[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00327205; PubMed=3323847 [NCBI, ExPASy, EBI, Israel, Japan] Kearsey S.E., Edwards J.; "Mutations that increase the mitotic stability of minichromosomes in yeast: characterization of RAR1."; Mol. Gen. Genet. 210:509-517(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00362081; PubMed=1645230 [NCBI, ExPASy, EBI, Israel, Japan] Oulmouden A., Karst F.; "Nucleotide sequence of the ERG12 gene of Saccharomyces cerevisiae encoding mevalonate kinase."; Curr. Genet. 19:9-14(1991).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169872 [NCBI, ExPASy, EBI, Israel, Japan] Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."; Nature 387:90-93(1997).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-246. STRAIN=SP1; Saito A., Kazuta Y., Kondo H., Tanabe T.; Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[5]	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).

Comments

FUNCTION: May contribute to the regulation of the isoprenoid and sterol pathway in living cells.
FUNCTION: RAR (regulation of autonomous replication) is a protein whose activity increases the mitotic stability of plasmids.
CATALYTIC ACTIVITY: ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate.
ENZYME REGULATION: Farnesyl pyrophosphate and geranyl pyrophosphate inhibit mevalonate kinase by binding competitively at the ATP-binding site.
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
MISCELLANEOUS: Present with 3300 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase subfamily.

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

X06114; CAA29487.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X55875; CAA39359.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z49809; CAA89923.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D78165; BAA24409.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S05875; BVBYR1.

RefSeq

NP_013935.1; -.

3D structure databases

HSSP

P17256; 1KVK. [HSSP ENTRY / PDB]

ModBase

P07277.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-651; -.

Organism-specific databases

YMR208w; -.

S000004821; ERG12.

Gene expression databases

ArrayExpress

P07277; -.

GermOnline

YMR208W; Saccharomyces cerevisiae.

Ontologies

GO:0004496;	Molecular function: mevalonate kinase activity (inferred from direct assay from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR006204; GHMP_kinase.
IPR013750; GHMP_kinase_C.
IPR006203; GHMP_knse_ATP_bd_CS.
IPR006205; Mev_gal_kin.
IPR006206; Mev_galkinase.
IPR014721; Ribosomal_S5_D2-type_fold.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1.

PANTHER

PTHR10457:SF4; Mev_gal_kin; 1.

Pfam

PF08544; GHMP_kinases_C; 1.
PF00288; GHMP_kinases_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00959; MEVGALKINASE.

TIGRFAMs

TIGR00549; mevalon_kin; 1.

PROSITE

PS00627; GHMP_KINASES_ATP; 1.

Proteomic databases

P07277; -.

Genome annotation databases

Ensembl

YMR208W; Saccharomyces cerevisiae. [Contig view]

855248; -.

Z71257_GR; YMR208W.

sce:YMR208W; -.

fig|4932.3.peg.4988; -.

Phylogenomic databases

HOGENOM

P07277; -.

Other

LinkHub

P07277; -.

NextBio

978816; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Complete proteome; Cytoplasm; Kinase; Lipid synthesis; Nucleotide-binding; Steroid biosynthesis; Sterol biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 443`	`443`	`Mevalonate kinase.`	`PRO_0000156662`
`NP_BIND`	`141 151`	`11`	`ATP (Potential).`

Sequence information

Length: 443 AA [This is the length of the unprocessed precursor]

Molecular weight: 48460 Da [This is the MW of the unprocessed precursor]

CRC64: 8B24052A72C97280 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLPFLTSAP GKVIIFGEHS AVYNKPAVAA SVSALRTYLL ISESSAPDTI ELDFPDISFN 

        70         80         90        100        110        120 
HKWSINDFNA ITEDQVNSQK LAKAQQATDG LSQELVSLLD PLLAQLSESF HYHAAFCFLY 

       130        140        150        160        170        180 
MFVCLCPHAK NIKFSLKSTL PIGAGLGSSA SISVSLALAM AYLGGLIGSN DLEKLSENDK 

       190        200        210        220        230        240 
HIVNQWAFIG EKCIHGTPSG IDNAVATYGN ALLFEKDSHN GTINTNNFKF LDDFPAIPMI 

       250        260        270        280        290        300 
LTYTRIPRST KDLVARVRVL VTEKFPEVMK PILDAMGECA LQGLEIMTKL SKCKGTDDEA 

       310        320        330        340        350        360 
VETNNELYEQ LLELIRINHG LLVSIGVSHP GLELIKNLSD DLRIGSTKLT GAGGGGCSLT 

       370        380        390        400        410        420 
LLRRDITQEQ IDSFKKKLQD DFSYETFETD LGGTGCCLLS AKNLNKDLKI KSLVFQLFEN 

       430        440 
KTTTKQQIDD LLLPGNTNLP WTS

P07277 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools