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P09417

- DHPR_HUMAN

UniProt

P09417 - DHPR_HUMAN

Protein

Dihydropteridine reductase

Gene

QDPR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 2 (28 Nov 2006)
      Previous versions | rss
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    Functioni

    The product of this enzyme, tetrahydrobiopterin (BH-4), is an essential cofactor for phenylalanine, tyrosine, and tryptophan hydroxylases.

    Catalytic activityi

    A 5,6,7,8-tetrahydropteridine + NAD(P)+ = a 6,7-dihydropteridine + NAD(P)H.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei150 – 1501Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi14 – 3825NADPAdd
    BLAST

    GO - Molecular functioni

    1. 6,7-dihydropteridine reductase activity Source: Reactome
    2. electron carrier activity Source: UniProtKB
    3. NADH binding Source: Ensembl
    4. NADPH binding Source: Ensembl

    GO - Biological processi

    1. cellular amino acid metabolic process Source: ProtInc
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. cellular response to drug Source: Ensembl
    4. dihydrobiopterin metabolic process Source: ProtInc
    5. liver development Source: Ensembl
    6. L-phenylalanine catabolic process Source: Reactome
    7. response to aluminum ion Source: Ensembl
    8. response to glucagon Source: Ensembl
    9. response to lead ion Source: Ensembl
    10. small molecule metabolic process Source: Reactome
    11. tetrahydrobiopterin biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Tetrahydrobiopterin biosynthesis

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07746-MONOMER.
    ReactomeiREACT_1786. Phenylalanine and tyrosine catabolism.
    SABIO-RKP09417.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydropteridine reductase (EC:1.5.1.34)
    Alternative name(s):
    HDHPR
    Quinoid dihydropteridine reductase
    Gene namesi
    Name:QDPR
    Synonyms:DHPR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:9752. QDPR.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. mitochondrion Source: Ensembl
    5. neuron projection Source: Ensembl

    Pathology & Biotechi

    Involvement in diseasei

    Hyperphenylalaninemia, BH4-deficient, C (HPABH4C) [MIM:261630]: Rare autosomal recessive disorder characterized by hyperphenylalaninemia and severe neurologic symptoms (malignant hyperphenylalaninemia) including axial hypotonia and truncal hypertonia, abnormal thermogenesis, and microcephaly. These signs are attributable to depletion of the neurotransmitters dopamine and serotonin, whose syntheses are controlled by tryptophan and tyrosine hydroxylases that use BH-4 as cofactor. Patients do not respond to phenylalanine-restricted diet. HPABH4C is lethal if untreated.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141L → P in HPABH4C; severe. 1 Publication
    VAR_008121
    Natural varianti17 – 171G → R in HPABH4C; severe. 1 Publication
    VAR_021767
    Natural varianti17 – 171G → V in HPABH4C; severe. 1 Publication
    VAR_008122
    Natural varianti18 – 181G → D in HPABH4C; severe. 1 Publication
    VAR_021768
    Natural varianti23 – 231G → D in HPABH4C; severe. 3 Publications
    VAR_006960
    Natural varianti36 – 361W → R in HPABH4C.
    VAR_006961
    Natural varianti66 – 661Q → R in HPABH4C; severe. 1 Publication
    VAR_021769
    Natural varianti74 – 741L → P in HPABH4C.
    VAR_006962
    Natural varianti108 – 1081W → G in HPABH4C. 1 Publication
    VAR_006963
    Natural varianti123 – 1231T → TT in HPABH4C. 1 Publication
    VAR_006964
    Natural varianti145 – 1451P → L in HPABH4C.
    VAR_006965
    Natural varianti149 – 1491G → R in HPABH4C. 1 Publication
    VAR_021770
    Natural varianti150 – 1501Y → C in HPABH4C; mild. 2 Publications
    VAR_006966
    Natural varianti151 – 1511G → S in HPABH4C; mild.
    VAR_006967
    Natural varianti158 – 1581H → Y in HPABH4C; severe. 1 Publication
    VAR_006968
    Natural varianti170 – 1701G → S in HPABH4C.
    VAR_006969
    Natural varianti212 – 2121F → C in HPABH4C; mild.
    VAR_006970
    Natural varianti218 – 2181G → GITG in HPABH4C; mild.
    VAR_006971

    Keywords - Diseasei

    Disease mutation, Phenylketonuria

    Organism-specific databases

    MIMi261630. phenotype.
    Orphaneti226. Dihydropteridine reductase deficiency.
    PharmGKBiPA34094.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 244243Dihydropteridine reductasePRO_0000054636Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei73 – 731N6-succinyllysineBy similarity
    Modified residuei79 – 791N6-succinyllysineBy similarity
    Modified residuei96 – 961N6-succinyllysineBy similarity
    Modified residuei102 – 1021N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP09417.
    PaxDbiP09417.
    PeptideAtlasiP09417.
    PRIDEiP09417.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00014439.
    UCD-2DPAGEP09417.

    PTM databases

    PhosphoSiteiP09417.

    Expressioni

    Gene expression databases

    ArrayExpressiP09417.
    BgeeiP09417.
    CleanExiHS_QDPR.
    GenevestigatoriP09417.

    Organism-specific databases

    HPAiHPA058951.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi111798. 8 interactions.
    IntActiP09417. 2 interactions.
    MINTiMINT-5002411.
    STRINGi9606.ENSP00000281243.

    Structurei

    Secondary structure

    1
    244
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi11 – 166
    Turni17 – 193
    Helixi21 – 3212
    Beta strandi36 – 438
    Beta strandi48 – 536
    Helixi60 – 7516
    Beta strandi80 – 856
    Helixi100 – 11011
    Helixi112 – 12514
    Beta strandi126 – 13510
    Helixi138 – 1414
    Helixi148 – 16518
    Beta strandi176 – 1816
    Helixi188 – 1914
    Helixi199 – 2013
    Helixi205 – 21612
    Turni217 – 2204
    Beta strandi227 – 2337
    Beta strandi236 – 2427

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HDRX-ray2.50A1-244[»]
    ProteinModelPortaliP09417.
    SMRiP09417. Positions 9-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09417.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1028.
    HOGENOMiHOG000232194.
    HOVERGENiHBG001000.
    InParanoidiP09417.
    KOiK00357.
    OMAiSDLMWKQ.
    OrthoDBiEOG7060RV.
    PhylomeDBiP09417.
    TreeFamiTF105932.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PROSITEiPS00061. ADH_SHORT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P09417-1) [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

    MAAAAAAGEA RRVLVYGGRG ALGSRCVQAF RARNWWVASV DVVENEEASA    50
    SIIVKMTDSF TEQADQVTAE VGKLLGEEKV DAILCVAGGW AGGNAKSKSL 100
    FKNCDLMWKQ SIWTSTISSH LATKHLKEGG LLTLAGAKAA LDGTPGMIGY 150
    GMAKGAVHQL CQSLAGKNSG MPPGAAAIAV LPVTLDTPMN RKSMPEADFS 200
    SWTPLEFLVE TFHDWITGKN RPSSGSLIQV VTTEGRTELT PAYF 244
    Length:244
    Mass (Da):25,790
    Last modified:November 28, 2006 - v2
    Checksum:i0852F9F0CA38AB1C
    GO
    Isoform 2 (identifier: P09417-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         36-66: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:213
    Mass (Da):22,408
    Checksum:i042BEB8C3F313C20
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti14 – 141L → P in HPABH4C; severe. 1 Publication
    VAR_008121
    Natural varianti17 – 171G → R in HPABH4C; severe. 1 Publication
    VAR_021767
    Natural varianti17 – 171G → V in HPABH4C; severe. 1 Publication
    VAR_008122
    Natural varianti18 – 181G → D in HPABH4C; severe. 1 Publication
    VAR_021768
    Natural varianti23 – 231G → D in HPABH4C; severe. 3 Publications
    VAR_006960
    Natural varianti36 – 361W → R in HPABH4C.
    VAR_006961
    Natural varianti51 – 511S → T.3 Publications
    VAR_013027
    Natural varianti66 – 661Q → R in HPABH4C; severe. 1 Publication
    VAR_021769
    Natural varianti74 – 741L → P in HPABH4C.
    VAR_006962
    Natural varianti108 – 1081W → G in HPABH4C. 1 Publication
    VAR_006963
    Natural varianti123 – 1231T → TT in HPABH4C. 1 Publication
    VAR_006964
    Natural varianti145 – 1451P → L in HPABH4C.
    VAR_006965
    Natural varianti149 – 1491G → R in HPABH4C. 1 Publication
    VAR_021770
    Natural varianti150 – 1501Y → C in HPABH4C; mild. 2 Publications
    VAR_006966
    Natural varianti151 – 1511G → S in HPABH4C; mild.
    VAR_006967
    Natural varianti158 – 1581H → Y in HPABH4C; severe. 1 Publication
    VAR_006968
    Natural varianti170 – 1701G → S in HPABH4C.
    VAR_006969
    Natural varianti212 – 2121F → C in HPABH4C; mild.
    VAR_006970
    Natural varianti218 – 2181G → GITG in HPABH4C; mild.
    VAR_006971

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei36 – 6631Missing in isoform 2. 1 PublicationVSP_054356Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04882 mRNA. Translation: CAA28571.1.
    M16447 mRNA. Translation: AAA52305.1.
    AJ006239
    , AJ006240, AJ006241, AJ006242, AJ006243, AJ006244, AJ006245 Genomic DNA. Translation: CAA06930.1.
    AB053170 Genomic DNA. Translation: BAB20429.1.
    AK124382 mRNA. Translation: BAG54033.1.
    AK289773 mRNA. Translation: BAF82462.1.
    AK223437 mRNA. Translation: BAD97157.1.
    AC093600 Genomic DNA. No translation available.
    CH471069 Genomic DNA. Translation: EAW92777.1.
    CH471069 Genomic DNA. Translation: EAW92778.1.
    BC000576 mRNA. Translation: AAH00576.1.
    CCDSiCCDS3421.1. [P09417-1]
    PIRiA93655. RDHUP.
    RefSeqiNP_000311.2. NM_000320.2. [P09417-1]
    UniGeneiHs.75438.

    Genome annotation databases

    EnsembliENST00000281243; ENSP00000281243; ENSG00000151552. [P09417-1]
    ENST00000428702; ENSP00000390944; ENSG00000151552. [P09417-2]
    GeneIDi5860.
    KEGGihsa:5860.
    UCSCiuc003gpd.3. human. [P09417-1]
    uc003gpe.3. human.

    Polymorphism databases

    DMDMi118572639.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04882 mRNA. Translation: CAA28571.1 .
    M16447 mRNA. Translation: AAA52305.1 .
    AJ006239
    , AJ006240 , AJ006241 , AJ006242 , AJ006243 , AJ006244 , AJ006245 Genomic DNA. Translation: CAA06930.1 .
    AB053170 Genomic DNA. Translation: BAB20429.1 .
    AK124382 mRNA. Translation: BAG54033.1 .
    AK289773 mRNA. Translation: BAF82462.1 .
    AK223437 mRNA. Translation: BAD97157.1 .
    AC093600 Genomic DNA. No translation available.
    CH471069 Genomic DNA. Translation: EAW92777.1 .
    CH471069 Genomic DNA. Translation: EAW92778.1 .
    BC000576 mRNA. Translation: AAH00576.1 .
    CCDSi CCDS3421.1. [P09417-1 ]
    PIRi A93655. RDHUP.
    RefSeqi NP_000311.2. NM_000320.2. [P09417-1 ]
    UniGenei Hs.75438.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HDR X-ray 2.50 A 1-244 [» ]
    ProteinModelPortali P09417.
    SMRi P09417. Positions 9-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111798. 8 interactions.
    IntActi P09417. 2 interactions.
    MINTi MINT-5002411.
    STRINGi 9606.ENSP00000281243.

    Chemistry

    BindingDBi P09417.
    ChEMBLi CHEMBL3730.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P09417.

    Polymorphism databases

    DMDMi 118572639.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00014439.
    UCD-2DPAGE P09417.

    Proteomic databases

    MaxQBi P09417.
    PaxDbi P09417.
    PeptideAtlasi P09417.
    PRIDEi P09417.

    Protocols and materials databases

    DNASUi 5860.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000281243 ; ENSP00000281243 ; ENSG00000151552 . [P09417-1 ]
    ENST00000428702 ; ENSP00000390944 ; ENSG00000151552 . [P09417-2 ]
    GeneIDi 5860.
    KEGGi hsa:5860.
    UCSCi uc003gpd.3. human. [P09417-1 ]
    uc003gpe.3. human.

    Organism-specific databases

    CTDi 5860.
    GeneCardsi GC04M017488.
    HGNCi HGNC:9752. QDPR.
    HPAi HPA058951.
    MIMi 261630. phenotype.
    612676. gene.
    neXtProti NX_P09417.
    Orphaneti 226. Dihydropteridine reductase deficiency.
    PharmGKBi PA34094.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1028.
    HOGENOMi HOG000232194.
    HOVERGENi HBG001000.
    InParanoidi P09417.
    KOi K00357.
    OMAi SDLMWKQ.
    OrthoDBi EOG7060RV.
    PhylomeDBi P09417.
    TreeFami TF105932.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07746-MONOMER.
    Reactomei REACT_1786. Phenylalanine and tyrosine catabolism.
    SABIO-RK P09417.

    Miscellaneous databases

    ChiTaRSi QDPR. human.
    EvolutionaryTracei P09417.
    GeneWikii QDPR.
    GenomeRNAii 5860.
    NextBioi 22758.
    PROi P09417.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09417.
    Bgeei P09417.
    CleanExi HS_QDPR.
    Genevestigatori P09417.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002198. DH_sc/Rdtase_SDR.
    IPR016040. NAD(P)-bd_dom.
    IPR020904. Sc_DH/Rdtase_CS.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PROSITEi PS00061. ADH_SHORT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human dihydropteridine reductase: characterisation of a cDNA clone and its use in analysis of patients with dihydropteridine reductase deficiency."
      Dahl H.-H.M., Hutchison W., McAdam W., Wake S., Morgan F.J., Cotton R.G.H.
      Nucleic Acids Res. 15:1921-1932(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-51.
    2. Dahl H.-H.M.
      Submitted (JUL-1987) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 51.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-51.
    4. "Dihydropteridine reductase deficiency: physical structure of the QDPR gene, identification of two new mutations and genotype-phenotype correlations."
      Dianzani I., de Sanctis L., Smooker P.M., Gough T.J., Alliaudi C., Brusco A., Spada M., Blau N., Dobos M., Zhang H.-P., Yang N., Ponzone A., Armarego W.L.F., Cotton R.G.H.
      Hum. Mutat. 12:267-273(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-51, VARIANTS HPABH4C ASP-23; CYS-150; TYR-158 AND ILE-THR-GLY-218 INS.
    5. "The complete sequence of human dihydropteridine reductase gene containing BAC clone 395N09."
      Hsiao K.-J., Yen P.-F., Lin C.-H., Liu T.-T., Chiang S.-H., Chen C.-Y., Tsai S.-F.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    7. 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: Cerebellum.
    8. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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 1).
      Tissue: Brain.
    11. Bienvenut W.V., Heiserich L., Gottlieb E.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11 AND 128-138, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    12. "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].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "The crystallographic structure of a human dihydropteridine reductase NADH binary complex expressed in Escherichia coli by a cDNA constructed from its rat homologue."
      Su Y., Varughese K.I., Xuong N.H., Bray T.L., Roche D.J., Whiteley J.M.
      J. Biol. Chem. 268:26836-26841(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    17. "Molecular basis of dihydropteridine reductase deficiency."
      Smooker P.M., Cotton R.G.H.
      Hum. Mutat. 5:279-284(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    18. "Two new mutations in the dihydropteridine reductase gene in patients with tetrahydrobiopterin deficiency."
      Dianzani I., Howells D.W., Ponzone A., Saleeba J.A., Smooker P.M., Cotton R.G.H.
      J. Med. Genet. 30:465-469(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HPABH4C ASP-23 AND GLY-108.
    19. "Insertion of an extra codon for threonine is a cause of dihydropteridine reductase deficiency."
      Howells D.W., Forrest S.M., Dahl H.-H.M., Cotton R.G.H.
      Am. J. Hum. Genet. 47:279-285(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HPABH4C THR-123 INS.
    20. "A series of mutations in the dihydropteridine reductase gene resulting in either abnormal RNA splicing or DHPR protein defects."
      Smooker P.M., Gough T.J., Cotton R.G.H., Alliaudi C., de Sanctis L., Dianzani I.
      Hum. Mutat. 13:503-504(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HPABH4C PRO-14 AND VAL-17.
    21. "Molecular analysis of 16 Turkish families with DHPR deficiency using denaturing gradient gel electrophoresis (DGGE)."
      Romstad A., Kalkanoglu H.S., Coskun T., Demirkol M., Tokatli A., Dursun A., Baykal T., Oezalp I., Guldberg P., Guettler F.
      Hum. Genet. 107:546-553(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HPABH4C ARG-17; ASP-18; ASP-23; ARG-66; ARG-149 AND CYS-150.

    Entry informationi

    Entry nameiDHPR_HUMAN
    AccessioniPrimary (citable) accession number: P09417
    Secondary accession number(s): A8K158
    , B3KW71, Q53F52, Q9H3M5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 168 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3