MVK

Functionⁱ

Catalyzes the phosphorylation of mevalonate to mevalonate 5-phosphate, a key step in isoprenoid and cholesterol biosynthesis (PubMed:9325256, PubMed:18302342).2 Publications

Catalytic activityⁱ

ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate.2 Publications

Cofactorⁱ

Mg²⁺By similarity

Activity regulationⁱ

Farnesyl pyrophosphate is a competitive inhibitor.1 Publication

Kineticsⁱ

K_M=
74 µM for ATP
1 Publication
Manual assertion based on experiment inⁱ
- Ref.3
  "Identification of catalytic residues in human mevalonate kinase."
  Potter D., Miziorko H.M.
  J. Biol. Chem. 272:25449-25454(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROBABLE ACTIVE SITE, ACTIVITY REGULATION, SUBUNIT, MUTAGENESIS OF GLU-19; GLU-193; ASP-204 AND GLU-296.
K_M=
178 µM for ATP
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Biochemical and structural basis for feedback inhibition of mevalonate kinase and isoprenoid metabolism."
  Fu Z., Voynova N.E., Herdendorf T.J., Miziorko H.M., Kim J.J.
  Biochemistry 47:3715-3724(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF ILE-56; THR-104; TYR-149 AND ILE-196.
K_M=
24 µM for (R)-mevalonate
1 Publication
Manual assertion based on experiment inⁱ
- Ref.3
  "Identification of catalytic residues in human mevalonate kinase."
  Potter D., Miziorko H.M.
  J. Biol. Chem. 272:25449-25454(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROBABLE ACTIVE SITE, ACTIVITY REGULATION, SUBUNIT, MUTAGENESIS OF GLU-19; GLU-193; ASP-204 AND GLU-296.
K_M=
40 µM for (R)-mevalonate
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Biochemical and structural basis for feedback inhibition of mevalonate kinase and isoprenoid metabolism."
  Fu Z., Voynova N.E., Herdendorf T.J., Miziorko H.M., Kim J.J.
  Biochemistry 47:3715-3724(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, MUTAGENESIS OF ILE-56; THR-104; TYR-149 AND ILE-196.

Pathwayⁱ: isopentenyl diphosphate biosynthesis via mevalonate pathway

This protein is involved in step 1 of the subpathway that synthesizes isopentenyl diphosphate from (R)-mevalonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:

Mevalonate kinase (MVK), Mevalonate kinase, Mevalonate kinase, Mevalonate kinase (MVK), Mevalonate kinase (MVK), Mevalonate kinase (MVK)
Phosphomevalonate kinase (PMVK)
no protein annotated in this organism

This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via mevalonate pathway, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from (R)-mevalonate, the pathway isopentenyl diphosphate biosynthesis via mevalonate pathway and in Isoprenoid biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	13	ATPBy similarity	1
Binding siteⁱ	55	ATPBy similarity	1
Binding siteⁱ	135	ATPBy similarity	1
Metal bindingⁱ	146	MagnesiumBy similarity	1
Metal bindingⁱ	193	MagnesiumBy similarity	1
Active siteⁱ	204	Proton acceptor1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	140 – 146	ATPBy similarity		7

GO - Molecular functionⁱ

ATP binding Source: UniProtKB
identical protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 9325256
magnesium ion binding Source: UniProtKB
mevalonate kinase activity
Source: UniProtKB
Inferred from direct assayⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cholesterol biosynthetic process
Source: UniProtKB
Inferred from direct assayⁱ
- 1377680
isopentenyl diphosphate biosynthetic process, mevalonate pathway
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
isoprenoid biosynthetic process
Source: UniProtKB
Inferred from direct assayⁱ
- 14680974
- 14730012
negative regulation of inflammatory response
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 16732551
regulation of cholesterol biosynthetic process Source: Reactome

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Kinase, Transferase
Biological process	Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
Ligand	ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCycⁱ	MetaCyc:ENSG00000110921-MONOMER
BRENDAⁱ	2.7.1.36 2681
Reactomeⁱ	R-HSA-191273 Cholesterol biosynthesis R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
SABIO-RKⁱ	Q03426
UniPathwayⁱ	UPA00057;UER00098

Chemistry databases

SwissLipidsⁱ	SLP:000001240

SwissLipidsⁱ

SLP:000001240

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Mevalonate kinaseCurated (EC:2.7.1.362 Publications) Short name: MK
Gene namesⁱ	Name:MVKImported
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 12

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000110921.11
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:7530 MVK
MIMⁱ	251170 gene
neXtProtⁱ	NX_Q03426

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Cytoplasm, Peroxisome

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Mevalonic aciduria (MEVA)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAccumulation of mevalonic acid which causes a variety of symptoms such as psychomotor retardation, dysmorphic features, cataracts, hepatosplenomegaly, lymphadenopathy, anemia, hypotonia, myopathy, and ataxia.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_010964	243	T → I in MEVA. 1 PublicationCorresponds to variant dbSNP:rs104895314EnsemblClinVar.	1
Natural variantⁱVAR_010965	264	L → F in MEVA. 2 PublicationsCorresponds to variant dbSNP:rs104895315EnsemblClinVar.	1
Natural variantⁱVAR_010966	265	L → P in MEVA. 1 PublicationCorresponds to variant dbSNP:rs104895316EnsemblClinVar.	1
Natural variantⁱVAR_004025	301	N → T in MEVA; diminished activity. 1 PublicationCorresponds to variant dbSNP:rs121917789EnsemblClinVar.	1
Natural variantⁱVAR_004026	334	A → T in MEVA. 3 PublicationsCorresponds to variant dbSNP:rs104895317EnsemblClinVar.	1

Hyperimmunoglobulinemia D and periodic fever syndrome (HIDS)5 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAutosomal recessive disease characterized by recurrent episodes of unexplained high fever associated with skin rash, diarrhea, adenopathy (swollen, tender lymph nodes), arthralgias and/or arthritis. Concentration of IgD, and often IgA, are above normal.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_010956	20	H → N in HIDS. 1 PublicationCorresponds to variant dbSNP:rs11544299Ensembl.	1
Natural variantⁱVAR_029519	20	H → Q in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895335EnsemblClinVar.	1
Natural variantⁱVAR_010957	39	L → P in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895296EnsemblClinVar.	1
Natural variantⁱVAR_029520	132	V → I in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895336EnsemblClinVar.	1
Natural variantⁱVAR_010959	135	S → L in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895297EnsemblClinVar.	1
Natural variantⁱVAR_010960	148	A → T in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895298EnsemblClinVar.	1
Natural variantⁱVAR_010961	150	S → L in HIDS. 1 PublicationCorresponds to variant dbSNP:rs747116992Ensembl.	1
Natural variantⁱVAR_004023	167	P → L in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895300EnsemblClinVar.	1
Natural variantⁱVAR_029521	171	G → R in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895337EnsemblClinVar.	1
Natural variantⁱVAR_029522	211	G → E in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895325EnsemblClinVar.	1
Natural variantⁱVAR_010963	215	R → Q in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895303EnsemblClinVar.	1
Natural variantⁱVAR_029523	250	V → I in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895339EnsemblClinVar.	1
Natural variantⁱVAR_029524	265	L → R in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895316EnsemblClinVar.	1
Natural variantⁱVAR_010967	309	G → S in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895305EnsemblClinVar.	1
Natural variantⁱVAR_010968	326	G → R in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895308EnsemblClinVar.	1
Natural variantⁱVAR_029527	376	G → V in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895340EnsemblClinVar.	1
Natural variantⁱVAR_004027	377	V → I in HIDS; most frequent mutation. 5 PublicationsCorresponds to variant dbSNP:rs28934897EnsemblClinVar.	1

Porokeratosis 3, multiple types (POROK3)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of porokeratosis, a disorder of faulty keratinization characterized by one or more atrophic patches surrounded by a distinctive hyperkeratotic ridgelike border called the cornoid lamella. The keratotic lesions can progress to overt cutaneous neoplasms, typically squamous cell carcinomas. Multiple clinical variants of porokeratosis are recognized, including porokeratosis of Mibelli, linear porokeratosis, disseminated superficial actinic porokeratosis, palmoplantar porokeratosis, and punctate porokeratosis. Different clinical presentations can be observed among members of the same family. Individuals expressing more than one variant have also been reported.

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	19	E → D: No change in protein stability. Weak decrease in kinase activity. Approximately 2-fold decrease in Vmax. Approximately 2-fold decrease affinity for ATP and mevalonate. 1 Publication	1
Mutagenesisⁱ	56	I → A: No effect on kinase activity. Approximately 4- and 5-fold decrease affinities for ATP and mevalonate, respectively. 1 Publication	1
Mutagenesisⁱ	104	T → A: No effect on kinase activity. Approximately 4-fold increase affinity for ATP. Normal affinity for mevalonate. 1 Publication	1
Mutagenesisⁱ	149	Y → A: No effect on kinase activity. Approximately 4- and 8-fold decrease affinities for ATP and mevalonate, respectively. 1 Publication	1
Mutagenesisⁱ	193	E → Q: No change in protein stability. Decreased kinase activity. Approximately 50-fold decrease in Vmax. Approximately 20- and 40-fold decrease affinities for ATP and mevalonate, respectively. 1 Publication	1
Mutagenesisⁱ	196	I → A: No effect on kinase activity. Approximately 2- and 3-fold decrease affinities for ATP and mevalonate, respectively. 1 Publication	1
Mutagenesisⁱ	204	D → A: No change in protein stability. Loss of kinase activity. Normal affinities for ATP and mevalonate. 1 Publication	1
Mutagenesisⁱ	204	D → N: No change in protein stability. Loss of kinase activity. Normal affinities for ATP and mevalonate. 1 Publication	1
Mutagenesisⁱ	296	E → Q: No change in protein stability. No effect on kinase activity. 1 Publication	1

Keywords - Diseaseⁱ

Cataract, Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	4598
MalaCards human disease database More...MalaCardsⁱ	MVK
MIMⁱ	175900 phenotype 260920 phenotype 610377 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000110921
Orphanetⁱ	79152 Disseminated superficial actinic porokeratosis 343 Hyperimmunoglobulinemia D with periodic fever 29 Mevalonic aciduria 735 Porokeratosis of Mibelli
PharmGKBⁱ	PA31331

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB04695 FARNESYL THIOPYROPHOSPHATE
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	640

Polymorphism and mutation databases

BioMutaⁱ	MVK
DMDMⁱ	417215

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000156657	1 – 396	Mevalonate kinaseAdd BLAST		396

Proteomic databases

EPDⁱ	Q03426
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q03426
PaxDbⁱ	Q03426
PeptideAtlas More...PeptideAtlasⁱ	Q03426
PRIDEⁱ	Q03426
ProteomicsDBⁱ	58211

PTM databases

iPTMnetⁱ	Q03426
PhosphoSitePlusⁱ	Q03426

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000110921 Expressed in 219 organ(s), highest expression level in C1 segment of cervical spinal cord
CleanExⁱ	HS_MVK
ExpressionAtlasⁱ	Q03426 baseline and differential
Genevisibleⁱ	Q03426 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA016961

HPAⁱ

HPA016961

Interactionⁱ

Subunit structureⁱ

Homodimer.1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		7	EBI-740630,EBI-740630
POT1	Q9NUX5	2	EBI-740630,EBI-752420

GO - Molecular functionⁱ

identical protein binding
Source: UniProtKB
Inferred from direct assayⁱ
- 9325256

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	110683, 17 interactors
IntActⁱ	Q03426, 4 interactors
STRINGⁱ	9606.ENSP00000228510

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	4 – 17	Combined sources	14
Turnⁱ	19 – 21	Combined sources	3
Helixⁱ	22 – 24	Combined sources	3
Beta strandⁱ	28 – 43	Combined sources	16
Beta strandⁱ	45 – 52	Combined sources	8
Turnⁱ	54 – 56	Combined sources	3
Beta strandⁱ	59 – 63	Combined sources	5
Helixⁱ	64 – 69	Combined sources	6
Helixⁱ	85 – 95	Combined sources	11
Helixⁱ	103 – 119	Combined sources	17
Beta strandⁱ	122 – 125	Combined sources	4
Beta strandⁱ	129 – 137	Combined sources	9
Beta strandⁱ	141 – 143	Combined sources	3
Helixⁱ	145 – 160	Combined sources	16
Turnⁱ	167 – 171	Combined sources	5
Beta strandⁱ	173 – 175	Combined sources	3
Helixⁱ	179 – 196	Combined sources	18
Beta strandⁱ	197 – 199	Combined sources	3
Helixⁱ	203 – 210	Combined sources	8
Beta strandⁱ	212 – 216	Combined sources	5
Beta strandⁱ	221 – 223	Combined sources	3
Beta strandⁱ	230 – 236	Combined sources	7
Helixⁱ	243 – 256	Combined sources	14
Helixⁱ	258 – 283	Combined sources	26
Helixⁱ	288 – 307	Combined sources	20
Helixⁱ	313 – 323	Combined sources	11
Turnⁱ	324 – 326	Combined sources	3
Beta strandⁱ	328 – 331	Combined sources	4
Beta strandⁱ	336 – 343	Combined sources	8
Helixⁱ	350 – 361	Combined sources	12
Turnⁱ	362 – 364	Combined sources	3
Beta strandⁱ	366 – 373	Combined sources	8
Beta strandⁱ	377 – 380	Combined sources	4
Helixⁱ	387 – 392	Combined sources	6

Show more details

3D structure databases

ProteinModelPortalⁱ	Q03426
SMRⁱ	Q03426
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q03426

EvolutionaryTraceⁱ

Q03426

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the GHMP kinase family. Mevalonate kinase subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG1511 Eukaryota COG1577 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000011860
HOVERGENⁱ	HBG000402
InParanoidⁱ	Q03426
KEGG Orthology (KO) More...KOⁱ	K00869
OMAⁱ	NTVCTYG
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G05QV
PhylomeDBⁱ	Q03426
TreeFamⁱ	TF313775

Family and domain databases

Gene3Dⁱ	3.30.230.10, 1 hit 3.30.70.890, 1 hit
InterProⁱ	View protein in InterPro IPR013750 GHMP_kinase_C_dom IPR036554 GHMP_kinase_C_sf IPR006204 GHMP_kinase_N_dom IPR006203 GHMP_knse_ATP-bd_CS IPR006205 Mev_gal_kin IPR020568 Ribosomal_S5_D2-typ_fold IPR014721 Ribosomal_S5_D2-typ_fold_subgr
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08544 GHMP_kinases_C, 1 hit PF00288 GHMP_kinases_N, 1 hit
SUPFAMⁱ	SSF54211 SSF54211, 1 hit SSF55060 SSF55060, 1 hit
TIGRFAMsⁱ	TIGR00549 mevalon_kin, 1 hit
PROSITEⁱ	View protein in PROSITE PS00627 GHMP_KINASES_ATP, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 9 potential isoforms that are computationally mapped.Show all Align All

Q03426-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MLSEVLLVSA PGKVILHGEH AVVHGKVALA VSLNLRTFLR LQPHSNGKVD 
        60         70         80         90        100
LSLPNIGIKR AWDVARLQSL DTSFLEQGDV TTPTSEQVEK LKEVAGLPDD 
       110        120        130        140        150
CAVTERLAVL AFLYLYLSIC RKQRALPSLD IVVWSELPPG AGLGSSAAYS 
       160        170        180        190        200
VCLAAALLTV CEEIPNPLKD GDCVNRWTKE DLELINKWAF QGERMIHGNP 
       210        220        230        240        250
SGVDNAVSTW GGALRYHQGK ISSLKRSPAL QILLTNTKVP RNTRALVAGV 
       260        270        280        290        300
RNRLLKFPEI VAPLLTSIDA ISLECERVLG EMGEAPAPEQ YLVLEELIDM 
       310        320        330        340        350
NQHHLNALGV GHASLDQLCQ VTRARGLHSK LTGAGGGGCG ITLLKPGLEQ 
       360        370        380        390 
PEVEATKQAL TSCGFDCLET SIGAPGVSIH SATSLDSRVQ QALDGL

Length:396

Mass (Da):42,451

Last modified:October 1, 1993 - v1

Checksum:ⁱC8F6B629B58CD229

GO

Computationally mapped potential isoform sequencesⁱ

There are 9 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

F5H8H2	F5H8H2_HUMAN	Mevalonate kinase Mevalonate kinase, MK, EC 2.7.1.36	MVK	344	Annotation score:
A0A1B0GWC2	A0A1B0GWC2_HUMAN	Mevalonate kinase Mevalonate kinase, MK, EC 2.7.1.36	MVK	346	Annotation score:
F5GXC0	F5GXC0_HUMAN	Mevalonate kinase Mevalonate kinase	MVK	170	Annotation score:
F5H092	F5H092_HUMAN	Mevalonate kinase Mevalonate kinase	MVK	200	Annotation score:
A0A0B4J236	A0A0B4J236_HUMAN	Mevalonate kinase (Mevalonic acidur... Mevalonate kinase (Mevalonic aciduria), isoform CRA_b	MVK hCG_40321	115	Annotation score:
A0A1B0GWF3	A0A1B0GWF3_HUMAN	Mevalonate kinase Mevalonate kinase	MVK	150	Annotation score:
F5H368	F5H368_HUMAN	Mevalonate kinase Mevalonate kinase	MVK	117	Annotation score:
F5H163	F5H163_HUMAN	Mevalonate kinase Mevalonate kinase	MVK	83	Annotation score:
A0A1W2PS16	A0A1W2PS16_HUMAN	Mevalonate kinase Mevalonate kinase	MVK	117	Annotation score:

Sequence cautionⁱ

The sequence CAA53059 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_075036	12	G → R in POROK3. 1 Publication	1
Natural variantⁱVAR_010956	20	H → N in HIDS. 1 PublicationCorresponds to variant dbSNP:rs11544299Ensembl.	1
Natural variantⁱVAR_004022	20	H → P in HIDS and MEVA. 3 PublicationsCorresponds to variant dbSNP:rs104895295EnsemblClinVar.	1
Natural variantⁱVAR_029519	20	H → Q in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895335EnsemblClinVar.	1
Natural variantⁱVAR_010957	39	L → P in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895296EnsemblClinVar.	1
Natural variantⁱVAR_075037	41	L → P in POROK3. 1 PublicationCorresponds to variant dbSNP:rs397514571EnsemblClinVar.	1
Natural variantⁱVAR_010958	52	S → N2 PublicationsCorresponds to variant dbSNP:rs7957619EnsemblClinVar.	1
Natural variantⁱVAR_029520	132	V → I in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895336EnsemblClinVar.	1
Natural variantⁱVAR_010959	135	S → L in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895297EnsemblClinVar.	1
Natural variantⁱVAR_010960	148	A → T in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895298EnsemblClinVar.	1
Natural variantⁱVAR_010961	150	S → L in HIDS. 1 PublicationCorresponds to variant dbSNP:rs747116992Ensembl.	1
Natural variantⁱVAR_004023	167	P → L in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895300EnsemblClinVar.	1
Natural variantⁱVAR_029521	171	G → R in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895337EnsemblClinVar.	1
Natural variantⁱVAR_010962	202	G → R in HIDS and POROK3. 2 PublicationsCorresponds to variant dbSNP:rs104895301EnsemblClinVar.	1
Natural variantⁱVAR_029522	211	G → E in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895325EnsemblClinVar.	1
Natural variantⁱVAR_010963	215	R → Q in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895303EnsemblClinVar.	1
Natural variantⁱVAR_010964	243	T → I in MEVA. 1 PublicationCorresponds to variant dbSNP:rs104895314EnsemblClinVar.	1
Natural variantⁱVAR_029523	250	V → I in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895339EnsemblClinVar.	1
Natural variantⁱVAR_075038	255	L → P in POROK3. 1 PublicationCorresponds to variant dbSNP:rs397514570EnsemblClinVar.	1
Natural variantⁱVAR_010965	264	L → F in MEVA. 2 PublicationsCorresponds to variant dbSNP:rs104895315EnsemblClinVar.	1
Natural variantⁱVAR_010966	265	L → P in MEVA. 1 PublicationCorresponds to variant dbSNP:rs104895316EnsemblClinVar.	1
Natural variantⁱVAR_029524	265	L → R in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895316EnsemblClinVar.	1
Natural variantⁱVAR_004024	268	I → T in HIDS and MEVA. 6 PublicationsCorresponds to variant dbSNP:rs104895304EnsemblClinVar.	1
Natural variantⁱVAR_075039	279	L → P in POROK3. 1 Publication	1
Natural variantⁱVAR_075040	291	Y → D in POROK3. 1 Publication	1
Natural variantⁱVAR_004025	301	N → T in MEVA; diminished activity. 1 PublicationCorresponds to variant dbSNP:rs121917789EnsemblClinVar.	1
Natural variantⁱVAR_010967	309	G → S in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895305EnsemblClinVar.	1
Natural variantⁱVAR_009068	310	V → M in MEVA and HIDS. 3 PublicationsCorresponds to variant dbSNP:rs104895319EnsemblClinVar.	1
Natural variantⁱVAR_075041	312	H → R in POROK3. 1 Publication	1
Natural variantⁱVAR_010968	326	G → R in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895308EnsemblClinVar.	1
Natural variantⁱVAR_004026	334	A → T in MEVA. 3 PublicationsCorresponds to variant dbSNP:rs104895317EnsemblClinVar.	1
Natural variantⁱVAR_029525	335	G → S. Corresponds to variant dbSNP:rs11614976Ensembl.	1
Natural variantⁱVAR_029526	356	T → M1 PublicationCorresponds to variant dbSNP:rs104895342EnsemblClinVar.	1
Natural variantⁱVAR_075042	365	F → S in POROK3. 1 PublicationCorresponds to variant dbSNP:rs398122911EnsemblClinVar.	1
Natural variantⁱVAR_075043	376	G → S in POROK3. 1 PublicationCorresponds to variant dbSNP:rs971159663Ensembl.	1
Natural variantⁱVAR_029527	376	G → V in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895340EnsemblClinVar.	1
Natural variantⁱVAR_004027	377	V → I in HIDS; most frequent mutation. 5 PublicationsCorresponds to variant dbSNP:rs28934897EnsemblClinVar.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M88468 mRNA Translation: AAB59362.1 X75311 mRNA Translation: CAA53060.1 X75311 mRNA Translation: CAA53059.1 Different initiation. AF217535 AF217534 Genomic DNA Translation: AAF82407.1 BC016140 mRNA Translation: AAH16140.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS9132.1
PIRⁱ	A42919
NCBI Reference Sequences More...RefSeqⁱ	NP_000422.1, NM_000431.3 NP_001107657.1, NM_001114185.2 NP_001288111.1, NM_001301182.1 XP_016874803.1, XM_017019314.1
UniGeneⁱ	Hs.130607

Genome annotation databases

Ensemblⁱ	ENST00000228510; ENSP00000228510; ENSG00000110921 ENST00000539575; ENSP00000443551; ENSG00000110921
GeneIDⁱ	4598
KEGGⁱ	hsa:4598
UCSC genome browser More...UCSCⁱ	uc009zvk.4 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Protein	Similar proteins		Species	Score	Length	Source
Q03426	Mevalonate kinase		HUMAN		396	UniRef100_Q03426
Mevalonate kinase (Fragment)		HUMAN		200
Mevalonate kinase (Fragment)		HUMAN		170

Protein	Similar proteins		Species	Score	Length	Source
Q03426	Mevalonate kinase		HUMAN		396	UniRef90_Q03426
Mevalonate kinase		PANTR		396
Mevalonate kinase		PANPA		396
Mevalonate kinase		GORGO		396
Mevalonate kinase		PONAB		396
+12

Protein	Similar proteins		Species	Score	Length	Source
Q03426	Mevalonate kinase		BOVIN		396	UniRef50_Q03426
Mevalonate kinase		HUMAN		396
Mevalonate kinase		PANTR		396
Mevalonate kinase		PANPA		396
Mevalonate kinase		GORGO		396
+29

Cross-referencesⁱ

Web resourcesⁱ

INFEVERS

Repertory of FMF and hereditary autoinflammatory disorders mutations

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M88468 mRNA Translation: AAB59362.1 X75311 mRNA Translation: CAA53060.1 X75311 mRNA Translation: CAA53059.1 Different initiation. AF217535 AF217534 Genomic DNA Translation: AAF82407.1 BC016140 mRNA Translation: AAH16140.1
CCDSⁱ	CCDS9132.1
PIRⁱ	A42919
RefSeqⁱ	NP_000422.1, NM_000431.3 NP_001107657.1, NM_001114185.2 NP_001288111.1, NM_001301182.1 XP_016874803.1, XM_017019314.1
UniGeneⁱ	Hs.130607

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2R3V	X-ray	2.50	A/B/C/D	1-396	[»]
ProteinModelPortalⁱ	Q03426
SMRⁱ	Q03426
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	110683, 17 interactors
IntActⁱ	Q03426, 4 interactors
STRINGⁱ	9606.ENSP00000228510

Chemistry databases

DrugBankⁱ	DB04695 FARNESYL THIOPYROPHOSPHATE
GuidetoPHARMACOLOGYⁱ	640
SwissLipidsⁱ	SLP:000001240

PTM databases

iPTMnetⁱ	Q03426
PhosphoSitePlusⁱ	Q03426

Polymorphism and mutation databases

BioMutaⁱ	MVK
DMDMⁱ	417215

Proteomic databases

EPDⁱ	Q03426
MaxQBⁱ	Q03426
PaxDbⁱ	Q03426
PeptideAtlasⁱ	Q03426
PRIDEⁱ	Q03426
ProteomicsDBⁱ	58211

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	4598
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000228510; ENSP00000228510; ENSG00000110921 ENST00000539575; ENSP00000443551; ENSG00000110921
GeneIDⁱ	4598
KEGGⁱ	hsa:4598
UCSCⁱ	uc009zvk.4 human

Organism-specific databases

CTDⁱ	4598
DisGeNETⁱ	4598
EuPathDBⁱ	HostDB:ENSG00000110921.11
GeneCardsⁱ	MVK
HGNCⁱ	HGNC:7530 MVK
HPAⁱ	HPA016961
MalaCardsⁱ	MVK
MIMⁱ	175900 phenotype 251170 gene 260920 phenotype 610377 phenotype
neXtProtⁱ	NX_Q03426
OpenTargetsⁱ	ENSG00000110921
Orphanetⁱ	79152 Disseminated superficial actinic porokeratosis 343 Hyperimmunoglobulinemia D with periodic fever 29 Mevalonic aciduria 735 Porokeratosis of Mibelli
PharmGKBⁱ	PA31331
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1511 Eukaryota COG1577 LUCA
GeneTreeⁱ	ENSGT00390000011860
HOVERGENⁱ	HBG000402
InParanoidⁱ	Q03426
KOⁱ	K00869
OMAⁱ	NTVCTYG
OrthoDBⁱ	EOG091G05QV
PhylomeDBⁱ	Q03426
TreeFamⁱ	TF313775

Enzyme and pathway databases

UniPathwayⁱ	UPA00057;UER00098
BioCycⁱ	MetaCyc:ENSG00000110921-MONOMER
BRENDAⁱ	2.7.1.36 2681
Reactomeⁱ	R-HSA-191273 Cholesterol biosynthesis R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
SABIO-RKⁱ	Q03426

Miscellaneous databases

ChiTaRSⁱ	MVK human
EvolutionaryTraceⁱ	Q03426
GeneWikiⁱ	Mevalonate_kinase
GenomeRNAiⁱ	4598
Protein Ontology More...PROⁱ	PR:Q03426
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000110921 Expressed in 219 organ(s), highest expression level in C1 segment of cervical spinal cord
CleanExⁱ	HS_MVK
ExpressionAtlasⁱ	Q03426 baseline and differential
Genevisibleⁱ	Q03426 HS

Family and domain databases

Gene3Dⁱ	3.30.230.10, 1 hit 3.30.70.890, 1 hit
InterProⁱ	View protein in InterPro IPR013750 GHMP_kinase_C_dom IPR036554 GHMP_kinase_C_sf IPR006204 GHMP_kinase_N_dom IPR006203 GHMP_knse_ATP-bd_CS IPR006205 Mev_gal_kin IPR020568 Ribosomal_S5_D2-typ_fold IPR014721 Ribosomal_S5_D2-typ_fold_subgr
Pfamⁱ	View protein in Pfam PF08544 GHMP_kinases_C, 1 hit PF00288 GHMP_kinases_N, 1 hit
SUPFAMⁱ	SSF54211 SSF54211, 1 hit SSF55060 SSF55060, 1 hit
TIGRFAMsⁱ	TIGR00549 mevalon_kin, 1 hit
PROSITEⁱ	View protein in PROSITE PS00627 GHMP_KINASES_ATP, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	KIME_HUMAN
Accessionⁱ	Q03426Primary (citable) accession number: Q03426
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
	Last sequence update:	October 1, 1993
	Last modified:	November 7, 2018
	This is version 200 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PATHWAY comments
Index of metabolic and biosynthesis pathways
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q03426 (KIME_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Mevalonate kinase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: isopentenyl diphosphate biosynthesis via mevalonate pathway

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Chemistry databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Peroxisome

Other locations

Cytosol

Peroxisome

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

Kineticsⁱ

Pathwayⁱ: isopentenyl diphosphate biosynthesis via mevalonate pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ