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P23293

- BUR1_YEAST

UniProt

P23293 - BUR1_YEAST

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Protein
Serine/threonine-protein kinase BUR1
Gene
SGV1, BUR1, YPR161C, P9584.8
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 BUR2.8 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891ATP By similarity
Active sitei195 – 1951Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi66 – 749ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. RNA polymerase II carboxy-terminal domain kinase activity Source: SGD
  3. cyclin-dependent protein serine/threonine kinase activity Source: SGD
  4. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. phosphorylation of RNA polymerase II C-terminal domain Source: SGD
  2. positive regulation of histone H3-K4 methylation Source: SGD
  3. protein phosphorylation Source: SGD
  4. transcription, DNA-templated Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34290-MONOMER.
BRENDAi2.7.11.22. 984.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:SGV1
Synonyms:BUR1
Ordered Locus Names:YPR161C
ORF Names:P9584.8
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

CYGDiYPR161c.
SGDiS000006365. SGV1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cyclin-dependent protein kinase holoenzyme complex Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi107 – 1071E → Q: Loss of kinase activity in vitro. 1 Publication
Mutagenesisi213 – 2131D → N: Loss of kinase activity in vitro. 1 Publication
Mutagenesisi240 – 2401T → A, D or E: No phosphorylation of SGV1. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 657657Serine/threonine-protein kinase BUR1
PRO_0000085687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei240 – 2401Phosphothreonine; by CAK1 Publication
Modified residuei400 – 4001Phosphoserine1 Publication
Modified residuei405 – 4051Phosphothreonine1 Publication
Modified residuei417 – 4171Phosphoserine3 Publications
Modified residuei634 – 6341Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP23293.
PaxDbiP23293.
PeptideAtlasiP23293.
PRIDEiP23293.

Expressioni

Gene expression databases

GenevestigatoriP23293.

Interactioni

Subunit structurei

Belongs to the BUR kinase complex composed of SGV1/BUR1 and BUR2. Interacts with BUR2 and RBP1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BUR2Q059496EBI-17078,EBI-30948

Protein-protein interaction databases

BioGridi36334. 135 interactions.
DIPiDIP-5916N.
IntActiP23293. 14 interactions.
MINTiMINT-668965.
STRINGi4932.YPR161C.

Structurei

3D structure databases

ProteinModelPortaliP23293.
SMRiP23293. Positions 27-374.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini60 – 366307Protein kinase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00740000116084.
HOGENOMiHOG000233024.
KOiK15562.
OMAiPRINLEM.
OrthoDBiEOG7K3TWD.

Family and domain databases

InterProiIPR011009. 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]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23293-1 [UniParc]FASTAAdd to Basket

« Hide

MSDNGSPAVL PKTEFNKYKI GKVKSTPAIQ RDAKTNLTYI KLRKRSSEKV    50
YGCTVFQNHY REDEKLGQGT FGEVYKGIHL ETQRQVAMKK IIVSVEKDLF 100
PITAQREITI LKRLNHKNII KLIEMVYDHS PDITNAASSN LHKSFYMILP 150
YMVADLSGVL HNPRINLEMC DIKNMMLQIL EGLNYIHCAK FMHRDIKTAN 200
ILIDHNGVLK LADFGLARLY YGCPPNLKYP GGAGSGAKYT SVVVTRWYRA 250
PELVLGDKQY TTAVDIWGVG CVFAEFFEKK PILQGKTDID QGHVIFKLLG 300
TPTEEDWAVA RYLPGAELTT TNYKPTLRER FGKYLSETGL DFLGQLLALD 350
PYKRLTAMSA KHHPWFKEDP LPSEKITLPT EESHEADIKR YKEEMHQSLS 400
QRVPTAPRGH IVEKGESPVV KNLGAIPRGP KKDDASFLPP SKNVLAKPPP 450
SKIRELHQNP RPYHVNSGYA KTAIPPPAAP AGVNRYGPNN SSRNNRFSGN 500
STAPNNSRNP VNRFHPETNV SSKYNKVPLP LGPQSRYQGN SNESRYKNSP 550
NDSRYHNPRY VNKPETNFNR QPQKYSRQES NAPINKNYNP SNGSRNMAGD 600
HHQGSRPSHP QFPISPSQGQ HQLTSKPIEK KNGSFKDERA KPDESKEFQN 650
SDIADLY 657
Length:657
Mass (Da):74,239
Last modified:November 1, 1991 - v1
Checksum:iCC9034A4B10A510E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90317 Genomic DNA. Translation: BAA14347.1.
L33835 Genomic DNA. Translation: AAB59314.1.
U28371 Genomic DNA. Translation: AAB68058.1.
BK006949 Genomic DNA. Translation: DAA11578.1.
PIRiA39526.
RefSeqiNP_015487.1. NM_001184258.1.

Genome annotation databases

EnsemblFungiiYPR161C; YPR161C; YPR161C.
GeneIDi856290.
KEGGisce:YPR161C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D90317 Genomic DNA. Translation: BAA14347.1 .
L33835 Genomic DNA. Translation: AAB59314.1 .
U28371 Genomic DNA. Translation: AAB68058.1 .
BK006949 Genomic DNA. Translation: DAA11578.1 .
PIRi A39526.
RefSeqi NP_015487.1. NM_001184258.1.

3D structure databases

ProteinModelPortali P23293.
SMRi P23293. Positions 27-374.
ModBasei Search...

Protein-protein interaction databases

BioGridi 36334. 135 interactions.
DIPi DIP-5916N.
IntActi P23293. 14 interactions.
MINTi MINT-668965.
STRINGi 4932.YPR161C.

Proteomic databases

MaxQBi P23293.
PaxDbi P23293.
PeptideAtlasi P23293.
PRIDEi P23293.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPR161C ; YPR161C ; YPR161C .
GeneIDi 856290.
KEGGi sce:YPR161C.

Organism-specific databases

CYGDi YPR161c.
SGDi S000006365. SGV1.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00740000116084.
HOGENOMi HOG000233024.
KOi K15562.
OMAi PRINLEM.
OrthoDBi EOG7K3TWD.

Enzyme and pathway databases

BioCyci YEAST:G3O-34290-MONOMER.
BRENDAi 2.7.11.22. 984.

Miscellaneous databases

NextBioi 981629.
PROi P23293.

Gene expression databases

Genevestigatori P23293.

Family and domain databases

InterProi IPR011009. 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 ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  11. 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].

Entry informationi

Entry nameiBUR1_YEAST
AccessioniPrimary (citable) accession number: P23293
Secondary accession number(s): D6W4G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: June 11, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3

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