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Q9UBQ7

- GRHPR_HUMAN

UniProt

Q9UBQ7 - GRHPR_HUMAN

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Protein
Glyoxylate reductase/hydroxypyruvate reductase
Gene
GRHPR, GLXR, MSTP035
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.

Catalytic activityi

Glycolate + NADP+ = glyoxylate + NADPH.
D-glycerate + NAD(P)+ = hydroxypyruvate + NAD(P)H.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei217 – 2171NADP
Binding sitei243 – 2431NADP; via carbonyl oxygen
Binding sitei245 – 2451Substrate
Binding sitei269 – 2691Substrate
Sitei274 – 2741Raises pKa of active site His
Active sitei293 – 2931Proton donor
Binding sitei295 – 2951NADP; via amide nitrogen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi162 – 1643NADP
Nucleotide bindingi185 – 1884NADP

GO - Molecular functioni

  1. NAD binding Source: UniProtKB
  2. NADPH binding Source: UniProtKB
  3. carboxylic acid binding Source: Ensembl
  4. glycerate dehydrogenase activity Source: UniProtKB
  5. glyoxylate reductase (NADP) activity Source: UniProtKB
  6. hydroxypyruvate reductase activity Source: UniProtKB
  7. protein homodimerization activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. dicarboxylic acid metabolic process Source: Ensembl
  3. excretion Source: UniProtKB
  4. glyoxylate metabolic process Source: Reactome
  5. metabolic process Source: UniProtKB
  6. oxidation-reduction process Source: UniProtKB
  7. protein oligomerization Source: UniProtKB
  8. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_16925. Glyoxylate metabolism.
SABIO-RKQ9UBQ7.

Names & Taxonomyi

Protein namesi
Recommended name:
Glyoxylate reductase/hydroxypyruvate reductase (EC:1.1.1.79, EC:1.1.1.81)
Gene namesi
Name:GRHPR
Synonyms:GLXR
ORF Names:MSTP035
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:4570. GRHPR.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. cytosol Source: Ensembl
  3. extracellular vesicular exosome Source: UniProt
  4. peroxisomal matrix Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Hyperoxaluria primary 2 (HP2) [MIM:260000]: A disorder characterized by elevated urinary excretion of oxalate and L-glycerate, progressive tissue accumulation of insoluble calcium oxalate, nephrolithiasis, nephrocalcinosis, and end-stage renal disease.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Organism-specific databases

MIMi260000. phenotype.
Orphaneti93599. Primary hyperoxaluria type 2.
PharmGKBiPA28965.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Glyoxylate reductase/hydroxypyruvate reductase
PRO_0000075944Add
BLAST

Proteomic databases

MaxQBiQ9UBQ7.
PaxDbiQ9UBQ7.
PRIDEiQ9UBQ7.

2D gel databases

REPRODUCTION-2DPAGEIPI00037448.
UCD-2DPAGEQ9UBQ7.

PTM databases

PhosphoSiteiQ9UBQ7.

Expressioni

Tissue specificityi

Ubiquitous. Most abundantly expressed in the liver.1 Publication

Gene expression databases

ArrayExpressiQ9UBQ7.
BgeeiQ9UBQ7.
CleanExiHS_GRHPR.
GenevestigatoriQ9UBQ7.

Organism-specific databases

HPAiHPA022971.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi114781. 14 interactions.
IntActiQ9UBQ7. 5 interactions.
MINTiMINT-5005010.
STRINGi9606.ENSP00000313432.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 137
Helixi17 – 259
Beta strandi29 – 335
Beta strandi36 – 383
Helixi42 – 498
Beta strandi53 – 575
Helixi65 – 717
Beta strandi77 – 837
Helixi90 – 956
Beta strandi99 – 1013
Helixi108 – 12316
Helixi126 – 1349
Beta strandi143 – 1464
Beta strandi155 – 1595
Helixi163 – 17210
Helixi173 – 1753
Beta strandi179 – 1868
Helixi189 – 1935
Turni194 – 1963
Beta strandi197 – 1993
Helixi202 – 2087
Beta strandi210 – 2145
Turni220 – 2245
Helixi228 – 2336
Beta strandi239 – 2424
Helixi246 – 2483
Helixi251 – 2599
Beta strandi262 – 2698
Beta strandi272 – 2754
Helixi281 – 2844
Beta strandi288 – 2903
Helixi299 – 31820

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GCGX-ray2.20A/B/C/D1-328[»]
2H1SX-ray2.45A/B/C/D2-328[»]
2Q50X-ray2.45A/B/C/D2-328[»]
2WWRX-ray2.82A/B/C/D1-328[»]
ProteinModelPortaliQ9UBQ7.
SMRiQ9UBQ7. Positions 5-328.

Miscellaneous databases

EvolutionaryTraceiQ9UBQ7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 842Substrate binding
Regioni293 – 2964Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1052.
HOVERGENiHBG051838.
KOiK00049.
OMAiHRTRNTM.
PhylomeDBiQ9UBQ7.
TreeFamiTF324791.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEiPS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UBQ7-1 [UniParc]FASTAAdd to Basket

« Hide

MRPVRLMKVF VTRRIPAEGR VALARAADCE VEQWDSDEPI PAKELERGVA    50
GAHGLLCLLS DHVDKRILDA AGANLKVIST MSVGIDHLAL DEIKKRGIRV 100
GYTPDVLTDT TAELAVSLLL TTCRRLPEAI EEVKNGGWTS WKPLWLCGYG 150
LTQSTVGIIG LGRIGQAIAR RLKPFGVQRF LYTGRQPRPE EAAEFQAEFV 200
STPELAAQSD FIVVACSLTP ATEGLCNKDF FQKMKETAVF INISRGDVVN 250
QDDLYQALAS GKIAAAGLDV TSPEPLPTNH PLLTLKNCVI LPHIGSATHR 300
TRNTMSLLAA NNLLAGLRGE PMPSELKL 328
Length:328
Mass (Da):35,668
Last modified:May 1, 2000 - v1
Checksum:i68A0E311AA4E5650
GO

Sequence cautioni

The sequence AAD54066.1 differs from that shown. Reason: Frameshift at positions 109 and 137.
The sequence AAG39286.1 differs from that shown. Reason: Frameshift at position 237.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1701R → Q.
Corresponds to variant rs12002324 [ dbSNP | Ensembl ].
VAR_032762

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF134895 mRNA. Translation: AAF00111.1.
AF146018 mRNA. Translation: AAD45886.1.
AF146689 Genomic DNA. Translation: AAD46517.1.
AF113215 mRNA. Translation: AAG39286.1. Frameshift.
AK315690 mRNA. Translation: BAG38053.1.
AL158155 Genomic DNA. Translation: CAI13848.1.
CH471071 Genomic DNA. Translation: EAW58284.1.
BC000605 mRNA. Translation: AAH00605.1.
AF113251 mRNA. Translation: AAD54066.1. Frameshift.
CCDSiCCDS6609.1.
PIRiJC7190.
RefSeqiNP_036335.1. NM_012203.1.
UniGeneiHs.155742.

Genome annotation databases

EnsembliENST00000318158; ENSP00000313432; ENSG00000137106.
GeneIDi9380.
KEGGihsa:9380.
UCSCiuc003zzt.1. human.

Polymorphism databases

DMDMi47116943.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF134895 mRNA. Translation: AAF00111.1 .
AF146018 mRNA. Translation: AAD45886.1 .
AF146689 Genomic DNA. Translation: AAD46517.1 .
AF113215 mRNA. Translation: AAG39286.1 . Frameshift.
AK315690 mRNA. Translation: BAG38053.1 .
AL158155 Genomic DNA. Translation: CAI13848.1 .
CH471071 Genomic DNA. Translation: EAW58284.1 .
BC000605 mRNA. Translation: AAH00605.1 .
AF113251 mRNA. Translation: AAD54066.1 . Frameshift.
CCDSi CCDS6609.1.
PIRi JC7190.
RefSeqi NP_036335.1. NM_012203.1.
UniGenei Hs.155742.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GCG X-ray 2.20 A/B/C/D 1-328 [» ]
2H1S X-ray 2.45 A/B/C/D 2-328 [» ]
2Q50 X-ray 2.45 A/B/C/D 2-328 [» ]
2WWR X-ray 2.82 A/B/C/D 1-328 [» ]
ProteinModelPortali Q9UBQ7.
SMRi Q9UBQ7. Positions 5-328.
ModBasei Search...

Protein-protein interaction databases

BioGridi 114781. 14 interactions.
IntActi Q9UBQ7. 5 interactions.
MINTi MINT-5005010.
STRINGi 9606.ENSP00000313432.

PTM databases

PhosphoSitei Q9UBQ7.

Polymorphism databases

DMDMi 47116943.

2D gel databases

REPRODUCTION-2DPAGE IPI00037448.
UCD-2DPAGE Q9UBQ7.

Proteomic databases

MaxQBi Q9UBQ7.
PaxDbi Q9UBQ7.
PRIDEi Q9UBQ7.

Protocols and materials databases

DNASUi 9380.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000318158 ; ENSP00000313432 ; ENSG00000137106 .
GeneIDi 9380.
KEGGi hsa:9380.
UCSCi uc003zzt.1. human.

Organism-specific databases

CTDi 9380.
GeneCardsi GC09P037412.
GeneReviewsi GRHPR.
HGNCi HGNC:4570. GRHPR.
HPAi HPA022971.
MIMi 260000. phenotype.
604296. gene.
neXtProti NX_Q9UBQ7.
Orphaneti 93599. Primary hyperoxaluria type 2.
PharmGKBi PA28965.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1052.
HOVERGENi HBG051838.
KOi K00049.
OMAi HRTRNTM.
PhylomeDBi Q9UBQ7.
TreeFami TF324791.

Enzyme and pathway databases

Reactomei REACT_16925. Glyoxylate metabolism.
SABIO-RK Q9UBQ7.

Miscellaneous databases

ChiTaRSi GRHPR. human.
EvolutionaryTracei Q9UBQ7.
GeneWikii GRHPR.
GenomeRNAii 9380.
NextBioi 35148.
PROi Q9UBQ7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UBQ7.
Bgeei Q9UBQ7.
CleanExi HS_GRHPR.
Genevestigatori Q9UBQ7.

Family and domain databases

Gene3Di 3.40.50.720. 2 hits.
InterProi IPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view ]
PROSITEi PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase."
    Rumsby G., Cregeen D.P.
    Biochim. Biophys. Acta 1446:383-388(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
    Tissue: Liver.
  2. "The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II."
    Cramer S.D., Ferree P.M., Lin K., Milliner D.S., Holmes R.P.
    Hum. Mol. Genet. 8:2063-2069(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INVOLVEMENT IN HP2.
    Tissue: Liver.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Aorta.
  4. "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: Testis.
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  8. "Cloning and characterization of a putative human D-2-hydroxyacid dehydrogenase in chromosome 9q."
    Huang T., Yang W., Pereira A.C., Craigen W.J., Shih V.E.
    Biochem. Biophys. Res. Commun. 268:298-301(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 45-328, TISSUE SPECIFICITY.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase."
    Booth M.P.S., Conners R., Rumsby G., Brady R.L.
    J. Mol. Biol. 360:178-189(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NADP AND SUBSTRATE, SUBUNIT.
  11. "Crystal structure of a glyoxylate/hydroxypyruvate reductase from Homo sapiens."
    Center for eukaryotic structural genomics (CESG)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 2-328.

Entry informationi

Entry nameiGRHPR_HUMAN
AccessioniPrimary (citable) accession number: Q9UBQ7
Secondary accession number(s): Q5T945, Q9H3E9, Q9UKX1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 132 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 9
    Human chromosome 9: 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

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