BUR2_YEAST
ID BUR2_YEAST Reviewed; 395 AA.
AC Q05949; D6VYM6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein BUR2;
DE AltName: Full=Bypass UAS requirement protein 2;
DE AltName: Full=Chromosome stability protein 4;
GN Name=BUR2; Synonyms=CST4; OrderedLocusNames=YLR226W;
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 [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 [2]
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 [3]
RP FUNCTION.
RX PubMed=8293972; DOI=10.1093/genetics/135.3.665;
RA Prelich G., Winston F.;
RT "Mutations that suppress the deletion of an upstream activating sequence in
RT yeast: involvement of a protein kinase and histone H3 in repressing
RT transcription in vivo.";
RL Genetics 135:665-676(1993).
RN [4]
RP GENE NAME.
RX PubMed=10454593; DOI=10.1093/nar/27.15.3001;
RA Ouspenski I.I., Elledge S.J., Brinkley B.R.;
RT "New yeast genes important for chromosome integrity and segregation
RT identified by dosage effects on genome stability.";
RL Nucleic Acids Res. 27:3001-3008(1999).
RN [5]
RP INTERACTION WITH BUR1, AND FUNCTION.
RX PubMed=10982824; DOI=10.1128/mcb.20.19.7080-7087.2000;
RA Yao S., Neiman A., Prelich G.;
RT "BUR1 and BUR2 encode a divergent cyclin-dependent kinase-cyclin complex
RT important for transcription in vivo.";
RL Mol. Cell. Biol. 20:7080-7087(2000).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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 [8]
RP FUNCTION.
RX PubMed=16040246; DOI=10.1016/j.cub.2005.07.028;
RA Laribee R.N., Krogan N.J., Xiao T., Shibata Y., Hughes T.R.,
RA Greenblatt J.F., Strahl B.D.;
RT "BUR kinase selectively regulates H3 K4 trimethylation and H2B
RT ubiquitylation through recruitment of the PAF elongation complex.";
RL Curr. Biol. 15:1487-1493(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, 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: Component of the BUR kinase complex involved in transcription
CC regulation. This complex phosphorylates 'Ser-120' of the UBC2/RAD6
CC ubiquitin-conjugating enzyme (E2), leading to monoubiquitination of
CC histone H2B, the localization of the PAF1 complex to the chromatin, and
CC the silencing of telomeric-associated genes. Also required for histone
CC H3 'Lys-4' trimethylation. May phosphorylate the 'Ser-5' of the RBP1
CC carboxy-terminal domain (CTD) repeats. Necessary for the recovery from
CC pheromone-induced growth arrest in the cell cycle G1 phase. Also
CC required for vegetative growth itself. The kinase activity of the
CC complex requires the presence of BUR2. Overexpression of BUR2
CC interferes with mitotic chromosome segregation.
CC {ECO:0000269|PubMed:10982824, ECO:0000269|PubMed:16040246,
CC ECO:0000269|PubMed:8293972}.
CC -!- SUBUNIT: Belongs to the BUR kinase complex composed of SGV1/BUR1 and
CC BUR2. Interacts with SGV1. {ECO:0000269|PubMed:10982824}.
CC -!- INTERACTION:
CC Q05949; P23293: SGV1; NbExp=6; IntAct=EBI-30948, EBI-17078;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2910 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U19027; AAB67407.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09542.1; -; Genomic_DNA.
DR PIR; S51449; S51449.
DR RefSeq; NP_013327.1; NM_001182113.1.
DR AlphaFoldDB; Q05949; -.
DR SMR; Q05949; -.
DR BioGRID; 31493; 65.
DR ComplexPortal; CPX-1685; BUR1-BUR2 kinase complex.
DR DIP; DIP-4787N; -.
DR IntAct; Q05949; 5.
DR MINT; Q05949; -.
DR STRING; 4932.YLR226W; -.
DR iPTMnet; Q05949; -.
DR MaxQB; Q05949; -.
DR PaxDb; Q05949; -.
DR PRIDE; Q05949; -.
DR EnsemblFungi; YLR226W_mRNA; YLR226W; YLR226W.
DR GeneID; 850923; -.
DR KEGG; sce:YLR226W; -.
DR SGD; S000004216; BUR2.
DR VEuPathDB; FungiDB:YLR226W; -.
DR eggNOG; ENOG502QQE8; Eukaryota.
DR HOGENOM; CLU_698596_0_0_1; -.
DR InParanoid; Q05949; -.
DR OMA; LFFRYWY; -.
DR BioCyc; YEAST:G3O-32340-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR PRO; PR:Q05949; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q05949; protein.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:SGD.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IMP:SGD.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IMP:SGD.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IBA:GO_Central.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:SGD.
DR GO; GO:0033184; P:positive regulation of histone ubiquitination; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:ComplexPortal.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..395
FT /note="Protein BUR2"
FT /id="PRO_0000076186"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 395 AA; 45721 MW; B317A7B429030FDF CRC64;
MSATSSSGDV KKFQAVPKPT SNASPPPASS GFNARTLWPD LIETPENQWV FECKDIIEKI
GTNGPIAVEI KKNMEKCLMY FYTLKKKLNL FDHTYTASCI LFYRYWFIYG IPTAITECIH
ISQGILVTAC KTMENNRPIE AYIKATCEFL MQNIPSLKSR TNIDKLKWEF RDKLVTNEKK
ILCLFGFDLN ISNPKELIEE VFSGYYRFNR DHNLPENFKK AFPKILQESR NFMVQAVTQP
VSLLCDGYTF IVLSLIYCGL EYKKLVDKDF RYPKNFFKDR FPIEVTPENF ANIFTDYKLL
EENFFNLKSN KGAKLQIDSS MIDSVIDESG DVENEVSEIS DPFNYELIKS GEVKEEFLNH
IETRVKDLLD KAKQESMKRK AKDPIRTPDA KKPKI
