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Protein

Mevalonate kinase

Gene

MVK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be a regulatory site in cholesterol biosynthetic pathway.

Catalytic activityi

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

Enzyme regulationi

Farnesyl- and geranyl-pyrophosphates are competitive inhibitors.

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 (MVK), Mevalonate kinase (MVK), Mevalonate kinase (MVK), Mevalonate kinase, Mevalonate kinase
  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 sitei55ATPBy similarity1
Binding sitei135ATPBy similarity1
Active sitei204Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi138 – 148ATPBy similarityAdd BLAST11

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • mevalonate kinase activity Source: UniProtKB

GO - Biological processi

  • cholesterol biosynthetic process Source: UniProtKB
  • isopentenyl diphosphate biosynthetic process, mevalonate pathway Source: GO_Central
  • isoprenoid biosynthetic process Source: UniProtKB
  • negative regulation of inflammatory response Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Cholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000110921-MONOMER.
ZFISH:ENSG00000110921-MONOMER.
BRENDAi2.7.1.36. 2681.
ReactomeiR-HSA-191273. Cholesterol biosynthesis.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
SABIO-RKQ03426.
UniPathwayiUPA00057; UER00098.

Chemistry databases

SwissLipidsiSLP:000001240.

Names & Taxonomyi

Protein namesi
Recommended name:
Mevalonate kinase (EC:2.7.1.36)
Short name:
MK
Gene namesi
Name:MVK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:7530. MVK.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

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_00402220H → P in HIDS and MEVA. 3 PublicationsCorresponds to variant rs104895295dbSNPEnsembl.1
Natural variantiVAR_010964243T → I in MEVA. 1 PublicationCorresponds to variant rs104895314dbSNPEnsembl.1
Natural variantiVAR_010965264L → F in MEVA. 2 PublicationsCorresponds to variant rs104895315dbSNPEnsembl.1
Natural variantiVAR_010966265L → P in MEVA. 1 PublicationCorresponds to variant rs104895316dbSNPEnsembl.1
Natural variantiVAR_004024268I → T in HIDS and MEVA. 6 PublicationsCorresponds to variant rs104895304dbSNPEnsembl.1
Natural variantiVAR_004025301N → T in MEVA; diminished activity. 1 PublicationCorresponds to variant rs28934896dbSNPEnsembl.1
Natural variantiVAR_009068310V → M in MEVA and HIDS. 3 PublicationsCorresponds to variant rs104895319dbSNPEnsembl.1
Natural variantiVAR_004026334A → T in MEVA. 3 PublicationsCorresponds to variant rs104895317dbSNPEnsembl.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 rs11544299dbSNPEnsembl.1
Natural variantiVAR_00402220H → P in HIDS and MEVA. 3 PublicationsCorresponds to variant rs104895295dbSNPEnsembl.1
Natural variantiVAR_02951920H → Q in HIDS. 1 PublicationCorresponds to variant rs104895335dbSNPEnsembl.1
Natural variantiVAR_01095739L → P in HIDS. 2 PublicationsCorresponds to variant rs104895296dbSNPEnsembl.1
Natural variantiVAR_029520132V → I in HIDS. 1 PublicationCorresponds to variant rs104895336dbSNPEnsembl.1
Natural variantiVAR_010959135S → L in HIDS. 1 PublicationCorresponds to variant rs104895297dbSNPEnsembl.1
Natural variantiVAR_010960148A → T in HIDS. 2 PublicationsCorresponds to variant rs104895298dbSNPEnsembl.1
Natural variantiVAR_010961150S → L in HIDS. 1 PublicationCorresponds to variant rs747116992dbSNPEnsembl.1
Natural variantiVAR_004023167P → L in HIDS. 2 PublicationsCorresponds to variant rs104895300dbSNPEnsembl.1
Natural variantiVAR_029521171G → R in HIDS. 1 PublicationCorresponds to variant rs104895337dbSNPEnsembl.1
Natural variantiVAR_010962202G → R in HIDS and POROK3. 2 PublicationsCorresponds to variant rs104895301dbSNPEnsembl.1
Natural variantiVAR_029522211G → E in HIDS. 1 PublicationCorresponds to variant rs104895325dbSNPEnsembl.1
Natural variantiVAR_010963215R → Q in HIDS. 2 PublicationsCorresponds to variant rs104895303dbSNPEnsembl.1
Natural variantiVAR_029523250V → I in HIDS. 1 PublicationCorresponds to variant rs104895339dbSNPEnsembl.1
Natural variantiVAR_029524265L → R in HIDS. 1 PublicationCorresponds to variant rs104895316dbSNPEnsembl.1
Natural variantiVAR_004024268I → T in HIDS and MEVA. 6 PublicationsCorresponds to variant rs104895304dbSNPEnsembl.1
Natural variantiVAR_010967309G → S in HIDS. 1 PublicationCorresponds to variant rs104895305dbSNPEnsembl.1
Natural variantiVAR_009068310V → M in MEVA and HIDS. 3 PublicationsCorresponds to variant rs104895319dbSNPEnsembl.1
Natural variantiVAR_010968326G → R in HIDS. 1 PublicationCorresponds to variant rs104895308dbSNPEnsembl.1
Natural variantiVAR_029527376G → V in HIDS. 1 PublicationCorresponds to variant rs104895340dbSNPEnsembl.1
Natural variantiVAR_004027377V → I in HIDS; most frequent mutation. 5 PublicationsCorresponds to variant rs28934897dbSNPEnsembl.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 rs397514571dbSNPEnsembl.1
Natural variantiVAR_010962202G → R in HIDS and POROK3. 2 PublicationsCorresponds to variant rs104895301dbSNPEnsembl.1
Natural variantiVAR_075038255L → P in POROK3. 1 PublicationCorresponds to variant rs397514570dbSNPEnsembl.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 rs398122911dbSNPEnsembl.1
Natural variantiVAR_075043376G → S in POROK3. 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.
PharmGKBiPA31331.

Chemistry databases

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.

PTM databases

iPTMnetiQ03426.
PhosphoSitePlusiQ03426.

Expressioni

Gene expression databases

BgeeiENSG00000110921.
CleanExiHS_MVK.
ExpressionAtlasiQ03426. baseline and differential.
GenevisibleiQ03426. HS.

Organism-specific databases

HPAiHPA016961.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-740630,EBI-740630
POT1Q9NUX52EBI-740630,EBI-752420

Protein-protein interaction databases

BioGridi110683. 16 interactors.
IntActiQ03426. 3 interactors.
MINTiMINT-1473671.
STRINGi9606.ENSP00000228510.

Structurei

Secondary structure

1396
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 17Combined sources14
Turni19 – 21Combined sources3
Helixi22 – 24Combined sources3
Beta strandi28 – 43Combined sources16
Beta strandi45 – 52Combined sources8
Turni54 – 56Combined sources3
Beta strandi59 – 63Combined sources5
Helixi64 – 69Combined sources6
Helixi85 – 95Combined sources11
Helixi103 – 119Combined sources17
Beta strandi122 – 125Combined sources4
Beta strandi129 – 137Combined sources9
Beta strandi141 – 143Combined sources3
Helixi145 – 160Combined sources16
Turni167 – 171Combined sources5
Beta strandi173 – 175Combined sources3
Helixi179 – 196Combined sources18
Beta strandi197 – 199Combined sources3
Helixi203 – 210Combined sources8
Beta strandi212 – 216Combined sources5
Beta strandi221 – 223Combined sources3
Beta strandi230 – 236Combined sources7
Helixi243 – 256Combined sources14
Helixi258 – 283Combined sources26
Helixi288 – 307Combined sources20
Helixi313 – 323Combined sources11
Turni324 – 326Combined sources3
Beta strandi328 – 331Combined sources4
Beta strandi336 – 343Combined sources8
Helixi350 – 361Combined sources12
Turni362 – 364Combined sources3
Beta strandi366 – 373Combined sources8
Beta strandi377 – 380Combined sources4
Helixi387 – 392Combined sources6

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...

Miscellaneous databases

EvolutionaryTraceiQ03426.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1511. Eukaryota.
COG1577. LUCA.
GeneTreeiENSGT00390000011860.
HOVERGENiHBG000402.
InParanoidiQ03426.
KOiK00869.
OMAiNRWTKED.
OrthoDBiEOG091G05QV.
PhylomeDBiQ03426.
TreeFamiTF313775.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
InterProiIPR013750. GHMP_kinase_C_dom.
IPR006204. GHMP_kinase_N_dom.
IPR006203. GHMP_knse_ATP-bd_CS.
IPR006205. Mev_gal_kin.
IPR006206. Mevalonate/galactokinase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10457. PTHR10457. 1 hit.
PTHR10457:SF4. PTHR10457:SF4. 1 hit.
PfamiPF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PRINTSiPR00959. MEVGALKINASE.
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 1 hit.
TIGRFAMsiTIGR00549. mevalon_kin. 1 hit.
PROSITEiPS00627. GHMP_KINASES_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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 rs11544299dbSNPEnsembl.1
Natural variantiVAR_00402220H → P in HIDS and MEVA. 3 PublicationsCorresponds to variant rs104895295dbSNPEnsembl.1
Natural variantiVAR_02951920H → Q in HIDS. 1 PublicationCorresponds to variant rs104895335dbSNPEnsembl.1
Natural variantiVAR_01095739L → P in HIDS. 2 PublicationsCorresponds to variant rs104895296dbSNPEnsembl.1
Natural variantiVAR_07503741L → P in POROK3. 1 PublicationCorresponds to variant rs397514571dbSNPEnsembl.1
Natural variantiVAR_01095852S → N.2 PublicationsCorresponds to variant rs7957619dbSNPEnsembl.1
Natural variantiVAR_029520132V → I in HIDS. 1 PublicationCorresponds to variant rs104895336dbSNPEnsembl.1
Natural variantiVAR_010959135S → L in HIDS. 1 PublicationCorresponds to variant rs104895297dbSNPEnsembl.1
Natural variantiVAR_010960148A → T in HIDS. 2 PublicationsCorresponds to variant rs104895298dbSNPEnsembl.1
Natural variantiVAR_010961150S → L in HIDS. 1 PublicationCorresponds to variant rs747116992dbSNPEnsembl.1
Natural variantiVAR_004023167P → L in HIDS. 2 PublicationsCorresponds to variant rs104895300dbSNPEnsembl.1
Natural variantiVAR_029521171G → R in HIDS. 1 PublicationCorresponds to variant rs104895337dbSNPEnsembl.1
Natural variantiVAR_010962202G → R in HIDS and POROK3. 2 PublicationsCorresponds to variant rs104895301dbSNPEnsembl.1
Natural variantiVAR_029522211G → E in HIDS. 1 PublicationCorresponds to variant rs104895325dbSNPEnsembl.1
Natural variantiVAR_010963215R → Q in HIDS. 2 PublicationsCorresponds to variant rs104895303dbSNPEnsembl.1
Natural variantiVAR_010964243T → I in MEVA. 1 PublicationCorresponds to variant rs104895314dbSNPEnsembl.1
Natural variantiVAR_029523250V → I in HIDS. 1 PublicationCorresponds to variant rs104895339dbSNPEnsembl.1
Natural variantiVAR_075038255L → P in POROK3. 1 PublicationCorresponds to variant rs397514570dbSNPEnsembl.1
Natural variantiVAR_010965264L → F in MEVA. 2 PublicationsCorresponds to variant rs104895315dbSNPEnsembl.1
Natural variantiVAR_010966265L → P in MEVA. 1 PublicationCorresponds to variant rs104895316dbSNPEnsembl.1
Natural variantiVAR_029524265L → R in HIDS. 1 PublicationCorresponds to variant rs104895316dbSNPEnsembl.1
Natural variantiVAR_004024268I → T in HIDS and MEVA. 6 PublicationsCorresponds to variant rs104895304dbSNPEnsembl.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 rs28934896dbSNPEnsembl.1
Natural variantiVAR_010967309G → S in HIDS. 1 PublicationCorresponds to variant rs104895305dbSNPEnsembl.1
Natural variantiVAR_009068310V → M in MEVA and HIDS. 3 PublicationsCorresponds to variant rs104895319dbSNPEnsembl.1
Natural variantiVAR_075041312H → R in POROK3. 1 Publication1
Natural variantiVAR_010968326G → R in HIDS. 1 PublicationCorresponds to variant rs104895308dbSNPEnsembl.1
Natural variantiVAR_004026334A → T in MEVA. 3 PublicationsCorresponds to variant rs104895317dbSNPEnsembl.1
Natural variantiVAR_029525335G → S.Corresponds to variant rs11614976dbSNPEnsembl.1
Natural variantiVAR_029526356T → M.1 PublicationCorresponds to variant rs104895342dbSNPEnsembl.1
Natural variantiVAR_075042365F → S in POROK3. 1 PublicationCorresponds to variant rs398122911dbSNPEnsembl.1
Natural variantiVAR_075043376G → S in POROK3. 1 Publication1
Natural variantiVAR_029527376G → V in HIDS. 1 PublicationCorresponds to variant rs104895340dbSNPEnsembl.1
Natural variantiVAR_004027377V → I in HIDS; most frequent mutation. 5 PublicationsCorresponds to variant rs28934897dbSNPEnsembl.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

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. 16 interactors.
IntActiQ03426. 3 interactors.
MINTiMINT-1473671.
STRINGi9606.ENSP00000228510.

Chemistry databases

GuidetoPHARMACOLOGYi640.
SwissLipidsiSLP:000001240.

PTM databases

iPTMnetiQ03426.
PhosphoSitePlusiQ03426.

Polymorphism and mutation databases

BioMutaiMVK.
DMDMi417215.

Proteomic databases

EPDiQ03426.
MaxQBiQ03426.
PaxDbiQ03426.
PeptideAtlasiQ03426.
PRIDEiQ03426.

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.
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.
PharmGKBiPA31331.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1511. Eukaryota.
COG1577. LUCA.
GeneTreeiENSGT00390000011860.
HOVERGENiHBG000402.
InParanoidiQ03426.
KOiK00869.
OMAiNRWTKED.
OrthoDBiEOG091G05QV.
PhylomeDBiQ03426.
TreeFamiTF313775.

Enzyme and pathway databases

UniPathwayiUPA00057; UER00098.
BioCyciMetaCyc:ENSG00000110921-MONOMER.
ZFISH:ENSG00000110921-MONOMER.
BRENDAi2.7.1.36. 2681.
ReactomeiR-HSA-191273. Cholesterol biosynthesis.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
SABIO-RKQ03426.

Miscellaneous databases

ChiTaRSiMVK. human.
EvolutionaryTraceiQ03426.
GeneWikiiMevalonate_kinase.
GenomeRNAii4598.
PROiQ03426.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000110921.
CleanExiHS_MVK.
ExpressionAtlasiQ03426. baseline and differential.
GenevisibleiQ03426. HS.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.30.70.890. 1 hit.
InterProiIPR013750. GHMP_kinase_C_dom.
IPR006204. GHMP_kinase_N_dom.
IPR006203. GHMP_knse_ATP-bd_CS.
IPR006205. Mev_gal_kin.
IPR006206. Mevalonate/galactokinase.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10457. PTHR10457. 1 hit.
PTHR10457:SF4. PTHR10457:SF4. 1 hit.
PfamiPF08544. GHMP_kinases_C. 1 hit.
PF00288. GHMP_kinases_N. 1 hit.
[Graphical view]
PRINTSiPR00959. MEVGALKINASE.
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55060. SSF55060. 1 hit.
TIGRFAMsiTIGR00549. mevalon_kin. 1 hit.
PROSITEiPS00627. GHMP_KINASES_ATP. 1 hit.
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Entry informationi

Entry nameiKIME_HUMAN
AccessioniPrimary (citable) accession number: Q03426
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 30, 2016
This is version 184 of the entry and version 1 of the sequence. [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. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.