BRE2_YEAST
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 03-AUG-2022, entry version 168.
DE RecName: Full=COMPASS component BRE2;
DE AltName: Full=Brefeldin-A sensitivity protein 2;
DE AltName: Full=Complex proteins associated with SET1 protein BRE2;
DE AltName: Full=Set1C component BRE2;
GN Name=BRE2; Synonyms=CPS60; 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 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 [7]
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 [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-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).
CC -!- FUNCTION: The COMPASS (Set1C) complex specifically mono-, di- and
CC trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays
CC a role in telomere length maintenance and transcription elongation
CC regulation. {ECO:0000269|PubMed:11742990, ECO:0000269|PubMed:11805083}.
CC -!- SUBUNIT: Component of the COMPASS (Set1C) complex which consists of
CC SET1(2), BRE2(2), SPP1(2), SDC1(1), SHG1(1), SWD1(1), SWD2(1), and
CC SWD3(1). {ECO:0000269|PubMed:11687631, ECO:0000269|PubMed:11742990}.
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 -!- MISCELLANEOUS: Present with 1310 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; 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 SMR; P43132; -.
DR BioGRID; 31289; 486.
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; P43132; -.
DR PRIDE; P43132; -.
DR EnsemblFungi; YLR015W_mRNA; YLR015W; YLR015W.
DR GeneID; 850702; -.
DR KEGG; sce:YLR015W; -.
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; CAREGSY; -.
DR BioCyc; YEAST:G3O-32176-MON; -.
DR Reactome; R-SCE-3214841; PKMTs methylate histone lysines.
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; IC: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:0051568; P:histone H3-K4 methylation; IDA:SGD.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:SGD.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IMP:SGD.
DR GO; GO:0000723; P:telomere maintenance; IMP:SGD.
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; PTHR10598; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 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 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 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
