Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23293 (BUR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase BUR1

EC=2.7.11.22
EC=2.7.11.23
Alternative name(s):
Bypass UAS requirement protein 1
Suppressor of GPA1-Vall50 mutation protein 1
Gene names
Name:SGV1
Synonyms:BUR1
Ordered Locus Names:YPR161C
ORF Names:P9584.8
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length657 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.13

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.

Subunit structure

Belongs to the BUR kinase complex composed of SGV1/BUR1 and BUR2. Interacts with BUR2 and RBP1. Ref.6 Ref.7

Subcellular location

Nucleus Ref.10.

Miscellaneous

Present with 2070 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BUR2Q059496EBI-17078,EBI-30948

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 657657Serine/threonine-protein kinase BUR1
PRO_0000085687

Regions

Domain60 – 366307Protein kinase
Nucleotide binding66 – 749ATP By similarity

Sites

Active site1951Proton acceptor By similarity
Binding site891ATP By similarity

Amino acid modifications

Modified residue2401Phosphothreonine; by CAK Ref.8
Modified residue4001Phosphoserine Ref.16
Modified residue4051Phosphothreonine Ref.16
Modified residue4171Phosphoserine Ref.15 Ref.17 Ref.18
Modified residue6341Phosphoserine Ref.17

Experimental info

Mutagenesis1071E → Q: Loss of kinase activity in vitro. Ref.9
Mutagenesis2131D → N: Loss of kinase activity in vitro. Ref.9
Mutagenesis2401T → A, D or E: No phosphorylation of SGV1. Ref.8 Ref.9

Sequences

Sequence LengthMass (Da)Tools
P23293 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: CC9034A4B10A510E

FASTA65774,239
        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 

« Hide

References

« Hide 'large scale' references
[1]"SGV1 encodes a CDC28/cdc2-related kinase required for a G alpha subunit-mediated adaptive response to pheromone in S. cerevisiae."
Irie K., Nomoto S., Miyajima I., Matsumoto K.
Cell 65:785-795(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: ATCC 204508 / S288c.
[2]"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."
Roemer T.D., Fortin N., Bussey H.
Yeast 10:1527-1530(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
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. expand/collapse author list , 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.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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."
Prelich G., Winston F.
Genetics 135:665-676(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"BUR1 and BUR2 encode a divergent cyclin-dependent kinase-cyclin complex important for transcription in vivo."
Yao S., Neiman A., Prelich G.
Mol. Cell. Biol. 20:7080-7087(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BUR2, FUNCTION.
[7]"Phosphorylation of the RNA polymerase II carboxy-terminal domain by the Bur1 cyclin-dependent kinase."
Murray S., Udupa R., Yao S., Hartzog G., Prelich G.
Mol. Cell. Biol. 21:4089-4096(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RBP1, FUNCTION.
[8]"Activation of the Bur1-Bur2 cyclin-dependent kinase complex by Cak1."
Yao S., Prelich G.
Mol. Cell. Biol. 22:6750-6758(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-240, MUTAGENESIS OF THR-240, FUNCTION.
[9]"Bur1 kinase is required for efficient transcription elongation by RNA polymerase II."
Keogh M.-C., Podolny V., Buratowski S.
Mol. Cell. Biol. 23:7005-7018(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLU-107; ASP-213 AND THR-240.
[10]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]"BUR kinase selectively regulates H3 K4 trimethylation and H2B ubiquitylation through recruitment of the PAF elongation complex."
Laribee R.N., Krogan N.J., Xiao T., Shibata Y., Hughes T.R., Greenblatt J.F., Strahl B.D.
Curr. Biol. 15:1487-1493(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"The Bur1/Bur2 complex is required for histone H2B monoubiquitination by Rad6/Bre1 and histone methylation by COMPASS."
Wood A., Schneider J., Dover J., Johnston M., Shilatifard A.
Mol. Cell 20:589-599(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF UBC2.
[14]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[15]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[16]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
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.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400 AND THR-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-634, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90317 Genomic DNA. Translation: BAA14347.1.
L33835 Genomic DNA. Translation: AAB59314.1.
U28371 Genomic DNA. Translation: AAB68058.1.
BK006949 Genomic DNA. Translation: DAA11578.1.
PIRA39526.
RefSeqNP_015487.1. NM_001184258.1.

3D structure databases

ProteinModelPortalP23293.
SMRP23293. Positions 31-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36334. 135 interactions.
DIPDIP-5916N.
IntActP23293. 14 interactions.
MINTMINT-668965.
STRING4932.YPR161C.

Proteomic databases

PaxDbP23293.
PeptideAtlasP23293.
PRIDEP23293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPR161C; YPR161C; YPR161C.
GeneID856290.
KEGGsce:YPR161C.

Organism-specific databases

CYGDYPR161c.
SGDS000006365. SGV1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000116084.
HOGENOMHOG000233024.
KOK15562.
OMAPRINLEM.
OrthoDBEOG7K3TWD.

Enzyme and pathway databases

BioCycYEAST:G3O-34290-MONOMER.
BRENDA2.7.11.22. 984.

Gene expression databases

GenevestigatorP23293.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio981629.
PROP23293.

Entry information

Entry nameBUR1_YEAST
AccessionPrimary (citable) accession number: P23293
Secondary accession number(s): D6W4G2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families