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Protein

GMP reductase 1

Gene

GMPR

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

Functioni

Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.UniRule annotation

Catalytic activityi

Inosine 5'-phosphate + NH3 + NADP+ = guanosine 5'-phosphate + NADPH.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781NADPUniRule annotation
Metal bindingi181 – 1811Potassium; via carbonyl oxygenUniRule annotation1 Publication
Metal bindingi183 – 1831Potassium; via carbonyl oxygenUniRule annotation1 Publication
Active sitei186 – 1861Thioimidate intermediateUniRule annotation
Metal bindingi186 – 1861Potassium; via carbonyl oxygenUniRule annotation1 Publication
Active sitei188 – 1881Proton donor/acceptorUniRule annotation
Metal bindingi189 – 1891PotassiumUniRule annotation1 Publication
Binding sitei269 – 2691NADP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 272NADP; shared with neighboring subunitUniRule annotation
Nucleotide bindingi129 – 1313NADPUniRule annotation
Nucleotide bindingi180 – 1812NADPUniRule annotation
Nucleotide bindingi285 – 2862NADPUniRule annotation
Nucleotide bindingi314 – 3174NADP; shared with neighboring subunitUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Purine metabolism

Keywords - Ligandi

Metal-binding, NADP, Potassium

Enzyme and pathway databases

ReactomeiR-HSA-74217. Purine salvage.

Names & Taxonomyi

Protein namesi
Recommended name:
GMP reductase 1UniRule annotation (EC:1.7.1.7UniRule annotation)
Short name:
GMPR 1UniRule annotation
Alternative name(s):
Guanosine 5'-monophosphate oxidoreductase 1UniRule annotation
Short name:
Guanosine monophosphate reductase 1UniRule annotation
Gene namesi
Name:GMPR
Synonyms:GMPR1UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:4376. GMPR.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28761.

Polymorphism and mutation databases

BioMutaiGMPR.
DMDMi544455.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345GMP reductase 1PRO_0000093723Add
BLAST

Proteomic databases

EPDiP36959.
MaxQBiP36959.
PaxDbiP36959.
PeptideAtlasiP36959.
PRIDEiP36959.

PTM databases

iPTMnetiP36959.
PhosphoSiteiP36959.

Expressioni

Gene expression databases

BgeeiP36959.
CleanExiHS_GMPR.
GenevisibleiP36959. HS.

Organism-specific databases

HPAiHPA000904.
HPA021476.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi109028. 2 interactions.
STRINGi9606.ENSP00000259727.

Structurei

Secondary structure

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi12 – 143Combined sources
Beta strandi15 – 173Combined sources
Helixi27 – 293Combined sources
Beta strandi34 – 374Combined sources
Turni39 – 413Combined sources
Beta strandi44 – 474Combined sources
Beta strandi50 – 523Combined sources
Turni56 – 583Combined sources
Helixi61 – 677Combined sources
Helixi68 – 703Combined sources
Beta strandi73 – 753Combined sources
Helixi82 – 9110Combined sources
Helixi93 – 986Combined sources
Beta strandi99 – 1035Combined sources
Helixi107 – 11913Combined sources
Beta strandi125 – 1295Combined sources
Helixi136 – 14813Combined sources
Beta strandi152 – 1598Combined sources
Helixi162 – 1709Combined sources
Beta strandi174 – 1785Combined sources
Helixi188 – 1914Combined sources
Helixi198 – 21013Combined sources
Turni211 – 2133Combined sources
Beta strandi215 – 2206Combined sources
Helixi225 – 23410Combined sources
Beta strandi237 – 2426Combined sources
Helixi243 – 2453Combined sources
Beta strandi251 – 2533Combined sources
Beta strandi263 – 2675Combined sources
Helixi272 – 2776Combined sources
Beta strandi285 – 2884Combined sources
Beta strandi292 – 2965Combined sources
Helixi301 – 31919Combined sources
Helixi324 – 3263Combined sources
Helixi327 – 3304Combined sources
Beta strandi333 – 3353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BLEX-ray1.90A1-345[»]
2BWGX-ray2.40A/B/C/D1-345[»]
ProteinModelPortaliP36959.
SMRiP36959. Positions 2-338.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36959.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni219 – 2213GMP bindingUniRule annotation1 Publication
Regioni242 – 2432GMP bindingUniRule annotation1 Publication
Regioni268 – 2703GMP bindingUniRule annotation1 Publication
Regioni286 – 2905GMP bindingUniRule annotation1 Publication

Sequence similaritiesi

Belongs to the IMPDH/GMPR family. GuaC type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165756.
HOVERGENiHBG051744.
InParanoidiP36959.
KOiK00364.
OMAiVEHTILD.
OrthoDBiEOG73804S.
PhylomeDBiP36959.
TreeFamiTF300378.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00596. GMP_reduct_type1.
InterProiIPR013785. Aldolase_TIM.
IPR005993. GMPR.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamiPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000235. GMP_reductase. 1 hit.
TIGRFAMsiTIGR01305. GMP_reduct_1. 1 hit.
PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36959-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRIDADLKL DFKDVLLRPK RSSLKSRAEV DLERTFTFRN SKQTYSGIPI
60 70 80 90 100
IVANMDTVGT FEMAAVMSQH SMFTAIHKHY SLDDWKLFAT NHPECLQNVA
110 120 130 140 150
VSSGSGQNDL EKMTSILEAV PQVKFICLDV ANGYSEHFVE FVKLVRAKFP
160 170 180 190 200
EHTIMAGNVV TGEMVEELIL SGADIIKVGV GPGSVCTTRT KTGVGYPQLS
210 220 230 240 250
AVIECADSAH GLKGHIISDG GCTCPGDVAK AFGAGADFVM LGGMFSGHTE
260 270 280 290 300
CAGEVFERNG RKLKLFYGMS SDTAMNKHAG GVAEYRASEG KTVEVPYKGD
310 320 330 340
VENTILDILG GLRSTCTYVG AAKLKELSRR ATFIRVTQQH NTVFS
Length:345
Mass (Da):37,419
Last modified:June 1, 1994 - v1
Checksum:i217E1A5A599CA510
GO

Polymorphismi

At least two different alleles are known.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti234 – 2341A → T.1 Publication
Corresponds to variant rs760571328 [ dbSNP | Ensembl ].
VAR_003969
Natural varianti256 – 2561F → I.2 Publications
Corresponds to variant rs1042391 [ dbSNP | Ensembl ].
VAR_003970

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35304 Genomic DNA. Translation: AAA52503.1.
M27941 Genomic DNA. Translation: AAA53106.1.
M24470 mRNA. Translation: AAA52498.1.
AL009031, AL138883 Genomic DNA. Translation: CAI21422.1.
AL138883, AL009031 Genomic DNA. Translation: CAI19917.1.
BC008281 mRNA. Translation: AAH08281.1.
CCDSiCCDS4537.1.
PIRiB32902.
RefSeqiNP_006868.3. NM_006877.3.
UniGeneiHs.484741.

Genome annotation databases

EnsembliENST00000259727; ENSP00000259727; ENSG00000137198.
GeneIDi2766.
KEGGihsa:2766.
UCSCiuc003nbs.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35304 Genomic DNA. Translation: AAA52503.1.
M27941 Genomic DNA. Translation: AAA53106.1.
M24470 mRNA. Translation: AAA52498.1.
AL009031, AL138883 Genomic DNA. Translation: CAI21422.1.
AL138883, AL009031 Genomic DNA. Translation: CAI19917.1.
BC008281 mRNA. Translation: AAH08281.1.
CCDSiCCDS4537.1.
PIRiB32902.
RefSeqiNP_006868.3. NM_006877.3.
UniGeneiHs.484741.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BLEX-ray1.90A1-345[»]
2BWGX-ray2.40A/B/C/D1-345[»]
ProteinModelPortaliP36959.
SMRiP36959. Positions 2-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109028. 2 interactions.
STRINGi9606.ENSP00000259727.

PTM databases

iPTMnetiP36959.
PhosphoSiteiP36959.

Polymorphism and mutation databases

BioMutaiGMPR.
DMDMi544455.

Proteomic databases

EPDiP36959.
MaxQBiP36959.
PaxDbiP36959.
PeptideAtlasiP36959.
PRIDEiP36959.

Protocols and materials databases

DNASUi2766.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259727; ENSP00000259727; ENSG00000137198.
GeneIDi2766.
KEGGihsa:2766.
UCSCiuc003nbs.3. human.

Organism-specific databases

CTDi2766.
GeneCardsiGMPR.
HGNCiHGNC:4376. GMPR.
HPAiHPA000904.
HPA021476.
MIMi139265. gene.
neXtProtiNX_P36959.
PharmGKBiPA28761.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2550. Eukaryota.
COG0516. LUCA.
GeneTreeiENSGT00530000062923.
HOGENOMiHOG000165756.
HOVERGENiHBG051744.
InParanoidiP36959.
KOiK00364.
OMAiVEHTILD.
OrthoDBiEOG73804S.
PhylomeDBiP36959.
TreeFamiTF300378.

Enzyme and pathway databases

ReactomeiR-HSA-74217. Purine salvage.

Miscellaneous databases

ChiTaRSiGMPR. human.
EvolutionaryTraceiP36959.
GenomeRNAii2766.
PROiP36959.
SOURCEiSearch...

Gene expression databases

BgeeiP36959.
CleanExiHS_GMPR.
GenevisibleiP36959. HS.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00596. GMP_reduct_type1.
InterProiIPR013785. Aldolase_TIM.
IPR005993. GMPR.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamiPF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFiPIRSF000235. GMP_reductase. 1 hit.
TIGRFAMsiTIGR01305. GMP_reduct_1. 1 hit.
PROSITEiPS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase."
    Kanno H., Huang I.Y., Kan Y.W., Yoshida A.
    Cell 58:595-606(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "Genomic structure and expression of human guanosine monophosphate reductase."
    Kondoh T., Kanno H., Chang L., Yoshida A.
    Hum. Genet. 88:219-224(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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], VARIANT ILE-256.
    Tissue: Placenta.
  5. "The human mRNA that provides the N-terminus of chimeric G6PD encodes GMP reductase."
    Henikoff S., Smith J.M.
    Cell 58:1021-1022(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO GMP REDUCTASE.
  6. "Origin of 'fused' glucose-6-phosphate dehydrogenase."
    Yoshida A., Kan Y.W.
    Cell 62:11-12(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF ROLE IN G6PD.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Structure of human guanosine monophosphate reductase GMPR1 in complex with GMP."
    Structural genomics consortium (SGC)
    Submitted (JUL-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH GMP AND POTASSIUM IONS.
  9. "Identification of common variant alleles of the human guanosine monophosphate reductase gene."
    Kondoh T., Kanno H., Chang L., Yoshida A.
    Hum. Genet. 88:225-227(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-234 AND ILE-256.

Entry informationi

Entry nameiGMPR1_HUMAN
AccessioniPrimary (citable) accession number: P36959
Secondary accession number(s): Q96HQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 6, 2016
This is version 159 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

Caution

The N-terminus was initially (PubMed:2758468) thought to be fused with glucose-6-phosphate-dehydrogenase (G6PD) protein in vivo. However, PubMed:2570640 showed that it encodes a GMP reductase, and PubMed:1694726 showed that the chimeric protein is an artifact.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

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 one 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.