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Protein

Mevalonate kinase

Gene

MVK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

  1. KM=74 µM for ATP1 Publication
  2. KM=178 µM for ATP1 Publication
  3. KM=24 µM for (R)-mevalonate1 Publication
  4. KM=40 µM for (R)-mevalonate1 Publication
  1. Vmax=37 µmol/min/mg enzyme with (R)-mevalonate as substrate1 Publication
  2. Vmax=28 µmol/min/mg enzyme with (R)-mevalonate as substrate1 Publication

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:
  1. Mevalonate kinase (MVK), Mevalonate kinase, Mevalonate kinase, Mevalonate kinase (MVK), Mevalonate kinase (MVK), Mevalonate kinase (MVK)
  2. Phosphomevalonate kinase (PMVK)
  3. 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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei13ATPBy similarity1
Binding sitei55ATPBy similarity1
Binding sitei135ATPBy similarity1
Metal bindingi146MagnesiumBy similarity1
Metal bindingi193MagnesiumBy similarity1
Active sitei204Proton acceptor1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi140 – 146ATPBy similarity7

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionKinase, Transferase
Biological processCholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000110921-MONOMER
BRENDAi2.7.1.36 2681
ReactomeiR-HSA-191273 Cholesterol biosynthesis
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
SABIO-RKiQ03426
UniPathwayi
UPA00057;UER00098

Chemistry databases

SwissLipidsiSLP:000001240

Names & Taxonomyi

Protein namesi
Recommended name:
Mevalonate kinaseCurated (EC:2.7.1.362 Publications)
Short name:
MK
Gene namesi
Name:MVKImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000110921.11
HGNCiHGNC:7530 MVK
MIMi251170 gene
neXtProtiNX_Q03426

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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.
See also OMIM:610377
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_010964243T → I in MEVA. 1 PublicationCorresponds to variant dbSNP:rs104895314EnsemblClinVar.1
Natural variantiVAR_010965264L → F in MEVA. 2 PublicationsCorresponds to variant dbSNP:rs104895315EnsemblClinVar.1
Natural variantiVAR_010966265L → P in MEVA. 1 PublicationCorresponds to variant dbSNP:rs104895316EnsemblClinVar.1
Natural variantiVAR_004025301N → T in MEVA; diminished activity. 1 PublicationCorresponds to variant dbSNP:rs121917789EnsemblClinVar.1
Natural variantiVAR_004026334A → 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.
See also OMIM:260920
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01095620H → N in HIDS. 1 PublicationCorresponds to variant dbSNP:rs11544299Ensembl.1
Natural variantiVAR_02951920H → Q in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895335EnsemblClinVar.1
Natural variantiVAR_01095739L → P in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895296EnsemblClinVar.1
Natural variantiVAR_029520132V → I in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895336EnsemblClinVar.1
Natural variantiVAR_010959135S → L in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895297EnsemblClinVar.1
Natural variantiVAR_010960148A → T in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895298EnsemblClinVar.1
Natural variantiVAR_010961150S → L in HIDS. 1 PublicationCorresponds to variant dbSNP:rs747116992Ensembl.1
Natural variantiVAR_004023167P → L in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895300EnsemblClinVar.1
Natural variantiVAR_029521171G → R in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895337EnsemblClinVar.1
Natural variantiVAR_029522211G → E in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895325EnsemblClinVar.1
Natural variantiVAR_010963215R → Q in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895303EnsemblClinVar.1
Natural variantiVAR_029523250V → I in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895339EnsemblClinVar.1
Natural variantiVAR_029524265L → R in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895316EnsemblClinVar.1
Natural variantiVAR_010967309G → S in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895305EnsemblClinVar.1
Natural variantiVAR_010968326G → R in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895308EnsemblClinVar.1
Natural variantiVAR_029527376G → V in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895340EnsemblClinVar.1
Natural variantiVAR_004027377V → 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.
See also OMIM:175900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07503612G → R in POROK3. 1 Publication1
Natural variantiVAR_07503741L → P in POROK3. 1 PublicationCorresponds to variant dbSNP:rs397514571EnsemblClinVar.1
Natural variantiVAR_075038255L → P in POROK3. 1 PublicationCorresponds to variant dbSNP:rs397514570EnsemblClinVar.1
Natural variantiVAR_075039279L → P in POROK3. 1 Publication1
Natural variantiVAR_075040291Y → D in POROK3. 1 Publication1
Natural variantiVAR_075041312H → R in POROK3. 1 Publication1
Natural variantiVAR_075042365F → S in POROK3. 1 PublicationCorresponds to variant dbSNP:rs398122911EnsemblClinVar.1
Natural variantiVAR_075043376G → S in POROK3. 1 PublicationCorresponds to variant dbSNP:rs971159663Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi19E → 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 Publication1
Mutagenesisi56I → A: No effect on kinase activity. Approximately 4- and 5-fold decrease affinities for ATP and mevalonate, respectively. 1 Publication1
Mutagenesisi104T → A: No effect on kinase activity. Approximately 4-fold increase affinity for ATP. Normal affinity for mevalonate. 1 Publication1
Mutagenesisi149Y → A: No effect on kinase activity. Approximately 4- and 8-fold decrease affinities for ATP and mevalonate, respectively. 1 Publication1
Mutagenesisi193E → 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 Publication1
Mutagenesisi196I → A: No effect on kinase activity. Approximately 2- and 3-fold decrease affinities for ATP and mevalonate, respectively. 1 Publication1
Mutagenesisi204D → A: No change in protein stability. Loss of kinase activity. Normal affinities for ATP and mevalonate. 1 Publication1
Mutagenesisi204D → N: No change in protein stability. Loss of kinase activity. Normal affinities for ATP and mevalonate. 1 Publication1
Mutagenesisi296E → Q: No change in protein stability. No effect on kinase activity. 1 Publication1

Keywords - Diseasei

Cataract, Disease mutation

Organism-specific databases

DisGeNETi4598
MalaCardsiMVK
MIMi175900 phenotype
260920 phenotype
610377 phenotype
OpenTargetsiENSG00000110921
Orphaneti79152 Disseminated superficial actinic porokeratosis
343 Hyperimmunoglobulinemia D with periodic fever
29 Mevalonic aciduria
735 Porokeratosis of Mibelli
PharmGKBiPA31331

Chemistry databases

DrugBankiDB04695 FARNESYL THIOPYROPHOSPHATE
GuidetoPHARMACOLOGYi640

Polymorphism and mutation databases

BioMutaiMVK
DMDMi417215

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001566571 – 396Mevalonate kinaseAdd BLAST396

Proteomic databases

EPDiQ03426
MaxQBiQ03426
PaxDbiQ03426
PeptideAtlasiQ03426
PRIDEiQ03426
ProteomicsDBi58211

PTM databases

iPTMnetiQ03426
PhosphoSitePlusiQ03426

Expressioni

Gene expression databases

BgeeiENSG00000110921 Expressed in 219 organ(s), highest expression level in C1 segment of cervical spinal cord
CleanExiHS_MVK
ExpressionAtlasiQ03426 baseline and differential
GenevisibleiQ03426 HS

Organism-specific databases

HPAiHPA016961

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110683, 17 interactors
IntActiQ03426, 4 interactors
STRINGi9606.ENSP00000228510

Structurei

Secondary structure

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ03426
SMRiQ03426
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03426

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1511 Eukaryota
COG1577 LUCA
GeneTreeiENSGT00390000011860
HOVERGENiHBG000402
InParanoidiQ03426
KOiK00869
OMAiNTVCTYG
OrthoDBiEOG091G05QV
PhylomeDBiQ03426
TreeFamiTF313775

Family and domain databases

Gene3Di3.30.230.10, 1 hit
3.30.70.890, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF08544 GHMP_kinases_C, 1 hit
PF00288 GHMP_kinases_N, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
SSF55060 SSF55060, 1 hit
TIGRFAMsiTIGR00549 mevalon_kin, 1 hit
PROSITEiView 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 allAlign All

Q03426-1 [UniParc]FASTAAdd 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.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5H8H2F5H8H2_HUMAN
Mevalonate kinase
MVK
344Annotation score:
A0A1B0GWC2A0A1B0GWC2_HUMAN
Mevalonate kinase
MVK
346Annotation score:
F5GXC0F5GXC0_HUMAN
Mevalonate kinase
MVK
170Annotation score:
F5H092F5H092_HUMAN
Mevalonate kinase
MVK
200Annotation score:
A0A0B4J236A0A0B4J236_HUMAN
Mevalonate kinase (Mevalonic acidur...
MVK hCG_40321
115Annotation score:
A0A1B0GWF3A0A1B0GWF3_HUMAN
Mevalonate kinase
MVK
150Annotation score:
F5H368F5H368_HUMAN
Mevalonate kinase
MVK
117Annotation score:
F5H163F5H163_HUMAN
Mevalonate kinase
MVK
83Annotation score:
A0A1W2PS16A0A1W2PS16_HUMAN
Mevalonate kinase
MVK
117Annotation score:

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07503612G → R in POROK3. 1 Publication1
Natural variantiVAR_01095620H → N in HIDS. 1 PublicationCorresponds to variant dbSNP:rs11544299Ensembl.1
Natural variantiVAR_00402220H → P in HIDS and MEVA. 3 PublicationsCorresponds to variant dbSNP:rs104895295EnsemblClinVar.1
Natural variantiVAR_02951920H → Q in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895335EnsemblClinVar.1
Natural variantiVAR_01095739L → P in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895296EnsemblClinVar.1
Natural variantiVAR_07503741L → P in POROK3. 1 PublicationCorresponds to variant dbSNP:rs397514571EnsemblClinVar.1
Natural variantiVAR_01095852S → N2 PublicationsCorresponds to variant dbSNP:rs7957619EnsemblClinVar.1
Natural variantiVAR_029520132V → I in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895336EnsemblClinVar.1
Natural variantiVAR_010959135S → L in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895297EnsemblClinVar.1
Natural variantiVAR_010960148A → T in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895298EnsemblClinVar.1
Natural variantiVAR_010961150S → L in HIDS. 1 PublicationCorresponds to variant dbSNP:rs747116992Ensembl.1
Natural variantiVAR_004023167P → L in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895300EnsemblClinVar.1
Natural variantiVAR_029521171G → R in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895337EnsemblClinVar.1
Natural variantiVAR_010962202G → R in HIDS and POROK3. 2 PublicationsCorresponds to variant dbSNP:rs104895301EnsemblClinVar.1
Natural variantiVAR_029522211G → E in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895325EnsemblClinVar.1
Natural variantiVAR_010963215R → Q in HIDS. 2 PublicationsCorresponds to variant dbSNP:rs104895303EnsemblClinVar.1
Natural variantiVAR_010964243T → I in MEVA. 1 PublicationCorresponds to variant dbSNP:rs104895314EnsemblClinVar.1
Natural variantiVAR_029523250V → I in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895339EnsemblClinVar.1
Natural variantiVAR_075038255L → P in POROK3. 1 PublicationCorresponds to variant dbSNP:rs397514570EnsemblClinVar.1
Natural variantiVAR_010965264L → F in MEVA. 2 PublicationsCorresponds to variant dbSNP:rs104895315EnsemblClinVar.1
Natural variantiVAR_010966265L → P in MEVA. 1 PublicationCorresponds to variant dbSNP:rs104895316EnsemblClinVar.1
Natural variantiVAR_029524265L → R in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895316EnsemblClinVar.1
Natural variantiVAR_004024268I → T in HIDS and MEVA. 6 PublicationsCorresponds to variant dbSNP:rs104895304EnsemblClinVar.1
Natural variantiVAR_075039279L → P in POROK3. 1 Publication1
Natural variantiVAR_075040291Y → D in POROK3. 1 Publication1
Natural variantiVAR_004025301N → T in MEVA; diminished activity. 1 PublicationCorresponds to variant dbSNP:rs121917789EnsemblClinVar.1
Natural variantiVAR_010967309G → S in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895305EnsemblClinVar.1
Natural variantiVAR_009068310V → M in MEVA and HIDS. 3 PublicationsCorresponds to variant dbSNP:rs104895319EnsemblClinVar.1
Natural variantiVAR_075041312H → R in POROK3. 1 Publication1
Natural variantiVAR_010968326G → R in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895308EnsemblClinVar.1
Natural variantiVAR_004026334A → T in MEVA. 3 PublicationsCorresponds to variant dbSNP:rs104895317EnsemblClinVar.1
Natural variantiVAR_029525335G → S. Corresponds to variant dbSNP:rs11614976Ensembl.1
Natural variantiVAR_029526356T → M1 PublicationCorresponds to variant dbSNP:rs104895342EnsemblClinVar.1
Natural variantiVAR_075042365F → S in POROK3. 1 PublicationCorresponds to variant dbSNP:rs398122911EnsemblClinVar.1
Natural variantiVAR_075043376G → S in POROK3. 1 PublicationCorresponds to variant dbSNP:rs971159663Ensembl.1
Natural variantiVAR_029527376G → V in HIDS. 1 PublicationCorresponds to variant dbSNP:rs104895340EnsemblClinVar.1
Natural variantiVAR_004027377V → 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
, AF217528, AF217529, AF217530, AF217531, AF217532, AF217533, AF217534 Genomic DNA Translation: AAF82407.1
BC016140 mRNA Translation: AAH16140.1
CCDSiCCDS9132.1
PIRiA42919
RefSeqiNP_000422.1, NM_000431.3
NP_001107657.1, NM_001114185.2
NP_001288111.1, NM_001301182.1
XP_016874803.1, XM_017019314.1
UniGeneiHs.130607

Genome annotation databases

EnsembliENST00000228510; ENSP00000228510; ENSG00000110921
ENST00000539575; ENSP00000443551; ENSG00000110921
GeneIDi4598
KEGGihsa:4598
UCSCiuc009zvk.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

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
, AF217528, AF217529, AF217530, AF217531, AF217532, AF217533, AF217534 Genomic DNA Translation: AAF82407.1
BC016140 mRNA Translation: AAH16140.1
CCDSiCCDS9132.1
PIRiA42919
RefSeqiNP_000422.1, NM_000431.3
NP_001107657.1, NM_001114185.2
NP_001288111.1, NM_001301182.1
XP_016874803.1, XM_017019314.1
UniGeneiHs.130607

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R3VX-ray2.50A/B/C/D1-396[»]
ProteinModelPortaliQ03426
SMRiQ03426
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110683, 17 interactors
IntActiQ03426, 4 interactors
STRINGi9606.ENSP00000228510

Chemistry databases

DrugBankiDB04695 FARNESYL THIOPYROPHOSPHATE
GuidetoPHARMACOLOGYi640
SwissLipidsiSLP:000001240

PTM databases

iPTMnetiQ03426
PhosphoSitePlusiQ03426

Polymorphism and mutation databases

BioMutaiMVK
DMDMi417215

Proteomic databases

EPDiQ03426
MaxQBiQ03426
PaxDbiQ03426
PeptideAtlasiQ03426
PRIDEiQ03426
ProteomicsDBi58211

Protocols and materials databases

DNASUi4598
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228510; ENSP00000228510; ENSG00000110921
ENST00000539575; ENSP00000443551; ENSG00000110921
GeneIDi4598
KEGGihsa:4598
UCSCiuc009zvk.4 human

Organism-specific databases

CTDi4598
DisGeNETi4598
EuPathDBiHostDB:ENSG00000110921.11
GeneCardsiMVK
HGNCiHGNC:7530 MVK
HPAiHPA016961
MalaCardsiMVK
MIMi175900 phenotype
251170 gene
260920 phenotype
610377 phenotype
neXtProtiNX_Q03426
OpenTargetsiENSG00000110921
Orphaneti79152 Disseminated superficial actinic porokeratosis
343 Hyperimmunoglobulinemia D with periodic fever
29 Mevalonic aciduria
735 Porokeratosis of Mibelli
PharmGKBiPA31331
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1511 Eukaryota
COG1577 LUCA
GeneTreeiENSGT00390000011860
HOVERGENiHBG000402
InParanoidiQ03426
KOiK00869
OMAiNTVCTYG
OrthoDBiEOG091G05QV
PhylomeDBiQ03426
TreeFamiTF313775

Enzyme and pathway databases

UniPathwayi
UPA00057;UER00098

BioCyciMetaCyc:ENSG00000110921-MONOMER
BRENDAi2.7.1.36 2681
ReactomeiR-HSA-191273 Cholesterol biosynthesis
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
SABIO-RKiQ03426

Miscellaneous databases

ChiTaRSiMVK human
EvolutionaryTraceiQ03426
GeneWikiiMevalonate_kinase
GenomeRNAii4598
PROiPR:Q03426
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000110921 Expressed in 219 organ(s), highest expression level in C1 segment of cervical spinal cord
CleanExiHS_MVK
ExpressionAtlasiQ03426 baseline and differential
GenevisibleiQ03426 HS

Family and domain databases

Gene3Di3.30.230.10, 1 hit
3.30.70.890, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF08544 GHMP_kinases_C, 1 hit
PF00288 GHMP_kinases_N, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
SSF55060 SSF55060, 1 hit
TIGRFAMsiTIGR00549 mevalon_kin, 1 hit
PROSITEiView protein in PROSITE
PS00627 GHMP_KINASES_ATP, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiKIME_HUMAN
AccessioniPrimary (citable) accession number: Q03426
Entry historyiIntegrated 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

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