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Q15126

- PMVK_HUMAN

UniProt

Q15126 - PMVK_HUMAN

Protein

Phosphomevalonate kinase

Gene

PMVK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    Vmax=46.4 µmol/min/mg enzyme with (R)-5-phosphomevalonate as substrate2 Publications

    Vmax=52 µmol/min/mg enzyme with ATP as substrate2 Publications

    Pathwayi

    Sites

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

    Regions

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

    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

    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. membrane Source: UniProtKB
    4. peroxisome Source: UniProtKB

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15126.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi190 – 1923Microbody targeting signalSequence Analysis

    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

    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: October 1, 2014
    This is version 128 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