BUR1_YEAST
ID BUR1_YEAST Reviewed; 657 AA.
AC P23293; D6W4G2;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Serine/threonine-protein kinase BUR1;
DE EC=2.7.11.22 {ECO:0000269|PubMed:11390638, ECO:0000305|PubMed:10982824};
DE EC=2.7.11.23 {ECO:0000269|PubMed:11390638};
DE AltName: Full=Bypass UAS requirement protein 1;
DE AltName: Full=Suppressor of GPA1-Vall50 mutation protein 1;
GN Name=SGV1; Synonyms=BUR1; OrderedLocusNames=YPR161C; ORFNames=P9584.8;
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], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1828190; DOI=10.1016/0092-8674(91)90386-d;
RA Irie K., Nomoto S., Miyajima I., Matsumoto K.;
RT "SGV1 encodes a CDC28/cdc2-related kinase required for a G alpha subunit-
RT mediated adaptive response to pheromone in S. cerevisiae.";
RL Cell 65:785-795(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7871892; DOI=10.1002/yea.320101117;
RA Roemer T.D., Fortin N., Bussey H.;
RT "DNA sequence analysis of a 10.4 kbp region on the right arm of yeast
RT chromosome XVI positions GPH1 and SGV1 adjacent to KRE6, and identifies two
RT novel tRNA genes.";
RL Yeast 10:1527-1530(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
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 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 [6]
RP INTERACTION WITH BUR2, FUNCTION, AND CATALYTIC ACTIVITY.
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 [7]
RP INTERACTION WITH RBP1, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11390638; DOI=10.1128/mcb.21.13.4089-4096.2001;
RA Murray S., Udupa R., Yao S., Hartzog G., Prelich G.;
RT "Phosphorylation of the RNA polymerase II carboxy-terminal domain by the
RT Bur1 cyclin-dependent kinase.";
RL Mol. Cell. Biol. 21:4089-4096(2001).
RN [8]
RP PHOSPHORYLATION AT THR-240, MUTAGENESIS OF THR-240, AND FUNCTION.
RX PubMed=12215532; DOI=10.1128/mcb.22.19.6750-6758.2002;
RA Yao S., Prelich G.;
RT "Activation of the Bur1-Bur2 cyclin-dependent kinase complex by Cak1.";
RL Mol. Cell. Biol. 22:6750-6758(2002).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF GLU-107; ASP-213 AND THR-240.
RX PubMed=12972617; DOI=10.1128/mcb.23.19.7005-7018.2003;
RA Keogh M.-C., Podolny V., Buratowski S.;
RT "Bur1 kinase is required for efficient transcription elongation by RNA
RT polymerase II.";
RL Mol. Cell. Biol. 23:7005-7018(2003).
RN [10]
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 [11]
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 [12]
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 [13]
RP FUNCTION IN PHOSPHORYLATION OF UBC2.
RX PubMed=16307922; DOI=10.1016/j.molcel.2005.09.010;
RA Wood A., Schneider J., Dover J., Johnston M., Shilatifard A.;
RT "The Bur1/Bur2 complex is required for histone H2B monoubiquitination by
RT Rad6/Bre1 and histone methylation by COMPASS.";
RL Mol. Cell 20:589-599(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400 AND THR-405, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-634, AND
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND IDENTIFICATION BY
RP 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: Serine/threonine-protein kinase component of the BUR kinase
CC complex involved in transcription regulation. This complex
CC phosphorylates 'Ser-120' of the UBC2/RAD6 ubiquitin-conjugating enzyme
CC (E2), leading to monoubiquitination of histone H2B, the localization of
CC the PAF1 complex to the chromatin, and the silencing of telomeric-
CC associated genes. Also required for histone H3 'Lys-4' trimethylation.
CC May phosphorylate the 'Ser-5' of the RBP1 carboxy-terminal domain (CTD)
CC repeats. Necessary for the recovery from pheromone-induced growth
CC arrest in the cell cycle G1 phase. The kinase activity of the complex
CC requires the presence of BUR2. {ECO:0000269|PubMed:10982824,
CC ECO:0000269|PubMed:11390638, ECO:0000269|PubMed:12215532,
CC ECO:0000269|PubMed:12972617, ECO:0000269|PubMed:16040246,
CC ECO:0000269|PubMed:16307922, ECO:0000269|PubMed:1828190,
CC ECO:0000269|PubMed:8293972}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22;
CC Evidence={ECO:0000269|PubMed:11390638, ECO:0000305|PubMed:10982824};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000305|PubMed:10982824, ECO:0000305|PubMed:11390638};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.22; Evidence={ECO:0000305|PubMed:10982824};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:10982824};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
CC Evidence={ECO:0000269|PubMed:11390638};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10217;
CC Evidence={ECO:0000305|PubMed:11390638};
CC -!- SUBUNIT: Belongs to the BUR kinase complex composed of SGV1/BUR1 and
CC BUR2. Interacts with BUR2 and RBP1. {ECO:0000269|PubMed:10982824,
CC ECO:0000269|PubMed:11390638}.
CC -!- INTERACTION:
CC P23293; Q05949: BUR2; NbExp=6; IntAct=EBI-17078, EBI-30948;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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; D90317; BAA14347.1; -; Genomic_DNA.
DR EMBL; L33835; AAB59314.1; -; Genomic_DNA.
DR EMBL; U28371; AAB68058.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11578.1; -; Genomic_DNA.
DR PIR; A39526; A39526.
DR RefSeq; NP_015487.1; NM_001184258.1.
DR AlphaFoldDB; P23293; -.
DR SMR; P23293; -.
DR BioGRID; 36334; 1135.
DR ComplexPortal; CPX-1685; BUR1-BUR2 kinase complex.
DR DIP; DIP-5916N; -.
DR IntAct; P23293; 15.
DR MINT; P23293; -.
DR STRING; 4932.YPR161C; -.
DR iPTMnet; P23293; -.
DR MaxQB; P23293; -.
DR PaxDb; P23293; -.
DR PRIDE; P23293; -.
DR EnsemblFungi; YPR161C_mRNA; YPR161C; YPR161C.
DR GeneID; 856290; -.
DR KEGG; sce:YPR161C; -.
DR SGD; S000006365; SGV1.
DR VEuPathDB; FungiDB:YPR161C; -.
DR eggNOG; KOG0600; Eukaryota.
DR GeneTree; ENSGT00940000155373; -.
DR HOGENOM; CLU_000288_167_0_1; -.
DR InParanoid; P23293; -.
DR OMA; HGWIDCL; -.
DR BioCyc; YEAST:G3O-34290-MON; -.
DR BRENDA; 2.7.11.22; 984.
DR BRENDA; 2.7.11.23; 984.
DR PRO; PR:P23293; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P23293; 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; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IDA:SGD.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
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; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..657
FT /note="Serine/threonine-protein kinase BUR1"
FT /id="PRO_0000085687"
FT DOMAIN 60..366
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 414..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 630..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 66..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 240
FT /note="Phosphothreonine; by CAK"
FT /evidence="ECO:0000269|PubMed:12215532"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 405
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 107
FT /note="E->Q: Loss of kinase activity in vitro."
FT /evidence="ECO:0000269|PubMed:12972617"
FT MUTAGEN 213
FT /note="D->N: Loss of kinase activity in vitro."
FT /evidence="ECO:0000269|PubMed:12972617"
FT MUTAGEN 240
FT /note="T->A,D,E: No phosphorylation of SGV1."
FT /evidence="ECO:0000269|PubMed:12215532,
FT ECO:0000269|PubMed:12972617"
SQ SEQUENCE 657 AA; 74239 MW; CC9034A4B10A510E CRC64;
MSDNGSPAVL PKTEFNKYKI GKVKSTPAIQ RDAKTNLTYI KLRKRSSEKV YGCTVFQNHY
REDEKLGQGT FGEVYKGIHL ETQRQVAMKK IIVSVEKDLF PITAQREITI LKRLNHKNII
KLIEMVYDHS PDITNAASSN LHKSFYMILP YMVADLSGVL HNPRINLEMC DIKNMMLQIL
EGLNYIHCAK FMHRDIKTAN ILIDHNGVLK LADFGLARLY YGCPPNLKYP GGAGSGAKYT
SVVVTRWYRA PELVLGDKQY TTAVDIWGVG CVFAEFFEKK PILQGKTDID QGHVIFKLLG
TPTEEDWAVA RYLPGAELTT TNYKPTLRER FGKYLSETGL DFLGQLLALD PYKRLTAMSA
KHHPWFKEDP LPSEKITLPT EESHEADIKR YKEEMHQSLS QRVPTAPRGH IVEKGESPVV
KNLGAIPRGP KKDDASFLPP SKNVLAKPPP SKIRELHQNP RPYHVNSGYA KTAIPPPAAP
AGVNRYGPNN SSRNNRFSGN STAPNNSRNP VNRFHPETNV SSKYNKVPLP LGPQSRYQGN
SNESRYKNSP NDSRYHNPRY VNKPETNFNR QPQKYSRQES NAPINKNYNP SNGSRNMAGD
HHQGSRPSHP QFPISPSQGQ HQLTSKPIEK KNGSFKDERA KPDESKEFQN SDIADLY
