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Dihydropteridine reductase (EC 1.5.1.34) (HDHPR) (Quinoid dihydropteridine reductase) (Short chain dehydrogenase/reductase family 33C member 1)

 DHPR_HUMAN              Reviewed;         244 AA.
P09417; A8K158; B3KW71; Q53F52; Q9H3M5;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
28-NOV-2006, sequence version 2.
25-OCT-2017, entry version 195.
RecName: Full=Dihydropteridine reductase;
EC=1.5.1.34;
AltName: Full=HDHPR;
AltName: Full=Quinoid dihydropteridine reductase;
AltName: Full=Short chain dehydrogenase/reductase family 33C member 1;
Name=QDPR; Synonyms=DHPR, SDR33C1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-51.
PubMed=3031582; DOI=10.1093/nar/15.5.1921;
Dahl H.-H.M., Hutchison W., McAdam W., Wake S., Morgan F.J.,
Cotton R.G.H.;
"Human dihydropteridine reductase: characterisation of a cDNA clone
and its use in analysis of patients with dihydropteridine reductase
deficiency.";
Nucleic Acids Res. 15:1921-1932(1987).
[2]
SEQUENCE REVISION TO 51.
Dahl H.-H.M.;
Submitted (JUL-1987) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-51.
PubMed=3033643; DOI=10.1073/pnas.84.10.3329;
Lockyer J., Cook R.G., Milstien S., Kaufman S., Woo S.L.C.,
Ledley F.D.;
"Structure and expression of human dihydropteridine reductase.";
Proc. Natl. Acad. Sci. U.S.A. 84:3329-3333(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-51, AND VARIANTS
HPABH4C ASP-23; CYS-150; TYR-158 AND ILE-THR-GLY-218 INS.
PubMed=9744478;
DOI=10.1002/(SICI)1098-1004(1998)12:4<267::AID-HUMU8>3.3.CO;2-0;
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.;
"Dihydropteridine reductase deficiency: physical structure of the QDPR
gene, identification of two new mutations and genotype-phenotype
correlations.";
Hum. Mutat. 12:267-273(1998).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Hsiao K.-J., Yen P.-F., Lin C.-H., Liu T.-T., Chiang S.-H.,
Chen C.-Y., Tsai S.-F.;
"The complete sequence of human dihydropteridine reductase gene
containing BAC clone 395N09.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cerebellum;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
PROTEIN SEQUENCE OF 2-11 AND 128-138, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Gottlieb E.;
Submitted (MAR-2008) to UniProtKB.
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=8262916;
Su Y., Varughese K.I., Xuong N.H., Bray T.L., Roche D.J.,
Whiteley J.M.;
"The crystallographic structure of a human dihydropteridine reductase
NADH binary complex expressed in Escherichia coli by a cDNA
constructed from its rat homologue.";
J. Biol. Chem. 268:26836-26841(1993).
[18]
REVIEW ON VARIANTS.
PubMed=7627180; DOI=10.1002/humu.1380050402;
Smooker P.M., Cotton R.G.H.;
"Molecular basis of dihydropteridine reductase deficiency.";
Hum. Mutat. 5:279-284(1995).
[19]
VARIANTS HPABH4C ASP-23 AND GLY-108.
PubMed=8326489; DOI=10.1136/jmg.30.6.465;
Dianzani I., Howells D.W., Ponzone A., Saleeba J.A., Smooker P.M.,
Cotton R.G.H.;
"Two new mutations in the dihydropteridine reductase gene in patients
with tetrahydrobiopterin deficiency.";
J. Med. Genet. 30:465-469(1993).
[20]
VARIANT HPABH4C THR-123 INS.
PubMed=2116088;
Howells D.W., Forrest S.M., Dahl H.-H.M., Cotton R.G.H.;
"Insertion of an extra codon for threonine is a cause of
dihydropteridine reductase deficiency.";
Am. J. Hum. Genet. 47:279-285(1990).
[21]
VARIANTS HPABH4C PRO-14 AND VAL-17.
PubMed=10408783;
DOI=10.1002/(SICI)1098-1004(1999)13:6<503::AID-HUMU13>3.0.CO;2-F;
Smooker P.M., Gough T.J., Cotton R.G.H., Alliaudi C., de Sanctis L.,
Dianzani I.;
"A series of mutations in the dihydropteridine reductase gene
resulting in either abnormal RNA splicing or DHPR protein defects.";
Hum. Mutat. 13:503-504(1999).
[22]
VARIANTS HPABH4C ARG-17; ASP-18; ASP-23; ARG-66; ARG-149 AND CYS-150.
PubMed=11153907; DOI=10.1007/s004390000407;
Romstad A., Kalkanoglu H.S., Coskun T., Demirkol M., Tokatli A.,
Dursun A., Baykal T., Oezalp I., Guldberg P., Guettler F.;
"Molecular analysis of 16 Turkish families with DHPR deficiency using
denaturing gradient gel electrophoresis (DGGE).";
Hum. Genet. 107:546-553(2000).
-!- FUNCTION: The product of this enzyme, tetrahydrobiopterin (BH-4),
is an essential cofactor for phenylalanine, tyrosine, and
tryptophan hydroxylases.
-!- CATALYTIC ACTIVITY: A 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a
6,7-dihydropteridine + NAD(P)H.
-!- SUBUNIT: Homodimer.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P09417-1; Sequence=Displayed;
Name=2;
IsoId=P09417-2; Sequence=VSP_054356;
Note=No experimental confirmation available.;
-!- DISEASE: 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. {ECO:0000269|PubMed:10408783,
ECO:0000269|PubMed:11153907, ECO:0000269|PubMed:2116088,
ECO:0000269|PubMed:8326489, ECO:0000269|PubMed:9744478}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
(SDR) family. {ECO:0000305}.
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EMBL; X04882; CAA28571.1; -; mRNA.
EMBL; M16447; AAA52305.1; -; mRNA.
EMBL; AJ006239; CAA06930.1; -; Genomic_DNA.
EMBL; AJ006240; CAA06930.1; JOINED; Genomic_DNA.
EMBL; AJ006241; CAA06930.1; JOINED; Genomic_DNA.
EMBL; AJ006242; CAA06930.1; JOINED; Genomic_DNA.
EMBL; AJ006243; CAA06930.1; JOINED; Genomic_DNA.
EMBL; AJ006244; CAA06930.1; JOINED; Genomic_DNA.
EMBL; AJ006245; CAA06930.1; JOINED; Genomic_DNA.
EMBL; AB053170; BAB20429.1; -; Genomic_DNA.
EMBL; AK124382; BAG54033.1; -; mRNA.
EMBL; AK289773; BAF82462.1; -; mRNA.
EMBL; AK223437; BAD97157.1; -; mRNA.
EMBL; AC093600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471069; EAW92777.1; -; Genomic_DNA.
EMBL; CH471069; EAW92778.1; -; Genomic_DNA.
EMBL; BC000576; AAH00576.1; -; mRNA.
CCDS; CCDS3421.1; -. [P09417-1]
CCDS; CCDS77904.1; -. [P09417-2]
PIR; A93655; RDHUP.
RefSeq; NP_000311.2; NM_000320.2. [P09417-1]
RefSeq; NP_001293069.1; NM_001306140.1. [P09417-2]
UniGene; Hs.75438; -.
PDB; 1HDR; X-ray; 2.50 A; A=1-244.
PDBsum; 1HDR; -.
ProteinModelPortal; P09417; -.
SMR; P09417; -.
BioGrid; 111798; 26.
IntAct; P09417; 4.
MINT; MINT-5002411; -.
STRING; 9606.ENSP00000281243; -.
BindingDB; P09417; -.
ChEMBL; CHEMBL3730; -.
DrugBank; DB03814; 2-(N-Morpholino)-Ethanesulfonic Acid.
DrugBank; DB00157; NADH.
iPTMnet; P09417; -.
PhosphoSitePlus; P09417; -.
BioMuta; QDPR; -.
DMDM; 118572639; -.
REPRODUCTION-2DPAGE; IPI00014439; -.
UCD-2DPAGE; P09417; -.
EPD; P09417; -.
MaxQB; P09417; -.
PaxDb; P09417; -.
PeptideAtlas; P09417; -.
PRIDE; P09417; -.
DNASU; 5860; -.
Ensembl; ENST00000281243; ENSP00000281243; ENSG00000151552. [P09417-1]
Ensembl; ENST00000428702; ENSP00000390944; ENSG00000151552. [P09417-2]
GeneID; 5860; -.
KEGG; hsa:5860; -.
UCSC; uc003gpd.4; human. [P09417-1]
CTD; 5860; -.
DisGeNET; 5860; -.
EuPathDB; HostDB:ENSG00000151552.11; -.
GeneCards; QDPR; -.
HGNC; HGNC:9752; QDPR.
HPA; HPA058951; -.
HPA; HPA065649; -.
MalaCards; QDPR; -.
MIM; 261630; phenotype.
MIM; 612676; gene.
neXtProt; NX_P09417; -.
OpenTargets; ENSG00000151552; -.
Orphanet; 226; Dihydropteridine reductase deficiency.
PharmGKB; PA34094; -.
eggNOG; KOG4022; Eukaryota.
eggNOG; ENOG4111D6J; LUCA.
GeneTree; ENSGT00390000000470; -.
HOGENOM; HOG000232194; -.
HOVERGEN; HBG001000; -.
InParanoid; P09417; -.
KO; K00357; -.
OMA; NRKSMPD; -.
OrthoDB; EOG091G0ILG; -.
PhylomeDB; P09417; -.
TreeFam; TF105932; -.
BioCyc; MetaCyc:HS07746-MONOMER; -.
BRENDA; 1.5.1.34; 2681.
Reactome; R-HSA-71182; Phenylalanine and tyrosine catabolism.
SABIO-RK; P09417; -.
ChiTaRS; QDPR; human.
EvolutionaryTrace; P09417; -.
GeneWiki; QDPR; -.
GenomeRNAi; 5860; -.
PRO; PR:P09417; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000151552; -.
CleanEx; HS_QDPR; -.
ExpressionAtlas; P09417; baseline and differential.
Genevisible; P09417; HS.
GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0004155; F:6,7-dihydropteridine reductase activity; EXP:Reactome.
GO; GO:0009055; F:electron carrier activity; TAS:UniProtKB.
GO; GO:0070404; F:NADH binding; IEA:Ensembl.
GO; GO:0070402; F:NADPH binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0006520; P:cellular amino acid metabolic process; TAS:ProtInc.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0051066; P:dihydrobiopterin metabolic process; TAS:ProtInc.
GO; GO:0006559; P:L-phenylalanine catabolic process; TAS:Reactome.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0010044; P:response to aluminum ion; IEA:Ensembl.
GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:UniProtKB-KW.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020904; Sc_DH/Rdtase_CS.
InterPro; IPR002347; SDR_fam.
Pfam; PF00106; adh_short; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00061; ADH_SHORT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; NADP; Oxidoreductase;
Phenylketonuria; Polymorphism; Reference proteome;
Tetrahydrobiopterin biosynthesis.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.11}.
CHAIN 2 244 Dihydropteridine reductase.
/FTId=PRO_0000054636.
NP_BIND 14 38 NADP.
ACT_SITE 150 150 Proton acceptor.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.11}.
MOD_RES 73 73 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BVI4}.
MOD_RES 79 79 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BVI4}.
MOD_RES 96 96 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BVI4}.
MOD_RES 102 102 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BVI4}.
VAR_SEQ 36 66 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054356.
VARIANT 14 14 L -> P (in HPABH4C; severe;
dbSNP:rs756639609).
{ECO:0000269|PubMed:10408783}.
/FTId=VAR_008121.
VARIANT 17 17 G -> R (in HPABH4C; severe;
dbSNP:rs757483045).
{ECO:0000269|PubMed:11153907}.
/FTId=VAR_021767.
VARIANT 17 17 G -> V (in HPABH4C; severe).
{ECO:0000269|PubMed:10408783}.
/FTId=VAR_008122.
VARIANT 18 18 G -> D (in HPABH4C; severe).
{ECO:0000269|PubMed:11153907}.
/FTId=VAR_021768.
VARIANT 23 23 G -> D (in HPABH4C; severe;
dbSNP:rs104893863).
{ECO:0000269|PubMed:11153907,
ECO:0000269|PubMed:8326489,
ECO:0000269|PubMed:9744478}.
/FTId=VAR_006960.
VARIANT 36 36 W -> R (in HPABH4C; dbSNP:rs104893865).
/FTId=VAR_006961.
VARIANT 51 51 S -> T. {ECO:0000269|PubMed:3031582,
ECO:0000269|PubMed:3033643,
ECO:0000269|PubMed:9744478}.
/FTId=VAR_013027.
VARIANT 66 66 Q -> R (in HPABH4C; severe).
{ECO:0000269|PubMed:11153907}.
/FTId=VAR_021769.
VARIANT 74 74 L -> P (in HPABH4C).
/FTId=VAR_006962.
VARIANT 108 108 W -> G (in HPABH4C; dbSNP:rs104893864).
{ECO:0000269|PubMed:8326489}.
/FTId=VAR_006963.
VARIANT 123 123 T -> TT (in HPABH4C).
{ECO:0000269|PubMed:2116088}.
/FTId=VAR_006964.
VARIANT 145 145 P -> L (in HPABH4C).
/FTId=VAR_006965.
VARIANT 149 149 G -> R (in HPABH4C).
{ECO:0000269|PubMed:11153907}.
/FTId=VAR_021770.
VARIANT 150 150 Y -> C (in HPABH4C; mild;
dbSNP:rs104893866).
{ECO:0000269|PubMed:11153907,
ECO:0000269|PubMed:9744478}.
/FTId=VAR_006966.
VARIANT 151 151 G -> S (in HPABH4C; mild).
/FTId=VAR_006967.
VARIANT 158 158 H -> Y (in HPABH4C; severe;
dbSNP:rs750201480).
{ECO:0000269|PubMed:9744478}.
/FTId=VAR_006968.
VARIANT 170 170 G -> S (in HPABH4C; dbSNP:rs769460415).
/FTId=VAR_006969.
VARIANT 212 212 F -> C (in HPABH4C; mild).
/FTId=VAR_006970.
VARIANT 218 218 G -> GITG (in HPABH4C; mild).
/FTId=VAR_006971.
STRAND 11 16 {ECO:0000244|PDB:1HDR}.
TURN 17 19 {ECO:0000244|PDB:1HDR}.
HELIX 21 32 {ECO:0000244|PDB:1HDR}.
STRAND 36 43 {ECO:0000244|PDB:1HDR}.
STRAND 48 53 {ECO:0000244|PDB:1HDR}.
HELIX 60 75 {ECO:0000244|PDB:1HDR}.
STRAND 80 85 {ECO:0000244|PDB:1HDR}.
HELIX 100 110 {ECO:0000244|PDB:1HDR}.
HELIX 112 125 {ECO:0000244|PDB:1HDR}.
STRAND 126 135 {ECO:0000244|PDB:1HDR}.
HELIX 138 141 {ECO:0000244|PDB:1HDR}.
HELIX 148 165 {ECO:0000244|PDB:1HDR}.
STRAND 176 181 {ECO:0000244|PDB:1HDR}.
HELIX 188 191 {ECO:0000244|PDB:1HDR}.
HELIX 199 201 {ECO:0000244|PDB:1HDR}.
HELIX 205 216 {ECO:0000244|PDB:1HDR}.
TURN 217 220 {ECO:0000244|PDB:1HDR}.
STRAND 227 233 {ECO:0000244|PDB:1HDR}.
STRAND 236 242 {ECO:0000244|PDB:1HDR}.
SEQUENCE 244 AA; 25790 MW; 0852F9F0CA38AB1C CRC64;
MAAAAAAGEA RRVLVYGGRG ALGSRCVQAF RARNWWVASV DVVENEEASA SIIVKMTDSF
TEQADQVTAE VGKLLGEEKV DAILCVAGGW AGGNAKSKSL FKNCDLMWKQ SIWTSTISSH
LATKHLKEGG LLTLAGAKAA LDGTPGMIGY GMAKGAVHQL CQSLAGKNSG MPPGAAAIAV
LPVTLDTPMN RKSMPEADFS SWTPLEFLVE TFHDWITGKN RPSSGSLIQV VTTEGRTELT
PAYF


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