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Q15126

- PMVK_HUMAN

UniProt

Q15126 - PMVK_HUMAN

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Protein

Phosphomevalonate kinase

Gene
PMVK, PMKI
Organism
Homo sapiens (Human)
Status
Reviewed - 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 ATP

Vmax=46.4 µmol/min/mg enzyme with (R)-5-phosphomevalonate as substrate

Vmax=52 µmol/min/mg enzyme with ATP as substrate

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei141 – 1411ATP Inferred
Binding sitei170 – 1701Substrate
Binding sitei171 – 1711ATP Inferred
Binding sitei176 – 1761ATP Inferred
Binding sitei180 – 1801ATP Inferred

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 237ATP Inferred

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. phosphomevalonate kinase activity Source: UniProtKB

GO - Biological processi

  1. cholesterol biosynthetic process Source: UniProtKB
  2. isopentenyl diphosphate biosynthetic process, mevalonate pathway Source: UniProtKB-UniPathway
  3. response to cholesterol Source: UniProtKB
  4. small molecule metabolic process Source: Reactome
  5. 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.
BRENDAi2.7.4.2. 2681.
ReactomeiREACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.
SABIO-RKQ15126.
UniPathwayiUPA00057; UER00099.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9141. PMVK.

Subcellular locationi

Peroxisome 1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi17 – 171K → M: Approximately 8-fold decrease in Vmax for MgATP and R-MVP. Approximately 5-fold increase in Km for MgATP and R-MVP. 1 Publication
Mutagenesisi18 – 181R → Q: Approximately 85-fold decrease in Vmax for MgATP and R-MVP. Approximately 5-fold increase in Km for MgATP and R-MVP. 1 Publication
Mutagenesisi19 – 191K → M: Approximately 9-fold decrease in Vmax for MgATP and R-MVP. Approximately 10-fold increase in Km for MgATP and R-MVP. 1 Publication
Mutagenesisi22 – 221K → M: Approximately 100000-fold decrease in Vmax for MgATP. 1 Publication
Mutagenesisi23 – 231D → 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 Publication
Mutagenesisi48 – 481K → M: Approximately 1400-fold decrease in Vmax for MgATP and R-MVP. Approximately 3-fold increase in Km for MgATP and R-MVP. 1 Publication
Mutagenesisi69 – 691K → M: Approximately 500-fold decrease in Vmax for MgATP and R-MVP. Approximately 3-fold increase in Km for MgATP and R-MVP. 1 Publication
Mutagenesisi73 – 731R → 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 Publication
Mutagenesisi84 – 841R → 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 Publication
Mutagenesisi93 – 931R → M: Almost no change in Km and Vmax for MgATP and R-MVP.
Mutagenesisi110 – 1101R → M: Approximately 20000-fold decrease in Vmax for MgATP. 1 Publication
Mutagenesisi111 – 1111R → 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 Publication
Mutagenesisi130 – 1301R → M: Approximately 4-fold decrease in Vmax for MgATP and R-MVP. Approximately 3-fold increase in Km for MgATP and R-MVP.
Mutagenesisi138 – 1381R → 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.
Mutagenesisi141 – 1411R → 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 Publication

Organism-specific databases

PharmGKBiPA33465.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192Phosphomevalonate kinasePRO_0000058472Add
BLAST

Proteomic databases

MaxQBiQ15126.
PaxDbiQ15126.
PeptideAtlasiQ15126.
PRIDEiQ15126.

2D gel databases

REPRODUCTION-2DPAGEIPI00220648.

PTM databases

PhosphoSiteiQ15126.

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

ArrayExpressiQ15126.
BgeeiQ15126.
CleanExiHS_PMVK.
GenevestigatoriQ15126.

Organism-specific databases

HPAiHPA029900.

Interactioni

Subunit structurei

Monomer By similarity.

Protein-protein interaction databases

BioGridi115897. 10 interactions.
IntActiQ15126. 2 interactions.
MINTiMINT-7034566.
STRINGi9606.ENSP00000357452.

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 168
Helixi22 – 3312
Turni35 – 373
Beta strandi38 – 414
Helixi44 – 5310
Turni54 – 563
Helixi72 – 8615
Turni88 – 914
Helixi92 – 954
Beta strandi102 – 1065
Helixi112 – 12211
Helixi123 – 1253
Beta strandi126 – 1338
Helixi135 – 1406
Turni147 – 1515
Helixi153 – 1564
Turni157 – 1604
Beta strandi165 – 1706
Helixi174 – 18916

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CH4X-ray1.76B1-192[»]
ProteinModelPortaliQ15126.
SMRiQ15126. Positions 1-192.

Miscellaneous databases

EvolutionaryTraceiQ15126.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi190 – 1923Microbody targeting signal Reviewed prediction

Phylogenomic databases

eggNOGiNOG71763.
HOGENOMiHOG000261666.
HOVERGENiHBG003277.
InParanoidiQ15126.
KOiK13273.
OMAiRISEPIK.
OrthoDBiEOG7Z95NC.
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

MAPLGGAPRL VLLFSGKRKS GKDFVTEALQ SRLGADVCAV LRLSGPLKEQ    50
YAQEHGLNFQ RLLDTSTYKE AFRKDMIRWG EEKRQADPGF FCRKIVEGIS 100
QPIWLVSDTR RVSDIQWFRE AYGAVTQTVR VVALEQSRQQ RGWVFTPGVD 150
DAESECGLDN FGDFDWVIEN HGVEQRLEEQ LENLIEFIRS RL 192
Length:192
Mass (Da):21,995
Last modified:January 23, 2007 - v3
Checksum:iD7E720D0DDCCA249
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti125 – 1251V → M.1 Publication
Corresponds to variant rs16836525 [ dbSNP | Ensembl ].
VAR_051283

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UCSCiuc001ffq.3. human.

Polymorphism databases

DMDMi3024422.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS1073.1.
RefSeqi NP_006547.1. NM_006556.3.
UniGenei Hs.30954.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CH4 X-ray 1.76 B 1-192 [» ]
ProteinModelPortali Q15126.
SMRi Q15126. Positions 1-192.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115897. 10 interactions.
IntActi Q15126. 2 interactions.
MINTi MINT-7034566.
STRINGi 9606.ENSP00000357452.

Chemistry

GuidetoPHARMACOLOGYi 641.

PTM databases

PhosphoSitei Q15126.

Polymorphism databases

DMDMi 3024422.

2D gel databases

REPRODUCTION-2DPAGE IPI00220648.

Proteomic databases

MaxQBi Q15126.
PaxDbi Q15126.
PeptideAtlasi Q15126.
PRIDEi Q15126.

Protocols and materials databases

DNASUi 10654.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368467 ; ENSP00000357452 ; ENSG00000163344 .
GeneIDi 10654.
KEGGi hsa:10654.
UCSCi uc001ffq.3. human.

Organism-specific databases

CTDi 10654.
GeneCardsi GC01M154897.
HGNCi HGNC:9141. PMVK.
HPAi HPA029900.
MIMi 607622. gene.
neXtProti NX_Q15126.
PharmGKBi PA33465.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG71763.
HOGENOMi HOG000261666.
HOVERGENi HBG003277.
InParanoidi Q15126.
KOi K13273.
OMAi RISEPIK.
OrthoDBi EOG7Z95NC.
PhylomeDBi Q15126.
TreeFami TF312935.

Enzyme and pathway databases

UniPathwayi UPA00057 ; UER00099 .
BioCyci MetaCyc:HS08830-MONOMER.
BRENDAi 2.7.4.2. 2681.
Reactomei REACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.
SABIO-RK Q15126.

Miscellaneous databases

ChiTaRSi PMVK. human.
EvolutionaryTracei Q15126.
GenomeRNAii 10654.
NextBioi 40503.
PROi Q15126.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15126.
Bgeei Q15126.
CleanExi HS_PMVK.
Genevestigatori Q15126.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005919. Pmev_kin_anim.
[Graphical view ]
PANTHERi PTHR13101. PTHR13101. 1 hit.
Pfami PF04275. P-mevalo_kinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036639. PMK_anim. 1 hit.
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01223. Pmev_kin_anim. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of human phosphomevalonate kinase and identification of a consensus peroxisomal targeting sequence."
    Chambliss K.L., Slaughter C.A., Schreiner R., Hoffmann G.F., Gibson K.M.
    J. Biol. Chem. 271:17330-17334(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-125.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin and Uterus.
  4. "Characterization of phosphomevalonate kinase: chromosomal localization, regulation, and subcellular targeting."
    Olivier L.M., Chambliss K.L., Gibson K.M., Krisans S.K.
    J. Lipid Res. 40:672-679(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-192, INDUCTION, SUBCELLULAR LOCATION.
  5. "Post-translational regulation of mevalonate kinase by intermediates of the cholesterol and nonsterol isoprene biosynthetic pathways."
    Hinson D.D., Chambliss K.L., Toth M.J., Tanaka R.D., Gibson K.M.
    J. Lipid Res. 38:2216-2223(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  6. "Phosphomevalonate kinase: functional investigation of the recombinant human enzyme."
    Herdendorf T.J., Miziorko H.M.
    Biochemistry 45:3235-3242(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-17; ARG-18; LYS-19; LYS-22 AND ASP-23, BIOPHYSICOCHEMICAL PROPERTIES.
  7. "Functional evaluation of conserved basic residues in human phosphomevalonate kinase."
    Herdendorf T.J., Miziorko H.M.
    Biochemistry 46:11780-11788(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-48; LYS-69; ARG-73; ARG-84; ARG-110; ARG-111 AND ARG-141.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structure of human phosphomevalonate kinase at 1.8 A resolution."
    Chang Q., Yan X.-X., Gu S.-Y., Liu J.-F., Liang D.-C.
    Proteins 73:254-258(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS).

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: September 3, 2014
This is version 127 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

External Data

Dasty 3

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