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P35270

- SPRE_HUMAN

UniProt

P35270 - SPRE_HUMAN

Protein

Sepiapterin reductase

Gene

SPR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    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

    1. aldo-keto reductase (NADP) activity Source: UniProtKB
    2. NADP binding Source: UniProtKB
    3. sepiapterin reductase activity Source: UniProtKB

    GO - Biological processi

    1. nitric oxide biosynthetic process Source: UniProtKB
    2. nitric oxide metabolic process Source: Reactome
    3. oxidation-reduction process Source: UniProtKB
    4. regulation of nitric-oxide synthase activity Source: Reactome
    5. small molecule metabolic process Source: Reactome
    6. tetrahydrobiopterin biosynthetic process Source: UniProtKB

    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: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:11257. SPR.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Dystonia, DOPA-responsive, due to sepiapterin reductase deficiency (DRDSPRD) [MIM:612716]: A 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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.

    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

    ArrayExpressiP35270.
    BgeeiP35270.
    CleanExiHS_SPR.
    GenevestigatoriP35270.

    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 – 149
    Helixi18 – 2811
    Beta strandi36 – 427
    Helixi44 – 5411
    Turni56 – 605
    Beta strandi62 – 676
    Helixi73 – 8412
    Beta strandi94 – 996
    Helixi111 – 1133
    Helixi117 – 12711
    Helixi129 – 14113
    Beta strandi149 – 1557
    Helixi158 – 1603
    Helixi168 – 18720
    Beta strandi191 – 1977
    Beta strandi200 – 2034
    Helixi204 – 2129
    Helixi216 – 22712
    Helixi234 – 24714
    Beta strandi254 – 2574

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOVERGENiHBG006973.
    InParanoidiP35270.
    KOiK00072.
    OMAiEVNSYWA.
    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

    MEGGLGRAVC LLTGASRGFG RTLAPLLASL LSPGSVLVLS ARNDEALRQL    50
    EAELGAERSG LRVVRVPADL GAEAGLQQLL GALRELPRPK GLQRLLLINN 100
    AGSLGDVSKG FVDLSDSTQV NNYWALNLTS MLCLTSSVLK AFPDSPGLNR 150
    TVVNISSLCA LQPFKGWALY CAGKAARDML FQVLALEEPN VRVLNYAPGP 200
    LDTDMQQLAR ETSVDPDMRK GLQELKAKGK LVDCKVSAQK LLSLLEKDEF 250
    KSGAHVDFYD K 261
    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. 1 PublicationCurated

    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi464801.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1920.1.
    PIRi JQ1176.
    RefSeqi NP_003115.1. NM_003124.4.
    UniGenei Hs.301540.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z6Z X-ray 2.50 A/B/C/D/E/F 5-261 [» ]
    4HWK X-ray 2.40 A/B/C/D 1-261 [» ]
    4J7U X-ray 2.44 A/B/C/D 1-261 [» ]
    4J7X X-ray 2.60 A/B/F/J 1-261 [» ]
    ProteinModelPortali P35270.
    SMRi P35270. Positions 4-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112575. 14 interactions.
    IntActi P35270. 1 interaction.
    MINTi MINT-3304575.
    STRINGi 9606.ENSP00000234454.

    PTM databases

    PhosphoSitei P35270.

    Polymorphism databases

    DMDMi 464801.

    Proteomic databases

    MaxQBi P35270.
    PaxDbi P35270.
    PeptideAtlasi P35270.
    PRIDEi P35270.

    Protocols and materials databases

    DNASUi 6697.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000234454 ; ENSP00000234454 ; ENSG00000116096 .
    GeneIDi 6697.
    KEGGi hsa:6697.
    UCSCi uc002sik.2. human.

    Organism-specific databases

    CTDi 6697.
    GeneCardsi GC02P073026.
    HGNCi HGNC:11257. SPR.
    HPAi HPA039505.
    MIMi 182125. gene.
    612716. phenotype.
    neXtProti NX_P35270.
    Orphaneti 70594. Dopa-responsive dystonia due to sepiapterin reductase deficiency.
    PharmGKBi PA36087.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1028.
    HOVERGENi HBG006973.
    InParanoidi P35270.
    KOi K00072.
    OMAi EVNSYWA.
    OrthoDBi EOG7327PS.
    PhylomeDBi P35270.
    TreeFami TF326358.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03979-MONOMER.
    Reactomei REACT_111176. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.

    Miscellaneous databases

    ChiTaRSi SPR. human.
    EvolutionaryTracei P35270.
    GeneWikii Sepiapterin_reductase.
    GenomeRNAii 6697.
    NextBioi 26111.
    PROi P35270.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35270.
    Bgeei P35270.
    CleanExi HS_SPR.
    Genevestigatori P35270.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR002198. DH_sc/Rdtase_SDR.
    IPR002347. Glc/ribitol_DH.
    IPR016040. NAD(P)-bd_dom.
    IPR006393. Sepiapterin_red.
    [Graphical view ]
    Pfami PF00106. adh_short. 1 hit.
    [Graphical view ]
    PRINTSi PR00081. GDHRDH.
    TIGRFAMsi TIGR01500. sepiapter_red. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. "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.
    12. "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.
    13. "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.
    14. "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: 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

    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