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P53602

- MVD1_HUMAN

UniProt

P53602 - MVD1_HUMAN

Protein

Diphosphomevalonate decarboxylase

Gene

MVD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Performs the first committed step in the biosynthesis of isoprenes.

    Catalytic activityi

    ATP + (R)-5-diphosphomevalonate = ADP + phosphate + isopentenyl diphosphate + CO2.1 Publication

    Kineticsi

    1. KM=7.4 µM for (R)-5-diphosphomevalonate1 Publication
    2. KM=0.32 mM for ATP1 Publication

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. diphosphomevalonate decarboxylase activity Source: UniProtKB
    3. Hsp70 protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. cholesterol biosynthetic process Source: UniProtKB
    3. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
    4. dolichyl diphosphate biosynthetic process Source: Reactome
    5. isoprenoid biosynthetic process Source: UniProtKB
    6. positive regulation of cell proliferation Source: UniProtKB
    7. post-translational protein modification Source: Reactome
    8. protein N-linked glycosylation via asparagine Source: Reactome
    9. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Lyase

    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:ENSG00000167508-MONOMER.
    ReactomeiREACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_22230. Synthesis of Dolichyl-phosphate.
    REACT_9405. Cholesterol biosynthesis.
    SABIO-RKP53602.
    UniPathwayiUPA00063.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Diphosphomevalonate decarboxylase (EC:4.1.1.33)
    Alternative name(s):
    Mevalonate (diphospho)decarboxylase
    Short name:
    MDDase
    Mevalonate pyrophosphate decarboxylase
    Gene namesi
    Name:MVD
    Synonyms:MPD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:7529. MVD.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi17 – 171N → A: 15-fold inflation in K(m) for mevalonate diphosphate. 1 Publication
    Mutagenesisi161 – 1611R → Q: 1000-fold diminution in specific activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA31330.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 400399Diphosphomevalonate decarboxylasePRO_0000087012Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei96 – 961Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP53602.
    PaxDbiP53602.
    PRIDEiP53602.

    PTM databases

    PhosphoSiteiP53602.

    Expressioni

    Tissue specificityi

    Expressed in heart, skeletal muscle, lung, liver, brain, pancreas, kidney and placenta.1 Publication

    Gene expression databases

    ArrayExpressiP53602.
    BgeeiP53602.
    CleanExiHS_MVD.
    GenevestigatoriP53602.

    Organism-specific databases

    HPAiHPA041404.
    HPA048250.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi110682. 28 interactions.
    IntActiP53602. 3 interactions.
    MINTiMINT-5004338.
    STRINGi9606.ENSP00000301012.

    Structurei

    Secondary structure

    1
    400
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 145
    Beta strandi17 – 215
    Beta strandi26 – 283
    Turni29 – 324
    Beta strandi33 – 364
    Beta strandi38 – 436
    Turni45 – 473
    Beta strandi50 – 567
    Beta strandi64 – 674
    Helixi77 – 8812
    Beta strandi110 – 1189
    Turni120 – 1223
    Helixi126 – 13914
    Turni140 – 1434
    Helixi149 – 1557
    Helixi157 – 1637
    Beta strandi164 – 1707
    Beta strandi178 – 1803
    Beta strandi183 – 1875
    Helixi189 – 1913
    Beta strandi195 – 2028
    Helixi211 – 22111
    Helixi223 – 2319
    Helixi233 – 24513
    Helixi249 – 26820
    Beta strandi270 – 2723
    Helixi279 – 29517
    Beta strandi300 – 3034
    Beta strandi306 – 3083
    Beta strandi310 – 3156
    Helixi316 – 3183
    Helixi319 – 32911
    Turni337 – 3393
    Beta strandi340 – 3434
    Helixi352 – 3587
    Beta strandi366 – 37510
    Helixi385 – 3873
    Beta strandi392 – 3943

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3D4JX-ray2.40A/B1-400[»]
    ProteinModelPortaliP53602.
    SMRiP53602. Positions 8-396.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53602.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG3407.
    HOVERGENiHBG051503.
    InParanoidiP53602.
    KOiK01597.
    OMAiDTDPPIF.
    OrthoDBiEOG7K0ZCW.
    PhylomeDBiP53602.
    TreeFamiTF105952.

    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.
    IPR005935. Mev_decarb.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    [Graphical view]
    PANTHERiPTHR10977. PTHR10977. 1 hit.
    PfamiPF00288. GHMP_kinases_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF015950. Mev_P_decrbx. 1 hit.
    SUPFAMiSSF54211. SSF54211. 1 hit.
    SSF55060. SSF55060. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P53602-1 [UniParc]FASTAAdd to Basket

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    MASEKPLAAV TCTAPVNIAV IKYWGKRDEE LVLPINSSLS VTLHQDQLKT    50
    TTTAVISKDF TEDRIWLNGR EEDVGQPRLQ ACLREIRCLA RKRRNSRDGD 100
    PLPSSLSCKV HVASVNNFPT AAGLASSAAG YACLAYTLAR VYGVESDLSE 150
    VARRGSGSAC RSLYGGFVEW QMGEQADGKD SIARQVAPES HWPELRVLIL 200
    VVSAEKKLTG STVGMRASVE TSPLLRFRAE SVVPARMAEM ARCIRERDFP 250
    SFAQLTMKDS NQFHATCLDT FPPISYLNAI SWRIIHLVHR FNAHHGDTKV 300
    AYTFDAGPNA VIFTLDDTVA EFVAAVWHGF PPGSNGDTFL KGLQVRPAPL 350
    SAELQAALAM EPTPGGVKYI IVTQVGPGPQ ILDDPCAHLL GPDGLPKPAA 400
    Length:400
    Mass (Da):43,405
    Last modified:October 1, 1996 - v1
    Checksum:i3FD4741BCC4B68D8
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti278 – 2781N → H.
    Corresponds to variant rs34519538 [ dbSNP | Ensembl ].
    VAR_051605

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49260 mRNA. Translation: AAC50440.1.
    BT006930 mRNA. Translation: AAP35576.1.
    CH471184 Genomic DNA. Translation: EAW66792.1.
    BC000011 mRNA. Translation: AAH00011.1.
    CCDSiCCDS10968.1.
    RefSeqiNP_002452.1. NM_002461.1.
    UniGeneiHs.252457.

    Genome annotation databases

    EnsembliENST00000301012; ENSP00000301012; ENSG00000167508.
    GeneIDi4597.
    KEGGihsa:4597.
    UCSCiuc002flf.1. human.

    Polymorphism databases

    DMDMi1706681.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U49260 mRNA. Translation: AAC50440.1 .
    BT006930 mRNA. Translation: AAP35576.1 .
    CH471184 Genomic DNA. Translation: EAW66792.1 .
    BC000011 mRNA. Translation: AAH00011.1 .
    CCDSi CCDS10968.1.
    RefSeqi NP_002452.1. NM_002461.1.
    UniGenei Hs.252457.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3D4J X-ray 2.40 A/B 1-400 [» ]
    ProteinModelPortali P53602.
    SMRi P53602. Positions 8-396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110682. 28 interactions.
    IntActi P53602. 3 interactions.
    MINTi MINT-5004338.
    STRINGi 9606.ENSP00000301012.

    Chemistry

    BindingDBi P53602.
    ChEMBLi CHEMBL4340.
    GuidetoPHARMACOLOGYi 642.

    PTM databases

    PhosphoSitei P53602.

    Polymorphism databases

    DMDMi 1706681.

    Proteomic databases

    MaxQBi P53602.
    PaxDbi P53602.
    PRIDEi P53602.

    Protocols and materials databases

    DNASUi 4597.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301012 ; ENSP00000301012 ; ENSG00000167508 .
    GeneIDi 4597.
    KEGGi hsa:4597.
    UCSCi uc002flf.1. human.

    Organism-specific databases

    CTDi 4597.
    GeneCardsi GC16M088718.
    HGNCi HGNC:7529. MVD.
    HPAi HPA041404.
    HPA048250.
    MIMi 603236. gene.
    neXtProti NX_P53602.
    PharmGKBi PA31330.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3407.
    HOVERGENi HBG051503.
    InParanoidi P53602.
    KOi K01597.
    OMAi DTDPPIF.
    OrthoDBi EOG7K0ZCW.
    PhylomeDBi P53602.
    TreeFami TF105952.

    Enzyme and pathway databases

    UniPathwayi UPA00063 .
    BioCyci MetaCyc:ENSG00000167508-MONOMER.
    Reactomei REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_22230. Synthesis of Dolichyl-phosphate.
    REACT_9405. Cholesterol biosynthesis.
    SABIO-RK P53602.

    Miscellaneous databases

    ChiTaRSi MVD. human.
    EvolutionaryTracei P53602.
    GenomeRNAii 4597.
    NextBioi 17676.
    PROi P53602.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53602.
    Bgeei P53602.
    CleanExi HS_MVD.
    Genevestigatori P53602.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    3.30.70.890. 1 hit.
    InterProi IPR013750. GHMP_kinase_C_dom.
    IPR006204. GHMP_kinase_N_dom.
    IPR005935. Mev_decarb.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    [Graphical view ]
    PANTHERi PTHR10977. PTHR10977. 1 hit.
    Pfami PF00288. GHMP_kinases_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF015950. Mev_P_decrbx. 1 hit.
    SUPFAMi SSF54211. SSF54211. 1 hit.
    SSF55060. SSF55060. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of the cDNAs encoding human and yeast mevalonate pyrophosphate decarboxylase."
      Toth M.J., Huwyler L.
      J. Biol. Chem. 271:7895-7898(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBUNIT, 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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Placenta.
    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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Human mevalonate diphosphate decarboxylase: characterization, investigation of the mevalonate diphosphate binding site, and crystal structure."
      Voynova N.E., Fu Z., Battaile K.P., Herdendorf T.J., Kim J.J., Miziorko H.M.
      Arch. Biochem. Biophys. 480:58-67(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), MUTAGENESIS OF ASN-17 AND ARG-161.

    Entry informationi

    Entry nameiMVD1_HUMAN
    AccessioniPrimary (citable) accession number: P53602
    Secondary accession number(s): Q53Y65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 129 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 16
      Human chromosome 16: 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

    External Data

    Dasty 3