Reviewed, UniProtKB/Swiss-Prot P23293 (BUR1_YEAST)

Names and origin

Protein names

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 names

Name:	SGV1
Synonyms:	BUR1
Ordered Locus Names:	YPR161C
ORF Names:	P9584.8

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	657 AA.
Sequence status	Complete.
Protein existence	Evidence 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.4 Ref.5 Ref.6 Ref.7 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.5 Ref.6
Subcellular location	Nucleus Ref.10.
Miscellaneous	Present with 2070 molecules/cell in log phase SD medium. Ref.11
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phosphorylation of RNA polymerase II C-terminal domain Ref.6 Inferred from direct assay. Source: SGD positive regulation of histone H3-K4 methylation Ref.12 Inferred from mutant phenotype. Source: SGD transcription Ref.5 Inferred from direct assay. Source: SGD
Cellular component	cyclin-dependent protein kinase holoenzyme complex Ref.5 Inferred from physical interaction. Source: SGD nucleus Ref.6 Inferred from physical interaction. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II carboxy-terminal domain kinase activity Inferred from electronic annotation. Source: EC cyclin-dependent protein kinase activity Ref.5 Inferred from direct assay. Source: SGD protein binding Ref.5 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BUR2	Q05949	2	EBI-17078,EBI-30948

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 657	657	Serine/threonine-protein kinase BUR1		PRO_0000085687
Regions
	Domain	60 – 366	307	Protein kinase
	Nucleotide binding	66 – 74	9	ATP By similarity
Sites
	Active site	195	1	Proton acceptor By similarity
	Binding site	89	1	ATP By similarity
Amino acid modifications
	Modified residue	240	1	Phosphothreonine; by CAK Ref.7 Ref.8 Ref.18
	Modified residue	241	1	Phosphoserine Ref.14
	Modified residue	400	1	Phosphoserine Ref.16
	Modified residue	405	1	Phosphothreonine Ref.16
	Modified residue	417	1	Phosphoserine Ref.18 Ref.15 Ref.17
	Modified residue	634	1	Phosphoserine Ref.18
Experimental info
	Mutagenesis	107	1	E → Q: Loss of kinase activity in vitro. Ref.9
	Mutagenesis	213	1	D → N: Loss of kinase activity in vitro. Ref.9
	Mutagenesis	240	1	T → A, D or E: No phosphorylation of SGV1. Ref.7 Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P23293-1 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: CC9034A4B10A510E	FASTA	657	74,239
	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

References

	« Hide 'large scale' referencesShow '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: 1828190] [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: 7871892] [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: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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: 8293972] [Abstract] Cited for: FUNCTION.
[5]	"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: 10982824] [Abstract] Cited for: INTERACTION WITH BUR2, FUNCTION.
[6]	"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: 11390638] [Abstract] Cited for: INTERACTION WITH RBP1, FUNCTION.
[7]	"Activation of the Bur1-Bur2 cyclin-dependent kinase complex by Cak1." Yao S., Prelich G. Mol. Cell. Biol. 22:6750-6758(2002) [PubMed: 12215532] [Abstract] Cited for: PHOSPHORYLATION AT THR-240, MUTAGENESIS OF THR-240, FUNCTION.
[8]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-240, MASS SPECTROMETRY.
[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: 12972617] [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: 14562095] [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: 14562106] [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: 16040246] [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: 16307922] [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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, MASS SPECTROMETRY.
[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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, MASS SPECTROMETRY.
[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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400 AND THR-405, MASS SPECTROMETRY.
[17]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417, MASS SPECTROMETRY.
[18]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-240; SER-417 AND SER-634, MASS SPECTROMETRY.
+	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.
PIR	A39526.
RefSeq	NP_015487.1.
3D structure databases
SMR	P23293. Positions 58-374.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5916N.
IntAct	P23293. 35 interactions.
STRING	P23293.
Proteomic databases
PeptideAtlas	P23293.
Genome annotation databases
Ensembl	YPR161C; YPR161C; YPR161C; Saccharomyces cerevisiae. [Genome view]
GeneID	856290.
KEGG	sce:YPR161C.
NMPDR	fig|4932.3.peg.6633.
Organism-specific databases
CYGD	YPR161c.
SGD	S000006365. SGV1.
Phylogenomic databases
eggNOG	fuNOG04620.
HOGENOM	HBG204009.
OMA	PTEESHE.
OrthoDB	EOG96T4J6.
PhylomeDB	P23293.
Enzyme and pathway databases
BRENDA	2.7.11.22. 250. 2.7.11.23. 250.
Gene expression databases
ArrayExpress	P23293.
Genevestigator	P23293.
GermOnline	YPR161C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	981629.

Entry information

Entry name

BUR1_YEAST

Accession

Primary (citable) accession number: P23293

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	January 19, 2010
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)