11742990, ECO:0000269|PubMed:25542209,
CC       ECO:0000269|PubMed:29071121, ECO:0000269|PubMed:30100186,
CC       ECO:0000269|PubMed:31922488}.
CC   -!- INTERACTION:
CC       P43132; Q03323: SDC1; NbExp=7; IntAct=EBI-27115, EBI-38307;
CC       P43132; P38827: SET1; NbExp=7; IntAct=EBI-27115, EBI-16977;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere
CC       {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to brefeldin A.
CC       {ECO:0000269|PubMed:11169758}.
CC   -!- MISCELLANEOUS: Present with 1310 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the cclA family. {ECO:0000305}.
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DR   EMBL; X90564; CAA62158.1; -; Genomic_DNA.
DR   EMBL; Z73187; CAA97537.1; -; Genomic_DNA.
DR   EMBL; L34405; AAA34835.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09333.1; -; Genomic_DNA.
DR   PIR; S64837; S64837.
DR   RefSeq; NP_013115.1; NM_001181902.1.
DR   PDB; 4RT4; X-ray; 2.00 A; E=476-505.
DR   PDB; 6BX3; EM; 4.30 A; K=87-503.
DR   PDB; 6VEN; EM; 3.37 A; O=1-505.
DR   PDBsum; 4RT4; -.
DR   PDBsum; 6BX3; -.
DR   PDBsum; 6VEN; -.
DR   AlphaFoldDB; P43132; -.
DR   EMDB; EMD-21157; -.
DR   EMDB; EMD-7303; -.
DR   SMR; P43132; -.
DR   BioGRID; 31289; 490.
DR   ComplexPortal; CPX-1039; COMPASS complex.
DR   DIP; DIP-1935N; -.
DR   IntAct; P43132; 11.
DR   MINT; P43132; -.
DR   STRING; 4932.YLR015W; -.
DR   iPTMnet; P43132; -.
DR   MaxQB; P43132; -.
DR   PaxDb; 4932-YLR015W; -.
DR   PeptideAtlas; P43132; -.
DR   EnsemblFungi; YLR015W_mRNA; YLR015W; YLR015W.
DR   GeneID; 850702; -.
DR   KEGG; sce:YLR015W; -.
DR   AGR; SGD:S000004005; -.
DR   SGD; S000004005; BRE2.
DR   VEuPathDB; FungiDB:YLR015W; -.
DR   eggNOG; KOG2626; Eukaryota.
DR   GeneTree; ENSGT00390000010474; -.
DR   HOGENOM; CLU_014420_4_1_1; -.
DR   InParanoid; P43132; -.
DR   OMA; NGFRYTY; -.
DR   OrthoDB; 5479497at2759; -.
DR   BioCyc; YEAST:G3O-32176-MONOMER; -.
DR   Reactome; R-SCE-9772755; Formation of WDR5-containing histone-modifying complexes.
DR   BioGRID-ORCS; 850702; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P43132; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P43132; Protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IPI:SGD.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; IMP:SGD.
DR   GO; GO:0000723; P:telomere maintenance; IMP:SGD.
DR   CDD; cd12872; SPRY_Ash2; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   InterPro; IPR037353; ASH2.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR003877; SPRY_dom.
DR   PANTHER; PTHR10598; SET1/ASH2 HISTONE METHYLTRANSFERASE COMPLEX SUBUNIT ASH2; 1.
DR   PANTHER; PTHR10598:SF0; SET1_ASH2 HISTONE METHYLTRANSFERASE COMPLEX SUBUNIT ASH2; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromosome; Nucleus; Phosphoprotein; Reference proteome;
KW   Telomere.
FT   CHAIN           1..505
FT                   /note="COMPASS component BRE2"
FT                   /id="PRO_0000064987"
FT   DOMAIN          70..295
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   REGION          271..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         318
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000303|PubMed:31922488,
FT                   ECO:0007744|PDB:6VEN"
FT   MOD_RES         227
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   STRAND          64..71
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          76..78
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          80..82
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          92..97
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          120..126
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          130..138
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          182..187
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          199..209
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          213..215
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          218..220
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          234..241
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   HELIX           244..260
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   HELIX           293..298
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          313..317
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          320..326
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          354..359
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          362..370
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   HELIX           385..391
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          435..442
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          448..451
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   HELIX           454..456
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   STRAND          458..461
FT                   /evidence="ECO:0007829|PDB:6VEN"
FT   HELIX           483..500
FT                   /evidence="ECO:0007829|PDB:4RT4"
SQ   SEQUENCE   505 AA;  58347 MW;  D5B33221E9F10379 CRC64;
     MKLGIIPYQE GTDIVYKNAL QGQQEGKRPN LPQMEATHQI KSSVQGTSYE FVRTEDIPLN
     RRHFVYRPCS ANPFFTILGY GCTEYPFDHS GMSVMDRSEG LSISRDGNDL VSVPDQYGWR
     TARSDVCIKE GMTYWEVEVI RGGNKKFADG VNNKENADDS VDEVQSGIYE KMHKQVNDTP
     HLRFGVCRRE ASLEAPVGFD VYGYGIRDIS LESIHEGKLN CVLENGSPLK EGDKIGFLLS
     LPSIHTQIKQ AKEFTKRRIF ALNSHMDTMN EPWREDAENG PSRKKLKQET TNKEFQRALL
     EDIEYNDVVR DQIAIRYKNQ LFFEATDYVK TTKPEYYSSD KRERQDYYQL EDSYLAIFQN
     GKYLGKAFEN LKPLLPPFSE LQYNEKFYLG YWQHGEARDE SNDKNTTSAK KKKQQQKKKK
     GLILRNKYVN NNKLGYYPTI SCFNGGTARI ISEEDKLEYL DQIRSAYCVD GNSKVNTLDT
     LYKEQIAEDI VWDIIDELEQ IALQQ
//