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Q5T2R2

- DPS1_HUMAN

UniProt

Q5T2R2 - DPS1_HUMAN

Protein

Decaprenyl-diphosphate synthase subunit 1

Gene

PDSS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Supplies decaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone-10.1 Publication

    Catalytic activityi

    (2E,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + all-trans-decaprenyl diphosphate.1 Publication

    Cofactori

    Binds 3 magnesium ions per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei134 – 1341Isopentenyl diphosphateBy similarity
    Binding sitei137 – 1371Isopentenyl diphosphateBy similarity
    Binding sitei173 – 1731Isopentenyl diphosphateBy similarity
    Metal bindingi180 – 1801Magnesium 1By similarity
    Metal bindingi180 – 1801Magnesium 2By similarity
    Metal bindingi184 – 1841Magnesium 1By similarity
    Metal bindingi184 – 1841Magnesium 2By similarity
    Binding sitei189 – 1891Polyprenyl diphosphateBy similarity
    Binding sitei190 – 1901Isopentenyl diphosphateBy similarity
    Binding sitei266 – 2661Polyprenyl diphosphateBy similarity
    Binding sitei267 – 2671Polyprenyl diphosphateBy similarity
    Binding sitei304 – 3041Polyprenyl diphosphateBy similarity
    Metal bindingi307 – 3071Magnesium 3By similarity
    Binding sitei321 – 3211Polyprenyl diphosphateBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein heterodimerization activity Source: HGNC
    3. trans-hexaprenyltranstransferase activity Source: Ensembl
    4. trans-octaprenyltranstransferase activity Source: Ensembl

    GO - Biological processi

    1. isoprenoid biosynthetic process Source: HGNC
    2. protein heterotetramerization Source: Ensembl
    3. small molecule metabolic process Source: Reactome
    4. ubiquinone biosynthetic process Source: HGNC

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Isoprene biosynthesis, Ubiquinone biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07530-MONOMER.
    BRENDAi2.5.1.11. 2681.
    ReactomeiREACT_160111. Ubiquinol biosynthesis.
    UniPathwayiUPA00232.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Decaprenyl-diphosphate synthase subunit 1 (EC:2.5.1.91)
    Alternative name(s):
    All-trans-decaprenyl-diphosphate synthase subunit 1
    Decaprenyl pyrophosphate synthase subunit 1
    Trans-prenyltransferase 1
    Short name:
    TPT 1
    Gene namesi
    Name:PDSS1
    Synonyms:DPS1, TPRT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:17759. PDSS1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Coenzyme Q10 deficiency, primary, 2 (COQ10D2) [MIM:614651]: An autosomal recessive multisystem disorder characterized by early-onset deafness, optic atrophy, mild mental retardation, peripheral neuropathy, obesity, livedo reticularis, and cardiac valvulopathy.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti308 – 3081D → E in COQ10D2. 1 Publication
    VAR_034879

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614651. phenotype.
    Orphaneti254898. Deafness - encephaloneuropathy - obesity - valvulopathy.
    PharmGKBiPA134982512.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 415415Decaprenyl-diphosphate synthase subunit 1PRO_0000123975Add
    BLAST

    Proteomic databases

    MaxQBiQ5T2R2.
    PaxDbiQ5T2R2.
    PRIDEiQ5T2R2.

    PTM databases

    PhosphoSiteiQ5T2R2.

    Expressioni

    Gene expression databases

    BgeeiQ5T2R2.
    CleanExiHS_PDSS1.
    GenevestigatoriQ5T2R2.

    Organism-specific databases

    HPAiHPA038032.

    Interactioni

    Subunit structurei

    Heterotetramer of 2 DPS1/TPRT and 2 DLP1 subunits.1 Publication

    Protein-protein interaction databases

    BioGridi117125. 1 interaction.
    STRINGi9606.ENSP00000365388.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5T2R2.
    SMRiQ5T2R2. Positions 94-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FPP/GGPP synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0142.
    HOGENOMiHOG000009104.
    HOVERGENiHBG054389.
    InParanoidiQ5T2R2.
    KOiK12504.
    OMAiKAFRPMI.
    OrthoDBiEOG7DNNWF.
    PhylomeDBiQ5T2R2.
    TreeFamiTF313548.

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    InterProiIPR000092. Polyprenyl_synt.
    IPR017446. Polyprenyl_synth-rel.
    IPR008949. Terpenoid_synth.
    [Graphical view]
    PANTHERiPTHR12001. PTHR12001. 1 hit.
    PfamiPF00348. polyprenyl_synt. 1 hit.
    [Graphical view]
    SUPFAMiSSF48576. SSF48576. 1 hit.
    PROSITEiPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
    PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5T2R2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASRWWRWRR GCSWKPAARS PGPGSPGRAG PLGPSAAAEV RAQVHRRKGL    50
    DLSQIPYINL VKHLTSACPN VCRISRFHHT TPDSKTHSGE KYTDPFKLGW 100
    RDLKGLYEDI RKELLISTSE LKEMSEYYFD GKGKAFRPII VALMARACNI 150
    HHNNSRHVQA SQRAIALIAE MIHTASLVHD DVIDDASSRR GKHTVNKIWG 200
    EKKAVLAGDL ILSAASIALA RIGNTTVISI LTQVIEDLVR GEFLQLGSKE 250
    NENERFAHYL EKTFKKTASL IANSCKAVSV LGCPDPVVHE IAYQYGKNVG 300
    IAFQLIDDVL DFTSCSDQMG KPTSADLKLG LATGPVLFAC QQFPEMNAMI 350
    MRRFSLPGDV DRARQYVLQS DGVQQTTYLA QQYCHEAIRE ISKLRPSPER 400
    DALIQLSEIV LTRDK 415
    Length:415
    Mass (Da):46,261
    Last modified:December 21, 2004 - v1
    Checksum:iF0B073C75CBD06D2
    GO
    Isoform 2 (identifier: Q5T2R2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         279-415: SVLGCPDPVV...LSEIVLTRDK → FPRNECYDHATVQFAWRCRQSSTVCTTE

    Note: No experimental confirmation available.

    Show »
    Length:306
    Mass (Da):34,304
    Checksum:iD5195700E8AFF902
    GO
    Isoform 3 (identifier: Q5T2R2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-42: MASRWWRWRRGCSWKPAARSPGPGSPGRAGPLGPSAAAEVRA → MPA

    Show »
    Length:376
    Mass (Da):42,089
    Checksum:iBB32C9961B92ED00
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301G → V in AAH63635. (PubMed:15489334)Curated
    Sequence conflicti44 – 441V → A in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti47 – 471R → Q in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti58 – 581I → F in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti66 – 661S → P in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti72 – 732CR → YS in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti76 – 761R → Q in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti83 – 831D → Y in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti109 – 1091D → G in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti114 – 1141L → P in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti119 – 1191S → T in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti124 – 1241M → I in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti131 – 1311G → V in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti142 – 1421A → V in AAD28559. (PubMed:10972372)Curated
    Sequence conflicti186 – 1861A → V in BAD97134. 1 PublicationCurated
    Sequence conflicti298 – 2981N → D in BAD97134. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti308 – 3081D → E in COQ10D2. 1 Publication
    VAR_034879

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4242MASRW…AEVRA → MPA in isoform 3. 1 PublicationVSP_017100Add
    BLAST
    Alternative sequencei279 – 415137SVLGC…LTRDK → FPRNECYDHATVQFAWRCRQ SSTVCTTE in isoform 2. 1 PublicationVSP_017101Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF118395 mRNA. Translation: AAD28559.1.
    AB210838 mRNA. Translation: BAE48216.1.
    AK223414 mRNA. Translation: BAD97134.1.
    AL390961 Genomic DNA. Translation: CAI17280.1.
    BC049211 mRNA. Translation: AAH49211.1.
    BC063635 mRNA. Translation: AAH63635.1.
    CCDSiCCDS31168.1. [Q5T2R2-1]
    RefSeqiNP_055132.2. NM_014317.3. [Q5T2R2-1]
    UniGeneiHs.558468.

    Genome annotation databases

    EnsembliENST00000376215; ENSP00000365388; ENSG00000148459. [Q5T2R2-1]
    GeneIDi23590.
    KEGGihsa:23590.
    UCSCiuc001isv.3. human. [Q5T2R2-1]
    uc001isw.3. human. [Q5T2R2-2]

    Polymorphism databases

    DMDMi74744657.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF118395 mRNA. Translation: AAD28559.1 .
    AB210838 mRNA. Translation: BAE48216.1 .
    AK223414 mRNA. Translation: BAD97134.1 .
    AL390961 Genomic DNA. Translation: CAI17280.1 .
    BC049211 mRNA. Translation: AAH49211.1 .
    BC063635 mRNA. Translation: AAH63635.1 .
    CCDSi CCDS31168.1. [Q5T2R2-1 ]
    RefSeqi NP_055132.2. NM_014317.3. [Q5T2R2-1 ]
    UniGenei Hs.558468.

    3D structure databases

    ProteinModelPortali Q5T2R2.
    SMRi Q5T2R2. Positions 94-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117125. 1 interaction.
    STRINGi 9606.ENSP00000365388.

    PTM databases

    PhosphoSitei Q5T2R2.

    Polymorphism databases

    DMDMi 74744657.

    Proteomic databases

    MaxQBi Q5T2R2.
    PaxDbi Q5T2R2.
    PRIDEi Q5T2R2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376215 ; ENSP00000365388 ; ENSG00000148459 . [Q5T2R2-1 ]
    GeneIDi 23590.
    KEGGi hsa:23590.
    UCSCi uc001isv.3. human. [Q5T2R2-1 ]
    uc001isw.3. human. [Q5T2R2-2 ]

    Organism-specific databases

    CTDi 23590.
    GeneCardsi GC10P026986.
    HGNCi HGNC:17759. PDSS1.
    HPAi HPA038032.
    MIMi 607429. gene.
    614651. phenotype.
    neXtProti NX_Q5T2R2.
    Orphaneti 254898. Deafness - encephaloneuropathy - obesity - valvulopathy.
    PharmGKBi PA134982512.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0142.
    HOGENOMi HOG000009104.
    HOVERGENi HBG054389.
    InParanoidi Q5T2R2.
    KOi K12504.
    OMAi KAFRPMI.
    OrthoDBi EOG7DNNWF.
    PhylomeDBi Q5T2R2.
    TreeFami TF313548.

    Enzyme and pathway databases

    UniPathwayi UPA00232 .
    BioCyci MetaCyc:HS07530-MONOMER.
    BRENDAi 2.5.1.11. 2681.
    Reactomei REACT_160111. Ubiquinol biosynthesis.

    Miscellaneous databases

    GeneWikii PDSS1.
    GenomeRNAii 23590.
    NextBioi 46232.
    PROi Q5T2R2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q5T2R2.
    CleanExi HS_PDSS1.
    Genevestigatori Q5T2R2.

    Family and domain databases

    Gene3Di 1.10.600.10. 1 hit.
    InterProi IPR000092. Polyprenyl_synt.
    IPR017446. Polyprenyl_synth-rel.
    IPR008949. Terpenoid_synth.
    [Graphical view ]
    PANTHERi PTHR12001. PTHR12001. 1 hit.
    Pfami PF00348. polyprenyl_synt. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48576. SSF48576. 1 hit.
    PROSITEi PS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
    PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Quinone-responsive multiple respiratory-chain dysfunction due to widespread coenzyme Q10 deficiency."
      Roetig A., Appelkvist E.-L., Geromel V., Chretien D., Kadhom N., Edery P., Lebideau M., Dallner G., Munnich A., Ernster L., Rustin P.
      Lancet 356:391-395(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    2. "Characterization of solanesyl and decaprenyl diphosphate synthases in mice and humans."
      Saiki R., Nagata A., Kainou T., Matsuda H., Kawamukai M.
      FEBS J. 272:5606-5622(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Coronary arterial endothelium.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-415 (ISOFORM 1).
      Tissue: Brain and Duodenum.
    6. "Prenyldiphosphate synthase, subunit 1 (PDSS1) and OH-benzoate polyprenyltransferase (COQ2) mutations in ubiquinone deficiency and oxidative phosphorylation disorders."
      Mollet J., Giurgea I., Schlemmer D., Dallner G., Chretien D., Delahodde A., Bacq D., de Lonlay P., Munnich A., Rotig A.
      J. Clin. Invest. 117:765-772(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT COQ10D2 GLU-308.

    Entry informationi

    Entry nameiDPS1_HUMAN
    AccessioniPrimary (citable) accession number: Q5T2R2
    Secondary accession number(s): Q53F75
    , Q6P473, Q86WQ8, Q9Y2W5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2006
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 97 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3