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Protein

Phosphomevalonate kinase

Gene

PMVK

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

Functioni

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 (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 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

  • cholesterol biosynthetic process Source: UniProtKB
  • isopentenyl diphosphate biosynthetic process, mevalonate pathway Source: GO_Central
  • response to cholesterol Source: UniProtKB
  • sterol biosynthetic process Source: UniProtKB
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:HS08830-MONOMER.
ZFISH:HS08830-MONOMER.
BRENDAi2.7.4.2. 2681.
ReactomeiR-HSA-191273. Cholesterol biosynthesis.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
SABIO-RKQ15126.
UniPathwayiUPA00057; 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

HGNCiHGNC:9141. PMVK.

Subcellular locationi

  • Peroxisome 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Involvement in diseasei

Porokeratosis 1, multiple types (POROK1)1 Publication
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

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.
MIMi175800. phenotype.
OpenTargetsiENSG00000163344.
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.

2D gel databases

REPRODUCTION-2DPAGEIPI00220648.

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.
CleanExiHS_PMVK.
ExpressionAtlasiQ15126. baseline and differential.
GenevisibleiQ15126. HS.

Organism-specific databases

HPAiHPA029900.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi115897. 24 interactors.
IntActiQ15126. 2 interactors.
MINTiMINT-7034566.
STRINGi9606.ENSP00000357452.

Structurei

Secondary structure

1192
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 16Combined sources8
Helixi22 – 33Combined sources12
Turni35 – 37Combined sources3
Beta strandi38 – 41Combined sources4
Helixi44 – 53Combined sources10
Turni54 – 56Combined sources3
Helixi72 – 86Combined sources15
Turni88 – 91Combined sources4
Helixi92 – 95Combined sources4
Beta strandi102 – 106Combined sources5
Helixi112 – 122Combined sources11
Helixi123 – 125Combined sources3
Beta strandi126 – 133Combined sources8
Helixi135 – 140Combined sources6
Turni147 – 151Combined sources5
Helixi153 – 156Combined sources4
Turni157 – 160Combined sources4
Beta strandi165 – 170Combined sources6
Helixi174 – 189Combined sources16

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...

Miscellaneous databases

EvolutionaryTraceiQ15126.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi190 – 192Microbody targeting signalSequence analysis3

Phylogenomic databases

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

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005919. Pmev_kin_anim.
[Graphical view]
PANTHERiPTHR13101. PTHR13101. 1 hit.
PfamiPF04275. P-mevalo_kinase. 1 hit.
[Graphical view]
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 → M.1 PublicationCorresponds to variant rs16836525dbSNPEnsembl.1

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

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. 24 interactors.
IntActiQ15126. 2 interactors.
MINTiMINT-7034566.
STRINGi9606.ENSP00000357452.

Chemistry databases

GuidetoPHARMACOLOGYi641.
SwissLipidsiSLP:000001241.

PTM databases

iPTMnetiQ15126.
PhosphoSitePlusiQ15126.

Polymorphism and mutation databases

BioMutaiPMVK.
DMDMi3024422.

2D gel databases

REPRODUCTION-2DPAGEIPI00220648.

Proteomic databases

EPDiQ15126.
PaxDbiQ15126.
PeptideAtlasiQ15126.
PRIDEiQ15126.

Protocols and materials databases

DNASUi10654.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368467; ENSP00000357452; ENSG00000163344.
GeneIDi10654.
KEGGihsa:10654.

Organism-specific databases

CTDi10654.
DisGeNETi10654.
GeneCardsiPMVK.
HGNCiHGNC:9141. PMVK.
HPAiHPA029900.
MIMi175800. phenotype.
607622. gene.
neXtProtiNX_Q15126.
OpenTargetsiENSG00000163344.
PharmGKBiPA33465.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00057; UER00099.
BioCyciMetaCyc:HS08830-MONOMER.
ZFISH:HS08830-MONOMER.
BRENDAi2.7.4.2. 2681.
ReactomeiR-HSA-191273. Cholesterol biosynthesis.
R-HSA-2426168. Activation of gene expression by SREBF (SREBP).
SABIO-RKQ15126.

Miscellaneous databases

ChiTaRSiPMVK. human.
EvolutionaryTraceiQ15126.
GenomeRNAii10654.
PROiQ15126.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163344.
CleanExiHS_PMVK.
ExpressionAtlasiQ15126. baseline and differential.
GenevisibleiQ15126. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005919. Pmev_kin_anim.
[Graphical view]
PANTHERiPTHR13101. PTHR13101. 1 hit.
PfamiPF04275. P-mevalo_kinase. 1 hit.
[Graphical view]
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 historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 149 of the entry and version 3 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 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

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.