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Q03393

- PTPS_HUMAN

UniProt

Q03393 - PTPS_HUMAN

Protein

6-pyruvoyl tetrahydrobiopterin synthase

Gene

PTS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.1 Publication

    Catalytic activityi

    7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Kineticsi

    1. KM=8.1 µM for 7,8-dihydroneopterin triphosphate1 Publication

    Vmax=120 nmol/min/mg enzyme1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi24 – 241ZincPROSITE-ProRule annotation
    Active sitei43 – 431Proton acceptorPROSITE-ProRule annotation
    Metal bindingi49 – 491ZincPROSITE-ProRule annotation
    Metal bindingi51 – 511ZincPROSITE-ProRule annotation
    Active sitei90 – 901Charge relay systemPROSITE-ProRule annotation
    Active sitei134 – 1341Charge relay systemPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 6-pyruvoyltetrahydropterin synthase activity Source: Reactome
    2. identical protein binding Source: IntAct
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cellular amino acid metabolic process Source: ProtInc
    2. central nervous system development Source: ProtInc
    3. nitric oxide metabolic process Source: Reactome
    4. regulation of nitric-oxide synthase activity Source: Reactome
    5. small molecule metabolic process Source: Reactome
    6. tetrahydrobiopterin biosynthetic process Source: ProtInc

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tetrahydrobiopterin biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07692-MONOMER.
    BRENDAi4.2.3.12. 2681.
    ReactomeiREACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    SABIO-RKQ03393.
    UniPathwayiUPA00849; UER00819.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    6-pyruvoyl tetrahydrobiopterin synthase (EC:4.2.3.12)
    Short name:
    PTP synthase
    Short name:
    PTPS
    Gene namesi
    Name:PTS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9689. PTS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb
    2. cytosol Source: Reactome
    3. mitochondrion Source: LIFEdb

    Pathology & Biotechi

    Involvement in diseasei

    Hyperphenylalaninemia, BH4-deficient, A (HPABH4A) [MIM:261640]: An autosomal recessive disorder characterized by hyperphenylalaninemia, depletion of the neurotransmitters dopamine and serotonin, and progressive cognitive and motor deficits. Neurological symptoms are unresponsive to the classic phenylalanine-low diet.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161R → C in HPABH4A; severe decrease in activity; diminishes phosphorylation by PKG. 1 Publication
    VAR_006816
    Natural varianti25 – 251R → G in HPABH4A; severe form. 1 Publication
    VAR_006817
    Natural varianti25 – 251R → Q in HPABH4A; abolishes activity; no effect on phosphorylation by PKG. 1 Publication
    VAR_006818
    Natural varianti26 – 261L → F in HPABH4A. 1 Publication
    VAR_058265
    Natural varianti35 – 351E → G in HPABH4A.
    VAR_006819
    Natural varianti36 – 361N → K in HPABH4A.
    VAR_006820
    Natural varianti47 – 471N → D in HPABH4A; transient phenotype; due to partial PTS deficiency; total loss of activity. 1 Publication
    VAR_008040
    Natural varianti52 – 521N → S in HPABH4A; severe form; common in Chinese population. 2 Publications
    VAR_006821
    Natural varianti56 – 561V → M in HPABH4A; mild form. 1 Publication
    VAR_006822
    Natural varianti57 – 571Missing in HPABH4A. 2 Publications
    VAR_006823
    Natural varianti67 – 671T → M in HPABH4A. 2 Publications
    VAR_006824
    Natural varianti70 – 701V → D in HPABH4A. 1 Publication
    VAR_006825
    Natural varianti87 – 871P → L in HPABH4A. 1 Publication
    VAR_006826
    Natural varianti87 – 871P → S in HPABH4A; severe form; common in Chinese population. 2 Publications
    Corresponds to variant rs104894276 [ dbSNP | Ensembl ].
    VAR_006827
    Natural varianti96 – 961D → N in HPABH4A; severe form. 1 Publication
    Corresponds to variant rs104894280 [ dbSNP | Ensembl ].
    VAR_006828
    Natural varianti97 – 971V → M in HPABH4A. 1 Publication
    VAR_058266
    Natural varianti99 – 991Y → C in HPABH4A. 1 Publication
    VAR_058267
    Natural varianti100 – 1001F → V in HPABH4A.
    VAR_006829
    Natural varianti106 – 1061T → M in HPABH4A. 1 Publication
    VAR_006830
    Natural varianti114 – 1141I → V in HPABH4A. 2 Publications
    VAR_006831
    Natural varianti116 – 1161D → G in HPABH4A; due to partial PTS deficiency; mild form. 1 Publication
    VAR_008041
    Natural varianti124 – 1241V → L in HPABH4A. 1 Publication
    VAR_058268
    Natural varianti129 – 1291K → E in HPABH4A. 1 Publication
    VAR_006832
    Natural varianti136 – 1361D → G in HPABH4A. 1 Publication
    VAR_058269
    Natural varianti136 – 1361D → V in HPABH4A. 2 Publications
    VAR_006833

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 191S → A: Decrease in activity; abolishes phosphorylation by PKG. 1 Publication

    Keywords - Diseasei

    Disease mutation, Phenylketonuria

    Organism-specific databases

    MIMi261640. phenotype.
    Orphaneti13. 6-pyruvoyl-tetrahydropterin synthase deficiency.
    PharmGKBiPA34032.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 1451456-pyruvoyl tetrahydrobiopterin synthasePRO_0000057914Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Phosphoserine; by PKG3 Publications

    Post-translational modificationi

    Phosphorylation of Ser-19 is required for maximal enzyme activity.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ03393.
    PaxDbiQ03393.
    PRIDEiQ03393.

    PTM databases

    PhosphoSiteiQ03393.

    Expressioni

    Gene expression databases

    ArrayExpressiQ03393.
    BgeeiQ03393.
    CleanExiHS_PTS.
    GenevestigatoriQ03393.

    Organism-specific databases

    HPAiHPA001481.

    Interactioni

    Subunit structurei

    Homohexamer formed of two homotrimers in a head to head fashion.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-712344,EBI-712344

    Protein-protein interaction databases

    BioGridi111769. 12 interactions.
    IntActiQ03393. 3 interactions.
    MINTiMINT-1419639.
    STRINGi9606.ENSP00000280362.

    Structurei

    Secondary structure

    1
    145
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 2414
    Beta strandi29 – 313
    Helixi33 – 408
    Helixi41 – 444
    Beta strandi49 – 6214
    Turni65 – 673
    Helixi73 – 8311
    Helixi85 – 884
    Helixi93 – 964
    Helixi98 – 1014
    Helixi107 – 11913
    Beta strandi127 – 1359
    Beta strandi138 – 1425

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3I2BX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L7-145[»]
    ProteinModelPortaliQ03393.
    SMRiQ03393. Positions 8-145.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03393.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PTPS family.Curated

    Phylogenomic databases

    eggNOGiCOG0720.
    HOGENOMiHOG000225069.
    HOVERGENiHBG004358.
    InParanoidiQ03393.
    KOiK01737.
    OMAiCHRLHSK.
    OrthoDBiEOG7NSB3V.
    PhylomeDBiQ03393.
    TreeFamiTF105796.

    Family and domain databases

    InterProiIPR007115. 6-PTP_synth/QueD.
    IPR022470. PTPS_Cys_AS.
    IPR022469. PTPS_His_AS.
    [Graphical view]
    PANTHERiPTHR12589. PTHR12589. 1 hit.
    PfamiPF01242. PTPS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006113. PTP_synth. 1 hit.
    TIGRFAMsiTIGR00039. 6PTHBS. 1 hit.
    PROSITEiPS00987. PTPS_1. 1 hit.
    PS00988. PTPS_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q03393-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTEGGGRRC QAQVSRRISF SASHRLYSKF LSDEENLKLF GKCNNPNGHG    50
    HNYKVVVTVH GEIDPATGMV MNLADLKKYM EEAIMQPLDH KNLDMDVPYF 100
    ADVVSTTENV AVYIWDNLQK VLPVGVLYKV KVYETDNNIV VYKGE 145
    Length:145
    Mass (Da):16,386
    Last modified:October 1, 1993 - v1
    Checksum:iA1CD0DC2F83187E0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti114 – 1141I → M in AAH18029. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161R → C in HPABH4A; severe decrease in activity; diminishes phosphorylation by PKG. 1 Publication
    VAR_006816
    Natural varianti25 – 251R → G in HPABH4A; severe form. 1 Publication
    VAR_006817
    Natural varianti25 – 251R → Q in HPABH4A; abolishes activity; no effect on phosphorylation by PKG. 1 Publication
    VAR_006818
    Natural varianti26 – 261L → F in HPABH4A. 1 Publication
    VAR_058265
    Natural varianti35 – 351E → G in HPABH4A.
    VAR_006819
    Natural varianti36 – 361N → K in HPABH4A.
    VAR_006820
    Natural varianti47 – 471N → D in HPABH4A; transient phenotype; due to partial PTS deficiency; total loss of activity. 1 Publication
    VAR_008040
    Natural varianti52 – 521N → S in HPABH4A; severe form; common in Chinese population. 2 Publications
    VAR_006821
    Natural varianti56 – 561V → M in HPABH4A; mild form. 1 Publication
    VAR_006822
    Natural varianti57 – 571Missing in HPABH4A. 2 Publications
    VAR_006823
    Natural varianti67 – 671T → M in HPABH4A. 2 Publications
    VAR_006824
    Natural varianti70 – 701V → D in HPABH4A. 1 Publication
    VAR_006825
    Natural varianti87 – 871P → L in HPABH4A. 1 Publication
    VAR_006826
    Natural varianti87 – 871P → S in HPABH4A; severe form; common in Chinese population. 2 Publications
    Corresponds to variant rs104894276 [ dbSNP | Ensembl ].
    VAR_006827
    Natural varianti96 – 961D → N in HPABH4A; severe form. 1 Publication
    Corresponds to variant rs104894280 [ dbSNP | Ensembl ].
    VAR_006828
    Natural varianti97 – 971V → M in HPABH4A. 1 Publication
    VAR_058266
    Natural varianti99 – 991Y → C in HPABH4A. 1 Publication
    VAR_058267
    Natural varianti100 – 1001F → V in HPABH4A.
    VAR_006829
    Natural varianti106 – 1061T → M in HPABH4A. 1 Publication
    VAR_006830
    Natural varianti114 – 1141I → V in HPABH4A. 2 Publications
    VAR_006831
    Natural varianti116 – 1161D → G in HPABH4A; due to partial PTS deficiency; mild form. 1 Publication
    VAR_008041
    Natural varianti124 – 1241V → L in HPABH4A. 1 Publication
    VAR_058268
    Natural varianti129 – 1291K → E in HPABH4A. 1 Publication
    VAR_006832
    Natural varianti136 – 1361D → G in HPABH4A. 1 Publication
    VAR_058269
    Natural varianti136 – 1361D → V in HPABH4A. 2 Publications
    VAR_006833

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97655 mRNA. Translation: AAA51541.1.
    D17400 mRNA. Translation: BAA04224.1.
    D25234 Genomic DNA. Translation: BAA04959.1.
    L76259 Genomic DNA. Translation: AAB64229.1.
    U63383
    , U63380, U63381, U63382 Genomic DNA. Translation: AAC16970.1.
    AB042297 Genomic DNA. Translation: BAA95486.1.
    EF445018 Genomic DNA. Translation: ACA06065.1.
    CH471065 Genomic DNA. Translation: EAW67195.1.
    BC009686 mRNA. Translation: AAH09686.1.
    BC018029 mRNA. Translation: AAH18029.1.
    CCDSiCCDS8359.1.
    PIRiJC1405.
    RefSeqiNP_000308.1. NM_000317.2.
    UniGeneiHs.503860.

    Genome annotation databases

    EnsembliENST00000280362; ENSP00000280362; ENSG00000150787.
    GeneIDi5805.
    KEGGihsa:5805.
    UCSCiuc001pnj.4. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M97655 mRNA. Translation: AAA51541.1 .
    D17400 mRNA. Translation: BAA04224.1 .
    D25234 Genomic DNA. Translation: BAA04959.1 .
    L76259 Genomic DNA. Translation: AAB64229.1 .
    U63383
    , U63380 , U63381 , U63382 Genomic DNA. Translation: AAC16970.1 .
    AB042297 Genomic DNA. Translation: BAA95486.1 .
    EF445018 Genomic DNA. Translation: ACA06065.1 .
    CH471065 Genomic DNA. Translation: EAW67195.1 .
    BC009686 mRNA. Translation: AAH09686.1 .
    BC018029 mRNA. Translation: AAH18029.1 .
    CCDSi CCDS8359.1.
    PIRi JC1405.
    RefSeqi NP_000308.1. NM_000317.2.
    UniGenei Hs.503860.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3I2B X-ray 2.30 A/B/C/D/E/F/G/H/I/J/K/L 7-145 [» ]
    ProteinModelPortali Q03393.
    SMRi Q03393. Positions 8-145.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111769. 12 interactions.
    IntActi Q03393. 3 interactions.
    MINTi MINT-1419639.
    STRINGi 9606.ENSP00000280362.

    PTM databases

    PhosphoSitei Q03393.

    Proteomic databases

    MaxQBi Q03393.
    PaxDbi Q03393.
    PRIDEi Q03393.

    Protocols and materials databases

    DNASUi 5805.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000280362 ; ENSP00000280362 ; ENSG00000150787 .
    GeneIDi 5805.
    KEGGi hsa:5805.
    UCSCi uc001pnj.4. human.

    Organism-specific databases

    CTDi 5805.
    GeneCardsi GC11P112097.
    HGNCi HGNC:9689. PTS.
    HPAi HPA001481.
    MIMi 261640. phenotype.
    612719. gene.
    neXtProti NX_Q03393.
    Orphaneti 13. 6-pyruvoyl-tetrahydropterin synthase deficiency.
    PharmGKBi PA34032.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0720.
    HOGENOMi HOG000225069.
    HOVERGENi HBG004358.
    InParanoidi Q03393.
    KOi K01737.
    OMAi CHRLHSK.
    OrthoDBi EOG7NSB3V.
    PhylomeDBi Q03393.
    TreeFami TF105796.

    Enzyme and pathway databases

    UniPathwayi UPA00849 ; UER00819 .
    BioCyci MetaCyc:HS07692-MONOMER.
    BRENDAi 4.2.3.12. 2681.
    Reactomei REACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
    SABIO-RK Q03393.

    Miscellaneous databases

    EvolutionaryTracei Q03393.
    GeneWikii PTS_(gene).
    GenomeRNAii 5805.
    NextBioi 22628.
    PROi Q03393.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q03393.
    Bgeei Q03393.
    CleanExi HS_PTS.
    Genevestigatori Q03393.

    Family and domain databases

    InterProi IPR007115. 6-PTP_synth/QueD.
    IPR022470. PTPS_Cys_AS.
    IPR022469. PTPS_His_AS.
    [Graphical view ]
    PANTHERi PTHR12589. PTHR12589. 1 hit.
    Pfami PF01242. PTPS. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006113. PTP_synth. 1 hit.
    TIGRFAMsi TIGR00039. 6PTHBS. 1 hit.
    PROSITEi PS00987. PTPS_1. 1 hit.
    PS00988. PTPS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human 6-pyruvoyltetrahydropterin synthase: cDNA cloning and heterologous expression of the recombinant enzyme."
      Thoeny B., Leimbacher W., Buergisser D., Heizmann C.W.
      Biochem. Biophys. Res. Commun. 189:1437-1443(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
      Tissue: Liver.
    2. "cDNA cloning, expression in Escherichia coli and purification of human 6-pyruvoyl-tetrahydropterin synthase."
      Ashida A., Hatakeyama K., Kagamiyama H.
      Biochem. Biophys. Res. Commun. 195:1386-1393(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "A missense mutation (A to G) of 6-pyruvoyltetrahydropterin synthase in tetrahydrobiopterin-deficient form of hyperphenylalaninemia."
      Ashida A., Owada M., Hatakeyama K.
      Genomics 24:408-410(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HPABH4A VAL-114.
    4. "Chromosomal localization, genomic structure and characterization of the human gene and a retropseudogene for 6-pyruvoyltetrahydropterin synthase."
      Kluge C., Brecevic L., Heizmann C.W., Blau N., Thoeny B.
      Eur. J. Biochem. 240:477-484(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Genomic structure of 6-pyruvoyl-tetrahydropterin synthase gene and a T/C polymorphism detected in Chinese."
      Liu T.T., Lu S.F., Hsiao K.J.
      J. Biomed. Lab. Sci. 10:39-47(1998)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Isolation and sequencing of human 6-pyruvoyl-tetrahydropterin synthase gene containing BAC clone 321H15."
      Hsiao K.-J., Liu T.-T., Chang Y.-H., Chiu Y.-H., Chiang S.-H., Chang H.-M., Chen C.-Y., Tsai S.-F.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. NHLBI resequencing and genotyping service (RS&G)
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Brain and Pancreas.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Serine 19 of human 6-pyruvoyltetrahydropterin synthase is phosphorylated by cGMP protein kinase II."
      Scherer-Oppliger T., Leimbacher W., Blau N., Thoeny B.
      J. Biol. Chem. 274:31341-31348(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS HPABH4A CYS-16 AND GLN-25, KINETIC PARAMETERS, PHOSPHORYLATION AT SER-19, MUTAGENESIS OF SER-19.
    13. "Mutations in the GTP cyclohydrolase I and 6-pyruvoyl-tetrahydropterin synthase genes."
      Thoeny B., Blau N.
      Hum. Mutat. 10:11-20(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    14. "Hyperphenylalaninemia due to defects in tetrahydrobiopterin metabolism: molecular characterization of mutations in 6-pyruvoyl-tetrahydropterin synthase."
      Thoeny B., Leimbacher W., Blau N., Harvie A., Heizmann C.W.
      Am. J. Hum. Genet. 54:782-792(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HPABH4A CYS-16 AND GLN-25.
    15. "Structural and functional consequences of mutations in 6-pyruvoyltetrahydropterin synthase causing hyperphenylalaninemia in humans. Phosphorylation is a requirement for in vivo activity."
      Oppliger T., Thoeny B., Nar H., Buergisser D., Huber R., Heizmann C.W., Blau N.
      J. Biol. Chem. 270:29498-29506(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS HPABH4A CYS-16; GLN-25; VAL-57 DEL AND LEU-87.
    16. "Identification of a common 6-pyruvoyl-tetrahydropterin synthase mutation at codon 87 in Chinese phenylketonuria caused by tetrahydrobiopterin synthesis deficiency."
      Liu T.T., Hsiao K.J.
      Hum. Genet. 98:313-316(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HPABH4A SER-52 AND SER-87.
    17. "Identification of mutations causing 6-pyruvoyl-tetrahydropterin synthase deficiency in four Italian families."
      Oppliger T., Thoeny B., Kluge C., Matasovic A., Heizmann C.W., Ponzone A., Spada M., Blau N.
      Hum. Mutat. 10:25-35(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HPABH4A VAL-57 DEL; MET-67; GLU-129 AND VAL-136.
    18. "6-pyruvoyl-tetrahydropterin synthase deficiency with generalized dystonia and diurnal fluctuation of symptoms: a clinical and molecular study."
      Hanihara T., Inoue K., Kawanishi C., Sugiyama N., Miyakawa T., Onishi H., Yamada Y., Osaka H., Kosaka K., Iwabuchi K., Owada M.
      Mov. Disord. 12:408-411(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HPABH4A VAL-114.
    19. "Mutation analysis of the 6-pyruvoyl-tetrahydropterin synthase gene in Chinese hyperphenylalaninemia caused by tetrahydrobiopterin synthesis deficiency."
      Liu T.-T., Hsiao K.-J., Lu S.-F., Wu S.-J., Wu K.-F., Chiang S.-H., Liu X.-Q., Chen R.-G., Yu W.-M.
      Hum. Mutat. 11:76-83(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HPABH4A GLY-25; SER-52; MET-56; ASP-70; SER-87; ASN-96 AND MET-106.
    20. "Single-step mutation scanning of the 6-pyruvoyltetrahydropterin synthase gene in patients with hyperphenylalaninemia."
      Romstad A., Guldberg P., Blau N., Guettler F.
      Clin. Chem. 45:2102-2108(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HPABH4A VAL-57 DEL AND MET-97.
    21. "Dominant negative allele (N47D) in a compound heterozygote for a variant of 6-pyruvoyltetrahydropterin synthase deficiency causing transient hyperphenylalaninemia."
      Scherer-Oppliger T., Matasovic A., Laufs S., Levy H.L., Quackenbush E.J., Blau N., Thoeny B.
      Hum. Mutat. 13:286-289(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HPABH4A ASP-47 AND GLY-116.
    22. "Isolated central form of tetrahydrobiopterin deficiency associated with hemizygosity on chromosome 11q and a mutant allele of PTPS."
      Blau N., Scherer-Oppliger T., Baumer A., Riegel M., Matasovic A., Schinzel A., Jaeken J., Thoeny B.
      Hum. Mutat. 16:54-60(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HPABH4A CYS-99.
    23. "Molecular analysis and long-term follow-up of patients with different forms of 6-pyruvoyl-tetrahydropterin synthase deficiency."
      Dudesek A., Roeschinger W., Muntau A.C., Seidel J., Leupold D., Thoeny B., Blau N.
      Eur. J. Pediatr. 160:267-276(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HPABH4A PHE-26; MET-67; LEU-87; LEU-124; GLY-136 AND VAL-136.

    Entry informationi

    Entry nameiPTPS_HUMAN
    AccessioniPrimary (citable) accession number: Q03393
    Secondary accession number(s): B0YJ87, Q8WVG8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 152 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

    Miscellaneous

    The active site is at the interface between 2 subunits. The proton acceptor Cys is on one subunit, and the charge relay system is on the other subunit.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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