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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

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

GO - Biological processi

  1. cell morphogenesis involved in neuron differentiation Source: Ensembl
  2. death Source: Ensembl
  3. dopamine metabolic process Source: Ensembl
  4. L-phenylalanine metabolic process Source: Ensembl
  5. nitric oxide biosynthetic process Source: UniProtKB
  6. nitric oxide metabolic process Source: Reactome
  7. norepinephrine metabolic process Source: Ensembl
  8. oxidation-reduction process Source: UniProtKB
  9. pteridine metabolic process Source: Ensembl
  10. regulation of multicellular organism growth Source: Ensembl
  11. regulation of nitric-oxide synthase activity Source: Reactome
  12. serotonin metabolic process Source: Ensembl
  13. small molecule metabolic process Source: Reactome
  14. tetrahydrobiopterin biosynthetic process Source: UniProtKB
  15. voluntary musculoskeletal movement Source: Ensembl
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

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. mitochondrion Source: Ensembl
  5. 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.

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.
ExpressionAtlasiP35270. baseline and differential.
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 – 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.
OMAiNSNCIFH.
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:January 31, 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.

Polymorphism databases

DMDMi464801.

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 databases

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.
OMAiNSNCIFH.
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.
ExpressionAtlasiP35270. baseline and differential.
GenevestigatoriP35270.

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(1990) [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(1992) [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(2003) [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 (MAR-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(2004) [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(2003) [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(1997) [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(2001) [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(2013) [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 (JAN-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(2000) [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(2005) [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(2005) [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: January 31, 1994
Last sequence update: January 31, 1994
Last modified: March 3, 2015
This is version 157 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.