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Protein

Phosphomevalonate kinase

Gene

PMVK

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

Functioni

Caution

Was originally thought to be located in the peroxisome (PubMed:10191291). However, was later shown to be cytosolic (PubMed:14729858, PubMed:27052676).1 Publication2 Publications

Catalytic activityi

ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate.1 Publication

Kineticsi

  1. KM=25 µM for (R)-5-phosphomevalonate2 Publications
  2. KM=0.26 mM for ATP2 Publications
  1. Vmax=46.4 µmol/min/mg enzyme with (R)-5-phosphomevalonate as substrate2 Publications
  2. Vmax=52 µmol/min/mg enzyme with ATP as substrate2 Publications

Pathwayi: isopentenyl diphosphate biosynthesis via mevalonate pathway

This protein is involved in step 2 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 sitei141ATP2 Publications1
Binding sitei170Substrate1 Publication1
Binding sitei171ATP1 Publication1
Binding sitei176ATP1 Publication1
Binding sitei180ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi17 – 23ATP2 Publications7

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • phosphomevalonate kinase activity Source: UniProtKB

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, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08830-MONOMER
BRENDAi2.7.4.2 2681
ReactomeiR-HSA-191273 Cholesterol biosynthesis
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
SABIO-RKiQ15126
UniPathwayi
UPA00057;UER00099

Chemistry databases

SwissLipidsiSLP:000001241

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomevalonate kinase (EC:2.7.4.2)
Short name:
PMKase
Short name:
hPMK
Gene namesi
Name:PMVK
Synonyms:PMKI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000163344.5
HGNCiHGNC:9141 PMVK
MIMi607622 gene
neXtProtiNX_Q15126

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

Pathology & Biotechi

Involvement in diseasei

Porokeratosis 1, multiple types (POROK1)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:175800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07505169K → E in POROK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_080138138 – 192Missing in POROK1; results in reduced expression and solubility; disturbs subcellular localization with punctate rather than diffuse cytoplasmic distribution. 1 PublicationAdd BLAST55

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi17K → M: Approximately 8-fold decrease in Vmax for MgATP and R-MVP. Approximately 5-fold increase in Km for MgATP and R-MVP. 1 Publication1
Mutagenesisi18R → Q: Approximately 85-fold decrease in Vmax for MgATP and R-MVP. Approximately 5-fold increase in Km for MgATP and R-MVP. 1 Publication1
Mutagenesisi19K → M: Approximately 9-fold decrease in Vmax for MgATP and R-MVP. Approximately 10-fold increase in Km for MgATP and R-MVP. 1 Publication1
Mutagenesisi22K → M: Approximately 100000-fold decrease in Vmax for MgATP. 1 Publication1
Mutagenesisi23D → N: Approximately 7-fold decrease in Vmax for MgATP and R-MVP. Approximately 10-fold increase in Km for MgATP and 5-fold increase in Km for R-MVP. 1 Publication1
Mutagenesisi48K → M: Approximately 1400-fold decrease in Vmax for MgATP and R-MVP. Approximately 3-fold increase in Km for MgATP and R-MVP. 1 Publication1
Mutagenesisi69K → M: Approximately 500-fold decrease in Vmax for MgATP and R-MVP. Approximately 3-fold increase in Km for MgATP and R-MVP. 1 Publication1
Mutagenesisi73R → M: Approximately 3000-fold decrease in Vmax for MgATP and R-MVP. No change in Km for MgATP and approximately 3-fold increase in Km for R-MVP. 1 Publication1
Mutagenesisi84R → M: Approximately 10-fold decrease in Vmax for MgATP and R-MVP. Approximately 3-fold increase in Km for MgATP and 50-fold increase in Km for R-MVP. 1 Publication1
Mutagenesisi93R → M: Almost no change in Km and Vmax for MgATP and R-MVP. 1
Mutagenesisi110R → M: Approximately 20000-fold decrease in Vmax for MgATP. 1 Publication1
Mutagenesisi111R → M: Approximately 65-fold decrease in Vmax for MgATP and R-MVP. Approximately 8-fold increase in Km for MgATP and 60-fold increase in Km for R-MVP. 1 Publication1
Mutagenesisi130R → M: Approximately 4-fold decrease in Vmax for MgATP and R-MVP. Approximately 3-fold increase in Km for MgATP and R-MVP. 1
Mutagenesisi138R → M: Approximately 3-fold decrease in Vmax for MgATP and R-MVP. Approximately 5-fold increase in Km for MgATP and no change in Km for R-MVP. 1
Mutagenesisi141R → M: Approximately 15-fold decrease in Vmax for MgATP and R-MVP. Approximately 50-fold increase in Km for MgATP and approximately 7-fold in Km for R-MVP. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi10654
MalaCardsiPMVK
MIMi175800 phenotype
OpenTargetsiENSG00000163344
Orphaneti735 Porokeratosis of Mibelli
PharmGKBiPA33465

Chemistry databases

GuidetoPHARMACOLOGYi641

Polymorphism and mutation databases

BioMutaiPMVK
DMDMi3024422

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000584721 – 192Phosphomevalonate kinaseAdd BLAST192

Proteomic databases

EPDiQ15126
PaxDbiQ15126
PeptideAtlasiQ15126
PRIDEiQ15126
ProteomicsDBi60453

2D gel databases

REPRODUCTION-2DPAGEiIPI00220648

PTM databases

iPTMnetiQ15126
PhosphoSitePlusiQ15126

Expressioni

Tissue specificityi

Heart, liver, skeletal muscle, kidney, and pancreas. Lower level in brain, placenta and lung.1 Publication

Inductioni

By sterol.1 Publication

Gene expression databases

BgeeiENSG00000163344 Expressed in 225 organ(s), highest expression level in nucleus accumbens
CleanExiHS_PMVK
ExpressionAtlasiQ15126 baseline and differential
GenevisibleiQ15126 HS

Organism-specific databases

HPAiHPA029900

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi115897, 31 interactors
IntActiQ15126, 6 interactors
STRINGi9606.ENSP00000357452

Structurei

Secondary structure

1192
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ15126
SMRiQ15126
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15126

Family & Domainsi

Phylogenomic databases

eggNOGiENOG410IZWN Eukaryota
ENOG4111IXB LUCA
GeneTreeiENSGT00390000014801
HOGENOMiHOG000261666
HOVERGENiHBG003277
InParanoidiQ15126
KOiK13273
OMAiNDIKWFR
OrthoDBiEOG091G0PNO
PhylomeDBiQ15126
TreeFamiTF312935

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR005919 Pmev_kin_anim
PANTHERiPTHR13101 PTHR13101, 1 hit
PfamiView protein in Pfam
PF04275 P-mevalo_kinase, 1 hit
PIRSFiPIRSF036639 PMK_anim, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01223 Pmev_kin_anim, 1 hit

Sequencei

Sequence statusi: Complete.

Q15126-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPLGGAPRL VLLFSGKRKS GKDFVTEALQ SRLGADVCAV LRLSGPLKEQ
60 70 80 90 100
YAQEHGLNFQ RLLDTSTYKE AFRKDMIRWG EEKRQADPGF FCRKIVEGIS
110 120 130 140 150
QPIWLVSDTR RVSDIQWFRE AYGAVTQTVR VVALEQSRQQ RGWVFTPGVD
160 170 180 190
DAESECGLDN FGDFDWVIEN HGVEQRLEEQ LENLIEFIRS RL
Length:192
Mass (Da):21,995
Last modified:January 23, 2007 - v3
Checksum:iD7E720D0DDCCA249
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07505169K → E in POROK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_051283125V → M1 PublicationCorresponds to variant dbSNP:rs16836525Ensembl.1
Natural variantiVAR_080138138 – 192Missing in POROK1; results in reduced expression and solubility; disturbs subcellular localization with punctate rather than diffuse cytoplasmic distribution. 1 PublicationAdd BLAST55

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77213 mRNA Translation: AAC37593.1
BT019976 mRNA Translation: AAV38779.1
BC006089 mRNA Translation: AAH06089.1
BC007694 mRNA Translation: AAH07694.1
AF026069 Genomic DNA Translation: AAC60791.1
CCDSiCCDS1073.1
RefSeqiNP_006547.1, NM_006556.3
UniGeneiHs.30954

Genome annotation databases

EnsembliENST00000368467; ENSP00000357452; ENSG00000163344
GeneIDi10654
KEGGihsa:10654

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77213 mRNA Translation: AAC37593.1
BT019976 mRNA Translation: AAV38779.1
BC006089 mRNA Translation: AAH06089.1
BC007694 mRNA Translation: AAH07694.1
AF026069 Genomic DNA Translation: AAC60791.1
CCDSiCCDS1073.1
RefSeqiNP_006547.1, NM_006556.3
UniGeneiHs.30954

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CH4X-ray1.76B1-192[»]
ProteinModelPortaliQ15126
SMRiQ15126
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115897, 31 interactors
IntActiQ15126, 6 interactors
STRINGi9606.ENSP00000357452

Chemistry databases

GuidetoPHARMACOLOGYi641
SwissLipidsiSLP:000001241

PTM databases

iPTMnetiQ15126
PhosphoSitePlusiQ15126

Polymorphism and mutation databases

BioMutaiPMVK
DMDMi3024422

2D gel databases

REPRODUCTION-2DPAGEiIPI00220648

Proteomic databases

EPDiQ15126
PaxDbiQ15126
PeptideAtlasiQ15126
PRIDEiQ15126
ProteomicsDBi60453

Protocols and materials databases

DNASUi10654
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368467; ENSP00000357452; ENSG00000163344
GeneIDi10654
KEGGihsa:10654

Organism-specific databases

CTDi10654
DisGeNETi10654
EuPathDBiHostDB:ENSG00000163344.5
GeneCardsiPMVK
HGNCiHGNC:9141 PMVK
HPAiHPA029900
MalaCardsiPMVK
MIMi175800 phenotype
607622 gene
neXtProtiNX_Q15126
OpenTargetsiENSG00000163344
Orphaneti735 Porokeratosis of Mibelli
PharmGKBiPA33465
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IZWN Eukaryota
ENOG4111IXB LUCA
GeneTreeiENSGT00390000014801
HOGENOMiHOG000261666
HOVERGENiHBG003277
InParanoidiQ15126
KOiK13273
OMAiNDIKWFR
OrthoDBiEOG091G0PNO
PhylomeDBiQ15126
TreeFamiTF312935

Enzyme and pathway databases

UniPathwayi
UPA00057;UER00099

BioCyciMetaCyc:HS08830-MONOMER
BRENDAi2.7.4.2 2681
ReactomeiR-HSA-191273 Cholesterol biosynthesis
R-HSA-2426168 Activation of gene expression by SREBF (SREBP)
SABIO-RKiQ15126

Miscellaneous databases

ChiTaRSiPMVK human
EvolutionaryTraceiQ15126
GenomeRNAii10654
PROiPR:Q15126
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163344 Expressed in 225 organ(s), highest expression level in nucleus accumbens
CleanExiHS_PMVK
ExpressionAtlasiQ15126 baseline and differential
GenevisibleiQ15126 HS

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR005919 Pmev_kin_anim
PANTHERiPTHR13101 PTHR13101, 1 hit
PfamiView protein in Pfam
PF04275 P-mevalo_kinase, 1 hit
PIRSFiPIRSF036639 PMK_anim, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01223 Pmev_kin_anim, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPMVK_HUMAN
AccessioniPrimary (citable) accession number: Q15126
Secondary accession number(s): Q5TZW9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 165 of the entry and version 3 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. Human chromosome 1
    Human chromosome 1: 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
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Main funding by: National Institutes of Health

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