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Protein

Sepiapterin reductase

Gene

SPR

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

Functioni

Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.

Catalytic activityi

L-erythro-7,8-dihydrobiopterin + NADP+ = sepiapterin + NADPH.
L-erythro-tetrahydrobiopterin + 2 NADP+ = 6-pyruvoyl-5,6,7,8-tetrahydropterin + 2 NADPH.

Kineticsi

  1. KM=14.3 µM for sepiapterin1 Publication
  2. KM=10 µM for NADPH1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei170 – 1701SubstrateBy similarity
    Binding sitei174 – 1741NADPBy similarity
    Binding sitei199 – 1991Substrate; via amide nitrogenBy similarity
    Binding sitei257 – 2571SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi14 – 207NADP1 Publication
    Nucleotide bindingi42 – 432NADP1 Publication
    Nucleotide bindingi69 – 702NADP1 Publication
    Nucleotide bindingi201 – 2066NADP1 Publication

    GO - Molecular functioni

    • aldo-keto reductase (NADP) activity Source: UniProtKB
    • NADP binding Source: UniProtKB
    • sepiapterin reductase activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03979-MONOMER.
    ReactomeiREACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sepiapterin reductase (EC:1.1.1.153)
    Short name:
    SPR
    Gene namesi
    Name:SPR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:11257. SPR.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • mitochondrion Source: Ensembl
    • nucleoplasm Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Dystonia, DOPA-responsive, due to sepiapterin reductase deficiency (DRDSPRD)3 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA form of DOPA-responsive dystonia. In the majority of cases, patients manifest progressive psychomotor retardation, dystonia and spasticity. Cognitive anomalies are also often present. The disease is due to severe dopamine and serotonin deficiencies in the central nervous system caused by a defect in BH4 synthesis. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures.

    See also OMIM:612716
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti150 – 1501R → G in DRDSPRD. 2 Publications
    VAR_058007
    Natural varianti163 – 1631P → L in DRDSPRD. 1 Publication
    VAR_058008

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi213 – 2131S → A: Abolishes phosphorylation by CaMK2. No effect on kinetic parameters. 1 Publication

    Keywords - Diseasei

    Disease mutation, Dystonia

    Organism-specific databases

    MIMi612716. phenotype.
    Orphaneti70594. Dopa-responsive dystonia due to sepiapterin reductase deficiency.
    PharmGKBiPA36087.

    Polymorphism and mutation databases

    BioMutaiSPR.
    DMDMi464801.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261Sepiapterin reductasePRO_0000072149Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei213 – 2131Phosphoserine; by CaMK2; in vitro1 Publication

    Post-translational modificationi

    In vitro phosphorylation of Ser-213 by CaMK2 does not change kinetic parameters.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP35270.
    PaxDbiP35270.
    PeptideAtlasiP35270.
    PRIDEiP35270.

    PTM databases

    PhosphoSiteiP35270.

    Expressioni

    Gene expression databases

    BgeeiP35270.
    CleanExiHS_SPR.
    GenevisibleiP35270. HS.

    Organism-specific databases

    HPAiHPA039505.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi112575. 14 interactions.
    IntActiP35270. 1 interaction.
    MINTiMINT-3304575.
    STRINGi9606.ENSP00000234454.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 149Combined sources
    Helixi18 – 2811Combined sources
    Beta strandi36 – 427Combined sources
    Helixi44 – 5411Combined sources
    Turni56 – 605Combined sources
    Beta strandi62 – 676Combined sources
    Helixi73 – 8412Combined sources
    Beta strandi94 – 996Combined sources
    Helixi111 – 1133Combined sources
    Helixi117 – 12711Combined sources
    Helixi129 – 14113Combined sources
    Beta strandi149 – 1557Combined sources
    Helixi158 – 1603Combined sources
    Helixi168 – 18720Combined sources
    Beta strandi191 – 1977Combined sources
    Beta strandi200 – 2034Combined sources
    Helixi204 – 2129Combined sources
    Helixi216 – 22712Combined sources
    Helixi234 – 24714Combined sources
    Beta strandi254 – 2574Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z6ZX-ray2.50A/B/C/D/E/F5-261[»]
    4HWKX-ray2.40A/B/C/D1-261[»]
    4J7UX-ray2.44A/B/C/D1-261[»]
    4J7XX-ray2.60A/B/F/J1-261[»]
    ProteinModelPortaliP35270.
    SMRiP35270. Positions 4-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35270.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni157 – 1582Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the sepiapterin reductase family.Curated

    Phylogenomic databases

    eggNOGiCOG1028.
    GeneTreeiENSGT00440000033609.
    HOVERGENiHBG006973.
    InParanoidiP35270.
    KOiK00072.
    OMAiMFREQRE.
    OrthoDBiEOG7327PS.
    PhylomeDBiP35270.
    TreeFamiTF326358.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR006393. Sepiapterin_red.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    TIGRFAMsiTIGR01500. sepiapter_red. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P35270-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MEGGLGRAVC LLTGASRGFG RTLAPLLASL LSPGSVLVLS ARNDEALRQL
    60 70 80 90 100
    EAELGAERSG LRVVRVPADL GAEAGLQQLL GALRELPRPK GLQRLLLINN
    110 120 130 140 150
    AGSLGDVSKG FVDLSDSTQV NNYWALNLTS MLCLTSSVLK AFPDSPGLNR
    160 170 180 190 200
    TVVNISSLCA LQPFKGWALY CAGKAARDML FQVLALEEPN VRVLNYAPGP
    210 220 230 240 250
    LDTDMQQLAR ETSVDPDMRK GLQELKAKGK LVDCKVSAQK LLSLLEKDEF
    260
    KSGAHVDFYD K
    Length:261
    Mass (Da):28,048
    Last modified:February 1, 1994 - v1
    Checksum:i9C9BF76212826F47
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101C → R in BAD96662 (Ref. 4) Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti150 – 1501R → G in DRDSPRD. 2 Publications
    VAR_058007
    Natural varianti163 – 1631P → L in DRDSPRD. 1 Publication
    VAR_058008

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M76231 mRNA. Translation: AAA60314.1.
    AK291856 mRNA. Translation: BAF84545.1.
    AK222942 mRNA. Translation: BAD96662.1.
    AC092630 Genomic DNA. Translation: AAY15035.1.
    CH471053 Genomic DNA. Translation: EAW99757.1.
    CH471053 Genomic DNA. Translation: EAW99758.1.
    BC017310 mRNA. Translation: AAH17310.1.
    AB017547 Genomic DNA. Translation: BAA34534.1.
    CCDSiCCDS1920.1.
    PIRiJQ1176.
    RefSeqiNP_003115.1. NM_003124.4.
    UniGeneiHs.301540.

    Genome annotation databases

    EnsembliENST00000234454; ENSP00000234454; ENSG00000116096.
    GeneIDi6697.
    KEGGihsa:6697.
    UCSCiuc002sik.2. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M76231 mRNA. Translation: AAA60314.1.
    AK291856 mRNA. Translation: BAF84545.1.
    AK222942 mRNA. Translation: BAD96662.1.
    AC092630 Genomic DNA. Translation: AAY15035.1.
    CH471053 Genomic DNA. Translation: EAW99757.1.
    CH471053 Genomic DNA. Translation: EAW99758.1.
    BC017310 mRNA. Translation: AAH17310.1.
    AB017547 Genomic DNA. Translation: BAA34534.1.
    CCDSiCCDS1920.1.
    PIRiJQ1176.
    RefSeqiNP_003115.1. NM_003124.4.
    UniGeneiHs.301540.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z6ZX-ray2.50A/B/C/D/E/F5-261[»]
    4HWKX-ray2.40A/B/C/D1-261[»]
    4J7UX-ray2.44A/B/C/D1-261[»]
    4J7XX-ray2.60A/B/F/J1-261[»]
    ProteinModelPortaliP35270.
    SMRiP35270. Positions 4-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi112575. 14 interactions.
    IntActiP35270. 1 interaction.
    MINTiMINT-3304575.
    STRINGi9606.ENSP00000234454.

    PTM databases

    PhosphoSiteiP35270.

    Polymorphism and mutation databases

    BioMutaiSPR.
    DMDMi464801.

    Proteomic databases

    MaxQBiP35270.
    PaxDbiP35270.
    PeptideAtlasiP35270.
    PRIDEiP35270.

    Protocols and materials databases

    DNASUi6697.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000234454; ENSP00000234454; ENSG00000116096.
    GeneIDi6697.
    KEGGihsa:6697.
    UCSCiuc002sik.2. human.

    Organism-specific databases

    CTDi6697.
    GeneCardsiGC02P073026.
    HGNCiHGNC:11257. SPR.
    HPAiHPA039505.
    MIMi182125. gene.
    612716. phenotype.
    neXtProtiNX_P35270.
    Orphaneti70594. Dopa-responsive dystonia due to sepiapterin reductase deficiency.
    PharmGKBiPA36087.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1028.
    GeneTreeiENSGT00440000033609.
    HOVERGENiHBG006973.
    InParanoidiP35270.
    KOiK00072.
    OMAiMFREQRE.
    OrthoDBiEOG7327PS.
    PhylomeDBiP35270.
    TreeFamiTF326358.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03979-MONOMER.
    ReactomeiREACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.

    Miscellaneous databases

    ChiTaRSiSPR. human.
    EvolutionaryTraceiP35270.
    GeneWikiiSepiapterin_reductase.
    GenomeRNAii6697.
    NextBioi26111.
    PROiP35270.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP35270.
    CleanExiHS_SPR.
    GenevisibleiP35270. HS.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR006393. Sepiapterin_red.
    [Graphical view]
    PfamiPF00106. adh_short. 1 hit.
    [Graphical view]
    PRINTSiPR00081. GDHRDH.
    TIGRFAMsiTIGR01500. sepiapter_red. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and sequencing of cDNA encoding human sepiapterin reductase -- an enzyme involved in tetrahydrobiopterin biosynthesis."
      Ichinose H., Katoh S., Sueoka T., Titani K., Fujita K., Nagatsu T.
      Biochem. Biophys. Res. Commun. 179:183-189(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Detection of a novel sepiapterin reductase mRNA: assay of mRNA in various cells and tissues of various species."
      Maier J., Schott K., Werner T., Bacher A., Ziegler I.
      Exp. Cell Res. 204:217-222(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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].
      Tissue: Salivary gland.
    4. Suzuki Y., Sugano S., 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].
      Tissue: Kidney.
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Pancreas.
    8. "Genomic organization and chromosomal localization of the human sepiapterin reductase gene."
      Ohye T., Hori T.A., Katoh S., Nagatsu T., Ichinose H.
      Biochem. Biophys. Res. Commun. 251:597-602(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    9. "Mutational analysis of sites in sepiapterin reductase phosphorylated by Ca2+/calmodulin-dependent protein kinase II."
      Fujimoto K., Takahashi S.Y., Katoh S.
      Biochim. Biophys. Acta 1594:191-198(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: KINETIC PARAMETERS, PHOSPHORYLATION AT SER-213, MUTAGENESIS OF SER-213.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    12. "Crystal structure of human sepiapterin reductase."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 5-261 IN COMPLEX WITH NADP.
    13. "Mutations in the sepiapterin reductase gene cause a novel tetrahydrobiopterin-dependent monoamine-neurotransmitter deficiency without hyperphenylalaninemia."
      Bonafe L., Thony B., Penzien J.M., Czarnecki B., Blau N.
      Am. J. Hum. Genet. 69:269-277(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DRDSPRD GLY-150.
    14. "Sepiapterin reductase deficiency an autosomal recessive DOPA-responsive dystonia."
      Abeling N.G.G.M., Duran M., Bakker H.D., Stroomer L., Thoeny B., Blau N., Booij J., Poll-The B.T.
      Mol. Genet. Metab. 89:116-120(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DRDSPRD LEU-163.
    15. "Dopa-responsive hypersomnia and mixed movement disorder due to sepiapterin reductase deficiency."
      Friedman J., Hyland K., Blau N., MacCollin M.
      Neurology 67:2032-2035(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DRDSPRD GLY-150.

    Entry informationi

    Entry nameiSPRE_HUMAN
    AccessioniPrimary (citable) accession number: P35270
    Secondary accession number(s): A8K741
    , D6W5H2, Q53GI9, Q9UBB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: July 22, 2015
    This is version 161 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 2
      Human chromosome 2: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.