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Q5T2R2

- DPS1_HUMAN

UniProt

Q5T2R2 - DPS1_HUMAN

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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

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

Mg2+By similarityNote: Binds 3 Mg(2+) 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
Complete GO annotation...

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
Complete GO annotation...

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. 3 interactions.
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.
GeneTreeiENSGT00530000063378.
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

        10         20         30         40         50
MASRWWRWRR GCSWKPAARS PGPGSPGRAG PLGPSAAAEV RAQVHRRKGL
60 70 80 90 100
DLSQIPYINL VKHLTSACPN VCRISRFHHT TPDSKTHSGE KYTDPFKLGW
110 120 130 140 150
RDLKGLYEDI RKELLISTSE LKEMSEYYFD GKGKAFRPII VALMARACNI
160 170 180 190 200
HHNNSRHVQA SQRAIALIAE MIHTASLVHD DVIDDASSRR GKHTVNKIWG
210 220 230 240 250
EKKAVLAGDL ILSAASIALA RIGNTTVISI LTQVIEDLVR GEFLQLGSKE
260 270 280 290 300
NENERFAHYL EKTFKKTASL IANSCKAVSV LGCPDPVVHE IAYQYGKNVG
310 320 330 340 350
IAFQLIDDVL DFTSCSDQMG KPTSADLKLG LATGPVLFAC QQFPEMNAMI
360 370 380 390 400
MRRFSLPGDV DRARQYVLQS DGVQQTTYLA QQYCHEAIRE ISKLRPSPER
410
DALIQLSEIV LTRDK
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 3 interactions.
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.
GeneTreei ENSGT00530000063378.
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

ChiTaRSi PDSS1. human.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 99 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