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Protein

Dihydropteridine reductase

Gene

QDPR

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

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
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tetrahydrobiopterin biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS07746-MONOMER.
BRENDAi1.5.1.34. 2681.
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
Short chain dehydrogenase/reductase family 33C member 1
Gene namesi
Name:QDPR
Synonyms:DHPR, SDR33C1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: 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: UniProtKB
  4. mitochondrion Source: Ensembl
  5. neuron projection Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Hyperphenylalaninemia, BH4-deficient, C (HPABH4C)5 Publications

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

Disease descriptionRare 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.

See also OMIM:261630
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

BgeeiP09417.
CleanExiHS_QDPR.
ExpressionAtlasiP09417. baseline and differential.
GenevestigatoriP09417.

Organism-specific databases

HPAiHPA058951.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi111798. 10 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 – 166Combined sources
Turni17 – 193Combined sources
Helixi21 – 3212Combined sources
Beta strandi36 – 438Combined sources
Beta strandi48 – 536Combined sources
Helixi60 – 7516Combined sources
Beta strandi80 – 856Combined sources
Helixi100 – 11011Combined sources
Helixi112 – 12514Combined sources
Beta strandi126 – 13510Combined sources
Helixi138 – 1414Combined sources
Helixi148 – 16518Combined sources
Beta strandi176 – 1816Combined sources
Helixi188 – 1914Combined sources
Helixi199 – 2013Combined sources
Helixi205 – 21612Combined sources
Turni217 – 2204Combined sources
Beta strandi227 – 2337Combined sources
Beta strandi236 – 2427Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000000470.
HOGENOMiHOG000232194.
HOVERGENiHBG001000.
InParanoidiP09417.
KOiK00357.
OMAiNRKSMPD.
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. AlignAdd to basket

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

        10         20         30         40         50
MAAAAAAGEA RRVLVYGGRG ALGSRCVQAF RARNWWVASV DVVENEEASA
60 70 80 90 100
SIIVKMTDSF TEQADQVTAE VGKLLGEEKV DAILCVAGGW AGGNAKSKSL
110 120 130 140 150
FKNCDLMWKQ SIWTSTISSH LATKHLKEGG LLTLAGAKAA LDGTPGMIGY
160 170 180 190 200
GMAKGAVHQL CQSLAGKNSG MPPGAAAIAV LPVTLDTPMN RKSMPEADFS
210 220 230 240
SWTPLEFLVE TFHDWITGKN RPSSGSLIQV VTTEGRTELT PAYF
Length:244
Mass (Da):25,790
Last modified:November 27, 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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi111798. 10 interactions.
IntActiP09417. 2 interactions.
MINTiMINT-5002411.
STRINGi9606.ENSP00000281243.

Chemistry

BindingDBiP09417.
ChEMBLiCHEMBL3730.

PTM databases

PhosphoSiteiP09417.

Polymorphism databases

DMDMi118572639.

2D gel databases

REPRODUCTION-2DPAGEIPI00014439.
UCD-2DPAGEP09417.

Proteomic databases

MaxQBiP09417.
PaxDbiP09417.
PeptideAtlasiP09417.
PRIDEiP09417.

Protocols and materials databases

DNASUi5860.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5860.
GeneCardsiGC04M017488.
HGNCiHGNC:9752. QDPR.
HPAiHPA058951.
MIMi261630. phenotype.
612676. gene.
neXtProtiNX_P09417.
Orphaneti226. Dihydropteridine reductase deficiency.
PharmGKBiPA34094.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00390000000470.
HOGENOMiHOG000232194.
HOVERGENiHBG001000.
InParanoidiP09417.
KOiK00357.
OMAiNRKSMPD.
OrthoDBiEOG7060RV.
PhylomeDBiP09417.
TreeFamiTF105932.

Enzyme and pathway databases

BioCyciMetaCyc:HS07746-MONOMER.
BRENDAi1.5.1.34. 2681.
ReactomeiREACT_1786. Phenylalanine and tyrosine catabolism.
SABIO-RKP09417.

Miscellaneous databases

ChiTaRSiQDPR. human.
EvolutionaryTraceiP09417.
GeneWikiiQDPR.
GenomeRNAii5860.
NextBioi22758.
PROiP09417.
SOURCEiSearch...

Gene expression databases

BgeeiP09417.
CleanExiHS_QDPR.
ExpressionAtlasiP09417. baseline and differential.
GenevestigatoriP09417.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-51.
  2. Dahl H.-H.M.
    Submitted (JUN-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(1997) [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 (NOV-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(2003) [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 (MAR-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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  11. Bienvenut W.V., Heiserich L., Gottlieb E.
    Submitted (FEB-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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "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.
  17. "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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  18. "Molecular basis of dihydropteridine reductase deficiency."
    Smooker P.M., Cotton R.G.H.
    Hum. Mutat. 5:279-284(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  19. "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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HPABH4C ASP-23 AND GLY-108.
  20. "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(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HPABH4C THR-123 INS.
  21. "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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HPABH4C PRO-14 AND VAL-17.
  22. "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(1999) [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: June 30, 1989
Last sequence update: November 27, 2006
Last modified: March 31, 2015
This is version 174 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

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.