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UniProtKB/Swiss-Prot entry P23293


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BUR1_YEAST
Primary accession number P23293
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1991
Sequence was last modified on November 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 93)
Name and origin of the protein
Protein name Serine/threonine-protein kinase BUR1
Synonyms EC 2.7.11.22
EC 2.7.11.23
Bypass UAS requirement protein 1
Suppressor of GPA1-Vall50 mutation protein 1
Gene name
Name: SGV1
Synonyms: BUR1
OrderedLocusNames: YPR161C
ORFNames: P9584.8
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 204508 / S288c;
DOI=10.1016/0092-8674(91)90386-D; PubMed=1828190 [NCBI, ExPASy, EBI, Israel, Japan]
Irie K., Nomoto S., Miyajima I., Matsumoto K.;
"SGV1 encodes a CDC28/cdc2-related kinase required for a G alpha subunit-mediated adaptive response to pheromone in S. cerevisiae.";
Cell 65:785-795(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/yea.320101117; PubMed=7871892 [NCBI, ExPASy, EBI, Israel, Japan]
Roemer T.D., Fortin N., Bussey H.;
"DNA sequence analysis of a 10.4 kbp region on the right arm of yeast chromosome XVI positions GPH1 and SGV1 adjacent to KRE6, and identifies two novel tRNA genes.";
Yeast 10:1527-1530(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan]
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[4]
FUNCTION.
PubMed=8293972 [NCBI, ExPASy, EBI, Israel, Japan]
Prelich G., Winston F.;
"Mutations that suppress the deletion of an upstream activating sequence in yeast: involvement of a protein kinase and histone H3 in repressing transcription in vivo.";
Genetics 135:665-676(1993).
[5]
INTERACTION WITH BUR2, AND FUNCTION.
DOI=10.1128/MCB.20.19.7080-7087.2000; PubMed=10982824 [NCBI, ExPASy, EBI, Israel, Japan]
Yao S., Neiman A., Prelich G.;
"BUR1 and BUR2 encode a divergent cyclin-dependent kinase-cyclin complex important for transcription in vivo.";
Mol. Cell. Biol. 20:7080-7087(2000).
[6]
INTERACTION WITH RBP1, AND FUNCTION.
DOI=10.1128/MCB.21.13.4089-4096.2001; PubMed=11390638 [NCBI, ExPASy, EBI, Israel, Japan]
Murray S., Udupa R., Yao S., Hartzog G., Prelich G.;
"Phosphorylation of the RNA polymerase II carboxy-terminal domain by the Bur1 cyclin-dependent kinase.";
Mol. Cell. Biol. 21:4089-4096(2001).
[7]
PHOSPHORYLATION AT THR-240, MUTAGENESIS OF THR-240, AND FUNCTION.
DOI=10.1128/MCB.22.19.6750-6758.2002; PubMed=12215532 [NCBI, ExPASy, EBI, Israel, Japan]
Yao S., Prelich G.;
"Activation of the Bur1-Bur2 cyclin-dependent kinase complex by Cak1.";
Mol. Cell. Biol. 22:6750-6758(2002).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-240, AND MASS SPECTROMETRY.
DOI=10.1038/nbt0302-301; PubMed=11875433 [NCBI, ExPASy, EBI, Israel, Japan]
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.;
"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae.";
Nat. Biotechnol. 20:301-305(2002).
[9]
FUNCTION, AND MUTAGENESIS OF GLU-107; ASP-213 AND THR-240.
DOI=10.1128/MCB.23.19.7005-7018.2003; PubMed=12972617 [NCBI, ExPASy, EBI, Israel, Japan]
Keogh M.-C., Podolny V., Buratowski S.;
"Bur1 kinase is required for efficient transcription elongation by RNA polymerase II.";
Mol. Cell. Biol. 23:7005-7018(2003).
[10]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02026; PubMed=14562095 [NCBI, ExPASy, EBI, Israel, Japan]
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[11]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[12]
FUNCTION.
DOI=10.1016/j.cub.2005.07.028; PubMed=16040246 [NCBI, ExPASy, EBI, Israel, Japan]
Laribee R.N., Krogan N.J., Xiao T., Shibata Y., Hughes T.R., Greenblatt J.F., Strahl B.D.;
"BUR kinase selectively regulates H3 K4 trimethylation and H2B ubiquitylation through recruitment of the PAF elongation complex.";
Curr. Biol. 15:1487-1493(2005).
[13]
FUNCTION IN PHOSPHORYLATION OF UBC2.
DOI=10.1016/j.molcel.2005.09.010; PubMed=16307922 [NCBI, ExPASy, EBI, Israel, Japan]
Wood A., Schneider J., Dover J., Johnston M., Shilatifard A.;
"The Bur1/Bur2 complex is required for histone H2B monoubiquitination by Rad6/Bre1 and histone methylation by COMPASS.";
Mol. Cell 20:589-599(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M400219-MCP200; PubMed=15665377 [NCBI, ExPASy, EBI, Israel, Japan]
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400 AND THR-405, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0701622104; PubMed=17563356 [NCBI, ExPASy, EBI, Israel, Japan]
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases.";
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-240; SER-417 AND SER-634, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
Comments
  • FUNCTION: Serine/threonine-protein kinase component of the BUR kinase complex involved in transcription regulation. This complex phosphorylates 'Ser-120' of the UBC2/RAD6 ubiquitin-conjugating enzyme (E2), leading to monoubiquitination of histone H2B, the localization of the PAF1 complex to the chromatin, and the silencing of telomeric-associated genes. Also required for histone H3 'Lys-4' trimethylation. May phosphorylate the 'Ser-5' of the RBP1 carboxy-terminal domain (CTD) repeats. Necessary for the recovery from pheromone-induced growth arrest in the cell cycle G1 phase. The kinase activity of the complex requires the presence of BUR2.
  • CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
  • CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
  • SUBUNIT: Belongs to the BUR kinase complex composed of SGV1/BUR1 and BUR2. Interacts with BUR2 and RBP1.
  • INTERACTION:
    Q05949:BUR2; NbExp=2; IntAct=EBI-17078, EBI-30948;
  • SUBCELLULAR LOCATION: Nucleus.
  • MISCELLANEOUS: Present with 2070 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.
  • SIMILARITY: Contains 1 protein kinase domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D90317; BAA14347.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L33835; AAB59314.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U28371; AAB68058.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39526; A39526.
RefSeq NP_015487.1; -.
3D structure databases
HSSP Q00534; 1BI8. [HSSP ENTRY / PDB]
ModBase P23293.
Protein-protein interaction databases
DIP DIP:5916N; -.
IntAct P23293; -.
Organism-specific databases
CYGD YPR161c; -.
SGD S000006365; SGV1.
Yeast-GFP YPR161C.
Gene expression databases
ArrayExpress P23293; -.
GermOnline YPR161C; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0004693; Molecular function: cyclin-dependent protein kinase activity (inferred from electronic annotation from EC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008353; Molecular function: RNA polymerase subunit kinase activity (inferred from electronic annotation from EC).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0006350; Biological process: transcription (inferred from direct assay from SGD).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P23293.
Proteomic databases
PeptideAtlas P23293; -.
Genome annotation databases
Ensembl YPR161C; Saccharomyces cerevisiae. [Contig view]
GeneID 856290; -.
GenomeReviews U00094_GR; YPR161C.
KEGG sce:YPR161C; -.
NMPDR fig|4932.3.peg.6633; -.
Phylogenomic databases
HOGENOM P23293; -.
Other
LinkHub P23293; -.
NextBio 981629; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   657  657     Serine/threonine-protein kinase BUR1. PRO_0000085687
DOMAIN   60   366  307     Protein kinase. 
NP_BIND   66    74  9     ATP (By similarity). 
ACT_SITE   195   195        Proton acceptor (By similarity). 
BINDING   89    89        ATP (By similarity). 
MOD_RES   240   240        Phosphothreonine; by CAK. 
MOD_RES   241   241        Phosphoserine. 
MOD_RES   400   400        Phosphoserine. 
MOD_RES   405   405        Phosphothreonine. 
MOD_RES   417   417        Phosphoserine. 
MOD_RES   634   634        Phosphoserine. 
MUTAGEN   107   107        E->Q: Loss of kinase activity in vitro. 
MUTAGEN   213   213        D->N: Loss of kinase activity in vitro. 
MUTAGEN   240   240        T->A,D,E: No phosphorylation of SGV1. 
Sequence information
Length: 657 AA [This is the length of the unprocessed precursor] Molecular weight: 74239 Da [This is the MW of the unprocessed precursor] CRC64: CC9034A4B10A510E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSDNGSPAVL PKTEFNKYKI GKVKSTPAIQ RDAKTNLTYI KLRKRSSEKV YGCTVFQNHY 

        70         80         90        100        110        120 
REDEKLGQGT FGEVYKGIHL ETQRQVAMKK IIVSVEKDLF PITAQREITI LKRLNHKNII 

       130        140        150        160        170        180 
KLIEMVYDHS PDITNAASSN LHKSFYMILP YMVADLSGVL HNPRINLEMC DIKNMMLQIL 

       190        200        210        220        230        240 
EGLNYIHCAK FMHRDIKTAN ILIDHNGVLK LADFGLARLY YGCPPNLKYP GGAGSGAKYT 

       250        260        270        280        290        300 
SVVVTRWYRA PELVLGDKQY TTAVDIWGVG CVFAEFFEKK PILQGKTDID QGHVIFKLLG 

       310        320        330        340        350        360 
TPTEEDWAVA RYLPGAELTT TNYKPTLRER FGKYLSETGL DFLGQLLALD PYKRLTAMSA 

       370        380        390        400        410        420 
KHHPWFKEDP LPSEKITLPT EESHEADIKR YKEEMHQSLS QRVPTAPRGH IVEKGESPVV 

       430        440        450        460        470        480 
KNLGAIPRGP KKDDASFLPP SKNVLAKPPP SKIRELHQNP RPYHVNSGYA KTAIPPPAAP 

       490        500        510        520        530        540 
AGVNRYGPNN SSRNNRFSGN STAPNNSRNP VNRFHPETNV SSKYNKVPLP LGPQSRYQGN 

       550        560        570        580        590        600 
SNESRYKNSP NDSRYHNPRY VNKPETNFNR QPQKYSRQES NAPINKNYNP SNGSRNMAGD 

       610        620        630        640        650 
HHQGSRPSHP QFPISPSQGQ HQLTSKPIEK KNGSFKDERA KPDESKEFQN SDIADLY 

P23293 in FASTA format

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View entry in raw text format (no links)
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